Swissknife_1.75/0000755005110600510130000000000013155517214014055 5ustar ecastroSwissProtSwissknife_1.75/README0000755005110600510130000000454412643153632014750 0ustar ecastroSwissProtOVERVIEW -------- Swissknife is a Perl module for creating and parsing Swiss-Prot files. AVAILABILITY ------------ The latest version of Swissknife is available from: https://sourceforge.net/projects/swissknife/files/latest/download ftp://ftp.ebi.ac.uk/pub/software/swissprot/Swissknife/ INSTALLATION ------------ Use the following commands: gunzip Swissknife.tar.gz tar xf Swissknife.tar cd SWISS perl Makefile.PL make install Alternatively, you may simply copy the lib/SWISS directory (the directory itself with all the files it contains) to a directory in your PERLLIB. REQUIREMENTS ------------ Swissknife has been tested with Perl version 5.00502 and higher. External modules used: Carp Data::Dumper Exporter All of these are part of the Perl distribution. BUGS ---- A segmentation fault occurs in very rare cases under some builds of perl 5.8. Run the test suite to check if this is the case on your platform. DOCUMENTATION ------------- The Swissknife modules are documented using the POD (plain old documentation format). When installed, the documentation is accessible by typing "perldoc SWISS::Entry" at the command prompt, and similarly for other modules. COPYRIGHT --------- Copyright (C) 1999-2016, the European Bioinformatics Institute and the Swiss Institute of Bioinformatics. The SWISS modules are free software; you can redistribute and/or modify them under the terms of the GNU General Public License as published by the Free Software Foundation; either version 2 of the License, or (at your option) any later version. These modules are distributed in the hope that they will be useful, but WITHOUT ANY WARRANTY; without even the implied warranty of MERCHANTABILITY or FITNESS FOR A PARTICULAR PURPOSE. See the GNU General Public License for more details. You should have received a copy of the GNU General Public License along with this program; if not, write to the Free Software Foundation, Inc., 59 Temple Place - Suite 330, Boston, MA 02111-1307, USA. AUTHORS ------- Wolfgang Fleischmann, Henning Hermjakob, Paul Kersey, Alexandre Gattiker, Eric Jain, Edouard de Castro, edouard.decastro@isb-sib.ch ACKNOWLEDGEMENTS ---------------- The Swissknife modules have been built on the example of the prEMBL modules by Matthew Pocock, mrp@sanger.ac.uk Thanks to Christian Iseli for help with the perl module setup. Swissknife_1.75/lib/0000755005110600510130000000000013155516754014633 5ustar ecastroSwissProtSwissknife_1.75/lib/SWISS/0000755005110600510130000000000013155516754015543 5ustar ecastroSwissProtSwissknife_1.75/lib/SWISS/GN.pm0000644005110600510130000000406110366115237016376 0ustar ecastroSwissProtpackage SWISS::GN; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( text => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $text = shift; # Parse out the evidence tags if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { my $tmp = $1; $self->evidenceTags($tmp); } $self->text($text); return $self; } sub toText { my $self = shift; return $self->text . $self->getEvidenceTagsString; } #Convert gene names to mixed case, according to one or more regular #expressions. This is done by changing the letters in the ORF name to #lowercase in all possible combinations until one is found which matches one of #the regular expressions given as parameters. sub toMixedCase { my ($self, @regexps) = @_; my $orfname = SWISS::TextFunc::toMixedCase($self->text, @regexps); $self->text($orfname); return $orfname; } 1; __END__ =head1 Name SWISS::GN.pm =head1 Description B represents one gene name from the GN line. The container object for several synonym gene names is SWISS::GeneGroup. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C One gene name. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Reading/Writing methods =over =item toMixedCase(@regexps) Convert gene names to mixed case, according to one or more regular expressions. This is typically useful for converting uppercase ORF numbers to mixed case. E.g. the E.coli gene "B1563" converted with the regexp '(b(\d{4}(\.\d)?))' will yield the gene name "b1563". The method also supports fused gene names, e.g. "B0690/B0691" is converted to "b0690/b0691". The method changes the text of the SWISS::GN object and also returns the new text value. =back Swissknife_1.75/lib/SWISS/TextFunc.pm0000644005110600510130000004415613147300101017625 0ustar ecastroSwissProtpackage SWISS::TextFunc; use vars qw( $AUTOLOAD @ISA @EXPORT_OK @lineObjects @linePattern %linePattern $evidencePattern $evidencePatternOld $evidencePatternNew $evidencePatternAsSep $evidencePatternReversed $textWrapPattern1 $textWrapPattern2 $lineLength $lineLengthMax $lineLengthStar $lineLengthSQ ); use Exporter; use Carp; use strict; BEGIN{ @EXPORT_OK = qw(wrap); @ISA = ( 'Exporter' ); @lineObjects = ('IDs', 'ACs', 'DTs', 'DEs', 'GNs', 'OSs', 'OGs', 'OCs', 'OXs', 'OHs', 'Refs', 'CCs', 'DRs', 'PE', 'KWs', 'FTs', 'Stars', 'SQs'); @linePattern = ('^( ?ID .*\n)+(\*\* .*\n)*', '^( ?AC .*\n)+(\*\* .*\n)*', '^( ?DT .*\n){3}', '^( ?DE .*\n)+', '^( ?GN .*\n)+', '^( ?OS .*\n)+', '^( ?OG .*\n)+', '^( ?OC .*\n)+', '^( ?OX .*\n)+', '^( ?OH .*\n)+', # Complex expression for Reference blocks '^( ?R. .*\n)+(( ?R. .*\n)|( ?\*\* .*\n))*( ?R. .*\n)+', '^( ?CC .*\n)+', # The block of DR lines may contain ** lines, except at the beginning, e.g. # ** PRINTS; PR01217; PRICHEXTENSN; FALSE_POS_1. '^( ?DR .*\n)+( ?DR .*\n| ?\*\* \w+;.+\n)*', '^( ?PE .*\n)+', '^( ?KW .*\n)+', '^( ?FT .*\n)+', # Take a complex extended expression to take the # LAST ** line group as the annotator's section # NB: the 'Stars' comment is used to identify the hash key as 'St' in Stars.pm '^(?#Stars)((\*\*\s*\n)|(\*\* \#.*\n))+(\*\*.*\n)*(?=((SQ .*\n)( .*\n)+)?(\/\/\n))', # The sequence contains two line types and is at the end. '^(SQ .*\n)( .*\n)+(?=\/\/\n)' ); my ($line, $lineId); foreach $line (@linePattern) { ($lineId) = $line =~ /(\w\S)/; $linePattern{$lineId} = $line; } # The general pattern for evidence tags, .Sets $1 to the evidence tag $evidencePattern = ' ?\{((?:ECO:\d+[^,}]+(?:, )?)+|(?:E[ACIP]\d+,?)+)\}'; $evidencePatternOld = '\{((?:E[ACIP]\d+\,?)+)\}'; $evidencePatternNew = ' \{((?:ECO:\d+[^,}]+(?:, )?)+)\}'; $evidencePatternAsSep = '(?:\. | )?\{((?:ECO:\d+[^,}]+(?:, )?)+)\}(?:\. )?'; # and its reversed form for the parsing of the DE lines TODO: check DE parsing! $evidencePatternReversed = '\}(\,?\d+[ACIP]E)*\{'; # General pattern and last-resort pattern # for wrapping text fields. # Wrap either at a whitespace that is not after a dash; or at a dash - not after a space (so as to not cut -Suffix) - # that is followed either by a letter/digit or an opening round or square bracket (so as to not cut at "->" or "--" or "-," etc). $textWrapPattern1 = '(?\- ])'; $lineLength = 75; $lineLengthMax = 255; $lineLengthStar = 32766; $lineLengthSQ = 60; } sub listFromText { my $class = shift; my $text = shift; my $sep = shift; my $end = shift || $sep; chomp $text; # remove \n from end of text $text =~ s/^$sep//; # remove separator at the beginning of the text $text =~ s/$end$//; # remove separator at the end of the text return split /$sep/, $text; } sub textFromList { my $class = shift; my $list = shift; my $sep = shift; my $end = shift; my $width = shift; my $text = (join $sep, @{$list}) . $end; # produce one funck off long string # work out how many characters can be per line $width -= length $sep; while($text =~ m/(.{1,$width}(($sep)|($)))/g) { push @_, $1; } return @_; } sub wrapText { my $class = shift; my $text = shift; my $width = shift; $text = '' unless $text; while($text =~ m/(.{1,$width})(\s+|$)/g) { push @_, $1; } return @_; } sub wrapOn { my ($class, $prefix1, $prefix2, $columns, $text, @separators) = @_; my ($newText, $prefix, $width, $trailingBlanks); my ($lineText, $sepText, $match, $postMatch); $newText = ''; push @separators, $textWrapPattern1, $textWrapPattern2, ''; # add default sep. to provided separators n.b. @separators might be empty: as a last resort, wrap anywhere # eventually use multiple separators (for some FT lines); triggered when provided separators first elem is array ref!... my ($separator1, $border, $separator2, $longWordChar); if (ref $separators[0] eq "ARRAY") { ($separator1, $border, $separator2, $longWordChar) = @{$separators[0]}; $separators[0] = $separator1; } $prefix=$prefix1; TEXT:while ($text) { # switch between using separator1 or separator2 depending on border (for some FT lines) $width = $columns - length ($prefix); if (defined($separator1) and $separators[0] eq $separator1) { #fugly! happen when $separators[0] eq "ARRAY"; "means": border is (/should have been!) set # if border is found in line to wrap (up to witdh) or in already wrapped lines # use separator2 instead of separator1! # e.g. # FT VARIANT 222 222 L -> P (in CLN1; late infantile blablablablablabla) # separator1 = '(?!\>)\s*', separator2 = "/|$SWISS::TextFunc::textWrapPattern1" border = '[{(]' # so here separator2 will be used has there is a "()" = textFunc::textWrapPattern1 = will wrap on ws before bla... # wheras with e,g. # FT CONFLICT 245 303 LKNNTITTHPKFQTITPINNSIIFFNSRCRHEVMSVVCPSRPPAAAESPSMH -> GLPKGSVPPAAAESPSMHRKQELDSSQAPQQPGKPPDPGRPTQPGLSKSR # separator1 will be use = (?!\>)\s*: wrap anywhere (at max witdh) if not after a > or on first space(s) = will wrap inside first "seq" if (($newText =~ /$border/) || (substr($text, 0, $width) =~ /$border/) ) { $separators[0] = $separator2; } }; for (my $i=0; $i<@separators; $i++) { $width = $columns - length ($prefix); # initialize each time if (length($text) <= $width) { # no wrapping needed $newText = $newText . $prefix . $text . "\n"; $text = ''; next TEXT; } else { # needs wrapping while (($lineText, $sepText) = $text =~ /\A(.{1,$width})($separators[$i]|\Z)/) { $match = $&; $postMatch = $'; my $spaces = $match =~ s/(\s+)\Z// ? $1 : ""; if (length($match) > $width) { # The separator extends # beyond the maximal line length. Retry with shorter $width. $width--; } else { if (defined $longWordChar) { # if a long word is found, cut it anywhere and append as much of it as possible to the uppermost line... if ($postMatch =~ /^$longWordChar {$width}/x) { my $cutPos = $width - length($match) - length($spaces); # ... however, try to cut the long word at any separators of lower priority than the current one, # except the empty last-resort separator for (my $j=$i+1; $j<@separators-1; $j++) { # TODO: this is currently only optimal for fixed separators # of length 1 ($sepLength = 1) my $sepLength = 1; my $w0 = $cutPos - $sepLength; my $w1 = $w0 > 0 ? $w0 : 0; if ($postMatch =~ /^(\S{0,$w1}$separators[$j])/) { $cutPos = length($1); last; } } # ok, now do the splicing if ($cutPos>0) { my $substr = substr($postMatch, 0, $cutPos); substr($postMatch, 0, $cutPos) = ""; $match .= $spaces . $substr; } } } $newText = $newText . $prefix . $match . "\n"; $text = $postMatch; $prefix=$prefix2; next TEXT; } } } }; # Wrapping failed if ($main::opt_warn) { carp "TextFunc::wrapOn: Cannot wrap $text"; }; $newText = $text . "\n"; $text = ''; } $newText =~ s/ +$//mg; return $newText; } sub cleanLine { my $class = shift; my $text = shift; # Drop trailing spaces $text =~ s/\s+$//; chomp($text); if(length($text) != 2) { $text = substr $text, 5; } else { $text = undef; } return $text; } sub joinWith { my $self = shift; my($text, $with, $noAddAfter, $addBefore, @list) = @_; unless ($text) { $text = shift @list; }; for my $line (@list) { unless ($text =~ /$noAddAfter$/ && $line !~ /^$addBefore/) { $text .= $with }; $text .= $line; } return $text; } sub insertLineGroup { my $class = shift; my $textRef = shift; my $text = shift; my $pattern = shift; my $found = -1; my $i; # The easy case: Replace a text block with a new one. if ($$textRef =~ /$pattern/m) { $$textRef = $` . $text . $'; return 1; } # Nothing to replace found. Seek insertion place. for ($i = $#linePattern; $i>=0; $i--) { if ($pattern eq $linePattern[$i]) { $found = $i; last; } } if ($found == -1) { $main::opt_warn && carp "Could not insert $text into $$textRef"; return 0; } for ($i = $found; $i>=0; $i--) { if ($$textRef =~ /$linePattern[$i]/m) { $$textRef = $` . $& . $text . $'; return 1; } } if (defined $main::opt_warn) { $main::opt_warn >2 && carp "Prepended $text to $$textRef"; } $$textRef = $text . $$textRef; return 0; } sub uniqueList { my $class = shift; my @oldList = @_; my @newList; my $element; foreach $element(@oldList) { unless (grep{$_ eq $element} @newList) { push @newList, $element; } }; return @newList; } sub currentSpDate { my ($dummy, $mday, $month, $year); my %month2number = ('1'=>'JAN', '2'=>'FEB', '3'=>'MAR', '4'=>'APR', '5'=>'MAY', '6'=>'JUN', '7'=>'JUL', '8'=>'AUG', '9'=>'SEP', '10'=>'OCT', '11'=>'NOV', '12'=>'DEC'); ($dummy, $dummy, $dummy, $mday, $month, $year, $dummy, $dummy, $dummy) = localtime (time); if ($mday < 10) { $mday = '0' . $mday; } $month = $month2number{$month+1}; $year += 1900; return "$mday-$month-$year"; } # # Functions used to cleanup entries in annotators' jobs # Author : Alexandre Gattiker # #removes wild ** comments throughout an entry, except after a DR line #they can be reinserted again, based on the line that follows them. #returns an pointer to a hash of "following lines" => "wild comment" sub removeInternalComments { my $textRef = shift; my $newText = ""; my %lines; my $afterACID = 0; my $inEnd = 0; my $inRef = 0; my $inDR = 0; my @comments; #remove everything before the ID line if ($$textRef =~ s/(.*?)^ID/ID/sm) { $lines{_start} = $1; } for (split /\n/, $$textRef) { $_ .= "\n"; if ($inEnd || /SOURCE SECTION|INTERNAL SECTION|ANNOTATOR'S SECTION/) { #comments right before source section should go just inside $inEnd++; my (@textComments, @otherComments); for my $comment (@comments) { if ($comment =~ /\w/) { push @textComments, $comment; } else { push @otherComments, $comment; } } $newText .= join '', @otherComments, $_, @textComments; undef @comments; next; } if (/^AC|^ID/) { $afterACID=1; if (@comments) { $lines{$_}=[@comments]; splice @comments; } $newText .= $_; next; } #annotators' comment lines begin either with ** or ++ elsif (/^ ?\*\*|^ ?\+\+/ && !$afterACID and (!$inRef or !/NO TITLE|=None/) and !($inDR and /^\*\* \S+; \S+; \S+; /) ) { push @comments, $_; } else { $afterACID=0; if (@comments and /(\S.*)/) { $lines{$1}=[@comments]; splice @comments; } $newText .= $_; next; } } continue { $inRef = /^R/; $inDR = /^DR/ || ($inDR && /^\*/); }; $$textRef=$newText; return \%lines; } #does the opposite... #returns an array with the internal comments that could not be restored at their proper position. #the caller should do something like $entry->Stars->ZZ->add them. sub restoreInternalComments { my($textRef, $lines)=@_; #comments going before ID line my $before = delete $lines->{_start}; #other comments : add before the relevant line my @newText; for my $line (split /(?<=\n)/, $$textRef) { if ($line =~ /(\S.*)/ and my ($comments) = delete $$lines{$1}) { push @newText, _wrapInternalComments(@$comments); } push @newText, $line; } #remaining comments : try to add before the relevant block my @newText2; for my $line (@newText) { if ($line =~ /^\s*(\w\w)/) { my $lineTag = $1; for my $prevline (keys %$lines) { if ($prevline =~ /^\s*($lineTag)/) { my $comments = delete $$lines{$prevline}; push @newText2, _wrapInternalComments(@$comments); } } } push @newText2, $line; } $$textRef=$before . join "", @newText2; #return comments that could not be inserted return map{s/^\s*\*\*\s*//; s/\n$//; $_} map {@$_} values %$lines; } #wrap internal comments at 75 characters sub _wrapInternalComments { foreach (@_) { my ($prefix) = s/^(\W+)// ? $1 : ""; s/\s+$//; $_ = wrapOn (undef, $prefix, $prefix, $SWISS::TextFunc::lineLength, $_, '\s+') } @_; } sub toMixedCase { my ($text, @regexps) = @_; my $ok_regexp; for my $regexp (@regexps) { #This regexp is made complex by the need to convert e.g. "B0690/B0691" to "b0690/b0691" $text =~ s!(?:^|\G)($regexp)($|\/)! my @char = split //, $1; my $postfix = substr $text, $-[-1], $+[-1] - $-[-1]; #this fetches the content of the '($|\/)' part of the regexp as the last matched subgroup (i.e. the possible slash), see man perlre for "@-" for an explanation if ($1 =~ /^($regexp)$/) { #if it matches the regexp case-sensitively, no need to convert $1 . $postfix; #return value } else { my $num_letter=0; my @letter_pos; for (my $i=0; $i<@char; $i++) { $letter_pos[$i] = (uc ($char[$i]) ne lc $char[$i]) ? 1 : 0; $num_letter += $letter_pos[$i]; } my $string_ok; for (my $binary=0; $binary<2**$num_letter; $binary++) { #combinatorially change casing of each letter my $string = ""; my $j=0; for (my $i=0; $i<@char; $i++) { if ($letter_pos[$i]) { my $mask = 1<<$j; my $bin_value = ($binary & $mask) >> $j; $string .= $bin_value ? uc($char[$i]) : lc($char[$i]); $j++; } else { $string .= $char[$i]; } } $string_ok = $string, last if $string =~ /^(?:$regexp)$/; #case-sensitive match } if (defined $string_ok) { $string_ok . $postfix; #return value } else { #this should never happen warn "INTERNAL ERROR: Could not find correct casing for ".join("",@char)." ($regexp)"; join("",@char) . $postfix; #return value } } !egi or next; $ok_regexp = $regexp; last; } return wantarray ? ($text, $ok_regexp) : $text; } 1; __END__ =head1 NAME SWISS::TextFunc =head1 DESCRIPTION This module is designed to be a repository of functions that are repeatedly used during parsing and formatting of SWISS-PROT/TREMBL lines. If more than two line types need to do aproximately the same thing then it is probably in here. All functions expect to be called as package->function(param list) =over =item listFromText Takes a piece of text, a seperator regex and a seperator that may appear at the end. Returns an array of items that were seperated in the text by that seperator. Takes care of null items (looses them for you). =item textFromList Takes an array of items, a separator, a terminating string, and a line width. Returns an array of strings, each ending with the separator or the terminator with a width less than or equal to the width specified. Seems to do the wrong thing for references - not sure why. Don't use it for that. =item wrapText Takes a string and a length. Returns an array of strings which are shorter or equal in length to length, spliting the string on white space. =item wrapOn ($firstLinePrefix, $linePrefix, $colums, $text[, @separators]) Wraps $text into lines with at most $colums colums. Prepends the prefixes to the lines. @separators is a list of expressions on which to wrap. The expression itself is part of the upper line. If no @separators are provided, the $text is wrapped at whitespace except in EC/TC numbers or at dashes that separate words. First tries to wrap on the first item of @separators, then the next etc. If no wrap on any element of @separators or whitespaces is possible, wraps into lines of exactly length $colums. A special case is that the first item of @separators may be a reference to an array. This is used internally for wrapping FT VARIANT-like lines. Example: wrapOn('DE ', 'DE ', 40, '14-3-3 PROTEIN BETA/ALPHA (PROTEIN KINASE C INHIBITOR PROTEIN-1)', '\s+') returns ['14-3-3 PROTEIN BETA/ALPHA (PROTEIN ', 'KINASE C INHIBITOR PROTEIN-1)'] wrapOn('DE ', 'DE ', 40, '14-3-3 PROTEIN BETA/ALPHA (PROTEIN KINASE C INHIBITOR PROTEIN-1)', ' (?=\()', '\s+') returns ['14-3-3 PROTEIN BETA/ALPHA ', '(PROTEIN KINASE C INHIBITOR PROTEIN-1)'] =item cleanLine Remove the leading line Identifier and three blanks and trailing spaces from an SP line. =item joinWith ($text, $with, $noAddAfter, @list) Concatenates $text and @list into one string. Adds $with between the original elements, unless the postfix of the current string is $noAddAfter. This is used to avoid inserting blanks after hyphens during concatenation. So unpleasant strings like 'CALMODULIN- DEPENDENT' are avoided. Unfortunately a correct reassembly of strings like 'CARBON-DIOXIDE' is not done. =item insertLineGroup ($textRef, $text, $pattern) Inserts text block $text into the text referred to by $textRef. $text will replace the text block in $textRef matched by $pattern. =item uniqueList (@list) Returns a list in which all duplicates from @list have been removed. =item currentSpDate returns the current date in SWISS-PROT format =item toMixedCase($text, @regexps) Convert a text to mixed case, according to one or more regular expressions. In scalar context, returns the new text; in array context, also returns the regexp with which the change was performed, or undef on failure. See corresponding item in SWISS::GN for more details. =back Swissknife_1.75/lib/SWISS/RCelement.pm0000644005110600510130000000254410366115237017754 0ustar ecastroSwissProtpackage SWISS::RCelement; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( text => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $text = shift; # Parse out the evidence tags if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { my $tmp = $1; $self->evidenceTags($tmp); } $self->text($text); $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; return $self->text . $self->getEvidenceTagsString; } sub cleanText { my $self = shift; $self->{text} =~ s/^ *and +//; return; } 1; __END__ =head1 Name SWISS::RCelement.pm =head1 Description Each RCelement object represents one element of the RC line. The container object for all RCelements of an entry is SWISS::Ref. =head1 Inherits from SWISS::BaseClass =head1 Attributes =over =item C The text of the keyword. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Writing methods =over =item cleanText Remove potentially leading "and" from text. =back Swissknife_1.75/lib/SWISS/CCinteraction.pm0000644005110600510130000000646412225030622020616 0ustar ecastroSwissProtpackage SWISS::CCinteraction; use vars qw($AUTOLOAD @ISA); use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @ISA = ('SWISS::ListBase'); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCinteraction; my $text = $$textRef; $self->initialize(); $text =~ s/ +/ /g; $text =~ s/\s*-!-.*?:\s*//; while (length $text) { if ($text =~ s/^\s*(([\w\-]+):(.+?)( \(xeno\))?|Self)\s*(;\s+|;\Z)//so) { my ($t, $ac, $identifier, $xeno) = ($1, $2, $3, $4); my %arg; $arg{'accession'} = $t eq 'Self' ? $t : $ac; $arg{'identifier'} = $identifier if defined $identifier; $arg{'xeno'} = $xeno if defined $xeno; while ($text =~ s/^(NbExp|IntAct)=(.*?)\s*(;\s+|;\Z)//) { #take Note=, Vmax=, ... my ($field, $ltext) = ($1, $2); if ($field eq 'IntAct') { $arg{$field} = [split /, */, $ltext]; } else { $arg{$field} = $ltext; } } $self->push(\%arg); } else { #dangling text carp "CC INTERACTION parse error, ignoring $text"; last; } } $self->sort; $self->{_dirty} = 0; return $self; } sub sort { my ($self) = @_; if ($self) { my (@self, @nogene, @rest); for my $t ($self->elements) { if ($t->{accession} eq 'Self') {push @self, $t} elsif (not defined $t->{identifier}) {push @nogene, $t} else {push @rest, $t} } $self->set ( @self, (sort {lc $a->{accession} cmp lc $b->{accession}} @nogene), (sort { lc $a->{identifier} cmp lc $b->{identifier} || $a->{identifier} cmp $b->{identifier} || lc $a->{accession} cmp lc $b->{accession} || $a->{accession} cmp $b->{accession} } @rest) ); } } sub toString { my $self = shift; my $text = "-!- INTERACTION:\n" . $self->comment; $text =~ s/^/CC /mg; $text =~ s/ //; return $text; } sub topic { return "INTERACTION"; } sub comment { my ($self) = @_; my $text = ""; if ($self) { for my $el ($self->elements) { $text .= $el->{accession}; $text .= ":" . $el->{identifier} if defined $el->{identifier}; $text .= $el->{xeno} if defined $el->{xeno}; $text .= ";"; $text .= " NbExp=" . $el->{NbExp} . ";" if defined $el->{NbExp}; $text .= " IntAct=" . join (", ", @{$el->{IntAct}}) . ";" if defined $el->{IntAct}; $text .= "\n"; } } $text; } 1; __END__ =head1 Name SWISS::CCinteraction =head1 Description B represents a comment on the topic 'INTERACTION' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. Each element of the list is a hash with the following keys: accession identifier xeno NbExp IntAct (array reference) =head1 Inherits from SWISS::ListBase.pm =head1 Methods =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/OHs.pm0000644005110600510130000000312210437124062016553 0ustar ecastroSwissProtpackage SWISS::OHs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::ListBase; use SWISS::TextFunc; use SWISS::OH; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $textRef = shift; my $line; my @resources; if ($$textRef =~ /($SWISS::TextFunc::linePattern{OH})/m) { foreach $line (split /\n/m, $1) { $self->{indentation} += $line =~ s/^ //; $line = SWISS::TextFunc->cleanLine($line); push @{$self->list()}, SWISS::OH->fromText($line); } } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my $newText = ''; for (@{$self->list()}) { $newText .= 'OH ' . $_->toText . "\n"; } $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{OH}); } # OXs must never be sorted, overwrite the inherited sort method. sub sort { return 1; } 1; __END__ =head1 Name SWISS::OHs =head1 Description B represents the OH lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OHs object is a container object which holds a list of SWISS::OH objects. =head1 Inherits from SWISS::BaseClass.pm =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/GNs.pm0000644005110600510130000005304513147300251016557 0ustar ecastroSwissProtpackage SWISS::GNs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::GeneGroup; use Data::Dumper; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( and => " AND ", or => " OR " , ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub initialize { } sub fromText { my $self = new(shift); my $textRef = shift; my $line = ''; my @tmp; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'GN'})/m){ $line = join ' ', map { $self->{indentation} += $_ =~ s/^ //; SWISS::TextFunc->cleanLine($_); } (split /\n/m, $1 ); $line =~ s/\.$//; } $self->text($line); return $self; } sub is_old_format { my $self = shift; if (@_) { map {$_->is_old_format(@_)} $self->elements; } else { return grep {$_->is_old_format} $self->elements; } } sub toText { my $self = shift; my $textRef = shift; if ($self->is_old_format) { $self->is_old_format(1); return _toText_old($self, $textRef, @_); } $self->is_old_format(0); my $newText = ''; my @groups; for my $group (@{$self->list}) { my $groupText = $group->toText; my $prefix = "GN "; my $col = $SWISS::TextFunc::lineLength; $col++, $prefix=" $prefix" if $self->{indentation}; push @groups, SWISS::TextFunc->wrapOn($prefix, $prefix, $col, $groupText, ';\s+', ',\s+', '\s+'); } my $indent = $self->{indentation} ? " " : ""; $newText = join "${indent}GN and\n", @groups; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'GN'}); } sub _toText_old { my $self = shift; my $textRef = shift; my $newText = ''; if ($self->size){ $newText = $self->text; return $textRef if !defined $newText; $newText .= "."; #wrapping rules : # - whenever possible, wrap after AND. # - else, wrap before or after an OR or AND, so as to maximize the length of # the uppermost line. my $or = $self->or; my $and = $self->and; for ($or,$and) { s/^\s+//; s/\s+$//; $_ = quotemeta $_; } my $pat = "(?<= $or )|(?<= $and )| (?=$or |$and )"; my $prefix = "GN "; my $col = $SWISS::TextFunc::lineLength; $col++, $prefix=" $prefix" if $self->{indentation}; $newText = SWISS::TextFunc->wrapOn($prefix, $prefix, $col, $newText, "\\s+$and\\s+", $pat, ',\s+', '(?=\()', '\s+'); }; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'GN'}); } sub text { my $self = shift; my $text = shift; if (defined $text) { #reset GNs object from $text my $sep = $text =~ /^ *(?:Name|Synonyms|OrderedLocusNames|ORFNames)=/ ? "; and " : " and "; @{$self->list} = map {SWISS::GeneGroup->fromText($_)} split /$sep/i, $text; $self->{and} = $1 if $text =~ /( AND )/i; $self->{or} = $1 if $text =~ /( OR )/i; $self->{_dirty} = 0; if (defined $main::opt_gn_check) { if ($text ne $self->text) { print STDERR "Warning: SWISS::GNs->text could not interpret the following line : \n". "$text\nDo not define \$main::opt_gn_check to remove this message.\n"; } } return $text; } else { #simply return text @{$self->list} = grep {$_->size} @{$self->list}; my $addParen = $self->size>1; return undef unless $self->size; return join $self->and, map { my $a=$_->_toText_old($self->or); $a="($a)" if $addParen && @{$_->list}>1; $a } @{$self->list}; } } sub update { my $self = shift; my $force = shift; # force update if ($force) { # make sure that GN line is deleted on update if GN object has no gene names @{$self->list} = grep {$_->size} @{$self->list}; return undef unless $self->size; } $self->sort(); return 1; } sub sort { my $self = shift; return map {$_->sort(@_)} @{$self->list}; } sub get { my $self = shift; return map {$_->get(@_)} @{$self->list}; } sub lowercase { my $self = shift; $self->{and}=~tr/A-Z/a-z/; $self->{or}=~tr/A-Z/a-z/; } sub uppercase { my $self = shift; $self->{and}=~tr/a-z/A-Z/; $self->{or}=~tr/a-z/A-Z/; } sub getFirst { my ($self) = @_; if ($self->is_old_format) { for my $ggroup ($self->elements) { return ${$ggroup->list}[0]->text; } } else { for my $ggroup (@{$self->list}) { return ${$ggroup->list()}[0] -> text(); } } } sub getTags { # return evidnece tags associated with a given gene name my ($self, $target) = @_; if ($self->is_old_format) { for my $ggroup ($self->elements) { for (my $n=0;$n<$ggroup->size;$n++) { if (${$ggroup->list}[$n]->text eq $target) { return ${$ggroup->list}[$n]->getEvidenceTags; } } } } else { for my $ggroup (@{$self->list}) { for (my $n=0;$n<$ggroup->size;$n++) { if (${$ggroup->list()}[$n] -> text() eq $target) { my $tags = ${$ggroup->list()}[0] -> evidenceTags(); $tags =~ s/{|}|,//g; return $tags; } } } } return; } sub isPresent { # method to identify whether a given name is present in the GN object my ($self, $target) = @_; if ($self->is_old_format) { my ($self, $target) = @_; for my $ggroup ($self->elements) { for (my $n=0;$n<$ggroup->size;$n++) { if (${$ggroup->list}[$n]->text eq $target) { return 1; } } } } else { for my $ggroup (@{$self->list}) { for (my $n=0;$n<$ggroup->size;$n++) { if (${$ggroup->list()}[$n] -> text() eq $target) { return 1; } } } } return; } sub needsReCasing { # method to identify whether a given name is present in the GN object, but # not in mixed case # returns match in current state my ($self, $target) = @_; if ($self->is_old_format) { for my $ggroup ($self->elements) { for (my $n=0;$n<$ggroup->size;$n++) { my $existingName = ${$ggroup->list}[$n]->text; if ((uc $existingName eq uc $target) && ($existingName ne $target)) { return $existingName; } } } } else { for my $ggroup (@{$self->list}) { for (my $n=0;$n<$ggroup->size;$n++) { my $existingName = ${$ggroup->list()}[$n] -> text(); if ((uc $existingName eq uc $target) && ($existingName ne $target)) { return $existingName; } } } } return; } sub replace { # replaces the first occurance of a given gene name in a GN line with the # replacement name. my ($self, $newName, $target, $evidenceTag) = @_; # no safety check: allow for adding identical names (tag addition) if ($self->is_old_format) { for my $ggroup ($self->elements) { for (my $n=0;$n<$ggroup->size;$n++) { my $geneText = ${$ggroup->list}[$n]->text; if ($geneText eq $target) { ${$ggroup->list}[$n]->text($newName); # may want to keep old evidence tags when replacing, i.e. add > 1 my @tags = split /, /, $evidenceTag; ${$ggroup->list}[$n] -> setEvidenceTags(@tags); return; } } } } else { for my $ggroup (@{$self->list}) { for (my $n=0;$n<$ggroup->size;$n++) { my $name = ${$ggroup->list()}[$n]; if ($name -> text() eq $target) { $name -> text($newName); my @tags = split /, /, $evidenceTag; $name -> setEvidenceTags(@tags); return; } } } } return; } sub delete { my ($self, $target) = @_; my $groupCount = 0; if ($self->is_old_format) { for my $ggroup ($self->elements) { for (my $n=0;$n<$ggroup->size;$n++) { my $geneText = ${$ggroup->list}[$n]->text; if ($geneText eq $target) { if ($ggroup->size == 0) { # remove gene group splice (@{$self->list}, $groupCount, 1); } else { # remove synonym from group splice (@{$ggroup -> list}, $n, 1); } return; } } $groupCount++; } } else { for my $ggroup ($self->elements) { CHECK: for (my $nameSet = 0; $nameSet < 3; $nameSet ++) { my @names; if ($nameSet == 0) { @names = $ggroup->Names->elements(); } elsif ($nameSet == 1) { @names = $ggroup->OLN->elements(); } else { @names = $ggroup->ORFNames->elements(); } for (my $n=0;$n text() eq $target) { if ($ggroup->size == 0) { # remove gene group splice (@{$self->list}, $groupCount, 1); } else { # remove synonym from group splice (@names, $n, 1); if ($nameSet == 0) { @names = $ggroup->Names->list([@names]); } elsif ($nameSet == 1) { @names = $ggroup->OLN->list([@names]); } else { @names = $ggroup->ORFNames->list([@names]); } last CHECK; } } } } } } return; } sub addAsNewSynonym { # user should first check that target exists using 'isPresent'. If target is # not found, method does nothing # otherwise method either adds new name in the gene group containing the # target, according to the parameter specified in $location # location > 1: insert name in first, second, third position etc. # location = 0: insert name before target # location = -1: insert name after target (default) # location = -2: insert name at end of gene group my ($self, $newName, $target, $evidenceTag, $location) = @_; # safety check: don't add duplicate gene names if (isPresent($self, $newName)) { return; } if ($location eq '') { $location = -1; } my $GN = SWISS::GN -> new(); $GN -> text($newName); $GN -> addEvidenceTag($evidenceTag); if ($self->is_old_format) { GENEGROUPS: for my $ggroup ($self->elements) { for (my $n=0;$n<$ggroup->size;$n++) { my $geneText = ${$ggroup->list}[$n]->text; if ($geneText eq $target) { my $position; if ($location == 0) { $position = $n; } elsif ($location == -1) { $position = $n + 1; } elsif ($location == -2) { $position = $ggroup->size; } else { $position = $location - 1; } splice @{$ggroup->list}, $position, 0, $GN; last GENEGROUPS; } } } } else { GENEGROUPS: for my $ggroup ($self->elements) { for (my $n=0;$n<$ggroup->size;$n++) { my $name = ${$ggroup->list()}[$n]; if ($name -> text() eq $target) { my $position; if ($location == 0) { $position = $n; } elsif ($location == -1) { $position = $n + 1; } elsif ($location == -2) { $position = $ggroup->size; } else { $position = $location - 1; } splice @{$ggroup->list}, $position, 0, $GN; last GENEGROUPS; } } } } return; } sub addAsNewGeneGroup { # method adds a new gene name in a new gene group, $target and $location can # be used to specify where in line new group should go # otherwise method either adds new name in the gene group containing the # target, according to the parameter specified in $location # location > 1: insert group in first, second, third position etc. # location = 0: insert group before group containing target # location = -1: insert group after group containing target (default) # location = -2: insert group at end # note that 'addSynonym requires a target to be specified (always). # 'addAsNewGeneGroup' only requires a target if $location is 0 or -1 my ($self, $newName, $target, $evidenceTag, $location) = @_; # safety check: don't add duplicate gene names if (isPresent($self, $newName)) { return $self; } if ($location eq '') { $location = -1; } my $match = 0; my $position; my $GN = SWISS::GN -> new(); $GN -> text($newName); $GN -> addEvidenceTag($evidenceTag); my $newGeneGroup = SWISS::GeneGroup -> new(); if ($self->is_old_format) { push @{$newGeneGroup -> list}, $GN; } else { push @{$newGeneGroup -> list}, $GN; } if ($location < 1) { if ($location == -2) { $position = $self -> size(); $match++; } else { my $p = 0; $p = -1; if ($self->is_old_format) { GENEGROUPS: for my $ggroup ($self->elements) { $p++; for (my $n=0;$n<$ggroup->size;$n++) { my $geneText = ${$ggroup->list}[$n]->text; if ($geneText eq $target) { if ($location == 0) { $position = $p; } elsif ($location == -1) { $position = $p + 1; } $match++; last GENEGROUPS; } } } } else { GENEGROUPS: for my $ggroup ($self->elements) { $p++; for (my $n=0;$n<$ggroup->size;$n++) { my $geneText = ${$ggroup->list}[$n]->text; if ($geneText eq $target) { if ($location == 0) { $position = $p; } elsif ($location == -1) { $position = $p + 1; } $match++; last GENEGROUPS; } } } } } } else { $position = $location - 1; $match++; } if ($match == 1) { splice @{$self -> list}, $position, 0, $newGeneGroup; } return; } sub replaceGeneGroup { # replaces the first gene group containing $target with the gene group # supplied as a paramter my ($self, $newGeneGroup, $target) = @_; my $groups = 0; my $hit = 0; my $thisGroup; if ($self->is_old_format) { GENEGROUPS: for my $ggroup ($self->elements) { $groups++; for (my $n=0;$n<$ggroup->size;$n++) { my $geneText = ${$ggroup->list}[$n]->text; if ($geneText eq $target) { $thisGroup = $groups; $hit++; last GENEGROUPS; } } } } else { GENEGROUPS: for my $ggroup ($self->elements) { $groups++; for (my $n=0;$n<$ggroup->size;$n++) { my $geneText = ${$ggroup->list}[$n]->text; if ($geneText eq $target) { $thisGroup = $groups; $hit++; last GENEGROUPS; } } } } if ($hit > 0) { splice @{$self -> list}, $thisGroup -1, 1, $newGeneGroup; } } sub getGeneGroup { my ($self, $target) = @_; GENEGROUPS: for my $ggroup ($self->elements) { for (my $n=0;$n<$ggroup->size;$n++) { my $geneText = ""; if ($self->is_old_format) { $geneText = ${$ggroup->list}[$n]->text; } else { $geneText = ${$ggroup->list}[$n]->text; } if ($geneText eq $target) { return $ggroup; } } } } sub setToOr { # needed when adding C to 'A AND B', when the realtionship of C to A and B is # unknown: ' or ' os the default setting my ($self) = @_; my $GNs = SWISS::GNs -> new(); my $geneGroup = SWISS::GeneGroup -> new(); # maintain 'and' and 'or' values $GNs -> or($self -> or()); $GNs -> and($self -> and()); for my $ggroup ($self->elements) { for (my $n=0;$n<$ggroup->size;$n++) { push @{$geneGroup -> list}, ${$ggroup->list}[$n]; } } push @{$GNs -> list}, $geneGroup; return $GNs; } 1; __END__ =head1 Name SWISS::GNs.pm =head1 Description B represents the GN lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The GNs object is a container object which holds a list of SWISS::GeneGroup objects. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each list element is a SWISS::GeneGroup object. =item C I<(deprecated, for old format only)> Delimiter used between genes. Defaults to " AND ". =item C I<(deprecated, for old format only)> Delimiter used between gene names. Defaults to " OR ". =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Reading/Writing methods =over =item text [($newText)] Sets the text of the GN line to the parameter if it is present, and returns the (unwrapped) text of the line. Also sets 'and' and 'or' delimiters to the first occurrences of the words "OR" and "AND" in the line, conserving the case. =item lowercase I<(deprecated, for old format only)> Sets the GNs::and and GNs::or delimiters to their lower case values. =item uppercase I<(deprecated, for old format only)> Sets the GNs::and and GNs::or delimiters to their upper case values. =item getFirst() Returns first gene name in gene line =item getTags($target) Returns evidence tags associated with $target $target is a string =item isPresent($target) Returns 1 if $target is present in the GN line $target is a string =item needsReCasing($target) If $target is present in the GN line, but wrongly cased, method returns the matching name in its current case $target is a string =item replace($newName, $target, $evidenceTag) Replaces the first GN object in the GN line whose text attribute is $target with a new GN object whose text attribute is set to $newName and whose evidenceTags attribute is is set using values set by splitting $evidenceTag on /, / (as name is not being changed, programs should keep old tag and add new tag). Does nothing if $target is not found. =item delete($target) Removes synonym/single-member gene group matching $target. Note that if a "Name" is deleted, the first "Synonym" will be promoted to "Name" =item addAsNewSynonym($newName, $target, $evidenceTag, $location) Adds a new GN object (with text attribute set to new $newName, and evidenceTags attribute set to ($evidenceTag)), as a synonym to the first gene group in which $target is a gene name. Does nothing if $target is not found. Will not add a duplicate gene name. $location determines where in gene group new object is added: if $location == 1, 2, 3, ..., new object added in the 1st, 2nd, 3rd, ... position; if $location == 0, new object added before $target; if $location == -1, new object added after $target (default); if $location == -2, new object added at end of gene group. Note that if the new synonym is inserted in the first postion, it will become the "Name" and the previous "Name" will be downgraded to first "Synonym" =item addAsNewGeneGroup($newName, $target, $evidenceTag, $location) Adds a new GeneGroup object, comprising 1 GN object (with text attribute set to new $newName, and evidenceTags attribute set to ($evidenceTag)). Will not add a duplicate gene name. $location and $target determine where in GNs line new group is added: if $location == 1, 2, 3, ..., new object added in the 1st, 2nd, 3rd, ... position; if $location == 0, new object added before $target; if $location == -1, new object added after $target (default); if $location == -2, new object added at end of GNs line. Does nothing if $target is not found, and $location == 0 or -1; otherwise $target does not need to be set. =item replaceGeneGroup($newGeneGroup, $target) Replaces the first gene group containing $target with $newGeneGroup. Creating the $newGeneGroup correctly is the user's responsibility =item getGeneGroup($target) Returns the first gene group that contains $target =item setToOr() Retruns a new GNs object, but with all GNs objects in a single gene group. Needed when adding 'C' to 'A and B', when the relationship of 'C' to 'A' and 'B' is unknown: the universal use of ' or ' is the default delimeter for TrEMBL entries =back =head1 TRANSITION The format of the GN line will change in 2004 from: GN (CYSA1 OR CYSA OR RV3117 OR MT3199 OR MTCY164.27) AND (CYSA2 OR GN RV0815C OR MT0837 OR MTV043.07C). to: GN Name=CysA1; Synonyms=CysA; OrderedLocusNames=Rv3117, MT3199; GN ORFNames=MtCY164.27; GN and GN Name=CysA2; OrderedLocusNames=Rv0815c, MT0837; ORFNames=MTV043.07c; This module supports both formats. To convert an entry from the old to the new format, do: $entry->GNs->is_old_format(0); Swissknife_1.75/lib/SWISS/CC.pm0000644005110600510130000002010512602234675016357 0ustar ecastroSwissProtpackage SWISS::CC; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::BaseClass; use SWISS::TextFunc; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( topic => undef, comment => undef, # comment str (without evs) blocks => undef # [ [ comment_block_str, ev_str ] ] ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub parse2Blocks { # class / static method: comment : String -> [ [ String, String ], ... ] # parse a (multi) [ block, block-ev ] comment (free text comment or Note= from structured comments, or even structured txt elems with one ev for "symetrical" parsing) into array of comment, ev pairs (as array) my $comment = shift; my @blocks; foreach my $elem ( split( $SWISS::TextFunc::evidencePatternAsSep, $comment ) ) { # split on evtag as sep! (includes evtag content in split output) if ( $elem !~ /^ECO:\d+/ ) { push @blocks, [ $elem, "" ] } # a blocktxt = ~sentence elsif ( ref( $blocks[ -1 ] ) eq 'ARRAY' ) { $blocks[ -1 ]->[ 1 ] = $elem } # EV(s) for the blocktxt else { push @blocks, [ $elem, "" ]; } # bad should not happen (block has first elem - should be txt - recognized as ev! save it as txt) } # one block = e.g. [ "Involved in riboflavin biosynthesis", "ECO:0000269|PubMed:22081402, ECO:0000269|PubMed:23203051" ] return \@blocks; } # p.s. a txt without ev will keep its final "." (as evidencePatternAsSep wont eat it) whereas when there is an ev the "." is gone!... (is selfhealing with blocks2String but asymetrical! ? TODO FIXME ?) sub fromText { my $_class = shift; my $textRef = shift; my $self = new SWISS::CC; my $text = $$textRef; my ( $topic, $comment ); if ($text ne '') { # split into topic and comment. if ($text =~ /\-\!\-\s+(.*?):\s*(.*)$/x ){ $topic = $1; $comment = $2; } else { $topic = ''; $comment = $text; } my $has_new_style_ev = $comment =~ /ECO:/; # Parse if ( $topic ne "MASS SPECTROMETRY" ) { # free text comment $self->{ blocks } = parse2Blocks( $comment ); } else { # TODO? create module for mass spec: CCmass_spec.pm to model individual fields! here just a big txt blob!... my $evs = ""; $evs = $1 if $comment =~ s/ Evidence=\{(.+)\}[;.]?\s*$/ Evidence=/; $self->{ blocks } = [ [ $comment, $evs ] ]; } # set evidenceTags 4 compatibility with existing ...EvidenceTag methods in BaseClass! + old tests (fixme: clean/remove that mess!?) # but the real evidences are now within blocks (2nd field of block array) my @evs = map { split /, ?/, $_->[1] } grep { $_->[1] } @{ $self->{ blocks } }; my $ev = $has_new_style_ev ? " {" . join( ", ", @evs ) . "}" : "{" . join( ",", @evs ) . "}"; $self->evidenceTags( $ev ) if @evs; $self->{ topic } = $topic; $self->{ comment } = join( ". ", map { $_->[0] } @{ $self->{ blocks } } )."."; # build comment (all sentences) string without evs! } else { $self->initialize; } $self->{ _dirty } = 0; return $self; } sub blocks2String { # class / static method: blocks : [ [ String, String ], ... ] -> String # serialize back to string sentence-ev blocks my $blocks = shift; my $ev4compat = shift; my $termin = shift; ;#shift // "."; # // does not work with old perl $termin = "." unless defined( $termin ); # defaut "." for real free text. multi/single sentence-ev in stuctured txt might need distinct sentence terminator (generaly "") my $has_new_style_ev = grep { $_->[1] =~ /ECO:/ } @$blocks; my $core = ""; if ( $ev4compat && $ev4compat ne "{}" && @$blocks == 1 ) { # if ev4compat (ev comming from evidenceTag method/field on BaseClass) not empty and there is only one block (= old non block style or new style with one block): # use this ev4compat instead evs stored in blocks! To be compatible with ev manip via "old" BaseClass::...EvidenceTag methods. FIXME: remove that mess!? $core = $blocks->[0]->[0] . ( $ev4compat =~ /^ / ? "." : "" ) . $ev4compat; } elsif ( $has_new_style_ev ) { $core = join ". ", map { $_->[0] . ( $_->[1] ? "${termin} {$_->[1]}" : "" ) } @$blocks; } else { $core = join ". ", map { $_->[0] . ( $_->[1] ? "${termin}{$_->[1]}" : "" ) } @$blocks; } return $core; } sub toString { my $self = shift; my $topic = $self -> {topic}; my $core = ""; if ( $topic ne "MASS SPECTROMETRY" ) { $core = blocks2String( $self->{ blocks }, $self -> evidenceTags ); } else { my $evs = $self->{ blocks }->[0]->[1]; $evs = "{".$evs."}" if $evs; $core = $self->{ blocks }->[0]->[0].$evs; } my $text = "CC -!- "; $text = $text . $topic . ": " if $topic; $text = $text . $core if $core; # specific fix for dealing with the format of 1 special CC section # note in general text wraping in comments is not guaranteed to be read-safe # by SWISSKNIFE # this specific fix keeps wrapping correct for 1 structured CC line # a better alternative would be to implement this section as a new class if ( defined( $topic ) and $topic =~ /^WEB RESOURCE|MASS SPECTROMETRY$/ ) { my $newText = ""; sub wrap { my $str = shift or return; my $has_head = shift; $str = ( $has_head ? '' : 'CC ' ).$str; $str =~ s/([\w\?] -)([A-Z])/$1 $2/g; # when ori line = ...Note=Molecular embrace -\n...Issue => # str will = Note=Molecular embrace -Issue => # put back space between - and Issue ... return SWISS::TextFunc->wrapOn('', "CC ", $SWISS::TextFunc::lineLength, $str ); } my @towrap; my $has_head = 1; foreach my $elem (split /;\s*/, $text) { unless ($elem =~ /https?:\/\/|[st]?ftp:\/\//) { # normal element, can be wrapped #$elem = "\n".$elem if $elem =~ /^Note=/; push @towrap, $elem; } else { # url non wrapable str: put it on a new line (without wrap) # FIXME: shoudn't SWISS::TextFunc->wrapOn do this! # wrap what's before elem: $newText .= wrap(join('; ',@towrap).';',$has_head) if @towrap; @towrap = (); $has_head = 0; # add element on new line $elem = 'CC '.$elem unless $elem =~ /^CC /; $newText .= $elem.";\n"; } } if (@towrap) {# add remaining txt if any $newText .= wrap(join('; ',@towrap).';',$has_head); } return $newText; } else { # for all other CC block: just warp the whole block (here large 'words' might # be wrapped on 2 lines) $text .= '.'; $text = SWISS::TextFunc->wrapOn('',"CC ", $SWISS::TextFunc::lineLength, $text); return $text; } } sub topic { my ($self,$value) = @_; if (defined $value) { $self->{'topic'} = $value; } return $self->{'topic'}; } sub comment { my ($self,$value) = @_; if (defined $value) { $self->{'comment'} = $value; } return $self->{'comment'}; } 1; __END__ =head1 Name SWISS::CC.pm =head1 Description B represents a comment on a single topic within a SWISS-PROT or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Each comment is stored in a separate object, either of the type SWISS::CC or of another type, depending on its topic (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item topic The topic of this comment. =item comment The text of this comment. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/OSs.pm0000644005110600510130000001214713147300251016572 0ustar ecastroSwissProtpackage SWISS::OSs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::OS; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub initialize { } sub fromText { my $self = new(shift); my $textRef = shift; my $line; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'OS'})/m){ $line = $1; $self->{indentation} = $line =~ s/^ //mg; $line = SWISS::TextFunc->joinWith('', ' ', '(?cleanLine($_)} (split "\n", $line)); $line =~ s/\.\r?\n?$//; push (@{$self->list()}, SWISS::OS->fromText( $line ) ); # n.b. identical entries from distinct species are not merged anymore # one entry has only one species! but keep OSs as a list of OS elems # to keep compatibility with old code! #@tmp = SWISS::TextFunc->listFromText($line, ',\s+(?i:and\s+)?(?![^\(]+\))', '\.'); #@tmp = map {SWISS::OS->fromText($_)} @tmp; #push (@{$self->list()}, @tmp); } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my @tmp; my $newText = ''; if ($self->size > 0) { @tmp = map {$_->toText} $self->elements(); # Add commas as separators map {$_ .= ','} @tmp; # delete last comma $tmp[$#tmp] =~ s/\,$//; # drop trailing spaces and dots # (Rattus SP.) $tmp[$#tmp] =~ s/[\. ]+(($SWISS::TextFunc::evidencePattern)*$)/$1/m; # add final dot $tmp[$#tmp] .= '.'; # insert an 'and' after the last but one species if ($#tmp > 0) { $tmp[$#tmp-1] .= ' and'; } # wrap lines where one OS extends beyond one line for (my $i=0; $i<@tmp; $i++) { my $prefix = "OS "; my $col = $SWISS::TextFunc::lineLength; $col++, $prefix=" $prefix" if $self->{indentation}; $tmp[$i] = SWISS::TextFunc->wrapOn($prefix, $prefix, $col, $tmp[$i], '\s+'); } # connect all OS lines $newText = join('', @tmp); }; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'OS'}); } # OSs must never be sorted, overwrite the inherited sort method. sub sort { return 1; } # convert scientific name to the abbreviated form as it is used # in the RC SPECIES line # input $scientific: Full scientific name (e.g. 'Escherichia coli') # $superregnum: 'V' for viruses, 'E' for eukaryotes etc. # (By now, only 'V' or not 'V' is important # returns abbreviated name (e.g. 'E.coli') sub scientific2rc { my $scientific = shift; my $superregnum = shift; unless ($scientific) { croak "No input"; return undef; } my $rc = $scientific; my %common= ('RATTUS NORVEGICUS' => 'Rat', 'HOMO SAPIENS' => 'Human', 'MUS MUSCULUS' => 'Mouse', 'BOS TAURUS' => 'Bovine', 'GALLUS GALLUS' => 'Chicken', 'SUS SCROFA' => 'Pig', 'ORYCTOLAGUS CUNICULUS' => 'Rabbit', 'OVIS ARIES' => 'Sheep', 'ZEA MAYS' => 'Maize', 'EQUUS CABALLUS' => 'Horse', 'GLYCINE MAX' => 'Soybean', ); if ($superregnum eq 'V') { $rc =~ s/\bBACTERIO(PHAGE)/$1/i; return $rc; } else { my $common = $common{uc($scientific)}; return $common if $common; return $scientific if $scientific =~ /^\w+ SP\.$/i; my $done = 0; die "no input" unless $rc; $done ||= ($rc =~ s/^(\w)\w+ ([A-Z\-]+)$/$1.$2/i); $done ||= ($rc =~ s/^(\w)\w+ (\w)[A-Z\-]+ ([A-Z\-]+)$/$1.$2.$3/i); $done ||= ($rc =~ s/^(\w)\w+ \(STRAIN (.*)\)$/$1.$2/i); $done ||= ($rc =~ s/^(\w)\w+ SP\. \(STRAIN (.*)\)$/$1.$2/i); $done ||= ($rc =~ s/^(\w)\w+ SP\.$/$1.$2/i); $done ||= ($rc =~ s/^(\w)\w+ X ([A-Z\-]+)$/$1.$2/i); if (!$done){ my $infix; foreach $infix ('SUBSP\.','STRAIN','VAR\.','PV\.','BIOVAR', 'BV\.','F\. SP\.' ){ $done ||= ($rc =~ s/^(\w)\w+ (\w)[A-Z\-]+ $infix (.*)$/$1.$2.$3/i); $done ||= ($rc =~ s/^(\w)\w+ (\w)[A-Z\-]+ \($infix (.*)\)$/$1.$2.$3/i); last if $done; } } return $done ? $rc : ''; } } 1; __END__ =head1 Name SWISS::OSs =head1 Description B represents the OS lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OSs object is a container object which holds a list of SWISS::OS objects. n.b. entries from distinct species are not merged anymore, OSs will therefore only contain one OS (OS is still divided into a list of OS elements to keep compatibility with old code)! =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each list element is a SWISS::OS object. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/OS.pm0000644005110600510130000000235510366115237016417 0ustar ecastroSwissProtpackage SWISS::OS; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( text => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $text = shift; # Parse out the evidence tags if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { my $tmp = $1; $self->evidenceTags($tmp); } # reset the dot of terms like sp., but not of "Bacteriophage SP" $text =~ s/(( sp)|( spp)|( s\.n))\Z/$1\./; $self->text($text); return $self; } sub toText { my $self = shift; return $self->text . $self->getEvidenceTagsString; } 1; __END__ =head1 Name SWISS::KWs =head1 Description B represents one organism name from the OS line. The container object holding all organism lines is SWISS::OSs. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C One organism name. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/DEs.pm0000644005110600510130000006407612132737553016565 0ustar ecastroSwissProtpackage SWISS::DEs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::DE; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ('text' => undef, 'hasFragment' => undef, 'isPrecursor' => undef, 'version' => undef, 'Contains' => undef, 'Includes' => undef, 'is_old_format' => undef, ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); $self->Contains (new SWISS::ListBase); $self->Includes (new SWISS::ListBase); $self->{is_old_format} = 0;# now the default is new format return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::DEs; my $line = ''; my $evidence = ''; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'DE'})/m) { $line = $1; $self->{indentation} = $line =~ s/^ //mg; # if not new DE format unless($line =~ / RecName:| AltName:| SubName:| Flags:/) { # is old format $self->{is_old_format} = 1; $line = SWISS::TextFunc->joinWith('', ' ', '(?cleanLine($_)} (split "\n", $line)); # Drop trailing spaces and dots $line =~ s/[\. ]*$//; } else { $self->{is_old_format} = 0; } }; if ($self->{is_old_format}) { # Parse for evidence tags if (($evidence) = $line =~ /($SWISS::TextFunc::evidencePattern)/m) { $line =~ s/$evidence//m; $self->evidenceTags($evidence); } } $self->{text} = $line; $self->{is_old_format} = 1 unless $line; $self->advancedParse(); $self->{_dirty} = 0; return $self; } sub fromString { my $class = shift; my $string = shift; my $is_old_format = shift; my $self = new SWISS::DEs; $self->{text} = $string; $self->{is_old_format} = $is_old_format; $self->advancedParse; $self->{_dirty} = 0; return $self; } sub text { my $self = shift; my $text = shift; if ($text) { $self->{_dirty} = 1; $self->{text} = $text; $self->{is_old_format} = ($text =~ /RecName:|AltName:|SubName:|Flags:/ ? 0 : 1); $self->advancedParse; } else { $text = $self->toString(); } return $text; } sub to_old_format { my $self = shift; $self->{is_old_format} = 1; $self->{_dirty} = 1; # stupid: in old format we want EC before short, in new they are after sub move_back_ec { my $de = shift or return; my $j=0; for (my $i=0;$i[$i]->{is_old_format} = 1; if ($de->[$i]->{type} eq 'Short') { $j++; } elsif ($de->[$i]->{type} eq 'EC' && $j) { my $tmp = $de->[$i]; for (my $k=0;$k<$j;$k++) { next if $i-$k <2; $de->[$i-$k] = $de->[$i-$k-1] } $de->[$i-$j] = $tmp;# put EC at beginning } else { $j=0; } } } if ($self->isPrecursor) { my $txt = $self->head->text; $self->head->text($txt . ' precursor') unless $txt =~ /precursor$/i; } foreach my $de ($self->{list}) { move_back_ec($de); } foreach my $dess ($self->Contains->{list}) { foreach my $des (@$dess) { foreach my $de ($des->{list}) { move_back_ec($de); } } } foreach my $dess ($self->Includes->{list}) { foreach my $des (@$dess) { foreach my $de ($des->{list}) { move_back_ec($de); } } } # FIXME: evtags (are flag evt!) remove them? } sub advancedParse { my $self = shift; # if is new format return $self->advancedParseNew() unless $self->{is_old_format}; # parse old format my $t = $self->{text}; $self->initialize; my($hasFragment, $version); #1)version if ($t =~ s/\s*\((Version \S+)\)//i) { $version = $1; } $self->version($version); #2)fragment if ($t =~ s/\s*\((Fragments?)\)//i) { $hasFragment = $1; } $self->hasFragment($hasFragment); #3)children $self->Contains->set(); $self->Includes->set(); #protect internal [] by converting to {- -} 1 while $t =~ s/(\[[^\[\]]*)\[(.*?)\]/$1\{-$2-\}/; #parse Contains/Includes while ($t =~ s/\s*\[((?:Contains)|(?:Includes)):\s*(.*?)\]//i) { my $type = lc $1 eq "contains" ? $self->Contains : $self->Includes; $type->push( map { s/\{-/[/g; s/-\}/]/g; SWISS::DEs->fromString($_,1); } split /;\s*/, $2); } # convert protected brackets back to original form $t =~ s/\{-/[/g; $t =~ s/-\}/]/g; #4)list #protect internal () by converting to {- -} 1 while $t =~ s/(\([^\(\)]*)\((.*?)\)/$1\{-$2-\}/; #must reverse before parsing to match successively all exprs between () $t = reverse $t; my $ev = $SWISS::TextFunc::evidencePatternReversed; while ($t =~ s/^($ev)?\)(.*?)\(\s+//) { my $a = $3; #$2 is set by the evidence pattern $a = $1.$a if $1; #evidence tag $a =~ s/-\{/\(/g; $a =~ s/\}-/\)/g; $self->unshift(SWISS::DE->fromText(scalar reverse $a)); } # convert protected brackets back to original form, # then add remaining text $t =~ s/-\{/\(/g; $t =~ s/\}-/\)/g; $self->unshift(SWISS::DE->fromText(scalar reverse $t)); # note: even if {text} is empty (no DE line) there will be a DE obj # so head method will work } sub advancedParseNew { # advance parsing for new format # Note: the new format is saved into the old simple structure !... # Code will work ~ the same with both format. # Adding a DE in the new format will just require specifying # category (RecName, AltName, SubName) and type (Full, Short, EC, Allergen, # CD_antigen) in DE stored in DEs my $self = shift; $self->Contains->set(); $self->Includes->set(); $self->initialize; my $by_mode = {# dispatch table to save new data into old structure 'Main' => sub { my ($str,$is_new_list,$cat,$type,$hide_in_old,$n) = @_; my $de = SWISS::DE->fromText($str); $de->category($cat); $de->type($type); $de->hide_in_old($hide_in_old); $de->{ _grp_n } = $n; $self->push($de); }, 'Contains' => sub { my ($str,$is_new_list,$cat,$type,$hide_in_old,$n) = @_; my $obj = $self->Contains; if ($is_new_list) { # is new contains: create new DEs to add names my $contains = new SWISS::DEs; $obj->push($contains); } # add DE (from str) to DEs(listbase) my $de = SWISS::DE->fromText($str); $de->category($cat); $de->type($type); $de->hide_in_old($hide_in_old); $de->{ _grp_n } = $n; $obj->item(-1)->push($de); }, 'Includes' => sub{ my ($str,$is_new_list,$cat,$type,$hide_in_old,$n) = @_; my $obj = $self->Includes; if ($is_new_list) { my $inludes = new SWISS::DEs; $obj->push($inludes); } my $de = SWISS::DE->fromText($str); $de->category($cat); $de->type($type); $de->hide_in_old($hide_in_old); $de->{ _grp_n } = $n; $obj->item(-1)->push($de); } }; my $process_txt_by_type = { # transform name string into the old format (so that new format could be # converted into old one, if needed [transitory period]) 'EC' => sub { my $str = shift or return; return "EC $str"; }, 'Allergen' => sub { my $str = shift or return; return "Allergen $str"; }, 'CD_antigen' => sub { my $str = shift or return; return "$str antigen"; } }; my $raw = $self->{text}; my $mode = 'Main'; my $is_new_list; my $cat = ''; my @flags; my $cd_antigen_outside = {}; my $grp_n = 0; foreach my $line (map {s/^DE //;$_} split '\r?\n',$raw) { if ($line =~ /^(Contains|Includes)/) {# Contains: | Includes: $mode = $1; $is_new_list = 1; next; } if ($line =~ /^Flags:\s+(.+)/) {# flags (Precursor, Fragment, Fragments) my $flags = $1; @flags = map { if (/($SWISS::TextFunc::evidencePattern)/m) { # store flag evtag as evtag for DEs self obj itself! (hack) my $ev = $1; $self->addEvidenceTag($ev); s/\Q$ev//;# strip evtag } # store hasFragment if (/(Fragments?)/) { $self->hasFragment(my $flag = $1);# !($1) doesn't work } # store isPrecursor $self->{isPrecursor} = 1 if /^precursor/i; $_; } sort {$b cmp $a} split '; *', $flags; next; } if ( $line =~ s/^ *(\w+): *// and !( $cat eq 'RecName' && $cat eq $1 ) ) { $cat = $1 ;# category: RecName: | AltName: $grp_n++; # increment group counter. ... to help distinguish grps; # generaly useless! (as grps can be detected by a change in cat # or type ne 'Short' nor 'EC' and as DEs built with SK won't # have this field set) except when parsing an existing entry DE # with Full missing from a Short / EC grp (curation error)... # (but do not inc grp if >1 RecName in a row...) } my ( $type, $val ) = split /= */, $line, 2; $type =~ s/\s+//g;# type: Full | Short | EC | Allergen | CD_antigen $val =~ s/;\s*$//g;# value: name/descriptor $cd_antigen_outside->{$1} = 1 if $type ne 'CD_antigen' && $val =~ /^(CDw?\d+) antigen/; my $hide_in_old = $type eq 'CD_antigen' && $cd_antigen_outside->{ $val } ? 1 : 0; # put data into old structure, so that new format could be converted # into old one!! (therefore structure of new format can only be deduced # by analazing category and type fields of elements in a simple list!) $val = $process_txt_by_type->{ $type }->( $val ) if $process_txt_by_type->{ $type }; $by_mode->{ $mode } ->( $val,$is_new_list,$cat,$type, $hide_in_old, $grp_n ) if $by_mode->{ $mode }; $is_new_list = 0; } } sub toString { my $self = shift; # if is new format return $self->toStringNew() unless $self->{is_old_format}; # rebuild old format my $newText = ''; if ($self->size > 0) {# Main names map {$_->{is_old_format} = 1} $self->elements; $newText = join(' ', $self->head->toText, grep {$_} map {$_->toText(1)} $self->tail); } # Includes/Contains for my $p (["Includes", $self->Includes], ["Contains", $self->Contains]) { my ($type, $obj) = @$p; next unless $obj->size; $newText .= ' ' if $newText; my $text = join '; ', grep {$_} map {$_->{is_old_format} = 1; $_->toString} $obj->elements; $newText .= "[$type: $text]"; } for ($self->hasFragment, $self->version) { next unless $_; $newText .= ' ' if $newText; $newText .= '(' . $_ . ')'; } return $newText; } sub toStringNew { my $self = shift; my $str_out = ''; my @flags; my $process_txt_by_type = { # transform stored name string (always old format! except Full, like old txt # but without 'precursor' at the end) into clean new names 'Full' => sub { my $str = shift or return; my $i = shift;# position #push @flags, 'Precursor' # if defined($i) && !$i # && $str =~ s/ precursor$//; return $str; }, 'EC' => sub { my $str = shift or return; $str =~ /^EC (\d.*)/; return $1; }, 'Allergen' => sub { my $str = shift or return; $str =~ /^Allergen (.*)/; return $1; }, 'CD_antigen' => sub { my $str = shift or return; $str =~ /^(.+) antigen$/; return $1; } }; my $main = new SWISS::DEs; # build main, includes, contains foreach my $d ( [ '' , ( $main->push($self) and $main ) ], [ 'Includes', $self->Includes ], [ 'Contains', $self->Contains ]) { my ($mode, $obj) = @$d; next unless $obj->size; my $indent = $mode ? ' ' : ''; foreach my $grp ( $obj->elements ) { $str_out .= "$mode:\n" if $mode; my $last_cat = ''; my $last_grp_n = 0; my $i = 0; foreach my $de ($grp->elements) { my $txt = $de->text() or next; my $ev = $de->getEvidenceTagsString() || ''; my $cat = $de->category() || ($i ? '???????' : 'RecName'); my $type = $de->type() || ($i ? '????' : 'Full'); my $grp_n = $de->{ _grp_n }; $str_out .= ( ($type ne 'Short' && $type ne 'EC') || $cat ne $last_cat || ( $grp_n && $grp_n != $last_grp_n ) ? "$indent$cat: " : "$indent " ); $txt = $process_txt_by_type->{ $type }->( $txt, $i ) if $process_txt_by_type->{ $type }; $str_out .= "$type=$txt$ev;\n"; $i ++; $last_cat = $cat; $last_grp_n = $grp_n; } } } # build flags push @flags, "Precursor" if $self->isPrecursor; push @flags, $self->hasFragment if $self->hasFragment; # add flag evtag (stored as DEs self evtags! if (my @flag_evtag = $self->getEvidenceTags()) { my $i = 0; @flags = map { my $ev = $flag_evtag[$i++] || ''; $ev = "{$ev}" if $ev; $_.$ev; } @flags; } $str_out .= 'Flags: '.join('; ',@flags).";\n" if @flags; chomp $str_out; return $str_out; } sub toText { my $self = shift; my $textRef = shift; unless ($self->{_dirty}) { return; } unless ($self->{is_old_format}) { # new format my $out_str = ''; my $prefix = "DE ";$prefix=' '.$prefix if $self->{indentation}; # FIXME: evtag in new format? foreach my $line (split '\r?\n',$self->toString) { $out_str .= $prefix.$line."\n"; } $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $out_str, $SWISS::TextFunc::linePattern{'DE'}); } my $newText = $self->toString . $self->getEvidenceTagsString; $newText .= "." if $newText; my $prefix = "DE "; my $col = $SWISS::TextFunc::lineLength; $col++, $prefix=" $prefix" if $self->{indentation}; $newText = SWISS::TextFunc->wrapOn($prefix, $prefix, $col, $newText); $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'DE'}); }; sub sort {# sort DE elements # - within "groups" sort Full first then Short, then EC (if any) # - within same types (Full, Short, EC) (within a grp), sort alphabetically # - sort AltName grps alphabetically by their Full (SDU-1000) # - for Allergen, Biotech, CD_antigen, INN AltNames grps; put them at the end: # Allergen first, then Biotech, CD_antigen, INN # - within multiple occurances of allergen, Biotech, CD_antigen, INN: sort # alphabetically # # (SDU-810) + new 'rule' with SDU-1000 # # n.b. "group": names listed after distinct Rec/SubName|AltName: # (e.g. Full,Short,EC under the same Rec/SubName|AltName) # (Allergen, Biotech, CD_antigen, INN each represent distinct groups) # # n.b. does not sort old DE format (<=2008) my $self = shift; return if $self->{ is_old_format }; # only sort DEs in new format! $self->{ _dirty } = 1; my $order = { # order for normal (non Allergen, Biotech, CD_antigen, INN) # name "groups" 'Full'=> 1, 'Short'=> 2, 'EC'=> 3, }; my $sort_des = sub { my $des = shift or return;# array ref to list of DE # first sort/fix Full/Short/EC position within groups # (so that Full is always first) foreach my $de ( @$des ) { my $type = $de->type; # (sub field order: Full, Short then EC, inside multiple Short/EC: # sort alphabetically) $de->{ __a } = $de->{ _grp_n } . ( $order->{ $type } || '?' ) . $de->text; } @$des = sort { $a->{ __a } cmp $b->{ __a }; } @$des; # sort (normal) AltName "grp" by their full, # put Allergen, Biotech, CD_antigen, INN at the end... # Rec|SubName at the beginning my $base_name = ''; my $last_grp_n = 0; foreach my $de (@$des) { my $cat = $de->category; my $type = $de->type; my $grp_n = $de->{ _grp_n }; if ( $cat eq 'RecName' or $cat eq 'SubName' ) { # Rec|SubName stay at the beginning $de->{ __a } = ' ' . $cat; } elsif ( $order->{ $type } ) { # (normal) AltName "grp" $base_name = $de->text if ( $grp_n && $grp_n != $last_grp_n ) || ( !$grp_n && $type eq 'Full' ); # memorize Full (1st) name of the "grp" to sort on it... # (nb. use first name in group, if Full is missing # will use first available name!) # if no DE has no _grp_n (not created by parsing an entry) # use Full field... $de->{ __a } = $base_name;# will be case insensitive sort } else { # (AltName) Allergen, Biotech, CD_antigen, INN stay at the end # (also use type + text so that multiple instances of the same type # will be sorted alphabetically) $de->{ __a } = '~' . $type . $de->text; } $last_grp_n = $grp_n; } @$des = sort { $a->{ __a } cmp $b->{ __a }; } @$des; }; # sort main names $sort_des->( $self->{ list } ); # sort contains names foreach my $desl ( $self->Contains->{ list } ) { foreach my $des ( @$desl ) { $sort_des->( $des->{ list } ); } } # sort includes names foreach my $desl ( $self->Includes->{ list } ) { foreach my $des ( @$desl ) { $sort_des->( $des->{ list } ); } } return 1; } # for old DE format # methods acting on evidence tag can be applied either to the entire DE line # (pass a string) or to each element (passing an ARRAY reference). # with new DE format: used to store Flags ev tag!, DE element ev tag are stored # in corresponding DE object itself sub addEvidenceTag { return ref $_[1] eq 'ARRAY' ? SWISS::ListBase::addEvidenceTag (@_) : SWISS::BaseClass::addEvidenceTag (@_) } sub deleteEvidenceTags { return ref $_[1] eq 'ARRAY' ? SWISS::ListBase::deleteEvidenceTags (@_) : SWISS::BaseClass::deleteEvidenceTags (@_) } sub getEvidenceTags { return ref $_[1] eq 'ARRAY' ? SWISS::ListBase::getEvidenceTags (@_) : SWISS::BaseClass::getEvidenceTags (@_) } sub getEvidenceTagsString { return ref $_[1] eq 'ARRAY' ? SWISS::ListBase::getEvidenceTagsString (@_) : SWISS::BaseClass::getEvidenceTagsString (@_) } sub hasEvidenceTag { return ref $_[1] eq 'ARRAY' ? SWISS::ListBase::hasEvidenceTag (@_) : SWISS::BaseClass::hasEvidenceTag (@_) } sub setEvidenceTags { return ref $_[1] eq 'ARRAY' ? SWISS::ListBase::setEvidenceTags (@_) : SWISS::BaseClass::setEvidenceTags (@_) } 1; __END__ =head1 Name SWISS::DEs.pm =head1 Description B represents the DE lines of a UniProt Knowledgebase (Swiss-Prot + TrEMBL) entry as specified in the user manual http://www.expasy.org/sprot/userman.html. The DEs object basically holds lists of DE objects, each of them representing a protein name element. The C, C, C and C attributes/methods work as follows : DE RecName: Full=CAD protein; DE Short=CAD; DE AltName: Full=Protein rudimentary; DE Includes: DE RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase; DE EC=6.3.5.5; DE Includes: DE RecName: Full=Aspartate carbamoyltransferase; DE EC=2.1.3.2; DE Flags: Fragment; -= Entry::DEs =- elements (for each DE object, see SWISS::DE.pm documentation) : toText: "CAD protein", "CAD", "Protein rudimentary" category: "RecName", "RecName", "AltName" type: "Full", "Short" "Full" hasFragment : "Fragment" Includes : ListBase of DEs (child1, child2) Contains : empty ListBase -= child1 =- elements (for each DE object) : toText: "Glutamine-dependent carbamoyl- phosphate synthase", "6.3.5.5" category: "RecName", "RecName", type: "Full", "EC" hasFragment : undef -= child2 =- elements (for each DE object) : toText: "Aspartate carbamoyltransferase", "2.1.3.2" category: "RecName", "RecName", type: "Full", "EC" hasFragment : undef Note: the old unstructured DE format can still be used, and will be parsed the same way into DE objects (but without setting their attributes 'category' and 'type'. DE CAD protein (Protein rudimentary) [Includes: Glutamine-dependent DE carbamoyl-phosphate synthase (EC 6.3.5.5); Aspartate DE carbamoyltransferase (EC 2.1.3.2)] (Fragment). =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C The (raw) text of the DE line (without the 'DE ' line type prefixes) =item C Array reference to the SWISS::DE objects containing the different names for the entry. The first element of the list is the recommended name. Note: use C method (inherited from ListBase) to get (and loop through) the array of DE objetcs. =item C =item C Each of these is a SWISS::ListBase object whose list contains a SWISS::DEs object for each 'child' of the protein (i.e. peptide or functional domain). See the UniProtKB user manual for an explanation. It is possible to have both Includes and Contains in a single entry: DE RecName: Full=Arginine biosynthesis bifunctional protein argJ; DE Includes: DE RecName: Full=Glutamate N-acetyltransferase; DE EC=2.3.1.35; DE AltName: Full=Ornithine acetyltransferase; DE Short=OATase; DE AltName: Full=Ornithine transacetylase; DE Includes: DE RecName: Full=Amino-acid acetyltransferase; DE EC=2.3.1.1; DE AltName: Full=N-acetylglutamate synthase; DE Short=AGS; DE RecName: Full=Arginine biosynthesis bifunctional protein argJ alpha chain; DE Contains: DE RecName: Full=Arginine biosynthesis bifunctional protein argJ beta chain; =item C Contains 'Fragment' or 'Fragments' (evaluates to true) if the DE lines contain the 'Fragment(s)' indication (in 'Flags:' line with the new DE line format), otherwise evaluates to false. Compare to the more robust Entry::isFragment which also checks the FT lines for a NON_CONS or NON_TER. =item C Returns 1 if the flag 'Precursor' is present (undef if not). Note: only with new DE line format. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head1 Evidence Tags With the new DE line format, each DE element can have distinct evidence tags, which are stored in the DE object themself (see SWISS::DE.pm documentation). The evidence tags for the 'Flags' line are stored in the parent DEs object itself. With the old DE line format, since the DE line did not have a fixed syntax in TrEMBL, it is impossible to reliably assign evidence tags separately to the different elements of the DE lines. Therefore, the DE line can only be evidence tagged as a whole, and the following methods have their prototype defined in SWISS::BaseClass instead of the direct parent of SWISS::DEs, SWISS::ListBase : addEvidenceTag deleteEvidenceTags getEvidenceTags getEvidenceTagsString hasEvidenceTag setEvidenceTags example : $evidenceTag = $entry->Stars->EV->addEvidence('P', 'DEfix', '-', 'v1.3'); # add global DE evtag if old DE line format, 'Flags' evtag if new format $entry -> DEs -> addEvidenceTag($evidenceTag); Swissknife_1.75/lib/SWISS/DTs.pm0000644005110600510130000001166411035646221016567 0ustar ecastroSwissProtpackage SWISS::DTs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields @DATENAMES @RELNAMES %UPPER2MIXED); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( 'CREATED_date' => undef, 'ANN_date' => undef, 'SQ_date' => undef, 'CREATED_rel' => undef, 'ANN_rel' => undef, 'SQ_rel' => undef, 'ANN_version' => undef, 'SQ_version' => undef, ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::DTs; my (@tmp, $date, $release, $version); if ($$textRef =~ /($SWISS::TextFunc::linePattern{'DT'})/m){ @tmp = map{SWISS::TextFunc->cleanLine($_)} split /\n/m, $1; #new format if ($tmp[0] =~ /(\d{2}\-\w{3}\-\d{4}), integrated into (.+)\./i){ $date = $1; $release = $2; $self->CREATED_date($date); $self->CREATED_rel($release); } #old format elsif ($tmp[0] =~ /(\d{2}\-\w{3}\-\d{4}) \(([^\,]+), Created\)/i){ $date = $1; $release = $2; $self->CREATED_date($date); $self->CREATED_rel($release); } #new format if ($tmp[1] =~ /(\d{2}\-\w{3}\-\d{4}), sequence version (\d+)/i){ $date = $1; $version = $2; $self->SQ_date($date); $self->SQ_version($version); } #old format elsif ($tmp[1] =~ /(\d{2}\-\w{3}\-\d{4}) \(([^\,]+), Last sequence update\)/i){ $date = $1; $release = $2; $self->SQ_date($date); $self->SQ_rel($release); } #new format if ($tmp[2] =~ /(\d{2}\-\w{3}\-\d{4}), entry version (\d+)/i){ $date = $1; $version = $2; $self->ANN_date($date); $self->ANN_version($version); } #old format elsif ($tmp[2] =~ /(\d{2}\-\w{3}\-\d{4}) \(([^\,]+), Last annotation update\)/i){ $date = $1; $release = $2; $self->ANN_date($date); $self->ANN_rel($release); } }; $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my $newText; if (defined $self->ANN_version) { $newText = 'DT ' . $self->CREATED_date . ', integrated into ' . $self->CREATED_rel . ".\n" . 'DT ' . $self->SQ_date . ', sequence version ' . $self->SQ_version . ".\n" . 'DT ' . $self->ANN_date . ', entry version ' . $self->ANN_version . ".\n"; } else { $newText = join ('', 'DT ', $self->CREATED_date, " \(", $self->CREATED_rel, ", Created\)\n", 'DT ', $self->SQ_date, " \(", $self->SQ_rel, ", Last sequence update\)\n", 'DT ', $self->ANN_date, " \(", $self->ANN_rel, ", Last annotation update\)\n"); } $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'DT'}); } sub set_Created { my $self=shift; my ($date, $release) = @_; $self->CREATED_date($date); $self->CREATED_rel($release); } sub set_AnnotationUpdate { my $self=shift; my ($date, $release, $version) = @_; $self->ANN_date($date); $self->ANN_rel($release); $self->ANN_version($version) if defined $version; } sub set_SequenceUpdate { my $self=shift; my ($date, $release, $version) = @_; $self->SQ_date($date); $self->SQ_rel($release); $self->SQ_version($version) if defined $version; } 1; __END__ =head1 Name SWISS::DTs =head1 Description B represents the DT lines within an Swiss-Prot + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C Creation date =item C Last annotation update =item C Last Sequence update =item C Created for release =item C Last annotation for release =item C Last sequence update for release =item C Version number for entry annotation =item C Version number for sequence =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item sort =back =head2 Writing methods =over =item set_Created ($date, $release) =item set_AnnotationUpdate ($date, $release[, $version]) =item set_SequenceUpdate ($date, $release[, $version]) =back =head1 TRANSITION The format of the DT line will change in early 2004 from: DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) to: DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 36. DT 28-FEB-2003, entry version 54. This module supports both formats. To convert an entry from the old to the new format, do: $entry->DTs->CREATED_rel("UniProtKB/Swiss-Prot"); $entry->DTs->ANN_version(54); $entry->DTs->SQ_version(36); Swissknife_1.75/lib/SWISS/DRs.pm0000644005110600510130000002355213147300251016560 0ustar ecastroSwissProtpackage SWISS::DRs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields %DBsortField $DBorder); use Exporter; use Carp; use strict; use Data::Dumper; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @EXPORT_OK = qw(); @ISA = qw(Exporter SWISS::ListBase); %fields = qw( ); } #initialization code: load dr_ord into hash { # Leading and trailing spaces are MANDATORY! $DBorder = ' '; for my $path (@INC) { my $file = $path . '/SWISS/dr_ord'; if (-r $file) { local $/ = "\n"; open my $in, '<', $file or carp "Can't load cross reference sort order from $file: $!"; while (<$in>) { next if /^#/; s/\s+\z//; my ($db, $sort_field) = split /\s+/, $_; $DBorder .= uc($db) . ' '; $DBsortField{uc $db} = $sort_field; } last; } } } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $self = shift; my $textRef = shift; my (@lines,$line); my @tokens; my $tag; $self = new SWISS::DRs; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'DR'})/m){ @lines = split /\n/m, $1; while ($line = shift @lines) { # set flag if it's a ** line if ($line=~ /\A ?\*\*/ ) { $tag = '_HIDDEN_' } else { $tag = ''; } my $indentation = $line =~ s/^ //; $line = SWISS::TextFunc->cleanLine($line); # Parse for evidence tags my $evidence = ''; if (($evidence) = $line =~ /($SWISS::TextFunc::evidencePattern)/m) { my $quotedEvidence = quotemeta $evidence; $line =~ s/$quotedEvidence//m; } @tokens = SWISS::TextFunc->listFromText($line, ';\s+', '\.'); if ( $tokens[-1] =~ /^(.+?)\. (\[\w{5,}-\d+\])$/ ) { # for new isoform identifiers in last "; " sep field pop @tokens; push @tokens, ( $1, $2 ); # make it as 2 elems } if ($tag eq '_HIDDEN_') { unshift @tokens, $tag; } my $drline = $evidence ? [@tokens, $evidence] : [@tokens]; push @{$self->list()}, $drline; # store DR lines which are indented push @{$self->{indentation}}, [@$drline] if $indentation; } }; $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my $newText = ''; my ($dr,@comments); # only reformat if the object is dirty unless ($self->{_dirty}) { return; } # Sort first $self->update(); foreach $dr ($self->elements) { my $tag; if (@$dr[0] eq '_HIDDEN_') { $tag = '**' } else { $tag = 'DR' } # reinsert indentation my $indent = ""; if ($self->{indentation}) { INDENTED: for my $indented (@{$self->{indentation}}) { next unless @$dr == @$indented; for (my $i=0; $i<@$dr; $i++) { next INDENTED unless $dr->[$i] eq $indented->[$i]; } $indent = " "; last; } } my $last = @$dr[-1] =~ /^\[[^\]]+\]$/ ? ' '.$& : ''; # trailling iso-id pop @$dr if $last; my $core = join "; ", grep {!/_HIDDEN_/ && !/$SWISS::TextFunc::evidencePattern/} @$dr; $newText .= ($indent . $tag . " " . $core . '.' . $last ); # add evidence tags $newText .= $self->getEvidenceTagsString($dr); # p.s. there is no ev on DR # add line break $newText .= "\n"; } $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'DR'}); } # EMBL DR lines must never be sorted. The sort order stems from EMBL # join statements and merges between entries. It is not possible to # recreate the order automatically. # MIM and HAMAP DR lines should not be sorted as they are presented # in SWISS-PROT with an internal logic. sub sort { my $self = shift; my @dbnames = (); my @sortedDRs = (); # get all DB names, ... @dbnames = map {$_->[0] eq '_HIDDEN_' ? $_->[1] : $_->[0]} $self->elements(); # ... sort into a unique ... @dbnames = SWISS::TextFunc->uniqueList(@dbnames); # .. and ordered list. @dbnames = sort {&_dbIndex($a) <=> &_dbIndex($b)} @dbnames; foreach my $db (@dbnames) { # hidden DRs (starting with **) should always be after the corresponding # block of visible DR lines my (@hiddenDR, @visibleDR); for my $dr (@{$self->list}) { if ($dr->[0] eq '_HIDDEN_') { push @hiddenDR, $dr if $dr->[1] eq $db; } else { push @visibleDR, $dr if $dr->[0] eq $db; } } my $sort_field = $DBsortField{uc $db}; $sort_field = 1 unless defined $sort_field; # Some DR lines must never be sorted if ($sort_field == 0) { push @sortedDRs, @visibleDR, @hiddenDR; } elsif ($sort_field == 2) { # Some DR lines are sorted by ID within one database. # (if the ID is identical, sort by AC) for my $ty ([\@visibleDR, 1], [\@hiddenDR, 2]) { my ($drtype, $field_number) = @$ty; push @sortedDRs, sort { lc @{$a}[$field_number+1] cmp lc @{$b}[$field_number+1] || @{$a}[$field_number+1] cmp @{$b}[$field_number+1] || lc @{$a}[$field_number] cmp lc @{$b}[$field_number] || @{$a}[$field_number] cmp @{$b}[$field_number] } @$drtype; } } else { # The rest is sorted on AC (then ID) for my $ty ([\@visibleDR, 1], [\@hiddenDR, 2]) { my ($drtype, $field_number) = @$ty; if ( defined( $drtype->[0] ) && defined( $drtype->[0]->[ $field_number+1 ] ) ) { push @sortedDRs, sort { my $nextf_a = lc @{$a}[$field_number+1]; $nextf_a='~' if $nextf_a eq '-'; # e.g. without this DR UniPathway; UPA00253; -. would come before DR UniPathway; UPA00253; UER00600. as '-' is < UER00600, replacing - by ~ fixes this my $nextf_b = lc @{$b}[$field_number+1]; $nextf_b='~' if $nextf_b eq '-'; lc @{$a}[$field_number] cmp lc @{$b}[$field_number] || @{$a}[$field_number] cmp @{$b}[$field_number] || $nextf_a cmp $nextf_b || @{$a}[$field_number+1] cmp @{$b}[$field_number+1] } @$drtype; } else { push @sortedDRs, sort { lc @{$a}[$field_number] cmp lc @{$b}[$field_number] || @{$a}[$field_number] cmp @{$b}[$field_number] } @$drtype; } } } } $self->list(\@sortedDRs); return 1; } sub update { my $self = shift; $self->sort(1); return 1; } # The EMBL protein identifiers introduced in 1999 are of the form # xxxxx.yy, e.g. CAA33128.1 # If $dropVersion is set, the version number (.yy) will be dropped from # each PID. sub pids { my $self = shift; my $dropVersion = shift; my @pids; # read command backwards: # get all EMBL DR line arrays, # get element 2 of each array (the pid), # drop it if it's a '-' from NOT_ANNOTATED_CDS @pids = grep {!/-/} map {$$_[2]} $self->get('EMBL'); if ($dropVersion) { map {s/\.\d+$//} @pids; }; return SWISS::TextFunc->uniqueList(@pids); } sub emblacs { my $self = shift; my @emblacs; # read command backwards: # get all EMBL DR line arrays, # get element 1 of each array (the primary accession number), @emblacs = map {$$_[1]} $self->get('EMBL'); return SWISS::TextFunc->uniqueList(@emblacs); } # * Private methods/functions sub _dbIndex { my $dbname = uc shift; my $index = index $DBorder, ' ' . $dbname . ' '; if ($main::opt_warn) { if ($index == -1) { carp "Database name $dbname not found."; } } # unknown databases should be at the end, not at the beginning if ($index == -1) { $index = length $DBorder; } return $index; } # * Filter functions # true if the first element of a DR line (the DB name) matches $dbTargetName # false otherwise sub dbName{ my ($dbTargetName) = @_; return sub { my $ref = shift; my $dbSourceName = @{$ref}[0]; return ($dbSourceName =~ /^$dbTargetName$/); } } # false if the first element of a DR line (the DB name) matches $dbTargetName # true otherwise sub notDbName{ my ($dbTargetName) = @_; return sub { my $ref = shift; my $dbSourceName = @{$ref}[0]; return ($dbSourceName !~ /^$dbTargetName$/); } } 1; __END__ =head1 Name SWISS::DRs =head1 Description B represents the DR (database crossreference) lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C An array of arrays. Each element is an array (Database_identifier, primary_key, secondary_key[,further elements]). =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item sort =back =head2 Reading methods =over =item emblacs Returns a list of all EMBL accession numbers. These are the primary keys of EMBL crossreferences. =item pids [$dropVersion] Returns a list of all PIDs. These are the secondary keys of EMBL crossreferences. B The EMBL protein identifiers introduced in 1999 are of the form xxxxx.yy, e.g. CAA33128.1 If $dropVersion is set, the version number (.yy) will be dropped from each PID. Example: If the EMBL DR line is DR EMBL; L37685; AAC41668.1; -. pids(1) will only return AAC41668, NOT AAC41668.1 =back =head2 Filter functions =over =item dbName($dbTargetName) True if the first element of a DR line (the DB name) matches $dbTargetName. $dbTargetName has to match in full, not only a partial match. =item notDbName($dbTargetName) True if the first element of a DR line (the DB name) does NOT macht $dbTargetName. =back =head2 ** lines (SWISS-PROT internal format) Each DR line may be followed by a ** line like ** DR PROSITE; PS12345; XXX_PAT; FALSE_POS_1 These will be stored internally as DR lines with the DB identifier '_HIDDEN_'. Therefore adding a ** PROSITE line is done as: $entry->DRs->add(['_HIDDEN_', 'PS12345', 'XXX_PAT', 'FALSE_POS_1']); Swissknife_1.75/lib/SWISS/GeneGroup.pm0000644005110600510130000001542213147300251017760 0ustar ecastroSwissProtpackage SWISS::GeneGroup; use vars qw($AUTOLOAD @ISA @EXPORT_OK @GN_LISTS %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::GN; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); @GN_LISTS = qw(Names OLN ORFNames); %fields = ( 'Names' => undef, 'OLN' => undef, 'ORFNames' => undef, 'is_old_format' => undef, ); } sub new { my $ref = CORE::shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub initialize { my $self = CORE::shift; for my $listname (@GN_LISTS) { $self->{$listname} = new SWISS::ListBase; } $self->{is_old_format} = 0; } sub fromText { my $class = CORE::shift; my $text = CORE::shift; unless ($text =~ /^ *(?:Name|Synonyms|OrderedLocusNames|ORFNames)=/) { return _fromText_old($class, $text, @_); } my $self = new($class); $self->initialize; $text =~ s/[;\s]+$//; if ($text =~ s/(^|; +)ORFNames=(.*?)(?=; |;\Z|\Z)//) { $self->ORFNames->set(map {SWISS::GN->fromText($_)} split ', +(?!ECO:\d)', $2); } if ($text =~ s/(^|; +)OrderedLocusNames=(.*?)(?=; |;\Z|\Z)//) { $self->OLN->set(map {SWISS::GN->fromText($_)} split ', +(?!ECO:\d)', $2); } my @names; if ($text =~ s/(^|; +)Synonyms=(.*?)(?=; |;\Z|\Z)//) { push @names, split ', +(?!ECO:\d)', $2; } if ($text =~ s/(^|; +)Name=(.*?)(?=; |;\Z|\Z)//) { unshift @names, split ', +(?!ECO:\d)', $2; #ensure space because valid names may contain a comma } if (length $text) { if ($main::opt_warn) { carp "GN parse error, left text $text"; } push @names, $text; } $self->Names->set(map {SWISS::GN->fromText($_)} @names); return $self; } sub _fromText_old { my $self = new(CORE::shift); my $text = CORE::shift; if( $text =~ /^\(/ && $text =~ /\)$/ ){ $text =~ s/^\(//; $text =~ s/\)$//; } $self->Names->set(map{SWISS::GN->fromText($_)}split / OR /i, $text); $self->is_old_format(1); return $self; } sub toText { my $self = CORE::shift; if ($self->is_old_format) { return _toText_old($self, @_); } my @newText; if ($self->Names->size) { push @newText, "Name=" . $self->Names->head->toText . ";"; if ($self->Names->size > 1) { push @newText, "Synonyms=" . join(", ", map {$_->toText} $self->Names->tail) . ";"; } } if ($self->OLN->size) { push @newText, "OrderedLocusNames=" . join(", ", map {$_->toText} $self->OLN->elements) . ";"; } if ($self->ORFNames->size) { push @newText, "ORFNames=" . join(", ", map {$_->toText} $self->ORFNames->elements) . ";"; } return join " ", @newText; } sub _toText_old { my $self = CORE::shift; my $delimiter = CORE::shift || ' OR '; my $a=join $delimiter, map{$_->toText} @{$self->list}; #FIXME return $a; } sub sort { my $self = CORE::shift; my @name1 = $self->Names->splice(0, 1); $self->ORFNames->set( sort { lc($a->text) cmp lc($b->text) || $a->text cmp $b->text } $self->ORFNames->elements ); return $self->Names->set(@name1, sort {lc($a->text) cmp lc($b->text) || $a->text cmp $b->text} $self->Names->elements); } # access Name and Synonyms sub Name { my $self = CORE::shift; if (@_) { my $newName = CORE::shift; return $self->Names->splice(0, 1, $newName); } else { return $self->Names->head; } } sub Synonyms { my $self = CORE::shift; if (@_) { if ($self->Names->size > 1) { return $self->Names->splice(1, $self->Names->size-1, @_); } else { return $self->Names->set(@_); } } else { return $self->Names->tail; } } # ListBase emulation sub list { my $self = CORE::shift; return [$self->elements]; } sub get { my $self = CORE::shift; my $pattern = CORE::shift; return grep {$_->text =~ /^$pattern$/} $self->elements; } sub head { my $self = CORE::shift; return $self->list->[0]; } sub tail { my $self = CORE::shift; my @el = $self->elements; CORE::shift @el if @el>0; return @el; } sub size { my $self = CORE::shift; return $self->Names->size + $self->OLN->size + $self->ORFNames->size; } sub isEmpty { my $self = CORE::shift; return not $self->size; } sub elements { my $self = CORE::shift; return $self->Names->elements, $self->OLN->elements, $self->ORFNames->elements; } sub item { my $self = CORE::shift; my $n = CORE::shift; return $self->list->[$n]; } sub push { my $self = CORE::shift; $self->Names->push(@_); } sub pop { my $self = CORE::shift; for my $listname (@GN_LISTS) { next unless $self->{$listname}->size; return $self->{$listname}->pop(@_); } return undef; } sub shift { my $self = CORE::shift; for my $listname (@GN_LISTS) { next unless $self->{$listname}->size; return $self->{$listname}->shift(@_); } return undef; } sub splice { my $self = CORE::shift; for my $listname (@GN_LISTS) { next unless $self->{$listname}->size; return $self->{$listname}->splice(@_); } return undef; } sub unshift { my $self = CORE::shift; $self->Names->unshift(@_); } sub set { my $self = CORE::shift; $self->initialize; $self->Names->set(@_); } sub add { my $self = CORE::shift; $self->Names->add(@_); } sub filter { my $self = CORE::shift; my $new = new ref($self); for my $listname (@GN_LISTS) { $new->{$listname} = $self->{$listname}->filter(@_); }; $new->{indentation} = $self->{indentation}; return $new; } 1; __END__ =head1 Name SWISS::GeneGroup.pm =head1 Description A B object contain all synonyms for a given gene name. See B for a description of the gene name format. =head1 Inherits from SWISS::BaseClass.pm (also implements many methods from SWISS::ListBase.pm) =head1 Attributes =over =item C Each list element is a SWISS::GN object, describing a primary name or synonym. Concatenation of Name and Synonyms lists. =item C Each list element is a SWISS::GN object, describing an OrderedLocusName. =item C Each list element is a SWISS::GN object, describing an ORFName. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Specific methods =over =item Name Returns the Name (primary name). =item Synonyms Returns the Synonyms. =item elements Concatenates all elements from Names, OLN and ORFNames in a single array. =back =head2 List manipulation methods Since GeneGroup was a previous implementation of SWISS::ListBase, the list manipulation methods below are provided to facilitate compatibility. =over =item size =item isEmpty =item elements =item filter =item get I<(deprecated)> =item head I<(deprecated)> =item tail I<(deprecated)> =item item I<(deprecated)> =item push I<(deprecated)> =item pop I<(deprecated)> =item shift I<(deprecated)> =item splice I<(deprecated)> =item unshift I<(deprecated)> =item set I<(deprecated)> =item add I<(deprecated)> =back Swissknife_1.75/lib/SWISS/CRC64.pm0000644005110600510130000000443110366115237016654 0ustar ecastroSwissProtpackage SWISS::CRC64; # ** Initialisation #32 first bits of generator polynomial for CRC64 #the 32 lower bits are assumed to be zero my $POLY64REVh = 0xd8000000; my @CRCTableh = 256; my @CRCTablel = 256; my $initialized; sub crc64 { my $sequence = shift; my $crcl = 0; my $crch = 0; if (!$initialized) { $initialized = 1; for (my $i=0; $i<256; $i++) { my $partl = $i; my $parth = 0; for (my $j=0; $j<8; $j++) { my $rflag = $partl & 1; $partl >>= 1; $partl |= (1 << 31) if $parth & 1; $parth >>= 1; $parth ^= $POLY64REVh if $rflag; } $CRCTableh[$i] = $parth; $CRCTablel[$i] = $partl; } } foreach (split '', $sequence) { my $shr = ($crch & 0xFF) << 24; my $temp1h = $crch >> 8; my $temp1l = ($crcl >> 8) | $shr; my $tableindex = ($crcl ^ (unpack "C", $_)) & 0xFF; $crch = $temp1h ^ $CRCTableh[$tableindex]; $crcl = $temp1l ^ $CRCTablel[$tableindex]; } return wantarray ? ($crch, $crcl) : sprintf("%08X%08X", $crch, $crcl); } 1; __END__ =head1 CRC64 perl module documentation =head2 NAME CRC64 - Calculate the cyclic redundancy check. =head2 SYNOPSIS use SWISS::CRC64; $crc = SWISS::CRC64::crc64("IHATEMATH"); #returns the string "E3DCADD69B01ADD1" ($crc_low, $crc_high) = SWISS::CRC64::crc64("IHATEMATH"); #returns two 32-bit unsigned integers, 3822890454 and 2600578513 =head2 DESCRIPTION SWISS-PROT + TREMBL use a 64-bit Cyclic Redundancy Check for the amino acid sequences. The algorithm to compute the CRC is described in the ISO 3309 standard. The generator polynomial is x64 + x4 + x3 + x + 1. Reference: W. H. Press, S. A. Teukolsky, W. T. Vetterling, and B. P. Flannery, "Numerical recipes in C", 2nd ed., Cambridge University Press. Pages 896ff. =head2 Functions =over =item crc64 string Calculate the CRC64 (cyclic redundancy checksum) for B. In array context, returns two integers equal to the higher and lower 32 bits of the CRC64. In scalar context, returns a 16-character string containing the CRC64 in hexadecimal format. =back =head1 AUTHOR Alexandre Gattiker, gattiker@isb-sib.ch =head1 ACKNOWLEDGEMENTS Based on SPcrc, a C implementation by Christian Iseli, available at ftp://ftp.ebi.ac.uk/pub/software/swissprot/Swissknife/old/SPcrc.tar.gz =cut Swissknife_1.75/lib/SWISS/CCcofactor.pm0000644005110600510130000001042512571072227020102 0ustar ecastroSwissProtpackage SWISS::CCcofactor; use vars qw($AUTOLOAD @ISA %fields); use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::CC; BEGIN { @ISA = ( 'SWISS::ListBase' ); %fields = ( form => undef, note => undef, # [ txt, ev ] note_blocks => undef # [ [txt, ev ] ] #list ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCcofactor; my $text = $$textRef; $self->initialize(); $text =~ s/ *-!- COFACTOR: +//; $text =~ s/; {2,}/; /g; $text =~ s/, {2,}/, /g; if ( $text !~ /Name=/ && $text !~ /Note=/ ) { # old format! my $note = $text; ( my $note_ev = $1 ) if $note =~ s/($SWISS::TextFunc::evidencePattern)\.?//; $self->{ note } = [ $note.".", $note_ev ] if $note; } else { # new format ( my $form = $1 ) if $text =~ s/^([^:]+): (?=N)//; ( my $note = $1 ) =~ s/;$// if $text =~ s/ ?Note=(.+)$//; $self->{ form } = $form if $form; $self->{ note_blocks } = SWISS::CC::parse2Blocks( $note ) if $note; #[ $note, $note_ev ] if $note; foreach my $name ( split / +(?=Name=)/, $text ) { my $ev = $name =~ s/ +Evidence=($SWISS::TextFunc::evidencePattern);// ? " ".$1 : undef; $self->add( [ $name, $ev ] ); } } $self->{_dirty} = 0; return $self; } sub topic { return "COFACTOR"; } sub toString { my ( $self ) = @_; my $form = $self->{ form } ? " $self->{ form }:" : ""; my $text = "CC -!- COFACTOR:$form\n"; foreach my $name_ev ( @{ $self->{ list } } ) { my ( $name, $ev ) = @$name_ev; my $line = $name; if ( $ev ) { $ev=~s/^ +//; $line .= " Evidence=".$ev.";" } $text .= SWISS::TextFunc->wrapOn( 'CC ',"CC ", $SWISS::TextFunc::lineLength, $line, "(?<=;) ", "(?<=,) ", $SWISS::TextFunc::textWrapPattern1 ); } if ( $self->{ note } ) { # old format my ( $note, $note_ev ) = @{ $self->{ note } }; $note_ev ||= ""; $note = "Note=" . $note . $note_ev . ";"; $text .= SWISS::TextFunc->wrapOn( 'CC ',"CC ", $SWISS::TextFunc::lineLength, $note ); } if ( $self->{ note_blocks } ) { my $note = "Note=" . SWISS::CC::blocks2String( $self->{ note_blocks }, "" ) . ";"; $text .= SWISS::TextFunc->wrapOn( 'CC ',"CC ", $SWISS::TextFunc::lineLength, $note ); } return $text; } sub comment { my ( $self, $with_ev ) = @_; my $text = ""; foreach my $name_ev ( @{ $self->{ list } } ) { my ( $name, $ev ) = @$name_ev; $text .= ( $text ? " " : "" ) . $name; if ( $ev && $with_ev ) { $ev=~s/^ +//; $text .= " Evidence=".$ev.";" } } if ( $self->{ note } ) { my ( $note, $note_ev ) = @{ $self->{ note } }; $note_ev = "" unless $with_ev && $note_ev; $note = "Note=" . $note . $note_ev . ";"; $text .= ( $text ? " " : "" ) . $note; } return $text; } #sub sort { # my $self = shift; # $self->{ list } = sort { lc( $a->[0] ) cmp lc( $b->[0] ) } @{ $self->{ list } }; #} 1; __END__ =head1 Name SWISS::CCcofactor =head1 Description B represents a comment on the topic 'COFACTOR' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item topic The topic of this comment ('COFACTOR'). =item comment The "text" version of this comment (without evidences and new lines). =item note The note and evidence (Note= in new format or full description in old format) reference to an array of [ $note, $note_ev ] (strings) =item elements An array of [name_str, evidence_tags_str], if any. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/SQs.pm0000644005110600510130000001165112350012212016563 0ustar ecastroSwissProtpackage SWISS::SQs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields $crcLabel %molWeight); use Exporter; use Carp; use strict; use SWISS::BaseClass; use SWISS::TextFunc; use SWISS::CRC64; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( 'seq' => undef, 'length' => undef, 'molWeight' => undef, 'crc' => undef, ); # integer part, and decimal part * 1e+4 of average (chemical) aa masses # [with 4 digits] minus a water molecule [18.0153] %molWeight = ( "A" => [ 71, 788], "C" => [103, 1388], "D" => [115, 886], "E" => [129, 1155], "F" => [147, 1766], "G" => [ 57, 519], "H" => [137, 1411], "I" => [113, 1594], "K" => [128, 1741], "L" => [113, 1594], "M" => [131, 1926], "N" => [114, 1038], "P" => [ 97, 1167], "Q" => [128, 1307], "R" => [156, 1875], "S" => [ 87, 782], "T" => [101, 1051], "V" => [ 99, 1326], "W" => [186, 2132], "Y" => [163, 1760], "J" => [113, 1594], #J = I or L "U" => [150, 388], # selenocysteine (Sec) 150.0388 "O" => [237, 3018], # pyrrolysine (Pyl) 237.3018 #The masses for the degenerate amino acids were computed by weighing them with the #amino acid frequencies in Swiss-Prot Release 45.0 of 25 Oct 2004 (total 99.9): #A=>7.82, Q=>3.94, L=>9.62, S=>6.87, R=>5.32, E=>6.60, K=>5.93, T=>5.46, N=>4.20, G=>6.94, #M=>2.37, W=>1.16, D=>5.30, H=>2.27, F=>4.01, Y=>3.07, C=>1.56, I=>5.90, P=>4.85, V=>6.71, "B" => [114, 6532], #B = N or D "Z" => [128, 7473], #Z = Q or E "X" => [111, 3306], #X = any aa ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub initialize { my $self = shift; $self->{'seq'} = ''; $self->{'length'} = 0; $self->{'molWeight'} = 0; $self->{'crc'} = 0; } # If the sequence is updated, the rest has to be updated, too. sub seq { my $self = shift; my $sq = ''; if (@_) { $self->{seq} = shift; $self->update; } else { return $self->{seq}; }; } sub update { my $self = shift; $self->length(length $self->seq); $self->molWeight(&calcMolWeight($self->seq)); $self->crc(scalar SWISS::CRC64::crc64($self->seq())); $self->{_dirty} = 0; return 1; } sub toText { my $self = shift; my $textRef = shift; my $sequence = $self->seq(); my (@tmp, @lines, $newText); # update if ($self->{_dirty}) { $self->update; }; # format SQ line $newText = sprintf("SQ SEQUENCE %d AA; %d MW; %s %s;\n", $self->length, int($self->molWeight+0.5), #true rounding (int() truncates) $self->crc(), 'CRC64'); # format the sequence $newText = $newText . ' ' . join("\n ", map {join " ", ($_ =~ m/.{1,10}/g)} ($sequence =~ m/.{1,$SWISS::TextFunc::lineLengthSQ}/g)) . "\n"; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'SQ'}); } sub fromText { my $self = new(shift); my $textRef = shift; my ($line, @lines); my @tmp; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'SQ'})/m){ @lines = split /\n/m, $1; # process SQ line $line = shift @lines; $line = SWISS::TextFunc->cleanLine($line); @tmp = SWISS::TextFunc->listFromText($line, ';*\s+', '\.'); $self->length($tmp[1]); $self->molWeight($tmp[3]); $self->crc($tmp[5]); # process the sequence $line = join '', @lines; # remove spaces $line =~ tr/ //d; # assign the sequence $self->{seq} = $line; $self->{_dirty} = 0; } else { $main::opt_warn && $main::opt_warn>1 && carp "No SQ lines in $$textRef"; }; $self->{_dirty} = 0; return $self; } # return the molecular weight of an amino acid chain sub calcMolWeight{ my ($string) = @_; my $mwInt = 18; #1 water molecule = 18.0153 Da my $mwFloat = 153; # water mass decimal part * 10^4 (leading zero removed) foreach my $aa (keys %molWeight){ my ($int, $float) = @{$molWeight{$aa}}; my $count = $string =~ s/$aa/$aa/g; $mwInt += $count * $int; $mwFloat += $count * $float; } return $mwInt + $mwFloat/1e4; } 1; __END__ =head1 NAME B =head1 DESCRIPTION B represents the SQ lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C The amino acid sequence in string representation. =item C The sequence length. =item C The molecular weight. =item C The CRC checksum of the sequence. This is recalculated using the C module. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item update Should be called if the sequence has been modified. =back =head2 Specific methods =over =item calcMolWeight string Calculate the molecular weight for B. =back Swissknife_1.75/lib/SWISS/OX.pm0000644005110600510130000000222310366115237016416 0ustar ecastroSwissProtpackage SWISS::OX; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( text => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $text = shift; # Parse out the evidence tags if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { my $tmp = $1; $self->evidenceTags($tmp); } $self->text($text); return $self; } sub toText { my $self = shift; return $self->text . $self->getEvidenceTagsString; } 1; __END__ =head1 Name SWISS::OX =head1 Description B represents one tax id from the OX line. The container object holding all tax ids is SWISS::OXs. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C One tax id. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head1 Example see documentation of OXs.pm Swissknife_1.75/lib/SWISS/IDs.pm0000644005110600510130000001033610512715457016556 0ustar ecastroSwissProtpackage SWISS::IDs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; # Example of an ID line: # ID FUCK_ECOLI STANDARD; PRT; 482 AA. # ID primaryID dataClass; moleculeType; length AA. #[** Further IDs] # # New format, starting with release 9.0: # ID CYC_PIG Reviewed; 104 AA. # ID Q3ASY8_CHLCH Unreviewed; 36805 AA. # ID %-24s%-11s%10d AA. BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( 'dataClass' => undef, 'moleculeType' => undef, 'stars' => undef, # should second ID line be ** line or not? 'length' => undef # Number of amino acids. ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub initialize { my $self = shift; $self->{'dataClass'} = 'PRELIMINARY'; $self->{'moleculeType'} = 'PRT'; $self->{'length'} = 0; $self->{'stars'} = 0; } sub fromText { my $self = new(shift); my $textRef = shift; my ($line, @lines); my @tmp; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'ID'})/m){ @lines = (split /\n/m, $1); # process main ID line $line = shift @lines; $self->{indentation} += $line =~ s/^ //; $line = SWISS::TextFunc->cleanLine($line); @tmp = SWISS::TextFunc->listFromText($line, ';*\s+', '\.'); push (@{$self->list()}, shift @tmp); # assign the rest of the first ID line $self->{'dataClass'} = shift @tmp; if (@tmp > 2) { $self->{'moleculeType'} = shift @tmp; } $self->{'length'} = shift @tmp; foreach $line (@lines) { if ($line =~/\*\*/) { $self->{stars} = 1; } $self->{indentation} += $line =~ s/^ //; $line = SWISS::TextFunc->cleanLine($line); @tmp = SWISS::TextFunc->listFromText($line, ';\s+', ';\s*'); push (@{$self->list()}, @tmp); } } else { ($main::opt_warn > 1) && carp "No ID line in $$textRef"; } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my (@tmp, $line, $newText); # print ID line if ($self->{dataClass} =~ /reviewed/i) { $newText = sprintf("ID %-24s%-11s%10d AA.\n", $self->head, $self->{dataClass} . ';', $self->{'length'}); } else { $newText = sprintf("ID %-11s %11s; %8s; %5d AA.\n", $self->head, $self->{dataClass}, $self->{moleculeType}, $self->{'length'}); } # print secondary IDs in ** line, or in ID line for STANDARD entries if ($#{$self->list} > 0) { @tmp = @{$self->list}; shift @tmp; my $indent = $self->{indentation} ? " " : ""; if (($self->{stars} == 0) && ($self->{dataClass} eq "STANDARD")) { $line = join "", map {"${indent}ID $_\n"} @tmp; } else { $line = join('; ', @tmp) . ";"; $line = SWISS::TextFunc->wrapOn("\*\* ", "\*\* ", $SWISS::TextFunc::lineLength, $line, '; '); } $newText .= $line; }; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'ID'}); } # IDs must never be sorted, overwrite the inherited sort method. sub sort { return 1; } 1; __END__ =head1 Name SWISS::IDs.pm =head1 Description B represents the ID lines of a SWISS-PROT + TREMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C This is an array containing a list of all the IDs associated with this entry. The first member will be the primary ID, and any following are the secondary IDs which are not shown in the public section of the entry. =item dataClass The data class, either STANDARD or PRELIMINARY for data from releases prior to 9.0, or Reviewed or Unreviewed for data from later releases. =item moleculeType The molecule type, currently only PRT. =item length The protein length in amino acids. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item sort IDs must never be sorted, so this method does nothing (but it overwrites the inherited method). Swissknife_1.75/lib/SWISS/Refs.pm0000644005110600510130000000367310366115237017001 0ustar ecastroSwissProtpackage SWISS::Refs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields $opt_debug); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::Ref; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::Refs; my $ref; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'R.'})/m){ foreach $ref (split /(?=^ ?RN)/m, $1) { $self->push(SWISS::Ref->fromText(\$ref)); } } else { $self->initialize; }; $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my $newText = ''; my $ref; foreach $ref (@{$self->list}) { $newText .= $ref->toText; # Now text and object representation are being synchronised, reset # the _dirty flag of $ref. $ref->{_dirty} = 0; }; if (defined $main::opt_debug && $main::opt_debug>1) { print STDERR "$newText"; }; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'R.'}); } # Overwrite the inherited sort method. sub sort { my ($self) = @_; return $self->set(sort {$a->RN <=> $b->RN} @{$self->list}); return 1; } # Overwrite the inherited update method. sub update { return 1; } 1; __END__ =head1 Name SWISS::Refs.pm =head1 Description B represents the Reference lines within an SWISS-PROT + TREMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C A list of SWISS::Ref objects. Each object represents one reference. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/KW.pm0000644005110600510130000000220110366115237016405 0ustar ecastroSwissProtpackage SWISS::KW; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( text => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $text = shift; # Parse out the evidence tags if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { my $tmp = $1; $self->evidenceTags($tmp); } $self->text($text); $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; return $self->text . $self->getEvidenceTagsString; } 1; __END__ =head1 Name SWISS::KW =head1 Description Each KW object represents one keyword. The container object for all keywords of an entry is SWISS::KWs =head1 Inherits from SWISS::BaseClass =head1 Attributes =over =item C The text of the keyword. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/CCdisease.pm0000644005110600510130000001243412571352124017716 0ustar ecastroSwissProtpackage SWISS::CCdisease; use vars qw($AUTOLOAD @ISA @_properties %fields); use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @ISA = ('SWISS::BaseClass'); %fields = ( disease => undef, mim => undef, descritption => undef, note => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCdisease; my $text = $$textRef; $self->initialize(); $self->{ disease } = undef; # [ txt, ev ]; $self->{ mim } = undef; # txt; $self->{ description } = undef; # txt; $self->{ note } = undef; # [[ sentence, ev ]]; $self->{ is_old_format } = 1; # p.s. if old non structured format, all is in note field (but do not show Note=) $self->{_dirty} = 0; if ( $text =~ /^ *-!- DISEASE: +(\S.+?\]): (.+?)$/ ) { # new format with named disease $self->{ is_old_format } = 0; my $disease = $1; my ( $descev, $note ) = split( /\.? Note=/, $2 ); my $p_desc_ev = _parse_txt_ev( $descev ); my $mim = $disease =~ /\[MIM:(\d+)\]/ ? $1 : undef; $self->{ disease } = [ $disease, $p_desc_ev->[1] ]; $self->{ mim } = $mim; $self->{ description } = $p_desc_ev->[0]; $self->{ note } = SWISS::CC::parse2Blocks( $note ); } elsif ( $text =~ /^ *-!- DISEASE: Note=(.+?)$/ ) { # new(er?) format without a named disease (but has Note= that now could be multi sentence-ev !) $self->{ is_old_format } = 0; $self->{ note } = SWISS::CC::parse2Blocks( $1 ); } elsif ( $text =~ /^-!- DISEASE: (.+)\.?$/ ) { # old format not structured $self->{ is_old_format } = 1; $self->{ note } = SWISS::CC::parse2Blocks( $1 ); # old format: only one block sentence(s)-ev but use parse2Blocks anyway to have uniform data stucture } return $self; } sub _parse_txt_ev { my $txt = shift; my ( $evidence ) = $txt =~ /($SWISS::TextFunc::evidencePattern)/m; if ( $evidence ) { my $quotedEvidence = quotemeta $evidence; $txt =~ s/$quotedEvidence//m; } $txt =~ s/\.$//; return [ $txt, $evidence ]; } sub toString { my $self = shift; my $text = "CC -!- DISEASE: " . $self->comment; $text = SWISS::TextFunc->wrapOn( '', "CC ", $SWISS::TextFunc::lineLength, $text); return $text; } sub comment { my $self = shift; my $text = ""; if ( defined $self->{ disease } ) { # "controled" disease (only new format) my $d_ev = $self->{ disease}->[ 1 ]; $text .= $self->{ disease }->[ 0 ].": ".$self->{ description }; if ( $d_ev && $d_ev ne '{}' ) { my $extra = $self->{is_old_format} ? "" : "."; $text .= $extra.$d_ev } $text .= "."; $text .= " " if defined $self->{note}; } if ( defined $self->{note} ) { my $note = SWISS::CC::blocks2String( $self->{ note } ); $text .= ( $self->{is_old_format} ? "" : "Note=" ).$note."."; # yes even with new structured format ends with . (instead of ;) } return $text; } sub topic { return "DISEASE"; } sub disease { my ( $self, $value, $ev ) = @_; if ( defined $value ) { my $new_ev = $ev ? $ev : $self->{ disease }->[0]; $self->{ disease } = [ $value, $new_ev ]; } return $self->{ disease }; } sub mim { my ( $self, $value ) = @_; if ( defined $value ) { $self->{ mim } = $value; } return $self->{ mim }; } sub description { my ( $self, $value ) = @_; if ( defined $value ) { $self->{ description } = $value; } return $self->{ description }; } sub note { my ( $self, $ref ) = @_; if ( defined $ref ) { $self->{ note } = $ref; } return $self->{ note }; } 1; __END__ =head1 Name SWISS::CCdisease.pm =head1 Description B represents a comment on the topic 'DISEASE' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item topic The topic of this comment ('DISEASE'). =back =head1 Methods =item disease The name and evidence of the disease (only for new structured CC diseases) reference to an array [ $disease, $disease_ev ] =item disease( [ $new_disease, $new_disease_ev ] ) Set disease to [ $new_disease, $new_disease_ev ] =item mim The disease mim id (only for new structured CC diseases) =item mim( $new_mim ) Set mim to $new_mim =item description The disease description (only for new structured CC diseases) =item note The note and evidence of the disease (Note= in new CC disease format or full description in old format) reference to an array of [ $block_txt, $block_ev ] arrays =item note( [[ $block_txt, $block_ev ]...] ) Set note to array of [ $block_txt, $block_ev ] arrays =item comment The "text" version of this comment. =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/CCcopyright.pm0000644005110600510130000000346310727215623020316 0ustar ecastroSwissProtpackage SWISS::CCcopyright; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( text => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCcopyright; my $text = $$textRef; $self->text($text); $self->{_dirty} = 0; return $self; } sub toString { my $self = shift; my $text = $self->text; $text =~ s/\A\-/CC \-/g; $text =~ s/-{74}/-----------------------------------------------------------------------/; # fix CC line punctuation issue (need full stop inside CC block, may be lost # in earlier processing of CC section) # 12/11/2007: this full stp is apparently no longer required # $text =~ s/(? text; } 1; __END__ =head1 Name SWISS::CCcopyright =head1 Description B represents the copyright statment within the comments block of a SWISS-PROT entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Collectively, comments of all types are stored within a SWISS::CCs container object. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item topic The topic of this comment ('Copyright'). =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Reading/Writing methods =over =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/Stars.pm0000644005110600510130000003127113147300251017161 0ustar ecastroSwissProtpackage SWISS::Stars; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields $defaultClass %month2number $header $footer $mheader $mfooter $headerPattern $footerPattern); use Exporter; use Carp; use strict; use SWISS::Stars::default; use SWISS::Stars::DR; use SWISS::Stars::aa; use SWISS::Stars::EV; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( ); # The default class which handles new tags in the PRELIMINARY SECTION $defaultClass = "SWISS::Stars::default"; $header = "** ################# SOURCE SECTION ##################\n"; $footer = "** ################# INTERNAL SECTION ##################\n"; $mheader = quotemeta $header; $mfooter = quotemeta $footer; $headerPattern = '\*\* \#+\s+SOURCE SECTION\s+\#+\n'; $footerPattern = '\*\* \#+\s+INTERNAL SECTION\s+\#+\n'; %month2number = ('01'=>'JAN', '02'=>'FEB', '03'=>'MAR', '04'=>'APR', '05'=>'MAY', '06'=>'JUN', '07'=>'JUL', '08'=>'AUG', '09'=>'SEP', '10'=>'OCT', '11'=>'NOV', '12'=>'DEC'); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub initialize { } sub AUTOLOAD { my $self = shift; my $value; my $name = $AUTOLOAD; my $fullname = $name; # * Initialise if (@_) { $value = shift; } else { undef $value; } # get only the bit we want $name =~ /::DESTROY/ && return; $name =~ s/.*://; # If a value is passed, try to set it # No type verification - use at your own risk!!! if (defined $value) { if ((exists $self->{$name}) || # is it a permitted object? (length ($name) == 2 && ref $value )) { $self->{_dirty} = 1; # if a subobject is set, it's dirty if (defined $self->{$name}->{_dirty}) { $self->{$name}->{_dirty} = 1; }; return $self->{$name} = $value; } else { confess "Can't set $name to $value. Probably passed a wrong variable name into " . ref($self); } } else { # * An object has been requested # If the object exists, return it if (defined $self->{$name}) { return $self->{$name}; } else { # no object $name yet, create and return it if (defined &{$fullname . "::fromText"}) { # use specific subclass return $self->{$name} = $fullname->fromText($self->{_textRef}); } else { # check if name is a valid object tag if (length $name == 2) { # use generic Stars::default $self->{$name} = $defaultClass->fromText($self->{_textRef}, $name); return $self->{$name}; } else { confess "Can't create $name. Probably passed a wrong variable name into " . ref($self); }; } } } } sub fromText { my $self = new(shift); my $textRef = shift; my $lines = ''; if ($$textRef =~ /$SWISS::TextFunc::linePattern{'St'}/m){ $lines = $&; # remove header and footer lines $lines =~ s/($headerPattern)|($footerPattern)//mg; # Cleanup empty lines at the beginning of the block $lines =~ s/\A\*\*\s*\*{0,2}\n//gm; }; $self->{'_textRef'} = \$lines; return $self; }; sub toText { my $self = shift; my $textRef = shift; my $subObject; # reparse (maybe this is called from entry reformat) if is set to 'dirty' $self->update( 1 ) if $self->{ _dirty }; # call toText for the subobjects foreach $subObject ( grep {length $_ == 2} sort keys %$self ) { # p.s. only toText already parsed/modified subObjects (not all!) if ($self->{$subObject}->{_dirty}) { # p.s. only call subobject toText if is dirty (modified or forced reparse/build asked) $self->{$subObject}->toText($self->{_textRef}, $subObject); # modifies _texRef content (that contains all **!) for the specified line type=subObject $self->{_dirty} = 1; } } if ($self->{_dirty}) { # add SOURCE SECTION header (unless it's already there) if there are any source ** lines unless ( ${$self->{_textRef}} =~ /$headerPattern/ ) { if ( $self->aa->size && grep { !/^PROSITE; PS/ } $self->aa->elements ) { # p.s. exclude ** PROSITE: are not source! ${$self->{_textRef}} = $header . ${$self->{_textRef}}; } # Add empty line at the beginning, unless it's already there unless (${$self->{_textRef}} =~ /^\*\*\n/) { ${$self->{_textRef}} = "\*\*\n" . ${$self->{_textRef}}; } } # add INTERNAL SECTION header, unless it's already there unless ( ${$self->{_textRef}} =~ /$footerPattern/) { if (${$self->{_textRef}} =~ /\n\*\*\S{2} .*/) { # no header yet, add it before first **XX (non source) line ${$self->{_textRef}} = $` . "\n" . $footer . substr($&, 1) . $'; } else { ${$self->{_textRef}} .= $footer; }; } SWISS::TextFunc->insertLineGroup($textRef, ${$self->{_textRef}}, $SWISS::TextFunc::linePattern{'St'}); $self->{_dirty} = 0; return 1; } else { return 1; }; }; # Stars is a master object like entry. Therefore it has to update itself # and its subobjects. The text representation has also to be updated. sub update { my $self = shift; my $force = shift; my $subObject; my @subObjects; if ($force) { # Make sure all subobjects are parsed if $force is set. @subObjects = ${$self->{'_textRef'}} =~ /\*\*(\w\w) .*/g; # p.s. "** " (source section **) not touched! @subObjects = SWISS::TextFunc->uniqueList(@subObjects); } else { @subObjects = grep {length $_ == 2} keys %$self; } # mark targeted (were accessed/modified or all if $force) subObjects as dirty, will lead to their re-parsing/building in toText foreach $subObject (@subObjects) { $self->$subObject()->{_dirty} = 1; $self->$subObject()->update();# p.s. update method is not re-implemented in Stars sub classes = is from ListBase: calls sort! } $self->{_dirty} = 1; return 1; } sub insertLineGroup { # update/insert back text (preserving original order) for specific **key (subObject) into object _textRef (containing all **) my ($class, $textRef, $text, $tag) = @_; my $seen = 0; # replace (1st) old targeted block with fresh data (grouped $tag lines into $text), subsequent targeted blocks (malformed: ** should be grouped in continuous blocks) should be removed $$textRef =~ s/^(\*\*$tag .*\n){1,}/{my $rep = $seen ? "": $text; $seen =1; $rep}/egm or $$textRef .= $text; return 1; }; # Function: transfer from the old into the new ** section format # Args : $curatedBlock : if set, the function supposes that # the curator's comments are in a block # started by $curatedStart and # terminated by $curatedStop # Returns : true sub translate { my $self = shift; my $curatedBlock = shift; my ($tmp, $tmpText, @tmp); # transfer # ** XXXX_ARATH if (@tmp = $self->aa->get('[A-Z0-9]{1,4}\_[A-Z0-9]{3,5}')){ $self->aa->del('[A-Z0-9]{1,4}\_[A-Z0-9]{3,5}'); # Remove duplicates if ($#tmp > 0) { $tmp = new SWISS::ListBase; $tmp->add(@tmp); $tmp->unique(); @tmp = $tmp->elements(); } $self->ID->add(@tmp); }; # Delete PFAM predictions, they will be redone. $self->aa->del('.*PREDICTED BY PFAM.*'); # Delete DR PRINTS, they are now in the main section $self->aa->del('DR PRINTS.*'); # Delete DR PROSITE $self->aa->del('PROSITE.*'); # Delete ** PSnnnnn lines $self->aa->del('PS\d{5}.*'); # Delete ** EMOTIF $self->aa->del('EMOTIF.*'); # Delete ** MISSING lines $self->aa->del('MISSING.*'); # Delete # ** -!- SUBCELLULAR LOCATION: NUCLEAR (POTENTIAL; # ** PREDICTED BY NNPSL; 57.9 ACCURACY). $self->aa->del('.*SUBCELLULAR LOCATION:.*POTENTIAL.*'); $self->aa->del('.*PREDICTED BY NNPSL.*'); # transfer # ** DR GENBANK JOURNAL-SCAN; G1754741. if (@tmp = $self->aa->get('DR GENBANK JOURNAL-SCAN.*')){ $self->aa->del('DR GENBANK JOURNAL-SCAN.*'); $self->GP->add(@tmp); }; # transfer # ** TAX_ID; 4932; Saccharomyces cerevisiae. my ($line) = $self->aa->get('TAX_ID; .*'); if ($line) { $line =~ /^TAX_ID; (-*\d+);/; $self->OX->add($1 . ";"); $self->aa->del('TAX_ID.*'); } # transfer # ** RULE RU000204. # ** RULE RU000195; 1998-01-22. # to # **RU RU000201; 22-SEP-1999. my ($rule, $rulenum, $year, $month, $day); if (@tmp = $self->aa->get('RULE\s+RU\d{6}.*')){ foreach $rule (@tmp) { ($rulenum) = $rule =~ /RULE\s+(RU\d{6})/; ($year, $month, $day) = $rule =~ /(\d{4})-(\d{2})-(\d{2})/; if ($year){ $month = $month2number{$month}; $self->RU->add("$rulenum; $day-$month-$year."); } else { $self->RU->add("$rulenum;"); } }; $self->aa->del('RULE\s+RU\d{6}.*'); } # transfer the curator's comments my $curatedStart = '((CREATED AND FINISHED BY)|(ANNOT )).*'; my $curatedText = '((FINISHED BY )|(ANNOTATED BY )|(UPDATED BY )|(ANNOT BY )).*'; my $curatedStop = 'CURATED\.?'; if ($curatedBlock) { # Parse a prestructured block of curator's comments my $inBlock = 0; foreach $line ($self->aa->elements) { if ($line =~ /\A$curatedStart\Z/i) { $inBlock = 1; }; if ($inBlock) { $self->aa->del(quotemeta $line); $self->ZZ->add($line); if ($line =~ /\A$curatedStop\Z/) { $inBlock = 0; }; } } } else { # Transfer only well-defined lines of curator's comments foreach $line ($self->aa->elements) { if ($line =~/\A$curatedStart\Z/i || $line =~/\A$curatedText\Z/i || $line =~/\A$curatedStop\Z/ ) { $self->aa->del(quotemeta $line); #$self->ZZ->add($line); } } } $self->{_dirty} = 1; return 1; } sub sort { my $self = shift; # sort **subblocks (toText sort parsed **subblocks, just force parsing) $self->update(1); # sort within each **subblock my $subObject; # Recursively call sort for the subobjects (already accessed) foreach $subObject (grep {length $_ == 2} keys %$self) { $self->{$subObject}->sort; }; return 1; } sub cleanUpReferences { my $self = shift; my @lines = @{$self->list()}; my ($start,$end,$dirty); REFERENCE: for ($start=0; $start <= $#lines; $start++){ # find a reference start while ($start<=$#lines && $lines[$start] !~ /^\[\d+\]/){ $start++; } last if $start>$#lines; $end=$start+1; while ($end<=$#lines && $lines[$end] !~ /^\[\d+\]/){$end++;} last if $end>$#lines; # now look for similar references my $length = $end - $start - 1; my $next; TRY: for ($next=$end; $next<=$#lines; $next++){ next if $lines[$next] !~ /^\[(\d+)\]/; my $j; for ($j=1; $j<=$length; $j++){ next REFERENCE if $j>$#lines; #printf "%03d<<<%-20.20s>>%-20.20s%03d\n" # ,$start+$j,$lines[$start+$j], # $lines[$next+$j],$next+$j; next TRY if ($lines[$start+$j] ne $lines[$next+$j]); } my @removed = splice(@lines, $next, $j); $main::opt_debug > 2 && print "Stars::cleanUpReferences: Removed\n". join("\n",@removed)."\n"; $dirty |= 1; $next--; } $start++ } if ($dirty){ @{$self->{'list'}} = @lines; $self->_dirty(1); } return $dirty; } 1; __END__ =head1 NAME B =head1 DESCRIPTION B represents the ** lines within an SWISS-PROT + TrEMBL entry. These are the lines with the line tag ** which are normally not publicly visible. B is a master object like SWISS::Entry. It contains subobjects which represent the different line types in the ** section. Each line type has a two letter tag in addition to the ** line tag. This module has been written to allow easy addition of new ** line types. To use a new ** line tag, just use the tag as an object dereference. Example: $entry->Stars->XX->add("New XX tag line.","Second new XX tag line."); If there is no class SWISS::Stars::XX, the class of the new object will be SWISS::Stars::default, which handles lines with the corresponding tag as an array of lines. If more specific handling is required, a new class SWISS::Stars::XX can be created following the template of SWISS::Stars::default. An example is SWISS::Stars::aa. Subclass names and new line tags have to be two-letter-tags. B Access to the (old) unstructured ANNOTATOR'S SECTION is provided by the line tag 'aa'. $entry->Stars->aa->add("Testline 1.","Second new test line."); will add these two lines to the ANNOTATOR'S SECTION. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over No public attributes apart from the subclasses. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item update =back Swissknife_1.75/lib/SWISS/CCseq_caution.pm0000644005110600510130000000627212351047725020622 0ustar ecastroSwissProtpackage SWISS::CCseq_caution; use vars qw($AUTOLOAD @ISA); use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::BaseClass; BEGIN { @ISA = ('SWISS::ListBase'); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCseq_caution; my $text = $$textRef; $self->initialize(); $text =~ s/ +/ /g; $text =~ s/\s*-!-.*?:\s*//; while (length $text) { if ($text =~ s/^\s*Sequence=(.*?); Type=(.*?);(?: Positions=(.*?);)?(?: Note=(.*?);)?(?: Evidence=(.+?);)?(?:\s*|\Z)//s) { my ($sequence, $type, $positions, $note, $new_style_evidence, $old_style_evidence) = ($1, $2, $3, $4, $5); my $arg = new SWISS::BaseClass; if ( $old_style_evidence && $old_style_evidence =~ /($SWISS::TextFunc::evidencePattern)/m ) { my $quotedEvidence = quotemeta $&; $sequence =~ s/$quotedEvidence//m; } $arg->{'sequence'} = $sequence; $arg->{'type'} = $type; $arg->{'positions'} = $positions if defined $positions; $arg->{'note'} = $note if defined $note; $arg->{'evidence'} = $new_style_evidence if defined $new_style_evidence; $arg->evidenceTags( $old_style_evidence ) if $old_style_evidence; $self->push($arg); } else { #dangling text carp "CC SEQUENCE CAUTION parse error, ignoring $text"; last; } } $self->sort; $self->{_dirty} = 0; return $self; } sub sort { my ($self) = @_; if ($self) { my @items; for my $item ($self->elements) { push @items, $item } $self->set(sort { lc $a->{sequence} cmp lc $b->{sequence} || $a->{type} cmp $b->{type} } @items); } } sub toString { my $self = shift; my $text = "-!- SEQUENCE CAUTION:\n" . $self->comment; $text =~ s/^/CC /mg; $text =~ s/ //; return $text; } sub topic { return "SEQUENCE CAUTION"; } sub comment { my ($self) = @_; my $text = ''; if ($self) { for my $el ($self->elements) { $text .= 'Sequence=' . $el->{sequence} . $el->getEvidenceTagsString(); $text .= '; Type=' . $el->{type}; $text .= '; Positions=' . $el->{positions} if $el->{positions}; $text .= '; Note=' . $el->{note} if $el->{note}; $text .= '; Evidence=' . $el->{evidence} if $el->{evidence}; $text .= ";\n"; } } $text; } 1; __END__ =head1 Name SWISS::CCinteraction =head1 Description B represents a comment on the topic 'INTERACTION' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. Each element of the list is a hash with the following keys: accession identifier xeno NbExp IntAct (array reference) =head1 Inherits from SWISS::ListBase.pm =head1 Methods =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/Journal.pm0000644005110600510130000007333510366115237017516 0ustar ecastroSwissProtpackage SWISS::Journal; use vars qw($AUTOLOAD @ISA @EXPORT_OK); use Exporter; use Carp; use strict; my %ISSN2JOURNAL = (); my %JOURNAL2ISSN = (); my %OLDISSN2NEWISSN = (); my %ABBREV = (); my $_STAGE1=0; my $_STAGE2=0; my $_STAGE3=0; sub issn2name { my $issn=shift; unless (%ISSN2JOURNAL or $_STAGE1){ _load_ISSN2JOURNAL_STAGE1(); } my $newissn = $OLDISSN2NEWISSN{$issn}; $issn=$newissn if $newissn; my $name = $ISSN2JOURNAL{$issn}; unless ($name or $_STAGE2) { _load_ISSN2JOURNAL_STAGE2(); $name = $ISSN2JOURNAL{$issn}; } return $name; } sub name2issn { my $name = shift; return undef unless $name; unless ($_STAGE3){ _load_JOURNAL2ISSN(); } $name =~ tr/a-z/A-Z/; $name =~ tr/A-Z//cd; my $issn = $JOURNAL2ISSN{$name}; return $issn; } sub name2swiss { my $name = shift; return undef unless $name; my $issn = name2issn($name); if ($issn) { my $newname = issn2name($issn); return $newname if $newname; } _load_JOURNAL_ABBREV() unless %ABBREV; my @words = split(' ',$name); for (my $i=0; $i <= $#words; $i++) { my $word = $words[$i]; $word =~ s/\.//g; my $abbr = $ABBREV{$word}; $words[$i] = "$abbr." if $abbr; } $name = join(' ',@words); return $name; } sub _load_ISSN2JOURNAL_STAGE1{ carp "Loading journal data, stage 1" if $main::opt_debug>1; $_STAGE1=1; %ISSN2JOURNAL = ( '0002-9297' => 'Am. J. Hum. Genet.', '0099-2240' => 'Appl. Environ. Microbiol.', '0003-9861' => 'Arch. Biochem. Biophys.', '0006-291X' => 'Biochem. Biophys. Res. Commun.', '0264-6021' => 'Biochem. J.', '0006-2960' => 'Biochemistry', '0006-3002' => 'Biochim. Biophys. Acta', '0006-4971' => 'Blood', '0092-8674' => 'Cell', '0172-8083' => 'Curr. Genet.', '0070-217X' => 'Curr. Top. Microbiol. Immunol.', '0012-1606' => 'Dev. Biol.', '0950-1991' => 'Development', '0198-0238' => 'DNA', '1044-5498' => 'DNA Cell Biol.', '1340-2838' => 'DNA Res.', '1042-5179' => 'DNA Seq.', '0173-0835' => 'Electrophoresis', '0261-4189' => 'EMBO J.', '0013-7227' => 'Endocrinology', '0014-2956' => 'Eur. J. Biochem.', '0014-5793' => 'FEBS Lett.', '0378-1097' => 'FEMS Microbiol. Lett.', '0378-1119' => 'Gene', '0890-9369' => 'Genes Dev.', '0016-6731' => 'Genetics', '0888-7543' => 'Genomics', '0340-6717' => 'Hum. Genet.', '0964-6906' => 'Hum. Mol. Genet.', '1059-7794' => 'Hum. Mutat.', '0093-7711' => 'Immunogenetics', '0019-9567' => 'Infect. Immun.', '0021-9193' => 'J. Bacteriol.', '0021-924X' => 'J. Biochem.', '0021-9258' => 'J. Biol. Chem.', '0021-9525' => 'J. Cell Biol.', '0021-9738' => 'J. Clin. Invest.', '0022-1007' => 'J. Exp. Med.', '0022-1287' => 'J. Gen. Microbiol.', '0022-1317' => 'J. Gen. Virol.', '0022-1767' => 'J. Immunol.', '0022-2836' => 'J. Mol. Biol.', '0022-2844' => 'J. Mol. Evol.', '0022-538X' => 'J. Virol.', '1350-0872' => 'Microbiology', '0166-6851' => 'Mol. Biochem. Parasitol.', '0737-4038' => 'Mol. Biol. Evol.', '0270-7306' => 'Mol. Cell. Biol.', '0888-8809' => 'Mol. Endocrinol.', '0026-8925' => 'Mol. Gen. Genet.', '0950-382X' => 'Mol. Microbiol.', '1061-4036' => 'Nat. Genet.', '1072-8368' => 'Nat. Struct. Biol.', '0028-0836' => 'Nature', '0896-6273' => 'Neuron', '0305-1048' => 'Nucleic Acids Res.', '0950-9232' => 'Oncogene', '1040-4651' => 'Plant Cell', '0167-4412' => 'Plant Mol. Biol.', '0735-9640' => 'Plant Mol. Biol. Rep.', '0032-0889' => 'Plant Physiol.', '0027-8424' => 'Proc. Natl. Acad. Sci. U.S.A.', '0961-8368' => 'Protein Sci.', '0036-8075' => 'Science', '0969-2126' => 'Structure', '0042-6822' => 'Virology', '0168-1702' => 'Virus Res.', '0749-503X' => 'Yeast', ); %OLDISSN2NEWISSN = ( '0301-5610' => '0305-1048', # Nucleic Acids Res ); } sub _load_ISSN2JOURNAL_STAGE2{ carp "Loading journal data, stage 2" if $main::opt_debug>1; my $save = $/; $/="\n"; while () { if (/^(\d\d\d\d-\d\d\d\S),(.*)/) { print STDERR "Read $1|$2\n" if $main::opt_debug>3; $ISSN2JOURNAL{$1}=$2; } else { last; } } $/ = $save; $_STAGE2 = 1; } sub _load_JOURNAL2ISSN { _load_ISSN2JOURNAL_STAGE1() unless $_STAGE1; _load_ISSN2JOURNAL_STAGE2() unless $_STAGE2; carp "Loading journal data, stage 3" if $main::opt_debug>1; while (my($issn,$name) = each %ISSN2JOURNAL){ next if $OLDISSN2NEWISSN{$issn}; $name =~ tr/a-z/A-Z/; $name =~ tr/A-Z//cd; $JOURNAL2ISSN{$name} = $issn; } $_STAGE3 = 1; } sub _load_JOURNAL_ABBREV { my @abbrev = ('Acad','Adhes','Adv','Alcohol','Am','An','Anal','Anat','Androl','Anim', 'Ann','Annu','Anthropol','Antibiot','Antimicrob','Appl','Arch', 'Arterioscler','Assoc','Autoimmun','Bacteriol','Biochem','Biochim', 'Bioenerg','Biokhim','Biol','Biomed','Biomembr','Biomol','Bioorg', 'Biophys','Biosci','Biotechnol','Boll','Br','Bras','Braz','Bull','C', 'Calcif','Can','Carcinog','Cardiol','Cardiovasc','Cell','Chem', 'Chemother','Chim','Chin','Cienc','Circ','Clin','Coagul','Commun', 'Comp','Connect','Craniofac','Crit','Crystallogr','Curr','Cytochem', 'Cytogenet','Cytol','Dent','Dermatol','Des','Dev','Diagn','Differ','Dis', 'Discov','Disord','Dispos','Domest','Dyn','Ecol','Endocr','Endocrinol', 'Eng','Engl','Entomol','Environ','Enzym','Enzymol','Epidemiol','Essent', 'Eukaryot','Eur','Evol','Exp','Expr','Fertil','Fiziol','Formos','Found', 'Funct','Gastroenterol','Gen','Genet','Glycoconj','Gynecol','Haematol', 'Haemost','Harb','Hear','Hematol','Hepat','Hepatol','Hered','Histochem', 'Horm','Hosp','Hum','Hyg','Hypertens','Immun','Immunobiol','Immunogenet', 'Immunol','Immunopathol','Infect','Inflamm','Inherit','Inhib','Inorg', 'Inst','Int','Interact','Intern','Invertebr','Invest','Isr','Ital','J', 'Jpn','Khim','Lab','Latinoam','Lett','Leukoc','Leukot','Lipidol', 'Macromol','Mamm','Mar','Mech','Med','Membr','Metab','Microb', 'Microbiol','Mikrobiol','Miner','Mitt','Mol','Motil','Mutagen','Mutat', 'Mycol','Nat','Natl','Nephrol','Netw','Neuroanat','Neurobiol', 'Neurochem','Neuroendocrinol','Neurogenet','Neuroimmunol','Neurol', 'Neuromuscul','Neurooncol','Neuropathol','Neurosci','Neurosurg','Nutr', 'Oncol','Ophthalmol','Opin','Organ','Paediatr','Parasitol','Pathog', 'Pathol','Pediatr','Pept','Perspect','Pharm','Pharmacol','Photobiol', 'Photochem','Phylogenet','Phys','Physiol','Pol','Poult','Primatol', 'Proc','Prog','Psychiatr','Purif','Q','Quant','R','Radiat','Rec', 'Recept','Recognit','Regul','Rep','Reprod','Res','Respir','Rev','Rheum', 'Rheumatol','Sang','Scand','Sci','Semin','Seq','Ser','Signal','Soc', 'Somat','Spectrom','Sper','Stand','Struct','Submicrosc','Symp','Syst', 'Technol','Teratog','Theor','Ther','Thromb','Top','Toxicol','Trans', 'Transduct','Transm','Treat','Trop','Tuber','Ukr','Ups','Urol','Vasc', 'Vet','Virol','Virusol','Vis','Vitam','Vopr','West','Z','Zh','Zool' ); my $abbr; foreach $abbr (@abbrev){ $ABBREV{$abbr}=$abbr; $ABBREV{uc($abbr)}=$abbr; } } 1; __DATA__ 0001-5253,Acta Biochim. Biophys. Acad. Sci. Hung. 0582-9879,Acta Biochim. Biophys. Sin. 0001-527X,Acta Biochim. Pol. 0138-4988,Acta Biotechnol. 0095-4195,Acta Bot. Sin. 0904-213X,Acta Chem. Scand. 0567-7394,Acta Crystallogr. A 0108-7681,Acta Crystallogr. B 0907-4449,Acta Crystallogr. D 0001-5598,Acta Endocrinol. 0001-5792,Acta Haematol. 0365-463X,Acta Med. Scand. Suppl. 0137-1320,Acta Microbiol. Pol. 0001-6322,Acta Neuropathol. 0374-5600,Acta Paediatr. Jpn. Overseas Ed. 0065-1583,Acta Protozool. 0001-6675,Acta Pharm. Suec. 0001-706X,Acta Trop. 0300-8924,Acta Vitaminol. Enzymol. 0065-227X,Adv. Biophys. 0065-2571,Adv. Enzyme Regul. 0065-258X,Adv. Enzymol. 0065-2598,Adv. Exp. Med. Biol. 0084-5957,Adv. Nephrol. Necker Hosp. 0732-8141,Adv. Prostaglandin Thromboxane Leukotriene Res. 0065-3233,Adv. Protein Chem. 1040-7952,Adv. Second Messenger Phosphoprotein Res. 0065-4299,Agents Actions 0002-1369,Agric. Biol. Chem. 0269-9370,AIDS 0889-2229,AIDS Res. Hum. Retroviruses 0741-8329,Alcohol 0145-6008,Alcohol. Clin. Exp. Res. 0105-3639,Alfred Benzon Symp. 0105-4538,Allergy 0002-8444,Am. Fern J. 0002-9122,Am. J. Bot. 0361-8609,Am. J. Hematol. 0002-9297,Am. J. Hum. Genet. 0895-7061,Am. J. Hypertens. 0002-9343,Am. J. Med. 0148-7299,Am. J. Med. Genet. 0002-9629,Am. J. Med. Sci. 0002-9394,Am. J. Ophthalmol. 0002-9440,Am. J. Pathol. 0002-9483,Am. J. Phys. Anthropol. 0002-9513,Am. J. Physiol. 1046-7408,Am. J. Reprod. Immunol. 1044-1549,Am. J. Respir. Cell Mol. Biol. 1073-449X,Am. J. Respir. Crit. Care Med. 0002-9637,Am. J. Trop. Med. Hyg. 0002-9645,Am. J. Vet. Res. 0003-1569,Am. Zool. 0001-3765,An. Acad. Bras. Cienc. 0003-2697,Anal. Biochem. 1049-5398,Anim. Biotechnol. 0268-9146,Anim. Genet. 0013-8746,Ann. Entomol. Soc. Am. 0003-4002,Ann. Genet. Sel. Anim. 0003-4800,Ann. Hum. Genet. 0769-2625,Ann. Inst. Pasteur Immunol. 0769-2617,Ann. Inst. Pasteur Virol. 0026-6493,Ann. Mo. Bot. Gard. 0077-8923,Ann. N.Y. Acad. Sci. 0364-5134,Ann. Neurol. 0031-9473,Ann. Phytopathol. Soc. Jpn. 0066-4154,Annu. Rev. Biochem. 0066-4197,Annu. Rev. Genet. 0066-4227,Annu. Rev. Microbiol. 0250-7005,Anticancer Res. 0066-4804,Antimicrob. Agents Chemother. 0003-6072,Antonie Van Leeuwenhoek 0903-4641,APMIS 0273-2289,Appl. Biochem. Biotechnol. 0099-2240,Appl. Environ. Microbiol. 0175-7598,Appl. Microbiol. Biotechnol. 0954-6642,Appl. Theor. Electroph. 0003-9861,Arch. Biochem. Biophys. 0739-4462,Arch. Insect Biochem. Physiol. 0003-9799,Arch. Int. Physiol. Biochim. 0188-0128,Arch. Med. Res. 0302-8933,Arch. Microbiol. 0003-9942,Arch. Neurol. 0003-9950,Arch. Ophthalmol. 0003-9969,Arch. Oral Biol. 0003-9985,Arch. Pathol. Lab. Med. 0304-8608,Arch. Virol. 0021-4884,Arerugi 0365-6128,Ark. Kemi 1049-8834,Arterioscler. Thromb. 1079-5642,Arterioscler. Thromb. Vasc. Biol. 0276-5047,Arteriosclerosis 0004-3591,Arthritis Rheum. 0128-7451,Asia Pac. J. Mol. Biol. Biotechnol. 0044-7897,ASM News 0021-9150,Atherosclerosis 0004-9417,Aust. J. Biol. Sci. 0004-9425,Aust. J. Chem. 0310-7841,Aust. J. Plant Physiol. 0307-9457,Avian Pathol. 0090-5542,Basic Life Sci. 0301-0457,Behring Inst. Mitt. 0749-5331,Biochem. Arch. 0006-291X,Biochem. Biophys. Res. Commun. 0829-8211,Biochem. Cell Biol. 0006-2928,Biochem. Genet. 0158-5231,Biochem. Int. 0264-6021,Biochem. J. 0885-4505,Biochem. Med. Metab. Biol. 1069-8302,Biochem. Mol. Biol. Int. 1077-3150,Biochem. Mol. Med. 0006-2952,Biochem. Pharmacol. 0015-3796,Biochem. Physiol. Pflanz. 0067-8694,Biochem. Soc. Symp. 0300-5127,Biochem. Soc. Trans. 0006-2960,Biochemistry 0006-3002,Biochim. Biophys. Acta 0300-9084,Biochimie 0923-9820,Biodegradation 0265-9247,Bioessays 0951-6433,Biofactors 0006-2979,Biokhimiia 0006-3185,Biol. Bull. 0248-4900,Biol. Cell 1431-6730,Biol. Chem. 0024-4066,Biol. J. Linn. Soc. Lond. 0918-6158,Biol. Pharm. Bull. 0006-3363,Biol. Reprod. 1016-0922,Biol. Signals 0232-766X,Biomed. Biochim. Acta 0887-6134,Biomed. Environ. Mass Spectrom. 0895-3988,Biomed. Environ. Sci. 0306-042X,Biomed. Mass Spectrom. 0388-6107,Biomed. Res. 0966-0844,Biometals 0045-2068,Bioorg. Chem. 0132-3423,Bioorg. Khim. 0968-0896,Bioorg. Med. Chem. 0301-4622,Biophys. Chem. 0006-3495,Biophys. J. 0340-1057,Biophys. Struct. Mech. 0006-3525,Biopolymers 0916-8451,Biosci. Biotechnol. Biochem. 0144-8463,Biosci. Rep. 0736-6205,BioTechniques 0885-4513,Biotechnol. Appl. Biochem. 0572-6565,Biotechnol. Bioeng. Symp. 0141-5492,Biotechnol. Lett. 8756-7938,Biotechnol. Prog. 0733-222X,Biotechnology 0890-734X,Biotekhnologiya 0006-4971,Blood 0340-4684,Blood Cells 0957-5235,Blood Coagul. Fibrinolysis 0959-8138,BMJ 0037-8771,Boll. Soc. Ital. Biol. Sper. 8756-3282,Bone 0932-8629,Bot. Acta 0006-8063,Bot. Bull. Acad. Sin. 0007-0769,Br. Heart J. 0007-0920,Br. J. Cancer 0007-1048,Br. J. Haematol. 0007-1188,Br. J. Pharmacol. 0007-1935,Br. Vet. J. 0006-8993,Brain Res. 0361-9230,Brain Res. Bull. 0165-3806,Brain Res. Dev. Brain Res. 0169-328X,Brain Res. Mol. Brain Res. 0100-879X,Braz. J. Med. Biol. Res. 0009-2673,Bull. Chem. Soc. Jpn. 0037-9042,Bull. Soc. Chim. Biol. 0040-8921,Bull. Tokyo Med. Dent. Univ. 0171-967X,Calcif. Tissue Int. 0008-4018,Can. J. Biochem. 0714-7511,Can. J. Biochem. Cell Biol. 0008-4026,Can. J. Bot. 0706-652X,Can. J. Fish. Aquat. Sci. 0045-5067,Can. J. For. Res. 0008-4166,Can. J. Microbiol. 0008-4212,Can. J. Physiol. Pharmacol. 0008-4301,Can. J. Zool. 0008-543X,Cancer 0955-3541,Cancer Commun. 0165-4608,Cancer Genet. Cytogenet. 0304-3835,Cancer Lett. 0008-5472,Cancer Res. 0143-3334,Carcinogenesis 0008-6363,Cardiovasc. Res. 0105-1938,Carlsberg Res. Commun. 0092-8674,Cell 1061-5385,Cell Adhes. Commun. 0143-4160,Cell Calcium 0045-6039,Cell Differ. 0922-3371,Cell Differ. Dev. 1044-9523,Cell Growth Differ. 0886-1544,Cell Motil. Cytoskeleton 0730-9554,Cell Muscle Motil. 1044-2030,Cell Regul. 0386-7196,Cell Struct. Funct. 0302-766X,Cell Tissue Res. 0008-8749,Cell. Immunol. 0145-5680,Cell. Mol. Biol. 0968-8773,Cell. Mol. Biol. Res. 1420-682X,Cell. Mol. Life Sci. 0272-4340,Cell. Mol. Neurobiol. 0898-6568,Cell. Signal. 0009-0352,Cereal Chem. 0009-2940,Chem. Ber. 1074-5521,Chem. Biol. 0009-2797,Chem. Biol. Interact. 0009-3068,Chem. Ind. 0009-2363,Chem. Pharm. Bull. 0009-3084,Chem. Phys. Lipids 0893-228X,Chem. Res. Toxicol. 0004-2056,Chem. Scr. 0379-864X,Chem. Senses 0306-0012,Chem. Soc. Rev. 0009-4293,Chimia 1000-8543,Chin. Biochem. J. 1042-749X,Chin. J. Biotechnol. 0253-2662,Chin. J. Microbiol. Immunol. 1001-6538,Chin. Sci. Bull. 0009-5915,Chromosoma 0967-3849,Chromosome Res. 0300-5208,Ciba Found. Symp. 0009-7330,Circ. Res. 0092-6213,Circ. Shock 0009-7322,Circulation 0009-9147,Clin. Chem. 0009-8981,Clin. Chim. Acta 1071-412X,Clin. Diagn. Lab. Immunol. 0954-7894,Clin. Exp. Allergy 1064-1963,Clin. Exp. Hypertens. 0009-9104,Clin. Exp. Immunol. 0009-9163,Clin. Genet. 0090-1229,Clin. Immunol. Immunopathol. 1058-4838,Clin. Infect. Dis. 0095-8654,Clin. Orthop. 0009-9279,Clin. Res. 0143-5221,Clin. Sci. 0091-7451,Cold Spring Harb. Symp. Quant. Biol. 0174-173X,Coll. Relat. Res. 0010-0765,Collect. Czech. Chem. Commun. 0010-406X,Comp. Biochem. Physiol. 0147-9571,Comp. Immunol. Microbiol. Infect. Dis. 0253-5076,Complement 0300-8207,Connect. Tissue Res. 0045-6411,CRC Crit. Rev. Biochem. 1040-841X,CRC Crit. Rev. Microbiol. 0960-9822,Curr. Biol. 0271-3683,Curr. Eye Res. 0172-8083,Curr. Genet. 0343-8651,Curr. Microbiol. 0955-0674,Curr. Opin. Cell Biol. 0957-9672,Curr. Opin. Lipidol. 0959-440X,Curr. Opin. Struct. Biol. 0070-2137,Curr. Top. Cell. Regul. 0070-217X,Curr. Top. Microbiol. Immunol. 0301-0171,Cytogenet. Cell Genet. 1043-4666,Cytokine 0021-5406,Denpun Kagaku 0012-1606,Dev. Biol. 0301-5149,Dev. Biol. Stand. 0145-305X,Dev. Comp. Immunol. 1058-8388,Dev. Dyn. 0949-944X,Dev. Genes Evol. 0192-253X,Dev. Genet. 0012-1592,Dev. Growth Differ. 0378-5866,Dev. Neurosci. 0950-1991,Development 0012-1797,Diabetes 0012-186X,Diabetologia 0301-4681,Differentiation 0278-0240,Dis. Markers 0198-0238,DNA 1044-5498,DNA Cell Biol. 1340-2838,DNA Res. 1042-5179,DNA Seq. 0002-3264,Dokl. Akad. Nauk SSSR 0012-4958,Dokl. Biochem. 0012-4966,Dokl. Biol. Sci. 0739-7240,Domest. Anim. Endocrinol. 1055-9612,Drug Des. Discov. 0090-9556,Drug Metab. Dispos. 0424-7086,Eisei Dobutsu 0173-0835,Electrophoresis 0261-4189,EMBO J. 0743-5800,Endocr. Res. 0969-711X,Endocrine 0013-7200,Endocrinol. Exp. 0013-7219,Endocrinol. Jpn. 0013-7227,Endocrinology 0256-1514,Endocyt. Cell Res. 1062-3329,Endothelium 0091-6765,Environ. Health Perspect. 0013-9432,Enzyme 0141-0229,Enzyme Microb. Technol. 1019-6773,Enzyme Protein 1148-5493,Eur. Cytokine Netw. 0195-668X,Eur. Heart J. 0014-2956,Eur. J. Biochem. 0171-9335,Eur. J. Cell Biol. 0014-2972,Eur. J. Clin. Invest. 0804-4643,Eur. J. Endocrinol. 0902-4441,Eur. J. Haematol. 1018-4813,Eur. J. Hum. Genet. 0014-2980,Eur. J. Immunol. 0953-816X,Eur. J. Neurosci. 0340-6199,Eur. J. Pediatr. 0014-2999,Eur. J. Pharmacol. 0014-3820,Evolution 0071-3384,Exp. Biol. Med. 0014-4827,Exp. Cell Res. 0232-7384,Exp. Clin. Endocrinol. 0906-6705,Exp. Dermatol. 0014-4835,Exp. Eye Res. 0301-472X,Exp. Hematol. 0190-2148,Exp. Lung Res. 0147-5975,Exp. Mycol. 0014-4886,Exp. Neurol. 0014-4894,Exp. Parasitol. 0014-4754,Experientia 0892-6638,FASEB J. 0014-5793,FEBS Lett. 0014-9446,Fed. Proc. 0378-1097,FEMS Microbiol. Lett. 0168-6445,FEMS Microbiol. Rev. 0268-9499,Fibrinolysis 0920-1742,Fish Physiol. Biochem. 1050-4648,Fish Shellfish Immunol. 8755-0199,Free Radic. Res. Commun. 0016-5085,Gastroenterology 0016-6480,Gen. Comp. Endocrinol. 0378-1119,Gene 0735-0651,Gene Anal. Tech. 1052-2166,Gene Expr. 1356-9597,Genes Cells 1045-2257,Genes Chromosomes Cancer 0890-9369,Genes Dev. 1341-7568,Genes Genet. Syst. 0741-0395,Genet. Epidemiol. 0016-6723,Genet. Res. 0016-6707,Genetica 0016-6731,Genetics 0016-6758,Genetika 0831-2796,Genome 1088-9051,Genome Res. 1070-2830,Genome Sci. Technol. 0888-7543,Genomics 0894-1491,Glia 0959-6658,Glycobiology 0282-0080,Glycoconj. J. 0897-7194,Growth Factors 0017-5749,Gut 0090-8258,Gynecol. Oncol. 0301-0147,Haemostasis 0378-5955,Hear. Res. 0018-019X,Helv. Chim. Acta 0363-0269,Hemoglobin 0270-9139,Hepatology 0018-0661,Hereditas 0018-2214,Histochem. J. 0367-6102,Hokkaido Igaku Zasshi 0018-5043,Horm. Metab. Res. 0257-7712,Hua Hsi I Ko Ta Hsueh Hsueh Pao 0340-6717,Hum. Genet. 0001-5652,Hum. Hered. 0198-8859,Hum. Immunol. 0964-6906,Hum. Mol. Genet. 1059-7794,Hum. Mutat. 0268-1161,Hum. Reprod. 0194-911X,Hypertension 0097-9023,ICN UCLA Symp. Mol. Cell. Biol. 1074-7613,Immunity 0171-2985,Immunobiology 0019-2791,Immunochemistry 0093-7711,Immunogenetics 0818-9641,Immunol. Cell Biol. 0882-0139,Immunol. Invest. 0165-2478,Immunol. Lett. 0105-2896,Immunol. Rev. 0092-6019,Immunol. Ser. 0167-4919,Immunol. Today 0019-2805,Immunology 0883-8364,In Vitro Cell. Dev. Biol. 0019-9567,Infect. Immun. 0360-3997,Inflammation 0020-1669,Inorg. Chem. 0020-1790,Insect Biochem. 0965-1748,Insect Biochem. Mol. Biol. 0962-1075,Insect Mol. Biol. 0020-5915,Int. Arch. Allergy Appl. Immunol. 1018-2438,Int. Arch. Allergy Immunol. 0958-6946,Int. Dairy J. 0953-8178,Int. Immunol. 0105-6263,Int. J. Androl. 0020-711X,Int. J. Biochem. 1357-2725,Int. J. Biochem. Cell Biol. 0141-8130,Int. J. Biol. Macromol. 0020-7136,Int. J. Cancer 0737-1454,Int. J. Cell Cloning 0940-5437,Int. J. Clin. Lab. Res. 0214-6282,Int. J. Dev. Biol. 0168-1605,Int. J. Food Microbiol. 0925-5710,Int. J. Hematol. 0934-8840,Int. J. Med. Microbiol. Virol. Parasitol. Infect. Dis. 0020-7519,Int. J. Parasitol. 0367-8377,Int. J. Pept. Protein Res. 1058-5893,Int. J. Plant Sci. 0164-0291,Int. J. Primatol. 0020-7551,Int. J. Protein Res. 0360-3016,Int. J. Radiat. Oncol. Biol. Phys. 0020-7713,Int. J. Syst. Bacteriol. 0300-5526,Intervirology 1354-2516,Invertebr. Neurosci. 0146-0404,Invest. Ophthalmol. Vis. Sci. 0268-8220,IRCS Med. Sci. 0160-3787,Isozymes Curr. Top. Biol. Med. Res. 0021-2148,Isr. J. Chem. 0021-2938,Ital. J. Biochem. 0021-8561,J. Agric. Food Chem. 0091-6749,J. Allergy Clin. Immunol. 0002-7863,J. Am. Chem. Soc. 1046-6673,J. Am. Soc. Nephrol. 0021-8782,J. Anat. 0196-3635,J. Androl. 0021-8812,J. Anim. Sci. 0021-8820,J. Antibiot. 0305-7453,J. Antimicrob. Chemother. 0021-8847,J. Appl. Bacteriol. 0921-8971,J. Appl. Phycol. 0896-8411,J. Autoimmun. 0021-9193,J. Bacteriol. 0233-111X,J. Basic Microbiol. 0021-924X,J. Biochem. 0145-479X,J. Bioenerg. Biomembr. 0021-9258,J. Biol. Chem. 0949-8257,J. Biol. Inorg. Chem. 0925-2738,J. Biomol. NMR 0739-1102,J. Biomol. Struct. Dyn. 0250-4774,J. Biosci. 0168-1656,J. Biotechnol. 0884-0431,J. Bone Miner. Res. 0021-9525,J. Cell Biol. 0021-9533,J. Cell Sci. 0730-2312,J. Cell. Biochem. 0021-9541,J. Cell. Physiol. 0891-0618,J. Chem. Neuroanat. 0022-4936,J. Chem. Soc. Chem. Commun. 0253-5106,J. Chem. Soc. Pak. 0021-9673,J. Chromatogr. 0021-972X,J. Clin. Endocrinol. Metab. 0021-9738,J. Clin. Invest. 0095-1137,J. Clin. Microbiol. 0021-9746,J. Clin. Pathol. 0021-9967,J. Comp. Neurol. 0174-1578,J. Comp. Physiol. B 0270-4145,J. Craniofac. Genet. Dev. Biol. 0022-0299,J. Dairy Res. 0022-0302,J. Dairy Sci. 0022-0345,J. Dent. Res. 0385-2407,J. Dermatol. 0923-1811,J. Dermatol. Sci. 0022-0795,J. Endocrinol. 0391-4097,J. Endocrinol. Invest. 0968-0519,J. Endotoxin Res. 8755-5093,J. Enzym. Inhib. 1066-5234,J. Eukaryot. Microbiol. 1010-061X,J. Evol. Biol. 0022-0949,J. Exp. Biol. 0022-0957,J. Exp. Bot. 0022-1007,J. Exp. Med. 0730-8485,J. Exp. Pathol. 0022-104X,J. Exp. Zool. 0041-9419,J. Fac. Med. Baghdad 0922-338X,J. Ferment. Bioeng. 0022-1112,J. Fish Biol. 0022-1198,J. Forensic Sci. 0815-9319,J. Gastroenterol. Hepatol. 0022-1260,J. Gen. Appl. Microbiol. 0022-1287,J. Gen. Microbiol. 0022-1295,J. Gen. Physiol. 0022-1317,J. Gen. Virol. 0022-1333,J. Genet. 0022-1503,J. Hered. 0022-1554,J. Histochem. Cytochem. 0305-1811,J. Immunogenet. 0022-1767,J. Immunol. 0169-4146,J. Ind. Microbiol. 0022-1899,J. Infect. Dis. 1078-7852,J. Inflamm. 0141-8955,J. Inherit. Metab. Dis. 0162-0134,J. Inorg. Biochem. 0022-1910,J. Insect Physiol. 1079-9907,J. Interferon Cytokine Res. 0197-8357,J. Interferon Res. 0022-2011,J. Invertebr. Pathol. 0022-202X,J. Invest. Dermatol. 0022-2143,J. Lab. Clin. Med. 0741-5400,J. Leukoc. Biol. 0022-2275,J. Lipid Res. 0022-2372,J. Mammal. 1064-7554,J. Mammal. Evol. 0022-2623,J. Med. Chem. 0022-2585,J. Med. Entomol. 0022-2593,J. Med. Genet. 0022-2615,J. Med. Microbiol. 0268-1218,J. Med. Vet. Mycol. 0146-6615,J. Med. Virol. 0022-2631,J. Membr. Biol. 1017-7825,J. Microbiol. Biotechnol. 0271-6801,J. Mol. Appl. Genet. 0022-2836,J. Mol. Biol. 0022-2828,J. Mol. Cell. Cardiol. 0952-5041,J. Mol. Endocrinol. 0022-2844,J. Mol. Evol. 0263-7855,J. Mol. Graph. 0946-2716,J. Mol. Med. 0895-8696,J. Mol. Neurosci. 0952-3499,J. Mol. Recognit. 0142-4319,J. Muscle Res. Cell. Motil. 0027-8874,J. Natl. Cancer Inst. 0300-9564,J. Neural Transm. 0022-3034,J. Neurobiol. 0022-3042,J. Neurochem. 0953-8194,J. Neuroendocrinol. 0167-7063,J. Neurogenet. 0165-5728,J. Neuroimmunol. 0022-510X,J. Neurol. Sci. 0167-594X,J. Neurooncol. 0022-3069,J. Neuropathol. Exp. Neurol. 0270-6474,J. Neurosci. 0360-4012,J. Neurosci. Res. 0022-3166,J. Nutr. 0955-2863,J. Nutr. Biochem. 0022-3476,J. Pediatr. 1397-002X,J. Pept. Res. 1075-2617,J. Pept. Sci. 0373-1022,J. Pharm. Pharmacol. 0022-3565,J. Pharmacol. Exp. Ther. 0022-3646,J. Phycol. 0176-1617,J. Plant Physiol. 0035-9173,J. Proc. Royal Soc. N.S. Wales 0277-8033,J. Protein Chem. 0022-3921,J. Protozool. 0197-5110,J. Recept. Res. 1079-9893,J. Recept. Signal Transduct. Res. 0916-8818,J. Reprod. Dev. 0022-4251,J. Reprod. Fertil. 0315-162X,J. Rheumatol. 0038-2078,J. S. Afr. Chem. Inst. 0730-8000,J. Shellfish Res. 0098-843X,J. South. Calif. Dent. Assoc. 0022-4731,J. Steroid Biochem. 0960-0760,J. Steroid Biochem. Mol. Biol. 1047-8477,J. Struct. Biol. 0022-4782,J. Submicrosc. Cytol. Pathol. 0091-7419,J. Supramol. Struct. 0022-5193,J. Theor. Biol. 0022-5347,J. Urol. 0931-1793,J. Vet. Med. B 0916-7250,J. Vet. Med. Sci. 0022-538X,J. Virol. 0166-0934,J. Virol. Methods 0098-7484,JAMA 0021-5074,Jinrui Idengaku Zasshi 0091-7400,Johns Hopkins Med. J. Suppl. 0047-1828,Jpn. Circ. J. 0910-5050,Jpn. J. Cancer Res. 0021-504X,Jpn. J. Genet. 0021-5139,Jpn. J. Microbiol. 0021-5198,Jpn. J. Pharmacol. 0047-1917,Jpn. J. Vet. Res. 0075-4617,Justus Liebigs Ann. Chem. 0368-5063,Kagoshima Daigaku Igaku Zasshi 0387-5911,Kansenshogaku Zasshi 0250-7862,Kexue Tongbao 0023-1150,Khim. Prirod. Soedin. 0085-2538,Kidney Int. 0300-9149,Kokubyo Gakkai Zasshi 0378-8512,Korean J. Biochem. 0440-2413,Korean J. Microbiol. 0023-6837,Lab. Invest. 0140-6736,Lancet 1072-0502,Learning Memory 0266-8254,Lett. Appl. Microbiol. 0929-5666,Lett. Pept. Sci. 0887-6924,Leukemia 0024-3205,Life Sci. 0024-4201,Lipids 0277-6766,Lymphokine Res. 0938-8990,Mamm. Genome 0141-1136,Mar. Environ. Res. 0934-8832,Matrix 0945-053X,Matrix Biol. 0025-6153,Maydica 0047-6374,Mech. Ageing Dev. 0925-4773,Mech. Dev. 0960-8931,Melanoma Res. 0091-679X,Meth. Cell Biol. 0076-6879,Meth. Enzymol. 1090-6592,Microb. Comp. Genomics 1076-6294,Microb. Drug Resist. 0882-4010,Microb. Pathog. 0385-5600,Microbiol. Immunol. 0944-5013,Microbiol. Res. 0146-0749,Microbiol. Rev. 1350-0872,Microbiology 0026-3788,Milchwissenschaft 0166-6851,Mol. Biochem. Parasitol. 0026-8933,Mol. Biol. 1059-1524,Mol. Biol. Cell 0737-4038,Mol. Biol. Evol. 0735-1313,Mol. Biol. Med. 0301-4851,Mol. Biol. Rep. 0899-1987,Mol. Carcinog. 1097-2765,Mol. Cell 0300-8177,Mol. Cell. Biochem. 0270-7306,Mol. Cell. Biol. 1065-3074,Mol. Cell. Differ. 0303-7207,Mol. Cell. Endocrinol. 1044-7431,Mol. Cell. Neurosci. 0890-8508,Mol. Cell. Probes 1016-8478,Mol. Cells 1044-7393,Mol. Chem. Neuropathol. 0962-1083,Mol. Ecol. 0888-8809,Mol. Endocrinol. 0026-8925,Mol. Gen. Genet. 0161-5890,Mol. Immunol. 1053-6426,Mol. Mar. Biol. Biotechnol. 1076-1551,Mol. Med. 0968-7688,Mol. Membrane Biol. 0950-382X,Mol. Microbiol. 0893-7648,Mol. Neurobiol. 0026-895X,Mol. Pharmacol. 1055-7903,Mol. Phylogenet. Evol. 0894-0282,Mol. Plant Microbe Interact. 1040-452X,Mol. Reprod. Dev. 0026-9247,Monatsh. Chem. 0148-639X,Muscle Nerve 0027-5107,Mutat. Res. 0953-7562,Mycol. Res. 0027-7649,Nagoya Med. J. 1087-0156,Nat. Biotechnol. 0385-6283,Nat. Cult. 1061-4036,Nat. Genet. 0254-7600,Nat. Immun. Cell Growth Regul. 1078-8956,Nat. Med. 1072-8368,Nat. Struct. Biol. 1056-9014,Nat. Toxins 0028-0836,Nature 0090-0028,Nature New Biol. 0028-1042,Naturwissenschaften 0028-1298,Naunyn Schmiedebergs Arch. Pharmacol. 0028-209X,Neth. Milk Dairy J. 0197-4580,Neurobiol. Aging 0197-0186,Neurochem. Int. 0364-3190,Neurochem. Res. 0028-3835,Neuroendocrinology 1021-7401,Neuroimmunomodulation 0028-3878,Neurology 0960-8966,Neuromuscul. Disord. 0896-6273,Neuron 0143-4179,Neuropeptides 0028-3908,Neuropharmacology 0893-133X,Neuropsychopharmacology 0959-4965,Neuroreport 0304-3940,Neurosci. Lett. 0168-0102,Neurosci. Res. 0893-6609,Neurosci. Res. Commun. 0306-4522,Neuroscience 1043-4674,New Biol. 0028-4793,New Engl. J. Med. 0914-5818,Nihon Hosenkin Gakkai Shi 0048-0444,Nippon Ika Daigaku Zasshi 0047-1852,Nippon Rinsho 0029-4810,Nouv. Rev. Fr. Hematol. 0305-1048,Nucleic Acids Res. 0309-1872,Nucleic Acids Res. Spec. Publ. 0261-3166,Nucleic Acids Symp. Ser. 0950-9232,Oncogene 0890-6467,Oncogene Res. 0030-3747,Ophthalmic Res. 0161-6420,Ophthalmology 0902-0055,Oral Microbiol. Immunol. 0030-493X,Org. Mass Spectrom. 0885-3177,Pancreas 1383-5769,Parasitol. Int. 0932-0113,Parasitol. Res. 0031-1820,Parasitology 0048-2951,Parassitologia 1054-9803,PCR Methods Appl. 0031-3998,Pediatr. Res. 0892-0672,Pediatrics 1040-5704,Pept. Res. 0196-9781,Peptides 0031-613X,Pestic. Sci. 0031-6768,Pflugers Arch. 0724-8741,Pharm. Res. 0960-314X,Pharmacogenetics 1043-6618,Pharmacol. Res. 0163-7258,Pharmacol. Ther. 0031-8655,Photochem. Photobiol. 0166-8595,Photosyn. Res. 0031-9325,Physiol. Chem. Phys. 0885-5765,Physiol. Mol. Plant Pathol. 0031-9317,Physiol. Plantarum 0031-9368,Physiol. Veg. 0031-9422,Phytochemistry 0031-949X,Phytopathology 0893-5785,Pigment Cell Res. 1000-8721,Ping Tu Hsueh Pao 1040-4651,Plant Cell 0032-0781,Plant Cell Physiol. 0721-7714,Plant Cell Rep. 0960-7412,Plant J. 0167-4412,Plant Mol. Biol. 0735-9640,Plant Mol. Biol. Rep. 0032-0889,Plant Physiol. 0981-9428,Plant Physiol. Biochem. 0168-9452,Plant Sci. 0304-4211,Plant Sci. Lett. 0378-2697,Plant Syst. Evol. 0032-0935,Planta 0147-619X,Plasmid 0032-5791,Poult. Sci. 0032-7484,Prep. Biochem. 0027-8424,Proc. Natl. Acad. Sci. U.S.A. 0037-9727,Proc. Soc. Exp. Biol. Med. 0083-8969,Proc. West. Pharmacol. Soc. 0079-6123,Prog. Brain Res. 0361-7742,Prog. Clin. Biol. Res. 0079-6751,Prog. Respir. Res. 0090-6980,Prostaglandins 0952-3278,Prostaglandins Leukot. Essent. Fatty Acids 0269-2139,Protein Eng. 1046-5928,Protein Expr. Purif. 0929-8665,Protein Pept. Lett. 0961-8368,Protein Sci. 0931-9506,Protein Seq. Data Anal. 0887-3585,Proteins 0955-8829,Psychiatr. Genet. 0033-4545,Pure Appl. Chem. 0951-4198,Rapid Commun. Mass Spectrom. 0079-9963,Recent Prog. Horm. Res. 1060-6823,Recept. Channels 1052-8040,Receptor 0167-0115,Regul. Pept. 1031-3613,Reprod. Fertil. Dev. 0923-2508,Res. Microbiol. 0034-5288,Res. Vet. Sci. 0923-2516,Res. Virol. 0338-4535,Rev. Fr. Transfus. Immunohematol. 0187-4640,Rev. Latinoam. Microbiol. 0047-1860,Rinsho Byori 1355-8382,RNA 1068-1620,Russ. J. Bioorg. Chem. 0379-4350,S. Afr. J. Chem. 0038-2353,S. Afr. J. Sci. 0257-2389,Sanop Misaengmul Hakhoe Chi 0036-472X,Sapporo Igaku Zasshi 0036-5521,Scand. J. Gastroenterol. 0300-9475,Scand. J. Immunol. 0036-8733,Sci. Am. 0250-7870,Sci. Sin. 0036-8075,Science 0031-9082,Seibutsubutsurikagaku 0037-1017,Seikagaku 0734-8630,Semin. Reprod. Endocrinol. 1044-5773,Semin. Virol. 0934-0882,Sex. Plant Reprod. 0253-9918,Shengwu Huaxue Yu Shengwu Wuli Jinzhan 0029-8484,Shigaku 0037-5349,Silvae Genetica 0583-421X,Singmul Hakhoe Chi 0740-7750,Somat. Cell Mol. Genet. 0360-4497,Sov. J. Bioorg. Chem. 0038-5638,Sov. Phys. Crystallogr. 0039-128X,Steroids 0039-2499,Stroke 0969-2126,Structure 0081-6337,Studia Biophys. 0039-6060,Surgery 0723-2020,Syst. Appl. Microbiol. 1063-5157,Syst. Biol. 0363-6445,Syst. Bot. 0039-7989,Syst. Zool. 0371-7682,Taiwan I Hsueh Hui Tsa Chih 1013-2791,Tanaguchi Symp. Brain Sci. 0040-4020,Tetrahedron 0040-4039,Tetrahedron Lett. 0040-4675,Tex. Rep. Biol. Med. 0040-5175,Text. Res. J. 0040-5752,Theor. Appl. Genet. 0093-691X,Theriogenology 0340-6245,Thromb. Haemost. 0049-3848,Thromb. Res. 0165-6090,Thymus 1050-7256,Thyroid 0001-2815,Tissue Antigens 0041-008X,Toxicol. Appl. Pharmacol. 0731-9193,Toxicologist 0041-0101,Toxicon 0066-0132,Trans. Am. Soc. Neurochem. 0066-9458,Trans. Assoc. Am. Physicians 0041-1132,Transfusion 0962-8819,Transgenic Res. 0041-1337,Transplantation 0376-5067,Trends Biochem. Sci. 1043-2760,Trends Endocrinol. Metab. 0168-9525,Trends Genet. 0378-5912,Trends Neurosci. 0165-6147,Trends Pharmacol. Sci. 0177-2392,Trop. Med. Parasitol. 0041-4093,Tumor Res. 0201-8470,Ukr. Biokhim. Zh. 0300-9734,Ups. J. Med. Sci. 0264-410X,Vaccine 0165-2427,Vet. Immunol. Immunopathol. 0378-1135,Vet. Microbiol. 0042-4900,Vet. Rec. 0165-7380,Vet. Res. Commun. 0042-6822,Virology 0920-8569,Virus Genes 0168-1702,Virus Res. 0952-5238,Vis. Neurosci. 0042-6989,Vision Res. 0300-0281,Viva Orig. 0042-8809,Vopr. Med. Khim. 0042-9007,Vox Sang. 0908-665X,Xenotransplantation 0749-503X,Yeast 0372-8609,Z. Vererbungsl. 0044-4529,Zh. Evol. Biokhim. Fiziol. 0372-9311,Zh. Mikrobiol. Epidemiol. Immunobiol. 0250-3263,Zool. Res. 0289-0003,Zool. Sci. 0967-1994,Zygote Swissknife_1.75/lib/SWISS/OCs.pm0000644005110600510130000000372610366115237016565 0ustar ecastroSwissProtpackage SWISS::OCs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields $uppercase); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; $uppercase = 0; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $textRef = shift; my @tmp; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'OC'})/m){ my $line=join " ", map { $self->{indentation} += s/^ //; SWISS::TextFunc->cleanLine($_) } split /\n/m, $1; @tmp = SWISS::TextFunc->listFromText($line, ';\s*', '\.\s*'); push (@{$self->list()}, @tmp); } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my (@lines, $newText); return unless @{$self->list}; $newText = join('; ', @{$self->list}) . "."; my $prefix = "OC "; my $col = $SWISS::TextFunc::lineLength; $col++, $prefix=" $prefix" if $self->{indentation}; $newText = SWISS::TextFunc->wrapOn($prefix, $prefix, $col, $newText , ';\s+'); $newText =~ tr/a-z/A-Z/ if $uppercase; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'OC'}); } # OCs must never be sorted, overwrite the inherited sort method. sub sort { return 1; } 1; __END__ =head1 Name SWISS::OCs =head1 Description B represents the OC lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each list element is an item giving one part of the taxonomic classification of the source organism of the protein. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item sort =back Swissknife_1.75/lib/SWISS/OGs.pm0000644005110600510130000000645113147300251016557 0ustar ecastroSwissProtpackage SWISS::OGs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::OG; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub initialize { } sub fromText { my $self = new(shift); my $textRef = shift; my $line = ""; my @tmp; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'OG'})/m){ $line = join ' ', map { $self->{indentation} += s/^ //; SWISS::TextFunc->cleanLine($_); } (split /\n/m, $1 ); # drop 'AND' $line =~ s/\s*,\s*(AND\s+)*/, /gi; # Step one: Split on dots separating organelle classes (Plasmid, Mitochondrion). # complex expression for separator to make sure commas within brackets are # not regarded as separators. @tmp = SWISS::TextFunc->listFromText($line, '\.\s+', '\.'); # Step two: Split on commas separating elements of organelle classes. my @resultList; foreach my $organelle (@tmp) { push @resultList, SWISS::TextFunc->listFromText($organelle, ',\s+(?![^\(\{]+[\)\}])', '\.'); } @resultList = map {SWISS::OG->fromText($_)} @resultList; push (@{$self->list()}, @resultList); } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my (@tmp, @lines); my (@plasmids, @nonPlasmids); my $nonPlasmidText = ''; my $plasmidText = ''; @tmp = $self->elements(); foreach my $element (@tmp) { if ($element->isPlasmid()) { push @plasmids, $element; } else { push @nonPlasmids, $element; } } # First format all non-plasmid elements foreach my $nonPlasmid (@nonPlasmids) { my $indent = $self->{indentation} ? " " : ""; $nonPlasmidText .= "${indent}OG " . $nonPlasmid->toText() . ".\n"; } # Format plasmids if ($#plasmids > -1) { # insert an 'AND' before the last species if appropriate @tmp = map {$_->toText} @plasmids; if ($#tmp > 0) { push(@tmp, 'and '. pop(@tmp)); } $plasmidText = join(", ", @tmp); $plasmidText .= "."; my $prefix = "OG "; my $col = $SWISS::TextFunc::lineLength; $col++, $prefix=" $prefix" if $self->{indentation}; $plasmidText = SWISS::TextFunc->wrapOn($prefix, $prefix, $col, $plasmidText, ',\s+and\s+', ',\s+', '(?=\()', '\s+'); }; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $nonPlasmidText . $plasmidText, $SWISS::TextFunc::linePattern{'OG'}); } # OGs must never be sorted, overwrite the inherited sort method. sub sort { return 1; } 1; __END__ =head1 Name SWISS::OGs =head1 Description B represents the OG lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OGs object is a container object which holds a list of SWISS::OG objects. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each list element is a SWISS::OG object. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/PE.pm0000644005110600510130000000241513147300251016367 0ustar ecastroSwissProtpackage SWISS::PE; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( text => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $textRef = shift; my $text = ""; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'PE'})/m){ $text = $1; $self->{indentation} += $text =~ s/^ //; $text = SWISS::TextFunc->cleanLine($text); if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { $self->evidenceTags($1); } $self->text($text); } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; if ($self->text) { return $self->text . $self->getEvidenceTagsString; } } 1; __END__ =head1 Name SWISS::PE =head1 Description Indicates what kind of evidence there is for the existence of a protein. =head1 Inherits from SWISS::BaseClass =head1 Attributes =over =item C The type of evidence. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/OG.pm0000644005110600510130000000243310366115237016400 0ustar ecastroSwissProtpackage SWISS::OG; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( text => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $text = shift; # Parse out the evidence tags if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { my $tmp = $1; $self->evidenceTags($tmp); } $self->text($text); return $self; } sub toText { my $self = shift; return $self->text . $self->getEvidenceTagsString; } sub isPlasmid { my $self = shift; return $self->text =~ /Plasmid/i; } 1; __END__ =head1 Name SWISS::OGs =head1 Description B represents one organelle or plasmid name from the OG line. The container object holding all organelle or plasmid names is SWISS::OGs. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C One OG line element. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Specific methods =over =item isPlasmid =back Swissknife_1.75/lib/SWISS/ACs.pm0000644005110600510130000000647110366115237016547 0ustar ecastroSwissProtpackage SWISS::ACs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $textRef = shift; my $line; my @tmp; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'AC'})/m){ foreach $line (split /\n/m, $1) { # drop ** Comment lines if (($line =~ /^\*\*/) && ($line !~ /^\*\* [OPQ][\w]{5};/)) { if ($main::opt_warn) { carp "Dropped \'$line\' from AC line block"; } next; } $self->{indentation} += $line =~ s/^ //; $line = SWISS::TextFunc->cleanLine($line); @tmp = SWISS::TextFunc->listFromText($line, ';\s*', ';\s*'); push (@{$self->list()}, @tmp); } } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my (@lines, $newText); $newText = join('; ', @{$self->list}) . ";"; my $prefix = "AC "; my $col = $SWISS::TextFunc::lineLength; $col++, $prefix=" $prefix" if $self->{indentation}; $newText = SWISS::TextFunc->wrapOn($prefix, $prefix, $col, $newText, '; '); $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'AC'}); } # sort secondary ACs sub sort { my $self = shift; my $l = $self->{list}; if (@$l > 1) { @$l = ($l->[0], sort @$l[1..$#$l]); } return 1; } sub update { my $self = shift; my $force = shift; # Potential duplicates should be removed. $self->unique(); # The secondary ACs should be sorted. $self->sort(); return 1; } 1; # says use was ok __END__ =head1 Name SWISS::ACs =head1 Description B represents the AC (accession) lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The SWISS-PROT format has recently been changed to multiple AC lines. This module will read Ordinary AC lines AC P10585; The old temporary format (for internal use only) AC Q57333; O08291; O08202; O08292; O08203; O08293; O08204; O08294; ** O08205; O08295; O08206; O08296; O08207; O08297; O08208; O08298; ** O08213; and the new format. AC Q57333; O08291; O08202; O08292; O08203; O08293; O08204; O08294; AC O08205; O08295; O08206; O08296; O08207; O08297; O08208; O08298; AC O08213; But, SWISS::ACs will DROP funny ** comment lines that are sometimes found following an AC line: AC Q48558; P71434; ** MERGED 2 TREMBL ENTRIES. This module will always write the new format with multiple AC lines. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C This is an array containing a list of all the accession numbers associated with this entry. The first member will be the primary accession number, and any following are the secondary accession numbers. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item sort This method sorts the secondary AC numbers alphanumerically, i.e. all but the first. The primary AC number must never be sorted. =back Swissknife_1.75/lib/SWISS/FTs.pm0000644005110600510130000002655613147300251016573 0ustar ecastroSwissProtpackage SWISS::FTs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields %KEYORDER); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } #initialization code: stuff DATA into hash { # Leading and trailing spaces are MANDATORY! local $/="\n"; my $index=0; my $line; while (defined ($line=)) { $line =~ s/\s+\z//; $index++; $KEYORDER{$_} = $index for split /\s+/, $line; } close DATA; } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::FTs; my $line; my $indentation = 0; my ($key, $from, $to, $description); # attributes of one feature if ( $$textRef =~ /($SWISS::TextFunc::linePattern{'FT'})/m ) { foreach $line ( split /\n/m, $1 ) { my $_indent = $line =~ s/^ //; $line = SWISS::TextFunc->cleanLine($line); if ( $line =~ /^(\S+)\s+(\S+)\s+(\S+)\s*(.*)$/ ) { # first line of a feature # if there is a previous line, write it if ($key) { $description = &_cleanDescription($key, $description); my $ft = [$key, $from, $to, _unpack($description)]; push @{$self->list()}, $ft; push @{$self->{indentation}}, [$ft->[0], $ft->[1], $ft->[2], $ft->[3]] if $indentation; $indentation = 0; } # assign new values $key = $1; $from = $2; $to = $3; $description = $4; } elsif ( $line =~ /^\s+(.*)$/ ) { # continuation of a feature description $description = SWISS::TextFunc->joinWith($description, ' ', '(?list() }, $ft; push @{ $self->{ indentation } }, [ $ft->[0], $ft->[1], $ft->[2], $ft->[3] ] if $indentation; } } else { $self->initialize; } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my $newText = ''; if ($#{$self->list()}>-1) { $newText = join('', map {$self->_FTtoText($_, @{$_})} @{$self->list()}); }; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'FT'}); } sub _unpack { my $text = shift; my ($evid, $ftid, $evidenceTags) = ('','','{}'); return ('','','','{}') unless $text; if ($text =~ s/(\/FTId=\S+)$//){ $ftid = $1; $ftid =~ s/\.$//; $text =~ s/[\n\.\s]+$//sg; } # Parse out the evidence tags if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { $evidenceTags = $1; # p.s. with new evtag format $1 = ' {ECO:...}' (with extra space), old format is e.g. '{EC1}' $evidenceTags =~s/: /:/ if $evidenceTags =~/ECO:/; # fugly: now evtag can be wrapped on : (to solve too long-because-of-ev FT lines problem!), will be unwrapped with an extra space after : (as I can not use variable lenght negative lookback in regex when using joinWith) } # Get the old-style Swiss-Prot evidence if ($text =~ s/ \((BY SIMILARITY|POTENTIAL|PROBABLE)\)$//i){ $evid = $1; } elsif (grep {$_ eq uc $text} ('BY SIMILARITY', 'POTENTIAL', 'PROBABLE')) { $evid = $text; $text = ""; } $text =~ s/[\n\.\s]+$//sg; return ($text, $evid, $ftid, $evidenceTags); } # remove wrongly inserted ' ' in description # of CONFLICT, VARIANT, VAR_SEQ and VARSPLIC sub _cleanDescription { my ($key, $description) = @_; # parts of the description of CONFLICT, VARIANT, VAR_SEQ and VARSPLIC my ($sequence, $ref); # Remove trailing dots and spaces $description =~ s/[\s\.]+$//; if (($key eq 'CONFLICT') || ($key eq 'VARIANT') || ($key eq 'VAR_SEQ') || ($key eq 'VARSPLIC')) { # The * is allowed as part of the description for cases like # AC Q50855: AVWKA -> R*SVP if ($description !~ /^Missing/) { if (($sequence, $ref) = $description =~ /([A-Z \-\>\*]+)(.*)/) { $sequence =~ s/(?/ \-\> /; $sequence .= ' ' unless $ref =~ /^\{/; $description = $sequence . $ref; } } } if ($key eq 'MUTAGEN') { if ($description !~ /^Missing/) { if (($sequence, $ref) = $description =~ /([A-Z \-\>\*,]+)(.*)/) { $sequence =~ tr/ //d; $description = $sequence . $ref; } } } return $description; } sub _FTtoText { my ($self, $ft, $key, $from, $to, $description, $evidence, $ftid, $evidenceTags) = @_; my ($prefix, $text); $text = ''; $prefix = sprintf("FT %-8s %5s %5s ", $key, $from, $to); if ($evidence) { if (length $description){ $description = "$description ($evidence)"; } else { $description = $evidence; } } # add the evidence tags if ($evidenceTags && $evidenceTags ne '{}' ) { if ( $evidenceTags =~/ECO:/ && $description ) { # with new evtag format put . before evtag (if the desc core is not empty) $description .= "." . $evidenceTags } else { $description .= $evidenceTags; } } if (length $description ) { $text = $description; # Add a dot at the end if the description does not consist only of # oldformat evidence tags. unless ($description =~ /\A$SWISS::TextFunc::evidencePatternOld\Z/) { $text .= '.'; } } else { # Text must not be empty, otherwise the wrapping will return '' $text .= ' '; } # Complex rules for the formatting of FT VARIANT, FT CONFLICT, FT VARSPLIC # according to softuse.txt, SFT006 if ( $prefix =~ /CONFLICT|VARIANT|VAR_SEQ|VARSPLIC/ ) { $text = SWISS::TextFunc->wrapOn($prefix, "FT ", $SWISS::TextFunc::lineLength, $text, ['(?!\>)\s*', '[{(]', "/|$SWISS::TextFunc::textWrapPattern1", '[^\s\-/]'], "/|:(?=[^}]+\\})|$SWISS::TextFunc::textWrapPattern2" ); # wrap on ws not after > or if already wrapped/current line has { or (: wrap on "/" or some ws or "-", # then "/" or ":" inside evtags or some "-" } elsif( $key eq "MUTAGEN" ) { $text = SWISS::TextFunc->wrapOn($prefix, "FT ", $SWISS::TextFunc::lineLength, $text, "$SWISS::TextFunc::textWrapPattern1", "/|:(?=[^}]+\\})|$SWISS::TextFunc::textWrapPattern2|(?<=.{39})[A-Z](?=->)" ); # wrap on some ws or "-", then "/" or ":" inside evtags or some "-", then # before default split on any char after max size: if "-" in XXX->YYY is at max pos, do wrap on previous AA } else { # wrapping for other FT lines $text = SWISS::TextFunc->wrapOn($prefix, "FT ", $SWISS::TextFunc::lineLength, $text, "$SWISS::TextFunc::textWrapPattern1", "/|:(?=[^}]+\\})|$SWISS::TextFunc::textWrapPattern2" ); # wrap on some ws or "-", then "/" or ":" inside evtags or some "-" }; # add a /FTId line if necessary if (length $ftid){ $text .= "FT $ftid.\n"; } # reinsert indentation if ($self->{indentation}) { for my $indented (@{$self->{indentation}}) { next unless $ft->[0] eq $indented->[0] and $ft->[1] eq $indented->[1] and $ft->[2] eq $indented->[2] and $ft->[3] eq $indented->[3]; $text =~ s/^/ /mg; last; } } return $text; } #sorting based on annotation rule ANN027, #and additional instructions from Amos. #FTs should be sorted based on : #-the priority index, or #-the starting position (lesser goes first), or #-the ending position (longer goes first), or #-the FT comment as a last resort. sub sort { my $self = shift; my $self_list = $self->list; my @indices = sort { my $item1 = ${$self_list}[$a]; my $item2 = ${$self_list}[$b]; my $sv = #sort by virtual key ($KEYORDER{$item1->[0]} || 0) <=> ($KEYORDER{$item2->[0]} || 0) || #or by start position _numericPosition($item1->[1], $item1->[2]) <=> _numericPosition($item2->[1], $item2->[2]) || #or by end position (reversed) _numericPosition($item2->[2], $item2->[1]) <=> _numericPosition($item1->[2], $item1->[1]); #for FT VARSPLIC and VAR_SEQ: #as a penultimate resort, alphabetically on what follows the parenthesis #in the FTcomment if (!$sv and $item1->[0] =~ /^VARSPLIC|VAR_SEQ$/ and my ($t1) = $item1->[3] =~ /\((.*)/ and my ($t2) = $item2->[3] =~ /\((.*)/ ) { $sv = lc($t1) cmp lc($t2) || $t1 cmp $t2; } #for FT CONFLICT+VARIANT: #as a penultimate resort, alphabetically on FTcomment #(except "Missing" that should go at the end) unless ($sv) { if (grep {$_ eq $item1->[0]} ("CONFLICT", "VARIANT", "MUTAGEN")) { if ($item1->[3] =~ /^Missing/i) { unless ($item2->[3] =~ /^Missing/i) { $sv = 1; } } else { if ($item2->[3] =~ /^Missing/i) { $sv = -1; } } } } #as a last resort, alphabetically on FTcomment (e.g. variants) $sv || lc($item1->[3]) cmp lc($item2->[3]) || $item1->[3] cmp $item2->[3] } 0..$#$self_list; my @newlist; for (@indices) { push @newlist, ${$self_list}[$_]; } $self->list(\@newlist); } # For a given feature position, return the numeric position. # This converts "fuzzy" positions for sorting purpose, according to the rule: # 11 => 11 # >14 => 14.1 # <1 => 0.9 # ?31 => 31 # if a position is only "?", the other position should be passed as a second # argument, to be used as a backup. For example, if a feature is # FT CHAIN ? 103 Potential. # the position 103 should be considered the best-guess start position for sorting. sub _numericPosition { for my $string (@_) { return $1+0.1 if $string =~ />(\d+)/; return $1-0.1 if $string =~ /<(\d+)/; return $1 if $string =~ /(\d+)/; } return 0; } 1; =head1 Name SWISS::FTs =head1 Description B represents the FT (feature) lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C An array of arrays. Each element is an array containing: a feature key, from position, to position, description, qualifier, FTId and an evidence tag. Example: ['CHAIN', 25, 126, 'Alpha chain', 'By similarity', '/FTId=PRO_0000023008', '{EC1}'] =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item sort =back =cut __DATA__ INIT_MET SIGNAL PROPEP TRANSIT CHAIN PEPTIDE TOPO_DOM TRANSMEM INTRAMEM DOMAIN REPEAT CA_BIND ZN_FING DNA_BIND NP_BIND REGION COILED MOTIF COMPBIAS ACT_SITE METAL BINDING SITE NON_STD MOD_RES LIPID CARBOHYD DISULFID CROSSLNK VAR_SEQ VARIANT MUTAGEN UNSURE CONFLICT NON_CONS NON_TER HELIX TURN STRAND Swissknife_1.75/lib/SWISS/Entry.pm0000644005110600510130000003267613147300251017200 0ustar ecastroSwissProtpackage SWISS::Entry; use 5.005; use vars qw($AUTOLOAD @ISA @EXPORT_OK $VERSION %fields %objects); use Exporter; use Carp; use strict; use SWISS::TextFunc; $VERSION='1.75'; # * Initialisation # The objects for the different line types my %objects = ( IDs => undef, ACs => undef, DTs => undef, DEs => undef, GNs => undef, OSs => undef, OGs => undef, OCs => undef, OXs => undef, OHs => undef, Refs => undef, CCs => undef, DRs => undef, PE => undef, KWs => undef, FTs => undef, Stars => undef, SQs => undef, ); # All attributes my %fields = ( _dirty => undef, _text => undef, _internalComments => undef, %objects, ); BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter'); } # * Methods sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = { '_permitted' => \%fields, %fields }; bless $self, $class; $self->initialize(); return $self; } sub initialize { my $self = shift; my $text = "\/\/\n"; $self->{_text} = \$text; return $self; } sub AUTOLOAD { my $self = shift; my $value; my $type = ref($self) || carp "Ok, $self is not an object of mine!"; my $name = $AUTOLOAD; # * Initialise if (@_) { $value = shift; } else { undef $value; } # get only the bit we want $name =~ /::DESTROY/ && return; $name =~ s/.*://; # Verify if the demanded name is permitted unless (exists $self->{'_permitted'}->{$name} ) { confess "In type $type, can't access $name - probably passed a wrong variable into $self "; }; # * If a value is passed, set it if (defined $value) { # if a subobject is set, it's dirty if (defined $value->{_dirty}) { $value->{_dirty} = 1; }; $self->{_dirty} = 1; return $self->{$name} = $value; } else { # nothing is set, a value has to be returned if (defined $self->{$name}) { # The object is defined, return it return $self->{$name}; } else { require 'SWISS/' . $name . '.pm'; if (exists $objects{$name}) { # create and return new object return $self->{$name} = ('SWISS::' . $name)->fromText($self->{_text}); } else { # return the undefined value return $self->{$name}; } } } }; sub update { my $self = shift; my $force = shift; # force update my $lineObject; # recursively check and update all existing line objects if ($force) { foreach $lineObject (grep {$self->{$_}} keys %objects) { $self->{$lineObject}->update($force); $self->{_dirty} = 1; }; }; # The entry itself # update interdependent lines if ($self->{IDs} && $self->{SQs}) { $self->IDs->length($self->SQs->length()); }; return 1; } sub fullParse { my $self = shift; my $lineObject; my $tmp; # Parse all known objects foreach $lineObject (@SWISS::TextFunc::lineObjects){ $tmp = $self->$lineObject(); } } sub reformat { my $self = shift; my $lineObject; $self->fullParse; # recursively reformat all existing line objects foreach $lineObject (grep {$self->{$_}} keys %objects) { $self->{$lineObject}->{_dirty} = 1; }; return 1; } sub fromText { my $class = shift; my $text = shift; my $fullParse = shift; my $removeInternalComments = shift; unless ($text) { confess "fromText called with an empty text reference."; }; my $self = new $class; $self->{_text} = \$text; #handle internal comments if ($removeInternalComments) { my $internalComments = SWISS::TextFunc::removeInternalComments(\$text); $self->{_internalComments} = $internalComments; } if ($fullParse) { $self->fullParse; } return $self; } sub toText { my $self = shift; my $insertCommentLines = shift; my $lineObject; # update the object $self->update(); # recursively update the text representation foreach $lineObject (keys %objects) { if (defined $self->{$lineObject}) { $self->$lineObject()->toText($self->{_text}); } }; #handle internal comments if ($insertCommentLines) { my $internalComments = $self->{_internalComments}; if ($internalComments) { my @remainingComments = SWISS::TextFunc::restoreInternalComments($self->{_text}, $internalComments); if (@remainingComments) { $self->Stars->ZZ->add(@remainingComments); #update Stars section $self->Stars->toText($self->{_text}); } } } # Now the object is clean $self->{_dirty}=0; return ${$self->{_text}}; } sub toFastaOld { my $self = shift; my $FASTA_LINELEN = 60; my $result = ""; # if there is no AC or sequence, return 0 and warn unless ($self->AC && $self->SQ){ if ($main::opt_warn) { carp "No Fasta written for $self"; }; return 0; } # fasta header ">AC|ID DE - OS" my $name = $self->DEs->text; my $organism = $self->OSs->head->text; my $namelen = 255 - 15 - length($self->ID) - length($organism); $namelen -= length($self->DEs->hasFragment) + 3 if $self->DEs->hasFragment; $name =~ s/ \(.+//; if ((length $name) > $namelen) { $name = substr($name, 0, $namelen); $name =~ s/\s+$//; $name .= '...'; }; $name .= ' (' . $self->DEs->hasFragment . ')' if $self->DEs->hasFragment; $result = '>' . $self->AC . '|' . $self->ID . ' ' . $name . ' - ' . $organism; $result .= "\n"; # format the sequence, $FASTA_LINELEN AAs per line $result .= join "\n", ($self->SQ =~ m/.{1,$FASTA_LINELEN}/g); $result .= "\n"; return $result; } sub toFasta { my $self = shift; my $FASTA_LINELEN = 60; my $result = ""; # if there is no AC or sequence, return 0 and warn unless ($self->AC && $self->SQ){ if ($main::opt_warn) { carp "No Fasta written for $self"; }; return 0; } # fasta header ">sp|AC|ID DE OS= [GN= ]PE= SV=" ( my $name = $self->DEs->head->text || '?' ) =~ s/ precursor$//; my $os = $self->OSs->head->text || '?'; ( my $organism = $os ) =~ s/ \(.+$//; $os =~ s/^.+? (?=\()//; foreach my $elem ( split /(?<=\))\s+(?=\()/, $os ) { $elem =~ s/^\(|\)\.?$//g; $organism.= ' ('.$elem.')' if $elem =~ /^strain|^isolate/; } my $gn = $self->GNs->getFirst(); ( my $pe = $self->PE->toText() ) =~ s/:.+$//; my $sv = $self->DTs->SQ_version(); $name .= ' (' . $self->DEs->hasFragment . ')' if $self->DEs->hasFragment; $result = '>' . ( $self->isCurated ? 'sp' : 'tr' ). '|' . $self->AC . '|' . $self->ID . ' ' . $name . ' OS=' . $organism . ( $gn ? " GN=$gn" : '' ) . ( $pe ? " PE=$pe" : '' ) . ( $sv ? " SV=$sv" : '' ); $result .= "\n"; # format the sequence, $FASTA_LINELEN AAs per line $result .= join "\n", ( $self->SQ =~ m/.{1,$FASTA_LINELEN}/g ); $result .= "\n"; return $result; } # If this funtion returns true for an entry, the entry should be # processed correctly by swissknife. It does not mean that the entry # is syntactically correct. sub syntaxOk { my $self = shift; my $text = ''; $text = $self->text; if ($text =~ / \A # Beginning of the entry ((ID .*\n)+(\*\* .*\n)*){1} ((AC .*\n)+(\*\* .*\n)*){1} (DT .*\n){3} (DE .*\n)* (GN .*\n)* (OS .*\n)+ (OG .*\n)* (OC .*\n)+ (OX .*\n)+ (OH .*\n)* # Complex expression for Reference blocks ((RN .*\n){1} (RP .*\n){1}(\*\* .*\n)* (RC .*\n)*(\*\* .*\n)* (RX .*\n)* (RG .*\n)* (RA .*\n)* (RT .*\n)* (\*\* .*NO TITLE.*\n)* (RL .*\n)+)+ (CC .*\n)* # Each DR line may be followed by a ** line ((DR .*\n)+(\*\* [^\*].+\n)*)* (PE .+?\n)? (KW .*\n)* (FT .*\n)* (\*\*.*\n)* (SQ .*\n){1} ( .*\n)+ (\/\/\n){1} # end-of-entry marker \Z /x) { return 1; } else { return 0; }; } # * Data access sub text { my $self = shift; return ${$self->{_text}}; } # * Convenience methods sub ID { my $self = shift; if (@_) { carp "Entry::ID is a short cut for reading access. To modify data please use e.g. Entry::IDs::add, Entry::IDs::set\n"; } else { return $self->IDs->head; }; } sub AC { my $self = shift; if (@_) { carp "Entry::AC is a short cut for reading access. To modify data please use e.g. Entry::ACs::add, Entry::ACs::set\n"; } else { return $self->ACs->head; } } sub SQ { my $self = shift; return $self->SQs->seq(@_); } sub EV { my $self = shift; return $self->Stars->EV; } # is it a SWISS-PROT, TREMBL or TREMBLNEW entry? # database_code tries to find it out sub database_code { my $self = shift; # look at the dataclass in the ID line. # it says STANDARD for SWISS-PROT but # PRELIMINARY for TREMBL and TREMBLNEW # # look at the release in the DT line # it says REL. for SWISS-PROT # TREMBLREL. for TREMBL # EMBLREL. for TREMBLNEW my $dataclass = $self->IDs->dataClass; if ($dataclass eq 'STANDARD' || $dataclass eq 'Reviewed') { # we have found a gold-standard ;-) protein: SWISS-PROT return 'S'; } elsif ($dataclass eq 'PRELIMINARY' || $dataclass eq 'Unreviewed') { # we have found an "avalanche of data" protein my $release = $self->DTs->CREATED_rel || ''; if ($self->AC =~ /[A-Z0-9]{6}/) { return '3'; } } return '?'; } sub equal { my ($self, $other) = @_; return SWISS::BaseClass::equal($self, $other); }; sub isFragment { my $self = shift; return $self->DEs->hasFragment; } sub isCurated { my $self = shift; return (($self->text() =~ /^\s*ID.*(STANDARD|Reviewed)/) || ($self->text() =~ /\n\*\*ZZ CURATED/)) || 0; } sub isVariant { my $self = shift; return $self->AC =~ /\-/ || 0; } 1; __END__ =head1 Name SWISS::Entry =head1 Description Main module to handle SWISS-PROT entries. One Entry object represents one SWISS-PROT entry and provides an API for its modification. The basic concept is the idea of lazy parsing. If an Entry object is created from the entry in flat file format, the text is simply stored in the private text attribute of the entry object. The member objects of the entry are only created if they are dereferenced. =head1 Example =for html 
use SWISS::Entry;
# Read an entire record at a time
$/ = "\/\/\n";
while (<>){
  $entry = SWISS::Entry->fromText($_);
  print $entry->AC, "\n";
}
This minimum program reads entries from a file in SWISS-PROT format and prints the primary accession number for each of the entries. =head1 Attributes The following attributes represent member objects. They can be accessed like e.g. $entry->IDs =over =item IDs ID line object =item ACs =item DTs =item DEs =item GNs =item OSs =item OCs =item Refs The reference block object =item CCs =item KWs =item DRs =item FTs =item Stars Object for the annotator's section stored in the ** lines. =item SQs The sequence object. =back =head1 Methods =over =item new Return a new Entry object =item initialize Initialise an Entry object and return it. =item update [force] Update an entry. The content of the member objects is written back into the private text attribute of the entry if necessary. If $force is true, an update of all member objects is forced. =item reformat Reformat all fields of an entry. =item fromText $text [, $fullParse[, $removeInternalComments]] Create an Entry object from the text $text. If $fullParse is true, the entry is parsed at creation time. Otherwise the individual line objects are only created if they are dereferenced. If $removeInternalComments is true, wild comments and indentation will be removed from the text before the parsing is done. [NOTE: wild comments are lines starting with a double asterisk located outside the Stars section, and indented lines are lines starting with spaces. Both are used internally by SWISS-PROT annotators during their work and excluded from internal and external releases.] =item toText [$insertInternalComments] Return the entry in flat file text format. If internal comments and indentation have been removed as specified in the parameters to fromText(), you may wish to reinsert them in the text output by setting $insertInternalComments to true. =item toFasta Return the entry in Fasta format. =item equal Returns True if two entries are equal, False otherwise =back The following methods are provided for your convenience. They are shortcuts for methods of the individual line objects. =over =item ID Returns the primary ID of the entry. =item AC Returns the primary AC of the entry. =item SQ Returns the sequence of the entry. =item EV Returns the EV (evidence) object of an entry. SWISS-PROT internal method. =back =head2 Data access methods =over =item text Returns the current text of the entry. B No update of the text is performed before. =item database_code Is it a SWISS-PROT, TREMBL or TREMBLNEW entry? database_code tries to find it out. Return values are S for SWISS-PROT, 3 for TREMBL, Q for TREMBLNEW, ? for unknown. =item isFragment Returns true if the DE line indicates a fragment, or of the entry contains a NON_CONS or NON_TER feature. =item isCurated Returns 1 if the entry is a curated entry, 0 otherwise. SWISS-PROT internal use only. Swissknife_1.75/lib/SWISS/CCrna_editing.pm0000644005110600510130000000522412571343361020566 0ustar ecastroSwissProtpackage SWISS::CCrna_editing; use vars qw($AUTOLOAD @ISA %fields); use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @ISA = ('SWISS::ListBase'); %fields = ( term => undef, note => undef, ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCrna_editing; my $text = $$textRef; $self->initialize(); if ($text =~ /\bModified_positions=(.*?)(;|\.?$)/) { for my $pos (split /, (?!ECO:\d)/, $1) { # p.s. do not split inside ev (new style only) tags my $ev = $pos =~ s/($SWISS::TextFunc::evidencePattern)// ? $1 : undef; if ($pos =~ /^[A-Za-z]/) { $self->{term} = $pos; } else { $self->add([$pos, $ev]); } } } if ( $text =~ /\bNote=(.+)/ ) { ( my $note = $1 ) =~ s/[;.]$//; $self->{note} = SWISS::CC::parse2Blocks( $note ); } $self->{_dirty} = 0; return $self; } sub toString { my $self = shift; my $text = "CC -!- RNA EDITING: " . $self->comment( "true" ) . ";"; return SWISS::TextFunc->wrapOn('',"CC ", $SWISS::TextFunc::lineLength, $text); } sub topic { return "RNA EDITING"; } sub comment { my ( $self, $with_ev ) = @_; my $text = "Modified_positions="; if ($self->size) { $text .= join ", ", map { my ($pos, $ev) = @$_; $pos .= $ev if defined $ev && $with_ev; $pos; } @{$self->{list}}; } else { $text .= $self->{term} || "Undetermined"; } if (defined $self->{note} and length $self->{note}) { $text .= "; Note=" . SWISS::CC::blocks2String( $self->{note} ); } $text; } 1; __END__ =head1 Name SWISS::CCrna_editing =head1 Description B represents a comment on the topic 'RNA EDITING' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item topic The topic of this comment ('RNA EDITING'). =item note The Note of this comment, if any. An array of [ sentence, evidence_tags ] =item term A string such as "Undetermined" or "Not_applicable", if any. =item elements An array of [position, evidence_tags], if any. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/OXs.pm0000644005110600510130000000626713147300251016605 0ustar ecastroSwissProtpackage SWISS::OXs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::ListBase; use SWISS::TextFunc; use SWISS::OX; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); # All possible taxonomic resources need to be listed here. %fields = ('NCBI_TaxID' => undef, ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub initialize { my $self = shift; $self->NCBI_TaxID(new SWISS::ListBase); } sub fromText { # Line format of the OX line is # NCBI_TaxID=126566, 38, 846, 23412; my $self = new(shift); my $textRef = shift; my $line = ""; my @resources; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'OX'})/m) { $line = join ' ', map { $self->{indentation} += s/^ //; SWISS::TextFunc->cleanLine($_) } (split /\n/m, $1 ); # split into different Taxonomic_resource name blocks @resources = split /\;\s*/, $line; foreach my $resource (@resources) { my ($resourceName, $taxids); if (($resourceName, $taxids) = $resource =~ /(\w+)\=(.*)/) { unless (defined $resourceName) { warn ("$resourceName is not a legal taxonomic resource identifier. Skipping \n$line!"); next; } # crete objects for the individual tax ids $self->$resourceName()->add(map {SWISS::OX->fromText($_)} split( /\, (?!ECO:\d)/, $taxids ) ); } else { warn ("Parse error in OX line $line"); } } } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my @tmp; my $newText = ''; if ($self->NCBI_TaxID()->size > 0) { @tmp = map {$_->toText} $self->NCBI_TaxID->elements(); $newText = "NCBI_TaxID\=". join(", ", @tmp) . "\;"; my $prefix = "OX "; my $col = $SWISS::TextFunc::lineLengthStar; $col++, $prefix=" $prefix" if $self->{indentation}; $newText = SWISS::TextFunc->wrapOn($prefix, $prefix, $col, $newText, ", ", ); }; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'OX'}); } # OXs must never be sorted, overwrite the inherited sort method. sub sort { return 1; } 1; __END__ =head1 Name SWISS::OXs =head1 Description B represents the OX lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OXs object is a container object which holds a list of SWISS::OX objects for each currently permitted taxonomic resource. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C A ListBase object which holds a list of tax ids. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head1 Example $taxid = new SWISS::OX; $taxid->text('1234'); $entry->OXs->NCBI_TaxID()->add($taxid); foreach my $taxid ($entry->OXs->NCBI_TaxID()->elements()) { print $taxid->text, "\n"; } Swissknife_1.75/lib/SWISS/Ref.pm0000644005110600510130000003147113147300251016603 0ustar ecastroSwissProtpackage SWISS::Ref; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields @RCtopics @RXtopics %linePattern @linePattern $print_titles $uppercase); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::BaseClass; use SWISS::RCelement; $print_titles = 1; $uppercase = 0; BEGIN { @EXPORT_OK = qw($print_titles $uppercase); @ISA = ( 'Exporter', 'SWISS::BaseClass'); @linePattern = ('^(RN .*\n){1}', '^(RP .*\n)+', '^(RC .*\n)+', '^(RX .*\n)+', '^(\*\* \S+=None\b.*\n)+', '^(RG .*\n)+', '^(RA .*\n)+', '^((RT .*\n)|(\*\* .*NO TITLE.*\n))+', '^(RL .*\n)+'); my ($line, $lineId); foreach $line (@linePattern) { ($lineId) = $line =~ /\(+(.\S)/; $linePattern{$lineId} = $line; } %fields = ('RN' => undef, 'RP' => undef, 'RC' => undef, 'RX' => undef, 'RG' => undef, 'RA' => undef, 'RT' => undef, 'RT_comment' => undef, 'RX_comment' => undef, 'RL' => undef, 'journal' => undef, 'issn' => undef, 'volume' => undef, 'pages' => undef, 'year' => undef, 'etal' => undef, ); @RCtopics = ('SPECIES', 'STRAIN', 'PLASMID', 'TRANSPOSON', 'TISSUE'); @RXtopics = qw(MEDLINE PubMed AGRICOLA DOI); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::Ref; my ($line, $tmp, @tmp); my ($token, $qualifiers, @qualifiers); my (%rc,%rx); my ($dbref, $dbid); my $match; # Remove indentation $self->{indentation}->{$1}++ while $$textRef =~ s/^ (\S+)/$1/m; # Parse RN if ($$textRef =~ /$SWISS::Ref::linePattern{'RN'}/){ my $rnline = $1; if ($rnline =~ /RN \[(\d+)\]/){ $self->RN("$1"); } if ($rnline =~ /\]( ?\{.*\})/) { $self->{'evidenceTags'} = $1; } } else { if ($main::opt_warn) { carp "RN parse error, ignoring $$textRef"; } return $self; } # Parse RP if ($$textRef =~ /$SWISS::Ref::linePattern{'RP'}/m){ $match = $&; $line = SWISS::TextFunc->joinWith('', ' ', '(?cleanLine($_)} (split "\n", $match)); $self->RP($line); } else { if ($main::opt_warn) { carp "RP parse error, ignoring $$textRef"; } } # Parse RC undef %rc; if ($$textRef =~ /$SWISS::Ref::linePattern{'RC'}/m){ $match = $&; $line = join " ", map{SWISS::TextFunc->cleanLine($_)}(split /\n/m, $match); # drop trailing semicolon $line =~ s/;$//; # don't drop 'AND', there are lines like # RC STRAIN=HOK-01, FERM P-8705; # $line =~ s/\s*,\s*(AND\s+)*/, /g; @tmp = split(/;\s*/, $line); foreach $tmp (@tmp){ ($token, $qualifiers) = $tmp =~ /^(\w+)\=(.*)/; # replace XXX AND YYY by XXX, AND YYY $qualifiers =~ s/(\w+)( AND)( \w+)$/$1,$2$3/; @qualifiers = split(/\,\s+(?!ECO:)/, $qualifiers); unless (grep(/$token/, @RCtopics)) { if ($main::opt_warn) { carp "Ignoring unknown RC token $token"; } next; } push@{$rc{$token}}, map {SWISS::RCelement->fromText($_)} @qualifiers; } $self->RC(\%rc); }; # Parse RX undef %rx; if ($$textRef =~ /$SWISS::Ref::linePattern{'RX'}/m){ @tmp = map {SWISS::TextFunc->cleanLine($_)} (split /\n/m, $& ); @tmp = map {split /\;(\s+|\z)/} @tmp; #some DOI may contain internal semicolons foreach $tmp (@tmp) { if (($dbref, $dbid) = $tmp =~ /(\w+)\=(.+)/) { $dbref = $1; $dbid = $2; # suppress duplicate dbxrefs unless (grep ($dbid, @{$rx{$dbref}})) { push @{$rx{$dbref}}, $dbid; } } }; $self->RX(\%rx); }; #parse 'RX' MEDLINE=None if ($$textRef =~ /$SWISS::Ref::linePattern{'\*'}/m){ $match = $&; $self->RX_comment($match); } # Parse RG if ($$textRef =~ /$SWISS::Ref::linePattern{'RG'}/m){ $line = SWISS::TextFunc->joinWith('', ' ', '(?cleanLine($_)} (split "\n", $&)); $self->RG($line); }; # Parse RA if ($$textRef =~ /$SWISS::Ref::linePattern{'RA'}/m){ $self->RA(new SWISS::ListBase); $line = join ' ', map {SWISS::TextFunc->cleanLine($_)} (split /\n/m, $&); $self->RA->push (SWISS::TextFunc->listFromText($line, ',\s*', ';')); }; # Parse RT if ($$textRef =~ /$SWISS::Ref::linePattern{'RT'}/m){ $match = $&; if ($match =~ /^\*\*/m) { $self->RT_comment($match); } else { my $line = SWISS::TextFunc->joinWith('', ' ', '(?cleanLine($_)} (split /\n/m, $match)); $line =~ s/(\A\")|(\";\s*\Z)//g; # Drop trailing spaces and embracing ""; $self->RT($line); } }; # Parse RL if ($$textRef =~ /$SWISS::Ref::linePattern{'RL'}/m){ $line = SWISS::TextFunc->joinWith('', ' ', '(?cleanLine($_)} (split /\n/m, $&))); # Drop trailing dot $line =~ s/\.$//; $self->RL($line); }; $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $newText = ''; my ($rc, $topic); my $ra; my $longWordLength = $SWISS::TextFunc::lineLength - 8; # Format RN line if (defined $self->RN) { $newText = $newText . "RN [" . $self->RN . "]" . $self->getEvidenceTagsString . "\n"; } # Format RP line if (defined $self->RP) { $newText .= SWISS::TextFunc->wrapOn('RP ','RP ', $SWISS::TextFunc::lineLength, $self->RP, '(?RC) { $rc = "RC "; my $rchash = $self->RC; foreach $topic (@RCtopics) { if (defined $rchash->{$topic}) { my @tmp = @{$rchash->{$topic}}; next unless @tmp; $rc = $rc . "$topic=" . join(", ", (map {$_->toText()} @tmp)) . "; "; } } $newText .= SWISS::TextFunc->wrapOn('',"RC ", $SWISS::TextFunc::lineLength, $rc, '; ', ', and ', ', ', '\s+') if $rc; }; # Format RX line my $rx=''; if (defined $self->RX) { my $rxhash = $self->RX; foreach $topic (@RXtopics) { if (defined(my $dbid_list = $rxhash->{$topic})) { $rx .= ' ' if length $rx; $rx .= ("$topic=$dbid_list->[0];"); } } } #wrap only before DOI if the line is longer than 75 chars, #but don't wrap within the DOI number even if it is very long if (length $rx > $SWISS::TextFunc::lineLength - 5) { $rx =~ s/(.*) /$1\nRX /; } $newText .= 'RX ' . $rx . "\n" if $rx; #don't use wrapOn if (defined $self->RX_comment) { $newText .= $self->RX_comment; }; # Format RG line if (defined $self->RG) { my $rg = $self->RG; foreach my $r (split ';\s*', $rg) {# every consortium (sep by ;) should be on a distinct line (that shouldn't be wrapped unless max 256 char...) $newText .= SWISS::TextFunc->wrapOn('RG ','RG ', $SWISS::TextFunc::lineLengthMax, $r.';'); } } # Format RA line if (defined $self->RA) { $ra = join ", ", @{$self->RA->list}; $ra .= ";"; $newText .= SWISS::TextFunc->wrapOn('RA ','RA ', $SWISS::TextFunc::lineLength, $ra, '\,\s+'); } # Format RT line if ($print_titles && defined $self->RT) { my $rt = $self->RT; $rt .= '.' unless $rt =~ m/[\.\?\!]$/; $rt = '"'.$rt.'";'; $newText .= SWISS::TextFunc->wrapOn('RT ','RT ', $SWISS::TextFunc::lineLength, $rt); } elsif (defined $self->RT_comment) { $newText .= $self->RT_comment; }; # Format RL line if (defined (my $rl = $self->RL)) { #after "cited by:", wrap line, and wrap again at every semicolon #before "(In) ", wrap line, and wrap again after it at every semicolon #NB: "cited by:" can be followed by "(In) " my @post_rl; if ($rl =~ s/(\(In\) .*)//) { @post_rl = split /(?<=;) /, $1; } my @rl; @rl = $rl if length $rl; if (my ($a, $b) = $rl =~ /(.*\bcited by:)\s*(.*)/) { @rl = ($a, split /(?<=;) /, $b); } push @rl, @post_rl; $rl[-1] .= "." if @rl; for (my $i=0; $i<@rl; $i++) { my @sep; #use comma (or parenthesis) separator in Author lists @sep = ',\s+|(?=\()' if $rl[$i] =~ /^\(In\) / or $rl[$i-1] =~ /cited by:$/; $newText .= SWISS::TextFunc->wrapOn('RL ','RL ', $SWISS::TextFunc::lineLength, $rl[$i], @sep, '\s+'); } }; $newText =~ tr/a-z/A-Z/ if $uppercase; # restore indentation if ($self->{indentation}) { $newText =~ s/^(?=\Q$_\E)/ /mg for keys %{$self->{indentation}}; } # No reset of _dirty because the text is only returned, not written # back to an internal buffer. return $newText; } sub unpackRL { my $self=shift; my $rl = $self->RL; if (defined $rl) { if ($rl =~ /^(.*?)\s+(\w+):(\w+-\w+)\((\d+)\)$/){ $self->{'journal'}= $1; $self->{'volume'} = $2; $self->{'pages'} = $3; $self->{'year'} = $4; } else { carp "RL parse error, ignoring $rl" if $main::opt_warn; } } } sub packRL { my $self=shift; my $journal = $self->journal || 'UNKNOWN JOURNAL'; my $volume = $self->volume || '0'; my $pages = $self->pages || '0-0'; my $year = $self->year || '0'; my $rl = "$journal $volume:$pages($year)"; $self->RL($rl); } sub pubtype { my $self=shift; my $rl = $self->RL || return undef; return 'JOURNAL' if $rl =~ /^[\w\.\s]+\s\d+:\d+-\d+\(\d+\)$/; return 'SUBMISSION' if $rl =~ /^SUBMITTED/i; return 'UNPUBLISHED' if $rl =~ /^UNPUBLISHED/i; return 'BOOK' if $rl =~ /^\(IN\)/i; return 'THESIS' if $rl =~ /^THESIS/i; return 'PATENT' if $rl =~ /^PATENT/i; return 'JOURNAL' if $rl =~ /\s\w*\d\w*:\w+-\w+\(\d+\)$/; return 'JOURNAL' if $rl =~ /\s\w*\d\w*:\w+\(\d+\)$/; carp "Cannot parse publication type of '$rl'" if $main::opt_warn; return undef; } sub isPendingJournalArticle { my $self=shift; my $pt = $self->pubtype(); return 0 if $pt ne 'JOURNAL'; $self->unpackRL(); return 1 if $self->volume eq 0; return 1 if $self->year == 0; return 1 if $self->pages eq '0-0'; return 0; } sub get_MedlineID { my $self=shift; my %rx; my @mid; if (defined $self->RX){ %rx = %{$self->RX}; @mid = @{$rx{'MEDLINE'}}; } return wantarray ? @mid : shift @mid; } sub add_MedlineID { my $self=shift; my @medline_ids = @_; my %rx; if (defined $self->RX){ %rx = %{$self->RX}; } my %already_there = map {$_,1} @{$rx{'MEDLINE'}}; @medline_ids = grep {!$already_there{$_}} @medline_ids; push @{$rx{'MEDLINE'}},@medline_ids; $self->RX(\%rx); } sub add_Author { my $self=shift; my @authors = @_; unless (defined $self->RA){ $self->RA(new SWISS::ListBase); } $self->RA->add(@authors); } sub rc_sort { my $self=shift; if (defined $self->RC) { for my $topic (@RCtopics) { if (my $rclist = $self->RC->{$topic}) { if (@$rclist > 1) { # remove leading "and" map {$_->cleanText} @$rclist; # sort @$rclist = sort {lc $a->text cmp lc $b->text || $a->text cmp $b->text} @$rclist; # add "and" back in $rclist->[-1]->text("and " . $rclist->[-1]->text) if @$rclist > 1; @{$self->RC->{$topic}} = @$rclist; $self->{_dirty} = 1; } } } } } 1; __END__ =head1 Name SWISS::Ref.pm =head1 Description B represents a single reference of a SWISS-PROT + TREMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C The reference number. =item C The RP line(s), unwrapped as a string. =item C Zero or more RC lines. Data structure: {Token}[qualifier1, qualifierN]. A hash of arrays. Hash keys are the RC tokens, array elements are the qualifiers for that token. =item C References to bibliographic databases. Data structure: {Database}[identifier1, identifierN]. A hash of arrays. Hash keys are the names of bibliographic databases, array elements are the identifiers of the reference for that database. =item C The RG line(s), unwrapped as a string. =item C The list of Authors. An object of type SWISS::ListBase. =item C The publication title, unwrapped as a string. =item C The RL line. Data structure: String. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Writing methods =over =item add_MedlineID Add a RX line 'MEDLINE; nnnnnnnn.' to the reference. =item add_Author Add an author to the RA line of the reference. =item rc_sort Sort elements of the RC line alphabetically. Swissknife_1.75/lib/SWISS/CCbpc_properties.pm0000644005110600510130000001245412571343361021326 0ustar ecastroSwissProtpackage SWISS::CCbpc_properties; use vars qw($AUTOLOAD @ISA @_properties %fields); use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @ISA = ('SWISS::BaseClass'); @_properties = ( ['Absorption', 'Abs(max)', 'Note'], ['Kinetic parameters', 'KM', 'Vmax', 'Note'], ['pH dependence'], ['Redox potential'], ['Temperature dependence'], ); # now each %fields = map { $_->[0], undef } @_properties; } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCbpc_properties; my $text = $$textRef; $self->initialize(); $text =~ s/ +/ /g; my $properties_re = join "|", map {$_->[0]} @_properties; $text =~ s/\s*-!-.*?:\s*//; my $last_property = $_properties[0][0]; #"default" property while (length $text) { if ($text =~ s/^\s*($properties_re):\s*(.*?)\s*(;\s*|\Z)//so) { my ( $property, $ltext ) = ( $1, $2 ); $last_property = $property; my @content; if ( $ltext =~ s/^(\S+)=// and length $ltext ) { # 1st sub property in $1 e.g. Vmax @content = [$1, SWISS::CC::parse2Blocks( $ltext ) ]; # n.b. a single sub property if not "Note" (e.g. Vmax) has (so far!) only one sentence - ev, but use parse2Blocks anyway! symetrical with free text prop + in case it gets multi block! # n.b caution: in real free text multi block; sentences ends with " ." then ev, here there is no " ."!... } elsif (length $ltext) { # no sub prop, just free text (e.g for pH dependence) @content = [undef, SWISS::CC::parse2Blocks( $ltext ) ]; } while ($text =~ s/^(\S+)=(.*?)\s*(;\s*|\Z)//) { # other sub prop. e.g. Note=, Vmax=, ... my ($field, $txt) = ($1, $2); next unless length $txt; push @content, [ $field, SWISS::CC::parse2Blocks( $txt ) ]; } $self->{$property} = \@content; } else { # dangling text my ($ltext) = $text =~ s/(.*?)\s*(;\s*|\Z)//; push @{$self->{$last_property}}, [ undef, SWISS::CC::parse2Blocks( $ltext ) ]; } } $self->sort; $self->{_dirty} = 0; return $self; } sub sort { my ($self) = @_; if ($self) { for my $property (@_properties) { my ($_property_name, @fields) = @$property; next unless @fields; my $fields = join " ", " ", @fields, " "; if (defined (my $val = $self->{$property->[0]})) { @$val = sort {index($fields, $a->[0] || "") <=> index($fields, $b->[0] || "") } @$val; } } } } sub toString { my $self = shift; my $text = "-!- BIOPHYSICOCHEMICAL PROPERTIES:\n" . $self->comment; $text =~ s/^/CC /mg; $text =~ s/ //; return $text; } sub topic { return "BIOPHYSICOCHEMICAL PROPERTIES"; } sub properties { my ($self) = @_; my @list; for my $property (@_properties) { next unless defined $self->{$property->[0]}; push @list, $property->[0]; } return @list; } sub fields { my ($self, $property) = @_; defined $property or confess "Must pass a property"; my @list; if (defined (my $val = $self->{$property})) { for my $item (@$val) { push @list, $item; } } return @list; } sub comment { my ($self) = @_; my $text = ""; if ($self) { for my $property (@_properties) { if (defined (my $val = $self->{$property->[0]})) { $text .= "$property->[0]:\n"; for my $item (@$val) { my ( $field, $blocks ) = @$item; my $termin = !defined( $field ) || $field eq "Note" ? "." : ""; my $value = SWISS::CC::blocks2String( $blocks, "", $termin ); my $field_text = defined $field ? "$field=" : ""; my $t = "$field_text$value;"; $text .= SWISS::TextFunc->wrapOn(' ',' ', $SWISS::TextFunc::lineLength-9, $t); } } } } $text; } 1; __END__ =head1 Name SWISS::CCbpc_properties.pm =head1 Description B represents a comment on the topic 'BIOPHYSICOCHEMICAL PROPERTIES' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item topic The topic of this comment ('BIOPHYSICOCHEMICAL PROPERTIES'). =item properties A list of all filled properties in this comment. =item fields($properties) A list of "records" for a given property (e.g. "Absorption") in this comment. Each "record" is a reference to an array of [$field_name, [[$sentence, $evidence_tags]] ]. $field is undefined for unnamed fields. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/OH.pm0000644005110600510130000000251510432340022016364 0ustar ecastroSwissProtpackage SWISS::OH; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( NCBI_TaxID => undef, text => undef, ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $text = shift; # Parse out the evidence tags if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { my $tmp = $1; $self->evidenceTags($tmp); } if ($text =~ /^NCBI_TaxID=(\d+); (.+)\.$/) { $self->{NCBI_TaxID} = $1; $text = $2; } $self->text($text); return $self; } sub toText { my $self = shift; my $text = ''; return 'NCBI_TaxID=' . $self->NCBI_TaxID . '; ' . $self->text . '.' . $self->getEvidenceTagsString; } 1; __END__ =head1 Name SWISS::OH =head1 Description B represents one taxon from the OH line. The container object is SWISS::OHs. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C Tax ID. =item C Name, common name and synonym of the organism. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/CCalt_prod.pm0000644005110600510130000014043313147300251020100 0ustar ecastroSwissProtpackage SWISS::CCalt_prod; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( events => undef ); } # hash to describe order of events lines my %order; $order{"Alternative promoter usage"} = 1; $order{"Alternative splicing"} = 2; $order{"Alternative initiation"} = 3; $order{"Ribosomal frameshifting"} = 4; sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCalt_prod; my (@events, @newEvents, %events, $topic, $comment, $commentTag); my $text = $$textRef; ($topic, @events) = ($text =~ /(.+?)(Event=.+?)(?=(Event=.*|$))/gm); for my $event (@events) { if ($event ne "") { push @newEvents, $event; } } my %eventHash; # want to be able to read old format data (i.e pre release 8.0) for my $event (@newEvents) { my ($eventType, $comment, $namedForms, $rest ); my (@namedForms, @formsList); $event = $event . ";" if $event !~ /;\s*$/; ($eventType, $rest) = ($event =~ /(Event=.+?;)(.*)/m); ($comment, $namedForms) = ($rest =~ /(.*?)(Name=.*)/); if (! defined $comment) { $comment = $rest; } # tidy up $eventType =~ s/Event=//; $eventType =~ s/;$//; # original model had isoforms stored under one of potentially several # Event lines # new model (UniProt 8.0) has only one Event key per entry (though this may # describe many events) # this change has been accomodated in Swissknife with the specific # intention of maintaining the API, which is event-centric # i.e. all isoforms are stored under each event that features in the # event line of the entry # note that the API itself could be improved/extended to better fit the # new data model # one hash to store all isoform data if ($comment ne "") { $comment =~ s/.+?Named isoforms=\d+;\s*//; } else { $comment = $rest; $comment =~ s/^\s*//; } $comment =~ s/Comment=//; $comment =~ s/\s\s+/ /g; $comment =~ s/;\s*$//; $comment =~ s/^\s*//; # look for tags # if parsing old format entries, aggregate comments from all Event blocks if ( $comment ) { #new: Comment= can now be multi "block", represented as [[blocktxt,blockevs]] $eventHash{ Comment } = SWISS::CC::parse2Blocks( $comment ); } if (defined $namedForms) { # under both new and old formats, there will only be a maximum of one # Event line with named forms attached $namedForms =~ s/Named isoforms\=\d+;\s*//; @namedForms = split /;\s+(?=Name)/, $namedForms; for my $namedForm (@namedForms) { my %thisFormHash; $namedForm = $namedForm . ";" unless $namedForm =~ /;\s*$/; my (@fields) = ($namedForm =~ /(Name\=.+?;)\s+(Synonyms\=.*?;)*\s*(IsoId\=.*?;)\s+(Sequence\=.*?;)\s*(Note\=.*;)*/); if (! defined $fields[0]) { die "Incorrect syntax. Can't parse entry at " . $namedForm . "\n"; } FIELD: for my $field (@fields) { if (defined $field) { my ($key, $value); ($key, $value) = ($field =~ /(.+?)=(.*);/); $value =~ s/ \s+/ /g; if ($value eq "") { next FIELD; } # isoform count is made dynamically, no need to store it if ($key ne 'Named isoforms') { if ($key eq "Synonyms") { # complex data item, possibly with synonyms attached to each element my (@values) = split /,\s+(?!ECO:\d)/, $value; my @realValues; foreach $value (@values) { if (my ($realData, $tags) = ($value =~ /(.+?) ?\{(.+?)\}$/)) { push @realValues, $realData; my (@tagValues) = split /,\s+/, $tags; ${$thisFormHash{"SynonymsTags"}}{$realData} = \@tagValues; # here keep ev tag separated } else { push @realValues, $value; } } $thisFormHash{$key} = \@realValues; } elsif ($key eq "IsoId" || $key eq "Sequence") { # complex data item, no synonyms my (@values) = split /,\s+(?!ECO:\d)/, $value; $thisFormHash{$key} = \@values; } elsif ( $key eq "Note" ) { # new: Note= can now be multi "block", represented as [[blocktxt,blockevs]] $thisFormHash{"Note"} = SWISS::CC::parse2Blocks( $value ); } elsif (my ($realData, $tags) = ($value =~ /(.+?) ?\{(.+?)\}$/)) { # (anything else then Note=!? wtf!?) left old code as is # simple data item, with tags $thisFormHash{$key} = $realData; my @tags = split /, ?/, $tags; my $tagKey = $key . "Tags"; $thisFormHash{$tagKey} = \@tags; } elsif ($key =~ /\w/) { # wtf!?... in old format!? # simple data item, no tags $thisFormHash{$key} = $value; } } } } push @formsList, \%thisFormHash; } $eventHash{"FormsList"} = \@formsList; } my @derivedEvents = split /, /, $eventType; for my $thisEvent (@derivedEvents) { # in the data model, the same event hash is keyed by each individual # event that references it $events{$thisEvent} = \%eventHash; } # this field is just a value that can be used to access the event hash, # when we are not interested in filtering by event if (! defined $self->{keyEvent}) { $self->{keyEvent} = $derivedEvents[0]; } } $self->{events} = \%events; $self->{_dirty} = 0; return $self; } sub toString { my $self = shift; my $text = "CC -!- ALTERNATIVE PRODUCTS:\n"; my @keys = keys %{$self->{'events'}}; my @sortedKeys = sort _byEvent @keys; my $eventText = ""; # reconstitute full Event header for my $event (@sortedKeys) { if ($eventText eq "") { $eventText = $event; } else { $eventText = $eventText . ", " . $event; } } if ($eventText !~ /;$/) { $eventText = $eventText . ";"; } # all the events key the same form hash, so we merely need one of these to # access the hash my $event = $self->{'keyEvent'}; my $commentData = $self->{ events }->{ $event }->{ Comment }; my $commentText = $commentData ? SWISS::CC::blocks2String( $commentData ).";" : ""; my $headerText = ""; if ( $eventText !~ /^Event=/ ) { $headerText = "Event=" . $eventText; } else { $headerText = $eventText; } # named isoform count only for certain events my $count = $self -> getNamedFormCount($event); $headerText = $headerText . " Named isoforms=" . $count . ";"; $text = $text . "CC " . $headerText . "\n"; #$text = $text . SWISS::TextFunc-> # wrapOn("CC ", # "CC ", # $SWISS::TextFunc::lineLength, $headerText , '\s+'); if ( $commentText ) { $headerText = "Comment=" . $commentText; $text = $text . SWISS::TextFunc-> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $headerText , '(?{'events'}}{$event}}{"FormsList"}}[0]}{"Name"}) { # forms list is not sorted, may contain blank elements in among the real # elements! FORM: for my $namedForm (@{${${$self->{'events'}}{$event}}{"FormsList"}}) { # quick fix until we find the real bug if (! defined $$namedForm{"IsoId"}) { die "Named isoforms incorrectly defined"; } ## form details # name, synonyms my $formText = ""; if ($namedForm !~ /;$/) { $formText = $formText . ";"; } $formText = "Name=" . $$namedForm{"Name"}; my $evTags = $self -> getEvidenceTagsString($event, "Name", $$namedForm{"Name"}); if (defined $evTags) { $formText = $formText . $evTags; } $formText = $formText . "; "; my $synonymText = ""; $synonymText = $self -> _printList("Synonyms", $$namedForm{"Synonyms"}, $$namedForm{"Name"}); if (defined $synonymText) { $formText = $formText . $synonymText; } $formText = SWISS::TextFunc-> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText , '\s+'); $allFormsText .= $formText; my $nb_isoid = scalar @{$$namedForm{"IsoId"}}; my $header_width = $nb_isoid > 1 ? 20 : 36; my $id_width = 10; my $separator_width = 2; my $ids_per_line = int (($SWISS::TextFunc::lineLength - $header_width - $id_width ) / ( $id_width + $separator_width ) + 1); # isoform ID, sequence if ($nb_isoid == 1) { if (scalar @{$$namedForm{"Sequence"}} < $ids_per_line+1) { # regular case, everything in one line $formText = $self -> _printList("IsoId", $$namedForm{"IsoId"}) . $self -> _printList("Sequence", $$namedForm{"Sequence"}); $formText = SWISS::TextFunc -> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText, '\s+'); $allFormsText = $allFormsText . $formText; } else { # need to split up VSPs across several lines, and format them # accordingly my $wrapperText = "CC"; for (my $i = 0; $i < scalar @{$$namedForm{"Sequence"}}; $i = $i + $ids_per_line) { my @tempList; for (my $j = $i; $j < ($i + $ids_per_line); $j++) { if (defined $$namedForm{"Sequence"}[$j]) { push @tempList, $$namedForm{"Sequence"}[$j] } } if ($i == 0) { # first line $formText = $self -> _printList("IsoId", $$namedForm{"IsoId"}) . $self -> _printList("Sequence", \@tempList); $formText = SWISS::TextFunc -> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText, '\s+'); $formText =~ s/;$/,/; $allFormsText = $allFormsText . $formText; my ($initialText) = ($formText =~ /(.*Sequence=)/); my $offset = (length $initialText) - 2; for (my $j = 0; $j < $offset; $j ++) { $wrapperText = $wrapperText . " "; } } else { $formText = join ', ', @tempList; # end in ',' if more lines are coming my $term = $i < scalar @{$$namedForm{"Sequence"}} - $ids_per_line ? ',' : ';'; $formText = $formText . $term; $formText = SWISS::TextFunc -> wrapOn($wrapperText, $wrapperText, $SWISS::TextFunc::lineLength, $formText, '\s+'); $allFormsText = $allFormsText . $formText; } } } } else { # ISO IDs and Sequence in separate lines if (scalar @{$$namedForm{"Sequence"}} < 5) { $formText = $self -> _printList("IsoId", $$namedForm{"IsoId"}); $formText = SWISS::TextFunc -> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText, '\s+'); $allFormsText = $allFormsText . $formText; $formText = $self -> _printList("Sequence", $$namedForm{"Sequence"}); $formText = SWISS::TextFunc -> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText, '\s+'); $allFormsText = $allFormsText . $formText; } else { # ISO IDs in separate lines from sequence, AND sequences spread over # several lines $formText = $self -> _printList("IsoId", $$namedForm{"IsoId"}); $formText = SWISS::TextFunc -> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText, '\s+'); $allFormsText = $allFormsText . $formText; # in this case, we can fit in 4 VSPs per line for (my $i = 0; $i < scalar @{$$namedForm{"Sequence"}}; $i = $i + $ids_per_line) { my @tempList; for (my $j = $i; $j < ($i + $ids_per_line); $j++) { if (defined $$namedForm{"Sequence"}[$j]) { push @tempList, ${$$namedForm{"Sequence"}}[$j] } } if ($i == 0) { $formText = $self -> _printList("Sequence", \@tempList); $formText = SWISS::TextFunc -> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText, '\s+'); $formText =~ s/;$/,/; $allFormsText = $allFormsText . $formText; } else { $formText = join ', ', @tempList; # end in ',' if more lines are coming my $term = $i < scalar @{$$namedForm{"Sequence"}} - $ids_per_line ? ',' : ';'; $formText = $formText . $term; $formText = SWISS::TextFunc -> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText, '\s+'); $allFormsText = $allFormsText . $formText; } } } } # note my $note_txt = ""; my $noteText = ""; if ( defined $namedForm->{ Note } ) { $note_txt = "Note=".SWISS::CC::blocks2String( $namedForm->{ Note } ).";"; $noteText = SWISS::TextFunc-> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $note_txt , '(? getEvidenceTagsString($self->{keyEvent}, "Synonyms", $name, $value); if (defined $evTags) { $keyText = $keyText . $evTags; } } } if ($count != 0) { return $keyText . "; "; } else { return; } } sub _byEvent { $order{$a} <=> $order{$b} || $a <=> $b } sub topic { return "ALTERNATIVE PRODUCTS"; } sub keyEvent { my ($self) = @_; return $self -> {'keyEvent'}; } sub comment { my ($self) = @_; my $str = $self->toString; $str =~ s/.*\n//; $str =~ s/^CC //mg; $str; } sub setEvents { my ($self, $eventHash) = @_; $self -> {'events'} = $eventHash; } # conveneience read/write methods sub addEvent { # note that behaviour changes with UniProt relase 8.0 # adding a new event now points this event at all existing isoforms my ($self, $eventName) = @_; $self->{'events'}->{$eventName} = $self-> {'events'}->{ $self->{keyEvent} }; } sub addForm { my ($self, $eventName, $name, $synonyms, $isoIds, $featIds, $note_data) = @_; if (defined ${$self -> {'events'}}{$eventName}) { my %newForm; $newForm{"Name"} = $name; $newForm{"Synonyms"} = $synonyms; $newForm{"IsoId"} = $isoIds; $newForm{"Sequence"} = $featIds; $newForm{"Note"} = $note_data; # now (end of 2015) note is an array of array ref! [ [ blocktxt,block_evs ] ] push @{${${$self -> {'events'}}{$eventName}}{"FormsList"}}, \%newForm; } } sub getComment { my ( $self, $eventName ) = @_; if ( defined $self->{'events'}->{$eventName} ) { return $self->{'events'}->{$eventName}->{ Comment }; # now (end of 2015) comment is an array of array ref! [ [ blocktxt,block_evs ]... ] } else { return undef; } } sub getEventNames { my ($self) = @_; return sort _byEvent keys %{$self -> {'events'}}; } sub getFormNames { my ($self, $event) = @_; my @formNames; if (defined ${$self -> {'events'}}{$event}) { for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { push @formNames, $$form{"Name"}; } } return @formNames; } sub getSynonyms { my ($self, $event, $formName) = @_; for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $formName) { if (defined $$form{"Synonyms"}) { return @{$$form{"Synonyms"}}; } } } return (); } sub getIsoIds { my ($self, $event, $formName) = @_; for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $formName) { if (defined $$form{"IsoId"}) { return @{$$form{"IsoId"}}; } } } return (); } sub getFeatIds { my ($self, $event, $formName) = @_; for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $formName) { if (defined $$form{"Sequence"}) { return @{$$form{"Sequence"}}; } } } return (); } sub getNote { my ($self, $event, $formName) = @_; if (defined ${$self -> {'events'}}{$event}) { for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $formName) { if (defined $$form{"Note"}) { return $$form{"Note"}; } } } } return undef; } sub getNamedFormCount { my ($self, $event) = @_; if (defined ${$self -> {'events'}}{$event}) { if (defined ${${${${$self -> {'events'}}{$event}}{"FormsList"}}[0]}{"Name"}) { return scalar @{${${$self -> {'events'}}{$event}}{"FormsList"}}; } else { return 0; } } return undef; } sub deleteEvent { my ($self, $event) = @_; return delete ${$self -> {'events'}}{$event}; } sub deleteComment { my ($self, $event ) = @_; if (defined ${$self -> {'events'}}{$event}) { return delete ${${$self -> {'events'}}{$event}}{"Comment"}; } return undef; } sub deleteForm { my ($self, $event, $formName) = @_; if (defined ${$self -> {'events'}}{$event}) { my $position = 0; for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $formName) { my @ret = splice (@{${${$self -> {'events'}}{$event}}{"FormsList"}}, $position, 1); if (scalar @{${${$self -> {'events'}}{$event}}{"FormsList"}} == 0) { delete ${${$self -> {'events'}}{$event}}{"FormsList"}; } return @ret; } $position++; } } return undef; } sub setComment { my ( $self, $eventName, $comment_data ) = @_; if ( ref( $comment_data ) eq 'ARRAY' ) { warn "comment data should be an array ref: [ [ blocktxt, blockevs ]... ] e.g. [ [ 'an event comment', '' ] ] "; return; } if ( defined $self->{ events }->{$eventName} ) { $self->{ events }->{$eventName}->{ Comment } = $comment_data; } } sub setFormName { my ($self, $event, $oldName, $newName) = @_; if (defined ${$self -> {'events'}}{$event}) { for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $oldName) { $$form{"Name"} = $newName; return; } } } } sub setSynonyms { my ($self, $event, $name, $synonyms) = @_; if (defined ${$self -> {'events'}}{$event}) { for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $name) { $$form{"Synonyms"} = $synonyms; return; } } } } sub setIsoIds { my ($self, $event, $name, $isoIds) = @_; if (defined ${$self -> {'events'}}{$event}) { for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $name) { $$form{"IsoId"} = $isoIds; return; } } } } sub setFeatIds { my ($self, $event, $name, $featIds) = @_; if (defined ${$self -> {'events'}}{$event}) { for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $name) { $$form{"Sequence"} = $featIds; return; } } } } sub setNote { my ($self, $event, $name, $note_data ) = @_; # now (end of 2015) note data is an array of array ref ref! [ [ blocktxt,block_evs ] ] if ( ref( $note_data ) eq 'ARRAY' ) { warn "note data should be an array ref: [ [ blocktxt, blockevs ]... ] e.g. [ [ 'a note', '' ] ] "; return; } if ( defined $self->{ events }->{$event} ) { for my $form ( @{ $self->{ events }->{$event}->{ FormsList } } ) { if ( $form->{ Name } eq $name ) { $form->{ Note } = $note_data; return; } } } } sub hasEvidenceTag { my ($self, $tag, $event, $type, $name, $synonym) = @_; if ( defined $self->{ events }->{ $event } ) { if ( $type eq 'Comment' ) { if ( $self->{ events }->{ $event }->{ Comment } ) { my $hastag = 0; map { $hastag = 1 if $_->[ 1 ] eq $tag } @{ $self->{ events }->{ $event }->{ Comment } }; return $hastag; } } elsif ( $type eq 'Name' || $type eq 'Note' ) { for my $form ( @{ $self->{ events }->{ $event }->{ FormsList } } ) { if ( $form->{ Name } eq $name ) { if ( $type eq 'Name' ) { my $tagType = "NameTags"; if (defined $$form{$tagType}) { for my $actualTag (@{$$form{$tagType}}) { if ($actualTag eq $tag) { return 1; } } } } else { my $hastag = 0; map { $hastag = 1 if $_->[ 1 ] eq $tag } @{ $form->{ Note } }; return $hastag; } } } } elsif ( $type eq 'Synonyms' ) { for my $form ( @{ $self->{ events }->{ $event }->{ FormsList } } ) { if ($$form{"Name"} eq $name) { if (defined $$form{"Synonyms"}) { for my $actualSynonym (@{$$form{"Synonyms"}}) { if ($synonym eq $actualSynonym) { # hash of tags for each synonym my $tagType = $type . "Tags"; if (defined${$$form{$tagType}}{$synonym}) { for my $actualTag (@{${$$form{$tagType}}{$synonym}}) { if ($actualTag eq $tag) { return 1; } } } } } } } } } } return 0; } sub getEvidenceTags { my ($self, $event, $type, $name, $synonym) = @_; if (defined ${$self -> {'events'}}{$event}) { if ($type eq 'Comment') { if ( $self -> { events }->{$event}->{ Comment } ) { my @evs; map { push @evs, split( /, ?/, $_->[1] ) } @{ $self -> { events }->{$event}->{ Comment } }; return \@evs; } } elsif ($type eq 'Name' || $type eq 'Note') { for my $form ( @{ $self->{ events }->{ $event }->{ FormsList } } ) { if ( $form->{ Name } eq $name ) { if ( $type eq 'Name' ) { return $form->{ NameTags }; } else { my @evs; map { push @evs, split( /, ?/, $_->[1] ) } @{ $form->{ Note } }; return \@evs; } } } } elsif ($type eq 'Synonyms') { for my $form ( @{ $self->{ events }->{ $event }->{ FormsList } } ) { if ($$form{"Name"} eq $name) { if (defined $$form{"Synonyms"}) { for my $actualSynonym (@{$$form{"Synonyms"}}) { if ($synonym eq $actualSynonym) { # hash of tags for each synonym my $tagType = $type . "Tags"; if (defined ${$$form{$tagType}}{$synonym}) { return @{${$$form{$tagType}}{$synonym}}; } } } } } } } } return undef; } sub getEvidenceTagsString { my ($self, $event, $type, $name, $synonym) = @_; if ( defined $self->{ events }->{ $event } ) { if ( $type eq 'Comment' ) { # n.b. method is used by some test if ( $self->{ events }->{ $event }->{ Comment } ) { my $evs = join ",", map { $_->[ 1 ] } @{ $self->{ events }->{ $event }->{ Comment } }; $evs = "{" . $evs . "}"; if ( $evs =~ /ECO:/ ) { # new style evidence $evs =~ s/,/, /g; $evs = " ".$evs; } return $evs; } } elsif ( $type eq 'Note' ) { foreach my $form ( @{ $self->{ events }->{ $event }->{ FormsList } } ) { if ( $form->{ Name } eq $name) { my $evs = join ",", map { $_->[ 1 ] } @{ $form->{ Note } }; $evs = "{" . $evs . "}"; if ( $evs =~ /ECO:/ ) { # new style evidence $evs =~ s/,/, /g; $evs = " ".$evs; } return $evs; } } } elsif ($type eq 'Name' ) { for my $form ( @{ $self->{ events }->{ $event }->{ FormsList } } ) { if ( $form->{ Name } eq $name) { if ( defined $form->{ NameTags } ) { my $text = join ',', @{ $form->{ NameTags } }; $text = "{" . $text . "}"; if ( $text =~ /ECO:/ ) { $text =~ s/,/, /g; $text = " ".$text; } return $text; } } } } elsif ($type eq 'Synonyms') { for my $form (@{${${$self -> {'events'}}{$event}}{'FormsList'}}) { if ($$form{"Name"} eq $name) { if (defined $$form{"Synonyms"}) { for my $actualSynonym (@{$$form{"Synonyms"}}) { if ($synonym eq $actualSynonym) { # hash of tags for each synonym my $tagType = $type . "Tags"; if (defined ${$$form{$tagType}}{$synonym}) { my $text = join ',', @{${$$form{$tagType}}{$synonym}}; $text = "{" . $text . "}"; if ( $text =~ /ECO:/ ) { $text =~ s/,/, /g; $text = " ".$text; } return $text; } } } } } } } } return undef; } sub setEvidenceTags { # don't allow tags to be added where there is no data my ($self, $tags, $event, $type, $name, $synonym) = @_; if ( defined $self->{ events }->{ $event } ) { if ( $type eq 'Comment' && ( defined $self->{ events }->{ $event }->{ Comment } ) ) { my $last_ev = $self->{ events }->{ $event }->{ Comment }->[-1]->[ 1 ]; ( my $cleaned_tag = $tags ) =~ s/\s*[{}]\s*//g; $self->{ events }->{ $event }->{ Comment }->[-1]->[ 1 ] = $cleaned_tag; warn "setting ev tag on last comment 'block' n.b. Comment is now a self contained data structure representing multi [ blocktxt, blockevs ] elements, it would be better to directly manipulate this [ [ blocktxt, blockevs ] ... ] structure obtained via getComment"; } elsif ( $type eq 'Note' ) { for my $form (@{ $self->{ events }->{ $event }->{ FormsList } } ) { if ( $form->{ Name } eq $name && defined $form->{ $type } ) { ( my $cleaned_tag = $tags ) =~ s/\s*[{}]\s*//g; $form->{ Note }->[-1]->[ 1 ] = $cleaned_tag; warn "setting ev tag on last Name=$name Note 'block' n.b. Note is now a self contained data structure representing multi [ blocktxt, blockevs ] elements, it would be better to directly manipulate this [ [ blocktxt, blockevs ] ... ] structure obtained via getNote"; } } } elsif ( $type eq 'Name' ) { for my $form (@{ $self->{ events }->{ $event }->{ FormsList } } ) { if ( $form->{ Name } eq $name && defined $form->{ $type } ) { $form->{ NameTags } = $tags; } } } elsif ($type eq 'Synonyms') { for my $form (@{ $self->{ events }->{ $event }->{ FormsList } } ) { if ($$form{"Name"} eq $name) { if (defined $$form{"Synonyms"}) { for my $actualSynonym (@{$$form{"Synonyms"}}) { if ($synonym eq $actualSynonym) { # hash of tags for each synonym my $tagType = $type . "Tags"; ${$$form{$tagType}}{$synonym} = $tags; } } } } } } } } sub addEvidenceTag { # don't allow tags to be added where there is no data my ($self, $tag, $event, $type, $name, $synonym) = @_; if (defined $self->{ events }->{ $event } ) { if ( $type eq 'Comment' && ( defined $self->{ events }->{ $event }->{ Comment } ) ) { my $last_ev = $self->{ events }->{ $event }->{ Comment }->[-1]->[ 1 ]; ( my $cleaned_tag = $tag ) =~ s/\s*[{}]\s*//g; # $tag supposed to be a single ev my $utd_ev_str = $last_ev ? $last_ev.", ".$cleaned_tag : $cleaned_tag; $self->{ events }->{ $event }->{ Comment }->[-1]->[ 1 ] = $utd_ev_str; warn "adding ev tag on last comment 'block' n.b. Comment is now a self contained data structure representing multi [ blocktxt, blockevs ] elements, it would be better to directly manipulate this [ [ blocktxt, blockevs ] ... ] structure obtained via getComment"; # todo CHECK if all those evtags methods could just be removed! } elsif ( $type eq 'Note' ) { for my $form (@{ $self->{ events }->{ $event }->{ FormsList } } ) { if ( $form->{ Name } eq $name && defined $form->{ $type } ) { my $last_ev = $form->{ Note }->[-1]->[ 1 ]; ( my $cleaned_tag = $tag ) =~ s/\s*[{}]\s*//g; my $utd_ev_str = $last_ev ? $last_ev.", ".$cleaned_tag : $cleaned_tag; $form->{ Note }->[-1]->[ 1 ] = $utd_ev_str; warn "setting ev tag on last Name=$name Note 'block' n.b. Note is now a self contained data structure representing multi [ blocktxt, blockevs ] elements, it would be better to directly manipulate this [ [ blocktxt, blockevs ] ... ] structure obtained via getNote"; } } } elsif ( $type eq 'Name' ) { for my $form (@{ $self->{ events }->{ $event }->{ FormsList } } ) { if ($form->{ Name } eq $name && defined $form->{ $type } ) { push @{ $form->{ NameTags } }, $tag; } } } elsif ($type eq 'Synonyms') { for my $form (@{${${$self -> {'events'}}{$event}}{'FormsList'}}) { if ($$form{"Name"} eq $name) { for my $actualSynonym (@{$$form{"Synonyms"}}) { if ($synonym eq $actualSynonym) { # hash of tags for each synonym my $tagType = "SynonymsTags"; push @{${$$form{$tagType}}{$synonym}}, $tag; } } } } } } } sub deleteEvidenceTags { my ($self, $tag, $event, $type, $name, $synonym) = @_; if ( defined $self->{ events }->{ $event } ) { if ( $type eq 'Comment' ) { map { $_->[ 1 ] = "" } @{$self->{ events }->{ $event }->{ Comment } }; } elsif ( $type eq 'Note') { for my $form (@{ $self->{ events }->{ $event }->{ FormsList } } ) { map { $_->[1] = "" } @$form->{ Note } if $form->{ Name } eq $name; } } elsif ( $type eq 'Name' ) { for my $form (@{ $self->{ events }->{ $event }->{ FormsList } } ) { if ( $form->{ Name } eq $name ) { my $tagType = $type . "Tags"; my $offset = 0; if (defined $$form{$tagType}) { my @tags = @{$$form{$tagType}}; for my $actualTag (@tags) { if ($tag eq $actualTag) { splice @tags, $offset, 1; } $offset ++; } if (scalar @tags == 0) { delete $$form{$tagType}; } } } } } elsif ($type eq 'Synonyms') { for my $form (@{${${$self -> {'events'}}{$event}}{'FormsList'}}) { if ($$form{"Name"} eq $name) { if (defined $$form{"Synonyms"}) { for my $actualSynonym (@{$$form{"Synonyms"}}) { if ($synonym eq $actualSynonym) { # hash of tags for each synonym my $tagType = "SynonymsTags"; my $offset = 0; if (defined $$form{$tagType}) { if (defined ${$$form{$tagType}}{$synonym}) { for my $actualSynonymTag (@{${$$form{$tagType}}{$synonym}}) { if ($tag eq $actualSynonymTag) { splice @{${$$form{$tagType}}{$synonym}}, $offset, 1; } $offset++; } if (scalar @{${$$form{$tagType}}{$synonym}} == 0) { delete ${$$form{$tagType}}{$synonym}; } } } } } } } if (scalar keys %{$$form{"SynonymsTags"}} == 0) { delete $$form{"SynonymsTags"}; } } } } } 1; __END__ =head1 Name SWISS::CCalt_prod.pm =head1 Description B represents a comment on the topic 'ALTERNATIVE PRODUCTS' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. B: This example is given to illustrate the internal construction of an CCalt_prod object. However, for most purposes it should be possible to use the convenience methods provided (e.g. the add, delete, get and set methods doocumented below) instead of constructing the section manually. The use of the convenience methods is also recommended to ensure the structual integrity of the CCalt_prod object. ## Create a new named isoform my %thisFormHash; ## give this some properties # some properties are single data values $thisFormHash{"Name"} = "This"; # some properties are lists of values push @{$thisFormHash{"Synonyms"}}, "That"; push @{$thisFormHash{"Synonyms"}}, "The Other"; push @{$thisFormHash{"IsoId"}}, "P00000-01"; push @{$thisFormHash{"IsoId"}}, "P00000-02"; push @{$thisFormHash{"Sequence"}}, "VSP_000001"; push @{$thisFormHash{"Sequence"}}, "VSP_000002"; $thisFormHash{"Notes"} = [ [ "this local note", "ECO:0000269|PubMed:22081402, ECO:0000269|PubMed:23203051" ] ]; $thisFormHash{"Notes"} = [ [ "another local note without ev", "" ] ]; $thisFormHash{"Notes"} = [ [ "note block1", "ECO:0000269|PubMed:22081402" ], [ "note block2", "ECO:0000269|PubMed:23203051" ] ]; ## put this form onto a list of all forms created by one type of event my @newFormsList; push @newFormsList, \%thisFormHash; ## put this list into a hash describing all characteristics of this event my %eventHash; $eventHash{"FormsList"} = \@newFormsList; ## set other values of this event $eventHash{"Comment"} = [ [ "This Comment", "ECO:0000269|PubMed:23203051" ] ]; ## put the description of this event into a hash descrinbing all events my %eventsHash; $eventsHash{"Alternative splicing"} = \%eventHash; ## put a reference to this hash into the CCalt_products object my $hashRef; $hashRef = \%eventsHash; my $newCC = SWISS::CCalt_prod; $newCC->setEvents($hashRef); $newCC->toString(); B: @synonyms = ("That", "The other"); @isoIds = ("P00000-1", "P00000-2"); @featIds = ("VSP_00001", "VSP_00002"); my $newCC = SWISS::CCalt_prod; $newCC -> addComment("Alternative splicing", "This comment"); $newCC -> addForm("Alternative splicing", "This", \@synonyms, \@isoIds, \@featIds, [ [ "This local note", "ECO:0000269|PubMed:22081402, ECO:0000269|PubMed:23203051" ] ]); print $newCC -> toString(); B CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=This comment. CC Name=This; Synonyms=That, The other; CC IsoId=P00000-1, P00000-2; Sequence=VSP_00001, VSP_00002; CC Note=This local note. CC {ECO:0000269|PubMed:22081402, ECO:0000269|PubMed:23203051}; B: $CC -> addEvidenceTag('EP8', "Alternative splicing", "Synonyms", "VI", "B"); to add the tag 'EP8' to synonym B of isoform VI, produced by alternative splicing B: With the release of UniProt 8.0, the format of the CC ALTERNATIVE PRODUCTS blocks has changed slightly. In particular, isoforms are no longer stored according to the events that have generated them, so this: CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=This comment. CC Name=This; Synonyms=That, The other; CC IsoId=P00000-1, P00000-2; Sequence=VSP_00001, VSP_00002; CC Note=This local note. CC Event=Alternative initiation; CC Comment=Another comment. has become this: CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initation; Named isoforms=1; CC Comment=This comment. Another comment; CC Name=This; Synonyms=That, The other; CC IsoId=P00000-1, P00000-2; Sequence=VSP_00001, VSP_00002; CC Note=Produced by alternative splicing. This local note; The API is quite event-centric, reflecting the previous file format (where different content was available according to the event type). To get all isoforms (for whatever events are annotated) under the new format, do: $CC->keyEvent; which will return an arbitrary event that can be used a parameter in other methods. Any of the events annotated will function as parameters to retrieve information about assocaticated isoforms: it is not necessary to supply the complete list. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item topic The topic of this comment ('ALTERNATIVE PRODUCTS'). =back =head1 Methods =head2 Standard methods =over =item new =item fromText =back =head2 Reading/Writing methods =over =item addEvent ($eventName) Allows the user to insert "events blocks" into the CCalt_prod object. =item addEvidenceTag($tag, $event, $type, $name, $synonym) Add $tag to the tag list associated with the specified component of a CCalt_prod object. The event and type (of the item to which the tag is to be added, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform to which the tag is being attached); the name of the synonym to which the tag are being attached must also be given if the type is "Synonyms". n.b. now Comment and Note are "multi block" ( [ [ blocktext, blockevs ]... ] , so here the ev tag will be added on last the 'block'; it would be better to directly manipulate this [ [ blocktxt, blockevs ] ... ] structure obtained via getComment/Note =item addForm ($eventName, $formName, \@synonyms, \@isoIds, \@featIds, $note) Allows the user to add a form into a given event block. See code example (above) for more details. =item deleteComment ($eventName) Deletes the comment associated with this event. =item deleteEvent ($eventName) Deletes an event from this CCalt_prod objects. =item deleteEvidenceTag($tag, $event, $type, $name, $synonym) Deletes $tag from the tag list associated with the specified component of a CCalt_prod object. The event and type (of the item from which the tag is to be deleted, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform from which the tag is being deleted); the name of the synonym from which the tag is being deleted must also be given if the type is "Synonyms". =item deleteForm ($eventName, $formName) Deletes a form associated with a given event. =item keyEvent () Extracts one of the events annotated in this entry, which can then be used to retrieve data associated with this event =item getComment($eventName) Returns the comment for this event. =item getEventNames Returns a list of all event names for this CCalt_prod object. =item getEvidenceTags($event, $type, $name, $synonym) Returns a list of the tags attached to the specified component of a CCalt_prod object. The event and type (of the item to which the tag is attached, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform whose tags are being fetched); the name of the synonym whose tags are being fetched must also be given if the type is "Synonyms". n.b. now Comment and Note are "multi block" ( [ [ blocktext, blockevs ]... ] , so here all the evidences from all the block are pooled together =item getEvidenceTagsString($event, $type, $name, $synonym) Returns the tags attached to the specified component of a CCalt_prod object as a string literal. The event and type (of the item to which the tag is attached, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform whose tags are being fetched); the name of the synonym whose tags are being fetched must also be given if the type is "Synonyms". n.b. now Comment and Note are "multi block" ( [ [ blocktext, blockevs ]... ] , so here all the evidences from all the block are pooled together =item getFeatIds ($eventName, $formName) Returns a list of all feature IDs associated with this form produced by this event. =item getFormNames ($eventName) Returns a list of all form names for this form produced by this event. =item getIsoIds ($eventName, $formName) Returns a list of all IsoIds for this form produced by this event. =item getNamedFormCount($eventName) Returns the number of named and identified forms for this event. =item getNote ($eventName, $formName) Returns the local note of this form produced by this event. =item getSynonyms ($eventName, $formName) Returns a list of all synonyms of this form produced by this event. =item hasEvidenceTag ($tag, $event, $type, $name, $synonym) Returns 1 if the specified component of a CCalt_prod object has the specified tag. The event and type (of the item to which the tag is attached, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform whose tags are being fetched); the name of the synonym whose tags are being fetched must also be given if the type is "Synonyms". =item setComment ($eventName, $comment) Allows the user to add a global comment for a particular event. =item setEvidenceTags(\@tags, $event, $type, $name, $synonym) Sets the evidence tags of the specified component of a CCalt_prod object to the array pointed to by \@tags. The event and type (of the item to which the tag are to be added, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform to which tags are being attached); the name of the synonym to which tags are being attached must also be given if the type is "Synonyms". n.b. now Comment and Note are "multi block" ( [ [ blocktext, blockevs ]... ] , so here the ev tag will be set on last the 'block'; it would be better to directly manipulate this [ [ blocktxt, blockevs ] ... ] structure obtained via getComment/Note =item setEvent (%eventHash) Can be used to manually insert a hash representing one event. Use of this method is not recommeded, see code examples for how to use the convenience methods to create a CCalt_prod object. =item setFeatIds($eventName, $oldName, \@featIds) Sets the feature Ids for the named form (associated with the specified event) to the supplied list. =item setFormName($eventName, $oldName, $newName) Changes the name of the formed named $OldName, associated with this event, to the $newName. =item setIsoIds($eventName, $oldName, \@isoIds) Sets the Isoform Ids for the named form (associated with the specified event) to the supplied list. =item setNote($eventName, $name, $note) Sets the local note for the named form (associated with the specified event). =item setSynonyms($eventName, $name, \@synonyms) Sets the synonyms for the named form (associated with the specified event) to the supplied list. =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/KWs.pm0000644005110600510130000000376013147300251016573 0ustar ecastroSwissProtpackage SWISS::KWs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::KW; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $textRef = shift; if ( $$textRef =~ /($SWISS::TextFunc::linePattern{'KW'})/m ) { ( my $raw_data_block = $1 ) =~ s/^( *)KW //mg; $self->{ indentation } = 1 if $1; foreach my $kw ( split /;\s?|\.\s?$/m, $raw_data_block ) { $kw =~ s/ *\r?\n/ /g; push @{ $self->list() }, SWISS::KW->fromText( $kw ); } } $self->{ _dirty } = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my @lines; my $newText = ''; if ($self->size > 0) { $newText = join('; ', map {$_->toText()} @{$self->list}) . "."; my $prefix = "KW "; my $col = $SWISS::TextFunc::lineLength; $col++, $prefix=" $prefix" if $self->{indentation}; $newText = SWISS::TextFunc->wrapOn($prefix, $prefix, $col, $newText , ';\s+'); }; $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'KW'}); } sub sort { my $self = shift; return $self->set(sort {lc($a->text) cmp lc($b->text)} @{$self->list}); } 1; __END__ =head1 Name SWISS::KWs =head1 Description B represents the KW lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each list element is a B object. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item sort sort() sorts the keywords alphabetically. =item toText =back Swissknife_1.75/lib/SWISS/Stars/0000755005110600510130000000000013155516754016637 5ustar ecastroSwissProtSwissknife_1.75/lib/SWISS/Stars/aa.pm0000644005110600510130000000355512350011015017536 0ustar ecastroSwissProtpackage SWISS::Stars::aa; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $textRef = shift; my $line; # The tag for the aa section is ' ' foreach $line ($$textRef =~ /^(\*\* .*\n)/gm) { $line = SWISS::TextFunc->cleanLine($line); $self->add($line); }; # we have only read, so the object is still clean $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my ($textRef) = @_; my $newText = ''; my $tag = ' '; # remove old aa lines $$textRef =~ s/^(\*\*$tag .*\n)//gm; # assemble new aa lines map ({$newText .= SWISS::TextFunc->wrapOn("\*\*$tag ", "\*\*$tag ", $SWISS::TextFunc::lineLengthStar, $_, ' ')} $self->elements); # now the object is clean $self->{_dirty} = 0; # add new aa lines at the beginning return $$textRef = $newText . $$textRef; } # The aa section should never be sorted sub sort { return 1; }; 1; __END__ =head1 Name SWISS::aa.pm =head1 Description B represents the unstructured part of the "annotator's section" (source section) within an SWISS-PROT + TrEMBL entry. The "annotator's section" is not visible to the public. The unstructured part of it has the line tag '** '. See also the general description in Stars.html. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each line is stored as one element of the list. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/Stars/default.pm0000644005110600510130000000367211542162414020615 0ustar ecastroSwissProtpackage SWISS::Stars::default; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase' ); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $textRef = shift; my $tag = shift; my $line; foreach $line ($$textRef =~ /^(\*\*$tag .*\n)/gm) { $line = SWISS::TextFunc->cleanLine($line); $self->add($line); } # we have only read, so the object is still clean $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my ($textRef, $tag) = @_; my $newText = ''; my $sep = ' '; my $len = $SWISS::TextFunc::lineLengthStar; if ($tag =~ /^(?:ZA|ZB|ZC)$/) { $sep = '; '; $len = 80; } # assemble new text if ($self->size > 0) { map ({$newText .= SWISS::TextFunc->wrapOn("\*\*$tag ", "\*\*$tag ", $len, $_, $sep)} $self->elements); }; # insert new text SWISS::Stars::insertLineGroup($self, $textRef, $newText, $tag); # now the object is clean $self->{_dirty} = 0; return 1; } # No sorting by default. sub sort { return 1; }; 1; __END__ =head1 Name SWISS::default =head1 Description B is the default class to represent structured information in the "annotator's section" within an SWISS-PROT + TrEMBL entry. The "annotator's section" is not visible to the public. The structured part has line tags of the form '**xx'. See also the general description in Stars.html. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each line is stored as one element of the list. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/Stars/DR.html0000755005110600510130000000256012244702702020024 0ustar ecastroSwissProt default

Name

SWISS::DR.pm

Description

SWISS/Stars/DR.pm is the class to represent DR information in the "annotator's section" (internal section) within an SWISS-PROT + TrEMBL entry. The "annotator's section" is not visible to the public. The structured part has line tags of the form '**xx'. See also the general description in Stars.html.

Inherits from SWISS::ListBase.pm

Attributes

list Each line is stored as one element of the list.

Standard methods

new
fromText
toText
Swissknife_1.75/lib/SWISS/Stars/DR.pm0000644005110600510130000000377212252123243017473 0ustar ecastroSwissProtpackage SWISS::Stars::DR; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase' ); %fields = ( ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $textRef = shift; my $line; foreach $line ($$textRef =~ /^(\*\*DR .*\n)/gm) { $line = SWISS::TextFunc->cleanLine($line); $self->add($line); } # p.s. PROSITE; PS..." lines are not handled (not considered as **DR)! (they should disappear anyway) $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my $newText = ''; my $sep = ' '; my $len = $SWISS::TextFunc::lineLengthStar; # assemble new text if ($self->size > 0) { map ({$newText .= SWISS::TextFunc->wrapOn("\*\*DR ", "\*\*DR ", $len, $_, $sep)} $self->elements); }; # insert new text SWISS::Stars::insertLineGroup($self, $textRef, $newText, "DR"); # now the object is clean $self->{_dirty} = 0; return 1; } # sort **DR alphab. sub sort { my $self = shift; return $self->set( sort { (my $i=$a)=~s/; / /g; (my $j=$b)=~s/; / /g; lc($i) cmp lc($j) } @{$self->list}); # p.s. set sets _dirty = 1 }; 1; __END__ =head1 Name SWISS::default =head1 Description B is the class to represent DR information in the "annotator's section" (internal section) within an SWISS-PROT + TrEMBL entry. The "annotator's section" is not visible to the public. The structured part has line tags of the form '**xx'. See also the general description in Stars.html. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each line is stored as one element of the list. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back Swissknife_1.75/lib/SWISS/Stars/EV.pm0000644005110600510130000001434513133345764017513 0ustar ecastroSwissProtpackage SWISS::Stars::EV; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } =head2 new =cut sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } =head2 fromText =cut sub fromText { my $self = new(shift); my $textRef = shift; my ($block, $line); # The tag for the EV section is 'EV' if ($$textRef =~ /((\*\*EV .*\n)+)/m) { $block = $1; # delete trailing dots and spaces $block =~ s/[\.\s]+\n/\n/gm; # unwrap multi-line evidence tags $block =~ s/\n\*\*EV\s{5}/ /gm; # now every comment is in a single line foreach $line (split /\n/, $block){ $line = SWISS::TextFunc->cleanLine($line); push (@{$self->list()}, [split(/\;\s*/, $line)]); }; }; # we have only read, so the object is still clean $self->{_dirty} = 0; return $self; } =head2 toText =cut sub toText { my $self = shift; my ($textRef) = @_; my $newText = ''; my $tag = 'EV'; $self->sort(); # always sort! # assemble new lines map ({$newText .= SWISS::TextFunc->wrapOn("\*\*$tag ", "\*\*$tag ", $SWISS::TextFunc::lineLengthStar, $_ . '.', '; ', ',\s*')} (map {join("; ", @$_)} $self->elements) ); # insert new text SWISS::Stars::insertLineGroup($self, $textRef, $newText, $tag); # now the object is clean $self->{_dirty} = 0; return 1; } =head2 sort =cut sub sort { my $self = shift; my $is_new_style = grep { $_->[0] =~ /^ECO/ } $self->elements; if ( $is_new_style ) { @{$self->list} = sort { # p.s. ->[0] eco code, e.g. ECO:0000269, ->[1] source (with id) e.g. PubMed:15466860, ->[2] curator id, ->[3] date $a->[0] cmp $b->[0] || lc( $a->[1] ) cmp lc( $b->[1] ) || $a->[2] cmp $b->[2]; #Sort by , For the same , sort by , For the same , sort by } $self->elements; } else { my ($x, $y, $u, $v); @{$self->list} = sort { ($u, $x) = @$a[0] =~ /(E[ACIP])(\d+)/; ($v, $y) = @$b[0] =~ /(E[ACIP])(\d+)/; $u cmp $v or $x <=> $y;} $self->elements; } $self->{_dirty} = 1; return 1; }; =head2 addEvidence( $evcode, $src, $author [, $date] ) Title: addEvidence Usage: $evidenceTag = $entry->Stars->EV->addEvidence($evcode, $src, $author [, $date]) Function: adds the evidence to the EV block if it does not yet exist or returns the correct evidence tag if the evidence already exists, possibly with a different date. Args: $evcode: the evidence code. e.g. ECO:0000269 $src: the source. e.g. PubMed:11433298 $author: the author (initials). e.g. XXX p.s. For programs this could be '-'. $date: optional. If present, it must be in standard SWISS-PROT date format. If not present the current date will be used. Returns: The correct evidence tag. =cut sub addEvidence { my $self = shift; my ( $evcode, $src, $author, $date ) = @_; # p.s. now only for new style evidences (Aug 2014) # set $date unless ( $date ) { $date = SWISS::TextFunc::currentSpDate; } return $self->_addEvidence( $evcode, $src, $author, $date ); } =head2 updateEvidence( $evcode, $src, $author [, $date] ) Title: updateEvidence Usage: $evidenceTag = $entry->Stars->EV->updateEvidence($evcode, $src, $author [, $date]) Function: updates the evidence to the EV block to $date or inserts it if it does not yet exist. Args: $evcode: the evidence code. e.g. ECO:0000269 $src: the source. e.g. PubMed:11433298 $author: the author (initials). e.g. XXX p.s. For programs this could be '-'. $date: optional. If present, it must be in standard SWISS-PROT date format. If not present the current date will be used. Returns: The correct evidence tag. =cut sub updateEvidence{ my $self = shift; my ( $evcode, $src, $author, $date ) = @_; # set $date unless ( $date ) { $date = SWISS::TextFunc::currentSpDate; } return $self->_addEvidence( $evcode, $src, $author, $date, 1 ); } # if $update is set, the evidence date will be updated if the entry already # exists. sub _addEvidence{ my $self = shift; my ( $evcode, $src, $author, $date, $update ) = @_; # check evcode unless ( $evcode =~ /^ECO:/ ) { croak( "Wrong evidence code type \'$evcode\'\n" ); } # set $date $date = SWISS::TextFunc::currentSpDate unless $date; # is ev to be added is already present (code and src) my @found = grep { $_->[ 0 ] eq $evcode && $_->[ 1 ] eq $src } $self->elements; $self->{ _dirty } = 1; my $ev = []; my $evtag = ''; if ( !@found ) { # ev is new, insert it $ev = [ $evcode, $src, $author, $date ]; $self->add( $ev ); } else { $ev = $found[ 0 ]; if ( $update ) { $ev->[ 2 ] = $author; $ev->[ 3 ] = $date; } } return $ev->[0].'|'.$ev->[1]; } sub max { my ($a, $b) = @_; if ($a > $b) { return $a; } else { return $b; } } 1; # says use was ok =head1 Name SWISS::Stars::EV.pm =head1 Description B represents the evidence section within an SWISS-PROT + TrEMBL entry. See http://www3.ebi.ac.uk/~sp/intern/projects/evidenceTags/index.html For a usage example, see evTest.pl in the Swissknife package. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each element of the list describes one evidence, itself represented as an array. =back Swissknife_1.75/lib/SWISS/dr_ord0000644005110600510130000000267612573276115016747 0ustar ecastroSwissProt#============== #DR lines order #============== # EMBL 0 CCDS 1 PIR 1 RefSeq 1 UniGene 1 PDB 1 PDBsum 1 DisProt 1 ProteinModelPortal 1 SMR 1 BioGrid 1 DIP 1 IntAct 1 MINT 1 STRING 1 BindingDB 1 ChEMBL 1 DrugBank 2 GuidetoPHARMACOLOGY 1 Allergome 1 CAZy 1 ESTHER 1 MEROPS 1 MoonProt 1 mycoCLAP 1 PeroxiBase 1 REBASE 1 TCDB 1 DEPOD 1 PhosphoSite 1 UniCarbKB 1 BioMuta 1 dbSNP 1 DMDM 1 COMPLUYEAST-2DPAGE 1 DOSAC-COBS-2DPAGE 1 OGP 1 REPRODUCTION-2DPAGE 1 SWISS-2DPAGE 1 UCD-2DPAGE 1 World-2DPAGE 1 MaxQB 1 PaxDb 1 PeptideAtlas 1 PRIDE 1 ProMEX 1 DNASU 1 Ensembl 1 EnsemblBacteria 1 EnsemblFungi 1 EnsemblMetazoa 1 EnsemblPlants 1 EnsemblProtists 1 GeneID 1 KEGG 1 PATRIC 1 UCSC 1 VectorBase 1 WBParaSite 1 ArachnoServer 2 CGD 2 ConoServer 2 CTD 1 dictyBase 2 EchoBASE 1 EcoGene 2 euHCVdb 1 EuPathDB 1 FlyBase 2 GeneCards 1 GeneFarm 1 GeneReviews 1 GenoList 1 Gramene 1 H-InvDB 1 HGNC 2 HPA 1 LegioList 1 Leproma 1 MaizeGDB 1 MGI 2 MIM 1 neXtProt 1 Orphanet 2 PharmGKB 1 PomBase 2 PseudoCAP 1 RGD 2 SGD 2 TAIR 1 TubercuList 1 WormBase 1 Xenbase 2 ZFIN 2 eggNOG 1 GeneTree 1 HOGENOM 1 HOVERGEN 1 InParanoid 1 KO 1 OMA 1 OrthoDB 1 PhylomeDB 1 TreeFam 1 BioCyc 1 BRENDA 1 Reactome 1 SABIO-RK 1 SignaLink 1 UniPathway 1 ChiTaRS 1 EvolutionaryTrace 1 GeneWiki 1 GenomeRNAi 1 NextBio 1 PMAP-CutDB 1 PRO 1 Proteomes 1 Bgee 1 CleanEx 1 ExpressionAtlas 1 Genevisible 1 GO 2 Gene3D 2 HAMAP 1 InterPro 2 PANTHER 2 Pfam 2 PIRSF 2 PRINTS 2 ProDom 2 SMART 2 SUPFAM 2 TIGRFAMs 2 PROSITE 2 Swissknife_1.75/lib/SWISS/ListBase.pm0000644005110600510130000004472313147300251017601 0ustar ecastroSwissProtpackage SWISS::ListBase; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use Data::Dumper; use SWISS::BaseClass; # * Initialisation BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass' ); %fields = ( list => undef, # the main array ); } # * Standard methods sub new { my ($ref) = @_; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub initialize { my ($self) = @_; $self->{'list'} = []; return $self; } # * Reading methods sub head { my ($self) = @_; return @{$self->{'list'}}[0]; } sub tail { my ($self) = @_; my @tmp = @{$self->{'list'}}; CORE::shift(@tmp); return @tmp; } sub get { my ($self, @patterns) = @_; my @result; # do nothing if the list is empty unless ($self->size > 0 ) { return (); }; # If first list element is a scalar if (not ref @{$self->list}[0]){ return (grep {/^$patterns[0]$/} @{$self->list}); }; # If first list element is an array if (ref @{$self->list}[0] eq 'ARRAY') { # The list of patterns might have one element, which is a list. # Unwrap it. if ((ref $patterns[0] eq 'ARRAY')) { @patterns = @{$patterns[0]}; }; @result = @{$self->list}; for (my $i=0; $i <= $#patterns; $i++) { my $pat = $patterns[$i]; if (defined($pat) and $pat ne ""){ @result = grep { $$_[$i] =~ /^$pat$/ } @result; } else { # empty patterns are regarded as matches. next; } } return @result; } # An undefined data type carp "get is currently not implemented for elements of type " . ref @{$self->list}[0]; return undef; } # Only maintained for backward compatibility sub mget { my ($self, @elements) = @_; confess "mget is deprecated. Please use get instead\n"; return $self->get(@elements); } sub size { my ($self) = @_; return scalar(@{$self->{'list'}}); } sub isEmpty { my ($self) = @_; return ($self->size == 0); } sub elements{ my ($self) = @_; return @{$self->{'list'}}; } # * Writing methods sub item { my ($self, $pos, $newValue) = @_; if ($newValue) { #set value return $self->{'list'}->[$pos] = $newValue; } else { #read value return $self->{'list'}->[$pos]; } } sub push { my ($self, @elements) = @_; $self->{_dirty} = 1; return CORE::push(@{$self->{'list'}}, @elements); } sub pop { my ($self) = @_; $self->{_dirty} = 1; return pop(@{$self->{'list'}}); } sub shift { my ($self) = @_; $self->{_dirty} = 1; return CORE::shift(@{$self->{'list'}}); } sub splice { my ($self, $offset, $length, @elements) = @_; $self->{_dirty} = 1; if (defined $length) { return splice(@{$self->{'list'}}, $offset, $length, @elements); } else { return splice(@{$self->{'list'}}, $offset); } } sub unshift { my ($self, @elements) = @_; $self->{_dirty} = 1; return unshift(@{$self->{'list'}}, @elements); } sub set { my ($self, @elements) = @_; $self->{_dirty} = 1; @{$self->{'list'}} = @elements; return $self; } sub add { my ($self, @elements) = @_; $self->{_dirty} = 1; return $self->push(@elements); } sub merge { my ($self, $other) = @_; $self->{_dirty} = 1; return $self->push($other->elements); } sub del { my ($self, @patterns) = @_; my @result; my ($i, $element); # do nothing if the list is empty unless ($self->size > 0) { return $self; }; # If first list element is a scalar if (not ref @{$self->list}[0]){ return ($self->set(grep {not /^$patterns[0]$/} @{$self->list})); }; # If first list element is an array if (ref @{$self->list}[0] eq 'ARRAY') { ELEMENT: foreach $element (@{$self->list}) { for ($i=0; $i <= $#patterns; $i++) { if ($patterns[$i] && ($$element[$i] !~ /^$patterns[$i]$/)){ CORE::push (@result, $element); next ELEMENT; } } }; return $self->set(@result); }; # An undefined data type carp "del is currently not implemented for elements of type " . ref @{$self->list}[0]; return undef; } # Only maintained for backward compatibility sub mdel { my ($self, @elements) = @_; carp "mdel is deprecated. Please use del instead\n"; return $self->del(@elements); } sub sort { my ($self, $coderef) = @_; if ($coderef) { return $self->set(sort $coderef @{$self->list}); } else { return $self->set(sort @{$self->list}); } } # make sure that an object is only contained once in a list. sub unique { my ($self) = @_; my @result = (); my @old = @{$self->list}; my ($arg, $pat); if ($#old > -1) { # list is not empty, delete duplicates $self->set(@{$self->list}[0]); foreach $arg (@old) { # The list elements might have Perl regexp wildcards. # These must be quoted in the search pattern. if (not ref $arg) { $pat = quotemeta $arg } elsif (ref $arg eq 'ARRAY') { $pat = [map {quotemeta $_} @$arg]; }; # save the element if it's not yet there unless ($self->get($pat)) { $self->push($arg); }; } } return 1; } sub update { my ($self, $force) = @_; $self->sort(); return 1; } # Return a new ListBase object which contains all elements for which # the filter function returns true. sub filter { my ($self, $filterFunc) = @_; my @matches = (); my $element; foreach $element ($self->elements()) { (&$filterFunc($element)) && (CORE::push(@matches, $element)); }; my $new = new ref($self); $new->set(@matches); $new->{indentation} = $self->{indentation}; return $new; }; # Examples for filter functions which might be used by ListBase::filter sub attributeDefined { _attributeDefined(@_); } sub attributeEquals { _attributeEquals(@_); } sub attributeMatchedBy { _attributeMatchedBy (@_); } sub _attributeDefined{ my $attributeName = CORE::shift(); return sub { my $self = CORE::shift(); return (defined $self->{$attributeName}); } } sub _attributeEquals{ my ($attributeName, $target) = @_; return sub { my $self = CORE::shift(); return ($self->{$attributeName} eq $target); } } sub _attributeMatchedBy{ my ($attributeName, $target) = @_; return sub { my $self = CORE::shift(); return ($self->{$attributeName} =~ /$target/); } } # Return a new ListBase object. Each of the elements of the new object # matches the parameter list of the method. sub getObject { my ($self, @elements) = @_; my $new = new ref($self); $new->set($self->get(@elements)); return $new; }; # Evidence tag handling sub evidenceTagPosition { # find index of evtag in an array "object" (e.g.a FT: [ key, from, to, text, evid!?, ftid, evidenceTags] evtag index is 6) my ($arrayP) = @_; if ($#$arrayP == -1) { return 0; } # generaly is last element if (@$arrayP[$#$arrayP] eq '{}') { return $#$arrayP; } elsif (@$arrayP[$#$arrayP] =~ $SWISS::TextFunc::evidencePattern) { # last element is evtag return $#$arrayP; } else { # not found in last element = array has yet no evtag # evtag should be added after end of array, index = 1 outside array (= array size) return $#$arrayP+1; } } sub setEvidenceTags { my ($self, $arrayP, @tags) = @_; unless (ref $arrayP eq 'ARRAY') { confess "$arrayP is not an array\n"; } my $evidenceTagPosition = evidenceTagPosition($arrayP); my $is_new = grep { /ECO:/ } @tags; my $joiner = $is_new ? ', ' : ','; @$arrayP[$evidenceTagPosition] = ( $is_new ? ' ' : '' ) . '{' . (join ', ', @tags) . '}'; $self->{_dirty} = 1; return $arrayP; } sub addEvidenceTag { my ($self, $arrayP, $tag) = @_; unless (ref $arrayP eq 'ARRAY') { confess "$arrayP is not an array\n"; } my $evidenceTagPosition = evidenceTagPosition($arrayP); my $evidenceTagPointer = \@$arrayP[$evidenceTagPosition]; # initialise $$evidenceTagPointer unless ($$evidenceTagPointer) { $$evidenceTagPointer = '{}'; } my $is_new_format = $tag =~ /ECO:/; unless ($$evidenceTagPointer =~ /[\{\,] ?\Q$tag\E[\}\,]/) { if ((!$$evidenceTagPointer) || ($$evidenceTagPointer eq '{}')) { $$evidenceTagPointer = ( $is_new_format ? ' ' : '' ) . '{' . $tag . '}'; } else { $$evidenceTagPointer =~ s/\{/ {/ if $is_new_format && $$evidenceTagPointer =~ /^\{/; if ( $is_new_format ) { $$evidenceTagPointer =~ s/\}/\, $tag\}/; } else { $$evidenceTagPointer =~ s/\}/\,$tag\}/; } } } $self->{_dirty} = 1; return $arrayP; } sub deleteEvidenceTag { my ($self, $arrayP, $tag) = @_; unless (ref $arrayP eq 'ARRAY') { confess "$arrayP is not an array\n"; } my $evidenceTagPosition = evidenceTagPosition($arrayP); my $evidenceTagPointer = \@$arrayP[$evidenceTagPosition]; $$evidenceTagPointer =~ s/([\{\,] ?)\Q$tag\E([\,\}])/$1$2/; $$evidenceTagPointer =~ s/\, ?\,/\,/; $$evidenceTagPointer =~ s/\, ?\}/\}/; $$evidenceTagPointer =~ s/\{\, ?/\{/; $$evidenceTagPointer =~ s/ ?\{\}//; if ( ! $$evidenceTagPointer ) { delete $arrayP->[ $evidenceTagPosition ]; } $self->{'_dirty'} = 1; return $arrayP; } sub hasEvidenceTag { my ($self, $arrayP, $tag) = @_; unless (ref $arrayP eq 'ARRAY') { confess "$arrayP is not an array\n"; } my $evidenceTagPosition = evidenceTagPosition($arrayP); return @$arrayP[$evidenceTagPosition] =~ /[\{\,] ?\Q$tag\E[\}\,]/; } sub getEvidenceTags { my ($self, $arrayP, $tag) = @_; unless (ref $arrayP eq 'ARRAY') { confess "$arrayP is not an array\n"; } my $tmp = @$arrayP[evidenceTagPosition($arrayP)]; $tmp =~ tr/\{\}//d; return map { s/^ +//; $_ } split /\,/, $tmp; } sub getEvidenceTagsString { my ($self, $arrayP, $tag) = @_; unless (ref $arrayP eq 'ARRAY') { confess "$arrayP is not an array\n"; } my $tmp = @$arrayP[evidenceTagPosition($arrayP)] || ''; if ($tmp eq '{}') { return ''; } else { return $tmp; } } # return the intersection with another list # usage: @myary = $mylistbase->intersect(@otherary); # or @myary = $mylistbase->intersect($otherlistbase); sub intersect { my ($self, @other) = @_; # if argument is another ListBase, get its contents into @other my $arg = $other[0]; if ($arg && ref($arg) eq ref($self)){ warn "ListBase::intersect doesnt allow two ListBases as input\n" if $main::opt_warn && $#other>0; @other = @{$arg->list}; } my %other_hash = map {$_,1} @other; my @result = grep { $other_hash{$_}} @{$self->list}; return @result; } # return the union with another list # usage: @myary = $mylistbase->union(@otherary,...); # or @myary = $mylistbase->union($otherlistbase,...); sub union { my ($self, @args) = @_; my @other = @{$self->list}; my $arg; foreach $arg (@args){ my $kind = ref $arg; if (not $kind){ CORE::push(@other,$arg); } elsif ($kind eq ref($self)){ CORE::push(@other, @{$arg->list}); } elsif ($kind eq 'SCALAR'){ CORE::push(@other, $$arg); } elsif ($kind eq 'ARRAY'){ CORE::push(@other, @$arg); } elsif ($kind eq 'HASH'){ CORE::push(@other, keys %$arg); } } my %result_hash = map {$_,1} @other, @{$self->list}; return keys %result_hash; } # return myself minus another list # usage: @myary = $mylistbase->minus(@otherary); # or @myary = $mylistbase->minus($otherlistbase); sub minus { no strict 'refs'; my ($self, @other) = @_; # if argument is another ListBase, get its contents into @other my $arg = $other[0]; my $ref = ref($arg); if ($ref && $ref->isa('SWISS::ListBase') ){ warn "ListBase::minus doesnt allow two ListBases as input\n" if $main::opt_warn && $#other>0; @other = @{$arg->list}; } my %other_hash = map {$_,1} @other; my @result = grep { !$other_hash{$_}} @{$self->list}; return @result; } # compare self to another list # returns 0 if both lists are equal, # -1 if self is subset of the argument # 1 if the argument is a subset of self # 2 if both list are unequal sub cmp { my ($self, @set_b) = @_; my @set_a = @{$self->list}; my %hash_a = map {$_,1} @set_a; my %hash_b = map {$_,1} @set_b; my @aminusb = grep { !$hash_b{$_}} @set_a; my @bminusa = grep { !$hash_a{$_}} @set_b; if (@aminusb){ if (@bminusa){ return 2; } else { return 1; } } else { if (@bminusa){ return -1; } else { return 0; } } } 1; __END__ =head1 Name SWISS::ListBase.pm =head1 Description Base class for list oriented classes in the SWISS:: hierarchy. It provides a set of quite general list manipulation methods to inheriting classes. =head1 Attributes =over =item list Holds an array, the essential content of the object. Array elements can be, and are in fact frequently, arrays themselves. =back =head1 Methods =head2 Standard methods =over =item new =item initialize =back =head2 Reading methods =over =item head Return the first element of the list =item tail Return all but the first element of the list =item get pattern Return a list of all elements matched by $pattern. Only exact matches are returned, but you can use Perls regular expressions. Example: $listBaseObject->set('EMBL', 'TREMBL', 'SWISSPROT'); $listBaseObject->get('.*EMBL'); returns ('EMBL', 'TREMBL') =item get @patternList To be used if the ListBase elements are arrays. An array is returned if all its elements are matched exactly by the elements from @patternList with the same index. Empty elements in @patternList always match. Example: $listBaseObject->set(['EMBL', 'M1', 'G1', '-'], ['EMBL', 'M2', 'A2', '-'], ['EMBL', 'M2', 'G3', 'ALT_TERM'], ['PROSITE', 'P00001', '1433_2', '1']); $listBaseObject->get('EMBL'); returns (['EMBL', 'M1', 'G1', '-'], ['EMBL', 'M2', 'A2', '-'], ['EMBL', 'M2', 'G3', 'ALT_TERM']) $listBaseObject->get('',M2); returns (['EMBL', 'M2', 'A2', '-'], ['EMBL', 'M2', 'G3', 'ALT_TERM']); Offering get in the interface is not particularly nice because it exports implementation details into the interface, but it is a powerful method which may save a lot of programming time. As an alternative, the 'filter' concept is available. =item getObject pattern =item getObject @patternList Same as get, but returns the results wrapped in a new ListBase object. =item filter Returns a new object containing all of the elements that match a search criteria. It takes a function as the only parameter. This function should expect a list element, and return true or false depending on whether the element matches the criteria. If the object is not a ListBase object but member of a subclass, a new object of that subclass will be returned. Example: $tmp = $entry->CCs->filter(&ccTopic('FUNCTION')); returns a SWISS::CCs object containing all CC blocks from $entry which have the topic 'FUNCTION'. Functions can also be anonymous functions. =item attributeEquals(string attributeName, string attributeValue) Filter function. If the elements of a ListBase object are objects, they will be returned by this function if they have the attribute and it equals the attributeValue. Example: $matchedKWs = $entry->KWs->filter(SWISS::ListBase::attributeEquals('text', $kw)); =item attributeMatchedBy(string attributeName, string pattern) Filter function. If the elements of a ListBase object are objects, they will be returned by this function if they have the attribute and the attribute is matched by the pattern. Example: $matchedKWs = $entry->KWs->filter(SWISS::ListBase::attributeMatchedBy('text', $kw)); =item isEmpty =item size The number of list elements in the object =item elements Returns the array of elements =item hasEvidenceTag $arrayPointer $tag Returns true if the array pointed to by $arrayPointer has the evidence tag $tag =item getEvidenceTags $arrayPointer returns the array of evidence tags of $arrayPointer =item getEvidenceTagsString $arrayPointer returns a string containing the evidence tags of $arrayPointer =back =head2 Writing methods =over =item item offset[, newValue] returns the list element at a specific offset, and optionally sets it to a new value. Negative offsets are relative to the end of the list. =item push list =item pop =item shift =item unshift list =item splice [offset[, length[, list]]] =item set list Sets the list attribute to @list =item add list Synonym for push =item merge (ListBase) Appends the elements of ListBase to the object =item sort [function] Applies a sort function to the list attribute, or by default, alphabetical sorting. Should be overwritten in derived classes with an adapted sort function. =item del pattern Deletes all items fully matching $pattern. Example: $listBaseObject->set('EMBL','TREMBL', 'SWISSPROT'); $listBaseObject->del('EMBL'); $listBaseObject->list(); returns ('TREMBL','SWISSPROT'). If you want to delete more, use something like $listBaseObject->del('.*EMBL') which deletes 'EMBL' and 'TREMBL'. =item del @patternList To be used if the ListBase objects are arrays. An array is deleted if all its elements are matched by the elements from @patternList with the same index. B Using the data from the get example above, $listBaseObject->del('','', 'A2') results in (['EMBL', 'M1', 'G1', '-'], ['EMBL', 'M2', 'G3', 'ALT_TERM'], ['PROSITE', 'P00001', '1433_2', '1']) =item update =item unique Makes sure each element is contained only once in a ListBase object. The second and subsequent occurrences of the same object are deleted. Example: $listBaseObject->set(EMBL, TREMBL, SWISSPROT); $listBaseObject->add(EMBL, MGD, EMBL); $listBaseObject->unique(); results in (EMBL, TREMBL, SWISSPROT, MGD) =item setEvidenceTags $arrayPointer @array sets the evidence Tags of the array pointed to by $arrayPointer to the contents of @array To be used if the ListBase elements are themselves arrays. A typical construct would be foreach $dr ($entry->DRs->elements()) { $entry->DRs->setEvidenceTags($dr, 'E2', 'E3'); } Returns $arrayPointer. =item addEvidenceTag $arrayPointer $tag adds $tag to the evidence tags of $arrayPointer To be used if the ListBase elements are themselves arrays. See documentation of setEvidenceTags. Returns $arrayPointer. =item deleteEvidenceTags $arrayPointer $evidenceTag deletes $evidenceTag from the array pointed to by $arrayPointer To be used if the ListBase elements are themselves arrays. A typical construct would be foreach $dr ($entry->DRs->elements()) { $entry->DRs->deleteEvidenceTags($dr, 'EC2'); } Returns $arrayPointer. =back Swissknife_1.75/lib/SWISS/CCs.pm0000644005110600510130000002506713147300251016543 0ustar ecastroSwissProtpackage SWISS::CCs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields %TOPICS); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::CC; use SWISS::CCcopyright; use SWISS::CCalt_prod; use SWISS::CCrna_editing; use SWISS::CCbpc_properties; use SWISS::CCinteraction; use SWISS::CCseq_caution; use SWISS::CCdisease; use SWISS::CCsubcell_location; use SWISS::CCcofactor; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } #initialization code: stuff DATA into hash { # Leading and trailing spaces are MANDATORY! local $/="\n"; my $index=0; my $line; while (defined ($line=)) { $line =~ s/\s+\z//; $TOPICS{$line} = $index++; } $TOPICS{'Copyright'} = $index++; close DATA; } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $self = new(shift); my $textRef = shift; my $line; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'CC'})/m) { my $block = $1; my ($main, $copyright) = split /CC +-{40,78}\nCC/, $block; # can't get regexp to work with two optional components to a block # ($block =~ /(.*)?(CC -{40,78}\n(.*\n)*CC -{40,78})*\n/s); # process each non-copyright comment type foreach $line (split /\n(?= ?CC +-!-)/m, $main) { my $indentation = $line =~ s/^ //mg; $line = SWISS::TextFunc->cleanLine($line); my $cc = _chooseType($line); $cc->{indentation} = $indentation if $indentation; push (@{$self->list()}, $cc); } # process copyright if (defined $copyright) { $copyright = "CC -----------------------------------------------------------------------\nCC".$copyright; $copyright =~ s/-{40,78}\r?\n$/-----------------------------------------------------------------------/; push (@{$self->list()}, _chooseType($copyright)); } } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my @lines; my $newText = ''; if (! $self->isEmpty()){ $newText = join('', map { my $str = $_->toString(); $str =~ s/^/ /mg if $_->{indentation}; $str; } @{$self->list}); }; $self->{_dirty} = 0; return SWISS::TextFunc-> insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{'CC'}); } sub toString { my $self = shift; my $string = ""; $self -> toText(\$string); return $string; } sub _chooseType { my $text = shift; my $CCs; # preparse text into a single line $text =~ s/-\nCC {7}(AND|OR|AND\/OR) /- $1 /mgi; # unwrap things like '-Val- bond' and 'Leu-|- bonds' (but not 'disulfide-bond') with space $text =~ s/(\b[A-Z]{3}-|-\|-)\nCC {7}(BOND)/$1 $2/mgi; $text =~ s/(?fromText(\$text); } elsif (($text =~ /-!- ALTERNATIVE PRODUCTS/) && ($text =~ /Event=/)) { # new format alternative products $CCs = SWISS::CCalt_prod->fromText(\$text); } elsif (($text =~ /-!- BIOPHYSICOCHEMICAL PROPERTIES/)) { $CCs = SWISS::CCbpc_properties->fromText(\$text); } elsif (($text =~ /-!- INTERACTION/)) { $CCs = SWISS::CCinteraction->fromText(\$text); } elsif (($text =~ /-!- RNA EDITING/)) { $CCs = SWISS::CCrna_editing->fromText(\$text); } elsif (($text =~ /-!- SEQUENCE CAUTION/)) { $CCs = SWISS::CCseq_caution->fromText(\$text); } elsif (($text =~ /-!- DISEASE/)) { $CCs = SWISS::CCdisease->fromText(\$text); } elsif (($text =~ /-!- SUBCELLULAR LOCATION/)) { $CCs = SWISS::CCsubcell_location->fromText(\$text); } elsif (($text =~ /-!- COFACTOR/)) { $CCs = SWISS::CCcofactor->fromText(\$text); } else { # standard $CCs = SWISS::CC->fromText(\$text); } return $CCs; } sub sort { my $self = shift; my $n = $self->size(); return 1 if $n < 2; my $rary = $self->list(); my $disorder; # nearly all entries will be in order, so test for it for (my $i=1; $i<$n; $i++) { if (_sort_cmp($rary->[$i-1], $rary->[$i]) > 0){ $disorder=1; last; } } return 1 unless $disorder; # simple sort to preserve order of same topics for (my $i=1; $i < $n; $i++){ for (my $j=1; $j < $n; $j++){ if (_sort_cmp($rary->[$j-1], $rary->[$j]) > 0){ ($rary->[$j-1],$rary->[$j]) = ($rary->[$j],$rary->[$j-1]); } } } return 1; } sub _sort_cmp { my ($cc1, $cc2) = @_; my $topic_1 = $cc1->topic; my $topic_2 = $cc2->topic; if ($topic_1 eq 'SIMILARITY' && $topic_2 eq 'SIMILARITY') { my $c_1 = $cc1->comment; my $c_2 = $cc2->comment; my @ord; for my $c ($c_1, $c_2) { if ($c =~ /\bbelongs to\b/i) { push @ord, 1; } elsif ($c =~ /^Contains\b/i) { push @ord, 2; } else { push @ord, 3; } } return $ord[0] <=> $ord[1] if $ord[0] != $ord[1]; if ($c_1 =~ /^CONTAINS (?:AT LEAST )?(?:\d+|\?) (.*)/i) { my $t_1 = $1; if ($c_2 =~ /^CONTAINS (?:AT LEAST )?(?:\d+|\?) (.*)/i) { return lc($t_1) cmp lc($1) || $t_1 cmp $1; } } return 0; } return $TOPICS{$topic_1} <=> $TOPICS{$topic_2}; } sub update { my $self = shift; my $force = shift; # CCs should be sorted, but unique() does not make sense $self->sort(); return 1; } sub get { # local override of global get method # get array of CC objects selected by topic my ($self, @patterns) = @_; my @result; # do nothing if the list is empty unless ($self->size > 0 ) { return (); }; if ((ref $patterns[0] eq 'ARRAY')) { @patterns = @{$patterns[0]}; }; @result = @{$self->list}; # empty patterns are regarded as matches. if (defined($patterns[0]) and $patterns[0] ne ""){ @result = grep { $_->topic() =~ /^$patterns[0]$/ } @result; } if (defined($patterns[1]) and $patterns[1] ne ""){ @result = grep { $_->comment() =~ /^$patterns[1]$/ } @result; } return @result; } sub unique { my ($self) = @_; my ($i, $j); for ($i = 0; $i < $#{$self->{list}}; $i++) { my $item1 = ${$self->list}[$i]; for ($j = $i+1; $j <= $#{$self->{list}}; $j++) { my $item2 = ${$self->list}[$j]; if ($item1->topic eq $item2->topic and $item1->comment eq $item2->comment) { splice @{$self->list}, $j--, 1; } } } return 1; } sub getObject { # local override of global get method # get ListBase object of CC objects selected by topic my ($self, @patterns) = @_; my $new = new ref($self); $new->set($self -> get(@patterns)); return $new; } sub del { # local override of global del method # delete CC objects if topic matches that specified my ($self, @patterns) = @_; my @result; my ($i, $pat, @elements); # do nothing if the list is empty unless ($self->size > 0 ) { return (); }; @elements = @{$self->list}; ELEMENT:for my $element (@elements) { my $match = 0; if ($patterns[0] && ($element->topic() =~ /^$patterns[0]$/)) { if ((! $patterns[1]) || ($element->comment() =~ /^$patterns[1]$/)) { $match ++; } } if ($match == 0) { CORE::push (@result, $element); } } return $self->set(@result); } sub copyright { # retrive copyright my ($self) = @_; my @elements = @{$self->list}; ELEMENT:for my $element (@elements) { if ($element->topic() eq 'Copyright') { return $element -> toString(); } } return; } sub ccTopic{ my ($ccTopic) = @_; return sub { my $ref = shift; my $topic = $ref -> topic(); return ($topic eq $ccTopic); } } 1; =head1 Name SWISS::CCs =head1 Description B represents the CC lines within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The CCs object is a container object which holds a list comprised of object of the type SWISS::CC or derived classes (see below). B local $/="\n//\n"; while (<>) { my $entry = SWISS::Entry-> fromText($_); my @CCs = $entry -> CCs -> elements(); for my $CC (@CCs) { if ($CC -> topic eq 'ALTERNATIVE PRODUCTS') { # now can call methods of CCalt_prod } elsif ($CC -> topic eq 'Copyright') { # now can call methods of CCcopyright } else { # now can call methods of CC } } } =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each list element is an object of one of the following classes, depending of the type of comment: topic object -------------------- -------------------- ALTERNATIVE PRODUCTS SWISS::CCalt_prod RNA EDITING SWISS::CCrna_editing BIOPHYSICOCHEMICAL PROPERTIES SWISS::CCbpc_properties INTERACTION SWISS::CCinteraction Copyright SWISS::CCcopyright (all other topics) SWISS::CC =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item sort Sort the CC block according to the order given in Swiss-Prot annotation note ANN017. =item toText =item update =back =head2 Reading/Writing methods =over =item ccTopic ($topic) Returns true if entry contains a comment block with the specified topic. =item copyright Returns a string representation of the copyright text. =item del (@patternList) Deletes all comment elements whose topic matches the first element of the pattern list. The second element is the used to specify a requirement for the comment to match as well. =item get (@patternList) An array is returned consisting of all comment elements elements whose topic matches any elements of the pattern list. =item getObject (@patternList) Same as get, but returns the results wrapped in a new ListBase object. =item toString Returns a string representation of the CCs object. =back =cut __DATA__ FUNCTION CATALYTIC ACTIVITY COFACTOR ENZYME REGULATION BIOPHYSICOCHEMICAL PROPERTIES PATHWAY SUBUNIT INTERACTION SUBCELLULAR LOCATION ALTERNATIVE PRODUCTS TISSUE SPECIFICITY DEVELOPMENTAL STAGE INDUCTION DOMAIN PTM RNA EDITING MASS SPECTROMETRY POLYMORPHISM DISEASE DISRUPTION PHENOTYPE ALLERGEN TOXIC DOSE BIOTECHNOLOGY PHARMACEUTICAL MISCELLANEOUS SIMILARITY CAUTION SEQUENCE CAUTION WEB RESOURCE Swissknife_1.75/lib/SWISS/CCsubcell_location.pm0000644005110600510130000001241112571343361021620 0ustar ecastroSwissProtpackage SWISS::CCsubcell_location; use vars qw($AUTOLOAD @ISA @_properties %fields); use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @ISA = ('SWISS::BaseClass'); %fields = ( locations => undef, note => undef ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCsubcell_location; my $text = $$textRef; $self->initialize(); $self->{ locations } = undef; $self->{ note } = undef; $text =~ s/^ *-!- SUBCELLULAR LOCATION: +//; # e.g.: isoform1:Cell membrane; Lipid-anchor, GPI-anchor. Nucleus membrane {ECO:0000269|PubMed:15282802}. # = form....:component....; topology................. a 2nd location... my ( $core, $note ) = split /\.? Note=/, $text; foreach my $lstr ( split /\. /, $core ) { my $form = $lstr =~ s/^(.+?)\: // ? $1 : ""; my @locs = split /; /, $lstr; push( @{ $self->{ locations } }, { 'form' => $form, 'component' => _parse_txt_ev( $locs[0] ), 'topology' => $locs[1] ? _parse_txt_ev( $locs[1] ) : undef, 'orientation' => $locs[2] ? _parse_txt_ev( $locs[2] ) : undef } ); } $self->{note} = SWISS::CC::parse2Blocks( $note ) if $note; return $self; } sub _parse_txt_ev { my $txt = shift; my ( $evidence ) = $txt =~ /($SWISS::TextFunc::evidencePattern)/m; if ( $evidence ) { my $quotedEvidence = quotemeta $evidence; $txt =~ s/$quotedEvidence//m; } $txt =~ s/\.$//; return [ $txt, $evidence ]; } sub topic { return "SUBCELLULAR LOCATION"; } sub toString { my $self = shift; my $text = "CC -!- SUBCELLULAR LOCATION: " . $self->comment( "true" ); $text = SWISS::TextFunc->wrapOn( '', "CC ", $SWISS::TextFunc::lineLength, $text); return $text; } sub comment { my ( $self, $with_ev ) = @_; my $text = ""; foreach my $location ( @{ $self->{locations} } ) { $text .= " " if $text; $text .= $location->{ form }.": " if $location->{ form }; my $component = $location->{ component }->[0]; my $comp_ev = $location->{ component }->[1] || ""; $text .= $component; $text .= $comp_ev if $with_ev; if ( $location->{ topology } ) { my $topology = $location->{ topology }->[0]; my $topo_ev = $location->{ topology }->[1] || ""; $text .= "; ".$topology; $text .= $topo_ev if $with_ev; } if ( $location->{ orientation } ) { my $orientation = $location->{ orientation }->[0]; my $orien_ev = $location->{ orientation }->[1] || ""; $text .= "; ".$orientation; $text .= $orien_ev if $with_ev; } $text .= "."; } if ( $self->{ note } ) { $text .= " " if $text; my $note = SWISS::CC::blocks2String( $self->{ note } ); $text .= "Note=".$note."."; } return $text; } sub locations { # TODO: check for DEL my ( $self, $value ) = @_; if ( defined $value ) { $self->{ locations } = $value; } return $self->{ locations }; } sub note { # TODO: check for DEL my ( $self, $value, $ev ) = @_; if ( defined $value ) { my $new_ev = $ev ? $ev : $self->{ note }->[0]->[0]; $self->{ note } = [ [ $value, $new_ev ] ]; } return $self->{'note'}; } 1; __END__ =head1 Name SWISS::CCsubcell_location.pm =head1 Description B represents a comment on the topic 'SUBCELLULAR LOCATION' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item topic The topic of this comment ('SUBCELLULAR LOCATION'). =back =head1 Methods =item locations The locations; reference to an array [ { 'form' => $in_form, 'component' => [ $component, $component_ev ], 'topology' => [ $topology, $topology_ev ], 'orientation' => [ $orientation, $orientation_ev ] }, ... ] =item locations( $new_locations ) Set locations to $new_locations, that should be an array: [ { 'form' => $in_form, 'component' => [ $component, $component_ev ], 'topology' => [ $topology, $topology_ev ], 'orientation' => [ $orientation, $orientation_ev ] }, ... ] =item note The note and evidence of the disease reference to an array of [ $note, $note_ev ] array =item note( [ $new_note, $new_note_ev ] ) Set note to [ $new_note, $new_note_ev ] =item comment The "text" version of this comment. =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back Swissknife_1.75/lib/SWISS/DE.pm0000644005110600510130000001252211055776453016374 0ustar ecastroSwissProtpackage SWISS::DE; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::BaseClass; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::BaseClass'); %fields = ( 'text' => undef, 'category' => undef, # (in new format) RecName | AltName 'type' => undef, # ... Full | Short | EC | Allergen | CD_antigen 'hide_in_old' => undef, # ... for CD_antigen already seen ouside CD_antigen (to be hidden in old format) ); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::BaseClass; $self->rebless($class); $self->{category} = shift; $self->{type} = shift; return $self; } sub fromText { my $self = new(shift); my $text = shift; # Parse out the evidence tags if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { my $tmp = $1; $self->evidenceTags($tmp); } $self->text($text); $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $addParen = shift; my $str = $self->text; if (my $type = $self->{type}) { # if defined = is new format: remove useless type txt inside name # (!legacy from old format!) my $process_txt_by_type = { # transform stored name string (old format) into clean new names 'Full' => sub { my $str = shift or return; #$str =~ s/ precursor$//; return $str; }, 'EC' => sub { my $str = shift or return; $str =~ /^EC (\d.+)/; return $1; }, 'Allergen' => sub { my $str = shift or return; $str =~ /^Allergen (.+)/; return $1; }, 'CD_antigen' => sub { my $str = shift or return; $str =~ /^(.+) antigen$/; return $1; } }; # process str (only if new format is asked! as # .... DEs->is_old_format(1) might be used to convert new format back # to old format ...) $str = $process_txt_by_type->{$type}->($self->{text}) if $process_txt_by_type->{$type} and !$self->{is_old_format}; } return '' if $self->{is_old_format} && $self->{hide_in_old}; return $addParen ? '(' . $str . ')' . $self->getEvidenceTagsString: $str . $self->getEvidenceTagsString; } 1; __END__ =head1 Name SWISS::DE.pm =head1 Description Each DE object represents one protein name. The container object for all names of an entry is SWISS::DEs =head1 Inherits from SWISS::BaseClass =head1 Attributes =over =item C The raw text of the protein name. Note: as SwissKnife works with both new and old DE line formats, for backward rcompatibility, with both formats everything is parsed and stored the same way as it was with the old format. Therefore the raw text for a name of type 'EC' e.g. 6.3.5.5 will be "EC 6.3.5.5" (instead of "6.3.5.5"). Other strings only present in old DE line text format ('precursor' flag and 'Allergen', 'antigen' strings) are also added in the stored raw text. The safe method to get the DE text is C (with both the new and old DE line format), which for "EC=6.3.5.5" (new DE line format), will return "6.3.5.5" (DE object of 'EC' type). For "(EC 6.3.5.5)" (old DE line format), will return "EC 6.3.5.5" =item C The category of the protein name: 'RecName', 'AltName', 'SubName' (TrEMBL only) DE RecName: Full=CAD protein; DE Short=CAD; Here both names (DE objects), are of category 'RecName' Category can be set/modified using C Note: with the old DE line format, this field is undef =item C The type of the protein name: 'Full', 'Short', 'EC' 'Allergen', 'CD_antigen', 'Biotech','INN' DE RecName: Full=CAD protein; DE Short=CAD; Here the first name (DE object), is of type 'Full', the second one is of type 'Short' Type can be set/modified using C Note: with the old DE line format, this field is undef =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText ($addParen) addParen : (meaningful only with old DE line format) if set to true, the name will be surrounded by parentheses, but not the evidence tags, e.g. : '(UMP SYNTHASE){E1}'. =back =head1 Evidence Tags Each protein name (DE object) can have independent evidence tags. DE SubName: Full=Histone H3{EI1}; DE EC=3.4.21.9{EC3}; DE AltName: Full=Enterokinase{EC5}; The following methods have their prototype defined in SWISS::BaseClass instead of the direct parent of SWISS::DEs, SWISS::ListBase : addEvidenceTag deleteEvidenceTags getEvidenceTags getEvidenceTagsString hasEvidenceTag setEvidenceTags example : $evidenceTag = $entry->Stars->EV->addEvidence('P', 'DEfix', '-', 'v1.3'); $entry->DEs->head->addEvidenceTag($evidenceTag); The easiest way to read the evidence tags of a protein name is to use c that will return the evidence tags as a string with the enclosing {} brackets. If there are no evidence tags, will return an empty string. Swissknife_1.75/lib/SWISS/BaseClass.pm0000644005110600510130000002371212400117505017725 0ustar ecastroSwissProtpackage SWISS::BaseClass; use vars qw($AUTOLOAD @ISA @EXPORT_OK); use Exporter; use Carp; use strict; use Data::Dumper; # Place functions/variables you want to *export*, ie be visible from the caller package into @EXPORT_OK @EXPORT_OK = qw(); use vars qw { @ISA $AUTOLOAD %fields }; BEGIN { # Our inheritance @ISA = ( 'Exporter' ); # our data members %fields = (_dirty => undef, evidenceTags => undef, indentation => undef, ); } # makes it appear that there are functions # of the same names as the member variables # which get and set their value sub AUTOLOAD { my $name = $AUTOLOAD; $name =~ /::DESTROY/ && return; $name =~ s/.*://; my $self = shift; my $type = ref($self) || confess "Cannot use the non-object $self to find $name\n"; unless (exists $self->{$name} ) { confess "In type $type, can't access $name. Incorrect function or member name.\n"; return undef; } if (@_) { # something is being set, so the object is dirty. $self->{_dirty} = 1; return $self->{$name} = shift; } else { return $self->{$name}; } } # reblesses a reference to a base class object into your class # adds the apropreate members with their default values as # defined in the %fields hash, and modified by initialize sub rebless { no strict 'refs'; my $self = shift || confess "You must parse an object to rebless"; my $class = shift || confess "You must give a package to rebless $self into"; %{$self} = (%{$self}, %{$class."::fields"}); bless $self, $class; $self->initialize(); return $self; } # returns a myBase object # use this for all derived classes sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = {}; rebless($self, $class); return $self; } # put any code that you want which initializes the virgin values of # your member variables in here sub initialize { my $self = shift; $self->{'evidenceTags'} = '{}'; $self->{'indentation'} = undef; return $self; } sub update { my $self = shift; return $self; } # checks for name clashes between a class and all of it's base classes. # Supports multiple inheritance, and multi-level inheritance # sub check4Clashes { no strict 'refs'; my $class = shift; my @fields = keys %{$class."::fields"}; my @parents = @{$class."::ISA"}; my $parent; my $override; my @found = (); foreach $parent (@parents) { $override = ($parent->can('_containsFields') && $parent->_containsFields(@fields)); $override && push @found, @$override; } if(@found) { confess "$class contains member variables that clash with base class members\n", map { "\t$_\n"} @found; } } # helper function for checkClashes # less said about this the better # sub _containsFields { no strict 'refs'; my $class = shift; my @fields = @_; my $field; my @parents = @{$class."::ISA"}; my $parent; my $override; my @found = (); foreach $field (@fields) { if(exists ${$class."::fields"}{$field}) { push @found, $class."::".$field; } } foreach $parent (@parents) { $override = ($parent->can('_containsFields') && $parent->_containsFields(@fields)); $override && push @found, @$override; } (@found) && return \@found; return undef; } # added by hhe@ebi.ac.uk sub equal { my ($self, $other) = @_; return Dumper($self) eq Dumper($other); }; # Returns a "deep copy" of the object sub copy { my $self = shift; my $new; eval Data::Dumper->Dump([$self], [qw(new *ary)]); return $new; } # Evidence tag handling sub setEvidenceTags { my $self = shift; my @tags = @_; my $is_new = grep { /ECO:/ } @tags; my $joiner = $is_new ? ', ' : ','; $self->{'evidenceTags'} = ( $is_new ? ' ' : '' ) . '{' . (join $joiner, @tags) . '}'; # p.s. fugly: there is a space before { in new ev format: automatically add it depending if added tag is in new format! $self->{'_dirty'} = 1; return; } sub addEvidenceTag { my $self = shift; my $tag = shift; my $is_new_format = $tag =~ /ECO:/; my $actual_ev = $self->{'evidenceTags'}; unless ( $actual_ev =~ /[\{\,] ?\Q$tag\E[\}\,]/ ) { # add only if new if ($actual_ev eq '{}') { $self->{'evidenceTags'} = ( $is_new_format ? ' ' : '' ) . '{' . $tag . '}'; } else { $self->{'evidenceTags'} =~ s/\{/ {/ if $is_new_format && $actual_ev =~ /^\{/; if ( $is_new_format ) { $self->{'evidenceTags'} =~ s/\}/\, $tag\}/; } else { $self->{'evidenceTags'} =~ s/\}/\,$tag\}/; } } # p.s. fugly: there is a space before { in new ev format: automatically add it depending if added tag is in new format! } $self->{'_dirty'} = 1; return; } sub deleteEvidenceTag { my $self = shift; my $tag = shift; $self->{'evidenceTags'} =~ s/([\{\,] ?)\Q$tag\E([\,\}])/$1$2/; $self->{'evidenceTags'} =~ s/\, ?\,/\,/; $self->{'evidenceTags'} =~ s/\, ?\}/\}/; $self->{'evidenceTags'} =~ s/\{\, ?/\{/; $self->{'evidenceTags'} =~ s/ ?\{\}//; $self->{'_dirty'} = 1; return; } sub hasEvidenceTag { my $self = shift; my $tag = shift; return $self->{'evidenceTags'} =~ /[\{\,] ?\Q$tag\E[\}\,]/; } sub getEvidenceTags { my $self = shift; my $tmp = $self->{'evidenceTags'}; $tmp =~ tr/\{\}//d; return map { s/^ +//; $_ } split /\, ?/, $tmp; } sub getEvidenceTagsString { my $self = shift; my $tmp = $self->{'evidenceTags'}; if ($tmp eq '{}') { return ''; } else { return $tmp; } } # Force Swissknife to reformat an object, even if it has not been modified. sub reformat { my $self = shift; $self->{_dirty} = 1; } 1; __END__ =head1 NAME SWISS::BaseClass =head1 DESCRIPTION This class is designed to impliment many of the properties that you expect in inheritance. All the housekeeping functions are defined in this module. See the notes on use for a description of how to make use of it. =head1 Functions =over =item new Returns a new SWISS::BaseClass object. =item rebless Converts a base class into your class! Call as $self->rebless($class) where $self is a base class object. It returns $self, reblessed, with the correct member variables. =item initialize Override this in each derived class to provide class specific initialization. For example, initialize may put arrays into member variables that need them. You must provide an initialize function. =item reformat Some line objects are implementing "lazy writing". This means that on writing an entry, they are only reformatted if they have been modified. The method reformat forces an object to be reformatted even if its content has not been modified. This may be useful e.g. to make sure the current formatting rules are applied. =item setEvidenceTags @array Sets the evidence tags of the object to the list passed in @array. =item addEvidenceTag string Adds the evidence tag to the object. =item deleteEvidenceTag string Deletes the evidence tag from the object. =item hasEvidenceTag string returns true if the object has the evidence tag. =item getEvidenceTags returns the array of evidence tags of the object =item Check4Clashes This function checks your classes member variable list for clashes with any class that it inherits from (any class that can(_containsFields) returns true on!). If it detects that in any base class that any data members have been already defined, it dies with a listing of the variables already used. It stops searching a root of an inheritance hierachy when it can find no baseclasses that support _containsFields. It will find all clashes in an entire inheritance tree. So in the inheritance hierachy of SWISS::BaseClass -> A -> B -\ > E SWISS::BaseClass -> C -> D -/ where E is the most derived class, if E contains names that clash with A members and names that clash with B members, both the A and B member clashes will be reported. If there were clashes with B and C, say, then again, all of the clashes would be reported. =item _containsFields This function is responsible for comparing a classes fields with the set in the calling package. This implimentation will work for cases where all of the classes that contribute fields are derived from SWISS::BaseClass. You may wish to make your own class fit this interface, so what follows is an interface API. _containsFields assumes that the first argument is the package that it is being called in. The following arguments are taken to be a list of fields which to check are not found in members of the current package. It should return either C or a reference to an array of name clashes in the format C. It should call it's self for each parental class that supports this function. So it would look something like _containsFields { my $class = shift; my @toCheck = @_; foreach @toCheck { check that they are not in me. If they are, add them to the list of clashes to return. } add all base class clashes to your list of clashes if there were name clashes return a reference to them otherwise return undef } =item equal If two objects are equal, it returns true. Warning: This funktion compares two objects using a simple dump in Perl format, see Data::Dumper module. The comparison also takes private variables into account. Therefore: If the method 'equal' returns true, the objects are guaranteed to be equal, but it might return false although the two objects are equal in they public attributes. =item copy Returns a "deep copy" of the object. =back =head1 A skeletal derived class package myDerived; use vars qw ( @ISA %fields ); BEGIN { @ISA = ('SWISS::BaseClass'); %fields = ( 'i' => 1, 'hash' => undef ); myDerived->check4Clashes(); } sub new { print "myDerived::new(@_)\n"; my $class = shift; my $self = new SWISS::BaseClass; $self->rebless ($class); return $self; } sub initialize { my $self = shift; $self->{'hash'} = {}; } A class derived from myDerived would just substitute the name myDerived for SWISS::BaseClass. Hey presto - all sorted! Swissknife_1.75/docs/0000755005110600510130000000000013155516754015015 5ustar ecastroSwissProtSwissknife_1.75/docs/CC.html0000644005110600510130000000431313155516743016167 0ustar ecastroSwissProt SWISS::CC

Name

SWISS::CC.pm

Description

SWISS::CC represents a comment on a single topic within a SWISS-PROT or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Each comment is stored in a separate object, either of the type SWISS::CC or of another type, depending on its topic (see SWISS::CCs for more information).


Collectively, comments of all types are stored within a SWISS::CCs container
object.

Inherits from

SWISS::BaseClass.pm

Attributes

topic

The topic of this comment.

comment

The text of this comment.

Methods

Standard methods

new
fromText
toString

Returns a string representation of this comment.

Swissknife_1.75/docs/GeneGroup.html0000644005110600510130000001035313155516743017576 0ustar ecastroSwissProt SWISS::GeneGroup

Name

SWISS::GeneGroup.pm

Description

A SWISS::GeneGroup object contain all synonyms for a given gene name. See SWISS::GNs for a description of the gene name format.

Inherits from

SWISS::BaseClass.pm

(also implements many methods from SWISS::ListBase.pm)

Attributes

Names
  Each list element is a SWISS::GN object, describing a primary name
  or synonym. Concatenation of Name and Synonyms lists.
OLN
  Each list element is a SWISS::GN object, describing an
  OrderedLocusName.
ORFNames
  Each list element is a SWISS::GN object, describing an ORFName.

Methods

Standard methods

new
fromText
toText

Specific methods

Name

Returns the Name (primary name).

Synonyms

Returns the Synonyms.

elements
  Concatenates all elements from Names, OLN and ORFNames in
  a single array.

List manipulation methods

Since GeneGroup was a previous implementation of SWISS::ListBase, the list manipulation methods below are provided to facilitate compatibility.

size
isEmpty
elements
filter
get (deprecated)
head (deprecated)
tail (deprecated)
item (deprecated)
push (deprecated)
pop (deprecated)
shift (deprecated)
splice (deprecated)
unshift (deprecated)
set (deprecated)
add (deprecated)
Swissknife_1.75/docs/OH.html0000644005110600510130000000344013155516743016210 0ustar ecastroSwissProt SWISS::OH

Name

SWISS::OH

Description

SWISS::OH represents one taxon from the OH line. The container object is SWISS::OHs.

Inherits from

SWISS::BaseClass.pm

Attributes

NCBI_TaxID

Tax ID.

text

Name, common name and synonym of the organism.

Methods

Standard methods

new
fromText
toText
Swissknife_1.75/docs/FTs.html0000644005110600510130000000406113155516743016376 0ustar ecastroSwissProt SWISS::FTs

Name

SWISS::FTs

Description

SWISS::FTs represents the FT (feature) lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

Inherits from

SWISS::ListBase.pm

Attributes

list

An array of arrays. Each element is an array containing: a feature key, from position, to position, description, qualifier, FTId and an evidence tag. Example: ['CHAIN', 25, 126, 'Alpha chain', 'By similarity', '/FTId=PRO_0000023008', '{EC1}']

Methods

Standard methods

new
fromText
toText
sort
Swissknife_1.75/docs/DE.html0000644005110600510130000001073213155516743016174 0ustar ecastroSwissProt SWISS::DE

Name

SWISS::DE.pm

Description

Each DE object represents one protein name. The container object for all names of an entry is SWISS::DEs

Inherits from

SWISS::BaseClass

Attributes

text

The raw text of the protein name. Note: as SwissKnife works with both new and old DE line formats, for backward rcompatibility, with both formats everything is parsed and stored the same way as it was with the old format. Therefore the raw text for a name of type 'EC' e.g. 6.3.5.5 will be "EC 6.3.5.5" (instead of "6.3.5.5"). Other strings only present in old DE line text format ('precursor' flag and 'Allergen', 'antigen' strings) are also added in the stored raw text. The safe method to get the DE text is toText (with both the new and old DE line format), which for "EC=6.3.5.5" (new DE line format), will return "6.3.5.5" (DE object of 'EC' type). For "(EC 6.3.5.5)" (old DE line format), will return "EC 6.3.5.5"

category

The category of the protein name: 'RecName', 'AltName', 'SubName' (TrEMBL only)

 DE   RecName: Full=CAD protein;
 DE            Short=CAD;
 
 Here both names (DE objects), are of category 'RecName'

Category can be set/modified using category(string)

Note: with the old DE line format, this field is undef

type

The type of the protein name: 'Full', 'Short', 'EC' 'Allergen', 'CD_antigen', 'Biotech','INN'

 DE   RecName: Full=CAD protein;
 DE            Short=CAD;
 
 Here the first name (DE object), is of type 'Full', the second one 
 is of type 'Short'

Type can be set/modified using type(string)

Note: with the old DE line format, this field is undef

Standard methods

new
fromText
toText ($addParen)
 addParen : (meaningful only with old DE line format) if set to true, 
 the name will be surrounded by parentheses, but not the evidence 
 tags, e.g. : '(UMP SYNTHASE){E1}'.

Evidence Tags

Each protein name (DE object) can have independent evidence tags.

 DE   SubName: Full=Histone H3{EI1};
 DE            EC=3.4.21.9{EC3};
 DE   AltName: Full=Enterokinase{EC5};

The following methods have their prototype defined in SWISS::BaseClass instead of the direct parent of SWISS::DEs, SWISS::ListBase :

 addEvidenceTag
 deleteEvidenceTags
 getEvidenceTags
 getEvidenceTagsString
 hasEvidenceTag
 setEvidenceTags

example :

 $evidenceTag = $entry->Stars->EV->addEvidence('P', 'DEfix', '-', 'v1.3');
 $entry->DEs->head->addEvidenceTag($evidenceTag);
 
The easiest way to read the evidence tags of a protein name is to use 
c<getEvidenceTagsString> that will return the evidence tags as a string with 
the enclosing {} brackets. If there are no evidence tags, will return an empty 
string.
Swissknife_1.75/docs/CCsubcell_location.html0000644005110600510130000000645313155516743021440 0ustar ecastroSwissProt SWISS::CCsubcell_location

Name

SWISS::CCsubcell_location.pm

Description

SWISS::CCdisease represents a comment on the topic 'SUBCELLULAR LOCATION' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information).

Collectively, comments of all types are stored within a SWISS::CCs container object.

Inherits from

SWISS::BaseClass.pm

Attributes

topic

The topic of this comment ('SUBCELLULAR LOCATION').

locations

The locations; reference to an array [ { 'form' => $in_form, 'component' => [ $component, $component_ev ], 'topology' => [ $topology, $topology_ev ], 'orientation' => [ $orientation, $orientation_ev ] }, ... ]

locations( $new_locations )

Set locations to $new_locations, that should be an array: [ { 'form' => $in_form, 'component' => [ $component, $component_ev ], 'topology' => [ $topology, $topology_ev ], 'orientation' => [ $orientation, $orientation_ev ] }, ... ]

note

The note and evidence of the disease reference to an array of [ $note, $note_ev ] array

note( [ $new_note, $new_note_ev ] )

Set note to [ $new_note, $new_note_ev ]

comment

The "text" version of this comment.

Standard methods

new
fromText
toString

Returns a string representation of this comment.

Swissknife_1.75/docs/OXs.html0000644005110600510130000000426013155516743016414 0ustar ecastroSwissProt SWISS::OXs

Name

SWISS::OXs

Description

SWISS::OXs represents the OX lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OXs object is a container object which holds a list of SWISS::OX objects for each currently permitted taxonomic resource.

Inherits from

SWISS::BaseClass.pm

Attributes

NCBI_TaxID
  A ListBase object which holds a list of tax ids.

Standard methods

new
fromText
toText

Example

  $taxid = new SWISS::OX;
  $taxid->text('1234');
  $entry->OXs->NCBI_TaxID()->add($taxid);


  foreach my $taxid ($entry->OXs->NCBI_TaxID()->elements()) {
    print $taxid->text, "\n";
  }
Swissknife_1.75/docs/PE.html0000644005110600510130000000316413155516743016211 0ustar ecastroSwissProt SWISS::PE

Name

SWISS::PE

Description

Indicates what kind of evidence there is for the existence of a protein.

Inherits from

SWISS::BaseClass

Attributes

text

The type of evidence.

Methods

Standard methods

new
fromText
toText
Swissknife_1.75/docs/Stars.html0000644005110600510130000000570013155516744017000 0ustar ecastroSwissProt SWISS::Stars

NAME

SWISS::Stars.pm

DESCRIPTION

SWISS::Stars represents the ** lines within an SWISS-PROT + TrEMBL entry. These are the lines with the line tag ** which are normally not publicly visible.

SWISS::Stars is a master object like SWISS::Entry. It contains subobjects which represent the different line types in the ** section. Each line type has a two letter tag in addition to the ** line tag. This module has been written to allow easy addition of new ** line types. To use a new ** line tag, just use the tag as an object dereference. Example:

 $entry->Stars->XX->add("New XX tag line.","Second new XX tag line.");

If there is no class SWISS::Stars::XX, the class of the new object will be SWISS::Stars::default, which handles lines with the corresponding tag as an array of lines. If more specific handling is required, a new class SWISS::Stars::XX can be created following the template of SWISS::Stars::default. An example is SWISS::Stars::aa.

Subclass names and new line tags have to be two-letter-tags. No checks are made wheter the dereferenced tag is allowed.

Access to the (old) unstructured ANNOTATOR'S SECTION is provided by the line tag 'aa'.

 $entry->Stars->aa->add("Testline 1.","Second new test line.");

will add these two lines to the ANNOTATOR'S SECTION.

Inherits from

SWISS::BaseClass.pm

Attributes

No public attributes apart from the subclasses.

Methods

Standard methods

new
fromText
toText
update
Swissknife_1.75/docs/Ref.html0000644005110600510130000000711713155516743016423 0ustar ecastroSwissProt SWISS::Ref

Name

SWISS::Ref.pm

Description

SWISS::Ref represents a single reference of a SWISS-PROT + TREMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

Inherits from

SWISS::BaseClass.pm

Attributes

RN

The reference number.

RP

The RP line(s), unwrapped as a string.

RC

Zero or more RC lines.

Data structure: {Token}[qualifier1, qualifierN].

A hash of arrays. Hash keys are the RC tokens, array elements are the qualifiers for that token.

RX

References to bibliographic databases.

Data structure: {Database}[identifier1, identifierN].

A hash of arrays. Hash keys are the names of bibliographic databases, array elements are the identifiers of the reference for that database.

RG

The RG line(s), unwrapped as a string.

RA

The list of Authors.

An object of type SWISS::ListBase.

RT

The publication title, unwrapped as a string.

RL

The RL line.

Data structure: String.

Methods

Standard methods

new
fromText
toText

Writing methods

add_MedlineID

Add a RX line 'MEDLINE; nnnnnnnn.' to the reference.

add_Author

Add an author to the RA line of the reference.

rc_sort

Sort elements of the RC line alphabetically.

Swissknife_1.75/docs/SQs.html0000644005110600510130000000526013155516743016412 0ustar ecastroSwissProt SWISS::SQs

NAME

SWISS::SQs.pm

DESCRIPTION

SWISS::SQs represents the SQ lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

Inherits from

SWISS::BaseClass.pm

Attributes

seq

The amino acid sequence in string representation.

length

The sequence length.

molWeight

The molecular weight.

crc

The CRC checksum of the sequence. This is recalculated using the SWISS::CRC64 module.

Methods

Standard methods

new
fromText
toText
update

Should be called if the sequence has been modified.

Specific methods

calcMolWeight string

Calculate the molecular weight for string.

Swissknife_1.75/docs/CCs.html0000644005110600510130000001065113155516743016354 0ustar ecastroSwissProt SWISS::CCs

Name

SWISS::CCs

Description

SWISS::CCs represents the CC lines within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The CCs object is a container object which holds a list comprised of object of the type SWISS::CC or derived classes (see below).

Code example

local $/="\n//\n";


while (<>) {

  my $entry = SWISS::Entry-> fromText($_);
  my @CCs = $entry -> CCs -> elements();

  for my $CC (@CCs) {

    if ($CC -> topic eq 'ALTERNATIVE PRODUCTS') {

      # now can call methods of CCalt_prod

    } elsif ($CC -> topic eq 'Copyright') {

      # now can call methods of CCcopyright

    } else {

      # now can call methods of CC
    }
  }
}

Inherits from

SWISS::ListBase.pm

Attributes

list

Each list element is an object of one of the following classes, depending of the type of comment:

 topic                           object
 --------------------            --------------------
 ALTERNATIVE PRODUCTS            SWISS::CCalt_prod
 RNA EDITING                     SWISS::CCrna_editing
 BIOPHYSICOCHEMICAL PROPERTIES   SWISS::CCbpc_properties
 INTERACTION                     SWISS::CCinteraction
 Copyright                       SWISS::CCcopyright
 (all other topics)              SWISS::CC

Methods

Standard methods

new
fromText
sort

Sort the CC block according to the order given in Swiss-Prot annotation note ANN017.

toText
update

Reading/Writing methods

ccTopic ($topic)

Returns true if entry contains a comment block with the specified topic.

copyright

Returns a string representation of the copyright text.

del (@patternList)

Deletes all comment elements whose topic matches the first element of the pattern list. The second element is the used to specify a requirement for the comment to match as well.

get (@patternList)

An array is returned consisting of all comment elements elements whose topic matches any elements of the pattern list.

getObject (@patternList)

Same as get, but returns the results wrapped in a new ListBase object.

toString

Returns a string representation of the CCs object.

Swissknife_1.75/docs/DEs.html0000644005110600510130000001617613155516743016367 0ustar ecastroSwissProt SWISS::DEs

Name

SWISS::DEs.pm

Description

SWISS::DEs represents the DE lines of a UniProt Knowledgebase (Swiss-Prot + TrEMBL) entry as specified in the user manual http://www.expasy.org/sprot/userman.html.

The DEs object basically holds lists of DE objects, each of them representing a protein name element. The elements, hasFragment, Includes and Contains attributes/methods work as follows :

 DE   RecName: Full=CAD protein;
 DE            Short=CAD;
 DE   AltName: Full=Protein rudimentary;
 DE   Includes:
 DE     RecName: Full=Glutamine-dependent carbamoyl-phosphate synthase;
 DE              EC=6.3.5.5;
 DE   Includes:
 DE     RecName: Full=Aspartate carbamoyltransferase;
 DE              EC=2.1.3.2;
 DE   Flags: Fragment;
 -= Entry::DEs =-
 elements (for each DE object, see SWISS::DE.pm documentation) :
    toText:    "CAD protein",  "CAD",       "Protein rudimentary"
    category:  "RecName",      "RecName",   "AltName"
    type:      "Full",         "Short"      "Full"    
 hasFragment : "Fragment"
 Includes : ListBase of DEs (child1, child2)
 Contains : empty ListBase
 -= child1 =-    
 elements (for each DE object) :
    toText:    "Glutamine-dependent carbamoyl-
                phosphate synthase",            "6.3.5.5"
    category:  "RecName",                       "RecName",
    type:      "Full",                          "EC"   
 hasFragment : undef
 -= child2 =-    
 elements (for each DE object) :
    toText:    "Aspartate carbamoyltransferase",  "2.1.3.2"
    category:  "RecName",                         "RecName",
    type:      "Full",                            "EC"  
 hasFragment : undef

Note: the old unstructured DE format can still be used, and will be parsed the same way into DE objects (but without setting their attributes 'category' and 'type'.

 DE   CAD protein (Protein rudimentary) [Includes: Glutamine-dependent
 DE   carbamoyl-phosphate synthase (EC 6.3.5.5); Aspartate
 DE   carbamoyltransferase (EC 2.1.3.2)] (Fragment).

Inherits from

SWISS::ListBase.pm

Attributes

text

The (raw) text of the DE line (without the 'DE ' line type prefixes)

list

Array reference to the SWISS::DE objects containing the different names for the entry. The first element of the list is the recommended name. Note: use elements method (inherited from ListBase) to get (and loop through) the array of DE objetcs.

Includes
Contains

Each of these is a SWISS::ListBase object whose list contains a SWISS::DEs object for each 'child' of the protein (i.e. peptide or functional domain). See the UniProtKB user manual for an explanation. It is possible to have both Includes and Contains in a single entry:

 DE   RecName: Full=Arginine biosynthesis bifunctional protein argJ;
 DE   Includes:
 DE     RecName: Full=Glutamate N-acetyltransferase;
 DE              EC=2.3.1.35;
 DE     AltName: Full=Ornithine acetyltransferase;
 DE              Short=OATase;
 DE     AltName: Full=Ornithine transacetylase;
 DE   Includes:
 DE     RecName: Full=Amino-acid acetyltransferase;
 DE              EC=2.3.1.1;
 DE     AltName: Full=N-acetylglutamate synthase;
 DE              Short=AGS;
 DE     RecName: Full=Arginine biosynthesis bifunctional protein argJ alpha chain;
 DE   Contains:
 DE     RecName: Full=Arginine biosynthesis bifunctional protein argJ beta chain;
hasFragment

Contains 'Fragment' or 'Fragments' (evaluates to true) if the DE lines contain the 'Fragment(s)' indication (in 'Flags:' line with the new DE line format), otherwise evaluates to false. Compare to the more robust Entry::isFragment which also checks the FT lines for a NON_CONS or NON_TER.

isPrecursor

Returns 1 if the flag 'Precursor' is present (undef if not). Note: only with new DE line format.

Methods

Standard methods

new
fromText
toText

Evidence Tags

With the new DE line format, each DE element can have distinct evidence tags, which are stored in the DE object themself (see SWISS::DE.pm documentation). The evidence tags for the 'Flags' line are stored in the parent DEs object itself. With the old DE line format, since the DE line did not have a fixed syntax in TrEMBL, it is impossible to reliably assign evidence tags separately to the different elements of the DE lines. Therefore, the DE line can only be evidence tagged as a whole, and the following methods have their prototype defined in SWISS::BaseClass instead of the direct parent of SWISS::DEs, SWISS::ListBase :

 addEvidenceTag
 deleteEvidenceTags
 getEvidenceTags
 getEvidenceTagsString
 hasEvidenceTag
 setEvidenceTags

example :

 $evidenceTag = $entry->Stars->EV->addEvidence('P', 'DEfix', '-', 'v1.3');
 # add global DE evtag if old DE line format, 'Flags' evtag if new format
 $entry -> DEs -> addEvidenceTag($evidenceTag);
Swissknife_1.75/docs/CCcopyright.html0000644005110600510130000000433513155516743020124 0ustar ecastroSwissProt SWISS::CCcopyright

Name

SWISS::CCcopyright

Description

SWISS::CCcopyright represents the copyright statment within the comments block of a SWISS-PROT entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Collectively, comments of all types are stored within a SWISS::CCs container object.

Inherits from

SWISS::BaseClass.pm

Attributes

topic
    The topic of this comment ('Copyright').

Methods

Standard methods

new
fromText
toText

Reading/Writing methods

toString
    Returns a string representation of this comment.
Swissknife_1.75/docs/CCcofactor.html0000644005110600510130000000500213155516742017703 0ustar ecastroSwissProt SWISS::CCcofactor

Name

SWISS::CCcofactor

Description

SWISS::CCcofactor represents a comment on the topic 'COFACTOR' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information).

Collectively, comments of all types are stored within a SWISS::CCs container object.

Inherits from

SWISS::ListBase.pm

Attributes

topic

The topic of this comment ('COFACTOR').

comment

The "text" version of this comment (without evidences and new lines).

note

The note and evidence (Note= in new format or full description in old format) reference to an array of [ $note, $note_ev ] (strings)

elements

An array of [name_str, evidence_tags_str], if any.

Standard methods

new
fromText
toString

Returns a string representation of this comment.

Swissknife_1.75/docs/CCrna_editing.html0000644005110600510130000000471513155516743020401 0ustar ecastroSwissProt SWISS::CCrna_editing

Name

SWISS::CCrna_editing

Description

SWISS::CCrna_editing represents a comment on the topic 'RNA EDITING' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information).

Collectively, comments of all types are stored within a SWISS::CCs container object.

Inherits from

SWISS::ListBase.pm

Attributes

topic

The topic of this comment ('RNA EDITING').

note

The Note of this comment, if any. An array of [ sentence, evidence_tags ]

term

A string such as "Undetermined" or "Not_applicable", if any.

elements

An array of [position, evidence_tags], if any.

Standard methods

new
fromText
toString

Returns a string representation of this comment.

Swissknife_1.75/docs/GNs.html0000644005110600510130000001732313155516743016376 0ustar ecastroSwissProt SWISS::GNs

Name

SWISS::GNs.pm

Description

SWISS::GNs represents the GN lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The GNs object is a container object which holds a list of SWISS::GeneGroup objects.

Inherits from

SWISS::ListBase.pm

Attributes

list
  Each list element is a SWISS::GeneGroup object.
and (deprecated, for old format only)
  Delimiter used between genes. Defaults to " AND ".
or (deprecated, for old format only)
  Delimiter used between gene names. Defaults to " OR ".

Methods

Standard methods

new
fromText
toText

Reading/Writing methods

text [($newText)]

Sets the text of the GN line to the parameter if it is present, and returns the (unwrapped) text of the line. Also sets 'and' and 'or' delimiters to the first occurrences of the words "OR" and "AND" in the line, conserving the case.

lowercase (deprecated, for old format only)

Sets the GNs::and and GNs::or delimiters to their lower case values.

uppercase (deprecated, for old format only)

Sets the GNs::and and GNs::or delimiters to their upper case values.

getFirst()

Returns first gene name in gene line

getTags($target)

Returns evidence tags associated with $target

$target is a string

isPresent($target)

Returns 1 if $target is present in the GN line

$target is a string

needsReCasing($target)

If $target is present in the GN line, but wrongly cased, method returns the matching name in its current case

$target is a string

replace($newName, $target, $evidenceTag)

Replaces the first GN object in the GN line whose text attribute is $target with a new GN object whose text attribute is set to $newName and whose evidenceTags attribute is is set using values set by splitting $evidenceTag on /, / (as name is not being changed, programs should keep old tag and add new tag). Does nothing if $target is not found.

delete($target)

Removes synonym/single-member gene group matching $target. Note that if a "Name" is deleted, the first "Synonym" will be promoted to "Name"

addAsNewSynonym($newName, $target, $evidenceTag, $location)

Adds a new GN object (with text attribute set to new $newName, and evidenceTags attribute set to ($evidenceTag)), as a synonym to the first gene group in which $target is a gene name. Does nothing if $target is not found. Will not add a duplicate gene name. $location determines where in gene group new object is added: if $location == 1, 2, 3, ..., new object added in the 1st, 2nd, 3rd, ... position; if $location == 0, new object added before $target; if $location == -1, new object added after $target (default); if $location == -2, new object added at end of gene group. Note that if the new synonym is inserted in the first postion, it will become the "Name" and the previous "Name" will be downgraded to first "Synonym"

addAsNewGeneGroup($newName, $target, $evidenceTag, $location)

Adds a new GeneGroup object, comprising 1 GN object (with text attribute set to new $newName, and evidenceTags attribute set to ($evidenceTag)). Will not add a duplicate gene name. $location and $target determine where in GNs line new group is added: if $location == 1, 2, 3, ..., new object added in the 1st, 2nd, 3rd, ... position; if $location == 0, new object added before $target; if $location == -1, new object added after $target (default); if $location == -2, new object added at end of GNs line. Does nothing if $target is not found, and $location == 0 or -1; otherwise $target does not need to be set.

replaceGeneGroup($newGeneGroup, $target)

Replaces the first gene group containing $target with $newGeneGroup. Creating the $newGeneGroup correctly is the user's responsibility

getGeneGroup($target)

Returns the first gene group that contains $target

setToOr()

Retruns a new GNs object, but with all GNs objects in a single gene group. Needed when adding 'C' to 'A and B', when the relationship of 'C' to 'A' and 'B' is unknown: the universal use of ' or ' is the default delimeter for TrEMBL entries

TRANSITION

The format of the GN line will change in 2004 from:

 GN   (CYSA1 OR CYSA OR RV3117 OR MT3199 OR MTCY164.27) AND (CYSA2 OR
 GN   RV0815C OR MT0837 OR MTV043.07C).

to:

 GN   Name=CysA1; Synonyms=CysA; OrderedLocusNames=Rv3117, MT3199;
 GN   ORFNames=MtCY164.27;
 GN   and
 GN   Name=CysA2; OrderedLocusNames=Rv0815c, MT0837; ORFNames=MTV043.07c;

This module supports both formats. To convert an entry from the old to the new format, do:

 $entry->GNs->is_old_format(0);
Swissknife_1.75/docs/OHs.html0000644005110600510130000000315713155516743016400 0ustar ecastroSwissProt SWISS::OHs

Name

SWISS::OHs

Description

SWISS::OHs represents the OH lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OHs object is a container object which holds a list of SWISS::OH objects.

Inherits from

SWISS::BaseClass.pm

Methods

Standard methods

new
fromText
toText
Swissknife_1.75/docs/OS.html0000644005110600510130000000312513155516743016223 0ustar ecastroSwissProt SWISS::OS

Name

SWISS::KWs

Description

SWISS::OS represents one organism name from the OS line. The container object holding all organism lines is SWISS::OSs.

Inherits from

SWISS::BaseClass.pm

Attributes

text

One organism name.

Standard methods

new
fromText
toText
Swissknife_1.75/docs/ListBase.html0000644005110600510130000002436113155516743017415 0ustar ecastroSwissProt SWISS::ListBase

Name

SWISS::ListBase.pm

Description

Base class for list oriented classes in the SWISS:: hierarchy. It provides a set of quite general list manipulation methods to inheriting classes.

Attributes

list

Holds an array, the essential content of the object. Array elements can be, and are in fact frequently, arrays themselves.

Methods

Standard methods

new
initialize

Reading methods

head

Return the first element of the list

tail

Return all but the first element of the list

get pattern

Return a list of all elements matched by $pattern. Only exact matches are returned, but you can use Perls regular expressions. Example:

  $listBaseObject->set('EMBL', 'TREMBL', 'SWISSPROT'); 
  $listBaseObject->get('.*EMBL');

returns ('EMBL', 'TREMBL')

get @patternList

To be used if the ListBase elements are arrays. An array is returned if all its elements are matched exactly by the elements from @patternList with the same index. Empty elements in @patternList always match. Example:

 $listBaseObject->set(['EMBL', 'M1', 'G1', '-'],
                      ['EMBL', 'M2', 'A2', '-'],
                      ['EMBL', 'M2', 'G3', 'ALT_TERM'],
                      ['PROSITE', 'P00001', '1433_2', '1']);
 $listBaseObject->get('EMBL');
 returns (['EMBL', 'M1', 'G1', '-'],
          ['EMBL', 'M2', 'A2', '-'],
          ['EMBL', 'M2', 'G3', 'ALT_TERM'])
 
 $listBaseObject->get('',M2);
 returns (['EMBL', 'M2', 'A2', '-'],
          ['EMBL', 'M2', 'G3', 'ALT_TERM']);

Offering get in the interface is not particularly nice because it exports implementation details into the interface, but it is a powerful method which may save a lot of programming time. As an alternative, the 'filter' concept is available.

getObject pattern
getObject @patternList

Same as get, but returns the results wrapped in a new ListBase object.

filter

Returns a new object containing all of the elements that match a search criteria. It takes a function as the only parameter. This function should expect a list element, and return true or false depending on whether the element matches the criteria. If the object is not a ListBase object but member of a subclass, a new object of that subclass will be returned.

Example:

 $tmp = $entry->CCs->filter(&ccTopic('FUNCTION'));

returns a SWISS::CCs object containing all CC blocks from $entry which have the topic 'FUNCTION'.

Functions can also be anonymous functions.

attributeEquals(string attributeName, string attributeValue)

Filter function. If the elements of a ListBase object are objects, they will be returned by this function if they have the attribute and it equals the attributeValue.

 Example:

$matchedKWs = $entry->KWs->filter(SWISS::ListBase::attributeEquals('text', $kw));

attributeMatchedBy(string attributeName, string pattern)

Filter function. If the elements of a ListBase object are objects, they will be returned by this function if they have the attribute and the attribute is matched by the pattern.

 Example:

$matchedKWs = $entry->KWs->filter(SWISS::ListBase::attributeMatchedBy('text', $kw));

isEmpty
size

The number of list elements in the object

elements

Returns the array of elements

hasEvidenceTag $arrayPointer $tag

Returns true if the array pointed to by $arrayPointer has the evidence tag $tag

getEvidenceTags $arrayPointer

returns the array of evidence tags of $arrayPointer

getEvidenceTagsString $arrayPointer

returns a string containing the evidence tags of $arrayPointer

Writing methods

item offset[, newValue]

returns the list element at a specific offset, and optionally sets it to a new value. Negative offsets are relative to the end of the list.

push list
pop
shift
unshift list
splice [offset[, length[, list]]]
set list

Sets the list attribute to @list

add list

Synonym for push

merge (ListBase)

Appends the elements of ListBase to the object

sort [function]

Applies a sort function to the list attribute, or by default, alphabetical sorting. Should be overwritten in derived classes with an adapted sort function.

del pattern

Deletes all items fully matching $pattern. Example:

  $listBaseObject->set('EMBL','TREMBL', 'SWISSPROT');
  $listBaseObject->del('EMBL');
  $listBaseObject->list();
  returns ('TREMBL','SWISSPROT').

If you want to delete more, use something like

  $listBaseObject->del('.*EMBL')

which deletes 'EMBL' and 'TREMBL'.

del @patternList

To be used if the ListBase objects are arrays. An array is deleted if all its elements are matched by the elements from @patternList with the same index.

Warning: Empty elements in @patternList always match!

Using the data from the get example above,

  $listBaseObject->del('','', 'A2')

results in

  (['EMBL', 'M1', 'G1', '-'],
   ['EMBL', 'M2', 'G3', 'ALT_TERM'],
   ['PROSITE', 'P00001', '1433_2', '1'])
update
unique

Makes sure each element is contained only once in a ListBase object. The second and subsequent occurrences of the same object are deleted. Example:

  $listBaseObject->set(EMBL, TREMBL, SWISSPROT);
  $listBaseObject->add(EMBL, MGD, EMBL);
  $listBaseObject->unique();

results in (EMBL, TREMBL, SWISSPROT, MGD)

setEvidenceTags $arrayPointer @array

sets the evidence Tags of the array pointed to by $arrayPointer to the contents of @array

To be used if the ListBase elements are themselves arrays. A typical construct would be

  foreach $dr ($entry->DRs->elements()) {
    $entry->DRs->setEvidenceTags($dr, 'E2', 'E3');
  }

Returns $arrayPointer.

addEvidenceTag $arrayPointer $tag

adds $tag to the evidence tags of $arrayPointer

To be used if the ListBase elements are themselves arrays. See documentation of setEvidenceTags.

Returns $arrayPointer.

deleteEvidenceTags $arrayPointer $evidenceTag

deletes $evidenceTag from the array pointed to by $arrayPointer

To be used if the ListBase elements are themselves arrays. A typical construct would be

  foreach $dr ($entry->DRs->elements()) {
    $entry->DRs->deleteEvidenceTags($dr, 'EC2');
  }

Returns $arrayPointer.

Swissknife_1.75/docs/GN.html0000644005110600510130000000467613155516743016222 0ustar ecastroSwissProt SWISS::GN

Name

SWISS::GN.pm

Description

SWISS::GN represents one gene name from the GN line. The container object for several synonym gene names is SWISS::GeneGroup.

Inherits from

SWISS::BaseClass.pm

Attributes

text

One gene name.

Methods

Standard methods

new
fromText
toText

Reading/Writing methods

toMixedCase(@regexps)

Convert gene names to mixed case, according to one or more regular expressions. This is typically useful for converting uppercase ORF numbers to mixed case. E.g. the E.coli gene "B1563" converted with the regexp '(b(\d{4}(\.\d)?))' will yield the gene name "b1563". The method also supports fused gene names, e.g. "B0690/B0691" is converted to "b0690/b0691". The method changes the text of the SWISS::GN object and also returns the new text value.

Swissknife_1.75/docs/Entry.html0000644005110600510130000001500013155516743016776 0ustar ecastroSwissProt SWISS::Entry

Name

SWISS::Entry

Description

Main module to handle SWISS-PROT entries. One Entry object represents one SWISS-PROT entry and provides an API for its modification.

The basic concept is the idea of lazy parsing. If an Entry object is created from the entry in flat file format, the text is simply stored in the private text attribute of the entry object. The member objects of the entry are only created if they are dereferenced.

Example

use SWISS::Entry;
# Read an entire record at a time
$/ = "\/\/\n";
while (<>){
  $entry = SWISS::Entry->fromText($_);
  print $entry->AC, "\n";
}

This minimum program reads entries from a file in SWISS-PROT format and prints the primary accession number for each of the entries.

Attributes

The following attributes represent member objects. They can be accessed like e.g. $entry->IDs

IDs

ID line object

ACs
DTs
DEs
GNs
OSs
OCs
Refs

The reference block object

CCs
KWs
DRs
FTs
Stars

Object for the annotator's section stored in the ** lines.

SQs

The sequence object.

Methods

new

Return a new Entry object

initialize

Initialise an Entry object and return it.

update [force]

Update an entry. The content of the member objects is written back into the private text attribute of the entry if necessary. If $force is true, an update of all member objects is forced.

reformat

Reformat all fields of an entry.

fromText $text [, $fullParse[, $removeInternalComments]]

Create an Entry object from the text $text. If $fullParse is true, the entry is parsed at creation time. Otherwise the individual line objects are only created if they are dereferenced. If $removeInternalComments is true, wild comments and indentation will be removed from the text before the parsing is done. [NOTE: wild comments are lines starting with a double asterisk located outside the Stars section, and indented lines are lines starting with spaces. Both are used internally by SWISS-PROT annotators during their work and excluded from internal and external releases.]

toText [$insertInternalComments]

Return the entry in flat file text format. If internal comments and indentation have been removed as specified in the parameters to fromText(), you may wish to reinsert them in the text output by setting $insertInternalComments to true.

toFasta

Return the entry in Fasta format.

equal

Returns True if two entries are equal, False otherwise

The following methods are provided for your convenience. They are shortcuts for methods of the individual line objects.

ID

Returns the primary ID of the entry.

AC

Returns the primary AC of the entry.

SQ

Returns the sequence of the entry.

EV

Returns the EV (evidence) object of an entry. SWISS-PROT internal method.

Data access methods

text

Returns the current text of the entry. Quick and dirty! No update of the text is performed before.

database_code

Is it a SWISS-PROT, TREMBL or TREMBLNEW entry? database_code tries to find it out. Return values are S for SWISS-PROT, 3 for TREMBL, Q for TREMBLNEW, ? for unknown.

isFragment

Returns true if the DE line indicates a fragment, or of the entry contains a NON_CONS or NON_TER feature.

isCurated

Returns 1 if the entry is a curated entry, 0 otherwise.

SWISS-PROT internal use only.

Swissknife_1.75/docs/OSs.html0000644005110600510130000000406213155516743016407 0ustar ecastroSwissProt SWISS::OSs

Name

SWISS::OSs

Description

SWISS::OSs represents the OS lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OSs object is a container object which holds a list of SWISS::OS objects.

n.b. entries from distinct species are not merged anymore, OSs will therefore only contain one OS (OS is still divided into a list of OS elements to keep compatibility with old code)!

Inherits from

SWISS::ListBase.pm

Attributes

list
  Each list element is a SWISS::OS object.

Methods

Standard methods

new
fromText
toText
Swissknife_1.75/docs/KWs.html0000644005110600510130000000371213155516743016410 0ustar ecastroSwissProt SWISS::KWs

Name

SWISS::KWs

Description

SWISS::KWs represents the KW lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

Inherits from

SWISS::ListBase.pm

Attributes

list

Each list element is a SWISS::KW object.

Methods

Standard methods

new
fromText
sort

sort() sorts the keywords alphabetically.

toText
Swissknife_1.75/docs/BaseClass.html0000644005110600510130000001521013155516742017537 0ustar ecastroSwissProt SWISS::BaseClass

NAME

SWISS::BaseClass

DESCRIPTION

This class is designed to impliment many of the properties that you expect in inheritance. All the housekeeping functions are defined in this module. See the notes on use for a description of how to make use of it.

Functions

new

Returns a new SWISS::BaseClass object.

rebless

Converts a base class into your class! Call as $self->rebless($class) where $self is a base class object. It returns $self, reblessed, with the correct member variables.

initialize

Override this in each derived class to provide class specific initialization. For example, initialize may put arrays into member variables that need them. You must provide an initialize function.

reformat

Some line objects are implementing "lazy writing". This means that on writing an entry, they are only reformatted if they have been modified. The method reformat forces an object to be reformatted even if its content has not been modified. This may be useful e.g. to make sure the current formatting rules are applied.

setEvidenceTags @array

Sets the evidence tags of the object to the list passed in @array.

addEvidenceTag string

Adds the evidence tag to the object.

deleteEvidenceTag string

Deletes the evidence tag from the object.

hasEvidenceTag string

returns true if the object has the evidence tag.

getEvidenceTags

returns the array of evidence tags of the object

Check4Clashes

This function checks your classes member variable list for clashes with any class that it inherits from (any class that can(_containsFields) returns true on!). If it detects that in any base class that any data members have been already defined, it dies with a listing of the variables already used.

It stops searching a root of an inheritance hierachy when it can find no baseclasses that support _containsFields. It will find all clashes in an entire inheritance tree.

So in the inheritance hierachy of

 SWISS::BaseClass -> A -> B -\
                             > E
 SWISS::BaseClass -> C -> D -/

where E is the most derived class, if E contains names that clash with A members and names that clash with B members, both the A and B member clashes will be reported.

If there were clashes with B and C, say, then again, all of the clashes would be reported.

_containsFields

This function is responsible for comparing a classes fields with the set in the calling package. This implimentation will work for cases where all of the classes that contribute fields are derived from SWISS::BaseClass. You may wish to make your own class fit this interface, so what follows is an interface API.

_containsFields assumes that the first argument is the package that it is being called in. The following arguments are taken to be a list of fields which to check are not found in members of the current package.

It should return either undef or a reference to an array of name clashes in the format package::variable. It should call it's self for each parental class that supports this function.

So it would look something like _containsFields { my $class = shift; my @toCheck = @_;

    foreach @toCheck {
      check that they are not in me.  If they are, add them to the list of clashes to return.
    }
    add all base class clashes to your list of clashes
    if there were name clashes return a reference to them
    otherwise return undef
  }
equal

If two objects are equal, it returns true.

Warning: This funktion compares two objects using a simple dump in Perl format, see Data::Dumper module. The comparison also takes private variables into account. Therefore: If the method 'equal' returns true, the objects are guaranteed to be equal, but it might return false although the two objects are equal in they public attributes.

copy

Returns a "deep copy" of the object.

A skeletal derived class

 package myDerived;
 use vars qw ( @ISA %fields );
 BEGIN {
    @ISA = ('SWISS::BaseClass');
    %fields = (
               'i' => 1,
               'hash' => undef
               );


    myDerived->check4Clashes();
 }


 sub new {
    print "myDerived::new(@_)\n";
    my $class = shift;
    my $self = new SWISS::BaseClass;
    
    $self->rebless ($class);
    
    return $self;
 }


 sub initialize {
    my $self = shift;
    $self->{'hash'} = {};
 }

A class derived from myDerived would just substitute the name myDerived for SWISS::BaseClass. Hey presto - all sorted!

Swissknife_1.75/docs/index.html0000644005110600510130000003440112366403770017010 0ustar ecastroSwissProt Swissknife

Swissknife

An object-oriented Perl library to handle Swiss-Prot entries

Swissknife has been developed in the Swiss-Prot groups at the European Bioinformatics Institute and the Swiss Institute of Bioinformatics.

The latest release is always available from https://sourceforge.net/projects/swissknife/files/latest/download.
The current and development version are hosted at SourceForge [Swissknife project page] [Browse CVS tree].

General information on installation etc. is contained in the file README. This document is the starting point to the usage documentation of the Swissknife modules.

Usage

To use Swissknife, include the line
use SWISS::Entry;
in your program.

A small program using Swissknife is example.pl.

The program benchmark.pl can be used to test the Swissknife components and to give a rough idea of the system performance. The program can be called with the Swiss-Prot example file SWISS100.dat.
Usage example:
cd SWISS/examples
perl benchmark.pl -file SWISS100.dat -repeats 10

The output should look similar to: 

*** Swissknife Benchmark and Test suite *** 
Read only:             :  0 wallclock secs ( 0.03 usr +  0.01 sys =  0.04 CPU) @ 250.00/s (n=10)
            (warning: too few iterations for a reliable count)
Read/Write NULL:       :  0 wallclock secs ( 0.03 usr +  0.01 sys =  0.04 CPU) @ 250.00/s (n=10)
            (warning: too few iterations for a reliable count)
Read/Write:            :  0 wallclock secs ( 0.03 usr +  0.03 sys =  0.06 CPU) @ 166.67/s (n=10)
            (warning: too few iterations for a reliable count)
Read/Write/addAC:      :  0 wallclock secs ( 0.11 usr +  0.03 sys =  0.14 CPU) @ 71.43/s (n=10)
            (warning: too few iterations for a reliable count)
Read/Write/Fullparse:  : 10 wallclock secs ( 9.29 usr +  0.05 sys =  9.34 CPU) @  1.07/s (n=10)
Read/Write/Fp/Update:  : 14 wallclock secs (14.22 usr +  0.04 sys = 14.26 CPU) @  0.70/s (n=10)
Read/equals:           :  0 wallclock secs ( 0.26 usr +  0.01 sys =  0.27 CPU) @ 37.04/s (n=10)
            (warning: too few iterations for a reliable count)
Read/Write/Modify:     :  4 wallclock secs ( 3.71 usr +  0.04 sys =  3.75 CPU) @  2.67/s (n=10)

A more comprehensive test set is provided in the t/ directory: 

cd SWISS/t
perl test.pl *.t
should produce an output similar to 

*** Swissknife test suite ***

DEs.t ............. ok   
FTId.t ............ ok   
GNs.t ............. ok   
annot.t ........... ok   
crc64.t ........... ok   
evidence.t ........ ok   
fasta.t ........... ok   
formatProblems.t .. ok   
identity.t ........ ok   
util.t ............ ok   
All tests successful.
Files=10, Tests=20,  2 wallclock secs ( 0.05 usr  0.02 sys +  1.39 cusr  0.09 csys =  1.55 CPU)
Result: PASS

Modules

Module Documentation Comment
The main module
Entry.pm Entry.html The main module to handle Swiss-Prot entries. One Entry object represents one Swiss-Prot entry and provides an API for its modification.
Line objects Each line object implements a class to handle one line object of an entry or (e.g. Ref.pm) a group of related line objects.
ACs.pm ACs.html Representation of the AC line.
DTs.pm DTs.html The date lines.
DEs.pm DEs.html The description lines.
DE.pm DE.html A single name for the protein.
DRs.pm DRs.html The DR lines, crossreferences to other databases.
CCs.pm  CCs.html  Comment lines.
CCcopyright.pm CCcopyright.html The copyright statement (part of the comment lines).
CCalt_prod.pm CCalt_prod.html One comment object of the topic ALTERNATIVE PRODUCTS.
CCrna_editing.pm CCrna_editing.html One comment object of the topic RNA EDITING.
CCbpc_properties.pm CCbpc_properties.html One comment object of the topic BIOPHYSICOCHEMICAL PROPERTIES.
CCinteraction.pm CCinteraction.html One comment object of the topic INTERACTION.
CCdisease.pm CCdisease.html One comment object of the topic DISEASE.
CCsubcell_location.pm CCsubcell_location.html One comment object of the topic SUBCELLULAR LOCATION.
CC.pm CC.html One comment object of any other topic.
FTs.pm FTs.html The feature lines.
GNs.pm GNs.html The gene lines.
GeneGroup.pm GeneGroup.html The different synonyms for a single gene name.
GN.pm GN.html One single gene name.
IDs.pm IDs.html The ID line.
KWs.pm KWs.html The keyword lines. KWs is a container object, it holds an array of KW objects.
KW.pm KW.html One keyword object.
OCs.pm OCs.html The OC line encoding the taxonomy of the source organism.
OGs.pm OGs.html The OG lines. OGs is a container object, it holds an array of OG objects.
OG.pm OG.html One organism name.
OSs.pm OSs.html The OS lines. OSs is a container object, it holds an array of OS objects.
OS.pm OS.html One organism name.
OXs.pm OXs.html The OX lines. OXs is a container object, for each valid taxonomic resource it contains a ListBase object which holds a list of OX objects.
OX.pm OX.html One tax id object.
Ref.pm Ref.html Represents one literature reference.
Refs.pm Refs.html Represents the list of literature references.
Stars.pm Stars.html The "annotator's section" (See note)
Stars/aa.pm Stars/aa.html Unstructured notes in the internal "annotator's section". See Stars.html
Stars/DR.pm Stars/DR.html DR in the internal "annotator's section". See Stars.html
Stars/EV.pm Stars/EV.html Evidence section. See Stars.html
Stars/default.pm Stars/default.html Default class for structured information in the internal "annotator's section". See Stars.html
SQs.pm SQs.html The sequence lines.
Base objects These modules implement the base classes from which all line object classes are derived.
BaseClass.pm BaseClass.html The base class, implementing common methods, e.g. equals
ListBase.pm ListBase.html Provides methods to manipulate list-based objects like KWs.pm
Auxiliary modules
TextFunc.pm TextFunc.html Auxiliary functions, mainly for text formatting.
CRC64.pm CRC64.html Provides a method to calculate the CRC64 checksum.

Bugs, Feedback

The Swissknife modules have been developed for internal use and are provided as they are. However, if they are actually used by external users, we'll happily try to incoporate any suggestions for improvement (especially on the documentation side?). Therefore:

Please report any bugs and suggestions for improvement to sk at ebi dot ac dot uk.

Notes

The ** lines (Stars.pm)

The Swissknife modules are used in the production of the TrEMBL protein database in the Swiss-Prot group at the EBI. The internal version of the entries may contain additional information for the database curators. This information is stored in lines with the line tag '**'. Therefore the Swissknife modules provide methods to handle these lines, although they are not visible to the public. As the ** lines may also be used to store additional information of the external users, the corresponding methods are not removed for the public release.

Evidence tags

From June 2000 onwards, we are introducing evidence tags into UniProtKB/Trembl. In the beginning, these will be deleted from the public version. However, Swissknife provides functions to handle them. See ListBase.html and BaseClass.html. Making Swissknife "Evidence tag compatible" also required a major change to the interface of the KWs, OGs and OSs modules. Originally they were simple ListBase classes, where each keyword/organism name was one element of the ListBase array. Now each keyword/organism name is held in its own object, see KW.html, OG.html and OS.html. evTest.pl is a sample program manipulating evidence tags.

Evidences in the UniProtKB flat file format

(Not public in UniProtKB before October 1, 2014) The evidence for annotations in UniProtKB entries has been available for several years in the XML and RDF representation of the data and we now intend to add this information to the text format (aka flat file format). Swissknife handles both those new evidences (in form {ECO:...[, ECO:...]}) and the old ones...

Authors

Swissknife has been developed by:
Wolfgang Fleischmann (European Bioinformatics Institute)
Alexandre Gattiker (Swiss Institute of Bioinformatics)
Henning Hermjakob (European Bioinformatics Institute)
Eric Jain (Swiss Institute of Bioinformatics)
Paul Kersey (European Bioinformatics Institute)
Edouard de Castro (Swiss Institute of Bioinformatics)

Swissknife_1.75/docs/TextFunc.html0000644005110600510130000001152413155516744017445 0ustar ecastroSwissProt SWISS::TextFunc

NAME

SWISS::TextFunc

DESCRIPTION

This module is designed to be a repository of functions that are repeatedly used during parsing and formatting of SWISS-PROT/TREMBL lines. If more than two line types need to do aproximately the same thing then it is probably in here.

All functions expect to be called as package->function(param list)

listFromText

Takes a piece of text, a seperator regex and a seperator that may appear at the end. Returns an array of items that were seperated in the text by that seperator. Takes care of null items (looses them for you).

textFromList

Takes an array of items, a separator, a terminating string, and a line width. Returns an array of strings, each ending with the separator or the terminator with a width less than or equal to the width specified.

Seems to do the wrong thing for references - not sure why. Don't use it for that.

wrapText

Takes a string and a length. Returns an array of strings which are shorter or equal in length to length, spliting the string on white space.

wrapOn ($firstLinePrefix, $linePrefix, $colums, $text[, @separators])

Wraps $text into lines with at most $colums colums. Prepends the prefixes to the lines. @separators is a list of expressions on which to wrap. The expression itself is part of the upper line.

If no @separators are provided, the $text is wrapped at whitespace except in EC/TC numbers or at dashes that separate words.

First tries to wrap on the first item of @separators, then the next etc. If no wrap on any element of @separators or whitespaces is possible, wraps into lines of exactly length $colums.

A special case is that the first item of @separators may be a reference to an array. This is used internally for wrapping FT VARIANT-like lines.

Example:

 wrapOn('DE ', 'DE ', 40, 
        '14-3-3 PROTEIN BETA/ALPHA (PROTEIN KINASE C INHIBITOR PROTEIN-1)', 
        '\s+') 
 returns ['14-3-3 PROTEIN BETA/ALPHA (PROTEIN ', 
          'KINASE C INHIBITOR PROTEIN-1)']
 wrapOn('DE ', 'DE ', 40, 
        '14-3-3 PROTEIN BETA/ALPHA (PROTEIN KINASE C INHIBITOR PROTEIN-1)', 
        ' (?=\()', '\s+')
 returns ['14-3-3 PROTEIN BETA/ALPHA ', 
          '(PROTEIN KINASE C INHIBITOR PROTEIN-1)']
cleanLine

Remove the leading line Identifier and three blanks and trailing spaces from an SP line.

joinWith ($text, $with, $noAddAfter, @list)

Concatenates $text and @list into one string. Adds $with between the original elements, unless the postfix of the current string is $noAddAfter. This is used to avoid inserting blanks after hyphens during concatenation. So unpleasant strings like 'CALMODULIN- DEPENDENT' are avoided. Unfortunately a correct reassembly of strings like 'CARBON-DIOXIDE' is not done.

insertLineGroup ($textRef, $text, $pattern)

Inserts text block $text into the text referred to by $textRef. $text will replace the text block in $textRef matched by $pattern.

uniqueList (@list)

Returns a list in which all duplicates from @list have been removed.

currentSpDate

returns the current date in SWISS-PROT format

toMixedCase($text, @regexps)

Convert a text to mixed case, according to one or more regular expressions. In scalar context, returns the new text; in array context, also returns the regexp with which the change was performed, or undef on failure. See corresponding item in SWISS::GN for more details.

Swissknife_1.75/docs/RCelement.html0000644005110600510130000000356613155516743017571 0ustar ecastroSwissProt SWISS::RCelement

Name

SWISS::RCelement.pm

Description

Each RCelement object represents one element of the RC line. The container object for all RCelements of an entry is SWISS::Ref.

Inherits from

SWISS::BaseClass

Attributes

text

The text of the keyword.

Standard methods

new
fromText
toText

Writing methods

cleanText

Remove potentially leading "and" from text.

Swissknife_1.75/docs/KW.html0000644005110600510130000000322513155516743016224 0ustar ecastroSwissProt SWISS::KW

Name

SWISS::KW

Description

Each KW object represents one keyword. The container object for all keywords of an entry is SWISS::KWs

Inherits from

SWISS::BaseClass

Attributes

text

The text of the keyword.

Methods

Standard methods

new
fromText
toText
Swissknife_1.75/docs/CCdisease.html0000644005110600510130000000633313155516743017531 0ustar ecastroSwissProt SWISS::CCdisease

Name

SWISS::CCdisease.pm

Description

SWISS::CCdisease represents a comment on the topic 'DISEASE' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information).

Collectively, comments of all types are stored within a SWISS::CCs container object.

Inherits from

SWISS::BaseClass.pm

Attributes

topic

The topic of this comment ('DISEASE').

disease

The name and evidence of the disease (only for new structured CC diseases) reference to an array [ $disease, $disease_ev ]

disease( [ $new_disease, $new_disease_ev ] )

Set disease to [ $new_disease, $new_disease_ev ]

mim

The disease mim id (only for new structured CC diseases)

mim( $new_mim )

Set mim to $new_mim

description

The disease description (only for new structured CC diseases)

note

The note and evidence of the disease (Note= in new CC disease format or full description in old format) reference to an array of [ $block_txt, $block_ev ] arrays

note( [[ $block_txt, $block_ev ]...] )

Set note to array of [ $block_txt, $block_ev ] arrays

comment

The "text" version of this comment.

Standard methods

new
fromText
toString

Returns a string representation of this comment.

Swissknife_1.75/docs/CCseq_caution.html0000644005110600510130000000400613155516743020421 0ustar ecastroSwissProt SWISS::CCseq_caution

Name

SWISS::CCinteraction

Description

SWISS::CCinteraction represents a comment on the topic 'INTERACTION' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information).

Collectively, comments of all types are stored within a SWISS::CCs container object.

Each element of the list is a hash with the following keys:

  accession
  identifier
  xeno
  NbExp
  IntAct      (array reference)

Inherits from

SWISS::ListBase.pm

Methods

Standard methods

new
fromText
toString

Returns a string representation of this comment.

Swissknife_1.75/docs/CCinteraction.html0000644005110600510130000000400613155516743020426 0ustar ecastroSwissProt SWISS::CCinteraction

Name

SWISS::CCinteraction

Description

SWISS::CCinteraction represents a comment on the topic 'INTERACTION' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information).

Collectively, comments of all types are stored within a SWISS::CCs container object.

Each element of the list is a hash with the following keys:

  accession
  identifier
  xeno
  NbExp
  IntAct      (array reference)

Inherits from

SWISS::ListBase.pm

Methods

Standard methods

new
fromText
toString

Returns a string representation of this comment.

Swissknife_1.75/docs/OX.html0000644005110600510130000000330213155516743016225 0ustar ecastroSwissProt SWISS::OX

Name

SWISS::OX

Description

SWISS::OX represents one tax id from the OX line. The container object holding all tax ids is SWISS::OXs.

Inherits from

SWISS::BaseClass.pm

Attributes

text

One tax id.

Standard methods

new
fromText
toText

Example

see documentation of OXs.pm

Swissknife_1.75/docs/OCs.html0000644005110600510130000000364713155516743016377 0ustar ecastroSwissProt SWISS::OCs

Name

SWISS::OCs

Description

SWISS::OCs represents the OC lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

Inherits from

SWISS::ListBase.pm

Attributes

list

Each list element is an item giving one part of the taxonomic classification of the source organism of the protein.

Methods

Standard methods

new
fromText
toText
sort
Swissknife_1.75/docs/CRC64.html0000644005110600510130000000533013155516743016463 0ustar ecastroSwissProt SWISS::CRC64

CRC64 perl module documentation

NAME

CRC64 - Calculate the cyclic redundancy check.

SYNOPSIS

   use SWISS::CRC64;
   
   $crc = SWISS::CRC64::crc64("IHATEMATH");
   #returns the string "E3DCADD69B01ADD1"
   ($crc_low, $crc_high) = SWISS::CRC64::crc64("IHATEMATH");
   #returns two 32-bit unsigned integers, 3822890454 and 2600578513

DESCRIPTION

SWISS-PROT + TREMBL use a 64-bit Cyclic Redundancy Check for the amino acid sequences.

The algorithm to compute the CRC is described in the ISO 3309 standard. The generator polynomial is x64 + x4 + x3 + x + 1. Reference: W. H. Press, S. A. Teukolsky, W. T. Vetterling, and B. P. Flannery, "Numerical recipes in C", 2nd ed., Cambridge University Press. Pages 896ff.

Functions

crc64 string

Calculate the CRC64 (cyclic redundancy checksum) for string.

In array context, returns two integers equal to the higher and lower 32 bits of the CRC64. In scalar context, returns a 16-character string containing the CRC64 in hexadecimal format.

AUTHOR

Alexandre Gattiker, gattiker@isb-sib.ch

ACKNOWLEDGEMENTS

Based on SPcrc, a C implementation by Christian Iseli, available at ftp://ftp.ebi.ac.uk/pub/software/swissprot/Swissknife/old/SPcrc.tar.gz

Swissknife_1.75/docs/ACs.html0000644005110600510130000000571713155516742016360 0ustar ecastroSwissProt SWISS::ACs

Name

SWISS::ACs

Description

SWISS::ACs represents the AC (accession) lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

The SWISS-PROT format has recently been changed to multiple AC lines. This module will read

 Ordinary AC lines
    AC   P10585;
 The old temporary format (for internal use only)
    AC   Q57333; O08291; O08202; O08292; O08203; O08293; O08204; O08294;
    **   O08205; O08295; O08206; O08296; O08207; O08297; O08208; O08298;
    **   O08213;
 and the new format.
    AC   Q57333; O08291; O08202; O08292; O08203; O08293; O08204; O08294;
    AC   O08205; O08295; O08206; O08296; O08207; O08297; O08208; O08298;
    AC   O08213;

But, SWISS::ACs will DROP funny ** comment lines that are sometimes found following an AC line:

    AC   Q48558; P71434;
    **   MERGED 2 TREMBL ENTRIES.

This module will always write the new format with multiple AC lines.

Inherits from

SWISS::ListBase.pm

Attributes

list

This is an array containing a list of all the accession numbers associated with this entry. The first member will be the primary accession number, and any following are the secondary accession numbers.

Methods

Standard methods

new
fromText
toText
sort

This method sorts the secondary AC numbers alphanumerically, i.e. all but the first. The primary AC number must never be sorted.

Swissknife_1.75/docs/Stars/0000755005110600510130000000000013155516744016110 5ustar ecastroSwissProtSwissknife_1.75/docs/Stars/EV.html0000644005110600510130000001011313155516744017304 0ustar ecastroSwissProt SWISS::Stars::EV

new

toText

sort

addEvidence( $evcode, $src, $author [, $date] )

 Title:    addEvidence
 Usage:    $evidenceTag = $entry->Stars->EV->addEvidence($evcode, 
                                                         $src, 
                                                         $author 
                                                         [, $date])
 Function: adds the evidence to the EV block if it does not yet exist 
           or returns the correct evidence tag if the evidence already exists, 
           possibly with a different date.
 Args:    $evcode: the evidence code. e.g. ECO:0000269
          $src:    the source. e.g. PubMed:11433298 
          $author: the author (initials). e.g. XXX p.s. For programs this could be '-'.
          $date: optional. If present, it must be in standard SWISS-PROT 
                 date format. If not present the current date will be used.
 Returns: The correct evidence tag.

updateEvidence( $evcode, $src, $author [, $date] )

 Title:    updateEvidence
 Usage:    $evidenceTag = $entry->Stars->EV->updateEvidence($evcode, 
                                                            $src, 
                                                            $author 
                                                            [, $date])
 Function: updates the evidence to the EV block to $date or inserts it 
           if it does not yet exist.
 Args:    $evcode: the evidence code. e.g. ECO:0000269
          $src:    the source. e.g. PubMed:11433298 
          $author: the author (initials). e.g. XXX p.s. For programs this could be '-'.
          $date: optional. If present, it must be in standard SWISS-PROT 
                 date format. If not present the current date will be used.
 Returns: The correct evidence tag.

Name

SWISS::Stars::EV.pm

Description

SWISS/Stars/EV.pm represents the evidence section within an SWISS-PROT + TrEMBL entry. See http://www3.ebi.ac.uk/~sp/intern/projects/evidenceTags/index.html

For a usage example, see evTest.pl in the Swissknife package.

Inherits from SWISS::ListBase.pm

Attributes

list Each element of the list describes one evidence, itself represented as an array.
Swissknife_1.75/docs/Stars/DR.html0000644005110600510130000000355713155516744017315 0ustar ecastroSwissProt SWISS::Stars::DR

Name

SWISS::default

Description

SWISS/Stars/DR.pm is the class to represent DR information in the "annotator's section" (internal section) within an SWISS-PROT + TrEMBL entry. The "annotator's section" is not visible to the public. The structured part has line tags of the form '**xx'. See also the general description in Stars.html.

Inherits from SWISS::ListBase.pm

Attributes

list Each line is stored as one element of the list.

Standard methods

new
fromText
toText
Swissknife_1.75/docs/Stars/aa.html0000644005110600510130000000354213155516744017363 0ustar ecastroSwissProt SWISS::Stars::aa

Name

SWISS::aa.pm

Description

SWISS/Stars/aa.pm represents the unstructured part of the "annotator's section" (source section) within an SWISS-PROT + TrEMBL entry. The "annotator's section" is not visible to the public. The unstructured part of it has the line tag '** '. See also the general description in Stars.html.

Inherits from SWISS::ListBase.pm

Attributes

list Each line is stored as one element of the list.

Standard methods

new
fromText
toText
Swissknife_1.75/docs/Stars/default.html0000644005110600510130000000356613155516744020434 0ustar ecastroSwissProt SWISS::Stars::default

Name

SWISS::default

Description

SWISS/Stars/default.pm is the default class to represent structured information in the "annotator's section" within an SWISS-PROT + TrEMBL entry. The "annotator's section" is not visible to the public. The structured part has line tags of the form '**xx'. See also the general description in Stars.html.

Inherits from SWISS::ListBase.pm

Attributes

list Each line is stored as one element of the list.

Standard methods

new
fromText
toText
Swissknife_1.75/docs/SKlogo.gif0000644005110600510130000002426507563750636016720 0ustar ecastroSwissProtGIF89ak{ZRc{sk{s{{!!!!9Js!))1!)!)!J))!)1)R){k)))1!1))1)19B191B91B1Z1k1{1119BB9J9c99B9BB9BBBsBJ))JB9JJJRJcJ{JRR!RJJRJRZcRcRkRRRRƭZZZcZZkkZkZZZcZcccccccƭkkB9kJRkZckcZkkskkkskkkƵk޵s!s!s1Bsksssֵ{!){s{{{{{{{{{{{{{ν{組!!{{Ƅֽ罌!)1BJRZkss{ƌƌƌƌƔƔΔΔΜƜ֜Μ֜ƥ))1ZcΥΥΥΥέ1BJRks֭֭έ֭֭֭ssε޵޵ֽֽƽ޽νƵ9JBRk{sΌΜνƽRkֽﵽ!,g H*\ȰÇ#JHŋ3jQ"duIɁʩg2u@}*w͛ ȱq2:H&#Ȃ*5JjոL IKUCʶCeBh(gu鶯_,ٳy~!qE$t^ĖYsD s ˈ*QϰMR 1IԖO%P_tw:jȩƈAh YKN r#9ѫ'/'.Օ_:u3IyWbzҡFy}|ץ0LBM9ds~*_) q{fe_a_4 0| -`|ha6ǎJšS&.x!KH+*܋YC"a!(SX_9͔~wxkyՓ띈YH%R0)| @ w /l# 3~O-oyI'w5&XdQ$B 1hS(|]3֔3^9bv"[ #LLAƴdL1J HAG-^X@焓Ml+# '{'O"̒NR믷1D: <H (NZZ;[d(COü (HtvJ"!w OKNQX1GvtXFԠDJKCd\L_ʤWr\ bij9dzr1Wo_o 5+p-NιcM-X84(w Sd[qO8hB%ՁA@ IGQ;0A !': NTd%0=9H!D ƅ @t(&͋b& P Ʊ'̀!AL īT =laTB#x%1 h <#(&AL(F1; VVD<@X* 5v8tH 4$4GIaG)H.e"d}"䠊D 1DiH9vAg}BEZ<Ua,u" -SwAQ* 'utPD(# a"RaQUGα@m\A<Uuey: )Um!`|D+r,G(U lI^@j,#NL}U-Ya _-5ưjƫ#mF%@`bMA0 bӔeB 0C++FQY@֐E#Ȗ2HVf s6r3[ Rk `Xnd>xUPD@#=:^'%+@žɹB:]|W@NQuPNg9 ToD%A8@5"@ aEFtc?,`u De6I|%Y쐞)- kq`=Z+w9,Q?Z8@t9zL\KԷ92C+.A ;vdZ>!JvTIe]Wp H +z"dY"hl 4XYW0 .ܓ(0o#]{H.1iDH) Q9We ($ aNZtQ^AH~hgkGtXc NtI·4b_A joY_+ D39^btRG$dv`TPHC,:Io B[ G\^o/%zG=?}EoM4PJ`)hvqzk$}7ZQ#dCPH0zT 7`zLJ|j'G6` G(AfB5S<>12 1yB x=n%w RoTnd ` geS> 4G5#?b1< hTOw2;B48I| K2(@f"Ɠ"R ^rS- 0(KY6G JgRO{Gjrї:֠D~#VGOh +A?=3ϑ{QI@  @)pFcs*;d` t@Ga|s qkO?P5U:D5f`PvpDH;;Ph$xOhWb A_cq'gIs9c u86NE@QuuW`4 2H P4 b*b@$P(O& 8؈ A)($%]s{qFDF0$͠nW0F+Fkȷ H0 @GZB ؍ QbhS ϱ ʒ!,,DA\H p5WL qk%%"$%d 'ǃp&P *+2eVv nfYHųlr@ 'R@)\\{8TI%RP. 68xBehttP& a &S.i2z0` )mUtyF&w!br:`9 8 ich9t!r}CsE d1+0|U8nGaslb&4 j[0asWWx2aeH3!h@" _ 2&3B G5`.吢i&cOGcӌ@n0fWP.nRPRi!U 2 whtd0OA.SY{8GrTnSCv`,_0@$m?!_ ?0$*|tȤ6{QQ.z+m=s rI?+3on%d'('p2:)@ P&S&H H pwUQڂ]F03٦D7` " Fy#$.'3  a7 @nISiaDq ncpxCIV!4yE3 Kh&Z*(@K33{pM @g&ϚMH&Q+r*bv@sg!o@kJy@G  c@(h!z2F.JsKPwbnZet6!`-{k (,$1$RLuYh 0!QGi~丳@3D@7ẏҔ~y]9GP q]GZ/lzË}2g 1 #pvPݒ݁{ApIy_z^)9nr05L¶Gi m2l8րb ۹! EGEvao3VFy ϐ+WȺa  $suTZx \R (fB;A%d F  )5$t@\ vp0琨لeț'DN[xbpC!Pg@vpv< p] D/W>Fy'dH,7!`j)pw W{p`: !5 6J`+N:5㾒teh4R W |3r΁{.֠ɳ%Z Nrb hF  '@qġjP !q #4=HGq'_~@^GUw Q*P$q$@ d |{v(H k4Z©K q԰R|h*qmm> ^G:Mڐk͇8H,tаO%zp z,4`TnOeIk䌧Ԋa }ӭ `(!߃?jJ$g(d cF }7+f0č\7\zk|<@ ֠ p`  00bݴfiy J zfu0 zڝһЊ }]yW 4|00"4$\NZY`|9 а:* +JQp.H͡YQ b  uY-`Y1٢@;y]7P}I8<-?X2E0\nh [ 7^ q`O8VEm]˽|ٗhW4x 0 ڃc˦lKe@wkL뺾0&u"= ،+I!pDk.sTx pA\7=Dcxn<}2 PZd@IT"0 VZ슡dn%5y_ P^|apWpA)a\ji̦fa7 zw0 Q6 ooU^K0"JJO^]g}6 5YG9.I&R sS^ p@ p 0ߊyX"50לz>^q"@ >㫘US&9_K2:GBEb^QBB"%& @_:OՅBuGi/I`w`*`;x$idBb~F4 0?3J,Ta |ba0 Vsd9:G@=ZUdr :tͤ s2-u2 Gf$A5IԹ\iS#"\]R`!Ǣ5%ņ;2?meyN L5g޼Ö.1B:uxZةT #%ͦUl4ңɎ$?h3]cnt͜tGQQKjF ܹu=ꌤhHA،k.ԜYOrTۭ%NL\PJױ'!ٕT oSu#_h29=($Ɏ\Sb%(Ekҳ.XρI :"*/A⎚PED*ʚ` rH!w0hpPJ39Ɩ&"&2Lb C~⤖tG"l8\%tfS4`:,@r2˕I2Yaml!tsS!7\ j-Rɋ;+ŲPHD j #LDw(4ZZ 5Xd5Ȁ%!t` 2PDb}h<2VEY83Z&YaƕQAYz-6 `:Y<$dCIHmWuNJD1t⤆G#F2'F,cCydA}X`PQsфTQ$t?A@/bC7k!a\ iAN}S^`·91m$" nn]Y !n{$zx 3 8!V6I )e; VD;4yVK7]!p !j&xj1")̾C`0: ($X:}yWw>Ek=[NTt( &.&!j]v$}~/A硧!`'!la! @a`l? _`PCyQB-xA f0["p;=@CۈD.fAW%oyNjA,´S+^.S6f pV!A 0A>&>0`0l݇X\ %1qW bĺH (I>-ȼ9]hRh[{Г8@=.k>-a pAP+8>@ @Ái@]H'0M< @H@ ?c.l ??p?={4[ [B8-[Ѕi؄S'ֹ0D]Gܲ`-0B0.p>CB(>E؂Q$0>Bnp* GX h.>;A>4FdCH+^gDHT>\ܲ pd4pjix; +'x IJOȦ8H @yJ#06I=pABS?\j$ÿʰ$ǮʰO@_HK%kIz܉ 5KkCaLƽdM;$j>Y8ߔ! G=8MT_S@̵T2܉Sܲ F4ִJ8Jp'F2^І֬ \`\έ!XTNOtIGόߓFI#F?lPs mpKaP4X묻$\HbP#SbHhGC>[;_$~Awds'uRsRh ?h'ՆpRm+݌bhXr\%[1bp1%2%ǫ\buA&RARmR+A%TAݸ09J 5e675npT3J%=耖:}44xxЪKUtspX@>\ZhU0nXVq0rtmT*PejmVrqT] ÿ 9628{9LF=pXMY4w wp{ ]|W\Psٹ%JhVtX֔@qʭX?]v.jz%Y>0'._KpA\̀HS0\ɏhceCX!<h֭DA 3(PW%S`TP;XRL?E`Ws.胕 CKA>胆ȵ;#4t\LP *ݭ(}˅P \LOY8а~yCK-s]= ^@ĥ&=t\ȅ+K_0؆'[ŨE WmX0Ѽ'ֲ5;U4> 5G ps< ؄(%s 7A\8A_)9Pa#;||t . `,Ye6b(V!N"nX3G@H_1c2.c36()n0"v Yy ѵ\<45^2"U^ct<^́=n<YpPMxxDfdOn(G*%8e!baXrm@zOee]e^e_e`fafb.fcά;Swissknife_1.75/docs/Journal.html0000644005110600510130000000077513155516743017324 0ustar ecastroSwissProt SWISS::Journal

Swissknife_1.75/docs/DTs.html0000644005110600510130000000764313155516743016405 0ustar ecastroSwissProt SWISS::DTs

Name

SWISS::DTs

Description

SWISS::DTs represents the DT lines within an Swiss-Prot + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

Inherits from

SWISS::BaseClass.pm

Attributes

CREATED_date

Creation date

ANN_date

Last annotation update

SQ_date

Last Sequence update

CREATED_rel

Created for release

ANN_rel

Last annotation for release

SQ_rel

Last sequence update for release

ANN_version

Version number for entry annotation

SQ_version

Version number for sequence

Methods

Standard methods

new
fromText
toText
sort

Writing methods

set_Created ($date, $release)
set_AnnotationUpdate ($date, $release[, $version])
set_SequenceUpdate ($date, $release[, $version])

TRANSITION

The format of the DT line will change in early 2004 from:

 DT   01-JUL-1993 (Rel. 26, Created)
 DT   01-JUL-1993 (Rel. 26, Last sequence update)
 DT   28-FEB-2003 (Rel. 41, Last annotation update)

to:

 DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
 DT   01-JUL-1993, sequence version 36.
 DT   28-FEB-2003, entry version 54.

This module supports both formats. To convert an entry from the old to the new format, do:

 $entry->DTs->CREATED_rel("UniProtKB/Swiss-Prot");
 $entry->DTs->ANN_version(54);
 $entry->DTs->SQ_version(36);
Swissknife_1.75/docs/IDs.html0000644005110600510130000000514613155516743016366 0ustar ecastroSwissProt SWISS::IDs

Name

SWISS::IDs.pm

Description

SWISS::IDs represents the ID lines of a SWISS-PROT + TREMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

Inherits from

SWISS::ListBase.pm

Attributes

list

This is an array containing a list of all the IDs associated with this entry. The first member will be the primary ID, and any following are the secondary IDs which are not shown in the public section of the entry.

dataClass

The data class, either STANDARD or PRELIMINARY for data from releases prior to 9.0, or Reviewed or Unreviewed for data from later releases.

moleculeType

The molecule type, currently only PRT.

length

The protein length in amino acids.

Methods

Standard methods

new
fromText
toText
sort

IDs must never be sorted, so this method does nothing (but it overwrites the inherited method).

Swissknife_1.75/docs/OGs.html0000644005110600510130000000342213155516743016372 0ustar ecastroSwissProt SWISS::OGs

Name

SWISS::OGs

Description

SWISS::OGs represents the OG lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OGs object is a container object which holds a list of SWISS::OG objects.

Inherits from

SWISS::ListBase.pm

Attributes

list
  Each list element is a SWISS::OG object.

Standard methods

new
fromText
toText
Swissknife_1.75/docs/CCbpc_properties.html0000644005110600510130000000504413155516742021131 0ustar ecastroSwissProt SWISS::CCbpc_properties

Name

SWISS::CCbpc_properties.pm

Description

SWISS::CCbpc_properties represents a comment on the topic 'BIOPHYSICOCHEMICAL PROPERTIES' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information).

Collectively, comments of all types are stored within a SWISS::CCs container object.

Inherits from

SWISS::BaseClass.pm

Attributes

topic

The topic of this comment ('BIOPHYSICOCHEMICAL PROPERTIES').

properties

A list of all filled properties in this comment.

fields($properties)

A list of "records" for a given property (e.g. "Absorption") in this comment. Each "record" is a reference to an array of [$field_name, [[$sentence, $evidence_tags]] ]. $field is undefined for unnamed fields.

Standard methods

new
fromText
toString

Returns a string representation of this comment.

Swissknife_1.75/docs/CCalt_prod.html0000644005110600510130000004016713155516742017722 0ustar ecastroSwissProt SWISS::CCalt_prod

Name

SWISS::CCalt_prod.pm

Description

SWISS::CCalt_prod represents a comment on the topic 'ALTERNATIVE PRODUCTS' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information).

Collectively, comments of all types are stored within a SWISS::CCs container object.

Code example:

This example is given to illustrate the internal construction of an CCalt_prod object. However, for most purposes it should be possible to use the convenience methods provided (e.g. the add, delete, get and set methods doocumented below) instead of constructing the section manually. The use of the convenience methods is also recommended to ensure the structual integrity of the CCalt_prod object.

 ## Create a new named isoform
 
 my %thisFormHash;
 
 ## give this some properties
 
 # some properties are single data values
 
 $thisFormHash{"Name"} = "This";
 
 # some properties are lists of values
  
 push @{$thisFormHash{"Synonyms"}}, "That";
 push @{$thisFormHash{"Synonyms"}}, "The Other";
 push @{$thisFormHash{"IsoId"}}, "P00000-01";
 push @{$thisFormHash{"IsoId"}}, "P00000-02";
 push @{$thisFormHash{"Sequence"}}, "VSP_000001";
 push @{$thisFormHash{"Sequence"}}, "VSP_000002";
 $thisFormHash{"Notes"} = [ [ "this local note", "ECO:0000269|PubMed:22081402, ECO:0000269|PubMed:23203051" ] ];
 $thisFormHash{"Notes"} = [ [ "another local note without ev", "" ] ];
 $thisFormHash{"Notes"} = [ [ "note block1", "ECO:0000269|PubMed:22081402" ], [ "note block2", "ECO:0000269|PubMed:23203051" ] ];
  
 ## put this form onto a list of all forms created by one type of event
 
 my @newFormsList;
 
 push @newFormsList, \%thisFormHash;
 
 ## put this list into a hash describing all characteristics of this event
 
 my %eventHash;
 $eventHash{"FormsList"} = \@newFormsList;
 
 ## set other values of this event
 
 $eventHash{"Comment"} = [ [ "This Comment", "ECO:0000269|PubMed:23203051" ] ];
 
 ## put the description of this event into a hash descrinbing all events
 
 my %eventsHash;
 $eventsHash{"Alternative splicing"} = \%eventHash;
 
 ## put a reference to this hash into the CCalt_products object
 
 my $hashRef;
 $hashRef = \%eventsHash;
 my $newCC = SWISS::CCalt_prod;
 $newCC->setEvents($hashRef);
 $newCC->toString();

More simply, using the convenience methods addComment and addForm:


 @synonyms = ("That", "The other");
 @isoIds = ("P00000-1", "P00000-2");
 @featIds = ("VSP_00001", "VSP_00002");
 my $newCC = SWISS::CCalt_prod;
 $newCC -> addComment("Alternative splicing", "This comment");
 $newCC -> addForm("Alternative splicing", 
                   "This", 
                   \@synonyms, 
                   \@isoIds, 
                   \@featIds,
                   [ [ "This local note", "ECO:0000269|PubMed:22081402, ECO:0000269|PubMed:23203051" ] ]);
 print $newCC -> toString();

Output from both approaches:

 CC   -!- ALTERNATIVE PRODUCTS:
 CC        Event=Alternative splicing; Named isoforms=1;
 CC          Comment=This comment.
 CC        Name=This; Synonyms=That, The other;
 CC          IsoId=P00000-1, P00000-2; Sequence=VSP_00001, VSP_00002;
 CC          Note=This local note.
 CC          {ECO:0000269|PubMed:22081402, ECO:0000269|PubMed:23203051};

Example of adding evidence tags to a synonym:

$CC -> addEvidenceTag('EP8', "Alternative splicing", "Synonyms", "VI", "B");

to add the tag 'EP8' to synonym B of isoform VI, produced by alternative splicing

Handling mutliple events:

With the release of UniProt 8.0, the format of the CC ALTERNATIVE PRODUCTS blocks has changed slightly. In particular, isoforms are no longer stored according to the events that have generated them, so this:

 CC   -!- ALTERNATIVE PRODUCTS:
 CC        Event=Alternative splicing; Named isoforms=1;
 CC          Comment=This comment.
 CC        Name=This; Synonyms=That, The other;
 CC          IsoId=P00000-1, P00000-2; Sequence=VSP_00001, VSP_00002;
 CC          Note=This local note.
 CC        Event=Alternative initiation;
 CC          Comment=Another comment.

has become this:

 CC   -!- ALTERNATIVE PRODUCTS:
 CC        Event=Alternative splicing, Alternative initation; Named isoforms=1;
 CC          Comment=This comment. Another comment;
 CC        Name=This; Synonyms=That, The other;
 CC          IsoId=P00000-1, P00000-2; Sequence=VSP_00001, VSP_00002;
 CC          Note=Produced by alternative splicing. This local note;
 
The API is quite event-centric, reflecting the previous file format (where
different content was available according to the event type).  To get all
isoforms (for whatever events are annotated) under the new format, do:
 $CC->keyEvent;
 
which will return an arbitrary event that can be used a parameter in other
methods.  Any of the events annotated will function as parameters to retrieve
information about assocaticated isoforms: it is not necessary to supply the
complete list.
 
=head1 Inherits from

SWISS::BaseClass.pm

Attributes

topic

The topic of this comment ('ALTERNATIVE PRODUCTS').

Standard methods

new
fromText

Reading/Writing methods

addEvent ($eventName)

Allows the user to insert "events blocks" into the CCalt_prod object.

addEvidenceTag($tag, $event, $type, $name, $synonym)

Add $tag to the tag list associated with the specified component of a CCalt_prod object. The event and type (of the item to which the tag is to be added, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform to which the tag is being attached); the name of the synonym to which the tag are being attached must also be given if the type is "Synonyms". n.b. now Comment and Note are "multi block" ( [ [ blocktext, blockevs ]... ] , so here the ev tag will be added on last the 'block'; it would be better to directly manipulate this [ [ blocktxt, blockevs ] ... ] structure obtained via getComment/Note

addForm ($eventName, $formName, \@synonyms, \@isoIds, \@featIds, $note)

Allows the user to add a form into a given event block. See code example (above) for more details.

deleteComment ($eventName)

Deletes the comment associated with this event.

deleteEvent ($eventName)

Deletes an event from this CCalt_prod objects.

deleteEvidenceTag($tag, $event, $type, $name, $synonym)

Deletes $tag from the tag list associated with the specified component of a CCalt_prod object. The event and type (of the item from which the tag is to be deleted, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform from which the tag is being deleted); the name of the synonym from which the tag is being deleted must also be given if the type is "Synonyms".

deleteForm ($eventName, $formName)

Deletes a form associated with a given event.

keyEvent ()

Extracts one of the events annotated in this entry, which can then be used to retrieve data associated with this event

getComment($eventName)

Returns the comment for this event.

getEventNames

Returns a list of all event names for this CCalt_prod object.

getEvidenceTags($event, $type, $name, $synonym)

Returns a list of the tags attached to the specified component of a CCalt_prod object. The event and type (of the item to which the tag is attached, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform whose tags are being fetched); the name of the synonym whose tags are being fetched must also be given if the type is "Synonyms". n.b. now Comment and Note are "multi block" ( [ [ blocktext, blockevs ]... ] , so here all the evidences from all the block are pooled together

getEvidenceTagsString($event, $type, $name, $synonym)

Returns the tags attached to the specified component of a CCalt_prod object as a string literal. The event and type (of the item to which the tag is attached, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform whose tags are being fetched); the name of the synonym whose tags are being fetched must also be given if the type is "Synonyms". n.b. now Comment and Note are "multi block" ( [ [ blocktext, blockevs ]... ] , so here all the evidences from all the block are pooled together

getFeatIds ($eventName, $formName)

Returns a list of all feature IDs associated with this form produced by this event.

getFormNames ($eventName)

Returns a list of all form names for this form produced by this event.

getIsoIds ($eventName, $formName)

Returns a list of all IsoIds for this form produced by this event.

getNamedFormCount($eventName)

Returns the number of named and identified forms for this event.

getNote ($eventName, $formName)

Returns the local note of this form produced by this event.

getSynonyms ($eventName, $formName)

Returns a list of all synonyms of this form produced by this event.

hasEvidenceTag ($tag, $event, $type, $name, $synonym)

Returns 1 if the specified component of a CCalt_prod object has the specified tag. The event and type (of the item to which the tag is attached, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform whose tags are being fetched); the name of the synonym whose tags are being fetched must also be given if the type is "Synonyms".

setComment ($eventName, $comment)
  Allows the user to add a global comment for a particular event.
setEvidenceTags(\@tags, $event, $type, $name, $synonym)

Sets the evidence tags of the specified component of a CCalt_prod object to the array pointed to by \@tags. The event and type (of the item to which the tag are to be added, i.e. "Comment", "Name", "Note", or "Synonyms") must always be specified: unless the type is "Comment", the name must also be specifed (i.e. the contents of the Name field for the isoform to which tags are being attached); the name of the synonym to which tags are being attached must also be given if the type is "Synonyms". n.b. now Comment and Note are "multi block" ( [ [ blocktext, blockevs ]... ] , so here the ev tag will be set on last the 'block'; it would be better to directly manipulate this [ [ blocktxt, blockevs ] ... ] structure obtained via getComment/Note

setEvent (%eventHash)

Can be used to manually insert a hash representing one event. Use of this method is not recommeded, see code examples for how to use the convenience methods to create a CCalt_prod object.

setFeatIds($eventName, $oldName, \@featIds)

Sets the feature Ids for the named form (associated with the specified event) to the supplied list.

setFormName($eventName, $oldName, $newName)

Changes the name of the formed named $OldName, associated with this event, to the $newName.

setIsoIds($eventName, $oldName, \@isoIds)

Sets the Isoform Ids for the named form (associated with the specified event) to the supplied list.

setNote($eventName, $name, $note)

Sets the local note for the named form (associated with the specified event).

setSynonyms($eventName, $name, \@synonyms)

Sets the synonyms for the named form (associated with the specified event) to the supplied list.

toString

Returns a string representation of this comment.

Swissknife_1.75/docs/OG.html0000644005110600510130000000364213155516743016213 0ustar ecastroSwissProt SWISS::OG

Name

SWISS::OGs

Description

SWISS::OG represents one organelle or plasmid name from the OG line. The container object holding all organelle or plasmid names is SWISS::OGs.

Inherits from

SWISS::BaseClass.pm

Attributes

text

One OG line element.

Methods

Standard methods

new
fromText
toText

Specific methods

isPlasmid
Swissknife_1.75/docs/DRs.html0000644005110600510130000000765113155516743016402 0ustar ecastroSwissProt SWISS::DRs

Name

SWISS::DRs

Description

SWISS::DRs represents the DR (database crossreference) lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

Inherits from

SWISS::ListBase.pm

Attributes

list

An array of arrays. Each element is an array (Database_identifier, primary_key, secondary_key[,further elements]).

Methods

Standard methods

new
fromText
toText
sort

Reading methods

emblacs

Returns a list of all EMBL accession numbers. These are the primary keys of EMBL crossreferences.

pids [$dropVersion]

Returns a list of all PIDs. These are the secondary keys of EMBL crossreferences.

ATTENTION: The EMBL protein identifiers introduced in 1999 are of the form xxxxx.yy, e.g. CAA33128.1 If $dropVersion is set, the version number (.yy) will be dropped from each PID.

Example:

If the EMBL DR line is

DR EMBL; L37685; AAC41668.1; -.

pids(1) will only return AAC41668, NOT AAC41668.1

Filter functions

dbName($dbTargetName)

True if the first element of a DR line (the DB name) matches $dbTargetName. $dbTargetName has to match in full, not only a partial match.

notDbName($dbTargetName)

True if the first element of a DR line (the DB name) does NOT macht $dbTargetName.

** lines (SWISS-PROT internal format)

Each DR line may be followed by a ** line like

 **   DR   PROSITE; PS12345; XXX_PAT; FALSE_POS_1


 These will be stored internally as DR lines with the DB identifier 
 '_HIDDEN_'. Therefore adding a ** PROSITE line is done as:


 $entry->DRs->add(['_HIDDEN_', 'PS12345', 'XXX_PAT', 'FALSE_POS_1']);
Swissknife_1.75/docs/Refs.html0000644005110600510130000000351313155516743016602 0ustar ecastroSwissProt SWISS::Refs

Name

SWISS::Refs.pm

Description

SWISS::Refs represents the Reference lines within an SWISS-PROT + TREMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html .

Inherits from

SWISS::ListBase.pm

Attributes

list
  A list of SWISS::Ref objects. Each object represents one reference.

Methods

Standard methods

new
fromText
toText
Swissknife_1.75/COPYING0000644005110600510130000004312707323534077015125 0ustar ecastroSwissProt GNU GENERAL PUBLIC LICENSE Version 2, June 1991 Copyright (C) 1989, 1991 Free Software Foundation, Inc. 59 Temple Place, Suite 330, Boston, MA 02111-1307 USA Everyone is permitted to copy and distribute verbatim copies of this license document, but changing it is not allowed. Preamble The licenses for most software are designed to take away your freedom to share and change it. By contrast, the GNU General Public License is intended to guarantee your freedom to share and change free software--to make sure the software is free for all its users. This General Public License applies to most of the Free Software Foundation's software and to any other program whose authors commit to using it. (Some other Free Software Foundation software is covered by the GNU Library General Public License instead.) You can apply it to your programs, too. When we speak of free software, we are referring to freedom, not price. Our General Public Licenses are designed to make sure that you have the freedom to distribute copies of free software (and charge for this service if you wish), that you receive source code or can get it if you want it, that you can change the software or use pieces of it in new free programs; and that you know you can do these things. To protect your rights, we need to make restrictions that forbid anyone to deny you these rights or to ask you to surrender the rights. These restrictions translate to certain responsibilities for you if you distribute copies of the software, or if you modify it. For example, if you distribute copies of such a program, whether gratis or for a fee, you must give the recipients all the rights that you have. You must make sure that they, too, receive or can get the source code. And you must show them these terms so they know their rights. We protect your rights with two steps: (1) copyright the software, and (2) offer you this license which gives you legal permission to copy, distribute and/or modify the software. Also, for each author's protection and ours, we want to make certain that everyone understands that there is no warranty for this free software. If the software is modified by someone else and passed on, we want its recipients to know that what they have is not the original, so that any problems introduced by others will not reflect on the original authors' reputations. Finally, any free program is threatened constantly by software patents. We wish to avoid the danger that redistributors of a free program will individually obtain patent licenses, in effect making the program proprietary. To prevent this, we have made it clear that any patent must be licensed for everyone's free use or not licensed at all. The precise terms and conditions for copying, distribution and modification follow. GNU GENERAL PUBLIC LICENSE TERMS AND CONDITIONS FOR COPYING, DISTRIBUTION AND MODIFICATION 0. This License applies to any program or other work which contains a notice placed by the copyright holder saying it may be distributed under the terms of this General Public License. The "Program", below, refers to any such program or work, and a "work based on the Program" means either the Program or any derivative work under copyright law: that is to say, a work containing the Program or a portion of it, either verbatim or with modifications and/or translated into another language. (Hereinafter, translation is included without limitation in the term "modification".) Each licensee is addressed as "you". Activities other than copying, distribution and modification are not covered by this License; they are outside its scope. The act of running the Program is not restricted, and the output from the Program is covered only if its contents constitute a work based on the Program (independent of having been made by running the Program). Whether that is true depends on what the Program does. 1. You may copy and distribute verbatim copies of the Program's source code as you receive it, in any medium, provided that you conspicuously and appropriately publish on each copy an appropriate copyright notice and disclaimer of warranty; keep intact all the notices that refer to this License and to the absence of any warranty; and give any other recipients of the Program a copy of this License along with the Program. You may charge a fee for the physical act of transferring a copy, and you may at your option offer warranty protection in exchange for a fee. 2. You may modify your copy or copies of the Program or any portion of it, thus forming a work based on the Program, and copy and distribute such modifications or work under the terms of Section 1 above, provided that you also meet all of these conditions: a) You must cause the modified files to carry prominent notices stating that you changed the files and the date of any change. b) You must cause any work that you distribute or publish, that in whole or in part contains or is derived from the Program or any part thereof, to be licensed as a whole at no charge to all third parties under the terms of this License. c) If the modified program normally reads commands interactively when run, you must cause it, when started running for such interactive use in the most ordinary way, to print or display an announcement including an appropriate copyright notice and a notice that there is no warranty (or else, saying that you provide a warranty) and that users may redistribute the program under these conditions, and telling the user how to view a copy of this License. (Exception: if the Program itself is interactive but does not normally print such an announcement, your work based on the Program is not required to print an announcement.) These requirements apply to the modified work as a whole. If identifiable sections of that work are not derived from the Program, and can be reasonably considered independent and separate works in themselves, then this License, and its terms, do not apply to those sections when you distribute them as separate works. But when you distribute the same sections as part of a whole which is a work based on the Program, the distribution of the whole must be on the terms of this License, whose permissions for other licensees extend to the entire whole, and thus to each and every part regardless of who wrote it. Thus, it is not the intent of this section to claim rights or contest your rights to work written entirely by you; rather, the intent is to exercise the right to control the distribution of derivative or collective works based on the Program. In addition, mere aggregation of another work not based on the Program with the Program (or with a work based on the Program) on a volume of a storage or distribution medium does not bring the other work under the scope of this License. 3. You may copy and distribute the Program (or a work based on it, under Section 2) in object code or executable form under the terms of Sections 1 and 2 above provided that you also do one of the following: a) Accompany it with the complete corresponding machine-readable source code, which must be distributed under the terms of Sections 1 and 2 above on a medium customarily used for software interchange; or, b) Accompany it with a written offer, valid for at least three years, to give any third party, for a charge no more than your cost of physically performing source distribution, a complete machine-readable copy of the corresponding source code, to be distributed under the terms of Sections 1 and 2 above on a medium customarily used for software interchange; or, c) Accompany it with the information you received as to the offer to distribute corresponding source code. (This alternative is allowed only for noncommercial distribution and only if you received the program in object code or executable form with such an offer, in accord with Subsection b above.) The source code for a work means the preferred form of the work for making modifications to it. For an executable work, complete source code means all the source code for all modules it contains, plus any associated interface definition files, plus the scripts used to control compilation and installation of the executable. However, as a special exception, the source code distributed need not include anything that is normally distributed (in either source or binary form) with the major components (compiler, kernel, and so on) of the operating system on which the executable runs, unless that component itself accompanies the executable. If distribution of executable or object code is made by offering access to copy from a designated place, then offering equivalent access to copy the source code from the same place counts as distribution of the source code, even though third parties are not compelled to copy the source along with the object code. 4. You may not copy, modify, sublicense, or distribute the Program except as expressly provided under this License. Any attempt otherwise to copy, modify, sublicense or distribute the Program is void, and will automatically terminate your rights under this License. However, parties who have received copies, or rights, from you under this License will not have their licenses terminated so long as such parties remain in full compliance. 5. You are not required to accept this License, since you have not signed it. However, nothing else grants you permission to modify or distribute the Program or its derivative works. These actions are prohibited by law if you do not accept this License. Therefore, by modifying or distributing the Program (or any work based on the Program), you indicate your acceptance of this License to do so, and all its terms and conditions for copying, distributing or modifying the Program or works based on it. 6. Each time you redistribute the Program (or any work based on the Program), the recipient automatically receives a license from the original licensor to copy, distribute or modify the Program subject to these terms and conditions. You may not impose any further restrictions on the recipients' exercise of the rights granted herein. You are not responsible for enforcing compliance by third parties to this License. 7. If, as a consequence of a court judgment or allegation of patent infringement or for any other reason (not limited to patent issues), conditions are imposed on you (whether by court order, agreement or otherwise) that contradict the conditions of this License, they do not excuse you from the conditions of this License. If you cannot distribute so as to satisfy simultaneously your obligations under this License and any other pertinent obligations, then as a consequence you may not distribute the Program at all. For example, if a patent license would not permit royalty-free redistribution of the Program by all those who receive copies directly or indirectly through you, then the only way you could satisfy both it and this License would be to refrain entirely from distribution of the Program. If any portion of this section is held invalid or unenforceable under any particular circumstance, the balance of the section is intended to apply and the section as a whole is intended to apply in other circumstances. It is not the purpose of this section to induce you to infringe any patents or other property right claims or to contest validity of any such claims; this section has the sole purpose of protecting the integrity of the free software distribution system, which is implemented by public license practices. Many people have made generous contributions to the wide range of software distributed through that system in reliance on consistent application of that system; it is up to the author/donor to decide if he or she is willing to distribute software through any other system and a licensee cannot impose that choice. This section is intended to make thoroughly clear what is believed to be a consequence of the rest of this License. 8. If the distribution and/or use of the Program is restricted in certain countries either by patents or by copyrighted interfaces, the original copyright holder who places the Program under this License may add an explicit geographical distribution limitation excluding those countries, so that distribution is permitted only in or among countries not thus excluded. In such case, this License incorporates the limitation as if written in the body of this License. 9. The Free Software Foundation may publish revised and/or new versions of the General Public License from time to time. Such new versions will be similar in spirit to the present version, but may differ in detail to address new problems or concerns. Each version is given a distinguishing version number. If the Program specifies a version number of this License which applies to it and "any later version", you have the option of following the terms and conditions either of that version or of any later version published by the Free Software Foundation. If the Program does not specify a version number of this License, you may choose any version ever published by the Free Software Foundation. 10. If you wish to incorporate parts of the Program into other free programs whose distribution conditions are different, write to the author to ask for permission. For software which is copyrighted by the Free Software Foundation, write to the Free Software Foundation; we sometimes make exceptions for this. Our decision will be guided by the two goals of preserving the free status of all derivatives of our free software and of promoting the sharing and reuse of software generally. NO WARRANTY 11. BECAUSE THE PROGRAM IS LICENSED FREE OF CHARGE, THERE IS NO WARRANTY FOR THE PROGRAM, TO THE EXTENT PERMITTED BY APPLICABLE LAW. EXCEPT WHEN OTHERWISE STATED IN WRITING THE COPYRIGHT HOLDERS AND/OR OTHER PARTIES PROVIDE THE PROGRAM "AS IS" WITHOUT WARRANTY OF ANY KIND, EITHER EXPRESSED OR IMPLIED, INCLUDING, BUT NOT LIMITED TO, THE IMPLIED WARRANTIES OF MERCHANTABILITY AND FITNESS FOR A PARTICULAR PURPOSE. THE ENTIRE RISK AS TO THE QUALITY AND PERFORMANCE OF THE PROGRAM IS WITH YOU. SHOULD THE PROGRAM PROVE DEFECTIVE, YOU ASSUME THE COST OF ALL NECESSARY SERVICING, REPAIR OR CORRECTION. 12. IN NO EVENT UNLESS REQUIRED BY APPLICABLE LAW OR AGREED TO IN WRITING WILL ANY COPYRIGHT HOLDER, OR ANY OTHER PARTY WHO MAY MODIFY AND/OR REDISTRIBUTE THE PROGRAM AS PERMITTED ABOVE, BE LIABLE TO YOU FOR DAMAGES, INCLUDING ANY GENERAL, SPECIAL, INCIDENTAL OR CONSEQUENTIAL DAMAGES ARISING OUT OF THE USE OR INABILITY TO USE THE PROGRAM (INCLUDING BUT NOT LIMITED TO LOSS OF DATA OR DATA BEING RENDERED INACCURATE OR LOSSES SUSTAINED BY YOU OR THIRD PARTIES OR A FAILURE OF THE PROGRAM TO OPERATE WITH ANY OTHER PROGRAMS), EVEN IF SUCH HOLDER OR OTHER PARTY HAS BEEN ADVISED OF THE POSSIBILITY OF SUCH DAMAGES. END OF TERMS AND CONDITIONS How to Apply These Terms to Your New Programs If you develop a new program, and you want it to be of the greatest possible use to the public, the best way to achieve this is to make it free software which everyone can redistribute and change under these terms. To do so, attach the following notices to the program. It is safest to attach them to the start of each source file to most effectively convey the exclusion of warranty; and each file should have at least the "copyright" line and a pointer to where the full notice is found. Copyright (C) 19yy This program is free software; you can redistribute it and/or modify it under the terms of the GNU General Public License as published by the Free Software Foundation; either version 2 of the License, or (at your option) any later version. This program is distributed in the hope that it will be useful, but WITHOUT ANY WARRANTY; without even the implied warranty of MERCHANTABILITY or FITNESS FOR A PARTICULAR PURPOSE. See the GNU General Public License for more details. You should have received a copy of the GNU General Public License along with this program; if not, write to the Free Software Foundation, Inc., 59 Temple Place, Suite 330, Boston, MA 02111-1307 USA Also add information on how to contact you by electronic and paper mail. If the program is interactive, make it output a short notice like this when it starts in an interactive mode: Gnomovision version 69, Copyright (C) 19yy name of author Gnomovision comes with ABSOLUTELY NO WARRANTY; for details type `show w'. This is free software, and you are welcome to redistribute it under certain conditions; type `show c' for details. The hypothetical commands `show w' and `show c' should show the appropriate parts of the General Public License. Of course, the commands you use may be called something other than `show w' and `show c'; they could even be mouse-clicks or menu items--whatever suits your program. You should also get your employer (if you work as a programmer) or your school, if any, to sign a "copyright disclaimer" for the program, if necessary. Here is a sample; alter the names: Yoyodyne, Inc., hereby disclaims all copyright interest in the program `Gnomovision' (which makes passes at compilers) written by James Hacker. , 1 April 1989 Ty Coon, President of Vice This General Public License does not permit incorporating your program into proprietary programs. If your program is a subroutine library, you may consider it more useful to permit linking proprietary applications with the library. If this is what you want to do, use the GNU Library General Public License instead of this License. Swissknife_1.75/PPM-Swissknife-1.75.tar.gz0000644005110600510130000061324313155517103020361 0ustar ecastroSwissProtCSIW]r 7qQ`7@ČIE_sNgtq 9/uꃓ_̝efZY3չ%K?3Uwffɪ ʗ9tkknui;oVս%=>`0 O;A-qw~X2=~9_f2zZ-ӍӞ"+???)ٗ ?joj̖ӍCCzK2͕'٣ڏ[ۻf}ըuC_Zn}ߪgMq B/__7Dx֩:=^{] ee 嬒Ş&޶bj 0 yT(ahs~5owhj׍W #PpW޿@~JjL>hNNś4hyYЫvThKP=T 4|``d[f=kwzVqToֳnƫ2'LWF{ii)تu螞1ѪF9ܓb]3CQw[|`C׻kaa:l>FV[_nv\oֳfɺk(COdVzѢTu<>?F꿞Fٙv_7:T]v<.i塑z[]m$;k&4NZW@ƉA'ZluuvZ|Ј7 ̎頓ڌWLw[5Up1tMdh&:Ln~%|H -y>#h41F _x?4^;ft>4*zRgB TT՛]SLFvh֧va٭񭝵~vAx;ԡIyl5ߝI)IAPOۭzuݠku@O܎6]BzG-O[?Vm?ڄ?w_TYȚvQ}1EUS  f۴ QOxD܃-A߿%}w8dط^l1Z,0[xZ>56u\CÏgLwuX\&a [7&$Fo!U5wY_j'笌@ ,=.lFgY=_?E??;oQ v"G;7m\P<*L˨uU)`2#=geTjRoET*y#EYd$jK٭[Y7xPGi"EID5Ys3}X_fݵ+v6wS9tt'!o޾?u)%<}('Xg5[G?*TW$$PFdCI5nju M:Ę/x!;zmzg^:7wj:cT[?Uؓ񊭩FlgoU.W*;!b~aeoHN9N"ύ0U0η- 9Rb"BGc6u`M8C]?ǨXb|/hj;ؠɦ+{ovƧACPC,"d.̍:dljX>ZI/=ɐ_$}Q<\Z[\;⧉/o}"CM^o^oO> 6mS*jӌ`gaiwo*{i ?jb;l![ёIgv'KQo09Aq{(bnC=.0u'1EB0k>psJ(X5c1ye{j0%~_&$+odW !ɝWgolUD#ÀũLGFjfwbb렍٠;*;<9N g/Uu|usr|#f6>2f&U^iCt2Jǜ3Wn 9I`E C@XgE"vŃ@҈DpA\,"̟I\fzGbOr8l'NlDN`MEl~nCXp|hh `p|;~(kK h%+ڙ Kjj{2`(L? xI=7NW.ȇLgڃo÷3Xf $qps V2A}DZA8v0iIA0\9xofFar?> iԃ?_-ɂn 2eMI`Uv|?>5ȷhC VZs\-Ccp]QG]l˅ c:Z;:pOHgI[aV 2kNLG?uWTZ?=[߽e#Ŭ/VG{nvJ bGǷB 3 *cӊ#x:fO0KmрțSSlp<@6SͳY}]k}F3b3/lj3pTK~W~H-N"c  hKZOQT`F?wIf qg sElXN3,*8å;#6fXSWuܴ|\d#ΏO^#1#H~6|Z5;K|Ȣ2y:G~]c<7!>G+ C;`"B- 񽬂ύq<{7G\Fj"%,Rӥ*זᳩ߯llm6;;[gl+곍}$ؑ\t&lK b&I !CE4Z}>@DTU:{ߖK" ?J;Uv҄Uo UUڃlFOK&hWk(Wls1*[P`F~˷f"pQyVDO^ ؽdЏ 7lo1eQɸqXdٱ1`PoAVxr[8kdFb~g+ҋ]Y0}1Xؼ pMh~y`fk(2I~BmgucjswJ Kpm͆M{K9N1r8|)xBYXN2Xkd9QֺUd&pޚ+ $G-ӐeAFlv1]dƺe)X{d拑FF.r2t&~^1sHF-Ti[p We(M,''ިg1r@$ĢPHDpi' /MV@0Nh״p! a6`)<P@@˃v\Pno9Fe xyOP"BO[^P Jan&curdbгZdDr5ypO{xX ُ昡]ː9~b˱p4.a/NwqulS6/ 2zt~zOjXqw`wTg r}Uǖ}eج>Xʶ>ʖ>?c zZ㟟]Ӽ==Yꌾlbc{b`@mMl~on'mm{cYz=\uƍ8 9^N뼍 d7GḕLN,@ucԀ}A+5yEDwV44Tv:j^|m[&e7JC08tj3"qs#2n`۳4 {&LԶd0D"/8 3aEz0mPFuƍ"8#EVn "1H#=טH8Oɑ5n3=?AS35jW3q $lǶ|TB+ Š }pʱ8>5<>)ۂ~%^qI*N԰FӶ {ت8[dI3yq=tK?󵔙ArTxOvV׷dp=>wDŽ*jA¯5GJ,]&[pbHb G,1*pf*ڎcۂ'7wwמ?~&WG"Eyd( ݢN y4ſ |' b8B,ޫdcS)@MEAQ>K 4 ( ^b =!@%Gw֨c+[>s5Ecc6&.u|QQ-lŮNa@vnis]D9XgOuERt}9*'Vk?uΙCC iv#@Q_ߪ/N- Q>҅,fE(z ucty*н_Mx4[Sگ5)QKxsTvYإVg~&ȰU'&8򽹻Fk++϶Y*ٷ+;kju8~fu3 ﾛwim\?~PDh/U4Р!_kx=&2_}' A?Qq=!h#TK1q)zQ 紑?(1Ahlg+{OIbgĥ&ǥjxQWXԻEpw#XE@~EB΢ |zZ4͛1X30sX2nբuK!3X('| I qυ5la82ڒ ZGV͸[]y|w7&9ȼE61ۚKv&k{.^ُ܍өJ,cX o?ܘ|5ceK{:EۯK[1i+2iH)"WNbvꉽS*y|>&2xDK D -dGgQqRF7tBH^9B&tsDs3;屍+.Gt@&5\}Jvf:Hr0;bl63  ÓOE3pB ڍo%?G2mQHpS<;gkK6bJ)DmDZdGuhDrDB? ^ s&:gI\X]3קo-3?Vgw{ءJ1)]';P=mA}澽ȄPhy$F/Ł7Jsł $UdU{;we@??K f- ?ӿ ?CSk(cXHDԈ!KωlƱ/aO,PrCH4ġQ\3?"m;O6I/[W&oNRA+EÉN\yYy+Yl?M=TpU~7[{+=D>Ƽu>|ӊhhP__ԆMqޒo y]XտvrM_G|1Fv~7eY0I]MD #ǯzF\ruTEb"*k_ovW܃*E2Or|<}It(Ph9@ω&xBw;OE /B$DvK,8g ^_jjBXc iV[Fd@`#G2'b45~X T3v0O=(}NkɛJDM(+TT|8!Ql[T@/H`v||!_(Î)th7Ln4bC$^T([HRH"GBb |! ʐ!AT}h!ɵTVy Y}ձ b?d+ dCq*|Az#qov,[PHo70 H+5!Q$VBӖXd^S\Kn XP֟C:;c_S?Q\%.ҁ/K7) `-.] `Ar6 b7Hwa{;̾‘$yڡT &~uz?r7 Tlh1oGoOQR"4 D~(y~4 x*BʑU?L2oNJQF1'k)q8D!w\0i"pjۯXvQujylS׋I}+Ȧ|t} qk`3{RI`n&R/]ɸ_rDgx/J@0[)X|ᰊTEFΏ.& ;Hב?[I,uR$k xԥdR S]O>AܵΑ~Ad 33{k|[2I Bŵ\%P lsJTlo~Ϧ?;z?必>oaOg ! Vtg.SrՖCy%[xe? y8ごc#&D( E+M$$RJ>(@>Y{1f"克dQ3֘b,5M'Hx$=""{䕒D}b+iTCs65-U.]'dFg{M:Nv]a͏qNE+UqC !^0(i׀F.i Poj$:ʃIU޵0c9@I <3~{-,\\1hwrg=둻-D4jğrenb ؘ` Qtُ{+*x6qq Ѻs,i9N>G7?yWL0ɇj1مh@]X}!q/[ ck{x4`Ϣ`+6:8_9+Pf'5\ KWHtǽdYX1͏_Eq9Ybp3B^2"$im[‰3yEcJ1t7 .b wy2ᲖOVhi2 9Ga,K 8A)#79S;%jqZ_l/Д{؎T5 M 9u̚ +eKec.+$D+a7Llv\J~T"va48}ۨt_y6 O[1)թ>? َ^B;eXDNYZ~=m<\q.Gv6@m>DTCKgv:K`Z[á a ψܮMiMlO#̲vJoì!ˌk84D#v=]`DB־5hʣ5䍉!˖< u 'K I#L)Z#Re]-F_6Á/̖۞in .܎Zj[}hi 3>?~!X,4"<^ԕ>ʥy=a1qSB_I2+JUE e]ouw\s% .W>8&j\NGCJ;8dȇfxJF`݂ -}HdUQMr#6JA~!K@NwFa`]'ս ^X tMYȧ!DkwrOU]d9]| C2s +&J! T 6د@rV*ޏA/[%yÖ';8[v:pAkT}[{9 5CR&gU\" ?1A S=a+T WGl$y?Ḿ[9pv}3}>#YS:e.I6E֌8dU$Ok<4ۻ|V&,.Rq@ZKi4^gqRyJP2UR#c/%E- .oyF܄é#qj ⿶<hS͏T4 4βe･vRcUPWh* ɲ#|{1Uꪰ|KmK20:n(c',Wє!Vj E S]o.s NS|m\^vp}W\[ku^Pð/GրP q mj{( s:g(V l37<zYw1ЖL5 !&5aei.g“~Ҵ/~[ >?iE5! A.etOOWby*Wcl8T^Կ,q\TԽ-O<$gJnbva)U\"N>?4Fj;}P{%iLFtס[nPr6BL[vC{T-@].'JkMZ+D4òZHG2+KH9s OHRc!0|{ 9+-B ޕ թJd05kKK)Ev\0ԶK[-^:Rg,R0nQt妢U# v"\-3枷& mپ LgvVϷ"vƒRQ3MBGPI zJ@L]j!􈃉|xŶT߰ W&y'{t+Uq3g*i?;Pwzr+a.Ĥ(g݅ݛ|S%{SkxD9̻29|y%dc|E&LHK8fr kJ Hp1v%Ў VN 8E &NX a1hb7+wqDe[M O6Fg6=H3 n.@Ņ;fVE BN=^SM5$$Mry2 !9A7 dP$9"a&l 9W"ύB\+pl1 }(I2mnn\ 1%hm Sw'2ITTT ߺSZ!T'm ;b&X+Y`NNSzqC ? i^`D`=I~[yxZ}B7+h]yW#?yn `: ,kP.sylNܰ +RhYvtGMNą6<8qKٲ#*hlŎ\=昭S9N F {L01p%ϛfms@pPTbK='M\XǙ6](v)X?Jw󈋭0cs@I7Kjo_S]kr?m4Y懪19/sk%6 2X5'b_ Yh9rY5)X́88j FCyfʼFO,F)['T"wB@2a0g€CZQO ?MW_Apq;L*8RE^4sѸ~8"wiɨx.mp[ڙhQY1Oi_gJb,iSL1le5ndՋⅾe-1HrgE8}uf/gŹ-i,3g=M*%vn/ױ{*MιbZ6WN8+r5|:mʬ)[p6gWfÛ~#lgBr\ٿ_k:??w=RKb--1m֩}}ᦳF:![Cv%f4R}Upo\4b>GLa1\8dF?׎cCCQ2.acwy_ u:CyE҉ֱ.{7:e,BzF x-!b%|DW6W! (AC>DlSfqX}؍~'.Gv)vf*Z,ae j/jXClP#ZF;PR4@F+17;]D%ʗIƩDHb{R^+1řDf?}"Bmh@m%0H\`)fqV5 #mEىUVdˆ/Tqc‡YR͵EL\[T7ICoo(x ɇ }>Uk+xe1}PCxHA|bbɠݰ)|3\)ar'sR˵XC۫"hw*`̃f] OۗHl!P$SeX0`6oAN$ X}'ȧfQE7e/:/s\ xhP4:LEZ,= TM0CcJd-2<5IpFɾLHфd.ְ, Rh+;Cܩ;;MبKG̼xѝ?wV%\zGUO.O7՚MheՅU/:sw.T~f~njΪnRtWuV t/k/g"Ew#d3 ~f7, HS_~?PSkBιMrtw[R(qp%"DejODvd“ Ԟd%Y7G@Oϟ/W1;S<;^]hs|T2AˍW~U3Եfx.Qg%>0:G㷹M'oQޚ}f/_>tBtu IT;>25}:X@:0 07jKW)_%kir8 C_@P{UkT!H[M|"!ܾEr66b=o} h?̆;0$Q6W+$дf"v,A)A~`L?͗)D`*AEOVqSe@hQo7W:;3Dx LQYDULnOޟK5wxݳp/@C[@ WˎU3Shun\k/EIi j&U>ngVW9f#,|"S)( }3ns)q7[쫞@Õ",}Ըĭ{R^g*֩Q Z6KT  u$L&=~A~DrV:_Z'iI 'Bvha`FÚ46ߙ{cEڜ2BDl yj"B7SW&m "-1q}ʅj%jv -ܔYCl+n>Npl8:(U}|O6|=DY5&}WJHʘE$X%w:CSK?:zcƸu:gm+*gUNh`x.ucNIC SI?7w;b͇_bA%YX"-T =,Z_p}D,m}FX˾#$wxl7D/y0XWŴojCqluU_AZ;'l"G -r$˂k;733ے 2ͬv6_0!]Oh{-\޻/O|tNg屴 A +ڷ#. KRKI\Իr͋ 1&h!9vOO1 '7E65KrWɋZG8ך).Bvox50k\^3 8B% m?7G[|G>D/2UK[l(C/ xĺ ̻yST3Z_|$KK`KЎeA2`lr+0_qf4?M\:œLJ繏x<_z |Bw©Cf&w ^KpϞ_40nddKwSN+7^0IN 3@NN>bK3/f#`yx*9q)_{}hQA֯=XHUt C_M#>*I 9ꥑ<*x%n nQX =l8}x|6x8[hRYE{k\9vc5CB%E ҏumn` w!+ ([% H=Cpܸq{u~X{ml~O'ASE_M [=WR SA OLݗhTN\LWގXT!$|rhPe0L|vVb×x_OΖlkLo_of-??a;=h^9 )7%5eBn'mҴl6+cDrUad૮7@ڠGݖsLڶ_覹떴qP> 3Zå/:ݗ_utqAq+RGK0/ 09ue1MxATųơZ9b%_p>8v gDkIl(1 Iy-#QڐH.kDen[}6D^rb4\(`kTbJ@ Sc&ҢtUH%jF?p +N'iENm3+ۢ5GBxE߳"=[X7.0%!IHAD. eD'̏]hϮ }䐥,6ok33:` AګbR:c~C{i)if y6}0I$!3.%} G2-둞~bY>lUh%2 d \Ԩ%HZc'eMYV_ fn ^Tzx̝NČ_=j.?(BψL\й5pKڞ4%=dCV!p^.˲x5Iˉ!ϐO+atRMX $G:AwB7B ;zq;`%8 OJ}%y\ΰ&R՛Eׅd%I3&PsA~}] g'_=?;Kwo=??v/RO̷ TTF=M+7V#*^^aj>(H)PKOA:* d&|۽EV %!@{!$kB< EMЖ0]oqF1t0YY^Sƣo='+:JÛ/~ګ7>.ٛr[$NEhާb3bƋ" S)Z{.-9Qv FIO'"Q"ֵSE?e,EjW/AZHf.ٿI d:&ФP,;`G uqoH?VjЯ5rYG9U ;2喞6_Me/oW(,m֨5cj Vz(rc3 i0^-MF!]X/V&H(ȓhyØ$@h0P0dCxr=-_ ;qѭ_!URY72m|e3a \بi {!~:Yy}8!Nn߆'z3{1zO8 fJ"j94.;V`jt5Ae~bp1oxCfy`BM৔ʏ>$ ?U2,b+_{j/- kb9&mٕ:ѩoefxF4k4 l{p;bF "'4W3X;8qG%0X&XY#coZd^\+ s&"}U,qlƧ<7i&rCy~13hAck~~ n w JX' 68h13*p Jx6>{AVe.LzR;U?o1ۭjd&uց: pފ̭2ߐmƶWvw66G^ngE8L7\cl>vV6BTsBR4=M9<[O,wW.KtEk^36UruM=}r;ۛ_Bѭq{sVR| m7_Vw^LMkm%{r1yTpߩו6Ԫ]6/?W7hT*eHЦo̧"i)t(6+k뛕oVن}$jRE#raClƉǍy歄ʇM4F/4dO{oo^Ft{/cq_| `{}Y%+*UI8v\훇somdGSx9a/U6F^eSh46Iqq amꔕ0kH>|m?7ynr~UUHTmT}B#{B3iRC&Evq.HFSgأN\l׃= (WG9("(΅۟[>kc?Y2۬6z$'/?2Q{1-2mW &PY@k@g?Pb܈A~8Qy,u~7oř?f; ںHئ#p>p?Jſ=sTXhϏ/ˇG%i#bh/Nc֡Y{z0`fmZNeӚW72J2iÏk5"kv=sM57GUQd1հ ed3kS8X?*}巒&>&s;aPH tIU,Y؅`I ( P`hh$QJBG0c}Op̝>AJ=?_S?Y/S3} ?c~ݮvy!{xƬ~y!%"rv./8\^ه{e`%&8(";  ƁE  5&ر5CRφp'pЏke l:/  hjy PQVd2r,xn̒ɚGe )n{ ȼf\-\:LH(. waއti |Ap)ɍZd _z "5k2M>4ldcFW1@`Vaؿ9nDM^;2=[H6?7C<S( 'uc1`nz-̀ 6iIԠOHI8 ۩XLء86`w0(@SkE&ρ@)R#͑/* %*-Z\&D&`0'³^4a/ FFKX)-= 4piV00#M=$ҏ"4J}9Jc-[ȕKK-04Nph-t܇-’Jz(s~mwÜSB w=̾H$OTaAJ",p-X;(|DUKd?Sɉub-5%?xμ_w7i'IGKLb:)jʣѣǢmprÐcY#By 2Lcy|Ys~ykcJ'0s缞cGA0SX0 X}hX<7W t2/ 󕈤4]nr>@ StCq#^J5M^-ef} } qnV,u# nQ >a1x.N/ӻvИtГU/5/C XnCڜf{*qf;c(H-ShPsq˼h|] z,CƠavԽ9c i.U# "/m/X&ڨDTD2'HRynA>T=%ކy\Z;}WYԨ*$E"Կ:Z㋭e[XČvnU*߻bj|؃@ 802:O\~ A=7s_i A,ka o46rrœ 'ًpAv"]LfcG_Gm.+{/~%1+/,K/&Gg'>r2pР7K JR,R,?>؁Ǘ>A5Pؾn # fzp T}WLL "~A>j/X*TwyQdT;^(wg:?kS+Laa;P7JB" HʜOjy~\[>󹇇|Wg7+~<J)UIcU ّN ԭzFՃÁ>8874jbQ-@>\eOv$\<[w~H-j4Bɾ0IK&Fu = {T ^.ީh!paΧWʥiQbdu&pr> w)śoSI<ؑP0<%Lo@Vd*r0R]y`i ZW$q:l睒6ZG/s&5&n!ʐ; .N$O`_j OipX"~F.R0!>\}A 8ako5[ 0?.C5XdE ۰;<>$0_P,.gPҳklԊ1vn321ݏ1B@V:S>FW,jreG&=.Ǿ7,ejD1Z4fQlf@f2\Y.F.9vȰU~"6S[ >o dӝܪydQAZ:ɒRi0\Pv%QgPLU8Ar/"$#Pۤ|6JŚqhCf_-G^L`ؒ O9Zs{45؄>_fMfz"*j:O';oGdAvo+N]3`g8x{|)ERT, 7 $g2<Ğjw *[ ɺ`y^f|{*hm(3}eoQzʮ#F/x]?9Ze?oV*#væLÉhT:7ͳė.\QɈK:`B: NaSmN W҃qffV܌ jn!IYt'k3&kD{4t4Yv M/P2##03q*A;UFxlZńXMhA5N,>zK = _ra#ع!BjO霢xt`}=’g x^Ca-b}z[JKZܓK&"N~ԷRTIzxbHSIw;m},|䂽X-";M5O҆K2/2P8a< gZ!zLM'!Di?gj~NCW\5'\)\#P>RMY8QQ %:.>P@ srKY»c޿1bX{ {GhthV;"FAe%jk@D@b(}Y\>]0#^6fw*XbI,=ٱ<(ֲlBGg6N#ALA.s'=OFN S1KWq/Zo p\Jfƥ-œ¤Ej׳e2TXkm?1HZKd2^k}*};pd ,E t=.sfEB䃸@5ԣk՘!Į_6~TS?ڴ@:h|UqeU!ec&)O ztАb%MDl8bʓ)gKGW /6¥gl=JHJ,P2']ҬV_̌5bG|mOݏq\.}5պio SOL!}YATRF6pH !\*ZWգ?LLrFi8 HL#wRԛn,ȕS1x%f;~F֚AU][Y"XS>L 6wƩ۷_^QryGD%z%́?ɱf1z]9qĀKy x:$zg:bG'caso&S, %=,RV odU3Yc\m Mmp~䝵eσJE;=Bw히Γ&333 k̼uyJuSJTЯ S&G9\N4G6  :f-ٙ. EI]O,l(D~н^D,&.՟9g``$IBSEG曉.G0.QErC\Q9dΟ4}p–GXq|#1P@>)avrX˨Ld-5~H ljKw(ksCLۧ>u G_1%Tj @qw#PLbQ>۷AC\~l@Al֊I=iౚ+:\}Fqقg] e&>X6.56NJ05US̾2unXA~tL:/P0lVd{63WvPKg*rvS>">6ko BEK YAP* hȱ9IGО6DPn &NKa"00 Er-88tYSyT?@ie㬾Gd)l? ]Dr* fol`F)fy"ԥ~F8u=hRHb?D&i̮[,R7aAM.RPNda2 8D۩ł;8]0[pBu1)$3xAWX 'Ybu]+.DnW#w$˅$M]&CDh8KH2L䮊 it\7N䳒L܏Xc`a9چVb:gVﱘscM(g"=? 3%zQ/h.D| -ԌnBA7wN콍Q( VT TpUE.'7z= 9!V%53?Ua_S1kOqf'ǃ#H2?XFxé (j@MH[^DLRóxVL3҂ekf|J9rm*;pmal:g\פ~)SwEUtj1La)N .Naa$'qd< yiV%mx4t#SULdSϫ/M h p.+`1&z۸EvPh`+R i p pZPoW@2( uS5x“.JII ˆBb;߸%"F-(OGuɔT;ioM[/KCRjuo (Rۭ^@+vD8"\eЅS̙m<1I֭:!@`lSWk of_Ž(E߰o=K1kIZGWjic6rnK}ҕ!%4gqnpJ"/GrU^{q B $^Mq1'&(2h.6js[W ڪߋq(ёt ÂqS7'6K"~IfEC(m8'FU*PAxZꈑl&QSF΃1+uZ4c%D YGx".l݆f/ @DryZV%Kv7oij)l>ZY}6L4ڮtHPIވt ӾGW#=ה!0opNTGW)kT]}%535)CaYt*=v(<߀ق .}=ǯ $bG2"n"wњγ:2HQu󖍘+x5LՆ"P1c@S S)yuevgS|uDmqLe%T( qE&L>NTnX' 3lgZ(.+EV]p\|6HE+m!d x:hpG ]Q< [%lLw')}dYD$ȹ0nh%͕ݒsY7[(A ׵^5@JcDX+qulBGBӝSv=ll4cq-]6͟t;;҂-HU%t(}ރJ]g@%asR9 !3*W:x¾br6Eqf6ƠY8q bqwr^Q&Wnb0vd@0ɹ C~ikկw;SqƎx>sTBۮw6U:*ZV1aJ%Ôyg9ڭW#yf_~]BԆ~9mEx%x= mVLe@2EFL_梯|DApYu bw"tBT!??8: vh舳tb.}523~UgC珟ᙱDUv"rmO\l8PJi"DOV"$u& a=^['T`{ /Q'%jmNXΝ,`#.7{+c[?@d]Y'kX+`}EM(3>M>0OTjKb?juqq?k4vh3ﶶֶgkr3y9hd}0v4ǁI+\w.KlNBn1'$J ԑ6']X%;t8@ݴ"9ڍ j)Y|J5BR [r.`2RE]R9Y+)-0ǟO,y,J("QKϋ%#d%b,/;BLZy@DZB;i{q.!g5O,S'a΁Iqp?5/Tf5E"(r>&:~)~7>V핍 +p=*ڵ[K`:@hV='my/XLu=޻7k^NŴ dbBXck'/6;ObAX_>s^ Ps\4Ff-O mss~&Cprk]VWL۰y{Mu[uu Bܖ'?sR𠡙VK-kO/^env9plsnOm9Gޡɨ~fr~:$ҽ8ȣy.s 'H"CT'\@x+h F?MZG#I K1c A=pQ#q`5dMVUݠ(ofon4( ;ss@p,0D1"ܺeU(b&w%Jpޭi;wCo֟u[cIkeo/&>Qr@-¥iI6mo[ O9gَd\BJc7}DZSʿQv7@?~Nns{Τ+۵ZIĭ}:nV4b GBS T.yQu~tAqxS VE'T!s$ ?::2˙ة{8Ce)&ۄإO|l&t -K+kSw>>ͼ&2k`9Ў\,/)AMCiiؠo=^m`ke6}ESQ,#6#ɸiY,[I6!iq"0lm.hodagf{(tҲAB }`(^^ˏ| k dF9H#.ʾɁ6+vUC'VD(N.I V]s|NBs ->ʯWd[k%RjYi:~7e`Dx-/8;BfMri컭مiF)ءwk3333Jh}ŧ)%WLj|0ЈRANC>Arp/[~"]%r\W_lJӜ{cy}J0Q,CUȫB+. g9>q9/uG9 bd {grC! >vkۇ{ҽ84U``FkOL6Jnœ /='YԻw;PWWV檳w[gA[gXc8K}v̨z.Uye # Fcd!G%%:IJis(14nI':՚FcW|]7w-gpF;"=fsyM2& em.GmuqfLac'#Q/ŕrOʙx|vWb8%uu9jc FY05l ,i?%l^+QGHv+j7~Aw YwžjZH5fO]#į2H¼(BLWYwz& J o$WsOMOL),wqW5cWky y,vɪ]dI ^ 7\Հd~Zoyb %V~l섶JOZ}'jQ0-jFwu@cv ;KGm26M!\]c kS=:G;a]K}@IE_*;^KN@LXs[F 6n~ȸ AY($M3w!ccD:fV3 afV0z'Ne %l^9~.YL`A3V!Kέ/&^YK]CE8f-mOЙлuxl&*sJ*OFp(Vw$]S*p' =bgsqh͏~6dϞY@jy#J]$aۉ'H[CglH@P:]h϶eM VzzIei=jJWmc%Öc<=B)铺]gL+{K!qJ,N:u@@kO7:`EnOlk:;7%[+WomWLPOJ+b-<9D=dm^_20.d8%^R&:ysa ?C ^"|,'i=LaglqI_2P,ߙ_"g{?l4 "N|lTRhǭoGO7d!~RVGOG!tpXNl#ھ<D`*{wBS}/Jr+ Onn--?<0cXtѩ"I)5A'(Xg-꣱| `)w@'Sz,P/&Uy󎫔ޝvo]?zF"܎D;qAُP/ʣlJlb0I" _ R&=GS~xԭ㕇~_ O,;#b 8\tcAN1ÛkK{G| ^ ^ g9`ՏD:aq]4 Q}P)xpG+;I!'!feǂϑkORL5-#?kЌ=.D Ʈhz!nXiiIt#눞@}bǧg,a T0Dh5s_hRh 񄽊EO,†KpmQJb;[q!*n>\,;#-GpW7,N 8ۣSfl2Ϙ"v<*lbFԅ\՜Ov*Qk`G$qo )BWvy.!ps5q;G2^|AX3QƮ ğַ@2GF?A a9] F(vSv0 a!3Uӻ2{(P@=v-VE`m+<^(*N#^1{ wzWr[GYl Q$Z"I$̉y4 pZ뺿2Mx7o|kZ!IFPy9ЯqN"}|yXg:6320̌3Sl buY =Ni%c̑ uC7_*V.iZ\ ؏+!dj'yjb IK^ V +Bfj38?8n"Z(W" ڋ|$<) B[cqBNp3Եfʾ˫DcԀPte 1"R?X5d;Uh*պoCϣ@NFg􌠷kt(eNMđ^ LڱDJ  py\FS0͜`MH`Tܗ] xE_U#v (\S>+D0V,ažp8TX^ը]5e 5J|ppC E@ aĐ}[ٻXŒ\W,8)[18ُsZnMlBfœsZx €q8c}tgh/r[c+l=|UlE/n銰,] ?֍ Iv‰ԛCMK%6paԈ&\JA KR!wȳiݯI%x4ŀ gA6`ʁ]\Z֤g}ےnv/&x !4ҔjR A}LYrWWl-&jjBs5ehzV,1_65lsV?ar/bsP])NE *\&M\O%)9G2{68UE͚0+rnY6OK4{lcfs `"g LX^#A`x;: SKCRCv7ƁEKĊ5b'~w>I^uʢI3w63w?r㲗_6֖y+}l]-޻ cWjoŸjK8ˈ\$VcLit\ J'Aj R̩X$XKC##CXJ "87F$`?vkHB.o}9oףP?XSمҷCS| %Fpq54.RL-Y[7mGw?CB<9N.cւs4,Spjl.gն 'X ˃Vv5l+86+:+Ty~ua[?i0|u,^_cPh2 JpɅS F< ߨo_sdlvޛTN3UK/Avom0.)uPJtbcɟtՒhߝ^׋C qIV(z SAay[ӽ|Xwk(2י?*\2Ru,N_zdAEz[|&<畮{ f3]@bMZJ8wX{CyȸK:ADL. `YsT+p7];ʑnG̀Z)H#8ٻfMp չ'k;[҆B-RheŪct;0j\;[ Yvr"SS <4m |37r}g37m JN]rB_ל>ukBHRT58.µLS Ay7y;}P7F=5q(5!73b+g9WD^N ֑E!t!jkpW9!i B/Feu;W.!r6q_9>-#kv;޺Q$&rշfIȒ=Tl7b[eXpR#i[o۵8IvPŽIĞNTF f+'m?hOg!ӣF`SW9֞<]{N3^^."f3HvM٠A:nݵ_0ƋЫ4i8u9SuDoWib)4\󳋄a y3*pW.wg?dhWO|EhOj]NM\}W9Ea)suUz!S;Ͳ˘&dJ2?q/^Dy=JI'=ȺdzY,oIGZdE* kfvsn}E3׹lɠ1PFXX{v^<W d#mFh ?;<Ļ<3ݚ*R1U摌ىDSMHffTre c0 s+2f䣑Nh`JzJR2+b-wuag\8u[՗g71j`$@pXP?Z#s$LK\̴#Al-C}ly; aVTP7UJAj$,j@(1פpi ݷS}$AڰO=W PPѱ6r&%M+ug\fmQ!UMSASu %sp=$BAڐ# C^9# :c*F-{k 9s$U|:Cik4j97SƧ+6̰34jϳas**1#.eqH{O ‘޼3G?"Kۣ4bL%ba>G^žB)Rf/6*Ae1j|];lTvl$Ѓz*1H7o4SWU>N3'xy5N-5Cgq:ב*,GPQ͈0' ܷ>PdA/}e[1^lXH5 X/Bz^qZAQηz/8_s d[XbxmsHM2 11C wH;oq1 hBM;XSŵ]N# 4{7FlȐk!'ѴITEⷦh2lt#x%*rGQ+Hc*)b[ˈ C툀ضg{6y|nAkA8R61O hcA7$&F)#jK*A ,2V;7ر!-l0DEd1B!~{'u &v]}vYn>vQluV&.I t>l@ LxseyҩVUҌr6̝H 7c;5.ҿa}hͫb c$}wG=#W]b3vS$ yY% ڭ;yZޤ4*d 큲(FgKaBŤ֌z 1+_8W(l/S~, ?X)V5Ru O>^r)`g-Ma'DrB6ErXZ0]ɾ9NG=p;sՅꝙ~s$+᳙?JI"d ֥]#3@l_m+7Ոqz:, `oǿ]i%`t1a  yt;mBT7a/r$4;!I#=ġ#c)@}.r]Z=@+8N;0/.ri˃J[V/E**^Edyϔ~±.%3@w<Ꞟq5J~[Ig|,3 ]Mvaj 51Y6V#?oVtu'(cO 9=30\V޴\YWO;t.XnX393Y-Xd4V y.ݰ84> ( ӄ=A20}O5ݖn|~~œt$NO]T'3"ªyeߚgf9cZ ͚A%u)X'\:;K`KNz3ujNж@),"742ΫBւb>#_s;G.ZJ!\ zJم&7}>D0h>A vJu}r.+RꜞqKh;Kk_ڰz gm4>#걱g|i5x.-VV4 ,4(ܚE.Aۉa:v0Ql*40ߠуzVWR`YٍTܼk!t6D@TI)n(nF(&>֡cGO߮c%rPj&Jqm5Z݈0bjOʯS30G0FѫX\e +#RRMt "e|a̴a>۔t[Yt)>k[;WhJ:qv@MQ [,U2k-ӳAZDqKΫ_(.)hCibXmasŇ6REZ(h%]NPmc oz+.%D*柎8#ºSWp ĕ[Rx4 "Elh'M9Qĭu"] ?z^$ƀ۞^|] =g c"3.%73ğ=!zVc]n SHg1hS hA({gIIˠw({Z>y ~s(0m۞eӌfu:XIK9d3s?a r??ke)_r]z la6ƒ\㗷] ?gSboeNò4^y$LwWjjN[{R{θ'U%&6^ r,H/{uPcί=Kv~Y0+|_.zy N\A|旗!) 'l0٥.0fQDЌH)65W q'\Y.wх/<)B^ZiEE\^vwzQ 3^0K̸ٝ<<rL~0jgj8^: jT=X=dL@>9-Qa1 LUlz [@`qp~~F\^}}F&I "vtޣS{™cҷ ~`"(%<"%.Af>(T jDYj!Nv#f(s#JQtȵj Cʗ/ >tZ %,8 XC.NˑɌWPv@)Nͯ3q*UJo_7twR"d͝c8TbT\,qkf9aLA< dӳ⒁!+JdC @4F=5+p=4Z+'>S29o٭(O>0B,U\>})%ip.]弁Z|b*$ihY8'y׼Wǡ; #T!o}~lnNoq/4jFuQyZ>> [T07c1f>+K_'e ZmEnvIA~SEKKRigGҌ$9E\ r4Vivi 1(`֫EV{&G9Fk @Qj(IMx5X0-qLGwsQRn )9uKr=Lx۔~{5(K# Q1ϖ|OП={&'kp"rK*FBVHS d9Xuu7`{#U:@M5M\Q/j5E9khWj}O`FR(/?d KG#â#]]Y[g~X| ؐ]"2Y>/fg9swv~2iGO>ȗY>ںWi[jL $qA>OR[p&3k6aa0x3R]$FH P ͐#H؉AY=+GR+zB0I ]#Lחbg_]=BsT *J2s)ԟş?(D1i?"cFNN_cNӗ 5;!0@nV:QypHـ9]+cW导K>Od߀a)fdVh.rEssr4 QWY9NS0iTP)S>> r/ʞeOWiD# FBgx[M2qbsQIw[`ͥnsȈpH,L@$ s,bt*'Ϣd}gmeg$ʕ^*/z{ xIRlDlT]@ɤW2)oCRi`Rb&J6Mcښlΰ%w r9davZjeaQx|wt{|R 4XI+G c`eƄjלeң@rceKWW/f줗 db΍r&Ro?[)Aq ݊iڝ ~H&HB޹H+c l Kz_hڅޓ{pށ+'p"u噆F3yJ ؒIjh*TSagiE+%vM8tƅF-2٬-O~M.(eCa,W N}(#=AGJK*5'5yȥ 1-jX0f4f]-f_R>sI $:=cw!%ۛEߐ׬R /ď lH3{v<%u"?E<3zU2'(R; t&#-甘Ui١DǑkyYWzCG7 a>QW !0} &#FpY/.POR < 20/s2߹ՃR+&\ .H ^JI4-Ն#P&8#||(.&gx 2sf(Hl) \<( D~+. 8,^QWCi+<<2ehu^Cfijݑ{8^ᨢ|$kt bݓ|@I /9.K˟Y4_,ktRȋwyX9w3*^܍+cq,9z`ޘ3HRK0F{0y849CRv%ge)3,Ob/AG`yiqb;uؠ#*t^ J C f,ȱ -K6NaB4$qVq B.2O]|!L T, C)V6 A3ϚP;U2SSS5 /K }IC7+'K28!4Zg?lU)?j67yilz"G< gM;,Mi@s ,M )]K_=Fuv-mtnoeorn*3azؑ]6~Վl'8w={#$ͺ `R;\v x;IOZ\ ( z}|GHtM8)2Xt:=;3sgOB~膃5gX<\2Mڿ%P }ܛkFMϓ6R8{tq0~\^lx5To/Ѣwc|XПo A5L}J%K B`&ֵ먔~ΐM+x܁vdOyw>zǝ3Nn,/\BJt8/~2#Ye M\*׭B޼! Bl4ƪ? 5pӷKZ\YgjGTcAU g-0٦'^aFԱWqe'*'OQ,I9(اȘ6b@Qxd{ZmӵΗJ=`bmOf~5gANt&֊']RwVw77p_Q&aF(!Ė͝I8GFFLz0W%- H7%OC. h${ޗ;m2jG=nz6o$goa 奱l)Tǖ}e̬|ؾm2/+[Bk,E}wܵ=-ԼG;k[z_ї]bll~o_ 'kR;Fd'<{D^ L $hzQk\@)cg+OON}1*fXSdN#\ϴDqfDȹP3ȯQHa:@n $ t~['xS:D(%ano/wZ`[Kq[](Aq6_ĔwcIJ+)di׭LJLZ8Zd}ysEנ:}${;{ōn\vF3گ#$ }?y]=Cd,|v 0}Kâ@w ƁX@E/F)CaMxs<> #N~6ws~ARhEL  t>(crt43L2ʺ6 jʹ$茿a, DL%.N9?gwf,`‘<90נ"FLfzu@5E Jla$FG|F4e94m0U&~ԑBQun8a-L~a.uSb`TFʙ7jSBIdFdEæ(Je:tmr+KwK[~"ًRDc6 0Ⲟ9t=mAlT[ubLEN^yB]uhyLS\!aBH8|C Kã*(a~hx8"39VL mF)kdkdGC K,me)ԺJ??D.H|,[q=;kqy< ZP?iڈ|>i jq;G겁_*WoY2 ʦi6Q'%L7HDz Adb~ge{eiC i; X佗unbxױP~J+AwZP3:0Iy=)僋lM[?*1aƒ<&qV'uhð֟'c¶^yNLakc7k iE-`OWwמdiL!\RXTژ t ,P[J{}M4fЄkA@[;M$wh[;{G ]{ h5י˝={ݳ|KwxR]]_y&: KESg;SWVIɠ _iXgkW6i b_ڂd_YǗZӭKQPvW~_v{s5 ]C4_FmAOD_`2ۉ=e+t~Ûah%54 H q Í$'e"43a\94gLcDz@\N~r2}Rx] GtxfR~Hs[(%2h!hz O/Dl@5ϋ0ž&w`,RnQ08z0Od?PR@50%Zk!*جyV`3#LxK߻{Et]!AU?YDIqЎ |΍$xN40uy~3|$2tҗ9u\R6K71Q On׶6VזK[1DrltڏnBkPNR\!""N[rh[k/&{O{/GH ZK SV e없j@ xgg3SRF:IM8oH3 A'-eJ2M-OH=^V5@H4#v9( YcGjXϜ ~6t` эus,l3sG_}4Lt<ׁB0[?OD}G~I0JĎ`+ڴte0k¿aGSTBz 9Rg,so(0_wtTj pjyOl<_㯊g e8GM;6-pm珟E=Zj i2*&WV!uvBI"(1QZk:a}f)@w,f*pzZVo[xw]rOHY]¢!0|-d-06;$3P(HrAyE-ݢ[ z<ڎ:a 0C&4iCvH0 O]+jmZA l҉C*hd fɓpҞ[.ΐp!Š) {fPjr枍GoO pS]z;Ľa,#B~RvP71h$bI%oʦI\.s‰}pXgZـ, A` U#/)TOӴ~ӄ aI@gFxUEͤ"O풙Td,ͤšؙ?SMbPФ 24f.(,xlndJ-.rȈo%IZo*a ]ovW!q(w EcLk|G{u{N\;sss =ܝ;g-aG)_4|,K6tW 7fC$ry=Ofxrͭf;+Oת`:[:&{[sT_-ѩ2Ċ=Iv_Vxy<ڈzўQ]Xw RY)i֎HB (|:.y6 ]^N$DQTHL0Sy0"F$ϕ\$vCtm?V\|gӇG\ CcHch9h+E7 wBUg~MVq[#T< D[1: dBrhYmکaG TڇHꬋ_3=\6hx̆ooLeX/F/)4puȬU!b%oã*9e7*G'*@@9Nhj|ಥP*ŸcۢYL ~zVu,:rktɾȲ]:yoޝ1J6r:}*朿Ozwjl"wxPf=Cr~4Z'y{wx5F 7-N^!V[Tgvq~rqf6t=QP. sm]Z+w'vG Qzuovyof@z73w›vwf&gwWn묈l].:;Y]YV1樿0*'3EH&}<;w74^Tg'/2FӕZBeɅ{ y}!gCё@{ajt=# u4wdu&.מ|@j5U;{S6s7:.N.ޙ 3eqqImjT&,{Z "XcyYWgM޹s/:'+i=0~`tZ<g(BT$!谋翴^Yl$xIHMXѪJĹ50h2}$܉$"X@ BC,3:R u>wQqũ%+=3-+`;[`MfqiZw\"kt0w7Gq cW/"${w!CV] RܝXZ;GYHVJִޝ J0'wRm~63ȹ V* 66U#`M@V¹hg^i(ǩHw;aoO㻹(p>NpVGc9\a8gB4039gl4n&b"s4_ a4;s p,Í ܋nݗɻTڭé 0+l1}73tئJN Ƒ0Wlw獜nElX?>OyglUNx{^;&f=2lڣq!CI~hL 7zjjZˤIWHt$kcf~ɑQܖCGd3>uFwvmog:?Z}?:+7^ivNҬ~ztYW:AJ~ԴFDY!Y#2$Ws&j(Q sfdAMb\vd$U֢,ISio J-/+dt6]%A7FhqY2_QX&VGau Ef5!jC"NK6M5h(m4Z^KtAtNwNPϻ>'9G] >Wo^땊Ga ~8=POz_T-RDHBXl97aoVICDmA#?RhԮIK [Q{F [v|.]ifR8hY]z;b"+7)=|53oӎLIǞž4jǂ퉅/^?it[^ f'8iF0䝪Z.{^RckMj>A϶gy'Xkכ;r곱Fʔۯ!R*T[Ͼzu?s0n7PSkb5$+= }zEz21=N }Sk=OoHg!pƾA/O7@opD_V/pANok6z|uR;U7!?54u"N$= 5m!NZڢv D;B:̟)j|YM=#QU(_cB|' hD( {^9H:& }@ogmx,}ۯZat-(F%oإh˔VC;2bшBK;-.+?Zq j(v]X;v_9l}{KcmyK:{2,vu4z[߽Qߝ ib0m4m،/s߻XoNofͿ'բ5j l{N-3W ddaKX )2XxEDIߗⱿ?t z&du_7ߜ7fb{e5v0vSIlw \޽L«o 6\hPT\hH ߙ7VIAw>7#}> TI½i.n޹7s a1B*kW4!Ydunvƫf"mZs87Z6S8F} &`9[Vfp7L❀dtx^? ,<¬̌LBF2}aBT 2ܚ.:>_ױu˻ROcvnbdwA½;rX?ȴ́!0}|W''Z8{|QZpEf@zd&12[Н{ L^eϕibc`Z{9YkDt4Ә,n~RY-0Ovd{4KYcڮX=DQ3ģRA xyf amfu0aO-ΩYݎZLLD<Oޢs1B,B&z*),^Zm<W jMNBbjaȪ8Jk Q9ybW6A1!L^y˗@U_o`o7d8 j Ձ1};%&Ɔ6.yF5m΂%6mBj·5 ihfawU kp;RjޝQÈB373w47VQϾ5aV`foQzle QޅESrR Php&bۈ5Խ|@hL̢o5A YrbV3aC`!.҆xgR l:^ [/Ϫt\53xB1"Yϱd rT߻ث@=\y;-n&mC̽ /Ckv'y1epܽ iv6!Λ[gw @:,FqFa2=daPg,= e9Pd{=̙#Fɳl "sU)߹eVmGV}my/PyVxN|*B|Qvw* )ߐp/,0Sy=2댟8q927W>_f6ۚ}(_P¨݅LV={olЂmS6 ڏգ3@R.ޕ#Jؚ0J$)J¨LUƌp^&3 T[,emajGePE."Ml nJyk:*x+]-=Y&{P 40YEcQ];B/nY /[k{ haR[8BeMo4J U <ԶgﱽSPuЌ0lFlՋD`aɹy2e eHNg]8}1"`!c;6@6 pIg+iuj=BJ&К6 m5 0iK` XNgǢ4փӁn,d.q*o'w|oң1V#-.F  Lj "!5dK_F"''v]\ p>9MuGSMn!ǘڠNuv b hK&~w|AI45GPapxgss.3%.I#,  - R|4|1%xk,SF`DE:;( XV/׎ ExFb`f=%_6Y?@4 <)XLixˎʂ[!3F-&E,tKV!_6#Qt.ˇ1Ckw X,x7塎EQۙuɎϝ$ޞޱ#}9j"LɕSDXŽOeF,MZo*iѿ{@aS2o"#*HQKL,M4A@^"&G *x>fm.vb׼v(8-1blU JfhD9 mh:<43%qgĐ"y#c`H ,= }If+x#U6/$&nXn/c N#a1":RdцT,%ߒ ,tD;:=,mn=y4dZup{S>EEFu\nQwg@3_EWYAG)k$ PnjoJ q]⠪M EV3z k%2U&Bϲ@ ˊ' \uymJ9%',6D/{|bb?gz =YXm+4p2N;O|>!j 䀘:P-r],C[_Ԅfh4cDA&6=RV`mJEBaF ipT q.8Ek$C\1 c?`UYs7Q*W< >.+;m*3]7!IH_Þѣ 98K=cCEZ`66DNk0P̙?^Ɔ\T.HrLjgO9iګ #qV=I)٦ bB`A$8QM=5(Ix&.Q(|s2KsG]=y<`h7z-ڸdͲ!I:Ue[Izz}wԪ;:$wO! aHϙS-e ,sR9r3@#d%>1;&zq&ŗMA:L7m}܀%iMFst߾m\,K+ jț?f(Bj i)oŦ>߄k.sEtWx*%iV\#?TriG"{?7ϑ{V+XA֬ C$0$XVtsryqர7eեo,6 t˹/!>܄Rt& e"a!6y j!Y];ũTo}q|L¶JuMC7dԡ! -ov5Il¨BC~vp΋a7qƋd) `/c>D=mɉyv4s3`w-KD5{Ț6҅; {C8*Bs`xʦR8ח;+9~o%-z*kaM mn| |~qzUUA U]^E0XJD~]8W5d\5pg_cf0cNp;:%rw\*/fˡC͘]4زF|4R2{/Xk@'e>0)>/qJ7tdɤ_",5Y X/|m[Xqm>LQ>r75\B(LwPd0`\ \w#o[?!$ȁ%!0v@cLEh$FxA.@u ^: L|%4m{W7;t `NjøPjzZ34BXkTFaUKB;G']$6 ^j`m' (XKðgHqEfiYrESw)T|Rd!-p(f!؅cEW101QT%o a(Ҟb>3%i,!slG MQLs/BM ^096/f%d/YmKr;/P(f X-Ī=3kB|9{Uٳ9QZY'Mx`3*PE>".qҴ4E=QI(b5X8ȕ)٠ѷ wiJ{_/ozU^"`8WԎHt3@\& o#!&+}OR$: %T8jLydE80#PENS8"40QdSdz9j*Dp}NyP,])Eמ\*BHh56@YD y^;zD _r u;ZTnvM540 Bi[!؂0 ?Q݂s !qV7Pi1nb\Z],O_0X;*b";{an;W9rax1ًMsfd/)%+br(HZc<$-5^[eʀ> ΁{O]Eϝs)X0kVT^z8bo}z:!zb t r`48J#>Ȇ]8ARaE}VT։,=]GSy{h@4;XNզMZ+6]ڿ\H]db7x\bdRE8&O0Н飉\u niֻ kHT|" `npNrrS^nhm'F:AH]D+I{:%%qM6 xPCaB$ =)D!`bÜc3T),}_THm{2)A "-($gnj`w"aSNM cg`d*_8Nr*ډ}Ɵw n^]x/9r:ǧ*hG|> =g|Z,PW,6ɔAS!P( wd35$PܬLHaǥtkxG )Ğu;ׄ*F?C$N] -i&&0g)uGn_pޑa7j1{3!d.9ޒo;{i!ooOwp}A:4YM'/hMثʗUpcm=’uNNpod%&q|"k$HՒ o C n9w{&[%a ߞ|+ Y%4s Õ\oLJn3AG[&10 8fi׀$"A9rb3PJ |#4֤7(Qq* B ͳEkjY\H];$ \SU;󦽛p)hf0k/Ȇ;J(햡a.Xy7ڐ诒94ub;ie geR!ȪCB0'ӏ!p嘘4H:4 ,k& q7/b PobȏjɎq,X#oҊbQB {HDZ* A0hCH3' dH(˜\oEbh }s#?WiڠV>2y8#ZS[@¹pd;xF +Gó/#(P|)tKAĮ)G@ (.7"Oe*9Yj Qtd'Vq#s&`-c uoS2[86;+N?rR D5T2NVǧXRm(N]9[A*孲iH# Ss!woO;;*@#N`W)$z>~&#"Yr%GcX(HꙂ6VP-gQwT4+(VT[w!54luh2"чvXttY}E s`BistD工BLʬoLdx=s| |lc2ɾD,Mgŏ_Z*WSPW n(2<Cp^Y!@43>؉ p~# 5r_$IK/tB {&#^-YkkH010`(OþR#ɛ*T`XB¾g&S+/Q'!lV-0NFcF\pvb g6; 0/KpmaqX}!)׫8G;BBƚEhn9N9%|JO©MĂhM v}ّ*+Θh;6ke[ǧL|׶i9M܇}t^d Z#.xмC3<ܴli|35Hװ@[ZL#ԪA ̪0yZN kgQ << Q<._bAFPn qΠp*P8U={ EwK-;El w(\r#=:OίD%+& CjKrL NueL6Ƨ u!l)hLDAs&N)Y}2LT͑1jD؄laŔ- ^a'rNZ|" {Qt|D .8q15U(Yt5rd`RM6b) W\썙,1)S0',Kyoq``gNi9'[8kEwF$sֺ71|XM Ng*L`56,tH7Ml++^/ &GJyp_|zK(Z,I RREVuzmQc=K$B aY$1SneG={p ȸ@uLn;c;oc<8)-Y8Jf[P(e̒i翰MJ`ntڒSY{?n-:* IFgV۽FHxVW_(^y]gl'*v`D J# {/C+YN VT@Zt쇎}doA\!g{sk\Pu.{bԧOX;qGǝOh)nrL or O-gZKa{1Als;ѿf%tC7DO&IOwt:f:`7'ǭ7m㴦2(w42c{p SɑjcK\YN#S ŽT ܛd;dbGcT6rs7R_"`y]T"dLtX0d2y/d. ~p)J-!Ug6 |MӪXP1 9u&=2^RֽPxeeMr%WZGh "m.ݽUf IYhЗ7GA'0ݿ2L2 uFQ.#.(9# ҚN tXW%@39N1)`hTcS_$R64T*)<XC''IЙQ_&Waf&˥&*Rٞf*'ISgF Puͤe7`zᓀ›G6Wۄ!Cl͊^ `(0Vz1%U]\-B'\Fp(0{Rqˑ >Hjiw|YdCrouOydxa_q:J)B8%ȈeLJN [{iqK^]}ڻ` +pB9'+pOXO?dQq_:b{CFF`dbik?$y'!ts [?5\}x\;1cx(g$WK'= 6t<Ɖ2x0=OѲun._/=]^K{yPnr4O㵦c8 *4>>"\Ku]7܆4v̕\ ] tS.z?Qk@Jj{JL=8n2昵hW֪@+^iPeMUN(7G',EtaX*Ls 8g㫋3 *q_7#dq:uY˞xr^\3?3vGJz@R3mmOX?~q1u8s0ue]Qh*}'N1 \858:%,TĽB`eq"{ DW;hy*H`^#@ac, 5W^{3(鑈Gh*.Zƃgh'oŮ_gJs,*ٷdp\=lS|gh˩^BV P3K6x%I nEN$Oq4Yhp>ZAh-]N ?{]pvޛ,|v8y.:MV}/a.g%z' Y~\Ѹf1p|"*ag,-U7q$Ż ٷ tR+=Y\ǩ!'+$tNް 1xsrr4?3ݻ/Gi D3= '3*G7'tiWDJ.`0 Z7 WfIKgz:3!+ ?:R+I뗮Fڮi[}wRA|)yHW$sDaCgYD;߄|.e忧zf俛7_.=`ODXb^>Ч"AzJE7rug*$$K&q!D[çQ8dD0j G>d(vxV41TtNJ=#n]ydA/(B$7yջ>d1mZk>;'B`s!853f!mۙ1p49QΏILpF1i)YpcWlO']@Y>޻s +i3g acq~}p$b$(K@r4bɻn0 P񡀏2xYpԨATϪNF QY1RO-!*כiu$ |q.@_CD}':P ǯn,Q L3X7a ::ǣa@^|?V>Ljfy,hK2_(xUfAӜ@9P<NbE#݈0YUSr*~9FdL-RQm*^me@ҋ\rQ2JI`25|)sAJM=pq 䳉Ax4>(SqRu$D'ъ]ǫc0: n{el;?(nĎ} اd,Ƨ@kg.f+ 'P1$.`W֛Qpml,WU-.(@MVI XhSi|-?**U-L Gv)Q~oӬ^Y?kOEtShUknJBXݝ)q|(\@C1~JE(}':<~UW 5kҧ?!v_5m)hW>Ink/DƟrW;)NL}Pr@?IC-Yo;RKree+-EUi|7o: {OY1e'@-@}ʀӪ8$Jo^s6v?;jޭzɻrXE>z;E*N"F67`~ԇ&R6n0:ě+~rȆ- :q){b L hpUUDӶ2 (.0k I&'؛'(h?kէf? ' q.vOtC,3q3|G"W? &rr<%kJN恣\k/V֡ybDnjV\MS-r><5vE(į1-ntәR>X`O+A'6`*9ηsp[Ĥ٧KsLCæM0/S_=pU-2B[;g}6e kI?BNj?o3LP?(pl4>/| oֹE!sCx'P'9b"Ovn Yh2wxy-΋յ|{3v.Fݣwd2(v9.FsRuĩָ ykY;;\ȩTCOL?:OS*fd4hq䦛gP䢐Ml 2٪.jά&Mߡ&riBUf:tָĠ~J'WU}ROLVj*&}USy^r8f{ؖsԝH?J GM(}ՕTY]7`F /P;>Y_۟zI/fF_ bs G{X4 h֧>P p;=-r'^Oi''0jBsx{fU 83'dz+9˜Y5JTTlrY$͝&MgW?:t 0xì-t~=oq;| 7?|43Ԍ7{uPHͲZ=Fgq^zEFfRwta+GchgE,Z{#6r UB7F|޸ra|M ܸ^7/nٛH|>5n }l_$,֗Z}-VJ'2:E%W]a~鬇W% n52Wӥ\._bies}yiZSK7v ?YNlUba`|nZǭQك~.]8v}qxz@1)p1.l2&]‘m1hy@{0bŲu`TZf20}9BwΛ{;Z,Q(n&AN:'t{!$`2 $%500H#-~'}_lM/#=T[PYXvKx RT -CGv&SW]9og&}ͫbǭk%[gܞ]5i" ~}&WIF BTj Jxa+׷C*]Ks6E+"UOBsm$`tN&kJf40}bs(ڊً6leL9k ?ZAt- R}i^Eit)5iCllL!7j ҚrCO,[Nsk?oN>167…<J.a"y Gi uNaW϶ydZ\ʊu&QDaOEyw/}g3Tb{-bRb:ö|f_ l.}5z0/Qn8ָ[ׇ)?E('YXgSآf[:۩JloҸIYŃVM(! uE.^2>ې\޿Gܯ`KcďVLyvLx'XܡoehEY6P,P~r{Mۓ"١t1Wק*pQ++R` a(PjXM"w ]"l|֧VX8cT1s@qZ" >"P+yR1:7\v~rv`JLN2%I_i[ad2I*htfVT}*RA<(Cde!/n~qƶ-Bj Txɿa ž%`7 BMCtţ| OEwv08VM۠3̓ pd8E_U|kBl֡b_^]I;>~V}J5FQBIe +ͯ,6/?[X_׵M ~% _?[>vB !!oA&xMh8u'.yҶoj޾ƣBgkօ9r{ 5C"![V-e5!;((5t@&XDl 9#kJY\]ylyqs+ [XK157xK]\;ffh[fzÂewYSy-N=X'ݢew2U~ mM}8'asҏG،iCA.(,vI";mX}n,!MԪ(_ٺ UC/$}{X.S7f헑|Ax|ڗl¤8~ baoփ_^LR{I_DMM]](^]/}`Eeꌵ]Sy!bl=#,/^qNԈb$I 7tie4l`, 1f [ST&T,EI?GLǨr)ʲo$p{l?YO07_ \g duKPhƛn얲`W!N-آV.`Zw _-UQRm-\*m->QiKW`'lpŐmQO10P>dmŶX*&`s ɷ^IL#c /\(KTW؞>dt [5tbk-Vȸ}X=@ߖP> ]/N%ϴX$|aι98kʪ32k+Akqd BO<)^tm͍1f# %9@,Ak_1{zLiw 4ϑ3lΧVFfFDj#S9FH:FI=ȮOsYK-{1 $ԃ˖"W^I[4 8j+@ :tǃ/EW#SI?L=MPQKn ,,`UD5$EKꭍ?bߓ:#w[j[$. eiph8o ]ڇrv%VZ 䇶kfR< װ VȜd3T^cDx6(FvlFu>LM?>S2`ť^v.Tb# ji@OfɜQ$(~= tF_vd $|_w3%)U\ܞu%&ݑ8`$ё0f}Ǥ&j' ):>KCyAY#}(ӟluܦu V'P:-FѴs ȹgŒJl)XSq)߃? (i52 DDX1:8L; CBCvwn2Ռ\7blOhU##GJ4W Lr¸=|?J&,bav1ZW[,v {,fD^-|kZ߾7Û妞DvP_<}ծ }q9kƧ†ڍm-x#T_ZRU`7 )7 \)CTSq0NBBBYM(\DTȸeYyL4{3,)D@4O`/Tnj@1|>vh$tGJ/~gYBwJfXWIH)#=&$,rȅ,2!nEϰ,&6"_2 d+%?ij= ,C}0x1n(цY'٦$C ~`9C:O끟sM5.㮧zg/czč>=%Qh`yeys&'OW vmi@ewyxx~X&Rc /--l6^^y\meJxf/X\]~|us _}XXܦZxPK4ҰG++x{}ilym1͏7{dqX\_xmV/!OuwKꇢ ̗ fw+ņ?B.q).^_ %r=lq{ui}-2ٓ*o hvNq[Zt/=ԳM1δ}?- tcL]6ۯ=^4 ?^Tvm)E,S8@(/N܋մ (pё1\?GXw-kր1Rt >1%"(>UuB dN(3ct1\0Fb|;:'k[!dڏ&kWe EȺ`RJtZkq8jɓ)|Uk?s#[3)˾lae&JG7 /]C!67s<RK#ngSa-y-SЅt*r!#=p w-e KNh*DHN4]a)jv@M++4p>JGͤp;P)1A嘟@^j#L%KDkaGuIgx,%K, s(MMiY^|+i]#I\ YÛ2B%6Xdr-ʗV̵i@K:h5nOf2)t8-IЂ255QPO{]f[`!wCl+.pFIS?( Wf}s.! %䭡ʨ0^KG(upoX`20 _r9Tfɐe7zːZ8-Ό@9pdE >Ĉbk2 N1J #I90'<'k;⒈()imhr4WAۧh7j[~"LgTge0n79 jܜPvߴB {6 <%ƌYC]iY/6Qj\ $O%g!>SY\žb;)n~wHrĭwN4F=f||]60 \ҡ_EFң C}aOCʯN,,z9@ߚ6 M2[;2 0!zS30J=:OcCs(Ͽ V(mADU:\  "ts , 6G#4Ujh*>+:]:W(@$*Qe[ ;qN1>.C~]Tpԑ'jDto-lN`54L!l%4DH*`kԃmubpEscwz/Z(r'%ZdOXb[ HR<.c' ؔ-,=[Z坔oP ߇]2'E~Q0QHy"T3KFUE-l(0Ҽ9kk'p1蛠8'J#ȃ_19?^* 9fFx QD{_赥}^Y-vk(7w6=WUY~<=-ۦaF Z|c0T/i'`'?0 xro"D@-uF S T(SDi`гy>Oﳉ^<6df' f}/`U<ddk e:`B ѳ8-["Xu-,ro@_6(:km?"3ff'ϼvT(4&ɀcO[=~z}ӷb)b *s^J TNB.Qtwk" xrx}wl%!CEul#ѻik"e0- M h?^j\{:;  s!vW4L2lU['kí3^CVW~Hɱq =mUZT'H "?u"|A-i"ktO]͵^R&"h3x:i& oe] vT\</_H"q!ދwz\i;~r D@oJҴjcf"wqqѻZ? prLP"s\W pa=0V1 NHX9aMu(qԕ[ quXQB-I-Lj x|j5i}|c:CG]a]1vOɵ+X>)4h.u9$_ Qn mM*ՔaT ;)8]φnڗz,G&kf~F|*G'+nGc)V8 mT|M|;Um ]3:fi6RIp(k*¸)Fiq|ҵLY\M붲Zl.o>[y۹>X3 }=,_.ۂRR)qCLCl/QO169,<}+}/\eG3CQŁMxl/5Fݳf:%q(X* of~"w=O1*w&ҧC-?q07~Zm6yرk.g4 a@ykK<![x4>L)DMDNNPw x_6[S[yT")M9,q?,9/w jjPaS`^d:/{pyQQChdM*k>h@SjOqrceɂ=mش yV"Hjgmd$CZRbF-ItAW%5?0RDF2Ci])Ara<6k\ܵk=_^YXъ:I }8FRQ+Aӡ#7aTXYJ*KK$v/c1&%Z!i l #] LM)9O<4ܞ4X{St|uioKNFݡ/zy!'x`4'\}X@K?X\&z#E{dǬ T#l<99kMm;]j]g c#ByAMD ֕avO@ 2p-/;N2`ĥ72[06v04I2{J2tMN0ƒX݆:) [!f8E n"N{^1_PC5ƥz{Cfp-Apzێg;`(EUayiKW!C4 3|oxTpQZ;ƕw$=S_8ݛs @#zZ[K-d٢b 4L$RAp id m5aӸ̉,yl8HuBI߸ݼuCR nn0,PlI )_'M*NL\FeJ[0%z1u[吮3>c<4! Vxoc0 7./olϫ ]c:HYb n*u2]'.bpRA^O AYͳ.bf~/s.hҖO3I|uoImnv9RCvL!w,7bm/|?}N$? Z;ȵr3:!DiLu7@S!]"B/CwWjh釵ocb XzKN>v_RWLI\/ďI7HXr9K>`JP^G&/R!3! C96"b7W^lrnn2i2 ]U,(rzhƵ+g9'g:q ZPIE}rݾC:w'0w  jgDɻvbWӾa JRmel||U Y$]OPOUWPDXe7dE ͱ="̨gok^0ކukp̆:$@\NKX1uW`NM3 80Nv+i_:{J VgXIF0SEsOwBj(%%%] bIz(u|@eetG|%h1o;GG::46(x)+Fu*᳖*;Aa L`<]\xe L?na!׹ukDxK[[%iĎc"k2Ev"Q06Y`'o[0">YulhRk4 }tDe >ڋ\~c+%)xx#ZA|l;G]Vzey5hHYpȴ&ԃYO|bN\D#6`꺿k(NtK2F٢zu )سBBr~-'4D aos_ƘbF 3$[;AzC FC` ATek3l?T^r 99\\Ds4z<G=8cбf`^}t%La`p?s;ni'G33޽&{?M wmuOfT{ƴ\0lZʜbk-<1 sԷ_//+ˡ,e(a4ltNt)^RC QOrHԽRt}1P Zr@X,eEU WT?U5%!/Yayha+8(n55ZefB6-B+Y2X3hL; A/׵9h"hmUՏכ[/^D.T]UP$.~疞> O16⠇? ztÅA7>$4Rᢗ;/nms ĀG x"@#o eG҆+>=[xr~muc^lrR@D@ ϗ+Pvq곅2%IԔ |DWc`}: Iw2OoۇJbT|;_DŽnw ͑Qd tT&u;sqT貧wvuWHreq7&kbflv E)'Di:%B -t~]߱WMX_4nǰdMll ?Mjl<#q#Va,jNgg5 ͈-m1 >5,U T ʨ-ʽBI+A ^P `8|i,PiYdb En\=?3]j(qyS*,RZ@x!u}wmXĵXDZ^|㊂*-srַy͖ w nu؍9bĦnb{):]%DS =p_( e-@$,9kS7fq_Z^MBW!hUGKB>&MilB ۟Λ3ܖ9x_6v!:Z*zk NEl&/7kn<=w-h=<#["Uf3%[/Eo?Zsܯ[- ̺Wp$Bryw~dM8ൖY´Ƌ=y K/HyģOvj9&jhbxQG1rI"Xu:}(MsՇӭϳUŒ8dtNch!oxiqpPbf+߾ ?u4g]?drH3q!P`F>V_߾ 3׎lObTuL$$x\a3!vg35ɚJ a39.x R(^xp*T~d{P*bskakdLj8p3 ,WLl,bT~ڕ2뒾lF|e,$Р|ݞ}=!ZTY95:ؘ*M[Iv,…w_WԔ_xK%=C߅5=&`vVx;{*QvBmW'duH)RЕvNIe%nl`#^o|yRT.{2} #?ص`x ڄӑ.v1Vu|248LzTL׶6Ƨk{Mٻ,6׈+|87kGyb7•nʘǨCѧ)xdjY: :ǻ`ˆxӎ17YKJt/ݏ6Ru`"UJ

߭|Jr%³m^)>PA+6U@4ڞHr5S ӧ"B$k,]'4`K^ #X4trarCur9q{׷o[*6*fݦ2v*߭}oVzu[ w5Q-FY#_#S 7'//@{^+EK6a$?OW;=zjUN0ZH?wZ@j}1Q;$ҀhH(r֊Rg%tV*YP O?*^6[oOaXжH3WS!]AgOE""SȾ:Oys21)Z41:c'璱 R}eV>3?61 Lb1,{Lükcftl^R#vydX$$/V|V$Zږx(cR/ ?)2Xb SIwSTD")Wu0AtՍb#JJ~exKaY?Juyp@ zߤ0m/rBKehJ~/̑/ {bI-ZP;;|.Cv }ì0L j!0Be=/9!* |a*ig@+zdY[JN_J\/[28 *!Cq@cj1< 7(riCR ΧY_!Vg=[,!Xj}- g#8Fsv @7nZD 1^")\'uΚCI]bNw(uXx&Hx e6+OGwYb!eٗUh)yiSԅ)XW[P' LDYwkLH&gX}of*"mB]t+fk ?gUbا"J^mFtNSOU`(+fLtrjBOՔ>1 ZkV+#Dj!Wrm*3mP>l_i5g"-wv $D)?E Ћfnݮ1w/_T&5a~}#d1 aJ An* `P$FTjAS1' NĄ ;HGSDG| }^!Kzær|̷Tq 2GbeC/d9AҒzlZ}͇ᐫٔAG&- T!m96viu|TJ%<$[2iEbJ+1j&YBt^Crvx Xج017F]&qv)u,̯ ߒ$9$5 ;ksr`,uO1NjŕV'qXѥ]#,vtĮE~/!ſs͢ecE:S4Lh8yS'ɿZJP~c3nl.~jA܋/^uؓbNh}ҸJNq(gg]D|sRU}ؾƮ #Pž᫑pzgZz+Fp Gzfʄ$zLu|x;,`! eJ[w׸tɊ<$iIhK#`1KRtvk}yPTr^ugfq& G?g#WɇoXҒGk?QyoD``MK;Y]5 v,TʥB+_n#Mo4i7#L;r ;OQAC.cvu D[[Ϭq7R?,lIV>!OmTdȬ_^,^ tqE  HOZ$aeG4 Y4)䅳3M SG߬mK,SC4Ъ9"e]3 $/)(Xmלm@UZ*r\ ūhرFQr~D޾}-v&ԏpK1C74јqGaD! pqWeqT3bԘ-S.ň`͏/~|yqYIL<^nNN_f,0=^=4*V`u(1r8~._u#+x$sXcZ͞~VoZͭXla[hV#g}*Y;҈b'2A9_) i8dlW*G iZ@\ `Hl"0Y3Y/^2|>uO 4O?׺, )7}2T>D؈1Bd?BL)bF}=-a*BC8'('L, 'A|vs%bvۖ˂@h/n~Q>wdKC:0ZiW2ye5#Fat܄~g:S U2"U?@StZ̈́0f VR;:^e¢b5).-qt4UJv%KT_ǙoN ݉Fʒ潌( *{D"++MjM}ap<tJv憧rh ]Thzm<;=kT] SSSez4Qؙyy5/Dz<vӸ攰zE$-~%X\!Dkv0{=|`N~u!ѿk5ڷsO(\goݸufqck@o3ci#cVwhv`cO{\^rxdׂrGbL&Q2c1-u?w={qgG$eOtU&"2l5$ԕh8#SPA%!V5cJKwvAn~g1&؏aĒRR)-d~Sfd=Y9>thKRS~BH1$vϚU $iےyХ CZT}|x?~ױjAF5Ƌ VȄ4\?V ³۹H RˉԤQ8DtŜ>s r,i|*F;}C! Dš QKc$3LBG:Q`t(>pz򡴥As4A9(<ſ_#RG1:t\MX-@_϶[WA+nӎ~N+6 Z¬a>᱐M }J'\n/W U]*uoVyy!/{}(fOeKN8-1UCSֳ 'oaGӐ ۃWáY6IJ=}`D.!2a(3U&766.pL򷇝Wd:B#E{Džtɜp kDx.0P.`K7vvmgWmsa.zo݄p47Mh2S1s7-" 'ŶX4ry/*#COꔥMV:uiHmZ٪VJINgj_NP;N}'N 71mjU'3qU꥾Q2t;˽^x lq3󦜣L]&ة" :NˇcNIp|AecX4|1 yޠ'Y҇'K'9ȆD%q;UZre):3 a筹hG %HKX[t.*$N%*0:ǖ$Zy_lJ*r0׃^Y :ri!D,V*M>Ra.+j`DkU4r~DTF߻S%-u`}O~L6r.oAɟ:UW0d({BkR*)1QMG:Ǥ/a?ZN9:}Ug+ϼ;W#^FC*lRep0MqGm0eRGRHwvG?N 1HTb'}CB@Z@Mzm Hm-##v[%Le$/oMÀRW{ 29|7=bi.,֐%x"ě(vl<`s F;, N^)E~i}PkvQY%K#V/h8{_e-fe5װ}f]2Ș֜ΐm‡`Nn#d؈vS|6 U뫏[4qTt'% Ac9Ʒ(6BaFHyOM6& bПcKbWY &]FVU p,E>{RN#?Bgo[b!8sC. y"II jFBp$-YfĹ+$=H1m-hWZJy6<>Y]^ljfBDxC, )X6XE8 I, 6WY[f׍`ӎwD+kcLI~)T.:MkBTC~%lk/+Z*?CE`Y(H8#ƯTϙtȮ\껾"P;Nm]QU7UX$-A:h}OB!{d d~kY[k̿z 6>pQH)Գf2&p W̱& s,J6DLl "%pWna3Ńaʃgu|AKxT—V#O'esė'|;ܒc8 . ߑnGtGSQ%u8H9w杼n㈥gC72}sAIQd}+=KwE1!CuS%"@v uf`"nn.ˏ- 뇿8j–oXؤ 0_U!vVX7ާZu%}̃ҠyVƾL#D)[\Z+Qam}}xɋ$_P">V^gGVVꑖͥji_ow’t"x/Q׍5Nv9KnJBR 7w9H}y +uE`Gqʸ%\:Iځ+kxFt ;dyН|? dGđ*Cvee(gIes@wzߟ09גors{~HK0cfS{uhWp[ F:GaWaͫ1:QjK\4"#}QRgU&(Whр壼&%_2iFs9Z%'QTgz? JˮLTj:$Ufk_ďiqO?GWt1Oɩb(6.Hў ۷A`Q2kU(fp>@UgW>yI\"qŲo lDZ3FB%Ud‡<_vDGk#++$;aғCڪ &8>Ɋ[,Gs)!S!N6q/ SQTtw)nWL[}IpDS G4Z[!Jdch||MՏTLYc~2D$b&+z(] FܯI-6+w|&w^&I_F8 2JjJa0&z)V~]Y8,m/A -W-'gK*fAcU V$KK7fHI꬐mA*orza*Օ8ǩSixm<͐_Ӎ?ǩ9w7 UT^T6Og*Iȑ1BQk|Ԩ$g0>ڊW'fK$~bwg$m !w"r^J5s#;Wz wt9rb]>vqs}1G8H[֘RIkV~; V]-^FyVzQ NM ܠ$ k0yN$t U. ¢SH-dhjtB:͛|V9\$IWŧ%]+qXvD|${t?F9@>(S1Uߩ(e9hpoSa,ob;oQ~o#4z)(t ̥^ iV&L^HfB~S'0ӹ'LG&F?r+^)z )=,/`UT6I> $xݦ h’&CtֱDE!c9)S _$NAEL "~A4LiS^iQ aCk%LCX'I2˹HB܋ז(7j==U,a*ti,5Vխ sq-~6-nK"׈󙔰u (BnB&Tf3MeC8[1iep2U!`j+tP`:"FToO& M(s$p[ۉˇљr QۿBq7: +7f`%7B> yr.\<1DR[0xZF ]7r_6kRv)(C^xz\a}t# =mFw0Ø<"cD,|>1}.#@#3 >O$W3c=tLG!)k2˿)IMMMA-PsDLmodh- !=-$%`R˜T"1Z.t(冠m~E E_ U` ?gfwb$4z$ xI=ViE&|RƩe$ @Yzt:4.)"`p_>}ƛR *A>RH́صb 2YTog%FDYR}NKq7p\E@;tB iC'<Ș!:@tBPeDYL: vO(j* PO6Vt vhV1r].2m0MXdBj*\I3y }"Fdv>Sna= nQY҈$Lp,[Ғ6 ج ZMC >fMlS1fuf KF(OL2='}v!y}j]_ B */LcLR"[G #*}:4W^!]'c@$mD+ZqulZBn)A?nP .+,vH{Aþbs°hm9~ษ%U_/„2Ic ͒׫ 5['$rI=ܪ*}ޗ ]<.ߣT>K3w,,oakZAJ0ZM9ImfD(0&FX.[>TPQ'j~ "菈Bnd`<6J&|^3༕cuøoEh\EBxBQ#i.F&=KQǵ Fj7,ʒW}+J dPjtвyg@㧋3P^H\MQO~8 SIfؔYJVHHYMe$V7{?_a3v=ڪ҅foݕ I3 wlÔܣ.J yI6[C cmEI |B#ڰ4`I\X,FaZ[(D0?rR${^U|6-.-ψ xNޓ<9" IRq qpb*bzeLz;1?IFLWYtMj>"/\H7-U3Q 'Z+U~Qrq `ݧdyE37@'4 u\HY= ǍO0 hF~}[2Bcn| j[+%,!~_i*MrG(ܜ ZCIYOm~h#RS{ئђ@B+l!/k H^4UG*Ȏ0u"oL:f?W%V8Yaj.TDٗA+IlH.lYa,#1nzqvҮĮXg+Vb -68hqk+ Y ;z#6K7.S_>g)$7C#J/bsD@ `E(QNosywL-m\>'}Na[EB)ZAx+_O!xeO@*ͣ9f Di(N8U(c7d5THɎ/R(XD.p +rCyVedJQ6YE42LB2kXA(*GQ6<,dGGYǽnⷢ >%l?pXE9ڕQ;t __FLiŕ%I@IplfJ[%V[&6{/XYzgtX(=>W-bj!l8CRvQrFڴ>ZCS[#ffprPwwu`%6ZnBkHt AJ5lQB+? b4Vx0>`9%Xb`H{݅.*E[r6 \QJJGP iJ\.h$e5vСZNK ýʴeRF6kJ'Km䫘U: &Zl aۯ,3BXֶ "ݬM6ϘеrU\3)~$T]ibbVOuP%ɇ @Ks*V1$^4a9/ ujv-:v~v-9b8Ƣz]~v:@ pB(9=OrI`(ш=4P:!ժ N_.@3@bmk̥}yjI`' &`?4E\81p`'~k@leqO@oHuNZZ;zdD=992t\bCa7)nIY>4IH֜ҁƶ(L 6Jj# UW+.VWjy~n~PW5υda}Ԡ" Su=bkD\pΗmzh9W8HrZJaFs!rVr@} }^ijN) (D1a1)Fš:#/]ASZ仩K,ڼ[60ch Ӟ,ZmX  ̰Me0f`aQd[A̤a3ݞn,BP!щd@"z/z^Z`٬i0(kVrlÓ13m7҈X(0I{HcJ# F}ee֮-X :0%he"0T osO_zxWo,G}EpqdGZxk)[xՠ7+O$vfۑ""u{a10o=bUGQB页;eG-ߵD~EA~77ɨ(T2{^^ng+a<6S,N+AԚ\@b#iq'fI{=3T(vg(tQҢH!݊]Ⱥ۱F@rA-&ȇM5 Y}h]P;~@B RFkrNP;l:[p&-,e5 2"aDPl^ ǀt)tQxp mHj8 {eMnY4wAMFf-FgzjʹO1 Z}6 bibzP]Ƴ\L$'lR᢭ -j;kIq3L~prJtb:oGBc&}u2}trldVX>> 7؆[ N%w ;߀ %3XH" 16 Eچ(r$^TrtI]] L9W:_~ Il&IQQ̜^.Uh|,vT٤& \eVpWL3*o+@L{`; ]BG9q'ʹx e:* Yqũl |P53IC&uU&o~5ݡ\ʎZҠO~ o6\D)ej#TE~[k;ujv&G@1vޮ%.jrq="PoPת; Ю4BJ>IZCKR6=ʞ(UM hɕI pƿUuT9Jށgқ 90O%\w~jR2FS~p4cBs{s7Js[$ݷb(3 Ul.&֘p"I6ڋM\[-//0ML 9DIi!)D jÏ ][7.t *69ҐDcd%*8Q&ÏBIRuL i2`rhDiPߥ6G>81&:$-h'I^ \V?_<{}-v֭? wٛSŝ9{/nܘS1{[x:Ӎ]2[wC#dH &!qz" X|^sSwͱ6W.<.-o,~X[]^䉨 Kqaq}[l'm]Hߠ'{{:o<{j6^zBN"'6<}px/Ɓ3xX: ]nτ .:" 鼲$zpv 4gZa!jChd-+#eʺ`Kӆgg`Ei%i c՘e|OߏO(iĎ[&mb6&Y|>9ȒpNfC}2s&:&GH|߾GK_=ukc38`Q+>:~u8ӗ8DDR9韌7~? .ƴ (v6磄mh^!xxಞtӢfXSAV |5tZZ;=.gxP܈` 9l+#|D͉,] T sG} Evy<_(Y@oH34 )=Pwa34M6>G]Z@Qם*wo_Ű<k׫_{,I)>Ŀ>9w8jQS!q}.-j52V"!Bq'C8Cb&n/ {rR}z}/y5OY:djth8'tir fIT,/ϛ(Eʔر{8'vFJ#ɴ;ݗw{]9aZ&>8:yOp&+c)7M+0.|˯8=!k g13fShͲ*s8MK|8i,Ή"c30C[0{e rK괱ɒMC8M0+5zؔUe~F _?B>(. g7 ոϜ9jXTMm]|;[ӓNUwUpқr$H-d5Z ,##,gp|޶_ІT_ѱxD3iC !KgjuHg qQQqߔ-FqnwB|ˁWňv+{zLh2t ohxM5`)V . . LR?ZZoB5=4{A{>";U`{#,.*mc c ٗ\TM;ȓEl$3GZ5LhkˤόDi,f,oEKLHV#~ݔc̀u8{\Ċ[Ee bc3 ^`K^BY**ziX-J|aC.{{Er ()@P"а쮱~M!E!c=E@BI]/qɷ%2U8ma5BI'%bꮌEdI2: QyPLƭ7tbQ SCbbh߂WIOFg}JU'֍e O3ͨG+kc&=5"[t H8ōT +u8PXGzH>3IljUM$n޴Wͣ3&^L6Z{y[ui*=%+I"A9;vL!]VgXM15gƠY5dӣ=]f5'oi+aq32E?2H DCk#ƀ~|J4Pk`?Yum95cYToDDdB 2uGYZBk-!7JG/C mXE|Q=8L*2(cYQ-G^Ctk; Ŝ<1'2)h5O{P˥Qyppf}NRo LK#X `@&$S~TM_߇zڗ4r>0@#X5BP*伎6>~S}%eaLpwS SconѠbNXUjABH}vVaF(Z.^fμI{Y|Dl^u{8~&!*VEtv !^\84YWBVE%)?qn%#OO#ּ6hP~d5 lfP E<@~LN$ gpv a'n՚i5z]au|f$| 0{1ވ3HڴT"hh?͈y2urbflvl~xmV$ |r  %jq& rzFc V^ܮQDW7GWGd2F%;7/oTX3JB\&.6\,./pPξ뙗_ ࡐlO8V/T\mZpfh.296<¿;>rϝUJJP*oh K&,[ʌ. /W2>8{SwdM=H1f,GQ /K+yUlv.DC"Qvt8h0%1b],"&ӲGkC2{G6;e&(<|.Vc)޹8y-b!,Fv7?=:ٶF% ڠG|5c̀pf4\l巡o(\'gW*}sʊgcܴR5cg{/T52S$ hBVDI]B^>PR㏀YnJ a 'YB*MoG;"j + iczp%?e B 6a8Pņmo,.<[X`,F|惇rq,l|s0?L;wpPGe  KjxLC2FB"tZ/G^PE^j qwAGvp23 Z EbSZb'IG%}T~2HFsO C{EqCr @C"x( @2d5 XVǘaVKYE5Wqzh0UX04Fa#YKQ~=g)T9U /3Ďfu2LR"0kvNXG;VZ}J޸0<&! ӠkW>\LiA9sAA.4Nхט=tUCt>0`'3"%S8VQś7\#W~}y0^۞}~ߛ$D爬~ 2־xgΦ[ وtNEWLWN F>qt`6`FJGLfcH鈝7`ީ.q~8IuT Y%.*)  ?up@*R =j5Q,/A@:cTpڝn %wY2k$ﻧPC6Z pL nvz8nszU]w :,t[!gPGv0 .hi˒ǟ}j1)^©}H7M{lj7@/U<~u^pCo^s}l:P_p.Pފ`5 vG̊rc3q#3@^[,BNhgqDsu/ボRk&0h" kW^5kN_7'Ɯ܈Finx,&3pJ# WXɄlSg>csF,!WUf7u5Qk0T:*Igx!qЎ5NwLb`@P@AT|rtEK6en6 Tmsc0S] |M D=pYky'i@pnKE@pg#\0[{%=F6"%QN#ؕ%}miR'9QroSiê /ϜΩ{ 9K44BDJ7ɶD,h#>.!|x~>u`4.?x2X۸Sb`A(V`m`0OTa"m7)V%ϕM`B]Z(:=3J1fV;#$ ? !\+%~LM&y֥a'nh% {ȏ!yT8O"fٛ5fY>8jE#SR:2+WQFztԋIQc۫/K9Zˎ ,+Ig-ázp;2wB d?1ᦋALq7? RFp='~+`K&Qg@/1JB`؋4Wb*%Svc術~&(oZQH=dXS6DgA, bzf^}:ѻ3d*eB X[*I]A$[r-a s7SaYB N~l yZG9TP6Β@ۏ4R0 cƉg0A/RKP MoV O5HdGb(X uQ.H%l5!TԿ Um `؏T\ֱdb=h4K%1 :ӊ5e?-h2D9VK4T>S__Ae7i4o7vء 0țD,|&Nc2ٛVtw=2ڢ.ғ25 3<6܅jVL-5š󧏹 rXmeK4ɂJβ1OiQpO_*/l.Y̍3Xhc2!pYIuPz +[]=ci󘝛A154)Jw,#W2ul֡bD͋.@e8ִ5Nw06Oy]ø̋XnݼN*vxS N/.Z:`y"GNl;OL[7&{u(SkVFu9~bjEF![O`4o Pe߰B34PӜ|aFP[WNhF٭5tB* `;J,Y[H yь͇צH2:svkk6OE\9M_:||Gxۻ.IX'˶ڥJ pZqD AUf*ո~.\Vj@W%JbX\"4?ȑ鲃8S@.=6i:x!08V֬Ls?讛2m"vg>jbDf(Fg VYBWГRc0[{눊%̳nDјKQ%+x֏sE׶/[8)*?0bq6n6[  ԾBљ0ٸG45/3*6 ۣUO:Eeҡ-(#M4'=ǍLюh/ΛH ʟbfJY˼'{4;a)S۳ԯ7^4u)qįW,NY g&Ty0g7ihש4WW+t v(*HW׶f&|&g~NouKhG>EfMƞ -GhcsVONMm>71UN&UP.ǼӨ٨hŠRM uFs/gd䤁G0#Nuw9 HijZHtžۯ R1[ S;Y-kvu-%8glkS3`V6T`>{G7+{)MDbDaC tin6*,>دW׾qcyqukkKK:ʱx nhy-2啧Ûtl~c/-,.j>2x4k6$M׋KϞ}GBlu p5eZ\} BV/h׳Ƌ ADH4p i,X*+jirO<"őRC~a]aZ[_}93MOtG*)\?充',#>vN!s0NcL,:m\IxӴ359}}9ayhc?GR}fcL~E9^4_0Es$وۑԈ' t,DVߙq):צP-QdFl5w.SBqퟁϳ;k\t1=\z$&Iϗ˛?[(gne84*{zZNլmVJmPa[;;!G'ݭN(#jkg|9ׯ@hTuZ 鸆TT囩ZN,$ IRESHb$ & H"3ZHFOr(K;Δ[[/-)+87xE# Ӕߐ—+%N\ i] "ğ,fd=|kv`fw-I>) yȱ^>.N6D^^4Vz\ }iǁw=KVDNAxp4 #B<x@XMW0vG]+gU^."- TXgi) H>hX,ӆՈM5tPlؐ"'rЇ"y0-& MM3.e՘6gM+:G| r0$} e_97ӖkkB4'^JT&#q~76Ѵ[.ظwrQBtF%* . ţBԆB 1fu 7R0ڌh=lĽ:odM`ni%`*{h.~ʡPLO&=25&b]19vkȩUpG͡TI1nrar6`,Vf%yj2 ˿(7=HU(ha2D 3KeTQ U1,XX?Qj]ʕl;KL^!%ݣxkcUD4&@G$$f"YYC-:qM %[qJ+$A+Fpcw&X\LtxT1)&"[nCdPz=Sk\daoNNgf޽{7M4K~{zdRN99' &%/EC>Zt~-<yHQ\X %u_-ܲ2V> ^MmWhGD?z`Jh}=$<ż6eVS Z'%k5Xu}Oi>LdFx~1EzֿW-cE}=vQXenI&-;`ycʢ.,lDwnF*!~z7 T l@QO?ǍyA'FVqEfGKϩJfKmjUMȍ" .bfn T+CɕOB.f%hĔ jR!h6{vwBw%k(gu 4.VVn~;.| f.% ŠEzp+UsgNeh&UF=GZMj:pD(sbt`M<հԐ$bKg10!+V|[Ϥ&؜BF4scY{ N١ΫT>ocl{MitGׅtý+Fl˻ m>ƅ3nOF-htF4*կ>M.>l`%] 4=emo%k{9},_*֗rNƅ ?68\ney1=;pi ȍ卍'ˋ㥿.=[]U5ml.<]q&jPWclm>odt|acZ\_}ccmُW׾YxJݚ*־YZYqm=[Z\<^X7YY}YXĹw |dQ?*k|5Xn}qRBE\:cv89P6?ؚǹx(Vȥ4g369%H]]sA,yI?ɸ8ՃJUI m/'ퟁ'gKJ%Ը&x3 UkMu-Qq557)ޤY5-P3-Iڒ6˹mYt@syk;CKzQRF4VMU@ b@=$}~Xp}XqfȜU%2 ?zr_ZlR8L"n^*0 i\U kE)fUȳ#l*d5:x!\l5,FYl#N=P&ٮ'?7¬kEe~ݵ""SjIL2 ]`b;NtĦP!VM1ݝycϼiO[i﴿.^RAW9 MjP1k(Q,OsTzpυ -%veȩ04Ը&)]2T/Oͬ^&X\bunzȽXçWޫ|}f8.L5dTy9c [—T>"uC1(46yTx U$ڧ <ԎnUɸ<{sNy[Lx"s7W}kKS969R8Q,q&PfV2gGVsV$75hgZ7ƞҸU\ n~'94mf G;,{#*U¸?Ϣ]G_MQ< ӕC^M<>0 OA)Knr[o0 ::$tA9031q7P<0_ ^CD+)2#3}%O\:%wss,8z'/Ek;5cNa3amOdDƒOV/BLW9lD bf*nYG`BSLڋvzs|2ruCDc%EՆTfF9[gbO;&hocT$Fo51Qh${ĦξY; /=?Q!}/8ࠣ|hEPK)U@/lZXI =*rL5)9Om\_=nZ17 xXgQC6HL)Ui?*z$,Lx֔e_Gx#{njv/u0.kKx/>Mڗ$?`fxn}0x&@꬐pFhI2iU گA&ص+-OW'%aUk>!b9;kȯ5>mvR2"%CoZ`Y?{I7VE 'I/ak$i!SpԜ(Iπɰ jG%-+-dH,.4ޕT54/dZ>s L싇ŚE+[ZA tLv͘~{iUC ўajRh,u,M*!#LK~S1m$;<1n `]4hDђ7*`E|oʝ5$W}e[QB],$`ĦO}*i߶Q9ӐGNlp5Pr֭ƵMn7;(=Qzhuu OFˤ$d{,jkKLƭsjOh߄ l80bành9,0=^1ɷT5\AhK@*{A_d2]1[f1?ArRعRFů\ >nqDWGXaf{=j[3K2_%xq"4=5c0xKfv2]$ǝ1<27ZS8 z1k^Z7"qg۴ȪaGو 2*ħ~Ejg-=('Lh >]|/^@GB-!8e"B=kp0YNb(P/dtLϳӞ>5[QKDJ2~R"/HS˱g\]rG'|l:SΟ*/PlYD)ǁ?;/}e.~"%KP"hH2_Q'Tn~1[߹3h=w1[ ޿ e1OHNXSuf7Cg&>jt9b;ʛJgbfԠQ~B>5(a'"(QKv!S)9e=A倃σK %/[ta쁐7fm9j_WCρ3ަ3$1A4d(h$2 e]##7m91Y3 &y+Oxw1Aۏ3f S+ӛfmt}:{!1"s+G-8,A52+C6Ҙ R sMӜRO8i(f, Dz%aX=Q7)".ٴ !f3-XGѬ.`;DЯG W:4 ln sj1j#> / %~);zc#8b#pI{h& .">5If w7bGV20:,HbH~L7ձQ~ ~FS$Efg<7H9~`DPz/S6ĭPYDme#6:fK-J(Bas|;X{OdG晊6\,kGӇE~ԟΚuA} \D㈬+ w E>X6n6Hg!xGvLc!@@pWR 'v#N 0|<Ġ-Sֿ;X`-KŔ MD$8P"7aF!#&MeU oJ!^!͛Ng;}֨ݢtL4:f1aXIf]͉%Ibxy='aG#Qw1icF! `.p"׵ rx$>9y'Ȍ\08,89'8lzmٙ.#3xnMc'G~r(wFR slJ*x)u8Qu騳cP;jo:y t%#-=d4 b#x='w']K弌90+sG!;j ں-+p}ϖkcR86ĵ٤/I5uPW5$qrAʠ~"Dsr_@TS'֭p"!O&_rvB]+pkbQ֎EUFPXuiQ?jKY=E0/b>0LZ` sE rmxԴm5F9n/B"i,ec,qoì!JwON:΀ _B֋i- qx_0YཅK)z ܥ eI6؛Fs{^TMKF((Ȍwo&5+3W-MJ'~$V4#_6}\ ]Q b$̝ArcҔhToȨymXz{Y-Lՙ>!me4txh@g<|PwGej(x=QGf._׊: o2Ât%keIOJNMr{OH` fF|^.U` ޴يGvUZbees/kkO _nbV%f>,;%Bd}xCmazO7J[[fD4oSvr9~u)Bb~럜۽#ru/3I)CW}AUbJb/-cap/U${bL.i`Uj$lJ"}49eNpf̆x0  cIRYWгkߑx_+Aqps<daDb?m48J:bd ~$SPR!EMolȉ>oXc[ Īn|h5(9.*d>Zmz%a9k{˗ASF?;H7#CyR0a!bOnUL$d^3X#.Kqpc=(r@1&Ɇ2jvr8*V";A 9pNvIaqUm#͌մq%xax)aa؍Z? fmVPnb W<1Sjs5(wO"u n vm"8,lӍ~4XP鯋-R$ yP, oS3 jKu^8~T㤃Wcˑk!:jzcX h>S8cx5XieAY6`MrL,FT{#ߎojۙ|ma;z4paUS:ֻteǮ @1>-cdv{um44p'q}ÅZ1Ja`AT(縶q>N``^XX[kDʡ,Ls_kã2@o?3SIa2;ow1e+-^ bSbbznLqOQDUK8OV֐s.RBUP&ERci*t[@aKI_u,y,[Szhe w3O!p#@>*5K 5ukX)؜赉4G| 5Q DC±NtqַYp0V`>mwb m  }Űi3ѭM?>-vtQNeϵ|ը.7acEj{,TcB~i/R)5jdďO};_<ˡ\򑰇Fx~ȱd.e/R}˂Tk~wrc1_92r[I\u4Hܳj 2vѦ4ˆQ12 }JݺY 2r0oZY$3.4@%.oBWaQT!R Md8*3 Pǀ-Q`=ER@J@/0āԢ,IIo;MBpJEym*{re?i |?t7nyoy?5Cv<%*?TN^gݤ/d|e R?˕LjyƊbJ#}6RNL= "E` d34@z1XNW [Hm.$ ,5, lxOZg-"+;R|C J+mwd!Q~}d\zT őJ/n)i<.B#/">@[}wwR4zK]'-CjHץ8t>GJpy`E=J0q &ZgZ_NEm9ѧ Pfg7%Mg o9+hąeP;ъf3$Z-i%RC1W7fH)~?!\:Hų⯣H ?nҷ ZzzXabW)Gq1.[rJTWuqCX ͊a֖Y>6핷Gg"5zrϟ22ȩ T%[P&[%*J?Q%YSuOMPWnc М$(欋P2Ya@)X~={;n­Zg~EٙT+r4^fqPs,b6+b pO7wͷ ;;^VCBQʆ*Z{mօvfN6)nxKPw<[r&{7GNT.?^)zxxU-qhD]zƑ?۳πEǛ#3/?:!]?}_2˿/ ؿJ~7Ɏԕ'ūTh\ P8VL*-De.%'.W~Kxw7p~1K΋x%%Ƃ2E% Z%o"A}ɉ%d!.?jt=>$ŀUZ}ckQmVpt=z>UE[:,0$KZeQ5*H%G3v7'~* ]8( 3uaW]#֠S,C?v"SLeUv^5Na,&C:ׄN*RWh+4l-"%A.o?^/4}]2 .Je(UQԱ2GmT:wl"aBg`!0"m%) GfGGjhuХNq^ʾHܡ jxkım'dSڼGTO :3%D`F4T rcjE8 ,ruŔq_@VI58yc\׏nP t`KER2d .u]nNǧB,i/rMqFلr2"% [8x' $iBY^6&sQD`CS5"->r}GHc nME \,Q# ejA^c_s$ <ZtL$CݻQm򗠺Oxhos[1RD@ X'YW$N! fm<_Kd/dpGG p?diEފZNpV?ǾbAcр4M6A1O^xJQ? $$E}`Mei'S[܃qUɡ&s"Im&F@0l_'dT,ڱ4=Iv"tbsCٿPTDd͏kQ=̒E6[z t y1zy;06w "r' Q k:),[>x<)HWxE~>l -HR07sL>W?@yK;h0V0>b<& O JHB֥#'|z7Y`+bchᡊDTpohn7) cf"A5ẴaH ҭn MSK:~?1p :S3 {O.Wm<À+p;%+)P@$Gq W!ABkpIb7T_t5=>>5k8n¦7xՖ*lT/à>:St$߽XOeAnB"3<^tHO3bʒ:xNe3,Ҕ"ƻu0{6`ֳ"ওe}-Z~f_ RT*ѿ328,+nwK+hT|3i \*#WmgeiͶGw1=9x*ї|Ssjp[9'V{\dU;qr>>Y &p&Zjx"va~j:~– MM KMp zƗCc\NxǕM_K . Cxo(E 赌46_9A?S1{ [c]s.KXJUD\x7+x̩"<3+f/V*8cNʕj?c4U)r祌ZBV]>]]&^|d!aG 5uMq0;wq4SO8{=~kl{qCl81?3sjA̽is1l5| MFK|@'G{V!ʑC,c}Wll3+&]pœNp Rbj? I 9…w!R-S}"8/$[ #-1.(ŻHPez9;p7P//l B%: ߨءK 巻pPH~wSDXHGgTD^<V-8LxEd/?DŽe %ĥ0ت ?~/?A~mF5 >$/! j}rJ-ӂ5#ႄu( - ;ʟ 'UDw^ E/SZZ\:n9Fo*q; uSsO舊ჸ.f& ֹOU o M@ye7R/Mԡ l0ʰ@O<s˷)8[ÃCT{\H!<\)u^(ތBm $G"Ý\UjxCSںPb%Qw?U`5[鹗"vsB ~">rZ5ֈ?" e2 AE4 J#O+s?s?s?sߋs?s9o7ڧ/^l,BІSܯmn# )pw(QTg[ߵ0E υ>j˸Īuc)v&) ǥiΣ& *9ZNBZj`jKq#բh@zm3Xe#|al >ьgU$sGҤBQoܶ% w10Ca HH}DO&,C$P7xA(I"`XPׇ8;DQ% @*P2W.m T幅} ݒb$?T&$!; fǃ/\_J]7,]b;GXp;v,V PJZ"D-%K‹mp3Mc{^M\ٕ&i¯ME+M`;3"eNIH?{N p9k$ ]rC\Oe*iHoCTI.]~Ԑ 8&F8KxB!&1n S$HM04'moԬ p_9t6Sc+P=>GM<7&֑=w*8;LcQF3+I p.¢d]|o|2]"R ˜ hYʈ<&"^~&,֤\̾˶֘6Er~Zmr2?p?BOrH7Gi'&s_?\S迼b@>ȅ, [NƘtgHΐ,LҒS;YC3" |C$D&*p}ܥ_>\=) HI`$^ꔵ Bp~#|Ho 7:#@Z~C{0lùyPmHyN$!ogq)'%bz|RE7D %{>*uxF9Lj=:P$;_m>z]_T,&PT_~_^^`==%mTp 탐HRH|z7B,#=Grۤ;~xtLԾHRmDf娐"tlply#l]x(VQ+x 8&JO8{J)*l0Բ`wouFog㿫Vݯ1\;>H-بh:߭߇HJGW Q|(%†gQԞv`&1=v6~`SI"89I@|-^9Rnc%jNܐȊ%y̫^s>i3([7}ⴀ'A`DSHG(D" K~J,te#iqX,I>6}lP9@[}v` :Ke1>'M .~/:h;zY= hXAɖK4ߺe&n5ʩ A#z_S{g :́? Q@@S3ߎۜ0\ufnQ`0#Kλ,0}o_.ovЩYQVKSXX\\5BuV}Xpk&/wJ>33j#sӝ~cBsh:3 ^.?.WLǕZeCo?gg~H*f=J\6!"w ʍX(FuZx JZ3 LY/!}{[F`:CĹ7rSGp1I5 W*\ $B@,mPD@-'WzMPRt./%v\XX; ?h':gu2O9\K7&D:Yv %e :&$udfak͓jX<,G0$WULm%Zaع{5 *-*p^W+V/MvPPrüv[.[ً^EuІ\Q&lza->j 6[==a Ԫ2&>" A5a j;J)yYn ?gL>keaĬ\= U-S5y WK_F%5 {75 &>oY^-5YX;'bfZGKsrsr40 -Hfba&F(6"[@] J06MOvgȲ&kwHt PBPܦ.\%S-|z-~4Bkw TP4>áI6'#JXy`2-\aũZr2L^ԠhMWhW`U<Ш`a@ )7 1l#R:ND#)kkuZ>4ZdP# b2* G@nzdQwf93';%(J~`B=ǥ`]X x顜Ǟa~gFz(Tp,JiL-Tc.IZB 1wl-JCG_L7Yd k*+U[@8%0`2C] ai x(/~H<8nrJQu^u[Ιw9҂_B r?)(" $eA+.!a2XK,v/{p+AqgܬV82aF#^Z%dWpeU1س͉L6V+9Izq`!3];3K4#a6_gJ=i+Vdy($F'%RӶ--Ѳ7BgJ1m'!X6b1RH^1D\2&?V?  t$kیI %qL;ψ`hES՚!+"d,q0RDƛ\/6#T)UȸvXE_}뙖 )Pl3-ȰmmknCFmHވ Z9e ~Fo= =vfmDdmD kɝ(mfĶb؁дB¡/R6%vM;cRXd5s.s赋]C2b_//X@5%a\Ȩ(xGC ə\F}AӥHlTa)2r9̀6r֤ Ւ$B)pwLNb*'df$˝ߧŵvh n2c; =~8qĠs~#hئDOG(h¬hJC֙2؎&Lʙ/:0M?0Ar3睒zI{{8aMx('xTČK˘,cseK=RcFfict{Cf[Tqf }VϊvqXf׊pԇ+z&7Uk|8#h\G{caN! \m@# IyfО {վM$hc=\R*ʎULc6{Dg @pjEͮpNA*|ǾZ[4]3hJ^xJQ? $2ߋhVm7eg'`\djarxr(TEnQ5TSpP;QhTi>#_ Qk Kq3hzP|\ 2@Sη| Dc9g]=DZ͏kQ=jᏍE7c"|W ]jA/rnX.F`1Xѣb|l~@q8g>^Q[u}(Ɛa^õS1$Fdەƨ1Cl,o4SED/"H+ ݴ#)X5 0ց5ruiP'f\K}zvt3bE.XdEˈz,<9_鍣kƻu%{g Ina +r +gŭNuie^ horVtz Vti]&aL$V*Eo Gf`W)6GT?'H~~&66Z )?y2踾r#^pqaȃ1Ζ#vmQ@D@q5* Ho73v5={4Rw6s ﴷt>|HΑ*w}aT J2 t zr #(ѭow~!B%7DI-!L!V(7nǔ=Fٍ"*ʆaNb ̚+ @ hܓvS wfZQmKf:ӔBLm(4*;@KlYӍSfc4X?ņOW|j4aHG'8\K@xڔZ,qkwdWWK%'|O<֊t%:s|TJo_wg~FKz\5k^#ϷD_YU(1ho { 2B]B¬16Q2mO&\l:făi2h*@G_&?uۤ7'@S[NDG}f}pk Na_@!Z<7+|`zL| o؀K5xMߐ2b`7ChjN L`i,]H :H p\rO.?XqorOlz!Dl7H>[Ϝ 뭗h+k0 IVdKʘ":^)WVݬh݋e4^($2b\l~m#.[b<_?@de3,Ҕ",K;R >~f_kK JSY^T\FΈ?-L^a1| ͩ_M~bFǶٗAm~ބv6,/@oϦ!_Vb+1&_X`"wmm-[/3z>oooo4=ygzkK\Ҝ9>/H<ξ$d%KAMPXэ=b1蓄| o ~f(hR9P D**y *ԑTrWf.W<>ǐQr6RYY[+͡SU@ Cڽ㿱Q@ׇ} ^k+?%(/:"w#X¿'`͓22 ERj Sߏ21v4eh㎒ZLlmEMjpꥐOy,xA[) dj. W'=[tʴ\65p YYAN݆ThZWߏj`*W|Ѐ?~ib#R=K0jdJ{U˖kw)F3 =.1L0̳Ά*wt-=mfvSM o=] +}A?/S߈"'SD{h;a""aS_P +^}U^&Ѷs705!ТlqKRve&-kVa:0qcC˩_yR&N3YWF݁ydnc qm=TGyzyZ rǚ8X'Dj ݝګ;8mJ2\mˠSRMbapZ= <^! {~G=L%8{*&=%k߾:c}>T?^'SY4c"9SL/XBbLOC[ePq\bKS$Iy 1'=󗀪(\*rȶds8jΐ D[]hϻ(|9ItwH]5^lrOv{>vw0q37M`,W/.;Ctw3+i6܍a^@s|'^&ޱ-Wݾ7w,9M9Zt< EԉW*zFfQ5Kd %r:kjٱʾW'XՃdN̬w+Qu Z 3Q}]yU*̬NfFa߸'+G Jp=4&@ 7ǑToXWX+ng'` 59&W'R". *^ 7nAw aB bA=C|l~PӇ](WcQ|WxE[m hTuL<`C$OB1``kkV}i=999A"B#ʠxN]A΃|q~+q `9L-+1&bHm,\RЉǣ#$Vjy|!3QC_P\pwY̧4tOȨXGcDo~7*}w*_ѡJ "^y{r >-m8(x "!6e ;(>1)P 撫hO7VZԍOD<ErzT zS`P !>Vk[~ Z+p|:ʨ/ @ L⿯>;{m>g!hHo.w//rӚ ^Wڤ3lűhܹғt^nD_&y8ۛ(AK<+Y UU%`GLH$Kh6\P 1YuH56Z9⿯&_VW_M__tGR0h( 5?b އ~XR`$􅟀NWޮ?z{}ژPN(G*ĵ̶g4[$T-alR;z 8[ %S~%4$7V`ɿcHmG 8j<1RD$PdDs~%3Y\1%˷`~oNt֗S]~N5~* g+ʽs7s7s7s7s7s oxx8N?ߍx3"|SۄQ$Їazmn1[/ͭ~֒ʄ̜EnpO?țoEݯS-hd<51XR>+4  Ά$y3FN * l{ak ~ .>2\s«//[J[._6:k R5:0ݣ'S¹ Oj\]Y^~Quy^Az!$`u+*M9y$uy^c.(uu*{re1kir9߫99991Ӝj!r_%*z=ŷ7"ׁ…g7Nr D4Rp0wt^F/u-F} iUr `Hτј`Q2\WU%O\[A7@c/)= HsDksAf9d#0H]KqI 񓜓< ;1N\[^(3#'OL#)#WnaX ϩLߜR$ lOii\t#Jɘ)׽г՞IDZcߨoߊGR/l@a<Vo.O?ܫ.999999o?XpA0KNCm^2@mu^ZePt;Ao 48>\ݮrLJK s0Kv4!wDjքָzsw+mEVLG| ]O݈U6awVKs[j/jվ5Yکe3QmlrVXKMvg 8Nng}Rm,Ƨ{JÍYyP>~yumU?XD l5v'/} ]!># N#![Ե1ѣ ?{pM|ҥ^20]cց` zʇ s?,_F [0)`S0AsN&xEB:0*ž(ٺl.h;аeS+ |׃2,cW " O;^ D1i7!Wto0vاS&y =x:4_OD9$RHο,M;/8zBpP؊k_1 !k0!r%g%tJ`[19):1\\< T5w>tYe5ִ6=zKv*ONpGlwQ"*P=|lgO3qYuׂ'o4jc;8l,2}KJn|s4'ؠEy.: ԍ gsxn'CCE vAƌ72`}i -,- ƇKAhtV>Zw:%ɵ<|ZO7 _w5]lj.["z?G]J[Fv1۳7Fsx⠇KzCwCT͝DOCh<&~L%X9ҏ[Ǻ&.0kb|\bVU*S9c=w;9x qn!yA_^'bv}pzcPUT.N94;~xt~F|6ї/>33D}jw͙$ʍY뉄Tm79D5ʨJDz[q*G/عQxϨ{VeVh-'RN%ONmN%k%9 Gȉcː!Ŷl%)eIPqVbC[[N[[o/H%s7s7sWϭg·7qoi&K峱`Ņ Yr;_3#D$F)0|&1*,vpxvy(bBB\pw/6Ns\3W {M`a} քF@n0W~XwS߮;w0LA;1jö}tKePl` ކ9e T8&ҷllBCD Kւ?7Q5+&O /젶 F`ʅ:kahڣK /Q$\&f@`R$#*vUE tQ Ҟl1Ǧ 0sXt3V%H}[Cv4(shss7x7gQ  ʈ!nc/Ns'^Bܜ, 굪Q8uuXqnh#c1=,Y(Bj|PVmؖM XGt =𭌜e79a},B{"8v H3h\HC0O\s_ }B(w +-${hjv'N}ȕPceUeBpʗҐh?A @&LPPUT##YhF1մ8(PNw8ce9[ Fj<*ZpTѰ}H,$Cz!o9`zʞ{?٣=zJ NA"q39ˬѼΏTX a6Q|sB` qwp' kF"s]UoEG%r1 =3 3G;k=$iKN.y]lDh"*s/dN_(F-mXe2uw{]Lz)51s{aJeGha󏣾l@Co0b"A@*b Jj(`C.Rz"KR;[CONdZ;lڟv튱h2qREqֵD_-.>4Pn]<`ͫ$0\PW:MԒK* @G'+tᐥ7$Oں.O|@)T.|DY5dW 7WAw9?@h6}J6H7 ؘ#1 1eG')JŊPVJD`oosB&RɵŵɏuO7mWy^%4]݅'GL8O ;[x6RxLNI{-[dz&+&A}`ޟqkfnNad'?mm3Q<2%>0"&K ds$t[k=6)Ap8 CES"L?♆aK w/)P`09F__S|YQyDk.Q LŷuT&DjjR: S17lv!¹~v T?l²fn"lM!4 #)](=@P?= BXv#vLTxk(uЇSPԿJ B ?"wXj\E H 1#^P+`a.=@EF\<}׏ܪH ܖ hW2jP^[Dp3*cpB Z c肖P-+0)l$DR8p3߄`}DX;pu >?%V#Գ t A SO#kGD6}U\aLfL#p;nZ&aq{c4&VL iY?G;$.m*ZEžTHԄo1(Y5:ɮ7}\YkTT34 T4mXSCRxIH972"%аlN4 AoQDuvr/l: Xr^Sc,Y qHM>92om[QQ>7=Xnt 6_N揅m˵N'fv GY 0eҔN53F\#98Ēӑ! SZ" y'Ȃ (X]D[в-i@͑*/HԈ@$%6KuCP_??l OT VbNTTjTFѭ~ 0\ ɤ5u Q 2<ыNjEEvQ> @mmGٹ  R=:T FH \ZNQ3&f;5pAp 95I);emo}H]ZM]*c1 76y9,?'b@Z9؄Am|Y͔ܻnm7bkk֓=X4 LU*חv2ak/Q7_h5+2$t=dnSd(/ˣ3ZhA=p]{8Ñc0!m&N1'iʉj,L\NoDΈ|?n1z^.=}qo@V+@b ^{bg[D76w77/I pGFc&VJ -9B./Xݩ+\yAw} 8LiM9;|@_ur͈xwZL M#/ؙwbG4* !Uqg$X#pD~%RrlpprFPiߢJy{piʻ #oZ?=Vö$% 7H" *JCj"BgAj"-ѧ:6y|2P9R7v O XPhBhv|Ψ ?V)>-Y=q ?T)!DAVJ[a"٭,=X߲hpp ;GXS¿DE*F󙏧+++wjwy~_?I,O{|>IUV\T~X[KcL$B![;F"WaήdhI8_Em F=y$TJ u0D񡄾цZ}߽_Y]I݋ͽ67LըbioksWJBeF9ΩRA}Ddq连_] LHu&>Ή\T%E|I6)-sY6;%d1MSdr}O@U @IpUvXN4E3 *VbXpL@*yQaU5[If|i{P !B 8GiV.Ru%)tڭ&!95unZ Z`BSú o!Vbu2z^5).1|rO.?'\s4nV72*u #Vɫ}JM6E&B Ez 䦀SR#C(tn- fM1I}{Sl&RdA,I >%El!#4ĥ7A)F2Լ/0J-1OF]ǗT\_+F(,fZ.YOhӘ+*UVFRx#0NU ׁͨTe=mI6gKQiDk][Hѥ 薺cQ$8dKқ"4¹PI-8-+@ G2C;.LJcf66Bf YL~+E j4 h \DU`#"k1|ϨɅo4owRXMԦ^(LPNyxQc%]-jKwX0r@u%P=­Iښil[,DafI _[mHh2oRԅFij"sȺ K %#C qV&<#/k?Xr ,z =5-Uڰ؋+ 4ZPɒo5Шq2PV{ZWF +eU ݝ e7Oj!͉[78ZB{/8ajpXQ4M}(N5nBO `e=YGp4$V 2gR$ 8Հ=7N`\1/D  NdffPH)>%[ǣ0ӘyZctW]G9)zE4^V]-ްvBQ; AFX/U\?(00`{Iv>()k32Rqީ6Ц LyT`Qo5ć->C]-FK܃c#,DJ sfkdaGm Bƞ >^p $) 4ޡ0lд;p8߰›1*f(tI>Wrs]KM8]R2s ٹWf_8)9XUڧdߨ׳ [F\rɀ@1sZh=c'z1z{W|^ no6,SK܋ i[xZ=iX!sAF>nhMΝe\ljC$h XAi01V9`̒7pş o&J%>* \1jS kʂW!؟ |1pBh\vG=&fUzdl[?GI۾Zz<+63˳ 9P1 ~ +G|/^?dn㿹Gn9㿹+"_(4,s7 J3?@qȻՁ'T*4o)^ǿ}pA  :g@8etDQig0T?*|Q Dv2?0t<%(',r$:^,y//ЎA0_IP_*˸N-T:-U ςf~N|* /a^0oKN+0Le|K¼S VR7jk wKk+ki7!s7s7s7s7SxT?I#"j|7yojȁ$o6ޘ[̭SSSg21;E,#|8x+IbuD̀zIm6T%af2h z(zUf!7K6ZO~6Jb4zs=%`G ՙ|m၇8C0Cd=/N =_ݣńŇ#s{ ao@bЖ~x6N#tf@ \$ o4Ypt,UeLAz|)מlm݃|qi[P>27 N~uFoar9H9Y6]dWcaHX4[K_jc|l.Yug-#Ysχ^ |6RJ?j񽰁pSUmjC/5OB`|LFȨ"ؠ`&V/?3+ J~"+mgqîP~ ҭC)qSv=:_MMFp`O)fb*` P(o ;aGˆKJwJɜ)\uwXWk5$?=_XK egX)< fLNſΗZ.0zo'!Sh?aMS4Gxtb{k)zQ?]^'LlRt#F+l C*%%MdbبK4W`W%")%i~IvDF4fQLI&[>nJQ#dIy qĖΝ{̟RFpE9 H:c$.hk*?<Ϛ59wYn{~sӄؓt0|乌EDU^cnB^p J^qL #ߘ3n%B"h'h2LLh{ B60bho)%8" I^ ~'SjYbGlZ@D,w7Y}&eהb!#B4ou3}\|*<).HmO$iMԣP4S*(sn-Nۊ9Ep()K < ]a;xfݔÜX]w\01c&Gdȕ Ɋ.[ pاdb'cJj $c.ֺ]ϠX5fy lo[bzɣT'^ԉw PܿBZy֚҂%Ӯ2Ɂlͭ!vjZ)f}%Į6MX=p (ZϪ\Zܗ Xqpdy O%9A]]kǶ)7!hpp+ed pT 7z78s$D*4EBp~T4pid&Ay"fO+yVq4G{#_2/:S}/7HήbC3mzJŒ\M& Tg⇑ɄqLiex̰N_0CQP6[Xqj!eLxF禠[/db|o XIZ_?/%@?\s.?\_\,T>~)#|kܳ ?h(D$JdLOTL$?{|Vy@`Mstp^Pq*Z% .5*-f9V4NF/GDb5#ypu?o3S*UƄ?:StZ@~b<# ļ1gvwLotiw(?͟a1T6ޭ7NbrqCq2x`Vό+8.2T8gAeqXBF?'kҋJwgFwU!jЉNj!P#]嵃ų̻a][(cdB=:Z(]ܺn=/U^o.3f }Jh}2@J¾t,bcl@TOW kV:2>3iZ;XZ* <, Pg_d\\nA-ZԚtpX64pge:"Hţ4Gli/%MX ,/Ysj,mTQS"8M9@;ZgƐ"551¯Ew!JoĤ+!OI'> 9gn-4xV6p+\рN :٢2B^rZ mT{X4XB'MԄTapQ0J1`ټ2M8WA* F+#Xz<>$@3~S(yE`3eM6VV$+'a 6:`;6pDƴg0%dhv4FQұ4Qw`|\脴ӯoF&fKr^-?ɨ.5,121=N8M>pG8'#X2 7J ?958) L7.[L֓5ѳ@c7yTp]bhQ)Fn6}:ɞVm"ۼN2 }ex7Ɖg3^F[0OAxnȩx15=c`FS y4?{mnp-Йc┕(<%k4 ؗbiPLV&W2 I@yF@~)8 ecP}25hޅbHyW_ȓuve| 0UDgCI;PH_"P Cf S"ޛpTra M$fֲbg>vĨ`(i!6)K _3?_ifCɴP0eu4:aDbƴ„p_^zVh:PJdׄ1sP|\,2)* G54a.B rXp ю4l]bO|jba\v9nC'Mex` hvog'j [}g؂!dy9XԬr=ՖʷHRLᮻ^sÖ/DMI?+~6N3)*jŎd nx&SqomT;MRvؐu@ȠY0270J8\I|]Cݞ1C*#t [ |ii?&\IZE,Yef= HhA%wIXs8l60h7qvIfɎs/s]3'Äo5 a bi:ۅt((Mjt'a *]WeDn׹0ʈ|RKȃqU@Y"LF}tq[kNC,#qr%p2k =X@yaTIzMYE[`BvxorJv?H1\r_.=&?rPWZj\[ fTvG\F{ /"jo5/FX-&5~g, a }L f*vC+T=q{(Ĺ 5 zg âH8z>%WߨOAWeW*)0hjg52ħ#w<&$&Oio$SEQ[ڜdCN˘2Ojyvwkʽ{'T9999)<AFFDj!9绑܀vH ayװkn6ޘ[1SSLJ9_:sM>ɛoCݯ!jGg$o  I|IϜF29/PK-ɨ1J4h[vĜ;XǼpcaP85)P|:)/8vgTV*kkk^|g*kJ5> cr/b"lrh Bo? 7Sѿ8FF_) h`t3w[A"hv䄠09pn!+uo  /=)AWA ݝ ps)?L;\9mI>-|X8*,}@F|Aym5zS̃zp?H~+͠$m~<x$~;2<X`b_q-0|>>|gZ `?SdRpۻoz < Y)WVaAI#DkyIX.<߰DA1g^ߞEb8|63>"qL?چL9کXT(@Z/`?D X :/rxX}ە0о Q[51pt-e Z>\bIlraٳaFq-ΣRz%5Р-ANHz~?#PˆpȴO dzݻQ{P!D`imd굤D>}w)dXGﯮ"7KZ $r[!.]"P1z};, O"jTS ,e@].w0Pml&htcOЇ(iң?J*~R,hL"Mei'S[܃10&W'R`aڒcĞ&|*wUm&F@0l_'dT,ڱ4b1eéf ' %:f3 <"C/Kci{{"$~W6~ cRa,Bҏ[ݠ %R^3,-W[u8\bVURa?! 7VNWm<ӣ64&?J#P9C8*ToFEhmoj_QD8WF-8K" W!ww<Ƌ{;r<79 sBg2N*ꢸ;rO Y< o~P`KzbC!r.p"(s P_Lt>|%R}c.6VmmqOS;Kx| Y WM/ױt۷6y^pA? my!)q|:)u)9sWP_9ߋQpZ3֜]vx|j=WhhWpȋ@[#̔J1܈wGWwʕqI { ˂Dfx"θ\ǁ\HMDH/s7Kjc_%} 7({ `"jKr7&J'[Oԉpe`zr{: L霊Q£mLZ͜|?%QyC7`p?K|,0} ;? NC*UiDG}yZNPL+rO i_I?C r8,Yc#BE?åei ܉t֩p΃"'PҟS?!:W$-EI'r/60r+ σg59|EQ;3sR+=1U|dSukBwiv hT\AS`R $J4m r /~L,O֓ 9wn㐔o/sဩ$T_Uj7踾oĞnlFXqh(g[!LipרWKy_V-'MӖg[7uD%^C+HndK|3)שi^Ш},|;CѲ>oqʹ$]Ì݋}0<~G'}(սLg+Dj, -o`A>`䪂Σ?Tr?b8W2gΦHa'ٌgtd:1=]%l5y:-ӚBx0hnc][Q xAJq ֶn$` ` (i)PM V V^s权uQJv 2%2' |St(Rh(~>>tr7\7Yc>L)\%eSڬ;p LƎɎ7䖅8ɕ}5$<\YD~QzgªxQ uu,%xTȘr_Iz$u h\)%P|ƜY[`Y4P1ҐG{b1gf2"/C^i coZh{-NRB 7:@gPrSGE2m9z50/XɕDr{`gc(Ak)D}RCMJB=*A,b]ŁSb K%y V8O3cbZăIQ@|%(bz5&҈**;EFE5EtT*!Qep\+dBPkHe7 |B)dw!r=K!>q:=˨/|W*nkʪ^N;{a*}j?z-p~6PL̀Уjy]  E$&?}%4 (V>' 2&K2TjfKU(C{6T5ʸ! LCa"2%)7!=/ngcs,x cxK>M0r+MpG/1RΒ򀹔l<_-RKƚ YS* nrF"\X*Um Ă<,(݆|'L~ $mlsPm lXEsު>zHˆݤM)N@ewcs&$e VaA҃0)lajLT|f(~;*Bڥ)@Z|gS56O]dz]ޏC]^&Ҳcؚo #n|!hL-ԕXwԧ2%wA1*2nSh6\4NB"[F)yqx/K҂Yk CqCc @cG8ý}rsWJH <%xCWdlaK%”NO tLy6~Qpxx8SeP )hݣ&.BEpۡPnn߅?ݘH+~m$ݪ'>eZ@~rpG/!Y):-Yuoc#8+OejHvy0l˞W*S`gkk*YIfI2r2Nt̏&>(Q^cy v²zӾN{{׊W\eיV9aZ<4Jzj8wAN;plTsy9 *HjFsvV 8qN>=PFyLLea9a@ԇ>N3'a<..XQ{10PtFhq=oa)gG\J3׾hwNN{͙hp 3IaiOC:P* >'+lc,|[X/rtk<).WV rr N8EA#['bC0BOT=PaA +Z"]U6̷}{W:NlJblzaTWŀ/R;b`8U~b[{R+_[-W +rAe^.םM)Ga|)A += [8׵G{,-4Kevj#W#ܪɳ.MϚ HPSsoF?KbdDzX{"8B[jQ!'¾`|ܵ4èx1]"[ ^Z'M"﫫մj%o^r#9/=+ p4C{]ey.1H)7]wgX/UǢw\^0zMۖOU /IhϐԠ%y,ڄk m=.7ɒm, W6iE5~r_ :`M[U*>ƕor^D`unzJ_Tвu|`~4:$Pid@ f++ކ$ ZEt-%xlI4zeF*Zް)&B@\RU/ p0==|(u`!Ź~&\o9om~o_W/3r/r/r/p`r>C@<16Cd*r/X.(nwK+ UdЇJ`A3[0geib_PP!$!* 0r.UM}6ux6VUqS7`jch %E`n7՗pP2L :Pt $.,%ط6`|ܴ$%5-Chx147eZLTS8uH&SL/4TY^4g~uN, Q;oq#KtMQ)n4.&zX. ;gBF`F*e^@d0rbnя؁ifu:ڛLjtY`Y+ T7̂#lqvց .W}Ȉ}$)lA%Ӡ݌Y] }:,ei/X/jnr4mr8_6et)OSk)-IK8 JSTk,bCےLR%犉y"/+e]?|Cۡ`cP>u;Bƒ .,^~0*:\YR>;D&Lp9mjQd^"4\W锔9-S 5 6v ,whOrž[6ƎaM焓j'X\^!so.忹7\/b忥Xs[/AN.*$JZX{[7!o4zc %"QSC>ih(5CiXT~bǕMwZn g<0Cf7,Ċ5俸ڧ$/)DݯbA'D :11wx wY\=0#x)p9Z"P Ri܄G2X۬ln\)=͖4׈gU|GZqܷ݇s׃M 7YkjD.ެ]MAg4y"xTm#`\%zۈK[jJ&l f *>%2QA*H6캐 {@VDos鍅Xղ!11fL6_2JE%a8e]đ5OF3ʢ_A#bOeT "ˊ%ȒgOU;6LpjtQC5hB?5=Wdqc݂uL|͚LImZ=8 [Gz=u#0AL8J[5$@#r6B%MK~<ٻ֙umJa!σ\ Ͻ6&|$LIt_&k@ɧ4+r뼰kVsTm֍7j66\fwHb{Iim53HV} o*4nޜ᧕K]`rm9RG/\r_.)yDISG 4@(/rO?/<2vt>[ͭ7ܡ^[OMVf5ص~__L[%v7*R^K`ѱw .y-J4uȄHF}N|eQ9ڲ(|?!@@| .4\5m# 7``<%`ڑ]!'z}-q*|3P_ro-!r/r/r/r/rO7 2]r=-j?U݇&{,ixW!MUpu@"jqB$M.!?h7Cm׀Fnnb(Z\js`l'kHh``0:˛, $d(#?lpB\F 2GֹhÂqm␰UYRJ"]r&tځ~CSs.b } &$(ۍ"1+`t~O=;uk"f?,(KLnhh(?YDžv+dmVp{4'l}}vy)0ƈ); }ri=&tV1/S#{P[ƹ ݩ.鸯Hnjp ԓ~ a=6P뙪(n!(6V'$i`9&ZzΙ!]Î@W?'K o  Ѓh$F 'ޑA'è?W,q(g4ZwnN?w_6@|>}4 IB d<5&^ĂdFNGTF|:0]Txc~KP)xq4)K%WT| >| _}lA:# NG >6]/O#y){Yeo?2mHS-7&ө4 iÉKE.G(=ʝgbT6Ԁn 횠#3$iWg}Bz8G`6,?[0:0Sdak#Rolm\=9]RC"l.i)F o1XGMao_K+\[K Kw&M5_0 TV*kkk(~T_9&Sp 9/ 7_@Gt{П?'OUXÓe5i.XW oCK{oiocaea]VAe?Ϙ?s^귿W䷗N;. ;MQd}zJX]?-86-Hol:1NȚ" `jg ~DmچDS+i: mlq?}7oޙa:N,q쵏|s+=5F'vrwZB jtyÖ)  =.sǼ >%>¢3jL ?HA,BS~ 2UDjMJze +R=?ޏuc?){W5D^}>_6;b ̩Ѐ$XsIhMH=w9x00@qCrFmtϛ#Ő`h1-RBּ,NTi[ɰ:)=݌pXeEbRRԃL#> ɱ0(.M%̔2;bOBFSX2:Cl 肧a^]NXlQvɾ_.Tr=:KТ.x\7=I9*E3r?LJӔ,G13o16y:tkva?!Gcl:e?@r$‚eDq68Š'.!7sIgG@몕Xj#ahU2ʼn-Ql7iLJvQښ?$%}}㭛 6yR\(nmomos9CAqM0/ +)23xC!l 0Zxio 'p|+ikBf)MvScY5UADƘ hMCGw|4.'/cq% 6錆c(d!v` >dNG U1ld:əN`ލ]jm,[msRYR^-W+QaS۰皐D vJvj8cP,XWU Өdxj3⡏"c#&~;YxVKY\^sfؗZb  Je!Jbۨ|ǣk+v5c?Jy8.%Ɛ4I'KU|}<4c ynebQuZc` tFSmMƪ!58c&3-ݴ.vXIw9laZOFLA/Fjtqu\ 9aσe*_CrR%;' 1-+1 ^]}_1|Ny@V|A]߅S z #8[@Fd<*lq'~^3w굃>؍9Wz^m'}-oȶMECe.1B@@Z=ga02c?A5P%!bڟ{b ,f;%)Mdl^P*PL nLd$iLQY:hdXmN[w 7f#\EΫf1 @\R?1ss>9_Dx*гA)!cS`/1qȇgޝW7h)}2H@ UD3@ bjX#+34(ƦvG=(."돇MͱK$md;$-+fB%ٝ2V9R/#ik M^Epw˼E sz5+hwFhZPy  r划ob*q $Hyy팒&=H@s%Ӽ{n#d-ϛ0]RE]^Y?"}j W<lֱƾM~.? oߡ2~krFB -o[tn_-#4PP P؁[4T$b.H"P:e\xn݌Z7S)73 N'xBw{R%-qrrCwQ$5Mڮugn/4/VM{o~%:_]^Y^FD_Gb~ _-PnizNb.5;Fܖ,g xct!@8lh{J@t(ZXlΝˆg\1ᙀA ૩ذ GfK`ݵv>D▬ O„\;ߡ˛ya6rb@I,U; Kb< UFa;-=ʆ)" 2:30.y4[6#P-c[h(>_89_!.dIMmgtpK#zKlqo?`vbY($h-BiĮhǐrz zo#W$y6IY.?jnΒMܘ%haud5+aN~DS* 'L V`cwF,O56J}hh*5\%;vIT8OC-+H_dW7!1Е^$< @fEʦCJkъL)>ɨy\D<٫Tg?绋_W.WJjy_>?ʞ{c74ymm/±#Q%A>jcO ǍJ.}QyK =|˸7g' kG^qͳx ؊P!}*OsMvpȨɺ9S=u8]66ئ){r&m_11 qڛۄadx w/ޮ %rY{gCo0W]\fv(횁A{u a0In ?^N*1'olQkOd:Ѹ@3>Ý0?ۈlM)"a.N &$.$X:]0C1z*z.M7 kv )zb;)셕iJQ6_c2F[UgРJqvt6=`.A%pfQ+ZYh/nlGE{,BIB`DkA'_ {ϥ‰ޅ}a-L/v;9@p/ 2><ؼY_1 >h˝g&IEJ 0~{7CɪՀ5{fOL͇gETbewܓٜQ* -IW)3/̰6÷};`65HGA=z;GЈ1"׿1(tD^>յ,v^%●a 4/TIPuRۈ}aOzd`I J!oRL1.1V# /EA4O,nڠؤ ˁ"txKmCk QbhCPN9j:/If% Dc%.YWns淏O |E^2w(%67(%_2:Cw5UC5ܓX2oNjr {6W(W; V ״[ L#k_UYB d),yFnD-Ԕ0\vpȆ+bnڥgPw@tIYk~~Yo bkuzg?nrn؜ @/ C ~4Py-ڴ.peBFlxۯ.3!K_> Oo/ِuCn9 oxqnJ$M/ Q'ǃKP OB?Z\@a>EPkʠ$}X8(YðJMBHMp̆Km%+\j^%ߍ! jd=rvCb$'2R6t-=1l&h0_NV؜&8d6QbMM7=>?ۆfwog~13cnZLLH{nG[X6 i!oɳ"OԟrϪ!rB /I*T 6)TM6j.b%0ɰNL#j#~;92޳|Ap04_GdfBv>z?]d f1/+bdMx,3`0O0ʰiڃ#'[;wSb^{ΉwaAS\#x,mLy~$O+X0V8 塏 lt,I0b mN/\KgCʘV_͂eDÞ5!ZW=ƞۣY;`e.(sAkDsr?df#80)Z?1@hM < Īw{>w{8 W4t=`Vv3oH#\;¹.kNWrI[< "q0x?qt8AA?pirUӾXi[`qFerӻ Mj0][}|p Xwo!1+ Jԫ> [S-7WhR$8xnYUj^FotG.{Bt#ێ_qAgs"|\A\hk.)'p(|Y.Q_ToG o}([q_! IK*}^בolZWk O9igJw۫[_pGU^U[j(ĻPc=R襫:P<:2 [#gvbGltB.D[<zǼ=xԾH^3F[9\xuz`7!@xcLK2 II1fonyTmQ6h G :XT'6pj9 &xDCQAX^i;\an ffѽJy>^i ;\V ` ;5jL.;h9-)f$:#n,2$1]ːqcˊiciI?SJ.~/2:JI$?.DJ0E_aKHإɱH0, 2$Ee"m lͺ ceD#Y9JMZR#f<`eڧ%էSl~'g@N_I/ա&a)ץrJruM]81ֳ ^n]QnX:cck"@da\IJ,;b#,ϼs`@e+0%aD7*7U@alGz%B(I)Ml53j޼vzdL#ÄKzaJucCtn QؘcJn. `Bu\ȔOz`"f;) b7JCl^@~cԈp AEKE"r\,G~\_%ͬRYJ~D)k$ Ӓjg26oj;cBD4Tp"2O kI d]0V”"Q,~h>!oa.tjw'RgVlt4Q;&]Xp{fKgxY}f-ŢEٮ*:P9RIx+ɡe /2΅GAwvolq60׶>jxDM({jCl~nge׾~:gp;vk="Inۿhu + w`u 8.׳ +;i8m$$a@/C*dMP$ s{Zi r9Vr&?R0ٹ]-wߜIS.-< MZmҖyOC-M2a<'4 ؂h~~z{<^%wc(7,E>)Fy0c,9|;}5#F+'1 Z*~==#ƼO[2hDWƛ>8Sc<"7; 瀿#샵aP!#k;'XPs|r&0 +O"Tn df1FFc]r,QyFqbs?0ޢl~"G4EP1^%mY 961Ur-(L+Y[WFPSe "p*1l\ 92BB0 Ri$R)Q#e4p"dBfw-h#dAD/Wq²o~15;,`WVl0$;V6^ˏ֪*+[p)uE򅬣Q-K@60R7#RfrND"B q=‰q \{o/T{֭6Hgv~hq (koR9[Mq.3ck wZTFk:[ _:?}O33eT*~]@\_ S.G<!@B`7ǃT0YnGL#fI&R$)w;;ÍƬ1>[Pm1(Xs/b#PbA@ @ !e.4d @P= AI*\b!ƤSzҍh@_p6WUό9H1/&Ot>I<^2l(Ԓ*}T6kL2 hQ+x:c =Ji92Sc9r1(^.Ks!o?\{h<`l@} yXB]Taf?́N` wѡ:l`ao5R|&"a //V_Es/ݟ^ *$b@,CHA2]{C Ũ5-VG POh=E_ Y bƘjf(} f`\}#(w#_3 Pvo|?4cq=3)a'K/l `O+G3 t,H yƯ,돚{ j;BQZll`d脈ݸ%~7VMJƈ 3VYﳸYZ؁RX*shq.avc•$*y1-4s]QY.io889ӏT}i}$CAa0YZP˥M*>T"Ĺ aM[+@d! -wql- 87vn@g„o6kNDYE -NV TR!pb !/ep"5'O*1 CzxgmWCEǺi/gv5lU@7g=im~-pkmT̠BR|k>7R7W.nn-WF ĹZL\ן^G0w`}(ԙߣ! J־ ;ǻ'(px&LϡDŽ!c؃7& ܥV~ӕؔZHV dq; l(Q0Бi#ן(1%F]xc|nF&sI[.@8z;O j'Bd"`X!rPv(кjAX-$>(pqjBn{^x$4}qMcIPv$blێ 8Y9O F@1<7G|p*:TXm,҃<ز葈[}oǹC!٨%6%%v,>H/3EP=x].kL%qxt- cԾv̟ AL-A'v\x6]P rC}nӣLApnEf ؞k& hN*>M Q~FPϐ֭mo g6" %($0L8֖\Ѝ3:%xN,Bj59F$hsy \0A}6u/׆$GY\8Alة3XzuY'Cʄ@&n2qh.py"Ba/؎3ªp\X^'!UUϻ˥}&4|^u+`u;7WDr^0v!zOϊ-AE1G+'M;V:ѻ'=} L ǫ0umF܏[dxyY[v ²!x[  6nQ]bl"X\vNU.mg`#܈☽nuV6m;jX—I#G*!XK}lI۶:!`MjRر9.F i;0Xo OvaMٯA3L93u/"{{IV!dgdB&\7ڽ"6VJ5 J =MHavX豇Ҩ܎/M+s҄=%۱PR?)@xxIMЪ`BdY z='_nɁ%k{wV{zІ,oq'S}~.~Wڨ? ŭR̢3vʍ ddVO~t|:5^_˦>rrF-sxoԌM=[^Kc[`T?gZH}gKY1?B|0# %w1Π _mjig߯Hgt)K&,O?x%YXA),&&|NVlno<$ d<2 l,FY-D]eI)'=۱枻}ѕz;u,w&+d,#Y]Hyf+8,?z{JQtRx Mf4BH NSv#]K /=<7P% 0X}-+߄1b&򋅿+Kσ05.n=4 3cQIB s!!爿\eNk d'or՘9yɮo7g88O'Uo8"7 }WⲾW_J&zv)^x&=Ve}4t*?Yj1L'8 >Opq9^8vUi%/-R i= ]/zI֘W92l>P`d.eZ欣<gh]3,]5Lj?W}~c;+:L/fuXG[6@(z>$["nS wi@u";dPbB0=Xx! bEGLWEP8g ۠o@ ;}ŇЏZfʌ좺v9MV' h3СPJ>ȭ0kS{;I'Uy4bFu˱AS0W D[?TbB;"U.&.殅TiEc{;ͪz5.L UvA@;1V)lae?!30}B ҄Φ'LfdUNS&7Y&ߓٖ%D3&6Q3. hv0@R3t~RSm>vf(ָW7fĽ^ 2`D3{_`n[R$ǵ3yHgZD)gir?P,#z ~*{dJB#"C pdԇz\Gۊ2EOTvM .ΡBd&Þ38۞1=?O+툭#n/'N&>W0})AbkQֺ=~&  Wp/D+0Y{-BT)1cлQ=R]ۋt$"Ix>ȵ[@.,H5xp-q q9O"(h)4 „=d\ &xiIߤOO+Ȋ"H5>u*F)rɿEOipvց$n$2D Tc=罽:T |ɾc]ec0g0v~$_,8'svAPmBuz$垮f/҅9)6 '4AHE~GuC9$gXhwRyk0Mæ>C^w0'-^ 9F.D:|Cj8fB*.;&yJQvJtڐP~MqrؚrlnJ6E8=lI :Ӑ|;R5z۞ư?Ӷ4zB Zyc../2UՉ4] b9eż~qIiL[/&KxAcP{'1o[Ű|*6l2ZG"JdxRNl )l6h&.]vԇ ўZλ7{_O}Vg |+Pq@,#e-{+C83/k: 1聢pڜ}IXRy~#`D:%Z9ׯ95ecG;sB}>kɽc51嗖)L\CU5xE?6688V8&x:Q%p~>LiN\0k533r>v#0IBwb[E Mgp̬= m-N삱{4OggN5,r_n=ɓzAo*s _6JOůǟ`ߜ/:{;i ~#FQ8}M_]Ov,rOUh%Vz?@q8<2N?A+a ahl>_vVWOnbjh}p? a=c }T ROjt@vqh58 XN -m_i"b.BhvKY"*mlp, :b,[?+\Ң#nZ.(IাYаucAqj"E_sooP ;3y"T0Y58B}^WÐκ.8,[@,ʴǪQmb^O],onT._/87< Lm0Ϡ)^pL a{rh4(kB=՗B K}WGȎA؇^M 6B#v)rh1>΍\{/26sEJB*"dEUuuBZL럲+x>ʂ";]߀<@v<}]"|95J;+sڇ[b1>$}KMC2p`4C[}Ć?`5hmR͡ gWɎz+]:Zޛ,w(Si1ɒJCǟ[KJ9:Fk!.Kq4.Y6B,Z^ٶ %Nh(e2$*q,tAx~ͫΨdt_wz(hb?v}E- ,;l%LV8 ##=1P8:y] 5"?| HAT-+YIHZ،M2([KEOϱPo>[>?'d X.c^>XyVv6yH{"fgeDM^>Pj^S}:sg:ild1DZf}QБ)H 0h ŸCRt#F=9#3$ qJ`sk5}76P(B6srPE%"_!se-rFϳ'"@QubSd [v.Lٱ |Yhy͍)babQ*XGQ8pG$3N=l|V9<8w9簚"i(،'Fb!S2*.;9ٰ}j(*{:UŚ(Q!Pr?e_t gV!Ƴ&iS GƆ ˘?NڔkC%rsW4Gņ*(0A1[Po.o%,FJ#1 H̬w49m~кwS@IaI*_rZ.L$eD_vbM z8;Wxr/L]g|2Pf檏Mɶ!`5>R1b#/U!6.%yU/[r+5O)+onG kS] 6!u.<|Eǯ8~д?6]p]Uńlݨ:Q=rU f^mԇ5lzT߱wASVex~2exP mee?ثT0+xH'>΁?QEh_cO$CH"@`EV&tqФwH%2` 3u٠.Aήz`{.J QeQ@]͜Gû!-DCV:Df.@~殀[A uՅΏa;h ?6DOuڧ$'I<0J; j@*6XEm:|a*p#Jk)pq*Lr ϥX0F7 X_7a)oMi2_[Ɵ2:q]66纎ƒ|(9>AUL ndM!*5Kү=f0y&\ kf +2աX8;hd5#ŮH( WCxai iIz vYP'( !%[P(I70bz n24rD}I_6֦nʌdg(Z2%GMALAOs|&骒&)$Q\~HV٢^?_`lh`"!JVV%Z{!A2Su2>Q S6,=@s |z6n`Ȯ[ _FYcԱhOCfg.';%R k7%1ZbFaG;C t;j!fɍ]X-eM1,"Cp0i>I+R<.G+r:%,2R2I/tPbc\Z `x C~kf]d.P>#v1M7ț&IœJ^x%Mū%@ ]p*% =;G1ʙ|cv@iI,)6c*M"/L6CD=_ ~B|eL$DbI. p~l|xuJK4̉S,-B,I~4i4ǤT\hXykEw$H3%̑ۉM6 L [}Pq!eN,i RF.gȑSl)u9-LJ"ve5n /ǷEp=N]UٹX. 1r\:Tr2SuЎAmbN-bN2_޶\״Lt3)PH:>X3#risljwb˪uPVS8à+-~=sRGWCښcG(39e8xa0rg%*8X\u*H٪c:0thޕ}ks p_xu54#vx?tZB>s[XsV"n V 2e פQvjn(` ')*!@P+xGJ'X B{Lpn &A7bnn$5'Eacyț۶лQel!R8HM[؈0Ynť\lazV' F氱TiƊ؍n/^scSQn&#q6lt?ۚmՖ) W7{j%+QHӌz?>:y] ӏ|U}`Ƀ/1c~6煑Ù[KJR^EhVH<˔`)zEuV͋PwPPಕb| 7 eoƻn\we&;1ޡ|8lZC,1 FΕ{ t"*aj64VSD#( ¿sJpۼ>u~==8]`}B_U W;E-.;zPgbXZ_Y[YsXw Cۣ֫wݓSA4O+%4?KzO|طoytQ7bp2 {˕{no!åqA׳8ٱ BvC3r")gŨu %Ei;Q })L6 $NxQŤwVjϼ .w5!t{}6M)#?WPRa8GB~C>7. i JNaǜIǙ" N돡 # JN~!ՀTB>*ƙ3CH=^4+hL^O@]1:50Zq0yPG!€`# G΁bY[5M& N~ȰzU8yR;Fڇ4mFo<@8lT}]~iN /Iz \g 8Q3=,qO; Mk lI E"ٳϠԷ +/iuş~Óbo[uk&Z] kKH ]H̪xtLZ\db<!_нo//4솙!BE~rf.ep,fU#Emak@kAȽPGz4?تp4g$0ޱRh>zSD؂T/LǏ {7nq/X x^ͅIWJ 0En_B~+<:˳Rb}eҺ/rL.0̵t ^M zo}cs#AC'4:WR|OθM/+s^ ^1p=oZ&6(9 NlA%)< 2Y>#*~MT6AӇZY- QG7QqK_R)D@}UK 5{|J9 =30E|6yW WXn\.m;+ޒC4 ) rLp/dx3QfLtgcVn7+`QZ[67'Z~{;E ꪴ_.Hrg%0QB+w/x.9JZ;x9 >ׯMW@9tRP-le U3ͽ8^7i# 5EjG27N\e I_kDhTQqc 詵vASϞy?s:q.`0<0&ˉME U^n{,k3rmV76k5\8vR2a;f 0e"c^z4wsãgՓӚ߰xUctAirX~"~/q?dL,kj5ꈊQ  Q܇DUD/en+&w},IS X(T 7:ޙv؂zRj V:=Yz)aʔ7U9#*m<"isÑN+P/ֹ nպr906tPI yli?׿m+z甭& UL5.^zcEM:(*(.4Ko=L} 6E >)dMVP ٮ^Hrhg vl/4&7u꣍++LUr)ܸ5޲fm$fk *: &#\ N5a,_lJik[FnĠr)#f8{)2$0ËؗOLk$}r$߳@zbЖ+q:ȉX> (a݂i3O26@۝TJe`>JbYO񥺗8:|Y9==8ُ2#eDd =CndCq715O4>TFߥZkߘ6*k 2*lYl0%$)>H}[ƺƻ][LJV01wꎝp7llmO(4ӣ!8n,aXm;|r,Kyϒ_h%@>o|=>n}no[~/6_xIzul4ƹ>l]/-;EW&Tԫ8lE0)Hv*xDkEM\˦}hcD77s ꘚ@iyxi͇c7-$2grb"vN2P:бXOy(8kx&Wfl0ߋ=oFS{dEZ)64o}7Zo!i c5#@8f$&P42g,M ٴ9 BJz;(aL3p?l܈-0͟N2l,"Ѹy7݅Dd5bkKKrT#T@}qoey(}M~@٭9#!eL듵~,VJx:h+:x.}L盺ݍ=748ɡt:CO1j9F/[%4sz~SAUdXQ/ka| = ̜[J8|kjS*W*gF ` Z(&q@@G>o7SqB+ \3*4?*_s~x%¾!ySpFf٠ۃGeя:ٯV~ۯ쾅z| EIT 8Ä}_tϫ<#9߂1{!HHR0֫FVv}I,#xU}pGI9oХc]QMPo#m;uP#E7=C|uUDcڽqn`0TwIУ('Zgq6f.\(6Ge|LSc.ݲ3<>oxV6_x^ӴB= Bd [dz W(RjRlf1rRcWURzgA^Z+YB@OA8Vgk@KFX|@䛃1ݚJ}{Z=>=J\u{Hc^uku4YQGv f2P ҂h jZR_0oMsI@%sL9remFTgTr՛M-"'.YG臂FSc\*xpf1ld 07Q=5U6b ^ oc?u$tUfipt N[ ŕ؝ZPۿʡՍߴ??ֽKd][\D5Lx"4|NrJa8z{> UohvNoڅORh۶ޥs2-+2*YuHuOȾoA +ESCFf I`S&=c[ (jUk(îUr.7Gówns\.~WZ/kZq ȁID֝:C{HfpvNG8PGJ™&dk㒙3Y$MnvDҽN{V@\9ʣ>(yyjq91 &ڊ?If#l Bp*Y8ŗtpv#4HJ+ȋ瀾iU{9dtS2`ƕNC8/},Q*gs& te~%N~]3Imǘ@p ?iǙCWg`7J&)-&8 :z+g/+N궝+[e 8~r1tsn"rm)gLI&#_64ẅ$g?A _$ωK~xmT D"t}cmd诖MR)Ka1@j9}) ̠hi_э:^SyZ{姣EOv|GȎeCU 2rר$ĸU?a FvTy+gGݗ3  :J蠠>ǐUId .;/0#aɮ[!h-0P޹f\<JspXPč)j ;]9KٝظUndZ \o?1Ke+"?hINTPR2Ϩ)KmCAM[ G^i2ucVPVj 6q%m%0URL 6@yPґhMO*b LȈ&[rXq#rL4QvYI±!Fdb며$H`$֤E"n+z2390B0T:@ yu<>vL rf ^Œ8zS`QEh} Q[FtW9r`Ol`J*;0$dUC֋~]ë*{Gf_FE]{ݙ2!N\Ě0pjevq^6]LJۦM]q`gf2<_nQ2'UXgWh3*6'rNM5p@[Ss 'ρ.9 Y0P-|.'&!|JpJ+}=>.mhq)j~pxEݱq.U(ѱgcIߖO!*O4]4&NC_NmၒJExF³2ψbv=Ȇe_Gf!穀|ݓ(][ Mk/ 09/} ZBV"V8I}".v% XNHJ ;CS +s"bMoF96]X(9pO#xq/j9EH҉f6~+}V 5Hk7R3EEe P(=x g*Д+;P I#!IlbQcSӒ=ψ Dkd }ʷ[3;<:6ݸY 0Eݒc,L,%L`G)9=U'G"/Yu #Dvy<+\#N^gT6 !"VM7֡= HpOޝՉ )2o8ǰWLo}X3ݼ~CkPhQvvgU_IŹGb*A5j0hImdGCqYg d"8`il}T:"d yk 0 Fb.Pń%.L(F&D:1 nu%*"hȓ9w' UbVl6j/ :KBLp(Q;J qI$y;s:+̯֔ёB5ҙX j')qk8EHQG%w Etlc>>٨Bm5X4{<`Wx}]5} o psP %#EFWŠ 3D v˅Rn#5r nk w^ 7T⛶rpqO0DSuT7w}#@7 STܔ7ߘRy#]kik4h^>~7sܗ}|Os/Uu^U8++8Bk Q xd^.jrV[CZ> W/_}PX"2Sv4L$X7k'|qK OtXy^&"&c) j|MJLZH@ƆBR/BAj~TQM 2L*ŔuyDoe1'/Z>F>3PੂZ 6Me_r}E UfYmOP% b1r&+H6*i2m|&[wF< \MPS *7P7m +v4 L1M$wy+D9.=ZEQ>p＿'~{zZ=8? ؂`WvwJ ; LY'(,NX$9&L2Ai| *cHwqő{ϝk[m²hXE3DJ=;hnV.#z8SF{o_"mu6P2?[o%! i[z89S(CWᰇITy&ڐ6.zL-2'" 3 Av J"I @dn${U*d`;}glK!ÞTkSiFPe+Z*KSA&Y+9Z7ljw^|Uhi %DZ> }o6Sя)ˌ)o|7Ţtk#?Hy㻜՟g)UZ+mll%y!ǯ #ޮ<7< 4*&v &NG8w?x3Xxnko[VCd/ R'6_@6^ߝpSl-o n)$aYȭb%5JcfusItҟ|^|mcY@_#j0C6qlo?Fwxl۷o]\5v6'0~+?S8Q@`;7@q?*4AktT|H>c5`83ūo[wDd3QCGۿ8fͶ< sq}ZѼ߰ϛʺ-PyPINuzȼf^{C!D]Pt/,m f!0i.0Jper0ҭ d䄙Uihyj V[flM@Ӷ&-pb;52s0A3QUqJ}ki% 'MɉIOlYڐ[4-zUt5Xv"@NzwĻS1u8pܳV( ??QK8ٻFު=MDvD!YV nʰk"MkpY*9BZuq:k2oYj1ZՔbϐ=rkk>Zݫ;5 E"&VP ~2 =oB _b`s7ȴF1߽{:[[a?M{`OVhP<*nmm !$km0m!5f>XW=ۦ׬[k8š<DV JiekcLwHAoWי46VƵ.tZDognC[~3lIծ:#L`C:ۧOȋ`KÓ.XĸE-A$"9皁EmӍ5>V5A4h&MhQd+lުC! ,EwtvD|٩c:f hf2u-N؋׭Lw:'茑7C5@?[OFg9sL'(?0}J ;qVIyuH?AjbV8sO8&㠦)Co)c\Ι{nj1݁$G$1 M ȎFw)7P#=?'#Aocغ~@@vWX`Dz@i\"WZƼD0"z]"ɏw3^q^"̎g]DۥA  L {ECO:0000305}. FT /FTId=VAR_000001. FT VARIANT 3 3 A -> LFSJFSHLJSDHFLSJLFHSJLLSJKDHFLSKJFHJ. FT /FTId=VAR_000002. ** ** ################# SOURCE SECTION ################## ** ################# INTERNAL SECTION ################## **EV EI1; EMBL; CAA80960.1; 03-SEP-1989. **EV EC2; Curator; MM; 06-SEP-1989. **EV EC3; Curator; TT; 10-JUN-1999. **OX 9913; SQ SEQUENCE 430 AA; 47513 MW; 16DDF475382035AA CRC64; MALLHSGRFL SGVAAAFHPG LAAAASARAS SWWAHVEMGP PDPILGVTEA FKRDTNSKKM NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIA GLAEFCKASA ELALGENNEV LKSGRYVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP TWGNHTPIFR DAGMQLQSYR YYDPKTCGFD FTGAIEDISK IPAQSVILLH ACAHNPTGVD PRPEQWKEMA TVVKKNNLFA FFDMAYQGFA SGDGNKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE AKRVESQLKI LIRPMYSNPP INGARIASTI LTSPDLRKQW LHEVKGMADR IISMRTQLVS NLKKEGSSHN WQHIIDQIGM FCYTGLKPEQ VERLTKEFSI YMTKDGRISV AGVTSGNVAY LAHAIHQVTK // Swissknife_1.75/t/evidence.t0000644005110600510130000000633712400120115016256 0ustar ecastroSwissProt## Swissknife Test Harness Script for evidence tags ## # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}evidence.txl"; my $testout = "${where}evidence.txl.out"; my $expectedout = "${where}evidence.txl.expected"; open (IN, $testin); open (OUT, ">$testout"); use SWISS::Entry; # Read an entire record at a time $/ = "\/\/\n"; while (){ # Read the entry $entry = SWISS::Entry->fromText($_, 1); #${$entry->DEs->list}[3]->deleteEvidenceTag('EC3'); #evidence tagging the DE elements currently not supported #${$entry->DEs->list}[2]->addEvidenceTag('EC3'); foreach $ref ($entry->Refs->elements()) { $ref->addEvidenceTag('ECO:0000269|PubMed:11433298'); } $ev1 = $entry->Stars->EV->addEvidence('ECO:0000269', 'PubMed:11433298', 'XXX', '28-Aug-2014'); # p.s. EV->add/updateEvidence now only work with new style evidences!... $ev2 = $entry->Stars->EV->addEvidence('ECO:0000269', 'PubMed:12665801', 'XXX', '28-Aug-2014'); $ev3 = $entry->Stars->EV->addEvidence('ECO:0000312', 'EMBL:EAL60914.1', 'XXX', '28-Aug-2014'); $entry->DEs->setEvidenceTags($ev3); $entry->DEs->addEvidenceTag($ev2); if ($entry->DEs->hasEvidenceTag($ev2)){ print OUT "Has evidence $ev2.\n"; } # test changed as no longer makes sense for revised CC module @CCs = $entry->CCs->elements(); foreach $cc (@CCs) { if (!$cc->isa('SWISS::ListBase')) { $cc->addEvidenceTag($ev1); } } foreach $dr ($entry->DRs->elements) { $entry->DRs->addEvidenceTag($dr, 'ECO:0000269|PubMed:11433298'); $entry->DRs->deleteEvidenceTag($dr, 'ECO:0000303'); } # Check conditional delete $entry->DRs->add(['ZFIN', 'P123', 'Q1234', ' {ECO:0000312|EMBL:EAL60914.1}']); $entry->DRs->add(['ZFIN', 'P123', 'Q1234', ' {ECO:0000269|PubMed:12527781}']); foreach $ft ($entry->FTs->elements) { $entry->FTs->addEvidenceTag($ft, 'ECO:0000269|PubMed:11433298'); $entry->FTs->deleteEvidenceTag($ft, 'ECO:0000305'); } foreach $kw ($entry->KWs->elements) { $kw->addEvidenceTag($ev2); $kw->deleteEvidenceTag('EC2'); } my $newkw = new SWISS::KW; $newkw->text('Key1'); $entry->KWs->add($newkw); $newkw->setEvidenceTags($ev3); $newkw = new SWISS::KW; $newkw->text('Key2'); $newkw->setEvidenceTags($ev3); $newkw->deleteEvidenceTag($ev3); $entry->KWs->add($newkw); my $newTax = new SWISS::OX; $newTax->text(3332); $entry->OXs->NCBI_TaxID->add($newTax); foreach $os ($entry->OSs->elements) { $os->addEvidenceTag('ECO:0000269|PubMed:11433298'); $os->deleteEvidenceTag('ECO:0000269|PubMed:11433298'); } # Test if the Swiss-Prot style evidence (POTENTIAL etc) and the # evidence tags are properly separated. foreach $ft ($entry->FTs->elements()) { print OUT join ",", @$ft, "\n"; } print OUT $entry->toText; } close IN; close OUT; print "checking expected output...\n"; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; Swissknife_1.75/t/GNs.t0000644005110600510130000000446010225167417015201 0ustar ecastroSwissProt# Swissknife Test Harness Script for GNs # # Purpose: # Check whether the advanced parser in GNs works well. # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } use SWISS::GNs; my $where = -d 't' ? "t/" : ""; my $testout = "${where}GNs.txl.out"; my $expectedout = "${where}GNs.txl.expected"; open (OUT, ">$testout"); my $out=""; my $text = "GN (A{EA1} OR B{EI2}) And C.\n"; my $gn=SWISS::GNs->fromText(\$text,1); $gn->toText(\$out); print OUT $out; #ev tags for my $gg ($gn->elements) { for(my $i=0;$i<$gg->size;$i++) { ${$gg->list}[$i]->evidenceTags($1.($2+1).$3) if ${$gg->list}[$i]->evidenceTags =~ /^(.*)(\d+)(.*)$/; ; } } $out=""; $gn->toText(\$out); print OUT $out; #delimiter $gn->lowercase; $out=""; $gn->toText(\$out); print OUT $out; my $gn2=SWISS::GNs->fromText(\"GN A{EA1} or B{EA2}.\n",1); $out=""; $gn2->toText(\$out); print OUT $out; $gn2=SWISS::GNs->fromText(\"GN Timeo danaos, and dona ferentes.\n",1); $gn2->and(" et "); $out=""; $gn2->toText(\$out); print OUT $out; #remove GN $gn->head->pop; $out=""; $gn->toText(\$out); print OUT $out; $gn->head->set; $out=""; $gn->toText(\$out); print OUT $out; $gn->head->set; $out=""; $gn->toText(\$out); print OUT $out || "(Nothing)\n"; #remove genegroups $gn=SWISS::GNs->fromText(\$text,1); @{$gn->list}=(); $out=""; $gn->toText(\$out); print OUT $out || "(Nothing)\n"; #adding genegroups @{$gn->list} = SWISS::GeneGroup->fromText("Wallace OR Gromit"); $out=""; $gn->toText(\$out); print OUT $out; #wrapping push @{$gn->list}, SWISS::GeneGroup->fromText("So long vict OR ious, happy 'n gl OR ious, long to reign over us"); $out=""; $gn->toText(\$out); print OUT $out; unshift @{$gn->list}, SWISS::GeneGroup->fromText("Foobar"); $out=""; $gn->toText(\$out); print OUT $out; $gn->is_old_format(0); $out=""; $gn->toText(\$out); print OUT $out; $out = ' ' . $out; $gn = SWISS::GNs->fromText(\$out); $gn->item(2)->Names->splice (1,1); $out=""; $gn->toText(\$out); print OUT $out; close OUT; print "checking expected output...\n"; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; Swissknife_1.75/t/annot.txl0000644005110600510130000006427610745674576016230 0ustar ecastroSwissProtID DCTQ_RHOSH Unreviewed; 227 AA. AC Q9LBD9; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE Putative small C4-dicarboxylate integral membrane transport protein. GN DCTQ. OS Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1063; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=4P1; ** nothing has been published RA Omrani M.D.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR C4-DICARBOXYLATE TRANSPORT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (BY SIMILARITY). **this miscellaneous CC line should be deleted CC -!- MISCELLANEOUS: SHOWS POOR SPECIFICITY. CC -!- SEQUENCE CAUTION: CC Sequence=CAI22254; Type=Miscellaneous discrepancy; Positions=Several; Note=Translated as Gln; CC Sequence=CAI22254; Type=Erroneous gene model prediction; Positions=1528, 1529; CC Sequence=CAI21743; Type=Miscellaneous discrepancy; Positions=1528; CC Sequence=CAI21743; Type=Erroneous gene model prediction; DR EMBL; AF005842; AAF72734.1; -. PE 1; Evidence at protein level; KW Transmembrane; Transport. FT TOPO_DOM 1 10 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 11 29 BY SIMILARITY. FT TOPO_DOM 30 68 PERIPLASMIC (BY SIMILARITY). FT TRANSMEM 69 91 BY SIMILARITY. FT TOPO_DOM 92 112 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 113 133 BY SIMILARITY. FT TOPO_DOM 134 152 PERIPLASMIC (BY SIMILARITY). FT TRANSMEM 153 173 BY SIMILARITY. **argh FT TOPO_DOM 174 227 CYTOPLASMIC (BY SIMILARITY). ** ** ################# SOURCE SECTION ################## ** Rhodobacter sphaeroides C4-dicarboxylate binding-protein precursor (dctP), ** small integral membrane transport protein (dctQ) and large integral ** membrane transport protein (dctM) genes, complete cds. ** source 1..3718 ** /db_xref="taxon:1063" ** /organism="Rhodobacter sphaeroides" ** /strain="4P1" ** CDS 1214..1897 ** /codon_start=1 ** /note="DctQ; contains four putative transmembrane helices" ** /transl_table=11 ** /gene="dctQ" ** /product="small integral membrane transport protein" ** /protein_id="AAF72734.1" ** CDS_IN_EMBL_ENTRY 3 ** 02-JUN-2000 (Rel. 63, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_RHOSH SQ SEQUENCE 227 AA; 24991 MW; 2208AD920C1230DA CRC64; MMRLLDRLEE TLIASLIAAA TGLIFVSVVQ RYSLGLLADG VAFFRGHDMP ELSAMMRSAY LGLREFNLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINKLDERK RGFFILLGLG AGALFTGIIA TLGGNFVWHM AQTSAISPDL ELPMWLVYLA IPLGSALMCF RFLQVAVIFA RTGELAHHDH GHVEGVDTED EGIDVLGSTF LKSPLTPRDL VEKPKDE // ID DCTQ_WOLSU PRELIMINARY; PRT; 170 AA. AC Q9ZEJ3; DT 01-MAY-1999 (TrEMBLrel. 10, Created) DT 01-MAY-1999 (TrEMBLrel. 10, Last sequence update) DT 01-MAY-1999 (TrEMBLrel. 10, Last annotation update) DE Small C4-dicarboxylate integral membrane transport protein. ** unsure gene name, ** will be deleted GN DCTQ. OS Wolinella succinogenes. OC Bacteria; Proteobacteria; epsilon subdivision; Helicobacter group; OC Wolinella. OX NCBI_TaxID=844; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DSMZ 1740; RX MEDLINE=20461222; PubMed=11004174; RA Ullmann R., Gross R., Simon J., Unden G., Kroeger A.; RT "Transport of C(4)-dicarboxylates in Wolinella succinogenes."; RL J. Bacteriol. 182:5757-5764(2000). CC -!- FUNCTION: INVOLVED IN THE ELECTROGENIC UNIPORT OF C4- CC DICARBOXYLATES. ** or should this be in similarity?, do things in similarity have to have ++ a dr line? CC -!- PATHWAY: BELONGS TO THE TRIPARTITE ATP-INDEPENDENT PERIPLASMIC CC (TRAP) TRANSPORTER FAMILY DR EMBL; AJ132740; CAA10757.1; -. ** ** ################# SOURCE SECTION ################## ** Wolinella succinogenes dctP, dctQ and dctM genes, and partial orfN ** source 1..3309 ** /organism="Wolinella succinogenes" ** /db_xref="taxon:844" ** CDS 1086..1598 ** /db_xref="PID:e1375211" ** /transl_table=11 ** /gene="dctQ" ** /product="small integral C4-dicarboxylate membrane ** transport protein, putative" ** /protein_id="CAA10757.1" ** CDS_IN_EMBL_ENTRY 4 ** 04-FEB-1999 (Rel. 58, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_WOLSU SQ SEQUENCE 170 AA; 18753 MW; 4CCF9F77E2F85C20 CRC64; MSKFFEILDL GIAAMNKSIA VIGISTGVIL AFINVVLRYF FDSGLTWAGE TINYLFIWSA LFGAAYGFKK GIHIAVTILV ERFPPLLAKA SLMIASLISL IFLLFIAYFG LHYVLLVKDM GFMSVDLGIP QWIPMVVIPV AFFAASYRVG EKIYEISKQP ADTVVKSAGR // ID DCTQ_RHOCA PRELIMINARY; PRT; 227 AA. AC O07837; DT 01-JUL-1997 (TrEMBLrel. 04, Created) DT 01-JUL-1997 (TrEMBLrel. 04, Last sequence update) DT 01-NOV-1998 (TrEMBLrel. 08, Last annotation update) DE Small C4-dicarboxylate integral membrane transport protein. GN DCTQ. OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1061; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=B11; RX MEDLINE=92236423; PubMed=1809844; RA Shaw J.G., Hamblin M.J., Kelly D.J.; RT "Purification, characterization and nucleotide sequence of the RT periplasmic C4-dicarboxylate-binding protein (DctP) from Rhodobacter RT capsulatus."; RL Mol. Microbiol. 5:3055-3062(1991). RN [2] RP SEQUENCE FROM N.A. ** I see SB10003 / St Louis as the strain from table 1, not B10. This may be due to an error. RC STRAIN=B11; RX MEDLINE=97431499; PubMed=9287004; RA Forward J.A., Behrendt M.C., Wyborn N.R., Cross R., Kelly D.J.; RT "TRAP transporters: a new family of periplasmic solute transport RT systems encoded by the dctPQM genes of Rhodobacter capsulatus and by RT homologs in diverse gram-negative bacteria."; RL J. Bacteriol. 179:5482-5493(1997). RN [3] RP DISCUSSION OF SEQUENCE. RX MEDLINE=20090467; PubMed=10627041; RA Rabus R., Jack D.L., Kelly D.J., Saier M.H. Jr; RT "TRAP transporters: an ancient family of extracytoplasmic RT solute-receptor-dependent secondary active transporters."; RL Microbiology 145:3431-3445(1999). RN [4] RP TOPOLOGY. RC STRAIN=B10; RX PubMed=11150659; RA Wyborn N.R., Alderson J., Andrews S.C., Kelly D.J.; RT "Topological analysis of DctQ, the small integral membrane protein of RT the C4-dicarboxylate TRAP transporter of Rhodobacter capsulatus."; RL FEMS Microbiol. Lett. 194:13-17(2001). CC -!- FUNCTION: REQUIRED FOR C4-DICARBOXYLATE TRANSPORT (table 2,ref2). ** we could also say that transport is thought to use the membrane ** potential, in that case we might put it into function. Note that in ** ref 4 the use of an electrochemical gradient for energy is now sure ** and is cited in the intro. CC -!- ENZYME REGULATION: TRANSPORT IS SENSITIVE TO MEMBRANE POTENTIAL CC UNCOUPLERS AND VANADATE INSENSITIVE (ref2 figs 6&7). ** inner membrane upon expression in ecoli, but can we extrapolate to Rhoca? CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (ref2 fig4). DR EMBL; AE009099; AAL42381.1; -. DR EMBL; X63974; CAA45386.1; -. DR Pfam; PF00627; UBA; 1. DR PROSITE; PS12345; TEST_DOMAIN; 1. ** PROSITE; PS12346; FALSE_DOMAIN; FALSE_POS. KW Transmembrane; Transport. FT TOPO_DOM 1 10 CYTOPLASMIC. FT TRANSMEM 11 29 FT TOPO_DOM 30 68 PERIPLASMIC. FT TRANSMEM 69 91 FT TOPO_DOM 92 112 CYTOPLASMIC. FT TRANSMEM 113 133 FT TOPO_DOM 134 152 PERIPLASMIC. FT TRANSMEM 153 173 FT TOPO_DOM 174 227 CYTOPLASMIC. ** transmembrane regions are unsure ** ** ################# SOURCE SECTION ################## ** R capsulatus dctP gene for C4-dicarboxylase binding protein ** source 1..4500 ** /organism="Rhodobacter capsulatus" ** /strain="B10" ** /clone_lib="Cosmid, pLAFR1" ** /clone="pDCT200, pDCT205" ** /chromosome="1" ** CDS 1084..1767 ** /gene="dctQ" ** /product="small integral membrane transport protein" ** /db_xref="PID:e324693" ** CDS_2_OUT_OF_5 ** 26-JUN-1997 (Rel. 52, Last updated, Version 20) ** ################# INTERNAL SECTION ################## **ID XXXX_RHOCA SQ SEQUENCE 227 AA; 24763 MW; 0DE9D59DE5450F99 CRC64; MLRILDRAEE VLIAALIATA TVLIFVSVTH RFTLGFVADF VGFFRGHGMT GAAAAAKSLY TTLRGINLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINRLDAPK RRFFILLGLG AGALFTGIIA TLGANFVLHM YHASSTSPDL ELPMWLVYLA IPMGSSLMCF RFLQVAFGFA RTGELPHHDH GHVDGVDTEN EGIDAEGDVL LHSPLTPRDL VEKPKDN // ID BL1A_HUMAN PRELIMINARY; PRT; 835 AA. **BCLA_human = O95999 AC Q9H165; Q86W14; Q8WU92; Q96JL6; Q9H163; Q9H164; Q9H3G9; Q9NWA7; DT 01-MAR-2001 (TrEMBLrel. 16, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-MAR-2003 (TrEMBLrel. 23, Last annotation update) DE B-cell CLL/lymphoma 11A. GN BCL11A OR EVI9 OR KIAA1809. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; ** Q9H3G9; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 4 AND 5). RC TISSUE=Fetal brain; RX PubMed=11161790; RA Saiki Y., Yamazaki Y., Yoshida M., Katoh O., Nakamura T.; RT "Human EVI9, a homologue of the mouse myeloid leukemia gene, is RT expressed in the hematopoietic progenitors and down-regulated during RT myeloid differentiation of HL60 cells."; RL Genomics 70:387-391(2000). ** Q9H165 Q9H163; Q9H164; RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 3). RX PubMed=11719382; RA Satterwhite E., Sonoki T., Willis T.G., Harder L., Nowak R., RA Arriola E.L., Liu H., Price H.P., Gesk S., Steinemann D., RA Schlegelberger B., Oscier D.G., Siebert R., Tucker P.W., Dyer M.J.; RT "The BCL11 gene family: involvement of BCL11A in lymphoid RT malignancies."; RL Blood 98:3413-3420(2001). **Q86W14; RN [3] RP SEQUENCE FROM N.A. (ISOFORM 6). RA Suriyapperuma S.P., Sarfarazi M.; RT "Identification of a new isoform for B-cell CLL/lymphoma 11A (BCL11A) RT gene."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. ** Q96JL6 RN [4] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11853319; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXII. RT The complete sequences of 50 new cDNA clones which code for large RT proteins."; RL DNA Res. 8:319-327(2001). ** Q9NWA7; RN [5] RP SEQUENCE FROM N.A. (ISOFORM 7). RC TISSUE=Embryo; RX PubMed=14702039; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J.-I., Saito K., Kawai Y., Isono Y., Nakamura Y., RA Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., RA Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., RA Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., RA Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., RA Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., RA Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., RA Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., RA Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., RA Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., RA Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). ** Q96JL6 RN [6] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Lymph; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length RT human and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). ** PG 387 REF1 CC -!- FUNCTION: An essential factor in lymphopoiesis and is required for CC B-cell formation in fetal liver. May play important roles in CC leukemogenesis and hematopoiesis. Might act as a dominant proto- CC oncogene. Potentiates ARP1-mediated transcriptional repression in CC a trichostatin-insensitive manner (By similarity). **CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=XL; CC IsoId=Q9H165-1; Sequence=Displayed; CC Note=; CC Name=2; Synonyms=L; CC IsoId=Q9H165-2; Sequence=?; CC Note=; CC Name=3; Synonyms=S; CC IsoId=Q9H165-3; Sequence=?; CC Note=May be due to an exon skipping; CC Name=4; CC IsoId=Q9H165-4; Sequence=?; CC Note=; CC Name=5; CC IsoId=Q9H165-5; Sequence=?; CC Note=; CC Name=6; CC IsoId=Q9H165-6; Sequence=?; CC Note=; CC Name=7; CC IsoId=Q9H165-7; Sequence=?; CC Note=; **PG 389 REF1 2 pg3415 CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, spleen CC thymus, bone marrow and testis. Expressed in CD34-positive myeloid CC precursor cells, B cells, monocytes, and megakaryoctes. Expression CC is tightly regulated during B-cell development. CC -!- DISEASE: May be involved in lymphoid malignancies through either CC chromosomal translocation t(2;14)(p13;q32.3), or amplification. **add standard line about chromosomal translocation, add Ft line for breakpoints if known **add cc similarity ** Q9H3G9; DR EMBL; AF080216; AAG49025.1; -. ** Q9H165; Q9H163;Q9H164; DR EMBL; AJ404611; CAC17723.1; -. DR EMBL; AJ404612; CAC17724.1; -. DR EMBL; AJ404613; CAC17725.1; -. **Q86W14; DR EMBL; AY228763; AAO88272.1; -. **Q96JL6; Q8WU92; DR EMBL; AB058712; BAB47438.1; ALT_INIT. ** Q9NWA7; DR EMBL; AK001035; BAA91476.1; -. **Q96JL6; Q8WU92; DR EMBL; BC021098; AAH21098.1; ALT_INIT. DR HSSP; P15822; 1BBO. DR HGNC; HGNC:13221; BCL11A. DR MIM; 606557; -. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 6. DR SMART; SM00355; ZnF_C2H2; 6. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. KW B-cell activation; Metal-binding; Zinc; Zinc-finger; KW Chromosomal translocation; Transcription regulation; KW Alternative splicing. FT ZN_FING 170 193 C2H2-type 1. FT ZN_FING 377 399 C2H2-type 2. FT ZN_FING 405 429 C2H2-type 3. FT ZN_FING 742 764 C2H2-type 4. FT ZN_FING 770 792 C2H2-type 5. FT ZN_FING 800 823 C2H2-type 6. FT COMPBIAS 260 373 Pro-rich. FT COMPBIAS 481 509 Glu-rich. FT VAR_SEQ 1 648 Missing (in isoform 7). FT VAR_SEQ 1 1 M -> MSKGTDEDIFSGVSFFLTRLSRCEPSRRPPAPQPT FT (in isoform 4 and isoform 5). FT VAR_SEQ 129 163 DKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGIC -> G FT (in isoform 6). FT VAR_SEQ 211 239 VGIPSGLGAECPSQPPLHGIHIADNNPFN -> CSSHTPIR FT RSTQRAQDVWQFSDGSRALKF (in isoform 5). FT VAR_SEQ 212 243 GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI -> LHTPP FT FGVVPRELKMCGSFRMEAREPLSSEKI (in isoform FT 3). FT VAR_SEQ 240 835 Missing (in isoform 5). FT VAR_SEQ 244 835 Missing (in isoform 3). FT VAR_SEQ 522 532 Missing (in isoform 4). FT VAR_SEQ 745 773 EYCGKVFKNCSNLTVHRRSHTGERPYKCE -> SSHTPIRR FT STQRAQDVWQFSDGSSRALKF (in isoform 2). FT VAR_SEQ 745 773 EYCGKVFKNCSNLTVHRRSHTGERPYKCE -> SSHTPIRR FT STQRAQDVWQFSDGSSRALKF (in isoform 4). FT VAR_SEQ 774 835 Missing (in isoform 2). FT CONFLICT 119 119 G -> R (in Ref. 2). FT CONFLICT 316 316 S -> F (in Ref. 1). FT CONFLICT 386 386 F -> L (in Ref. 1). FT CONFLICT 648 648 A -> T (in Ref. 2; CAC17723/CAC17724). FT CONFLICT 653 653 E -> D (in Ref. 1). FT CONFLICT 730 730 P -> T (in Ref. 2; CAC17723/CAC17724). ** ** ################# INTERNAL SECTION ################## **CL 2p16.1; **NI BCLLA **IS Q9H165-8. SQ SEQUENCE 835 AA; 91196 MW; D36A7D0BE6976DCF CRC64; MSRRKQGKPQ HLSKREFSPE PLEAILTDDE PDHGPLGAPE GDHDLLTCGQ CQMNFPLGDI LIFIEHKRKQ CNGSLCLEKA VDKPPSPSPI EMKKASNPVE VGIQVTPEDD DCLSTSSRGI CPKQEHIADK LLHWRGLSSP RSAHGALIPT PGMSAEYAPQ GICKDEPSSY TCTTCKQPFT SAWFLLQHAQ NTHGLRIYLE SEHGSPLTPR VGIPSGLGAE CPSQPPLHGI HIADNNPFNL LRIPGSVSRE ASGLAEGRFP PTPPLFSPPP RHHLDPHRIE RLGAEEMALA THHPSAFDRV LRLNPMAMEP PAMDFSRRLR ELAGNTSSPP LSPGRPSPMQ RLLQPFQPGS KPPFLATPPL PPLQSAPPPS QPPVKSKSCE FCGKTFKFQS NLVVHRRSHT GEKPYKCNLC DHACTQASKL KRHMKTHMHK SSPMTVKSDD GLSTASSPEP GTSDLVGSAS SALKSVVAKF KSENDPNLIP ENGDEEEEED DEEEEEEEEE EEEELTESER VDYGFGLSLE AARHHENSSR GAVVGVGDES RALPDVMQGM VLSSMQHFSE AFHQVLGEKH KRGHLAEAEG HRDTCDEDSV AGESDRIDDG TVNGRGCSPG ESASGGLSKK LLLGSPSSLS PFSKRIKLEK EFDLPPAAMP NTENVYSQWL AGYAASRQLK DPFLSFGDSR QSPFASSSEH SSENGSLRFS TPPGELDGGI SGRSGTGSGG STPHISGPGP GRPSSKEGRR SDTCEYCGKV FKNCSNLTVH RRSHTGERPY KCELCNYACA QSSKLTRHMK THGQVGKDVY KCEICKMPFS VYSTLEKHMK KWHSDRVLNN DIKTE // ID NUSG_SULAC STANDARD; PRT; 152 AA. AC P27341; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative transcription antitermination protein nusG. OS Sulfolobus acidocaldarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=2285; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92048486; PubMed=1658539; RA Ramirez C., Matheson A.T.; RT "A gene in the archaebacterium Sulfolobus solfataricus that codes for RT a protein equivalent to the alpha subunits of the signal recognition RT particle receptor in eukaryotes."; RL Mol. Microbiol. 5:1687-1693(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 33909 / NCIB 11770 / DSM 639; RX MEDLINE=95226466; PubMed=7711082; RA Moll R., Schmidtke S., Schaefer G.; RT "Nucleotide sequence of a gene cluster encoding ribosomal proteins in RT the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius."; RL Biochim. Biophys. Acta 1261:315-318(1995). RN [3] RP SIMILARITY. RX MEDLINE=95206934; PubMed=7899076; RA Ouzounis C., Kyrpides N., Sander C.; RT "Novel protein families in archaean genomes."; RL Nucleic Acids Res. 23:565-570(1995). CC -!- SIMILARITY: TO BACTERIAL PROTEINS NUSG AND ALSO TO THE L24P FAMILY CC OF RIBOSOMAL PROTEINS. CC -!- CAUTION: Was originally (Ref.1) thought to originate from CC S.solfataricus strain P1, but the culture was contaminated with CC S.acidocaldarius. DR EMBL; X58538; CAA41431.1; -. DR EMBL; X77509; CAA54645.1; -. DR PIR; S53705; S53705. DR InterPro; IPR003257; Bac_NusG. DR InterPro; IPR005824; KOW. DR InterPro; IPR006646; KOW_sub. DR InterPro; IPR006645; NgN. DR InterPro; IPR008991; Transl_SH3_like. DR Pfam; PF00467; KOW; 1. DR ProDom; PD005267; Bac_NusG; 1. DR SMART; SM00739; KOW; 1. DR SMART; SM00738; NGN; 1. ** PROSITE; PS01108; RIBOSOMAL_L24; FALSE_POS_1. ** PROSITE; PS00430; TONB_DEPENDENT_REC_1; FALSE_POS_1. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 152 AA; 16877 MW; 316F31BBCC22620D CRC64; MEDFKYRNYY VLRVTGGQEI NVALILEERI KTNNINEIFS VVVPPNIKGY VILEATGPHV VKLISSGIRH VKGVAHGLIQ KEDVTKFVSK SVALPAVKEG DLVEVISGPF RGMQAQVVRV ESTKNEVVLN ILESSYPVQV TVPLEQVKPV KR // ID NUSG_SULAC STANDARD; PRT; 152 AA. AC P27341; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative transcription antitermination protein nusG. OS Sulfolobus acidocaldarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=2285; CC -!- FUNCTION: Nonselective ADPR-gated cation channel mediating sodium CC and calcium ion influx in response to oxidative stress. CC Extracellular calcium passes through the channel and acts from the CC intracellular side as a positive regulator in channel activation CC by hydrogen superoxide. Also activated by nicotinamide adenine CC dinucleotide (NAD(+)), reactive nitrogen species and arachidonic CC acid. Confers susceptibility to cell death following oxidative CC stress. Isoform 2 does not seem to be regulated by ADPR. Has an CC ADP-ribose pyrophosphatase activity. CC -!- CATALYTIC ACTIVITY: ADP-ribose + H(2)O = AMP + D-ribose 5- CC phosphate. **no evidence found CC -!- COFACTOR: Binds NAD(+). CC -!- SUBUNIT: Isoform 1 can interact with isoform 3. This interaction CC decreases calcium influx through isoform 1 and suppresses CC susceptibility to oxidative stress-induced cell death. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=1; Synonyms=TRPM2-L; CC IsoId=O94759-1; Sequence=Displayed; CC Name=2; CC IsoId=O94759-2; Sequence=VSP_006574, VSP_006575; CC Name=3; Synonyms=TRPM2-S; CC IsoId=O94759-3; Sequence=?; CC -!- TISSUE SPECIFICITY: Highly expressed in brain and peripheral blood CC cells, such as neutrophils. Also detected in bone marrow, spleen, CC heart, liver and lung. Isoform 2 is found in neutrophil CC granulocytes. CC -!- SIMILARITY: Belongs to the transient receptor family. LTrpC CC subfamily. CC -!- CAUTION: Ref.5 sequence differs from that shown due to frameshifts CC in positions 1227 and 1237. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=100 uM for ADP-ribose; CC Vmax=0.1 umol/min/mg enzyme; ** ################# INTERNAL SECTION ################## SQ SEQUENCE 152 AA; 16877 MW; 316F31BBCC22620D CRC64; MEDFKYRNYY VLRVTGGQEI NVALILEERI KTNNINEIFS VVVPPNIKGY VILEATGPHV VKLISSGIRH VKGVAHGLIQ KEDVTKFVSK SVALPAVKEG DLVEVISGPF RGMQAQVVRV ESTKNEVVLN ILESSYPVQV TVPLEQVKPV KR // ID PAX3_HUMAN STANDARD; PRT; 479 AA. AC P23760; Q16448; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Paired box protein Pax-3 (HUP2). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 479 AA; 52968 MW; 8AFCA674E3ACB4FE CRC64; MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNPDS SSAYCLPSTR HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE PTTTVSASCS QRLDHMKSLD SLPTSQSYCP PTYSTTGYSM DPVTGYQYGQ YGQSKPWTF // Swissknife_1.75/t/evidence.txl.expected0000644005110600510130000001103412573303763020437 0ustar ecastroSwissProtHas evidence ECO:0000269|PubMed:12665801. TRANSIT,1,29,MITOCHONDRION,,, {ECO:0000303, ECO:0000269|PubMed:11433298}, CHAIN,30,430,ASPARTATE AMINOTRANSFERASE,,, {ECO:0000303, ECO:0000269|PubMed:11433298}, BINDING,279,279,PYRIDOXAL PHOSPHATE,BY SIMILARITY,, {ECO:0000269|PubMed:11433298}, VARIANT,3,3,A -> L,,/FTId=VAR_000001, {ECO:0000269|PubMed:11433298}, VARIANT,3,3,A -> LFSJFSHLJSDHFLSJLFHSJLLSJKDHFLSKJFHJ,,/FTId=VAR_000002, {ECO:0000269|PubMed:11433298}, ID AATM_BOVIN STANDARD; PRT; 430 AA. AC P12344; DT 01-OCT-1989 (Rel. 12, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL PRECURSOR (EC 2.6.1.1) DE (TRANSAMINASE A) (GLUTAMATE OXALOACETATE TRANSAMINASE-2) DE {ECO:0000312|EMBL:EAL60914.1, ECO:0000269|PubMed:12665801}. GN GOT2{EI1}. OG Plasmid pCP301 {ECO:0000313|EMBL:AAH50488.1, OG ECO:0000269|PubMed:11285225}, Plasmid pWR100, Plasmid pINV_F6_M1382, OG and Plasmid pSF5; Chloroplast. OS Bos taurus (Bovine){EI1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=126566, 55{EC2}, 3332; RN [1] {EI1, ECO:0000269|PubMed:11433298} RP SEQUENCE FROM N.A. RC TISSUE=HEART; RA Palmisano A.; RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases. RN [2] {EI1, ECO:0000269|PubMed:11433298} RP SEQUENCE OF 30-41. RX MEDLINE=79191877; PubMed=446759; RA Capasso S., Garzillo A.M., Marino G., Mazzarella L., Pucci P., RA Sannia G.; RT "Mitochondrial bovine aspartate aminotransferase. Preliminary sequence RT and crystallographic data."; RL FEBS Lett. 101:351-354(1979). CC -!- CATALYTIC ACTIVITY: L-ASPARTATE + 2-OXOGLUTARATE = OXALOACETATE + CC L-GLUTAMATE{EC3}. {ECO:0000269|PubMed:11433298}. CC -!- COFACTOR: CC Note=PYRIDOXAL PHOSPHATE.{EC3}; CC -!- SEQUENCE CAUTION: CC Sequence=CAI21743; Type=Erroneous gene model prediction; CC Sequence=CAI22254{EC1,EI1}; Type=Miscellaneous discrepancy; Positions=Several; Note=Translated as Gln; CC -!- RNA EDITING: Modified_positions=1, 4, 18, 33 CC {ECO:0000269|PubMed:10707984, ECO:0000269|PubMed:11285225}, 34, CC 72, 80, 86, 95, 121, 123, 154, 155, 156, 163, 169, 193, 196, 233, CC 295, 346; Note=The initiator methionine is created by RNA editing. CC The nonsense codons at positions 72, 121, 169, 193 and 346 are CC modified to sense codons. {ECO:0000269|PubMed:10707984}; DR EMBL; Z25466; CAA80960.1; -. {ECO:0000269|PubMed:11433298} DR ZFIN; P123; Q1234. {ECO:0000312|EMBL:EAL60914.1} DR ZFIN; P123; Q1234. {ECO:0000269|PubMed:12527781} DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. {ECO:0000269|PubMed:11433298} KW Transferase {ECO:0000269|PubMed:12665801}; KW Aminotransferase {ECO:0000269|PubMed:12665801}; KW Key1 {ECO:0000312|EMBL:EAL60914.1}; Key2. FT TRANSIT 1 29 MITOCHONDRION. {ECO:0000303, FT ECO:0000269|PubMed:11433298}. FT CHAIN 30 430 ASPARTATE AMINOTRANSFERASE. {ECO:0000303, FT ECO:0000269|PubMed:11433298}. FT BINDING 279 279 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT {ECO:0000269|PubMed:11433298}. FT VARIANT 3 3 A -> L. {ECO:0000269|PubMed:11433298}. FT /FTId=VAR_000001. FT VARIANT 3 3 A -> LFSJFSHLJSDHFLSJLFHSJLLSJKDHFLSKJFHJ FT . {ECO:0000269|PubMed:11433298}. FT /FTId=VAR_000002. ** ** ################# INTERNAL SECTION ################## **EV EC2; Curator; MM; 06-SEP-1989. **EV EC3; Curator; TT; 10-JUN-1999. **EV ECO:0000269; PubMed:11433298; XXX; 28-Aug-2014. **EV ECO:0000269; PubMed:12665801; XXX; 28-Aug-2014. **EV ECO:0000312; EMBL:EAL60914.1; XXX; 28-Aug-2014. **EV EI1; EMBL; CAA80960.1; 03-SEP-1989. **OX 9913; SQ SEQUENCE 430 AA; 47513 MW; 16DDF475382035AA CRC64; MALLHSGRFL SGVAAAFHPG LAAAASARAS SWWAHVEMGP PDPILGVTEA FKRDTNSKKM NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIA GLAEFCKASA ELALGENNEV LKSGRYVTVQ TISGTGALRI GASFLQRFFK FSRDVFLPKP TWGNHTPIFR DAGMQLQSYR YYDPKTCGFD FTGAIEDISK IPAQSVILLH ACAHNPTGVD PRPEQWKEMA TVVKKNNLFA FFDMAYQGFA SGDGNKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE AKRVESQLKI LIRPMYSNPP INGARIASTI LTSPDLRKQW LHEVKGMADR IISMRTQLVS NLKKEGSSHN WQHIIDQIGM FCYTGLKPEQ VERLTKEFSI YMTKDGRISV AGVTSGNVAY LAHAIHQVTK // Swissknife_1.75/t/DEs.t0000644005110600510130000000322010225167417015156 0ustar ecastroSwissProt# Swissknife Test Harness Script for DEs # # Purpose: # Check whether the advanced parser in DEs works well. # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}DEs.txl"; my $testout = "${where}DEs.txl.out"; my $expectedout = "${where}DEs.txl.expected"; open (IN, $testin); open (OUT, ">$testout"); use SWISS::Entry; # Read an entire record at a time $/ = "\/\/\n"; while (){ # Read the entry my $entry = SWISS::Entry->fromText($_,1); my $i; print OUT $entry->DEs->toString; for my $DEs ($entry->DEs) { print OUT "\nlist : ", join ', ', map {'"'.$_->text.'"'} $DEs->elements; print OUT "\nhasFragment : ", $DEs->hasFragment; print OUT "\nchildType : ", ""; } print OUT "\n>"; for my $p (["Includes", $entry->DEs->Includes], ["Contains", $entry->DEs->Contains]) { my ($type, $obj) = @$p; for my $child ($obj->elements) { print OUT "\nlist : ", join ', ', map {'"'.$_->text.'"'} $child->elements; print OUT "\nhasFragment : ", $child->hasFragment; print OUT "\nchildType : ", $type; } } print OUT "\n//\n"; unless ($is_not_first_entry++) { print OUT $entry->toText; $entry->DEs->text("Some strange protein (Fragment) (Version 2)"); print OUT $entry->toText; } } close IN; close OUT; print "checking expected output...\n"; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; Swissknife_1.75/t/FTId.txl0000644005110600510130000000073010265736434015645 0ustar ecastroSwissProtID XXXX_XXXXX PRELIMINARY; PRT; 1 AA. AC P00001; DT 01-JAN-2000 (TrEMBLrel. 15, Created) DT 01-JAN-2000 (TrEMBLrel. 15, Last sequence update) DT 01-JAN-2000 (TrEMBLrel. 15, Last annotation update) DE Foo protein. OC 1. FT TOPIC 1 10 Text. FT /FTId=FOO_0000000001. FT TOPIC 11 20 FT /FTId=FOO_0000000002. SQ SEQUENCE 1 AA; 0 MW; 0 CRC64; X // Swissknife_1.75/t/formatProblems.txl.expected0000644005110600510130000032166513133402155021653 0ustar ecastroSwissProtID PPK5_PERAM PRELIMINARY; PRT; 17 AA. AC P82617; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE PYROKININ-5 (PEA-PK-5) (FXPRL-AMIDE). OS Periplaneta americana (American cockroach). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Orthopteroidea; Dictyoptera; Blattaria; OC Blattoidea; Blattidae; Periplaneta. OX NCBI_TaxID=6978; RN [1] RP SEQUENCE, FUNCTION, AND MASS SPECTROMETRY. RC TISSUE=ABDOMINAL PERISYMPATHETIC ORGANS; RX MEDLINE=99212469; PubMed=10196736; RG The Three Stooges; RA Predel R., Kellner R., Nachman R.J., Holman G.M., Rapus J., Gaede G.; RT "Differential distribution of pyrokinin-isoforms in cerebral and RT abdominal neurohemal organs of the American cockroach."; RL Insect Biochem. Mol. Biol. 29:139-144(1999). RN [2] RP TISSUE SPECIFICITY. RC STRAIN=12,714 / SCARLATINA; RX MEDLINE=20189894; PubMed=10723010; RG The Three Stooges; RT "Tagma-specific distribution of FXPRLamides in the nervous system of RT the American cockroach."; RL J. Comp. Neurol. 419:352-363(2000). CC -!- FUNCTION: MEDIATES VISCERAL MUSCLE CONTRACTILE ACTIVITY (MYOTROPIC CC ACTIVITY). CC -!- TISSUE SPECIFICITY: MAINLY IN ABDOMINAL PERISYMPATHETIC ORGANS AND CC TO A LESSER EXTENT IN RETROCEREBRAL COMPLEX. CC -!- RNA EDITING: Modified_positions=2; CC -!- MASS SPECTROMETRY: Mass=1651.7; Method=MALDI; CC -!- SIMILARITY: BELONGS TO THE PYROKININ FAMILY. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR INTERPRO; IPR001484; -. DR PROSITE; PS00539; PYROKININ; UNKNOWN_1. KW Amidation; Neuropeptide; Pyrokinin. FT DOMAIN 638 758 CONTAINS CONSERVED RESIDUES USED FOR 3' FT -> 5' EXONUCLEASE ACTIVITIES. FT MOD_RES 17 17 AMIDATION. FT MOD_RES 17 17 AMIDATIONAMIDATIONAMIDATIONAMIDATIONAMIDA FT TIONAMIDATION. FT VARIANT 67 67 K -> M (IN ALLELE PGM1*7+, ALLELE FT PGM1*7-, ALLELE PGM1*3+ AND ALLELE FT PGM1*3-). FT /FTId=VAR_006090. FT VARIANT 74 74 Q -> R (IN A VERY SELDOM ENCOUNTERED RARE FT FORM OF HYPOGONADISMHYPOGONADISMHYPOGONAD FT ISMHYPOGONADISM; LACK OF RECEPTOR- FT BINDING). FT VARIANT 74 74 Q -> R (IN HYPOGONADISM; LACK OF FT RECEPTOR-BINDING). FT VARIANT 74 74 Q -> R (IN FT HYPOGONADISMHYPOGONADISMHYPOGONADISM- FT HYPOGONADISM; LACK OF RECEPTOR-BINDING). FT VARIANT 74 74 Q -> R (IN HYPOGONADISMHYPOGONADISMHYPOGO FT NADISMHYPOGONADISM; LACK OF RECEPTOR- FT BINDING). FT VARIANT 74 74 Q -> RRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRR FT (IN HYPOGONADISM). ** ** ################# INTERNAL SECTION ################## **ZZ CREATED AND FINISHED BY NICO. **ZZ DS 43484. **ZZ UPDATED BY NICO (7/8/00). ADDED TISSUE SPECIFICITY. **ZZ CURATED. SQ SEQUENCE 17 AA; 1653 MW; 8527162EA45BBA54 CRC64; GGGGSGETSG MWFGPRL // 1 ID PPK5_PERAM PRELIMINARY; PRT; 17 AA. AC P82617; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE Light-independent protochlorophyllide reductase subunit B (EC DE 1.18.-.-) (LI-POR subunit B) (DPOR subunit B). OS Periplaneta americana (American cockroach). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Orthopteroidea; Dictyoptera; Blattaria; OC Blattoidea; Blattidae; Periplaneta. OX NCBI_TaxID=6978; RN [1] RP SEQUENCE, FUNCTION, AND MASS SPECTROMETRY. RC TISSUE=ABDOMINAL PERISYMPATHETIC ORGANS; RX MEDLINE=99212469; PubMed=10196736; RG French Parkinson's disease genetics study group; RG European consortium on genetic susceptibility on Parkinson's disease; RA Predel R., Kellner R., Nachman R.J., Holman G.M., Rapus J., Gaede G.; RT "Differential distribution of pyrokinin-isoforms in cerebral and RT abdominal neurohemal organs of the American cockroach."; RL Insect Biochem. Mol. Biol. 29:139-144(1999). RN [2] RP TISSUE SPECIFICITY. RX MEDLINE=20189894; PubMed=10723010; RA Predel R., Eckert M.; RT "Tagma-specific distribution of FXPRLamides in the nervous system of RT the American cockroach."; RL J. Comp. Neurol. 419:352-363(2000). CC -!- FUNCTION: MEDIATES VISCERAL MUSCLE CONTRACTILE ACTIVITY (MYOTROPIC CC ACTIVITY). CC -!- TISSUE SPECIFICITY: MAINLY IN ABDOMINAL PERISYMPATHETIC ORGANS AND CC TO A LESSER EXTENT IN RETROCEREBRAL COMPLEX. CC -!- MASS SPECTROMETRY: MW=1651.7; METHOD=MALDI; CC -!- SIMILARITY: BELONGS TO THE PYROKININ FAMILY. DR INTERPRO; IPR001484; -. DR PRODOM; PD010497; -; 1. DR PROSITE; PS00539; PYROKININ; UNKNOWN_1. ** PROSITE; PS00537; PYROKININ; FALSE_POS_1. ** ** ################# INTERNAL SECTION ################## **PM PROSITE; PS00539; PYROKININ; 13; 17; ?; 06-SEP-2000; **ZZ CREATED AND FINISHED BY NICO. **ZZ DS 43484. **ZZ UPDATED BY NICO (7/8/00). ADDED TISSUE SPECIFICITY. **ZZ CURATED. SQ SEQUENCE 17 AA; 1653 MW; 8527162EA45BBA54 CRC64; GGGGSGETSG MWFGPRL // 1 ID O54521 PRELIMINARY; PRT; 144 AA. AC O54521; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE SLYA. GN SLYA. OS Salmonella enterica serovar Typhi. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Salmonella. OX NCBI_TaxID=90370, 119912; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=RF-1, and TY2; RA Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., RA Nonaka T., Matsui H., Kawahara K., Danbara H.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. DR EMBL; AB010777; BAA24582.1; -. DR EMBL; AB010776; BAA24581.1; -. DR INTERPRO; IPR000835; -. DR PFAM; PF01047; MarR; 1. DR PRINTS; PR00598; HTHMARR. ** PROSITE pattern is not entirely correct. Test comment. ** ** ################# SOURCE SECTION ################## ** PSMID1233 STANDARD ** Salmonella choleraesuis serovar Typhi gene for SlyA, complete cds. ** [1] ** 1-636 ** Okada N.; ** ; ** Submitted (27-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Nobuhiko Okada, Kitasato University, School of Pharmaceutical ** Sciences, ** Department of Microbiology; 5-9-1 Shirokane, Minato, Tokyo 108-8641, ** Japan (E-mail:okadan@platinum.pharm.kitasato-u.ac.j p, ** Tel:03-3444-6161, ** Fax:03-3444-4831) ** [2] ** Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., Nonaka ** T., ** Matsui H., Kawahara K., Danbara H.; ** "Identification of TTG initiation codon in slyA of Salmonella, a gene ** required for survival within macrophages"; ** Unpublished. ** [1] ** 1-636 ** Okada N.; ** ; ** Submitted (27-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Nobuhiko Okada, Kitasato University, School of Pharmaceutical ** Sciences, ** Department of Microbiology; 5-9-1 Shirokane, Minato, Tokyo 108-8641, ** Japan (E-mail:okadan@platinum.pharm.kitasato-u.ac.j p, ** Tel:03-3444-6161, ** Fax:03-3444-4831) ** [2] ** Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., Nonaka ** T., ** Matsui H., Kawahara K., Danbara H.; ** "Identification of TTG initiation codon in slyA of Salmonella, a gene ** required for survival within macrophages"; ** Unpublished. ** source 1..636 ** /organism="Salmonella choleraesuis serovar Typhi" ** /sequenced_mol="DNA" ** /strain="Ty2" ** CDS 154..588 ** /codon_start=1 ** /db_xref="PID:d1025502" ** /transl_table=11 ** /gene="slyA" ** /product="SlyA" ** CDS_IN_EMBL_ENTRY 1 ** ORGANISM DOESN'T EXIST IN SP ** 11-FEB-1998 (Rel. 54, Last updated, Version 2) ** source 1..636 ** /organism="Salmonella choleraesuis choleraesuis" ** /sequenced_mol="DNA" ** /strain="RF-1" ** CDS 154..588 ** /codon_start=1 ** /db_xref="PID:d1025501" ** /transl_table=11 ** /gene="slyA" ** /product="SlyA" ** CDS_IN_EMBL_ENTRY 1 ** ORGANISM DOESN'T EXIST IN SP ** 11-FEB-1998 (Rel. 54, Last updated, Version 2) ** ** ################# INTERNAL SECTION ################## **PM PFAM; PF01047; MarR; 29; 133; T; 28-JAN-2000; **PM PRINTS; PR00598; HTHMARR; 47; 63; T; 28-JAN-2000; **PM PRINTS; PR00598; HTHMARR; 64; 79; T; 28-JAN-2000; **PM PRINTS; PR00598; HTHMARR; 83; 99; T; 28-JAN-2000; **PM PRINTS; PR00598; HTHMARR; 113; 133; T; 28-JAN-2000; **PM PROSITE; PS01117; HTH_MARR_FAMILY; 62; 96; T; 02-MAY-2000; SQ SEQUENCE 144 AA; 16448 MW; 4647F7704F2D78DE CRC64; MESPLGSDLA RLVRIWRALI DHRLKPLELT QTHWVTLHNI HQLPPDQSQI QLAKAIGIEQ PSLVRTLDQL EDKGLISRQT CASDRRAKRI KLTEKAEPLI AEMEEVIHKT RGEILAGISS EEIELLIKLV AKLEHNIMEL HSHD // 0 ID FXR1_MOUSE PRELIMINARY; PRT; 677 AA. AC Q61584; Q9R1E2; Q9R1E3; Q9R1E4; Q9R1E5; Q9WUA7; Q9WUA8; Q9WUA9; DT 01-JUL-1997 (TrEMBLrel. 04, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-MAR-2001 (TrEMBLrel. 16, Last annotation update) DE Fragile X mental retardation syndrome related proteinase precursor DE domain - like protein. GN FXR1 OR FXR1H. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=010090; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RC TISSUE=FETAL BRAIN; RX MEDLINE=96177651; PubMed=8634689; RA Coy J.F., Sedlacek Z., Baechner D., Hameister H., Joos S., Lichter P., RA Delius H., Poustka A.; RT "Highly conserved 3' UTR and expression pattern of FXR1 points to a RT divergent gene regulation of FXR1 and FMR1."; RL Hum. Mol. Genet. 4:2209-2218(1995). RN [2] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX MEDLINE=99339984; PubMed=10409431; RA Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; RT "Alternative splicing in the murine and human FXR1 genes."; RL Genomics 59:193-202(1999). CC -!- FUNCTION: RNA-BINDING PROTEIN. INTERACTS WITH FMR1 AND FXR2 (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=E{EP1}; Synonyms=Alice, Barbara, Chloe, Deborah, Emily, CC Frida; CC IsoId=Q61584-1; Sequence=VSP_02391, VSP_02392, VSP_02393, CC VSP_02394, VSP_02395; CC Name=A; CC IsoId=Q61584-2; Sequence=VSP_02391, VSP_02393, VSP_02395; CC Name=B; CC IsoId=Q61584-3; Sequence=VSP_02393; CC Name=C; CC IsoId=Q61584-4; Sequence=VSP_02394; CC Name=D; CC IsoId=Q61584-5; Sequence=VSP_02391, VSP_02394; CC Name=F; CC IsoId=Q61584-6; Sequence=VSP_02391; CC Name=G; CC IsoId=Q61584-7; Sequence=VSP_02392; CC -!- TISSUE SPECIFICITY: IN EARLY EMBRYOGENESIS, HIGHEST EXPRESSION IN CC SOMITES AND CENTRAL NERVOUS SYSTEM. ALSO EXPRESSED IN SPINAL CORD, CC SURROUNDING MESENCHYMAL TISSUE AND UNDIFFERENTIATED GONAD. IN MID- CC EMBRYOGENESIS, MOST PROMINENT IN GONAD AND MUSCLE TISSUE. ALSO CC EXPRESSED IN LIVER, RETINA, TELENCEPHALON AND MESENCEPHALON. IN CC LATE EMBRYOGENESIS, RESTRICTED TO SKELETAL MUSCLE AND CC PROLIFERATIVE ACTIVE LAYERS OF BRAIN. AFTER BIRTH, HIGHLY CC EXPRESSED IN POSTMEIOTIC SPERMATIDS. INTERMEDIATE LEVELS ARE FOUND CC IN HEART, LIVER AND KIDNEY WITH LOWER LEVELS IN BRAIN AND SKELETAL CC MUSCLE. CC -!- SIMILARITY: BELONGS TO THE FMR1 FAMILY. DR EMBL; X90875; CAA62383.1; -. DR EMBL; AF124385; AAD30211.1; -. DR EMBL; AF124394; AAD30212.1; -. DR EMBL; AF124386; AAD30212.1; JOINED. DR EMBL; AF124387; AAD30212.1; JOINED. DR EMBL; AF124388; AAD30212.1; JOINED. DR EMBL; AF124389; AAD30212.1; JOINED. DR EMBL; AF124390; AAD30212.1; JOINED. DR EMBL; AF124391; AAD30212.1; JOINED. DR EMBL; AF124392; AAD30212.1; JOINED. DR EMBL; AF124393; AAD30212.1; JOINED. DR EMBL; AF124394; AAD30213.1; -. DR EMBL; AF124386; AAD30213.1; JOINED. DR EMBL; AF124387; AAD30213.1; JOINED. DR EMBL; AF124388; AAD30213.1; JOINED. DR EMBL; AF124389; AAD30213.1; JOINED. DR EMBL; AF124390; AAD30213.1; JOINED. DR EMBL; AF124391; AAD30213.1; JOINED. DR EMBL; AF124392; AAD30213.1; JOINED. DR EMBL; AF124393; AAD30213.1; JOINED. DR EMBL; AF124394; AAD30214.1; -. DR EMBL; AF124386; AAD30214.1; JOINED. DR EMBL; AF124387; AAD30214.1; JOINED. DR EMBL; AF124388; AAD30214.1; JOINED. DR EMBL; AF124389; AAD30214.1; JOINED. DR EMBL; AF124390; AAD30214.1; JOINED. DR EMBL; AF124391; AAD30214.1; JOINED. DR EMBL; AF124392; AAD30214.1; JOINED. DR EMBL; AF124393; AAD30214.1; JOINED. DR EMBL; AF124394; AAD30215.1; -. DR EMBL; AF124386; AAD30215.1; JOINED. DR EMBL; AF124387; AAD30215.1; JOINED. DR EMBL; AF124388; AAD30215.1; JOINED. DR EMBL; AF124389; AAD30215.1; JOINED. DR EMBL; AF124390; AAD30215.1; JOINED. DR EMBL; AF124391; AAD30215.1; JOINED. DR EMBL; AF124392; AAD30215.1; JOINED. DR EMBL; AF124393; AAD30215.1; JOINED. DR EMBL; AF124394; AAD30216.1; -. DR EMBL; AF124386; AAD30216.1; JOINED. DR EMBL; AF124387; AAD30216.1; JOINED. DR EMBL; AF124388; AAD30216.1; JOINED. DR EMBL; AF124389; AAD30216.1; JOINED. DR EMBL; AF124390; AAD30216.1; JOINED. DR EMBL; AF124391; AAD30216.1; JOINED. DR EMBL; AF124392; AAD30216.1; JOINED. DR EMBL; AF124393; AAD30216.1; JOINED. DR EMBL; AF124394; AAD30217.1; -. DR EMBL; AF124386; AAD30217.1; JOINED. DR EMBL; AF124387; AAD30217.1; JOINED. DR EMBL; AF124388; AAD30217.1; JOINED. DR EMBL; AF124389; AAD30217.1; JOINED. DR EMBL; AF124390; AAD30217.1; JOINED. DR EMBL; AF124391; AAD30217.1; JOINED. DR EMBL; AF124392; AAD30217.1; JOINED. DR EMBL; AF124393; AAD30217.1; JOINED. DR EMBL; AF124394; AAD30218.1; -. DR EMBL; AF124386; AAD30218.1; JOINED. DR EMBL; AF124387; AAD30218.1; JOINED. DR EMBL; AF124388; AAD30218.1; JOINED. DR EMBL; AF124389; AAD30218.1; JOINED. DR EMBL; AF124390; AAD30218.1; JOINED. DR EMBL; AF124391; AAD30218.1; JOINED. DR EMBL; AF124392; AAD30218.1; JOINED. DR EMBL; AF124393; AAD30218.1; JOINED. DR MGI; MGI:104860; Fxr1h.{EI2} DR INTERPRO; IPR000958; -. DR PFAM; PF00013; KH-domain; 2. DR HSSP; Q06787; 2FMR.{EI1} KW Alternative splicing; Repeat; RNA-binding. FT DOMAIN 222 251 KH. FT DOMAIN 285 314 KH. FT DOMAIN 471 490 RNA-BINDING (RGG-BOX). FT COMPBIAS 50 53 POLY-PRO. FT COMPBIAS 531 539 POLY-ARG. FT VAR_SEQ 380 408 Missing (in isoform A, isoform D and FT isoform F). FT /FTId=VSP_02391. FT VAR_SEQ 430 455 Missing (in isoform G). FT /FTId=VSP_02392. FT VAR_SEQ 564 590 Missing (in isoform C and isoform D). FT /FTId=VSP_02394. FT VAR_SEQ 564 568 DDSEK -> GKRCD (in isoform A and isoform FT B). FT /FTId=VSP_02393. FT VAR_SEQ 569 677 Missing (in isoform A). FT /FTId=VSP_02395. FT VARIANT 23 23 R -> H (IN LILLE/TAIPEI/VARESE/KOMAGOME- FT 3). FT VARIANT 79 79 R -> C (IN TOURS/ALGER/AMIENS/TOYAMA/ FT PARIS-1/PARIS-2/PADUA-2/BARCELONA-2/ FT KUMAMOTO; LACKS HEPARIN-BINDING ABILITY). FT /FTId=VAR_007037. FT VARIANT 425 425 R -> C (IN NORTHWICK/MILANO/FRANKFURT/ FT COPENHAGEN/LONDON; TYPE-II). FT /FTId=VAR_007075. FT VARIANT 425 425 R -> C (IN NORTHWICK/MILANO/FRANKFURT123/ FT COPENHAGEN/LONDON; TYPE-II). FT VARIANT 425 425 R -> C (IN NORTHWICK/MILANO/ FT FRANKFURT1234/COPENHAGEN/LONDON; TYPE- FT II). FT VARIANT 425 425 R -> CDCDCDDCDDCDCDDCDDCDCDCDCDCDCDDCDDCC FT DCDCDCD (IN A STRAIN). FT VARIANT 608 608 Missing (in NPD type B; prevalent among FT NPD type B patients from the North- FT African Maghreb region). FT /FTId=VAR_005068. FT CONFLICT 425 425 R -> CDCDCDDCDDCDCDDCDDCDCDCDCDCDCDDCDDCC FT DCDCDCD (IN A STRAIN). FT CONFLICT 425 425 RRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRR FT -> C. FT CONFLICT 425 425 Missing. ** ** ################# SOURCE SECTION ################## ** M.musculus mRNA for FXR1 protein ** [1] ** Coy J.F., Sedlacek Z., Baechner D., Hameister H., Joos S., Lichter P., ** Delius H., Poustka A.; ** "Highly conserved 3' UTR and expression pattern of FXR1 points to a ** divergent gene regulation of FXR1 and FMR1"; ** Hum. Mol. Genet. 4:2209-2218(1995). ** [2] ** 1-2060 ** Coy J.F.; ** ; ** Submitted (14-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** J.F. Coy, DKFZ-Heidelberg, Molekulare Genomanalyse, Im Neuenheimer ** Feld ** 280, 69120 Heidelberg, FRG ** MGD; MGI:104860; Fxr1h. ** [1] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative Splicing in the Murine and Human FXR1 Genes"; ** Genomics 0:0-0(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** source 1..2060 ** /organism="Mus musculus" ** CDS 14..1633 ** /db_xref="PID:e196394" ** /db_xref="MGD:MGI:104860" ** /gene="FXR1" ** CDS_IN_EMBL_ENTRY 1 ** 08-DEC-1995 (Rel. 46, Last updated, Version 2) ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..347, ** AF124392.1:435..497,AF124393.1:391..594, ** AF124393.1:2679..2879,911..927) ** /codon_start=1 ** /db_xref="PID:g4835741" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform a" ** /protein_id="AAD30213.1" ** CDS_IN_EMBL_ENTRY 7 ** 17-MAY-1999 (Rel. 59, Last updated, Version 1) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** MEDLINE; 99339984. ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative splicing in the murine and human FXR1 genes"; ** Genomics 59(2):193-202(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, ** Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..347, ** AF124392.1:435..497,AF124393.1:391..594, ** AF124393.1:2679..2879,156..247,911..1081) ** /codon_start=1 ** /db_xref="PID:g4835744" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform d" ** /protein_id="AAD30216.1" ** CDS_IN_EMBL_ENTRY 7 ** 10-AUG-1999 (Rel. 60, Last updated, Version 2) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** MEDLINE; 99339984. ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative splicing in the murine and human FXR1 genes"; ** Genomics 59(2):193-202(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, ** Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..497, ** AF124393.1:391..594,AF124393.1:2679..2879,911..927) ** /codon_start=1 ** /db_xref="PID:g4835742" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform b" ** /protein_id="AAD30214.1" ** CDS_IN_EMBL_ENTRY 7 ** 10-AUG-1999 (Rel. 60, Last updated, Version 2) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** MEDLINE; 99339984. ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative splicing in the murine and human FXR1 genes"; ** Genomics 59(2):193-202(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, ** Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..347, ** AF124392.1:435..497,AF124393.1:391..594, ** AF124393.1:2679..2879,AF124393.1:3534..3614,156..247, ** 911..1081) ** /codon_start=1 ** /db_xref="PID:g4835745" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform f" ** /protein_id="AAD30217.1" ** CDS_IN_EMBL_ENTRY 7 ** 10-AUG-1999 (Rel. 60, Last updated, Version 2) ** Mus musculus fragile-X-related protein 1 (Fxr1h) mRNA, partial cds. ** [1] ** 1-1674 ** MEDLINE; 99339984. ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative splicing in the murine and human FXR1 genes"; ** Genomics 59(2):193-202(1999). ** [2] ** 1-1674 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (26-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, ** Houston, TX 77030, USA ** source 1..1674 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** /strain="C57BL/6 x DBA" ** /clone="IMAGE:559877" ** CDS <1..1401 ** /codon_start=1 ** /db_xref="PID:g4835729" ** /note="FXR1" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1" ** /protein_id="AAD30211.1" ** CDS_IN_EMBL_ENTRY 1 ** 10-AUG-1999 (Rel. 60, Last updated, Version 2) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative Splicing in the Murine and Human FXR1 Genes"; ** Genomics 0:0-0(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..497, ** AF124393.1:469..594,AF124393.1:2679..2879, ** AF124393.1:3534..3614,156..247,911..1081) ** /codon_start=1 ** /db_xref="PID:g4835746" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform g" ** /protein_id="AAD30218.1" ** CDS_IN_EMBL_ENTRY 7 ** 17-MAY-1999 (Rel. 59, Last updated, Version 1) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative Splicing in the Murine and Human FXR1 Genes"; ** Genomics 0:0-0(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..497, ** AF124393.1:391..594,AF124393.1:2679..2879,156..247, ** 911..1081) ** /codon_start=1 ** /db_xref="PID:g4835743" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform c" ** /protein_id="AAD30215.1" ** CDS_IN_EMBL_ENTRY 7 ** 17-MAY-1999 (Rel. 59, Last updated, Version 1) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative Splicing in the Murine and Human FXR1 Genes"; ** Genomics 0:0-0(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..497, ** AF124393.1:391..594,AF124393.1:2679..2879, ** AF124393.1:3534..3614,156..247,911..1081) ** /codon_start=1 ** /db_xref="PID:g4835740" ** /note="FXR1" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform e" ** /protein_id="AAD30212.1" ** CDS_IN_EMBL_ENTRY 7 ** 17-MAY-1999 (Rel. 59, Last updated, Version 1) ** ** ################# INTERNAL SECTION ################## **EV EI1; HSSP_ADD; Q06787; 29-SEP-2000. **EV EI2; MGD_ADD; MGI:104860; 29-SEP-2000. **ID XXXX_MOUSE **PM PFAM; PF00013; KH-domain; 222; 269; T; 02-FEB-2000; **PM PFAM; PF00013; KH-domain; 285; 334; T; 02-FEB-2000; **PM PROSITE; PS50084; KH_DOMAIN; 218; 277; T; 28-JAN-2000; **PM PROSITE; PS50084; KH_DOMAIN; 281; 331; T; 28-JAN-2000; **TT Test case. Wrongly positioned ** line. **ZZ CREATED AND FINISHED BY Serenella. **ZZ UPDATED BY Michele M. (10-NOV-2000). **ZZ Comment: MERGED 7 TREMBL ENTRIES TO THIS ONE. **ZZ CURATED. SQ SEQUENCE 677 AA; 76222 MW; 908104FC95431A11 CRC64; MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN IQQARKVPGV TAIELDEDTG TFRIYGESAE AVKKARGFLE FVEDFIQVPR NLVGKVIGKN GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE VEQLRMERLQ IDEQLRQIGM GFRPSSTRGP EREKGYATDE STVSSVQGSR SYSGRGRGRR GPNYTSGYGT NSELSNPSET ESERKDELSD WSLAGEDDRE TRHQRDSRRR PGGRGRSVSG GRGRGGPRGG KSSISSVLKD PDSNPYSLLD NTESDQTADT DASESHHSTN RRRRSRRRRT DEDAVLMDGL TESDTASVNE NGLDDSEKKP QRRNRSRRRR FRGQAEDRQP VTVADYISRA ESQSRQRNLP RETLAKNKKE MAKDVIEEHG PSEKAINGPT SASGDEIPKL PRTLGEEKTK TLKEDSTQEA AVLNGVS // 1 ID AATM_RABIT STANDARD; PRT; 30 AA. AC P12345; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Aspartate aminotransferase, mitochondrial (EC 2.6.1.1) (Transaminase DE A) (Glutamate oxaloacetate transaminase-2) (Fragment). GN GOT2. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE. RC TISSUE=Liver; RX MEDLINE=85289123; PubMed=4030726; RA Kuramitsu S., Inoue K., Kondo K., Aki K., Kagamiyama H.; RT "Aspartate aminotransferase isozymes from rabbit liver. Purification RT and properties."; RL J. Biochem. 97:1337-1345(1985). CC -!- CATALYTIC ACTIVITY: L-ASPARTATE + 2-OXOGLUTARATE = OXALOACETATE + CC L-GLUTAMATE. CC -!- CATALYTIC ACTIVITY: Catalyzes the reduction and hydrolysis of CC (1->6)-alpha-D-glucosidic linkages in pullulan and in amylopectin CC and glycogen, and the alpha- and beta-limit dextrins of CC amylopectin and glycogen. CC -!- COFACTOR: CC Note=PYRIDOXAL PHOSPHATE.; CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- MISCELLANEOUS: IN EUKARYOTES THERE ARE TWO ISOZYMES: A CYTOPLASMIC CC ONE AND A MITOCHONDRIAL ONE. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR PIR; B27103; B27103. DR InterPro; IPR001511; Aminotran_1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; PARTIAL. DR HSSP; P00508; 1TAT. KW Aminotransferase; Mitochondrion; Pyridoxal phosphate; Transferase. FT NON_TER 30 30 ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 30 AA; 3401 MW; 410321530B95B673 CRC64; SSWWAHVEMG PPDPILGVTE AYKRDTNSKK // 1 ID AATM_RABIT STANDARD; PRT; 30 AA. AC P12345; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Aspartate aminotransferase, mitochondrial (EC 2.6.1.1) (Transaminase DE A) (Glutamate oxaloacetate transaminase-2) (Fragment). GN abcdefghijklmnopqrstuvwx abcdefghijklmnopqrstuvwx OR GN abcdefghijkl mnOR A. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE. RC TISSUE=Liver; RX MEDLINE=85289123; PubMed=4030726; RA Kuramitsu S., Inoue K., Kondo K., Aki K., Kagamiyama H.; RT "Aspartate aminotransferase isozymes from rabbit liver. Purification RT and properties."; RL J. Biochem. 97:1337-1345(1985). FT NON_TER 30 30 ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 30 AA; 3401 MW; 410321530B95B673 CRC64; SSWWAHVEMG PPDPILGVTE AYKRDTNSKK // 1 ID AATM_RABIT STANDARD; PRT; 30 AA. AC P12345; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Aspartate aminotransferase, mitochondrial (EC 2.6.1.1) (Transaminase DE A) (Glutamate oxaloacetate transaminase-2) (Fragment). GN abcdefghijklmnopqrstuvwx OR abcdefghijkl mnOR A OR GN abcdefghijklmnopqrstuvwxyzabcdefghikjlmn. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE. RC TISSUE=Liver; RX MEDLINE=85289123; PubMed=4030726; RA Kuramitsu S., Inoue K., Kondo K., Aki K., Kagamiyama H.; RT "Aspartate aminotransferase isozymes from rabbit liver. Purification RT and properties."; RL J. Biochem. 97:1337-1345(1985). CC -!- SIMILARITY: Contains 4 C3H1-type zinc fingers. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. FT NON_TER 30 30 ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 30 AA; 3401 MW; 410321530B95B673 CRC64; SSWWAHVEMG PPDPILGVTE AYKRDTNSKK // 1 ID COAT_BPSP STANDARD; PRT; 132 AA. AC P09673; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 01-FEB-1994 (Rel. 28, Last annotation update) DE Coat protein. OS Bacteriophage SP. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Leviviridae; OC Allolevivirus. OX NCBI_TaxID=12027, 10685; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88289362; PubMed=3399390; RA Hirashima A., Hirose T., Inayama S., Inokuchi Y., Jacobson A.B.; RT "Analysis of the complete nucleotide sequence of the group IV RNA RT coliphage SP."; RL Nucleic Acids Res. 16:6205-6221(1988). CC -!- FUNCTION: FORMS THE PHAGE SHELL; BINDS TO THE PHAGE RNA. DR EMBL; X07489; CAA30374.1; -. DR InterPro; IPR002703; Levi_coat. DR Pfam; PF01819; Levi_coat; 1. DR HSSP; P03615; 1QBE. KW Coat protein; RNA-binding. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 132 AA; 14129 MW; 50B1E6CC6AF0A254 CRC64; MAKLNQVTLS KIGKNGDQTL TLTPRGVNPT NGVASLSEAG AVPALEKRVT VSVAQPSRNR KNFKVQIKLQ NPTACTRDAC DPSVTRSAFA DVTLSFTSYS TDEERALIRT ELAALLADPL IVDAIDNLNP AY // 1 ID X_WHV1 STANDARD; PRT; 141 AA. AC P03167; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Trans-activating protein X. GN X. OS Woodchuck hepatitis virus 1 (WHV 1). OC Viruses; Retroid viruses; Hepadnaviridae; Orthohepadnavirus. OX NCBI_TaxID=10430; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82216969; PubMed=7086958; RA Galibert F., Chen T.N., Mandart E.; RT "Nucleotide sequence of a cloned woodchuck hepatitis virus genome: RT comparison with the hepatitis B virus sequence."; RL J. Virol. 41:51-65(1982). DR EMBL; J02442; -; NOT_ANNOTATED_CDS. DR PIR; A03720; QQVLC1. DR InterPro; IPR000236; TransactX. DR Pfam; PF00739; X; 1. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 141 AA; 15222 MW; 4728019844561D85 CRC64; MAARLCCQLD PARDVLLLRP FGSQSSGPPF PRPSAGSAAS PASSLSASDE SDLPLGRLPA CFASASGPCC LVVTCAELRT MDSTVNFVSW HANRQLGMPS KDLWTPYIRD QLLTKWEEGS IDPRLSIFVL GGCRHKCMRL P // 1 ID ROCKY_NICSY PRELIMINARY; PRT; 276 AA. AC P19682; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 28 kDa ribonucleoprotein, chloroplast precursor (28RNP). OS Nicotiana sylvestris (Wood tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4096; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 58-78. RC STRAIN=CV. BRIGHT YELLOW 4; RX MEDLINE=91005997; PubMed=1698606; RA Li Y., Sugiura M.; RT "Three distinct ribonucleoproteins from tobacco chloroplasts: each RT contains a unique amino terminal acidic domain and two RT ribonucleoprotein consensus motifs."; RL EMBO J. 9:3059-3066(1990). CC -!- FUNCTION: PROBABLY INVOLVED IN THE 3'END PROCESSING OF CHLOROPLAST CC MRNA'S. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: IN THE CENTRAL SECTION; BELONGS TO THE RRM FAMILY. CC -!- SIMILARITY: CONTAINS 3 ABL DOMAINS. CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIFS (RRM). CC -!- SIMILARITY: STRONG, TO PROTEIN X. DR EMBL; X53933; CAA37880.1; -. DR PIR; S12109; S12109. DR InterPro; IPR000504; RRM. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; 2. DR HSSP; P09651; 1UP1. KW Chloroplast; mRNA processing; Repeat; Ribonucleoprotein; RNA-binding; KW Transit peptide. FT TRANSIT 1 57 CHLOROPLAST. FT CHAIN 58 276 28 kDa RIBONUCLEOPROTEIN. FT DOMAIN 97 175 RNA-BINDING (RRM) 1. FT DOMAIN 191 269 RNA-BINDING (RRM) 2. FT COMPBIAS 58 96 ASP/GLU-RICH (ACIDIC). FT COMPBIAS 80 85 COILED COIL. FT COMPBIAS 92 >100 ALA-RICH. FT COMPBIAS 92 100 ASP/GLU-RICH (ACIDIC). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 276 AA; 30699 MW; 48FF3DED534133BA CRC64; MATNGCLISL PPFFTTTKSI SSYPFLSTQL KPISLSSSLP TLLSLNKRTT QFPTFVSVLS EDDNTLVLDD QEQGGDFPSF VGEAGETEEY QEPSEDAKLF VGNLPYDIDS EGLAQLFQQA GVVEIAEVIY NRETDRSRGF GFVTMSTVEE ADKAVELYSQ YDLNGRLLTV NKAAPRGSRP ERAPRTFQPT YRIYVGNIPW DIDDARLEQV FSEHGKVVSA RVVFDRESGR SRGFGFVTMS SEAEMSEAIA NLDGQTLDGR TIRVNAAEER PRRNTY // 0 ID CA54_HUMAN STANDARD; PRT; 1685 AA. AC P29400; Q16006; Q16126; DT 01-DEC-1992 (Rel. 24, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Collagen alpha 5(IV) chain precursor. GN COL4A5. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94165049; PubMed=8120014; RA Zhou J., Leinonen A., Tryggvason K.; RT "Structure of the human type IV collagen COL4A5 gene."; RL J. Biol. Chem. 269:6608-6614(1994). RN [2] RP SEQUENCE OF 1-910 FROM N.A., AND VARIANT AS CYS-521. RC TISSUE=Kidney, and Liver; RX MEDLINE=92316923; PubMed=1352287; RA Zhou J., Hertz J.M., Leinonen A., Tryggvason K.; RT "Complete amino acid sequence of the human alpha 5 (IV) collagen chain RT and identification of a single-base mutation in exon 23 converting RT glycine 521 in the collagenous domain to cysteine in an Alport RT syndrome patient."; RL J. Biol. Chem. 267:12475-12481(1992). RN [3] RP SEQUENCE OF 85-1685 FROM N.A. RC TISSUE=Placenta; RX MEDLINE=90337990; PubMed=2380186; RA Pihlajaniemi T., Pohjolainen E.R., Myers J.C.; RT "Complete primary structure of the triple-helical region and the RT carboxyl-terminal domain of a new type IV collagen chain, alpha RT 5(IV)."; RL J. Biol. Chem. 265:13758-13766(1990). RN [4] RP SEQUENCE OF 924-1685 FROM N.A. RX MEDLINE=91169491; PubMed=2004755; RA Zhou J., Hostikka S.L., Chow L.T., Tryggvason K.; RT "Characterization of the 3' half of the human type IV collagen alpha 5 RT gene that is affected in the Alport syndrome."; RL Genomics 9:1-9(1991). RN [5] RP SEQUENCE OF 914-1685 FROM N.A. RX MEDLINE=90160375; PubMed=1689491; RA Hostikka S.L., Eddy R.L., Byers M.G., Hoeyhtyae M., Shows T.B., RA Tryggvason K.; RT "Identification of a distinct type IV collagen alpha chain with RT restricted kidney distribution and assignment of its gene to the locus RT of X chromosome-linked Alport syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1606-1610(1990). RN [6] RP SEQUENCE OF 1442-1471 FROM N.A. RX MEDLINE=90252791; PubMed=2339699; RA Myers J.C., Jones T.A., Pohjolainen E.R., Kadri A.S., Goddard A.D., RA Sheer D., Solomon E., Pihlajaniemi T.; RT "Molecular cloning of alpha 5(IV) collagen and assignment of the gene RT to the region of the X chromosome containing the Alport syndrome RT locus."; RL Am. J. Hum. Genet. 46:1024-1033(1990). RN [7] RP SEQUENCE OF 1-20 FROM N.A. RA Guo C., van Damme B., Vanrenterghem Y., Devriendt K., Cassiman J.-J., RA Marynen P.; RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases. RN [8] RP SEQUENCE OF 1258-1270 FROM N.A. (SPLICED FORM). RX MEDLINE=94133540; PubMed=8301933; RA Guo C., van Damme B., van Damme-Lombaerts R., van den Berghe H., RA Cassiman J.-J., Marynen P.; RT "Differential splicing of COL4A5 mRNA in kidney and white blood cells: RT a complex mutation in the COL4A5 gene of an Alport patient deletes the RT NC1 domain."; RL Kidney Int. 44:1316-1321(1993). RN [9] RP REVIEW ON VARIANTS. RX MEDLINE=97338662; PubMed=9195222; RA Lemmink H.H., Schroeder C.H., Monnens L.A.H., Smeets H.J.M.; RT "The clinical spectrum of type IV collagen mutations."; RL Hum. Mutat. 9:477-499(1997). RN [10] RP VARIANT AS SER-1564. RX MEDLINE=91169492; PubMed=1672282; RA Zhou J., Barker D.F., Hostikka S.L., Gregory M.C., Atkin C.L., RA Tryggvason K.; RT "Single base mutation in alpha 5(IV) collagen chain gene converting a RT conserved cysteine to serine in Alport syndrome."; RL Genomics 9:10-18(1991). RN [11] RP VARIANT AS ARG-325. RX MEDLINE=92303559; PubMed=1376965; RA Knebelmann B., Deschenes G., Gros F., Hors M.-C., Gruenfeld J.-P., RA Tryggvason K., Gubler M.-C., Antignac C.; RT "Substitution of arginine for glycine 325 in the collagen alpha 5 (IV) RT chain associated with X-linked Alport syndrome: characterization of RT the mutation by direct sequencing of PCR-amplified lymphoblast cDNA RT fragments."; RL Am. J. Hum. Genet. 51:135-142(1992). RN [12] RP VARIANT AS GLU-325. RX MEDLINE=93244772; PubMed=1363780; RA Renieri A., Seri M., Myers J.C., Pihlajaniemi T., Massella L., RA Rizzoni G.F., de Marchi M.; RT "De novo mutation in the COL4A5 gene converting glycine 325 to RT glutamic acid in Alport syndrome."; RL Hum. Mol. Genet. 1:127-129(1992). RN [13] RP VARIANTS AS THR-1517; SER-1538 AND GLN-1563. RX MEDLINE=94010948; PubMed=8406498; RA Lemmink H.L., Schroeder C.H., Brunner H.G., Nelen M.R., Zhou J., RA Tryggvason K., Haggsma-Schouten W.A.G., Roodvoets A.P., Rascher W., RA van Oost B.A., Smeets H.J.M.; RT "Identification of four novel mutations in the COL4A5 gene of patients RT with Alport syndrome."; RL Genomics 17:485-489(1993). RN [14] RP VARIANTS AS E-400;V-406;V-638;A-638;R-653;R-796;R-869;R-872 & C-1241. RX MEDLINE=95322976; PubMed=7599631; RA Boye E., Flinter F., Zhou J., Tryggvason K., Bobrow M., Harris A.; RT "Detection of 12 novel mutations in the collagenous domain of the RT COL4A5 gene in Alport syndrome patients."; RL Hum. Mutat. 5:197-204(1995). RN [15] RP VARIANT AS ARG-1649. RX MEDLINE=96213750; PubMed=8651292; RA Barker D.F., Pruchno C.J., Jiang X., Atkin C.L., Stone E.M., RA Denison J.C., Fain P.R., Gregory M.C.; RT "A mutation causing Alport syndrome with tardive hearing loss is RT common in the western United States."; RL Am. J. Hum. Genet. 58:1157-1165(1996). RN [16] RP VARIANTS AS. RX MEDLINE=96213754; PubMed=8651296; RA Renieri A., Bruttini M., Galli L., Zanelli P., Neri T.M., Rossetti S., RA Turco A.E., Heiskari N., Zhou J., Gusmano R., Massella L., Banfi G., RA Scolari F., Sessa A., Rizzoni G.F., Tryggvason K., Pignatti P.F., RA Savi M., Ballabio A., de Marchi M.; RT "X-linked Alport syndrome: an SSCP-based mutation survey over all 51 RT exons of the COL4A5 gene."; RL Am. J. Hum. Genet. 58:1192-1204(1996). RN [17] RP VARIANTS AS, AND VARIANTS ASP-430;SER-444;SER-619;ASN-664 & MET-1428. RX MEDLINE=97094179; PubMed=8940267; RA Knebelmann B., Breillat C., Forestier L., Arrondel C., Jacassier D., RA Giatras I., Drouot L., Deschenes G., Gruenfeld J.-P., Broyer M., RA Gubler M.-C., Antignac C.; RT "Spectrum of mutations in the COL4A5 collagen gene in X-linked Alport RT syndrome."; RL Am. J. Hum. Genet. 59:1221-1232(1996). RN [18] RP VARIANT AS ASP-1498. RX MEDLINE=96233932; PubMed=8829632; RA Tverskaya S., Bobrynina V., Tsalykova F., Ignatova M., RA Krasnopolskaya X., Evgrafov O.; RT "Substitution of A1498D in noncollagen domain of a5(IV) collagen chain RT associated with adult-onset X-linked Alport syndrome."; RL Hum. Mutat. 7:149-150(1996). RN [19] RP VARIANT AS GLN-1677. RX MEDLINE=97295089; PubMed=9150741; RA Barker D.F., Denison J.C., Atkin C.L., Gregory M.C.; RT "Common ancestry of three Ashkenazi-American families with Alport RT syndrome and COL4A5 R1677Q."; RL Hum. Genet. 99:681-684(1997). RN [20] RP VARIANTS AS R-174; R-177; R-325; C-1410; W-1421; T-1517 AND D-1596. RX MEDLINE=98112435; PubMed=9452056; RA Neri T.M., Zanelli P., de Palma G., Savi M., Rossetti S., Turco A.E., RA Pignatti G.F., Galli L., Bruttini M., Renieri A., Mingarelli R., RA Trivelli A., Pinciaroli A.R., Ragaiolo M., Rizzoni G.F., de Marchi M.; RT "Missense mutations in the COL4A5 gene in patients with X-linked RT Alport syndrome."; RL Hum. Mutat. Suppl. 1:S106-S109(1998). RN [21] RP VARIANTS AS. RX MEDLINE=99063529; PubMed=9848783; RA Martin P., Heiskari N., Zhou J., Leinonen A., Tumelius T., Hertz J.M., RA Barker D.F., Gregory M.C., Atkin C.L., Styrkarsdottir U., Neumann H., RA Springate J., Shows T.B., Pettersson E., Tryggvason K.; RT "High mutation detection rate in the COL4A5 collagen gene in suspected RT Alport syndrome using PCR and direct DNA sequencing."; RL J. Am. Soc. Nephrol. 9:2291-2301(1998). RN [22] RP VARIANTS AS GLU-579; LYS-633; ASP-947; VAL-953; ARG-1107; ARG-1158; RP SER-1170 AND TRP-1678, AND VARIANTS SER-444 AND ALA-739. RX MEDLINE=20030197; PubMed=10561141; RA Inoue Y., Nishio H., Shirakawa T., Nakanishi K., Nakamura H., RA Sumino K., Nishiyama K., Iijima K., Yoshikawa N.; RT "Detection of mutations in the COL4A5 gene in over 90% of male RT patients with X-linked Alport's syndrome by RT-PCR and direct RT sequencing."; RL Am. J. Kidney Dis. 34:854-862(1999). RN [23] RP VARIANT AS ARG-822. RX MEDLINE=20025011; PubMed=10563487; RA Cruz-Robles D., Garcia-Torres R., Antignac C., Forestier L., RA Garcia de la Puente S., Correa-Rotter R., Garcia-Lopez E., Orozco L.; RT "Three novel mutations in the COL4A5 gene in Mexican Alport syndrome RT patients."; RL Clin. Genet. 56:242-243(1999). RN [24] RP VARIANTS AS, AND VARIANTS. RX MEDLINE=99140256; PubMed=10094548; RA Plant K.E., Green P.M., Vetrie D., Flinter F.A.; RT "Detection of mutations in COL4A5 in patients with Alport syndrome."; RL Hum. Mutat. 13:124-132(1999). RN [25] RP VARIANT AS CYS-177. RX MEDLINE=20460632; PubMed=11004279; RA Blasi M.A., Rinaldi R., Renieri A., Petrucci R., De Bernardo C., RA Bruttini M., Grammatico P.; RT "Dot-and-fleck retinopathy in Alport syndrome caused by a novel RT mutation in the COL4A5 gene."; RL Am. J. Ophthalmol. 130:130-131(2000). RN [26] RP VARIANTS AS R-216; R-415; E-1045; D-1086; S-1167 AND 864-S--G-875 DEL. RX MEDLINE=20321306; PubMed=10862091; RA Martin P., Heiskari N., Pajari H., Groenhagen-Riska C., RA Kaeaeriaeinen H., Koskimies O., Tryggvason K.; RT "Spectrum of COL4A5 mutations in Finnish Alport syndrome patients."; RL Hum. Mutat. 15:579-579(2000). RN [27] RP VARIANTS AS ARG-319;SER-739;VAL-902;GLU-911;ASP-1229 AND HIS-1511. RX MEDLINE=20148403; PubMed=10684360; RA Cheong H.I., Park H.W., Ha I.S., Choi Y.; RT "Mutational analysis of COL4A5 gene in Korean Alport syndrome."; RL Pediatr. Nephrol. 14:117-121(2000). RN [28] RP VARIANTS AS R-192; R-292; D-295; R-325; R-558; V-603; D-624; D-629; RP E-722; V-898; A-1006; V-1006; D-1244; R-1649 AND P-1677, AND VARIANT RP S-444. RX MEDLINE=21123908; PubMed=11223851; RA Barker D.F., Denison J.C., Atkin C.L., Gregory M.C.; RT "Efficient detection of Alport syndrome COL4A5 mutations with RT multiplex genomic PCR-SSCP."; RL Am. J. Med. Genet. 98:148-160(2001). CC -!- FUNCTION: TYPE IV COLLAGEN IS THE MAJOR STRUCTURAL COMPONENT OF CC GLOMERULAR BASEMENT MEMBRANES (GBM), FORMING A 'CHICKEN-WIRE' CC MESHWORK TOGETHER WITH LAMININS, PROTEOGLYCANS AND ENTACTIN/ CC NIDOGEN. CC -!- SUBUNIT: THERE ARE SIX TYPE IV COLLAGEN ISOFORMS, ALPHA 1(IV)- CC ALPHA 6(IV), EACH OF WHICH CAN FORM A TRIPLE HELIX STRUCTURE WITH CC 2 OTHER CHAINS TO GENERATE TYPE IV COLLAGEN NETWORK. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P29400-1; Sequence=Displayed; CC Name=2; CC IsoId=P29400-2; Sequence=VSP_00759; CC Note=Longer found in kidney, in which 2 extra G-X-X repeats into CC the triple-helix domain are introduced; CC -!- DOMAIN: ALPHA CHAINS OF TYPE IV COLLAGEN HAVE A NONCOLLAGENOUS CC DOMAIN (NC1) AT THEIR C-TERMINUS, FREQUENT INTERRUPTIONS OF THE G- CC X-Y REPEATS IN THE LONG CENTRAL TRIPLE-HELICAL DOMAIN (WHICH MAY CC CAUSE FLEXIBILITY IN THE TRIPLE HELIX), AND A SHORT N-TERMINAL CC TRIPLE-HELICAL 7S DOMAIN. CC -!- PTM: PROLINES AT THE THIRD POSITION OF THE TRIPEPTIDE REPEATING CC UNIT (G-X-Y) ARE HYDROXYLATED IN SOME OR ALL OF THE CHAINS. CC -!- PTM: TYPE IV COLLAGENS CONTAIN NUMEROUS CYSTEINE RESIDUES WHICH CC ARE INVOLVED IN INTER- AND INTRAMOLECULAR DISULFIDE BONDING. 12 OF CC THESE, LOCATED IN THE NC1 DOMAIN, ARE CONSERVED IN ALL KNOWN TYPE CC IV COLLAGENS. CC -!- DISEASE: DEFECTS IN COL4A5 ARE A CAUSE OF X-LINKED ALPORT SYNDROME CC (AS). ALPORT SYNDROME IS CHARACTERIZED BY PROGRESSIVE CC GLOMERULONEPHRITIS, OFTEN ASSOCIATED WITH HIGH-TONE SENSORINEURAL CC DEAFNESS, SPECIFIC EYE ABNORMALITIES (LENTICONOUS AND MACULAR CC FLECKS), AND GLOMERULAR BASEMENT MEMBRANE DEFECTS. IN MALES, THE CC TYPICAL TIME COURSE FOR THE PROGRESS OF ALPORT SYNDROME IS: CC HEMATURIA BY THE AGE OF 5 YEARS, DEAFNESS AND HYPERTENSION IN CC EARLY TEENAGE LIFE, DETERIORATION OF RENAL FUNCTION BY AGE 20, AND CC END-STAGE RENAL FAILURE SOON THEREAFTER. FEMALES TEND TO FOLLOW A CC MUCH MILDER COURSE AND RARELY GO INTO RENAL FAILURE. DR EMBL; M58526; AAA99480.1; -. DR EMBL; M90464; AAA52046.1; -. DR EMBL; U04520; AAC27816.1; -. DR EMBL; U04470; AAC27816.1; JOINED. DR EMBL; U04471; AAC27816.1; JOINED. DR EMBL; U04472; AAC27816.1; JOINED. DR EMBL; U04473; AAC27816.1; JOINED. DR EMBL; U04474; AAC27816.1; JOINED. DR EMBL; U04476; AAC27816.1; JOINED. DR EMBL; U04477; AAC27816.1; JOINED. DR EMBL; U04478; AAC27816.1; JOINED. DR EMBL; U04479; AAC27816.1; JOINED. DR EMBL; U04480; AAC27816.1; JOINED. DR EMBL; U04483; AAC27816.1; JOINED. DR EMBL; U04485; AAC27816.1; JOINED. DR EMBL; U04486; AAC27816.1; JOINED. DR EMBL; U04487; AAC27816.1; JOINED. DR EMBL; U04488; AAC27816.1; JOINED. DR EMBL; U04489; AAC27816.1; JOINED. DR EMBL; U04490; AAC27816.1; JOINED. DR EMBL; U04491; AAC27816.1; JOINED. DR EMBL; U04492; AAC27816.1; JOINED. DR EMBL; U04493; AAC27816.1; JOINED. DR EMBL; U04494; AAC27816.1; JOINED. DR EMBL; U04495; AAC27816.1; JOINED. DR EMBL; U04496; AAC27816.1; JOINED. DR EMBL; U04497; AAC27816.1; JOINED. DR EMBL; U04498; AAC27816.1; JOINED. DR EMBL; U04499; AAC27816.1; JOINED. DR EMBL; U04500; AAC27816.1; JOINED. DR EMBL; U04501; AAC27816.1; JOINED. DR EMBL; U04502; AAC27816.1; JOINED. DR EMBL; U04503; AAC27816.1; JOINED. DR EMBL; U04504; AAC27816.1; JOINED. DR EMBL; U04505; AAC27816.1; JOINED. DR EMBL; U04506; AAC27816.1; JOINED. DR EMBL; U04507; AAC27816.1; JOINED. DR EMBL; U04508; AAC27816.1; JOINED. DR EMBL; U04509; AAC27816.1; JOINED. DR EMBL; U04510; AAC27816.1; JOINED. DR EMBL; U04511; AAC27816.1; JOINED. DR EMBL; U04512; AAC27816.1; JOINED. DR EMBL; U04514; AAC27816.1; JOINED. DR EMBL; U04515; AAC27816.1; JOINED. DR EMBL; U04516; AAC27816.1; JOINED. DR EMBL; U04517; AAC27816.1; JOINED. DR EMBL; U04518; AAC27816.1; JOINED. DR EMBL; U04519; AAC27816.1; JOINED. DR EMBL; U04520; AAF66217.2; -. DR EMBL; U04470; AAF66217.2; JOINED. DR EMBL; U04471; AAF66217.2; JOINED. DR EMBL; U04472; AAF66217.2; JOINED. DR EMBL; U04473; AAF66217.2; JOINED. DR EMBL; U04474; AAF66217.2; JOINED. DR EMBL; U04476; AAF66217.2; JOINED. DR EMBL; U04477; AAF66217.2; JOINED. DR EMBL; U04478; AAF66217.2; JOINED. DR EMBL; U04479; AAF66217.2; JOINED. DR EMBL; U04480; AAF66217.2; JOINED. DR EMBL; U04483; AAF66217.2; JOINED. DR EMBL; U04485; AAF66217.2; JOINED. DR EMBL; U04486; AAF66217.2; JOINED. DR EMBL; U04487; AAF66217.2; JOINED. DR EMBL; U04488; AAF66217.2; JOINED. DR EMBL; U04489; AAF66217.2; JOINED. DR EMBL; U04490; AAF66217.2; JOINED. DR EMBL; U04491; AAF66217.2; JOINED. DR EMBL; U04492; AAF66217.2; JOINED. DR EMBL; U04493; AAF66217.2; JOINED. DR EMBL; U04494; AAF66217.2; JOINED. DR EMBL; U04495; AAF66217.2; JOINED. DR EMBL; U04496; AAF66217.2; JOINED. DR EMBL; U04497; AAF66217.2; JOINED. DR EMBL; U04498; AAF66217.2; JOINED. DR EMBL; U04499; AAF66217.2; JOINED. DR EMBL; U04500; AAF66217.2; JOINED. DR EMBL; U04501; AAF66217.2; JOINED. DR EMBL; U04502; AAF66217.2; JOINED. DR EMBL; U04503; AAF66217.2; JOINED. DR EMBL; U04504; AAF66217.2; JOINED. DR EMBL; U04505; AAF66217.2; JOINED. DR EMBL; U04506; AAF66217.2; JOINED. DR EMBL; U04507; AAF66217.2; JOINED. DR EMBL; U04508; AAF66217.2; JOINED. DR EMBL; U04509; AAF66217.2; JOINED. DR EMBL; U04510; AAF66217.2; JOINED. DR EMBL; AF199451; AAF66217.2; JOINED. DR EMBL; AF199452; AAF66217.2; JOINED. DR EMBL; U04511; AAF66217.2; JOINED. DR EMBL; U04512; AAF66217.2; JOINED. DR EMBL; U04514; AAF66217.2; JOINED. DR EMBL; U04515; AAF66217.2; JOINED. DR EMBL; U04516; AAF66217.2; JOINED. DR EMBL; U04517; AAF66217.2; JOINED. DR EMBL; U04518; AAF66217.2; JOINED. DR EMBL; U04519; AAF66217.2; JOINED. DR EMBL; M63473; AAA51558.1; -. DR EMBL; M63455; AAA51558.1; JOINED. DR EMBL; M63456; AAA51558.1; JOINED. DR EMBL; M63457; AAA51558.1; JOINED. DR EMBL; M63458; AAA51558.1; JOINED. DR EMBL; M63459; AAA51558.1; JOINED. DR EMBL; M63460; AAA51558.1; JOINED. DR EMBL; M63461; AAA51558.1; JOINED. DR EMBL; M63462; AAA51558.1; JOINED. DR EMBL; M63463; AAA51558.1; JOINED. DR EMBL; M63464; AAA51558.1; JOINED. DR EMBL; M63465; AAA51558.1; JOINED. DR EMBL; M63466; AAA51558.1; JOINED. DR EMBL; M63467; AAA51558.1; JOINED. DR EMBL; M63468; AAA51558.1; JOINED. DR EMBL; M63470; AAA51558.1; JOINED. DR EMBL; M63471; AAA51558.1; JOINED. DR EMBL; M63472; AAA51558.1; JOINED. DR EMBL; M31115; AAA52045.1; -. DR EMBL; Z37153; CAA85512.1; -. DR EMBL; S69168; AAC60612.1; -. DR EMBL; S59334; AAD13909.1; -. DR PIR; S22917; S22917. DR MIM; 301050; -. DR MIM; 303630; -. DR InterPro; IPR001442; C4. DR InterPro; IPR000087; Collagen. DR Pfam; PF01413; C4; 2. DR Pfam; PF01391; Collagen; 21. DR ProDom; PD003923; C4; 2. DR SMART; SM00111; C4; 2. KW Alport syndrome; Alternative splicing; Basement membrane; Collagen; KW Connective tissue; Disease mutation; Extracellular matrix; KW Hydroxylation; Polymorphism; Repeat; Signal. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 1685 COLLAGEN ALPHA 5(IV) CHAIN. FT DOMAIN 27 41 NONHELICAL REGION (NC2). FT DOMAIN 42 1456 TRIPLE-HELICAL REGION. FT DOMAIN 1457 1685 NONHELICAL REGION (NC1). FT DOMAIN 1457 1568 REPEAT NC1-1. FT DOMAIN 1569 1685 REPEAT NC1-2. FT CARBOHYD 125 125 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 451 451 INTERCHAIN (POTENTIAL). FT DISULFID 481 481 INTERCHAIN (POTENTIAL). FT DISULFID 484 484 INTERCHAIN (POTENTIAL). FT DISULFID 1476 1567 OR 1564 (BY SIMILARITY). FT DISULFID 1509 1564 OR 1567 (BY SIMILARITY). FT DISULFID 1521 1527 BY SIMILARITY. FT DISULFID 1586 1681 OR 1678 (BY SIMILARITY). FT DISULFID 1620 1678 OR 1681 (BY SIMILARITY). FT DISULFID 1632 1638 BY SIMILARITY. FT VAR_SEQ 1264 1264 G -> GPTGFQG (in isoform 2). FT /FTId=VSP_00759. FT VARIANT 54 54 G -> D (IN AS; ADULT TYPE). FT /FTId=VAR_001914. FT VARIANT 114 114 G -> S (IN AS). FT /FTId=VAR_007991. FT VARIANT 129 129 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_001915. FT VARIANT 129 129 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_001916. FT VARIANT 174 174 G -> R (IN AS). FT /FTId=VAR_001917. FT VARIANT 177 177 G -> C (IN AS WITH DOT-AND-FLECK FT RETINOPATHY). FT /FTId=VAR_011220. FT VARIANT 177 177 G -> R (IN AS; ADULT TYPE). FT /FTId=VAR_001918. FT VARIANT 192 192 G -> R (IN AS). FT /FTId=VAR_011221. FT VARIANT 204 204 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_011222. FT VARIANT 216 216 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_001919. FT VARIANT 219 219 G -> S (IN AS). FT /FTId=VAR_001920. FT VARIANT 230 230 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_011223. FT VARIANT 239 239 G -> E (IN AS). FT /FTId=VAR_011224. FT VARIANT 264 264 G -> R (IN AS; ADULT TYPE). FT /FTId=VAR_011225. FT VARIANT 289 289 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_001921. FT VARIANT 292 292 G -> R (IN AS). FT /FTId=VAR_011226. FT VARIANT 292 292 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_001922. FT VARIANT 295 295 G -> D (IN AS). FT /FTId=VAR_011227. FT VARIANT 298 298 G -> S (IN AS). FT /FTId=VAR_011228. FT VARIANT 319 319 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_011229. FT VARIANT 325 325 G -> E (IN AS). FT /FTId=VAR_001923. FT VARIANT 325 325 G -> R (IN AS; JUVENILE AND ADULT TYPES). FT /FTId=VAR_001924. FT VARIANT 331 331 G -> V (IN AS). FT /FTId=VAR_007992. FT VARIANT 365 367 MISSING (IN AS; JUVENILE TYPE). FT /FTId=VAR_001926. FT VARIANT 365 365 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_001925. FT VARIANT 371 371 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_001927. FT VARIANT 374 374 G -> A (IN AS). FT /FTId=VAR_001928. FT VARIANT 383 383 G -> D (IN AS; JUVENILE TYPE). FT /FTId=VAR_001929. FT VARIANT 400 400 G -> E (IN AS; ADULT TYPE). FT /FTId=VAR_001930. FT VARIANT 406 406 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_001931. FT VARIANT 409 409 G -> D (IN AS). FT /FTId=VAR_001932. FT VARIANT 412 412 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_011230. FT VARIANT 415 415 G -> R (IN AS). FT /FTId=VAR_011231. FT VARIANT 420 420 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_011232. FT VARIANT 420 420 G -> V (IN AS). FT /FTId=VAR_011233. FT VARIANT 423 423 G -> E (IN AS). FT /FTId=VAR_011234. FT VARIANT 430 430 A -> D. FT /FTId=VAR_001933. FT VARIANT 444 444 I -> S. FT /FTId=VAR_001934. FT VARIANT 456 458 MISSING (IN AS). FT /FTId=VAR_001935. FT VARIANT 466 466 G -> E (IN AS). FT /FTId=VAR_001936. FT VARIANT 472 472 G -> R (IN AS). FT /FTId=VAR_007993. FT VARIANT 491 491 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_011235. FT VARIANT 494 494 G -> D (IN AS; ADULT TYPE). FT /FTId=VAR_001937. FT VARIANT 496 507 MISSING (IN AS; JUVENILE TYPE). FT /FTId=VAR_001938. FT VARIANT 497 497 G -> C (IN AS; ADULT TYPE). FT /FTId=VAR_011236. FT VARIANT 521 521 G -> C (IN AS). FT /FTId=VAR_001939. FT VARIANT 521 521 G -> S (IN AS). FT /FTId=VAR_001940. FT VARIANT 524 524 G -> D (IN AS; ADULT TYPE). FT /FTId=VAR_011237. FT VARIANT 545 545 G -> R (IN AS). FT /FTId=VAR_007994. FT VARIANT 545 545 G -> V (IN AS). FT /FTId=VAR_007995. FT VARIANT 558 558 G -> R (IN AS). FT /FTId=VAR_011238. FT VARIANT 561 561 G -> R (IN AS). FT /FTId=VAR_007996. FT VARIANT 567 567 G -> A (IN AS; JUVENILE TYPE). FT /FTId=VAR_001941. FT VARIANT 573 573 G -> D (IN AS). FT /FTId=VAR_011239. FT VARIANT 579 579 G -> E (IN AS). FT /FTId=VAR_011240. FT VARIANT 579 579 G -> R (IN AS; ADULT TYPE). FT /FTId=VAR_007997. FT VARIANT 603 603 G -> V (IN AS). FT /FTId=VAR_011241. FT VARIANT 609 609 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_011242. FT VARIANT 609 609 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_001942. FT VARIANT 619 619 P -> S. FT /FTId=VAR_011243. FT VARIANT 621 621 G -> C (IN AS). FT /FTId=VAR_011244. FT VARIANT 624 624 G -> D (IN AS). FT /FTId=VAR_011245. FT VARIANT 629 629 G -> D (IN AS). FT /FTId=VAR_011246. FT VARIANT 632 632 G -> D (IN AS). FT /FTId=VAR_011247. FT VARIANT 633 633 E -> K (IN AS). FT /FTId=VAR_011248. FT VARIANT 635 635 G -> D (IN AS). FT /FTId=VAR_007998. FT VARIANT 638 638 G -> A (IN AS). FT /FTId=VAR_001944. FT VARIANT 638 638 G -> S (IN AS; JUVENILE TYPE). FT /FTId=VAR_007999. FT VARIANT 638 638 G -> V (IN AS). FT /FTId=VAR_001943. FT VARIANT 653 653 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_001945. FT VARIANT 664 664 K -> N. FT /FTId=VAR_001946. FT VARIANT 669 669 G -> A (IN AS; JUVENILE TYPE). FT /FTId=VAR_008000. FT VARIANT 681 681 G -> D (IN AS). FT /FTId=VAR_011249. FT VARIANT 684 684 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_001947. FT VARIANT 687 687 G -> E (IN AS). FT /FTId=VAR_008001. FT VARIANT 722 722 G -> E (IN AS). FT /FTId=VAR_011250. FT VARIANT 739 739 P -> A. FT /FTId=VAR_011251. FT VARIANT 739 739 P -> S (IN AS; JUVENILE TYPE). FT /FTId=VAR_011252. FT VARIANT 740 740 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_001948. FT VARIANT 743 743 G -> D (IN AS). FT /FTId=VAR_008002. FT VARIANT 772 772 G -> D (IN AS; JUVENILE TYPE). FT /FTId=VAR_001949. FT VARIANT 796 796 G -> R (IN AS). FT /FTId=VAR_001950. FT VARIANT 802 807 MISSING (IN AS). FT /FTId=VAR_011254. FT VARIANT 802 802 G -> R (IN AS). FT /FTId=VAR_011253. FT VARIANT 808 808 G -> E (IN AS; ADULT TYPE). FT /FTId=VAR_008003. FT VARIANT 811 811 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_011255. FT VARIANT 822 824 MISSING (IN AS). FT /FTId=VAR_008004. FT VARIANT 822 822 G -> R (IN AS). FT /FTId=VAR_011256. FT VARIANT 852 852 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_008005. FT VARIANT 852 852 G -> R (IN AS). FT /FTId=VAR_001951. FT VARIANT 864 875 MISSING (IN AS). FT /FTId=VAR_011257. FT VARIANT 866 866 G -> E (IN AS; ADULT TYPE). FT /FTId=VAR_001952. FT VARIANT 869 869 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_001953. FT VARIANT 872 872 G -> R (IN AS). FT /FTId=VAR_001954. FT VARIANT 878 878 G -> R (IN AS). FT /FTId=VAR_008006. FT VARIANT 898 898 M -> V (IN AS; MILD PHENOTYPE). FT /FTId=VAR_011258. FT VARIANT 902 902 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_011259. FT VARIANT 911 911 G -> E (IN AS). FT /FTId=VAR_011260. FT VARIANT 941 941 G -> C (IN AS). FT /FTId=VAR_011261. FT VARIANT 942 942 MISSING (IN AS). FT /FTId=VAR_001955. FT VARIANT 947 947 G -> D (IN AS). FT /FTId=VAR_011262. FT VARIANT 953 953 G -> V (IN AS; FOUND ON THE SAME ALLELE FT AS VARIANT E-1211). FT /FTId=VAR_011263. FT VARIANT 988 992 MISSING (IN AS; ADULT TYPE). FT /FTId=VAR_008007. FT VARIANT 1006 1006 G -> A (IN AS). FT /FTId=VAR_011264. FT VARIANT 1006 1006 G -> V (IN AS). FT /FTId=VAR_011265. FT VARIANT 1015 1015 G -> E (IN AS). FT /FTId=VAR_011266. FT VARIANT 1015 1015 G -> V (IN AS). FT /FTId=VAR_011267. FT VARIANT 1030 1030 G -> S (IN AS). FT /FTId=VAR_011268. FT VARIANT 1036 1036 G -> V (IN AS). FT /FTId=VAR_011269. FT VARIANT 1039 1039 G -> S (IN AS; JUVENILE TYPE). FT /FTId=VAR_011270. FT VARIANT 1045 1045 G -> E (IN AS). FT /FTId=VAR_011271. FT VARIANT 1066 1066 G -> R (IN AS). FT /FTId=VAR_011272. FT VARIANT 1066 1066 G -> S (IN AS). FT /FTId=VAR_011273. FT VARIANT 1086 1086 G -> D (IN AS). FT /FTId=VAR_011274. FT VARIANT 1104 1104 G -> V (IN AS). FT /FTId=VAR_001956. FT VARIANT 1107 1107 G -> R (IN AS). FT /FTId=VAR_008008. FT VARIANT 1143 1143 G -> D (IN AS; JUVENILE TYPE). FT /FTId=VAR_001957. FT VARIANT 1143 1143 G -> S (IN AS; ADULT TYPE). FT /FTId=VAR_001958. FT VARIANT 1158 1158 G -> R (IN AS). FT /FTId=VAR_011275. FT VARIANT 1161 1161 G -> R (IN AS). FT /FTId=VAR_008009. FT VARIANT 1167 1167 G -> S (IN AS). FT /FTId=VAR_011276. FT VARIANT 1170 1170 G -> S (IN AS). FT /FTId=VAR_011277. FT VARIANT 1182 1182 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_001959. FT VARIANT 1196 1196 G -> R (IN AS). FT /FTId=VAR_011278. FT VARIANT 1205 1205 G -> C (IN AS; JUVENILE TYPE). FT /FTId=VAR_011279. FT VARIANT 1211 1211 G -> E (IN AS; FOUND ON THE SAME ALLELE FT AS VARIANT V-953). FT /FTId=VAR_011280. FT VARIANT 1211 1211 G -> R (IN AS). FT /FTId=VAR_008010. FT VARIANT 1220 1220 G -> D (IN AS). FT /FTId=VAR_008011. FT VARIANT 1229 1229 G -> D (IN AS; ADULT TYPE). FT /FTId=VAR_011281. FT VARIANT 1241 1241 G -> C (IN AS). FT /FTId=VAR_001960. FT VARIANT 1244 1244 G -> D (IN AS). FT /FTId=VAR_011282. FT VARIANT 1252 1252 G -> S (IN AS; ADULT TYPE). FT /FTId=VAR_011283. FT VARIANT 1261 1261 G -> E (IN AS). FT /FTId=VAR_011284. FT VARIANT 1270 1270 G -> S (IN AS). FT /FTId=VAR_001961. FT VARIANT 1333 1333 G -> S (IN AS). FT /FTId=VAR_008012. FT VARIANT 1357 1357 G -> S (IN AS). FT /FTId=VAR_011285. FT VARIANT 1379 1379 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_001962. FT VARIANT 1410 1410 R -> C (IN AS; ADULT AND JUVENILE TYPES). FT /FTId=VAR_001963. FT VARIANT 1421 1421 G -> W (IN AS; ADULT TYPE). FT /FTId=VAR_001964. FT VARIANT 1422 1422 R -> C (IN AS; JUVENILE TYPE). FT /FTId=VAR_001965. FT VARIANT 1427 1427 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_008013. FT VARIANT 1428 1428 L -> M. FT /FTId=VAR_011286. FT VARIANT 1442 1442 G -> D (IN AS). FT /FTId=VAR_008014. FT VARIANT 1451 1451 G -> S (IN AS). FT /FTId=VAR_001966. FT VARIANT 1486 1486 G -> A (IN AS; ADULT TYPE). FT /FTId=VAR_008015. FT VARIANT 1488 1488 S -> F (IN AS). FT /FTId=VAR_011287. FT VARIANT 1498 1498 A -> D (IN AS). FT /FTId=VAR_001967. FT VARIANT 1511 1511 R -> H (IN AS; JUVENILE TYPE; COULD BE A FT NON PATHOGENIC VARIANT). FT /FTId=VAR_011288. FT VARIANT 1517 1517 P -> T (IN AS; JUVENILE TYPE). FT /FTId=VAR_001968. FT VARIANT 1538 1538 W -> S (IN AS; ADULT TYPE). FT /FTId=VAR_001969. FT VARIANT 1559 1559 P -> A. FT /FTId=VAR_008016. FT VARIANT 1563 1563 R -> Q (IN AS). FT /FTId=VAR_001970. FT VARIANT 1564 1564 C -> S (IN AS; ADULT TYPE). FT /FTId=VAR_001971. FT VARIANT 1567 1567 C -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_011289. FT VARIANT 1596 1596 G -> D (IN AS). FT /FTId=VAR_001972. FT VARIANT 1649 1649 L -> R (IN AS; ADULT TYPE). FT /FTId=VAR_001973. FT VARIANT 1677 1677 R -> P (IN AS). FT /FTId=VAR_011290. FT VARIANT 1677 1677 R -> Q (IN AS). FT /FTId=VAR_001974. FT VARIANT 1678 1678 C -> W (IN AS). FT /FTId=VAR_011291. FT CONFLICT 440 441 AG -> GS (IN REF. 3). FT CONFLICT 625 628 FGPP -> LALQ (IN REF. 3). FT CONFLICT 667 668 LP -> FR (IN REF. 3). FT CONFLICT 888 888 A -> R (IN REF. 3). ** ** ################# INTERNAL SECTION ################## **CL Xq22; SQ SEQUENCE 1685 AA; 161044 MW; 4450A6762F12A626 CRC64; MKLRGVSLAA GLFLLALSLW GQPAEAAACY GCSPGSKCDC SGIKGEKGER GFPGLEGHPG LPGFPGPEGP PGPRGQKGDD GIPGPPGPKG IRGPPGLPGF PGTPGLPGMP GHDGAPGPQG IPGCNGTKGE RGFPGSPGFP GLQGPPGPPG IPGMKGEPGS IIMSSLPGPK GNPGYPGPPG IQGLPGPTGI PGPIGPPGPP GLMGPPGPPG LPGPKGNMGL NFQGPKGEKG EQGLQGPPGP PGQISEQKRP IDVEFQKGDQ GLPGDRGPPG PPGIRGPPGP PGGEKGEKGE QGEPGKRGKP GKDGENGQPG IPGLPGDPGY PGEPGRDGEK GQKGDTGPPG PPGLVIPRPG TGITIGEKGN IGLPGLPGEK GERGFPGIQG PPGLPGPPGA AVMGPPGPPG FPGERGQKGD EGPPGISIPG PPGLDGQPGA PGLPGPPGPA GPHIPPSDEI CEPGPPGPPG SPGDKGLQGE QGVKGDKGDT CFNCIGTGIS GPPGQPGLPG LPGPPGSLGF PGQKGEKGQA GATGPKGLPG IPGAPGAPGF PGSKGEPGDI LTFPGMKGDK GELGSPGAPG LPGLPGTPGQ DGLPGLPGPK GEPGGITFKG ERGPPGNPGL PGLPGNIGPM GPPGFGPPGP VGEKGIQGVA GNPGQPGIPG PKGDPGQTIT QPGKPGLPGN PGRDGDVGLP GDPGLPGQPG LPGIPGSKGE PGIPGIGLPG PPGPKGFPGI PGPPGAPGTP GRIGLEGPPG PPGFPGPKGE PGFALPGPPG PPGLPGFKGA LGPKGDRGFP GPPGPPGRTG LDGLPGPKGD VGPNGQPGPM GPPGLPGIGV QGPPGPPGIP GPIGQPGLHG IPGEKGDPGP PGLDVPGPPG ERGSPGIPGA PGPIGPPGSP GLPGKAGASG FPGTKGEMGM MGPPGPPGPL GIPGRSGVPG LKGDDGLQGQ PGLPGPTGEK GSKGEPGLPG PPGPMDPNLL GSKGEKGEPG LPGIPGVSGP KGYQGLPGDP GQPGLSGQPG LPGPPGPKGN PGLPGQPGLI GPPGLKGTIG DMGFPGPQGV EGPPGPSGVP GQPGSPGLPG QKGDKGDPGI SSIGLPGLPG PKGEPGLPGY PGNPGIKGSV GDPGLPGLPG TPGAKGQPGL PGFPGTPGPP GPKGISGPPG NPGLPGEPGP VGGGGHPGQP GPPGEKGKPG QDGIPGPAGQ KGEPGQPGFG NPGPPGLPGL SGQKGDGGLP GIPGNPGLPG PKGEPGFHGF PGVQGPPGPP GSPGPALEGP KGNPGPQGPP GRPGLPGPEG PPGLPGNGGI KGEKGNPGQP GLPGLPGLKG DQGPPGLQGN PGRPGLNGMK GDPGLPGVPG FPGMKGPSGV PGSAGPEGEP GLIGPPGPPG LPGPSGQSII IKGDAGPPGI PGQPGLKGLP GPQGPQGLPG PTGPPGDPGR NGLPGFDGAG GRKGDPGLPG QPGTRGLDGP PGPDGLQGPP GPPGTSSVAH GFLITRHSQT TDAPQCPQGT LQVYEGFSLL YVQGNKRAHG QDLGTAGSCL RRFSTMPFMF CNINNVCNFA SRNDYSYWLS TPEPMPMSMQ PLKGQSIQPF ISRCAVCEAP AVVIAVHSQT IQIPHCPQGW DSLWIGYSFM MHTSAGAEGS GQALASPGSC LEEFRSAPFI ECHGRGTCNY YANSYSFWLA TVDVSDMFSK PQSETLKAGD LRTRISRCQV CMKRT // 1 ID O21165 PRELIMINARY; PRT; 262 AA. AC O21165; DT 01-JAN-1998 (TrEMBLrel. 05, Created) DT 01-JAN-1998 (TrEMBLrel. 05, Last sequence update) DT 01-JUN-2002 (TrEMBLrel. 21, Last annotation update) DE Putative reverse transcriptase (Fragment){EI2}. GN RT{EI2}. OS Fusarium oxysporum. OG Mitochondrion{EI2}. OG Plasmid pFOXC1{EI2}. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreales; mitosporic Hypocreales; Fusarium. OX NCBI_TaxID=5507{EP3}; RN [1]{EI2} RP SEQUENCE FROM N.A. RC TISSUE=Kidney{EI2}, and Liver{EI2}; RX MEDLINE=97394960; PubMed=9251222; RA Kistler H.C., Benny U., Powell W.A.; RT "Linear mitochondrial plasmids of Fusarium oxysporum contain genes RT with sequence similarity to genes encoding a reverse transcriptase RT from Neurospora spp."; RL Appl. Environ. Microbiol. 63:3311-3313(1997). DR EMBL; AF005240; AAD12231.1; -.{EI2} DR InterPro; IPR000477; RVTse. DR Pfam; PF00078; rvt; 1. KW Plasmid{EP3}; RNA-directed DNA polymerase{EP3,EA1}. FT NON_TER 1 1 {EI2} FT NON_TER 262 262 {EI2} ** ** ################# SOURCE SECTION ################## ** Fusarium oxysporum plasmid pFOXC1 putative reverse transcriptase (RT) gene, ** mitochondrial plasmid gene, partial cds. ** [1] ** 1-785 ** MEDLINE; 97394960. ** Kistler H.C., Benny U., Powell W.A.; ** "Linear mitochondrial plasmids of Fusarium oxysporum contain genes with ** sequence similarity to genes encoding a reverse transcriptase from ** Neurospora spp"; ** Appl. Environ. Microbiol. 63(8):3311-3313(1997). ** [2] ** 1-785 ** Kistler H.C., Benny U., Powell W.A.; ** ; ** Submitted (23-MAY-1997) to the EMBL/GenBank/DDBJ databases. ** Plant Pathology, University of Florida, PO Box 110680, Gainesville, FL ** 32611-0680, USA ** SPTREMBL; O21165; O21165. ** source 1..785 ** /db_xref="taxon:5507" ** /organelle="mitochondrion" ** /organism="Fusarium oxysporum" ** /plasmid="pFOXC1" ** CDS complement(<1..>785) ** /codon_start=1 ** /evidence=NOT_EXPERIMENTAL ** /transl_table=4 ** /gene="RT" ** /product="putative reverse transcriptase" ** /protein_id="AAD12231.1" ** CDS_IN_EMBL_ENTRY 1 ** 03-MAR-2000 (Rel. 62, Last updated, Version 3) ** ** ################# INTERNAL SECTION ################## **EV EA1; Rulebase; -; RU000322; 30-JAN-2002. **EV EI2; EMBL; -; AAD12231.1; 30-SEP-2001. **EV EP3; TrEMBL; -; AAD12231.1; 30-SEP-2001. **ID XXXX_FUSOX **PM Pfam; PF00078; rvt; 12; 241; T; 18-MAR-2002; SQ SEQUENCE 262 AA; 30050 MW; 00F0D8B1DAA6A0F4 CRC64; RSELIEIMNQ CRAFRLTMDL KRYYLTKPNG KYRPIGSPTL GSKVISKALT DIWTTIADKR RGVMQHAFRP KLGVWSAAFA VCQKLRSRKP SDVIIEFDLK GFFNTIKRNS VQEAANRFSL LLGNCVRHII DNTRYVFEEL KPETELHIIN DYTHHKYKRA IPIYRTGVPQ GLPLSPVAAT IALENEVNMP EMVMYADDGI LIGGKEKFAE FVKKAIRVGA EVAPEKTREV TKEFKFLGLT FNLEKETVSN GDSYRFWNDK DL // 0 ID NUCA_SERMA STANDARD; PRT; 266 AA. AC P13717; DT 01-JAN-1990 (Rel. 13, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Nuclease precursor (EC 3.1.30.2) (Endonuclease). GN NUCA OR NUC. OS Serratia marcescens. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Serratia. OX NCBI_TaxID=615; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=W225; RX MEDLINE=88084425; PubMed=3319779; RA Ball T.K., Saurugger P.N., Benedick M.J.; RT "The extracellular nuclease gene of Serratia marcescens and its RT secretion from Escherichia coli."; RL Gene 57:183-192(1987). RN [2] RP REVISIONS TO 7-11. RC STRAIN=W225; RA Benedick M.J.; RL Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 21-266, AND DISULFIDE BONDS. RC STRAIN=B10M1; RX MEDLINE=93385170; PubMed=8373817; RA Pedersen J., Filimonova M.N., Roepstorff P., Biedermann K.; RT "Characterization of Serratia marcescens nuclease isoforms by plasma RT desorption mass spectrometry."; RL Biochim. Biophys. Acta 1202:13-21(1993). RN [4] RP PARTIAL SEQUENCE, AND DISULFIDE BONDS. RX MEDLINE=89322554; PubMed=2665765; RA Biedermann K., Jepsen P.K., Riise E., Svendsen I.; RT "Purification and characterization of a Serratia marcescens nuclease RT produced by Escherichia coli."; RL Carlsberg Res. Commun. 54:17-27(1989). RN [5] RP ACTIVE SITE. RX MEDLINE=94359798; PubMed=8078761; RA Friedhoof P., Gimadutdinow O., Pingoud A.; RT "Identification of catalytically relevant amino acids of the RT extracellular Serratia marcescens endonuclease by alignment-guided RT mutagenesis."; RL Nucleic Acids Res. 22:3280-3287(1994). RN [6] RP KINETIC STUDIES. RX MEDLINE=95102530; PubMed=7804150; RA Filimonova M.N., Krause K.L., Benedik M.J.; RT "Kinetic studies of the Serratia marcescens extracellular nuclease RT isoforms."; RL Biochem. Mol. Biol. Int. 33:1229-1236(1994). RN [7] RP MUTAGENESIS. RX MEDLINE=96313223; PubMed=8758988; RA Firedhoff P., Kolmes B., Gimadutdinow O., Wende W., Krause K.L., RA Pingoud A.; RT "Analysis of the mechanism of the Serratia nuclease using site- RT directed mutagenesis."; RL Nucleic Acids Res. 24:2632-2639(1996). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX MEDLINE=95393180; PubMed=7664065; RA Miller M.D., Tanner J., Alpaugh M., Benedik M.J., Krause K.L.; RT "2.1-A structure of Serratia endonuclease suggests a mechanism for RT binding to double-stranded DNA."; RL Nat. Struct. Biol. 1:461-468(1994). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX MEDLINE=97400229; PubMed=9257723; RA Lunin V.Y., Levdikov V.M., Shlyapnikov S.V., Blagova E.V., Lunin V.V., RA Wilson K.S., Mikhailov A.M.; RT "Three-dimensional structure of Serratia marcescens nuclease at 1.7-A RT resolution and mechanism of its action."; RL FEBS Lett. 412:217-220(1997). CC -!- FUNCTION: CATALYZES THE HYDROLYSIS OF BOTH DNA AND RNA, DOUBLE- OR CC SINGLE-STRANDED, AT THE 3'POSITION OF THE PHOSPHODIESTER BOND TO CC PRODUCE 5'-PHOSPHORYLATED MONO-, DI-, TRI- AND TETRANUCLEOTIDES. CC DNA IS A SLIGHTLY BETTER SUBSTRATE THAN RNA. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomononucleotide and 5'-phosphooligonucleotide end-products. CC -!- COFACTOR: CC Note=MAGNESIUM IS IMPORTANT FOR ACTIVITY; IN ITS ABSENCE NUCLEASE CC ACTIVITY IS SIGNIFICANTLY REDUCED.; CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: BELONGS TO THE DNA/RNA NON-SPECIFIC ENDONUCLEASES CC FAMILY. DR EMBL; M19495; AAA26560.1; -. DR PIR; A27356; A27356. DR PDB; 1SMN; 29-JAN-96. DR InterPro; IPR001604; Endonuclease. DR Pfam; PF01223; Endonuclease; 1. DR SMART; SM00477; NUC; 1. DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1. KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Nuclease; Signal. FT SIGNAL 1 20 FT CHAIN 21 266 NUCLEASE, ISOFORM SM2. FT CHAIN 22 266 NUCLEASE, ISOFORM SM3. FT CHAIN 24 266 NUCLEASE, ISOFORM SM1. FT ACT_SITE 110 110 FT DISULFID 30 34 FT DISULFID 222 264 ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 266 AA; 28945 MW; A0FF0C1430677B9E CRC64; MRFNNKMLAL AALLFAAQAS ADTLESIDNC AVGCPTGGSS NVSIVRHAYT LNNNSTTKFA NWVAYHITKD TPASGKTRNW KTDPALNPAD TLAPADYTGA NAALKVDRGH QAPLASLAGV SDWESLNYLS NITPQKSDLN QGAWARLEDQ ERKLIDRADI SSVYTVTGPL YERDMGKLPG TQKAHTIPSA YWKVIFINNS PAVNHYAAFL FDQNTPKGAD FCQFRVTVDE IEKRTGLIIW AGLPDDVQAS LKSKPGVLPE LMGCKN // 1 ID CLP1_AGRT5 STANDARD; PRT; 202 AA. AC Q8UEX6; DT 15-JUN-2002 (Rel. 41, Created) DT 15-JUN-2002 (Rel. 41, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE ATP-dependent Clp protease proteolytic subunit 1 (EC 3.4.21.92) DE (Endopeptidase Clp 1). GN CLPP1 OR AGR_C_3003 OR ATU1627. OS Agrobacterium tumefaciens (strain C58 / ATCC 33970). OC Bacteria; Proteobacteria; alpha subdivision; Rhizobiaceae group; OC Rhizobiaceae; Rhizobium. OX NCBI_TaxID=176299; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21608550; PubMed=11743193; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., RA Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., RA Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., RA Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., RA Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., RA Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., RA Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., RA Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=21608551; PubMed=11743194; DOI=10.1002; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., RA Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in CC the presence of ATP and magnesium. Alpha-casein is the usual test CC substrate. In the absence of ATP, only oligopeptides shorter than CC five residues are cleaved (such as succinyl-Leu-Tyr-|-NHMEC; and CC Leu-|-Tyr-Trp, in which the cleavage of the -Tyr-|-Leu- bond also CC occurs). CC -!- CATALYTIC ACTIVITY: Cleaves Leu-|- bonds and disulfide-bonds. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=1; CC Comment=This is just a test; CC Name=1; CC IsoId=Q8UEX6-1; Sequence=Displayed; CC -!- RNA EDITING: Modified_positions=Not_applicable; Note=a; CC -!- RNA EDITING: Modified_positions=Undetermined; DR EMBL; AE009120; AAL42629.1; -. DR EMBL; AE008085; AAK87406.1; -. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; FALSE_NEG. KW Complete proteome; Hydrolase; Serine protease. FT ACT_SITE 102 102 BY SIMILARITY. FT ACT_SITE 127 127 Performs a certain function (By FT similarity). ** ** ################# INTERNAL SECTION ################## **HA SAM; Annotated by PicoHamap 1.56; MF_00444.2; 21-JUN-2002. **HF HAMAP; MF_00444; 1. **NI CLPP1 SQ SEQUENCE 202 AA; 22834 MW; 754E1B1D1A82C36C CRC64; MRETMQLVPM VVEQSSRGER SFDIYSRLLR ERIIFLNGEV DDTVSALVCA QLLFLEAENP KKPIHLYINS PGGMVTSGFA MYDTMRYIRA PVHTLCMGTA RSMGSFLLMA GEPGTRAALP NASILIHQPS GGFQGQASDM LIHAEEIRQT KHRMTRLYAE HCGRSYEEFE TAMDRDRFMT VQEALEWGLI DRILEVREDA AA // 1 ID CPB2_STRPN STANDARD; PRT; 243 AA. AC Q54518; O08049; O08278; O52232; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Protein-tyrosine phosphatase cpsB (EC 3.1.3.48). GN CPSB OR CAP1B OR CPS19FB. OS Streptococcus pneumoniae. OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1313; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NCTC 11906 / Serotype 19F, PO-329 / Serotype 19F, RC SP-496 / Serotype 19F, SP-GA71 / Serotype 19F, SP-VA92 / Serotype 19F, RC and SP-VA96 / Serotype 19F; RC TISSUE=Adrenal, Adrenal gland, Carcinoma, Femoral artery, RC Pancreatic acinar, and Pituitary; RX MEDLINE=98125733; PubMed=9466257; RA Coffey T.J., Enright M.C., Daniels M., Morona J.K., Morona R., RA Hryniewicz W., Paton J.C., Spratt B.G.; RT "Recombinational exchanges at the capsular polysaccharide biosynthetic RT locus lead to frequent serotype changes among natural isolates of RT Streptococcus pneumoniae."; RL Mol. Microbiol. 27:73-83(1998). CC -!- FUNCTION: Dephosphorylates cpsD. Involved in the regulation of CC capsular polysaccharide biosynthesis. CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- COFACTOR: CC Note=Manganese.; CC -!- PATHWAY: Capsular polysaccharide (CPS) biosynthesis. CC -!- RNA EDITING: Modified_positions=1306; Note=Partially edited. A CC stop codon is created at this position; CC -!- RNA EDITING: Modified_positions=Undetermined; CC -!- SIMILARITY: BELONGS TO THE CPSB/CAPC FAMILY. DR EMBL; U09239; AAC44959.1; -. DR EMBL; Z83335; CAB05935.1; -. DR EMBL; AF030367; AAC38717.1; -. DR EMBL; AF030368; AAC38722.1; -. DR EMBL; AF030369; AAC38727.1; -. DR EMBL; AF030370; AAC38731.1; -. DR EMBL; AF030371; AAC38736.1; -. DR EMBL; AF030372; AAC38741.1; -. DR EMBL; AF106137; AAD17985.1; -. DR InterPro; IPR004013; PHP_C. DR Pfam; PF02811; PHP_C; 1. KW Bacterial capsule; Exopolysaccharide synthesis; Hydrolase; Manganese. FT VARIANT 226 226 A -> V (IN STRAIN NCTC 11906). FT MUTAGEN 199 199 D->N: LOSS OF ACTIVITY; WHEN ASSOCIATED FT WITH Q-201. FT MUTAGEN 201 201 H->Q: LOSS OF ACTIVITY; WHEN ASSOCIATED FT WITH N-199. ** ** ################# INTERNAL SECTION ################## **NI CPSB2 **ZA CAR, 22-JAN-2003; SQ SEQUENCE 243 AA; 28354 MW; 810A4C802EC43079 CRC64; MIDIHSHIVF DVDDGPKSRE ESKALLAESY RQGVRTIVST SHRRKGMFET PEEKIAENFL QVREIAKEVA DDLVIAYGAE IYYTLDALEK LEKKEIPTLN DSRYALIEFS MHTSYRQIHT GLSNILMLGI TPVIAHIERY DALENNEKRV RELIDMGCYT QINSYHVSKP KFFGEKYKFM KKRARYFLER DLVHVVASDM HNLDSRPPYM QQAYDIIAKK YGAKKAKELF VDNPRKIIMD QLI // 1 ID ATL_STAAU STANDARD; PRT; 1256 AA. AC P52081; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Bifunctional autolysin precursor [Includes: N-acetylmuramoyl-L-alanine DE amidase (EC 3.5.1.28); Mannosyl-glycoprotein endo-beta-N- DE acetylglucosamidase (EC 3.2.1.96)]. GN ATL. OS Staphylococcus aureus. OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=1280; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 205-214 AND 776-792. RC STRAIN=RN450; RX MEDLINE=95116542; PubMed=7816834; RX DOI=10.1002/1615-9861(200212)2:12<1682::AID-PROT1682>3.0.COAID-PROT1682>3.0.CO;2-Y; RA Oshida T., Sugai M., Komatsuzawa H., Hong Y.-M., Suginaka H., RA Tomasz A.; RT "A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L- RT alanine amidase domain and an endo-beta-N-acetylglucosaminidase RT domain: cloning, sequence analysis, and characterization."; RL Proc. Natl. Acad. Sci. U.S.A. 92:285-289(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=NCTC 8325-4; RA Foster S.J.; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 1-28. RX MEDLINE=81090973; PubMed=6108877; RA Bennett C.D.; ** /NO TITLE. RL Unpublished results, cited by: RL Norton T.R.; RL Fed. Proc. 40:21-25(1981). CC -!- FUNCTION: ENDOHYDROLYSIS OF THE DI-N-ACETYLCHITOBIOSYL UNIT IN CC HIGH-MANNOSE GLYCOPEPTIDES AND GLYCOPROTEINS CONTAINING THE CC -[(MAN)5(GLCNAC)2]-ASN STRUCTURE. ONE N-ACETYL-D-GLUCOSAMINE CC RESIDUE REMAINS ATTACHED TO THE PROTEIN; THE REST OF THE CC OLIGOSACCHARIDE IS RELEASED INTACT. CC -!- CATALYTIC ACTIVITY: Hydrolyzes the link between N-acetylmuramoyl CC residues and L-amino acid residues in certain bacterial cell-wall CC glycopeptides. CC -!- CATALYTIC ACTIVITY: Endohydrolysis of the di-N-acetylchitobiosyl CC unit in high-mannose glycopeptides and glycoproteins containing CC the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine CC residue remains attached to the protein; the rest of the CC oligosaccharide is released intact. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: Undergoes proteolytic processing to generate the two CC extracellular lytic enzymes. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE N- CC ACETYLMURAMOYL-L-ALANINE AMIDASE FAMILY 2. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO FAMILY 73 OF CC GLYCOSYL HYDROLASES. DR EMBL; D17366; BAA04185.1; -. DR EMBL; L41499; AAA99982.1; -. DR InterPro; IPR002502; Amidase_2. DR InterPro; IPR002901; Amidase_4. DR Pfam; PF01510; Amidase_2; 1. DR Pfam; PF01832; Amidase_4; 1. DR SMART; SM00644; Ami_2; 1. DR SMART; SM00047; LYZ2; 1. KW Cell wall; Hydrolase; Multifunctional enzyme; Repeat; Signal. FT SIGNAL 1 29 Potential. FT CHAIN 30 1256 Bifunctional autolysin. FT DOMAIN 199 775 N-acetylmuramoyl-L-alanine amidase. FT REPEAT 425 589 1. FT REPEAT 596 758 2. FT REPEAT 770 932 3. FT DOMAIN 776 1256 ENDO-BETA-N-ACETYLGLUCOSAMIDASE. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 1256 AA; 137384 MW; 2BB76CAA292FDD20 CRC64; MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA TTEQAKAEVK NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ VNGDTRANQS ATTNNTQPVA KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE NQINPELIKS AAKPAALETQ YKTAAPKAAT TSAPKAKTEA TPKVTTFSAS AQPRSVAATP KTSLPKYKPQ VNSSINDYIC KNNLKAPKIE EDYTSYFPKY AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ YYGLKPDSAE YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY DLINEKYLIK MGKVAPWGTQ STTTPTTPSK PTTPSKPSTG KLTVAANNGV AQIKPTNSGL YTTVYDKTGK ATNEVQKTFA VSKTATLGNQ KFYLVQDYNS GNKFGWVKEG DVVYNTAKSP VNVNQSYSIK PGTKLYTVPW GTSKQVAGSV SGSGNQTFKA SKQQQIDKSI YLYGSVNGKS GWVSKAYLVD TAKPTPTPTP KPSTPTTNNK LTVSSLNGVA QINAKNNGLF TTVYDKTGKP TKEVQKTFAV TKEASLGGNK FYLVKDYNSP TLIGWVKQGD VIYNNAKSPV NVMQTYTVKP GTKLYSVPWG TYKQEAGAVS GTGNQTFKAT KQQQIDKSIY LFGTVNGKSG WVSKAYLAVP AAPKKAVAQP KTAVKAYTVT KPQTTQTVSK IAQVKPNNTG IRASVYEKTA KNGAKYADRT FYVTKERAHG NETYVLLNNT SHNIPLGWFN VKDLNVQNLG KEVKTTQKYT VNKSNNGLSM VPWGTKNQVI LTGNNIAQGT FNATKQVSVG KDVYLYGTIN NRTGWVNAKD LTAPTAVKPT TSAAKDYNYT YVIKNGNGYY YVTPNSDTAK YSLKAFNEQP FAVVKEQVIN GQTWYYGKLS NGKLAWIKST DLAKELIKYN QTGMTLNQVA QIQAGLQYKP QVQRVPGKWT DAKFNDVKHA MDTKRLAQDP ALKYQFLRLD QPQNISIDKI NQFLKGKGVL ENQGAAFNKA AQMYGINEVY LISHALLETG NGTSQLAKGA DVVNNKVVTN SNTKYHNVFG IAAYDNDPLR EGIKYAKQAG WDTVSKAIVG GAKFIGNSYV KAGQNTLYKM RWNPAHPGTH QYATDVDWAN INAKIIKGYY DKIGEVGKYF DIPQYK // 1 ID ALBU_BOVIN STANDARD; PRT; 607 AA. AC P02769; O02787; DT 21-JUL-1986 (Rel. 01, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serum albumin precursor (Allergen Bos d 6). GN Name=ALB; Synonyms=aal, abl, ALB1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RA Holowachuk E.W., Stoltenborg J.K., Reed R.G., Peters T. Jr.; RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A., AND VARIANT THR-214. RC TISSUE=Liver; RA Barry T., Power S., Gannon F.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RA Hilger C., Grigioni F., de Beaufort C., Michel G., Hentges F.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A., AND VARIANT THR-214. RA Wu H.T., Huang M.C.; RT "The complete cDNA sequence of bovine serum albumin."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 1-32. RX MEDLINE=80024278; PubMed=488109; RA McGillivray R.T.A., Chung D.W., Davie E.W.; RT "Biosynthesis of bovine plasma proteins in a cell-free system. Amino- RT terminal sequence of preproalbumin."; RL Eur. J. Biochem. 98:477-485(1979). RN [6] RP SEQUENCE OF 25-424 AND 429-607, AND VARIANT THR-214. ** MEDLINE=None; PubMed=None; RA Brown J.R.; RT "Structure of bovine serum albumin."; RL Fed. Proc. 34:591-591(1975). RN [7] RP REVISIONS TO 190-195. RA Brown J.R.; RL Submitted (APR-1975) to the PIR data bank. RN [8] RP SEQUENCE OF 402-433. RX MEDLINE=82023364; PubMed=7283978; RA Reed R.G., Putnam F.W., Peters T. Jr.; RT "Sequence of residues 400-403 of bovine serum albumin."; RL Biochem. J. 191:867-868(1980). RN [9] RP SEQUENCE OF 19-28. RX MEDLINE=77134075; PubMed=843354; RA Patterson J.E., Geller D.M.; RT "Bovine microsomal albumin: amino terminal sequence of bovine RT proalbumin."; RL Biochem. Biophys. Res. Commun. 74:1220-1226(1977). RN [10] RP SEQUENCE, AND REVISIONS TO 118-119 AND 180. RX MEDLINE=91083649; PubMed=2260975; RA Hirayama K., Akashi S., Furuya M., Fukuhara K.-I.; RT "Rapid confirmation and revision of the primary structure of bovine RT serum albumin by ESIMS and Frit-FAB LC/MS."; RL Biochem. Biophys. Res. Commun. 173:639-646(1990). RN [11] RP SEQUENCE OF 25-41. RX MEDLINE=88267456; PubMed=3389500; RA Hsieh J.C., Lin F.P., Tam M.F.; RT "Electroblotting onto glass-fiber filter from an analytical RT isoelectrofocusing gel: a preparative method for isolating proteins RT for N-terminal microsequencing."; RL Anal. Biochem. 170:1-8(1988). RN [12] RP SEQUENCE OF 437-451. RA Vilbois F.; RL Submitted (AUG-1998) to Swiss-Prot. RN [13] RP DISULFIDE BONDS. ** MEDLINE=None; PubMed=None; RA Brown J.R.; RT "Structure of serum albumin: disulfide bridges."; RL Fed. Proc. 33:1389-1389(1974). CC -!- FUNCTION: Serum albumin, the main protein of plasma, has a good CC binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, CC hormones, bilirubin and drugs. Its main function is the regulation CC of the colloidal osmotic pressure of blood. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=62 mM for glucose{EA1}; CC KM=90 mM for maltose{EP1}; CC Vmax=0.11 mmol/min/mg enzyme when maltose is used as the CC substrate; CC Vmax=0.20 mmol/min/mg enzyme when glucose is used as the CC substrate; CC Note=Acetylates glucose, maltose, mannose, galactose, and CC fructose with a decreasing relative rate of 1, 0.55, 0.20, 0.07, CC 0.04; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC -!- INTERACTION: CC P38936:CDKN1A; NbExp=1; IntAct=EBI-374862, EBI-375077; CC P42771:CDKN2A; NbExp=1; IntAct=EBI-374862, EBI-375053; CC Q9H211:CDT1; NbExp=1; IntAct=EBI-374862, EBI-456953; CC Q96H67:cdt1; NbExp=1; IntAct=EBI-374862, EBI-371677; CC Q7L590:MCM10; NbExp=1; IntAct=EBI-374862, EBI-374912; CC P49736:MCM2; NbExp=1; IntAct=EBI-374862, EBI-374819; CC P25205:MCM3; NbExp=1; IntAct=EBI-374862, EBI-355153; CC Q13415:ORC1L; NbExp=1; IntAct=EBI-374862, EBI-374847; CC Q13416:ORC2L; NbExp=1; IntAct=EBI-374862, EBI-374957; CC Q9UBD5:ORC3L; NbExp=1; IntAct=EBI-374862, EBI-374916; CC O43913:ORC5L; NbExp=1; IntAct=EBI-374862, EBI-374928; CC Q9Y5N6:ORC6L; NbExp=1; IntAct=EBI-374862, EBI-374840; CC P62988:RPS27A; NbExp=1; IntAct=EBI-374862, EBI-413034; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q92482-1; Sequence=Displayed; CC Name=2; Synonyms=delta5; CC IsoId=Q92482-2, Q92482-3; CC Sequence=VSP_003229, VSP_003230, VSP_003229, VSP_003230, CC VSP_003229, VSP_003230; CC Note=Due to a polymorphism at the 5'-splice donor site of intron CC 5, leading to exon 5 skipping and premature termination of CC translation. This is the molecular basis of the GIL blood group; CC -!- TISSUE SPECIFICITY: Plasma. CC -!- ALLERGEN: Causes an allergic reaction in human. CC -!- TOXIC DOSE: LD(50) of the glycosylated and non-glycosylated forms CC are 13.4 +/- 0.7 and 5.8 +/- 0.3 nmol/g by intra-abdominal CC injection into the cricket G.assimilis, respectively. LD(50) of CC the glycosylated and non-glycosylated forms are 15 +/- 1 and 0.16 CC +/- 0.01 uM for human HL-60 cells, respectively. CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. CC -!- SIMILARITY: Contains 3 albumin domains. DR EMBL; M73993; AAA51411.1; -. DR EMBL; X58989; CAA41735.1; -. DR EMBL; Y17769; CAA76847.1; -. DR EMBL; AF542068; AAN17824.1; -. DR InterPro; IPR000264; Serum_albumin. DR Pfam; PF00273; Serum_albumin; 3. DR PRINTS; PR00802; SERUMALBUMIN. DR ProDom; PD002486; Serum_albumin; 1. DR SMART; SM00103; ALBUMIN; 3. DR PROSITE; PS00212; ALBUMIN; 3. DR HSSP; P02768; 1HK1. KW Allergen; Copper; Lipid-binding; Metal-binding; Polymorphism; Repeat; KW Signal. FT SIGNAL 1 18 FT PROPEP 19 24 FT CHAIN 25 607 Serum albumin. FT DOMAIN 25 204 Albumin 1. FT DOMAIN 211 396 Albumin 2. FT DOMAIN 403 594 Albumin 3. FT METAL 27 27 Copper (By similarity). FT DISULFID 77 86 FT DISULFID 99 115 FT DISULFID 114 125 FT DISULFID 147 192 FT DISULFID 191 200 FT DISULFID 223 269 FT DISULFID 268 276 FT DISULFID 288 302 FT DISULFID 301 312 FT DISULFID 339 384 FT DISULFID 383 392 FT DISULFID 415 461 FT DISULFID 460 471 FT DISULFID 484 500 FT DISULFID 499 510 FT DISULFID 537 582 FT DISULFID 581 590 FT VARIANT 214 214 A -> T. FT MUTAGEN 398 429 KRSRSDRAVTGPSAQQSFEVRVPEQRDALHLPLSWRVKRP FT ->TA: Complete loss of HR activity. FT MUTAGEN 399 429 TYEGKHNHHLLLSPPSSSTLPFNSPQLSKQTI->SLQPTRV FT NIIIICS: In ttg2-2; defects in trichome FT development, seed coat color and mucilage FT production. FT CONFLICT 302 302 C -> K (in Ref. 6). FT CONFLICT 304 305 KP -> PC (in Ref. 6). FT CONFLICT 324 324 N -> D (in Ref. 6). FT CONFLICT 394 395 ST -> TS (in Ref. 6). FT CONFLICT 437 437 K -> R (in Ref. 12). FT CONFLICT 493 494 SE -> ES (in Ref. 6). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 607 AA; 69293 MW; 39167DFE768585D4 CRC64; MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFKDLGE EHFKGLVLIA FSQYLQQCPF DEHVKLVNEL TEFAKTCVAD ESHAGCEKSL HTLFGDELCK VASLRETYGD MADCCEKQEP ERNECFLSHK DDSPDLPKLK PDPNTLCDEF KADEKKFWGK YLYEIARRHP YFYAPELLYY ANKYNGVFQE CCQAEDKGAC LLPKIETMRE KVLASSARQR LRCASIQKFG ERALKAWSVA RLSQKFPKAE FVEVTKLVTD LTKVHKECCH GDLLECADDR ADLAKYICDN QDTISSKLKE CCDKPLLEKS HCIAEVEKDA IPENLPPLTA DFAEDKDVCK NYQEAKDAFL GSFLYEYSRR HPEYAVSVLL RLAKEYEATL EECCAKDDPH ACYSTVFDKL KHLVDEPQNL IKQNCDQFEK LGEYGFQNAL IVRYTRKVPQ VSTPTLVEVS RSLGKVGTRC CTKPESERMP CTEDYLSLIL NRLCVLHEKT PVSEKVTKCC TESLVNRRPC FSALTPDETY VPKAFDEKLF TFHADICTLP DTEKQIKKQT ALVELLKHKP KATEEQLKTV MENFVAFVDK CCAADDKEAC FAVEGPKLVV STQTALA // 1 Swissknife_1.75/t/formatProblems.txl0000644005110600510130000032165712377410251020061 0ustar ecastroSwissProtID PPK5_PERAM PRELIMINARY; PRT; 17 AA. AC P82617; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE PYROKININ-5 (PEA-PK-5) (FXPRL-AMIDE). OS Periplaneta americana (American cockroach). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Orthopteroidea; Dictyoptera; Blattaria; OC Blattoidea; Blattidae; Periplaneta. OX NCBI_TaxID=6978; RN [1] RP SEQUENCE, FUNCTION, AND MASS SPECTROMETRY. RC TISSUE=ABDOMINAL PERISYMPATHETIC ORGANS; RX MEDLINE=99212469; PubMed=10196736; RG The Three Stooges; RA Predel R., Kellner R., Nachman R.J., Holman G.M., Rapus J., Gaede G.; RT "Differential distribution of pyrokinin-isoforms in cerebral and RT abdominal neurohemal organs of the American cockroach."; RL Insect Biochem. Mol. Biol. 29:139-144(1999). RN [2] RP TISSUE SPECIFICITY. RC STRAIN=12,714 / SCARLATINA; RX MEDLINE=20189894; PubMed=10723010; RG The Three RG Stooges; RT "Tagma-specific distribution of FXPRLamides in the nervous system of RT the American cockroach."; RL J. Comp. Neurol. 419:352-363(2000). CC -!- FUNCTION: MEDIATES VISCERAL MUSCLE CONTRACTILE ACTIVITY CC (MYOTROPIC ACTIVITY). CC -!- TISSUE SPECIFICITY: MAINLY IN ABDOMINAL PERISYMPATHETIC ORGANS AND CC TO A LESSER EXTENT IN RETROCEREBRAL COMPLEX. CC -!- MASS SPECTROMETRY: Mass=1651.7; Method=MALDI; CC -!- SIMILARITY: BELONGS TO THE PYROKININ FAMILY. CC -!- SIMILARITY: BELONGS TO THE PYROKININ FAMILY. CC -!- RNA EDITING: Modified_positions=2. CC -------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License. CC -------------------------------------------------------------------------- DR INTERPRO; IPR001484; -. DR PROSITE; PS00539; PYROKININ; UNKNOWN_1. KW Amidation; Neuropeptide; Pyrokinin. FT MOD_RES 17 17 AMIDATION. FT MOD_RES 17 17 AMIDATIONAMIDATIONAMIDATIONAMIDATIONAMIDATIONAMIDATION. FT DOMAIN 638 758 CONTAINS CONSERVED RESIDUES USED FOR FT 3' -> 5' EXONUCLEASE ACTIVITIES. FT VARIANT 74 74 Q -> R (IN HYPOGONADISM; LACK OF FT RECEPTOR-BINDING). FT VARIANT 74 74 Q -> R (IN A VERY SELDOM ENCOUNTERED RARE FORM OF HYPOGONADISMHYPOGONADISMHYPOGONADISMHYPOGONADISM; LACK OF FT RECEPTOR-BINDING). FT VARIANT 74 74 Q -> R (IN HYPOGONADISMHYPOGONADISMHYPOGONADISMHYPOGONADISM; LACK OF FT RECEPTOR-BINDING). FT VARIANT 74 74 Q -> R (IN HYPOGONADISMHYPOGONADISMHYPOGONADISM-HYPOGONADISM; LACK OF FT RECEPTOR-BINDING). FT VARIANT 74 74 Q -> RRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRR (IN HYPOGONADISM). FT VARIANT 67 67 K -> M (IN ALLELE PGM1*7+, ALLELE PGM1*7- FT , ALLELE PGM1*3+ AND ALLELE PGM1*3-). FT /FTId=VAR_006090. ** ################# SOURCE SECTION ################## ** ################# INTERNAL SECTION ################## **ZZ CREATED AND FINISHED BY NICO. **ZZ DS 43484. **ZZ UPDATED BY NICO (7/8/00). ADDED TISSUE SPECIFICITY. **ZZ CURATED. SQ SEQUENCE 17 AA; 1653 MW; 8527162EA45BBA54 CRC64; GGGGSGETSG MWFGPRL // ID PPK5_PERAM PRELIMINARY; PRT; 17 AA. AC P82617; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE Light-independent protochlorophyllide reductase subunit B (EC DE 1.18.-.-) (LI-POR subunit B) (DPOR subunit B). OS Periplaneta americana (American cockroach). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Orthopteroidea; Dictyoptera; Blattaria; OC Blattoidea; Blattidae; Periplaneta. OX NCBI_TaxID=6978; RN [1] RP SEQUENCE, FUNCTION, AND MASS SPECTROMETRY. RC TISSUE=ABDOMINAL PERISYMPATHETIC ORGANS; RX MEDLINE=99212469; PubMed=10196736; RA Predel R., Kellner R., Nachman R.J., Holman G.M., Rapus J., Gaede G.; RT "Differential distribution of pyrokinin-isoforms in cerebral and RT abdominal neurohemal organs of the American cockroach."; RG French Parkinson's disease genetics study group; RG European consortium on genetic susceptibility on Parkinson's disease; RL Insect Biochem. Mol. Biol. 29:139-144(1999). RN [2] RP TISSUE SPECIFICITY. RX MEDLINE=20189894; PubMed=10723010; RA Predel R., Eckert M.; RT "Tagma-specific distribution of FXPRLamides in the nervous system of RT the American cockroach."; RL J. Comp. Neurol. 419:352-363(2000). CC -!- FUNCTION: MEDIATES VISCERAL MUSCLE CONTRACTILE ACTIVITY CC (MYOTROPIC ACTIVITY). CC -!- TISSUE SPECIFICITY: MAINLY IN ABDOMINAL PERISYMPATHETIC ORGANS AND CC TO A LESSER EXTENT IN RETROCEREBRAL COMPLEX. CC -!- MASS SPECTROMETRY: MW=1651.7; METHOD=MALDI; CC -!- SIMILARITY: BELONGS TO THE PYROKININ FAMILY. DR PRODOM; PD010497; -; 1. DR INTERPRO; IPR001484; -. DR PROSITE; PS00539; PYROKININ; UNKNOWN_1. ** PROSITE; PS00537; PYROKININ; FALSE_POS_1. ** ################# SOURCE SECTION ################## ** ################# INTERNAL SECTION ################## **PM PROSITE; PS00539; PYROKININ; 13; 17; ?; 06-SEP-2000; **ZZ CREATED AND FINISHED BY NICO. **ZZ DS 43484. **ZZ UPDATED BY NICO (7/8/00). ADDED TISSUE SPECIFICITY. **ZZ CURATED. SQ SEQUENCE 17 AA; 1653 MW; 8527162EA45BBA54 CRC64; GGGGSGETSG MWFGPRL // ID O54521 PRELIMINARY; PRT; 144 AA. AC O54521; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE SLYA. GN SLYA. OS Salmonella enterica serovar Typhi. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Salmonella. OX NCBI_TaxID=90370, 119912; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=TY2, RF-1; RA Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., RA Nonaka T., Matsui H., Kawahara K., Danbara H.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. DR EMBL; AB010777; BAA24582.1; -. DR EMBL; AB010776; BAA24581.1; -. DR INTERPRO; IPR000835; -. DR PFAM; PF01047; MarR; 1. DR PRINTS; PR00598; HTHMARR. DR PROSITE; PS01117; HTH_MARR_FAMILY; 1. ** PROSITE pattern is not entirely correct. Test comment. ** ** ################# SOURCE SECTION ################## ** PSMID1233 STANDARD ** Salmonella choleraesuis serovar Typhi gene for SlyA, complete cds. ** [1] ** 1-636 ** Okada N.; ** ; ** Submitted (27-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Nobuhiko Okada, Kitasato University, School of Pharmaceutical ** Sciences, ** Department of Microbiology; 5-9-1 Shirokane, Minato, Tokyo 108-8641, ** Japan (E-mail:okadan@platinum.pharm.kitasato-u.ac.j p, ** Tel:03-3444-6161, ** Fax:03-3444-4831) ** [2] ** Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., Nonaka ** T., ** Matsui H., Kawahara K., Danbara H.; ** "Identification of TTG initiation codon in slyA of Salmonella, a gene ** required for survival within macrophages"; ** Unpublished. ** [1] ** 1-636 ** Okada N.; ** ; ** Submitted (27-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Nobuhiko Okada, Kitasato University, School of Pharmaceutical ** Sciences, ** Department of Microbiology; 5-9-1 Shirokane, Minato, Tokyo 108-8641, ** Japan (E-mail:okadan@platinum.pharm.kitasato-u.ac.j p, ** Tel:03-3444-6161, ** Fax:03-3444-4831) ** [2] ** Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., Nonaka ** T., ** Matsui H., Kawahara K., Danbara H.; ** "Identification of TTG initiation codon in slyA of Salmonella, a gene ** required for survival within macrophages"; ** Unpublished. ** source 1..636 ** /organism="Salmonella choleraesuis serovar Typhi" ** /sequenced_mol="DNA" ** /strain="Ty2" ** CDS 154..588 ** /codon_start=1 ** /db_xref="PID:d1025502" ** /transl_table=11 ** /gene="slyA" ** /product="SlyA" ** CDS_IN_EMBL_ENTRY 1 ** ORGANISM DOESN'T EXIST IN SP ** 11-FEB-1998 (Rel. 54, Last updated, Version 2) ** source 1..636 ** /organism="Salmonella choleraesuis choleraesuis" ** /sequenced_mol="DNA" ** /strain="RF-1" ** CDS 154..588 ** /codon_start=1 ** /db_xref="PID:d1025501" ** /transl_table=11 ** /gene="slyA" ** /product="SlyA" ** CDS_IN_EMBL_ENTRY 1 ** ORGANISM DOESN'T EXIST IN SP ** 11-FEB-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **PM PFAM; PF01047; MarR; 29; 133; T; 28-JAN-2000; **PM PRINTS; PR00598; HTHMARR; 47; 63; T; 28-JAN-2000; **PM PRINTS; PR00598; HTHMARR; 64; 79; T; 28-JAN-2000; **PM PRINTS; PR00598; HTHMARR; 83; 99; T; 28-JAN-2000; **PM PRINTS; PR00598; HTHMARR; 113; 133; T; 28-JAN-2000; **PM PROSITE; PS01117; HTH_MARR_FAMILY; 62; 96; T; 02-MAY-2000; SQ SEQUENCE 144 AA; 16448 MW; 4647F7704F2D78DE CRC64; MESPLGSDLA RLVRIWRALI DHRLKPLELT QTHWVTLHNI HQLPPDQSQI QLAKAIGIEQ PSLVRTLDQL EDKGLISRQT CASDRRAKRI KLTEKAEPLI AEMEEVIHKT RGEILAGISS EEIELLIKLV AKLEHNIMEL HSHD // ID FXR1_MOUSE PRELIMINARY; PRT; 677 AA. AC Q61584; Q9R1E2; Q9R1E3; Q9R1E4; Q9R1E5; Q9WUA7; Q9WUA8; Q9WUA9; DT 01-JUL-1997 (TrEMBLrel. 04, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-MAR-2001 (TrEMBLrel. 16, Last annotation update) DE Fragile X mental retardation syndrome related proteinase precursor domain - DE like protein. GN FXR1 OR FXR1H. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=010090; RN [1] RP SEQUENCE FROM N.A. (ISOFORM A). RC TISSUE=FETAL BRAIN; RX MEDLINE=96177651; PubMed=8634689; RA Coy J.F., Sedlacek Z., Baechner D., Hameister H., Joos S., Lichter P., RA Delius H., Poustka A.; RT "Highly conserved 3' UTR and expression pattern of FXR1 points to a RT divergent gene regulation of FXR1 and FMR1."; RL Hum. Mol. Genet. 4:2209-2218(1995). RN [2] RP SEQUENCE FROM N.A., ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX MEDLINE=99339984; PubMed=10409431; RA Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; RT "Alternative splicing in the murine and human FXR1 genes."; RL Genomics 59:193-202(1999). CC -!- FUNCTION: RNA-BINDING PROTEIN. INTERACTS WITH FMR1 AND FXR2 (BY CC SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=E; CC IsoId=Q61584-1; Sequence=Displayed; CC Name=A; CC IsoId=Q61584-2; Sequence=VSP_02391, VSP_02393, VSP_02395; CC Name=B; CC IsoId=Q61584-3; Sequence=VSP_02393; CC Name=C; CC IsoId=Q61584-4; Sequence=VSP_02394; CC Name=D; CC IsoId=Q61584-5; Sequence=VSP_02391, VSP_02394; CC Name=F; CC IsoId=Q61584-6; Sequence=VSP_02391; CC Name=G; CC IsoId=Q61584-7; Sequence=VSP_02392; CC -!- TISSUE SPECIFICITY: IN EARLY EMBRYOGENESIS, HIGHEST EXPRESSION IN CC SOMITES AND CENTRAL NERVOUS SYSTEM. ALSO EXPRESSED IN SPINAL CORD, CC SURROUNDING MESENCHYMAL TISSUE AND UNDIFFERENTIATED GONAD. IN MID- CC EMBRYOGENESIS, MOST PROMINENT IN GONAD AND MUSCLE TISSUE. ALSO CC EXPRESSED IN LIVER, RETINA, TELENCEPHALON AND MESENCEPHALON. IN CC LATE EMBRYOGENESIS, RESTRICTED TO SKELETAL MUSCLE AND CC PROLIFERATIVE ACTIVE LAYERS OF BRAIN. AFTER BIRTH, HIGHLY CC EXPRESSED IN POSTMEIOTIC SPERMATIDS. INTERMEDIATE LEVELS ARE FOUND CC IN HEART, LIVER AND KIDNEY WITH LOWER LEVELS IN BRAIN AND SKELETAL CC MUSCLE. CC -!- SIMILARITY: BELONGS TO THE FMR1 FAMILY. DR EMBL; X90875; CAA62383.1; -. DR EMBL; AF124385; AAD30211.1; -. DR EMBL; AF124394; AAD30212.1; -. DR EMBL; AF124386; AAD30212.1; JOINED. DR EMBL; AF124387; AAD30212.1; JOINED. DR EMBL; AF124388; AAD30212.1; JOINED. DR EMBL; AF124389; AAD30212.1; JOINED. DR EMBL; AF124390; AAD30212.1; JOINED. DR EMBL; AF124391; AAD30212.1; JOINED. DR EMBL; AF124392; AAD30212.1; JOINED. DR EMBL; AF124393; AAD30212.1; JOINED. DR EMBL; AF124394; AAD30213.1; -. DR EMBL; AF124386; AAD30213.1; JOINED. DR EMBL; AF124387; AAD30213.1; JOINED. DR EMBL; AF124388; AAD30213.1; JOINED. DR EMBL; AF124389; AAD30213.1; JOINED. DR EMBL; AF124390; AAD30213.1; JOINED. DR EMBL; AF124391; AAD30213.1; JOINED. DR EMBL; AF124392; AAD30213.1; JOINED. DR EMBL; AF124393; AAD30213.1; JOINED. DR EMBL; AF124394; AAD30214.1; -. DR EMBL; AF124386; AAD30214.1; JOINED. DR EMBL; AF124387; AAD30214.1; JOINED. DR EMBL; AF124388; AAD30214.1; JOINED. DR EMBL; AF124389; AAD30214.1; JOINED. DR EMBL; AF124390; AAD30214.1; JOINED. DR EMBL; AF124391; AAD30214.1; JOINED. DR EMBL; AF124392; AAD30214.1; JOINED. DR EMBL; AF124393; AAD30214.1; JOINED. DR EMBL; AF124394; AAD30215.1; -. DR EMBL; AF124386; AAD30215.1; JOINED. DR EMBL; AF124387; AAD30215.1; JOINED. DR EMBL; AF124388; AAD30215.1; JOINED. DR EMBL; AF124389; AAD30215.1; JOINED. DR EMBL; AF124390; AAD30215.1; JOINED. DR EMBL; AF124391; AAD30215.1; JOINED. DR EMBL; AF124392; AAD30215.1; JOINED. DR EMBL; AF124393; AAD30215.1; JOINED. DR EMBL; AF124394; AAD30216.1; -. DR EMBL; AF124386; AAD30216.1; JOINED. DR EMBL; AF124387; AAD30216.1; JOINED. DR EMBL; AF124388; AAD30216.1; JOINED. DR EMBL; AF124389; AAD30216.1; JOINED. DR EMBL; AF124390; AAD30216.1; JOINED. DR EMBL; AF124391; AAD30216.1; JOINED. DR EMBL; AF124392; AAD30216.1; JOINED. DR EMBL; AF124393; AAD30216.1; JOINED. DR EMBL; AF124394; AAD30217.1; -. DR EMBL; AF124386; AAD30217.1; JOINED. DR EMBL; AF124387; AAD30217.1; JOINED. DR EMBL; AF124388; AAD30217.1; JOINED. DR EMBL; AF124389; AAD30217.1; JOINED. DR EMBL; AF124390; AAD30217.1; JOINED. DR EMBL; AF124391; AAD30217.1; JOINED. DR EMBL; AF124392; AAD30217.1; JOINED. DR EMBL; AF124393; AAD30217.1; JOINED. DR EMBL; AF124394; AAD30218.1; -. DR EMBL; AF124386; AAD30218.1; JOINED. DR EMBL; AF124387; AAD30218.1; JOINED. DR EMBL; AF124388; AAD30218.1; JOINED. DR EMBL; AF124389; AAD30218.1; JOINED. DR EMBL; AF124390; AAD30218.1; JOINED. DR EMBL; AF124391; AAD30218.1; JOINED. DR EMBL; AF124392; AAD30218.1; JOINED. DR EMBL; AF124393; AAD30218.1; JOINED. DR HSSP; Q06787; 2FMR.{EI1} DR MGI; MGI:104860; Fxr1h.{EI2} DR INTERPRO; IPR000958; -. DR PFAM; PF00013; KH-domain; 2. KW Alternative splicing; RNA-binding; Repeat. FT COMPBIAS 50 53 POLY-PRO. FT DOMAIN 222 251 KH. FT DOMAIN 285 314 KH. FT DOMAIN 471 490 RNA-BINDING (RGG-BOX). FT COMPBIAS 531 539 POLY-ARG. FT VAR_SEQ 380 408 Missing (in isoform A, isoform D and FT isoform F). FT /FTId=VSP_02391. FT VAR_SEQ 430 455 Missing (in isoform G). FT /FTId=VSP_02392. FT VAR_SEQ 564 568 DDSEK -> GKRCD (in isoform A and isoform FT B). FT /FTId=VSP_02393. FT VAR_SEQ 564 590 Missing (in isoform C and isoform D). FT /FTId=VSP_02394. FT VAR_SEQ 569 677 Missing (in isoform A). FT /FTId=VSP_02395. FT VARIANT 79 79 R -> C (IN FT TOURS/ALGER/AMIENS/TOYAMA/PARIS-1/PARIS- FT 2/PADUA-2/BARCELONA-2/KUMAMOTO; LACKS FT HEPARIN-BINDING ABILITY). FT /FTId=VAR_007037. FT VARIANT 425 425 R -> CDCDCDDCDDCDCDDCDDCDCDCDCDCD FT CDDCDDCCDCDCDCD (IN FT A STRAIN). FT CONFLICT 425 425 Missing. FT CONFLICT 425 425 R -> CDCDCDDCDDCDCDDCDDCDCDCDCDCD FT CDDCDDCCDCDCDCD (IN FT A STRAIN). FT CONFLICT 425 425 RRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRRR FT -> C. FT VARIANT 425 425 R -> C (IN NORTHWICK/MILANO/ FT FRANKFURT/COPENHAGEN/LONDON; TYPE-II). FT /FTId=VAR_007075. FT VARIANT 425 425 R -> C (IN NORTHWICK/MILANO/ FT FRANKFURT123/COPENHAGEN/LONDON; TYPE-II). FT VARIANT 425 425 R -> C (IN NORTHWICK/MILANO/ FT FRANKFURT1234/COPENHAGEN/LONDON; TYPE-II). FT VARIANT 23 23 R -> H (IN LILLE/TAIPEI/VARESE/KOMAGOME- FT 3). FT VARIANT 608 608 Missing (in NPD type B; prevalent among FT NPD type B patients from the FT North-African Maghreb region). FT /FTId=VAR_005068. ** ** ################# SOURCE SECTION ################## ** M.musculus mRNA for FXR1 protein ** [1] ** Coy J.F., Sedlacek Z., Baechner D., Hameister H., Joos S., Lichter P., ** Delius H., Poustka A.; ** "Highly conserved 3' UTR and expression pattern of FXR1 points to a ** divergent gene regulation of FXR1 and FMR1"; ** Hum. Mol. Genet. 4:2209-2218(1995). ** [2] ** 1-2060 ** Coy J.F.; ** ; ** Submitted (14-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** J.F. Coy, DKFZ-Heidelberg, Molekulare Genomanalyse, Im Neuenheimer ** Feld ** 280, 69120 Heidelberg, FRG ** MGD; MGI:104860; Fxr1h. ** [1] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative Splicing in the Murine and Human FXR1 Genes"; ** Genomics 0:0-0(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** source 1..2060 ** /organism="Mus musculus" ** CDS 14..1633 ** /db_xref="PID:e196394" ** /db_xref="MGD:MGI:104860" ** /gene="FXR1" ** CDS_IN_EMBL_ENTRY 1 ** 08-DEC-1995 (Rel. 46, Last updated, Version 2) ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..347, ** AF124392.1:435..497,AF124393.1:391..594, ** AF124393.1:2679..2879,911..927) ** /codon_start=1 ** /db_xref="PID:g4835741" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform a" ** /protein_id="AAD30213.1" ** CDS_IN_EMBL_ENTRY 7 ** 17-MAY-1999 (Rel. 59, Last updated, Version 1) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** MEDLINE; 99339984. ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative splicing in the murine and human FXR1 genes"; ** Genomics 59(2):193-202(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, ** Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..347, ** AF124392.1:435..497,AF124393.1:391..594, ** AF124393.1:2679..2879,156..247,911..1081) ** /codon_start=1 ** /db_xref="PID:g4835744" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform d" ** /protein_id="AAD30216.1" ** CDS_IN_EMBL_ENTRY 7 ** 10-AUG-1999 (Rel. 60, Last updated, Version 2) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** MEDLINE; 99339984. ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative splicing in the murine and human FXR1 genes"; ** Genomics 59(2):193-202(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, ** Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..497, ** AF124393.1:391..594,AF124393.1:2679..2879,911..927) ** /codon_start=1 ** /db_xref="PID:g4835742" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform b" ** /protein_id="AAD30214.1" ** CDS_IN_EMBL_ENTRY 7 ** 10-AUG-1999 (Rel. 60, Last updated, Version 2) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** MEDLINE; 99339984. ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative splicing in the murine and human FXR1 genes"; ** Genomics 59(2):193-202(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, ** Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..347, ** AF124392.1:435..497,AF124393.1:391..594, ** AF124393.1:2679..2879,AF124393.1:3534..3614,156..247, ** 911..1081) ** /codon_start=1 ** /db_xref="PID:g4835745" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform f" ** /protein_id="AAD30217.1" ** CDS_IN_EMBL_ENTRY 7 ** 10-AUG-1999 (Rel. 60, Last updated, Version 2) ** Mus musculus fragile-X-related protein 1 (Fxr1h) mRNA, partial cds. ** [1] ** 1-1674 ** MEDLINE; 99339984. ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative splicing in the murine and human FXR1 genes"; ** Genomics 59(2):193-202(1999). ** [2] ** 1-1674 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (26-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor Plaza, ** Houston, TX 77030, USA ** source 1..1674 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** /strain="C57BL/6 x DBA" ** /clone="IMAGE:559877" ** CDS <1..1401 ** /codon_start=1 ** /db_xref="PID:g4835729" ** /note="FXR1" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1" ** /protein_id="AAD30211.1" ** CDS_IN_EMBL_ENTRY 1 ** 10-AUG-1999 (Rel. 60, Last updated, Version 2) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative Splicing in the Murine and Human FXR1 Genes"; ** Genomics 0:0-0(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..497, ** AF124393.1:469..594,AF124393.1:2679..2879, ** AF124393.1:3534..3614,156..247,911..1081) ** /codon_start=1 ** /db_xref="PID:g4835746" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform g" ** /protein_id="AAD30218.1" ** CDS_IN_EMBL_ENTRY 7 ** 17-MAY-1999 (Rel. 59, Last updated, Version 1) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative Splicing in the Murine and Human FXR1 Genes"; ** Genomics 0:0-0(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..497, ** AF124393.1:391..594,AF124393.1:2679..2879,156..247, ** 911..1081) ** /codon_start=1 ** /db_xref="PID:g4835743" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform c" ** /protein_id="AAD30215.1" ** CDS_IN_EMBL_ENTRY 7 ** 17-MAY-1999 (Rel. 59, Last updated, Version 1) ** Mus musculus fragile-X-related protein 1 (Fxr1h) gene, exons 16 and ** 17, alternative splice products, complete cds. ** [1] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** "Alternative Splicing in the Murine and Human FXR1 Genes"; ** Genomics 0:0-0(1999). ** [2] ** 1-1200 ** Kirkpatrick L.L., McIlwain K.A., Nelson D.L.; ** ; ** Submitted (28-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** Molecular & Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** source 1..1200 ** /db_xref="taxon:10090" ** /organism="Mus musculus" ** CDS join(AF124386.1:971..1021,AF124387.1:387..439, ** AF124387.1:1926..2019,AF124388.1:641..712, ** AF124388.1:1046..1194,AF124388.1:1575..1668, ** AF124388.1:2247..2363,AF124389.1:433..603, ** AF124389.1:1355..1433,AF124390.1:422..531, ** AF124391.1:187..273,AF124392.1:290..497, ** AF124393.1:391..594,AF124393.1:2679..2879, ** AF124393.1:3534..3614,156..247,911..1081) ** /codon_start=1 ** /db_xref="PID:g4835740" ** /note="FXR1" ** /gene="Fxr1h" ** /product="fragile-X-related protein 1 isoform e" ** /protein_id="AAD30212.1" ** CDS_IN_EMBL_ENTRY 7 ** 17-MAY-1999 (Rel. 59, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **EV EI1; HSSP_ADD; Q06787; 29-SEP-2000. **EV EI2; MGD_ADD; MGI:104860; 29-SEP-2000. **ID XXXX_MOUSE **PM PFAM; PF00013; KH-domain; 222; 269; T; 02-FEB-2000; **PM PFAM; PF00013; KH-domain; 285; 334; T; 02-FEB-2000; **TT Test case. Wrongly positioned ** line. **PM PROSITE; PS50084; KH_DOMAIN; 218; 277; T; 28-JAN-2000; **PM PROSITE; PS50084; KH_DOMAIN; 281; 331; T; 28-JAN-2000; **ZZ CREATED AND FINISHED BY Serenella. **ZZ UPDATED BY Michele M. (10-NOV-2000). **ZZ Comment: MERGED 7 TREMBL ENTRIES TO THIS ONE. **ZZ CURATED. SQ SEQUENCE 677 AA; 76222 MW; 908104FC95431A11 CRC64; MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN IQQARKVPGV TAIELDEDTG TFRIYGESAE AVKKARGFLE FVEDFIQVPR NLVGKVIGKN GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE VEQLRMERLQ IDEQLRQIGM GFRPSSTRGP EREKGYATDE STVSSVQGSR SYSGRGRGRR GPNYTSGYGT NSELSNPSET ESERKDELSD WSLAGEDDRE TRHQRDSRRR PGGRGRSVSG GRGRGGPRGG KSSISSVLKD PDSNPYSLLD NTESDQTADT DASESHHSTN RRRRSRRRRT DEDAVLMDGL TESDTASVNE NGLDDSEKKP QRRNRSRRRR FRGQAEDRQP VTVADYISRA ESQSRQRNLP RETLAKNKKE MAKDVIEEHG PSEKAINGPT SASGDEIPKL PRTLGEEKTK TLKEDSTQEA AVLNGVS // ID AATM_RABIT STANDARD; PRT; 30 AA. AC P12345; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Aspartate aminotransferase, mitochondrial (EC 2.6.1.1) (Transaminase DE A) (Glutamate oxaloacetate transaminase-2) (Fragment). GN GOT2. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE. RC TISSUE=Liver; RX MEDLINE=85289123; PubMed=4030726; RA Kuramitsu S., Inoue K., Kondo K., Aki K., Kagamiyama H.; RT "Aspartate aminotransferase isozymes from rabbit liver. Purification RT and properties."; RL J. Biochem. 97:1337-1345(1985). CC -!- CATALYTIC ACTIVITY: L-ASPARTATE + 2-OXOGLUTARATE = OXALOACETATE + CC L-GLUTAMATE. CC -!- CATALYTIC ACTIVITY: Catalyzes the reduction and hydrolysis of (1->6)-alpha-D-glucosidic CC linkages in pullulan and in amylopectin and glycogen, and the alpha- CC and beta-limit dextrins of amylopectin and glycogen. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- MISCELLANEOUS: IN EUKARYOTES THERE ARE TWO ISOZYMES: A CYTOPLASMIC CC ONE AND A MITOCHONDRIAL ONE. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR PIR; B27103; B27103. DR HSSP; P00508; 1TAT. DR InterPro; IPR001511; Aminotran_1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; PARTIAL. KW Transferase; Aminotransferase; Pyridoxal phosphate; Mitochondrion. FT NON_TER 30 30 ** ################# INTERNAL SECTION ################## SQ SEQUENCE 30 AA; 3401 MW; 410321530B95B673 CRC64; SSWWAHVEMG PPDPILGVTE AYKRDTNSKK // ID AATM_RABIT STANDARD; PRT; 30 AA. AC P12345; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Aspartate aminotransferase, mitochondrial (EC 2.6.1.1) (Transaminase A) (Glutamate oxaloacetate transaminase-2) (Fragment). GN abcdefghijklmnopqrstuvwx abcdefghijklmnopqrstuvwx OR abcdefghijkl mnOR A. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE. RC TISSUE=Liver; RX MEDLINE=85289123; PubMed=4030726; RA Kuramitsu S., Inoue K., Kondo K., Aki K., Kagamiyama H.; RT "Aspartate aminotransferase isozymes from rabbit liver. Purification RT and properties."; RL J. Biochem. 97:1337-1345(1985). FT NON_TER 30 30 ** ################# INTERNAL SECTION ################## SQ SEQUENCE 30 AA; 3401 MW; 410321530B95B673 CRC64; SSWWAHVEMG PPDPILGVTE AYKRDTNSKK // ID AATM_RABIT STANDARD; PRT; 30 AA. AC P12345; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE Aspartate aminotransferase, mitochondrial (EC 2.6.1.1) (Transaminase DE A) (Glutamate oxaloacetate transaminase-2) (Fragment). GN abcdefghijklmnopqrstuvwx OR abcdefghijklmnopqrstuvwxyzabcdefghikjlmn OR abcdefghijkl mnOR A. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE. RC TISSUE=Liver; RX MEDLINE=85289123; PubMed=4030726; RA Kuramitsu S., Inoue K., Kondo K., Aki K., Kagamiyama H.; RT "Aspartate aminotransferase isozymes from rabbit liver. Purification RT and properties."; RL J. Biochem. 97:1337-1345(1985). CC -!- SIMILARITY: Contains 1 RING-type zinc finger. CC -!- SIMILARITY: Contains 4 C3H1-type zinc fingers. FT NON_TER 30 30 ** ################# INTERNAL SECTION ################## SQ SEQUENCE 30 AA; 3401 MW; 410321530B95B673 CRC64; SSWWAHVEMG PPDPILGVTE AYKRDTNSKK // ID COAT_BPSP STANDARD; PRT; 132 AA. AC P09673; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 01-FEB-1994 (Rel. 28, Last annotation update) DE Coat protein. OS Bacteriophage SP. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Leviviridae; OC Allolevivirus. OX NCBI_TaxID=12027, 10685; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88289362; PubMed=3399390; RA Hirashima A., Hirose T., Inayama S., Inokuchi Y., Jacobson A.B.; RT "Analysis of the complete nucleotide sequence of the group IV RNA RT coliphage SP."; RL Nucleic Acids Res. 16:6205-6221(1988). CC -!- FUNCTION: FORMS THE PHAGE SHELL; BINDS TO THE PHAGE RNA. DR EMBL; X07489; CAA30374.1; -. DR HSSP; P03615; 1QBE. DR InterPro; IPR002703; Levi_coat. DR Pfam; PF01819; Levi_coat; 1. KW Coat protein; RNA-binding. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 132 AA; 14129 MW; 50B1E6CC6AF0A254 CRC64; MAKLNQVTLS KIGKNGDQTL TLTPRGVNPT NGVASLSEAG AVPALEKRVT VSVAQPSRNR KNFKVQIKLQ NPTACTRDAC DPSVTRSAFA DVTLSFTSYS TDEERALIRT ELAALLADPL IVDAIDNLNP AY // ID X_WHV1 STANDARD; PRT; 141 AA. AC P03167; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Trans-activating protein X. GN X. OS Woodchuck hepatitis virus 1 (WHV 1). OC Viruses; Retroid viruses; Hepadnaviridae; Orthohepadnavirus. OX NCBI_TaxID=10430; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=82216969; PubMed=7086958; RA Galibert F., Chen T.N., Mandart E.; RT "Nucleotide sequence of a cloned woodchuck hepatitis virus genome: RT comparison with the hepatitis B virus sequence."; RL J. Virol. 41:51-65(1982). DR EMBL; J02442; -; NOT_ANNOTATED_CDS. DR PIR; A03720; QQVLC1. DR InterPro; IPR000236; TransactX. DR Pfam; PF00739; X; 1. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 141 AA; 15221 MW; 4728019844561D85 CRC64; MAARLCCQLD PARDVLLLRP FGSQSSGPPF PRPSAGSAAS PASSLSASDE SDLPLGRLPA CFASASGPCC LVVTCAELRT MDSTVNFVSW HANRQLGMPS KDLWTPYIRD QLLTKWEEGS IDPRLSIFVL GGCRHKCMRL P // ID ROCKY_NICSY PRELIMINARY; PRT; 276 AA. AC P19682; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 28 kDa ribonucleoprotein, chloroplast precursor (28RNP). OS Nicotiana sylvestris (Wood tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4096; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 58-78. RC STRAIN=CV. BRIGHT YELLOW 4; RX MEDLINE=91005997; PubMed=1698606; RA Li Y., Sugiura M.; RT "Three distinct ribonucleoproteins from tobacco chloroplasts: each RT contains a unique amino terminal acidic domain and two RT ribonucleoprotein consensus motifs."; RL EMBO J. 9:3059-3066(1990). CC -!- FUNCTION: PROBABLY INVOLVED IN THE 3'END PROCESSING OF CHLOROPLAST CC MRNA'S. CC -!- SUBCELLULAR LOCATION: Chloroplast. CC -!- SIMILARITY: STRONG, TO PROTEIN X. CC -!- SIMILARITY: CONTAINS 2 RNA RECOGNITION MOTIFS (RRM). CC -!- SIMILARITY: CONTAINS 3 ABL DOMAINS. CC -!- SIMILARITY: IN THE CENTRAL SECTION; BELONGS TO THE RRM FAMILY. DR EMBL; X53933; CAA37880.1; -. DR PIR; S12109; S12109. DR HSSP; P09651; 1UP1. DR InterPro; IPR000504; RRM. DR Pfam; PF00076; rrm; 2. DR SMART; SM00360; RRM; 2. DR PROSITE; PS50102; RRM; 2. DR PROSITE; PS00030; RRM_RNP_1; 2. KW RNA-binding; Ribonucleoprotein; Repeat; mRNA processing; Chloroplast; KW Transit peptide. FT TRANSIT 1 57 CHLOROPLAST. FT CHAIN 58 276 28 kDa RIBONUCLEOPROTEIN. FT COMPBIAS 58 96 ASP/GLU-RICH (ACIDIC). FT COMPBIAS 92 100 ASP/GLU-RICH (ACIDIC). FT COMPBIAS 92 >100 ALA-RICH. FT COMPBIAS 80 85 COILED COIL. FT DOMAIN 97 175 RNA-BINDING (RRM) 1. FT DOMAIN 191 269 RNA-BINDING (RRM) 2. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 276 AA; 30699 MW; 48FF3DED534133BA CRC64; MATNGCLISL PPFFTTTKSI SSYPFLSTQL KPISLSSSLP TLLSLNKRTT QFPTFVSVLS EDDNTLVLDD QEQGGDFPSF VGEAGETEEY QEPSEDAKLF VGNLPYDIDS EGLAQLFQQA GVVEIAEVIY NRETDRSRGF GFVTMSTVEE ADKAVELYSQ YDLNGRLLTV NKAAPRGSRP ERAPRTFQPT YRIYVGNIPW DIDDARLEQV FSEHGKVVSA RVVFDRESGR SRGFGFVTMS SEAEMSEAIA NLDGQTLDGR TIRVNAAEER PRRNTY // ID CA54_HUMAN STANDARD; PRT; 1685 AA. AC P29400; Q16126; Q16006; DT 01-DEC-1992 (Rel. 24, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Collagen alpha 5(IV) chain precursor. GN COL4A5. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94165049; PubMed=8120014; RA Zhou J., Leinonen A., Tryggvason K.; RT "Structure of the human type IV collagen COL4A5 gene."; RL J. Biol. Chem. 269:6608-6614(1994). RN [2] RP SEQUENCE OF 1-910 FROM N.A., AND VARIANT AS CYS-521. RC TISSUE=Liver, and Kidney; RX MEDLINE=92316923; PubMed=1352287; RA Zhou J., Hertz J.M., Leinonen A., Tryggvason K.; RT "Complete amino acid sequence of the human alpha 5 (IV) collagen RT chain and identification of a single-base mutation in exon 23 RT converting glycine 521 in the collagenous domain to cysteine in an RT Alport syndrome patient."; RL J. Biol. Chem. 267:12475-12481(1992). RN [3] RP SEQUENCE OF 85-1685 FROM N.A. RC TISSUE=Placenta; RX MEDLINE=90337990; PubMed=2380186; RA Pihlajaniemi T., Pohjolainen E.R., Myers J.C.; RT "Complete primary structure of the triple-helical region and the RT carboxyl-terminal domain of a new type IV collagen chain, alpha RT 5(IV)."; RL J. Biol. Chem. 265:13758-13766(1990). RN [4] RP SEQUENCE OF 924-1685 FROM N.A. RX MEDLINE=91169491; PubMed=2004755; RA Zhou J., Hostikka S.L., Chow L.T., Tryggvason K.; RT "Characterization of the 3' half of the human type IV collagen alpha RT 5 gene that is affected in the Alport syndrome."; RL Genomics 9:1-9(1991). RN [5] RP SEQUENCE OF 914-1685 FROM N.A. RX MEDLINE=90160375; PubMed=1689491; RA Hostikka S.L., Eddy R.L., Byers M.G., Hoeyhtyae M., Shows T.B., RA Tryggvason K.; RT "Identification of a distinct type IV collagen alpha chain with RT restricted kidney distribution and assignment of its gene to the RT locus of X chromosome-linked Alport syndrome."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1606-1610(1990). RN [6] RP SEQUENCE OF 1442-1471 FROM N.A. RX MEDLINE=90252791; PubMed=2339699; RA Myers J.C., Jones T.A., Pohjolainen E.R., Kadri A.S., Goddard A.D., RA Sheer D., Solomon E., Pihlajaniemi T.; RT "Molecular cloning of alpha 5(IV) collagen and assignment of the gene RT to the region of the X chromosome containing the Alport syndrome RT locus."; RL Am. J. Hum. Genet. 46:1024-1033(1990). RN [7] RP SEQUENCE OF 1-20 FROM N.A. RA Guo C., van Damme B., Vanrenterghem Y., Devriendt K., Cassiman J.-J., RA Marynen P.; RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases. RN [8] RP SEQUENCE OF 1258-1270 FROM N.A. (SPLICED FORM). RX MEDLINE=94133540; PubMed=8301933; RA Guo C., van Damme B., van Damme-Lombaerts R., van den Berghe H., RA Cassiman J.-J., Marynen P.; RT "Differential splicing of COL4A5 mRNA in kidney and white blood RT cells: a complex mutation in the COL4A5 gene of an Alport patient RT deletes the NC1 domain."; RL Kidney Int. 44:1316-1321(1993). RN [9] RP REVIEW ON VARIANTS. RX MEDLINE=97338662; PubMed=9195222; RA Lemmink H.H., Schroeder C.H., Monnens L.A.H., Smeets H.J.M.; RT "The clinical spectrum of type IV collagen mutations."; RL Hum. Mutat. 9:477-499(1997). RN [10] RP VARIANT AS SER-1564. RX MEDLINE=91169492; PubMed=1672282; RA Zhou J., Barker D.F., Hostikka S.L., Gregory M.C., Atkin C.L., RA Tryggvason K.; RT "Single base mutation in alpha 5(IV) collagen chain gene converting a RT conserved cysteine to serine in Alport syndrome."; RL Genomics 9:10-18(1991). RN [11] RP VARIANT AS ARG-325. RX MEDLINE=92303559; PubMed=1376965; RA Knebelmann B., Deschenes G., Gros F., Hors M.-C., Gruenfeld J.-P., RA Tryggvason K., Gubler M.-C., Antignac C.; RT "Substitution of arginine for glycine 325 in the collagen alpha 5 RT (IV) chain associated with X-linked Alport syndrome: characterization RT of the mutation by direct sequencing of PCR-amplified lymphoblast RT cDNA fragments."; RL Am. J. Hum. Genet. 51:135-142(1992). RN [12] RP VARIANT AS GLU-325. RX MEDLINE=93244772; PubMed=1363780; RA Renieri A., Seri M., Myers J.C., Pihlajaniemi T., Massella L., RA Rizzoni G.F., de Marchi M.; RT "De novo mutation in the COL4A5 gene converting glycine 325 to RT glutamic acid in Alport syndrome."; RL Hum. Mol. Genet. 1:127-129(1992). RN [13] RP VARIANTS AS THR-1517; SER-1538 AND GLN-1563. RX MEDLINE=94010948; PubMed=8406498; RA Lemmink H.L., Schroeder C.H., Brunner H.G., Nelen M.R., Zhou J., RA Tryggvason K., Haggsma-Schouten W.A.G., Roodvoets A.P., Rascher W., RA van Oost B.A., Smeets H.J.M.; RT "Identification of four novel mutations in the COL4A5 gene of RT patients with Alport syndrome."; RL Genomics 17:485-489(1993). RN [14] RP VARIANTS AS E-400;V-406;V-638;A-638;R-653;R-796;R-869;R-872 & C-1241. RX MEDLINE=95322976; PubMed=7599631; RA Boye E., Flinter F., Zhou J., Tryggvason K., Bobrow M., Harris A.; RT "Detection of 12 novel mutations in the collagenous domain of the RT COL4A5 gene in Alport syndrome patients."; RL Hum. Mutat. 5:197-204(1995). RN [15] RP VARIANT AS ARG-1649. RX MEDLINE=96213750; PubMed=8651292; RA Barker D.F., Pruchno C.J., Jiang X., Atkin C.L., Stone E.M., RA Denison J.C., Fain P.R., Gregory M.C.; RT "A mutation causing Alport syndrome with tardive hearing loss is RT common in the western United States."; RL Am. J. Hum. Genet. 58:1157-1165(1996). RN [16] RP VARIANTS AS. RX MEDLINE=96213754; PubMed=8651296; RA Renieri A., Bruttini M., Galli L., Zanelli P., Neri T.M., Rossetti S., RA Turco A.E., Heiskari N., Zhou J., Gusmano R., Massella L., Banfi G., RA Scolari F., Sessa A., Rizzoni G.F., Tryggvason K., Pignatti P.F., RA Savi M., Ballabio A., de Marchi M.; RT "X-linked Alport syndrome: an SSCP-based mutation survey over all 51 RT exons of the COL4A5 gene."; RL Am. J. Hum. Genet. 58:1192-1204(1996). RN [17] RP VARIANTS AS, AND VARIANTS ASP-430;SER-444;SER-619;ASN-664 & MET-1428. RX MEDLINE=97094179; PubMed=8940267; RA Knebelmann B., Breillat C., Forestier L., Arrondel C., Jacassier D., RA Giatras I., Drouot L., Deschenes G., Gruenfeld J.-P., Broyer M., RA Gubler M.-C., Antignac C.; RT "Spectrum of mutations in the COL4A5 collagen gene in X-linked Alport RT syndrome."; RL Am. J. Hum. Genet. 59:1221-1232(1996). RN [18] RP VARIANT AS ASP-1498. RX MEDLINE=96233932; PubMed=8829632; RA Tverskaya S., Bobrynina V., Tsalykova F., Ignatova M., RA Krasnopolskaya X., Evgrafov O.; RT "Substitution of A1498D in noncollagen domain of a5(IV) collagen RT chain associated with adult-onset X-linked Alport syndrome."; RL Hum. Mutat. 7:149-150(1996). RN [19] RP VARIANT AS GLN-1677. RX MEDLINE=97295089; PubMed=9150741; RA Barker D.F., Denison J.C., Atkin C.L., Gregory M.C.; RT "Common ancestry of three Ashkenazi-American families with Alport RT syndrome and COL4A5 R1677Q."; RL Hum. Genet. 99:681-684(1997). RN [20] RP VARIANTS AS R-174; R-177; R-325; C-1410; W-1421; T-1517 AND D-1596. RX MEDLINE=98112435; PubMed=9452056; RA Neri T.M., Zanelli P., de Palma G., Savi M., Rossetti S., Turco A.E., RA Pignatti G.F., Galli L., Bruttini M., Renieri A., Mingarelli R., RA Trivelli A., Pinciaroli A.R., Ragaiolo M., Rizzoni G.F., de Marchi M.; RT "Missense mutations in the COL4A5 gene in patients with X-linked RT Alport syndrome."; RL Hum. Mutat. Suppl. 1:S106-S109(1998). RN [21] RP VARIANTS AS. ** VARIANTS AS V-420; 456-P-G-P-458 DEL; D-573; D-624; D-635; 802-G--P- ** 807 DEL; R-869; C-941; S-1030; S-1066; D-1143; R-1196; E-1261; S-1357 ** AND R-1649. RX MEDLINE=99063529; PubMed=9848783; RA Martin P., Heiskari N., Zhou J., Leinonen A., Tumelius T., Hertz J.M., RA Barker D.F., Gregory M.C., Atkin C.L., Styrkarsdottir U., Neumann H., RA Springate J., Shows T.B., Pettersson E., Tryggvason K.; RT "High mutation detection rate in the COL4A5 collagen gene in suspected RT Alport syndrome using PCR and direct DNA sequencing."; RL J. Am. Soc. Nephrol. 9:2291-2301(1998). RN [22] RP VARIANTS AS GLU-579; LYS-633; ASP-947; VAL-953; ARG-1107; ARG-1158; RP SER-1170 AND TRP-1678, AND VARIANTS SER-444 AND ALA-739. RX MEDLINE=20030197; PubMed=10561141; RA Inoue Y., Nishio H., Shirakawa T., Nakanishi K., Nakamura H., RA Sumino K., Nishiyama K., Iijima K., Yoshikawa N.; RT "Detection of mutations in the COL4A5 gene in over 90% of male RT patients with X-linked Alport's syndrome by RT-PCR and direct RT sequencing."; RL Am. J. Kidney Dis. 34:854-862(1999). RN [23] RP VARIANT AS ARG-822. RX MEDLINE=20025011; PubMed=10563487; RA Cruz-Robles D., Garcia-Torres R., Antignac C., Forestier L., RA Garcia de la Puente S., Correa-Rotter R., Garcia-Lopez E., Orozco L.; RT "Three novel mutations in the COL4A5 gene in Mexican Alport syndrome RT patients."; RL Clin. Genet. 56:242-243(1999). RN [24] RP VARIANTS AS, AND VARIANTS. RX MEDLINE=99140256; PubMed=10094548; RA Plant K.E., Green P.M., Vetrie D., Flinter F.A.; RT "Detection of mutations in COL4A5 in patients with Alport syndrome."; RL Hum. Mutat. 13:124-132(1999). RN [25] RP VARIANT AS CYS-177. RX MEDLINE=20460632; PubMed=11004279; RA Blasi M.A., Rinaldi R., Renieri A., Petrucci R., De Bernardo C., RA Bruttini M., Grammatico P.; RT "Dot-and-fleck retinopathy in Alport syndrome caused by a novel RT mutation in the COL4A5 gene."; RL Am. J. Ophthalmol. 130:130-131(2000). RN [26] RP VARIANTS AS R-216; R-415; E-1045; D-1086; S-1167 AND 864-S--G-875 DEL. RX MEDLINE=20321306; PubMed=10862091; RA Martin P., Heiskari N., Pajari H., Groenhagen-Riska C., RA Kaeaeriaeinen H., Koskimies O., Tryggvason K.; RT "Spectrum of COL4A5 mutations in Finnish Alport syndrome patients."; RL Hum. Mutat. 15:579-579(2000). RN [27] RP VARIANTS AS ARG-319;SER-739;VAL-902;GLU-911;ASP-1229 AND HIS-1511. RX MEDLINE=20148403; PubMed=10684360; RA Cheong H.I., Park H.W., Ha I.S., Choi Y.; RT "Mutational analysis of COL4A5 gene in Korean Alport syndrome."; RL Pediatr. Nephrol. 14:117-121(2000). RN [28] RP VARIANTS AS R-192; R-292; D-295; R-325; R-558; V- RP 603; D-624; D-629; RP E-722; V-898; A-1006; V-1006; D-1244; R-1649 AND P-1677, AND VARIANT S-444. RX MEDLINE=21123908; PubMed=11223851; RA Barker D.F., Denison J.C., Atkin C.L., Gregory M.C.; RT "Efficient detection of Alport syndrome COL4A5 mutations with RT multiplex genomic PCR-SSCP."; RL Am. J. Med. Genet. 98:148-160(2001). CC -!- FUNCTION: TYPE IV COLLAGEN IS THE MAJOR STRUCTURAL COMPONENT OF CC GLOMERULAR BASEMENT MEMBRANES (GBM), FORMING A 'CHICKEN-WIRE' CC MESHWORK TOGETHER WITH LAMININS, PROTEOGLYCANS AND ENTACTIN/ CC NIDOGEN. CC -!- SUBUNIT: THERE ARE SIX TYPE IV COLLAGEN ISOFORMS, ALPHA 1(IV)- CC ALPHA 6(IV), EACH OF WHICH CAN FORM A TRIPLE HELIX STRUCTURE CC WITH 2 OTHER CHAINS TO GENERATE TYPE IV COLLAGEN NETWORK. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P29400-1; Sequence=Displayed; CC Name=2; CC IsoId=P29400-2; Sequence=VSP_00759; CC Note=Longer found in kidney, in which 2 extra G-X-X repeats into CC the triple-helix domain are introduced; CC -!- DOMAIN: ALPHA CHAINS OF TYPE IV COLLAGEN HAVE A NONCOLLAGENOUS CC DOMAIN (NC1) AT THEIR C-TERMINUS, FREQUENT INTERRUPTIONS OF THE CC G-X-Y REPEATS IN THE LONG CENTRAL TRIPLE-HELICAL DOMAIN (WHICH MAY CC CAUSE FLEXIBILITY IN THE TRIPLE HELIX), AND A SHORT N-TERMINAL CC TRIPLE-HELICAL 7S DOMAIN. CC -!- PTM: PROLINES AT THE THIRD POSITION OF THE TRIPEPTIDE REPEATING CC UNIT (G-X-Y) ARE HYDROXYLATED IN SOME OR ALL OF THE CHAINS. CC -!- PTM: TYPE IV COLLAGENS CONTAIN NUMEROUS CYSTEINE RESIDUES WHICH CC ARE INVOLVED IN INTER- AND INTRAMOLECULAR DISULFIDE BONDING. 12 OF CC THESE, LOCATED IN THE NC1 DOMAIN, ARE CONSERVED IN ALL KNOWN TYPE CC IV COLLAGENS. CC -!- DISEASE: DEFECTS IN COL4A5 ARE A CAUSE OF X-LINKED ALPORT SYNDROME CC (AS). ALPORT SYNDROME IS CHARACTERIZED BY PROGRESSIVE CC GLOMERULONEPHRITIS, OFTEN ASSOCIATED WITH HIGH-TONE SENSORINEURAL CC DEAFNESS, SPECIFIC EYE ABNORMALITIES (LENTICONOUS AND MACULAR CC FLECKS), AND GLOMERULAR BASEMENT MEMBRANE DEFECTS. IN MALES, THE CC TYPICAL TIME COURSE FOR THE PROGRESS OF ALPORT SYNDROME IS: CC HEMATURIA BY THE AGE OF 5 YEARS, DEAFNESS AND HYPERTENSION IN CC EARLY TEENAGE LIFE, DETERIORATION OF RENAL FUNCTION BY AGE 20, AND CC END-STAGE RENAL FAILURE SOON THEREAFTER. FEMALES TEND TO FOLLOW A CC MUCH MILDER COURSE AND RARELY GO INTO RENAL FAILURE. DR EMBL; M58526; AAA99480.1; -. DR EMBL; M90464; AAA52046.1; -. DR EMBL; U04520; AAC27816.1; -. DR EMBL; U04470; AAC27816.1; JOINED. DR EMBL; U04471; AAC27816.1; JOINED. DR EMBL; U04472; AAC27816.1; JOINED. DR EMBL; U04473; AAC27816.1; JOINED. DR EMBL; U04474; AAC27816.1; JOINED. DR EMBL; U04476; AAC27816.1; JOINED. DR EMBL; U04477; AAC27816.1; JOINED. DR EMBL; U04478; AAC27816.1; JOINED. DR EMBL; U04479; AAC27816.1; JOINED. DR EMBL; U04480; AAC27816.1; JOINED. DR EMBL; U04483; AAC27816.1; JOINED. DR EMBL; U04485; AAC27816.1; JOINED. DR EMBL; U04486; AAC27816.1; JOINED. DR EMBL; U04487; AAC27816.1; JOINED. DR EMBL; U04488; AAC27816.1; JOINED. DR EMBL; U04489; AAC27816.1; JOINED. DR EMBL; U04490; AAC27816.1; JOINED. DR EMBL; U04491; AAC27816.1; JOINED. DR EMBL; U04492; AAC27816.1; JOINED. DR EMBL; U04493; AAC27816.1; JOINED. DR EMBL; U04494; AAC27816.1; JOINED. DR EMBL; U04495; AAC27816.1; JOINED. DR EMBL; U04496; AAC27816.1; JOINED. DR EMBL; U04497; AAC27816.1; JOINED. DR EMBL; U04498; AAC27816.1; JOINED. DR EMBL; U04499; AAC27816.1; JOINED. DR EMBL; U04500; AAC27816.1; JOINED. DR EMBL; U04501; AAC27816.1; JOINED. DR EMBL; U04502; AAC27816.1; JOINED. DR EMBL; U04503; AAC27816.1; JOINED. DR EMBL; U04504; AAC27816.1; JOINED. DR EMBL; U04505; AAC27816.1; JOINED. DR EMBL; U04506; AAC27816.1; JOINED. DR EMBL; U04507; AAC27816.1; JOINED. DR EMBL; U04508; AAC27816.1; JOINED. DR EMBL; U04509; AAC27816.1; JOINED. DR EMBL; U04510; AAC27816.1; JOINED. DR EMBL; U04511; AAC27816.1; JOINED. DR EMBL; U04512; AAC27816.1; JOINED. DR EMBL; U04514; AAC27816.1; JOINED. DR EMBL; U04515; AAC27816.1; JOINED. DR EMBL; U04516; AAC27816.1; JOINED. DR EMBL; U04517; AAC27816.1; JOINED. DR EMBL; U04518; AAC27816.1; JOINED. DR EMBL; U04519; AAC27816.1; JOINED. DR EMBL; U04520; AAF66217.2; -. DR EMBL; U04470; AAF66217.2; JOINED. DR EMBL; U04471; AAF66217.2; JOINED. DR EMBL; U04472; AAF66217.2; JOINED. DR EMBL; U04473; AAF66217.2; JOINED. DR EMBL; U04474; AAF66217.2; JOINED. DR EMBL; U04476; AAF66217.2; JOINED. DR EMBL; U04477; AAF66217.2; JOINED. DR EMBL; U04478; AAF66217.2; JOINED. DR EMBL; U04479; AAF66217.2; JOINED. DR EMBL; U04480; AAF66217.2; JOINED. DR EMBL; U04483; AAF66217.2; JOINED. DR EMBL; U04485; AAF66217.2; JOINED. DR EMBL; U04486; AAF66217.2; JOINED. DR EMBL; U04487; AAF66217.2; JOINED. DR EMBL; U04488; AAF66217.2; JOINED. DR EMBL; U04489; AAF66217.2; JOINED. DR EMBL; U04490; AAF66217.2; JOINED. DR EMBL; U04491; AAF66217.2; JOINED. DR EMBL; U04492; AAF66217.2; JOINED. DR EMBL; U04493; AAF66217.2; JOINED. DR EMBL; U04494; AAF66217.2; JOINED. DR EMBL; U04495; AAF66217.2; JOINED. DR EMBL; U04496; AAF66217.2; JOINED. DR EMBL; U04497; AAF66217.2; JOINED. DR EMBL; U04498; AAF66217.2; JOINED. DR EMBL; U04499; AAF66217.2; JOINED. DR EMBL; U04500; AAF66217.2; JOINED. DR EMBL; U04501; AAF66217.2; JOINED. DR EMBL; U04502; AAF66217.2; JOINED. DR EMBL; U04503; AAF66217.2; JOINED. DR EMBL; U04504; AAF66217.2; JOINED. DR EMBL; U04505; AAF66217.2; JOINED. DR EMBL; U04506; AAF66217.2; JOINED. DR EMBL; U04507; AAF66217.2; JOINED. DR EMBL; U04508; AAF66217.2; JOINED. DR EMBL; U04509; AAF66217.2; JOINED. DR EMBL; U04510; AAF66217.2; JOINED. DR EMBL; AF199451; AAF66217.2; JOINED. DR EMBL; AF199452; AAF66217.2; JOINED. DR EMBL; U04511; AAF66217.2; JOINED. DR EMBL; U04512; AAF66217.2; JOINED. DR EMBL; U04514; AAF66217.2; JOINED. DR EMBL; U04515; AAF66217.2; JOINED. DR EMBL; U04516; AAF66217.2; JOINED. DR EMBL; U04517; AAF66217.2; JOINED. DR EMBL; U04518; AAF66217.2; JOINED. DR EMBL; U04519; AAF66217.2; JOINED. DR EMBL; M63473; AAA51558.1; -. DR EMBL; M63455; AAA51558.1; JOINED. DR EMBL; M63456; AAA51558.1; JOINED. DR EMBL; M63457; AAA51558.1; JOINED. DR EMBL; M63458; AAA51558.1; JOINED. DR EMBL; M63459; AAA51558.1; JOINED. DR EMBL; M63460; AAA51558.1; JOINED. DR EMBL; M63461; AAA51558.1; JOINED. DR EMBL; M63462; AAA51558.1; JOINED. DR EMBL; M63463; AAA51558.1; JOINED. DR EMBL; M63464; AAA51558.1; JOINED. DR EMBL; M63465; AAA51558.1; JOINED. DR EMBL; M63466; AAA51558.1; JOINED. DR EMBL; M63467; AAA51558.1; JOINED. DR EMBL; M63468; AAA51558.1; JOINED. DR EMBL; M63470; AAA51558.1; JOINED. DR EMBL; M63471; AAA51558.1; JOINED. DR EMBL; M63472; AAA51558.1; JOINED. DR EMBL; M31115; AAA52045.1; -. DR EMBL; Z37153; CAA85512.1; -. DR EMBL; S69168; AAC60612.1; -. DR EMBL; S59334; AAD13909.1; -. DR PIR; S22917; S22917. DR MIM; 303630; -. DR MIM; 301050; -. DR InterPro; IPR001442; C4. DR InterPro; IPR000087; Collagen. DR Pfam; PF01413; C4; 2. DR Pfam; PF01391; Collagen; 21. DR ProDom; PD003923; C4; 2. DR SMART; SM00111; C4; 2. KW Extracellular matrix; Connective tissue; Basement membrane; KW Repeat; Hydroxylation; Collagen; Signal; Disease mutation; KW Polymorphism; Alternative splicing; Alport syndrome. FT SIGNAL 1 26 POTENTIAL. FT CHAIN 27 1685 COLLAGEN ALPHA 5(IV) CHAIN. FT DOMAIN 27 41 NONHELICAL REGION (NC2). FT DOMAIN 42 1456 TRIPLE-HELICAL REGION. FT DOMAIN 1457 1685 NONHELICAL REGION (NC1). FT DOMAIN 1457 1568 REPEAT NC1-1. FT DOMAIN 1569 1685 REPEAT NC1-2. FT DISULFID 451 451 INTERCHAIN (POTENTIAL). FT DISULFID 481 481 INTERCHAIN (POTENTIAL). FT DISULFID 484 484 INTERCHAIN (POTENTIAL). FT DISULFID 1476 1567 OR 1564 (BY SIMILARITY). FT DISULFID 1509 1564 OR 1567 (BY SIMILARITY). FT DISULFID 1521 1527 BY SIMILARITY. FT DISULFID 1586 1681 OR 1678 (BY SIMILARITY). FT DISULFID 1620 1678 OR 1681 (BY SIMILARITY). FT DISULFID 1632 1638 BY SIMILARITY. FT CARBOHYD 125 125 N-LINKED (GLCNAC...) (POTENTIAL). FT VAR_SEQ 1264 1264 G -> GPTGFQG (in isoform 2). FT /FTId=VSP_00759. FT VARIANT 54 54 G -> D (IN AS; ADULT TYPE). FT /FTId=VAR_001914. FT VARIANT 114 114 G -> S (IN AS). FT /FTId=VAR_007991. FT VARIANT 129 129 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_001915. FT VARIANT 129 129 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_001916. FT VARIANT 174 174 G -> R (IN AS). FT /FTId=VAR_001917. FT VARIANT 177 177 G -> C (IN AS WITH DOT-AND-FLECK FT RETINOPATHY). FT /FTId=VAR_011220. FT VARIANT 177 177 G -> R (IN AS; ADULT TYPE). FT /FTId=VAR_001918. FT VARIANT 192 192 G -> R (IN AS). FT /FTId=VAR_011221. FT VARIANT 204 204 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_011222. FT VARIANT 216 216 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_001919. FT VARIANT 219 219 G -> S (IN AS). FT /FTId=VAR_001920. FT VARIANT 230 230 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_011223. FT VARIANT 239 239 G -> E (IN AS). FT /FTId=VAR_011224. FT VARIANT 264 264 G -> R (IN AS; ADULT TYPE). FT /FTId=VAR_011225. FT VARIANT 289 289 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_001921. FT VARIANT 292 292 G -> R (IN AS). FT /FTId=VAR_011226. FT VARIANT 292 292 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_001922. FT VARIANT 295 295 G -> D (IN AS). FT /FTId=VAR_011227. FT VARIANT 298 298 G -> S (IN AS). FT /FTId=VAR_011228. FT VARIANT 319 319 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_011229. FT VARIANT 325 325 G -> E (IN AS). FT /FTId=VAR_001923. FT VARIANT 325 325 G -> R (IN AS; JUVENILE AND ADULT TYPES). FT /FTId=VAR_001924. FT VARIANT 331 331 G -> V (IN AS). FT /FTId=VAR_007992. FT VARIANT 365 365 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_001925. FT VARIANT 365 367 MISSING (IN AS; JUVENILE TYPE). FT /FTId=VAR_001926. FT VARIANT 371 371 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_001927. FT VARIANT 374 374 G -> A (IN AS). FT /FTId=VAR_001928. FT VARIANT 383 383 G -> D (IN AS; JUVENILE TYPE). FT /FTId=VAR_001929. FT VARIANT 400 400 G -> E (IN AS; ADULT TYPE). FT /FTId=VAR_001930. FT VARIANT 406 406 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_001931. FT VARIANT 409 409 G -> D (IN AS). FT /FTId=VAR_001932. FT VARIANT 412 412 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_011230. FT VARIANT 415 415 G -> R (IN AS). FT /FTId=VAR_011231. FT VARIANT 420 420 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_011232. FT VARIANT 420 420 G -> V (IN AS). FT /FTId=VAR_011233. FT VARIANT 423 423 G -> E (IN AS). FT /FTId=VAR_011234. FT VARIANT 430 430 A -> D. FT /FTId=VAR_001933. FT VARIANT 444 444 I -> S. FT /FTId=VAR_001934. FT VARIANT 456 458 MISSING (IN AS). FT /FTId=VAR_001935. FT VARIANT 466 466 G -> E (IN AS). FT /FTId=VAR_001936. FT VARIANT 472 472 G -> R (IN AS). FT /FTId=VAR_007993. FT VARIANT 491 491 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_011235. FT VARIANT 494 494 G -> D (IN AS; ADULT TYPE). FT /FTId=VAR_001937. FT VARIANT 496 507 MISSING (IN AS; JUVENILE TYPE). FT /FTId=VAR_001938. FT VARIANT 497 497 G -> C (IN AS; ADULT TYPE). FT /FTId=VAR_011236. FT VARIANT 521 521 G -> C (IN AS). FT /FTId=VAR_001939. FT VARIANT 521 521 G -> S (IN AS). FT /FTId=VAR_001940. FT VARIANT 524 524 G -> D (IN AS; ADULT TYPE). FT /FTId=VAR_011237. FT VARIANT 545 545 G -> R (IN AS). FT /FTId=VAR_007994. FT VARIANT 545 545 G -> V (IN AS). FT /FTId=VAR_007995. FT VARIANT 558 558 G -> R (IN AS). FT /FTId=VAR_011238. FT VARIANT 561 561 G -> R (IN AS). FT /FTId=VAR_007996. FT VARIANT 567 567 G -> A (IN AS; JUVENILE TYPE). FT /FTId=VAR_001941. FT VARIANT 573 573 G -> D (IN AS). FT /FTId=VAR_011239. FT VARIANT 579 579 G -> E (IN AS). FT /FTId=VAR_011240. FT VARIANT 579 579 G -> R (IN AS; ADULT TYPE). FT /FTId=VAR_007997. FT VARIANT 603 603 G -> V (IN AS). FT /FTId=VAR_011241. FT VARIANT 609 609 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_011242. FT VARIANT 609 609 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_001942. FT VARIANT 619 619 P -> S. FT /FTId=VAR_011243. FT VARIANT 621 621 G -> C (IN AS). FT /FTId=VAR_011244. FT VARIANT 624 624 G -> D (IN AS). FT /FTId=VAR_011245. FT VARIANT 629 629 G -> D (IN AS). FT /FTId=VAR_011246. FT VARIANT 632 632 G -> D (IN AS). FT /FTId=VAR_011247. FT VARIANT 633 633 E -> K (IN AS). FT /FTId=VAR_011248. FT VARIANT 635 635 G -> D (IN AS). FT /FTId=VAR_007998. FT VARIANT 638 638 G -> A (IN AS). FT /FTId=VAR_001944. FT VARIANT 638 638 G -> S (IN AS; JUVENILE TYPE). FT /FTId=VAR_007999. FT VARIANT 638 638 G -> V (IN AS). FT /FTId=VAR_001943. FT VARIANT 653 653 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_001945. FT VARIANT 664 664 K -> N. FT /FTId=VAR_001946. FT VARIANT 669 669 G -> A (IN AS; JUVENILE TYPE). FT /FTId=VAR_008000. FT VARIANT 681 681 G -> D (IN AS). FT /FTId=VAR_011249. FT VARIANT 684 684 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_001947. FT VARIANT 687 687 G -> E (IN AS). FT /FTId=VAR_008001. FT VARIANT 722 722 G -> E (IN AS). FT /FTId=VAR_011250. FT VARIANT 739 739 P -> A. FT /FTId=VAR_011251. FT VARIANT 739 739 P -> S (IN AS; JUVENILE TYPE). FT /FTId=VAR_011252. FT VARIANT 740 740 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_001948. FT VARIANT 743 743 G -> D (IN AS). FT /FTId=VAR_008002. FT VARIANT 772 772 G -> D (IN AS; JUVENILE TYPE). FT /FTId=VAR_001949. FT VARIANT 796 796 G -> R (IN AS). FT /FTId=VAR_001950. FT VARIANT 802 802 G -> R (IN AS). FT /FTId=VAR_011253. FT VARIANT 802 807 MISSING (IN AS). FT /FTId=VAR_011254. FT VARIANT 808 808 G -> E (IN AS; ADULT TYPE). FT /FTId=VAR_008003. FT VARIANT 811 811 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_011255. FT VARIANT 822 822 G -> R (IN AS). FT /FTId=VAR_011256. FT VARIANT 822 824 MISSING (IN AS). FT /FTId=VAR_008004. FT VARIANT 852 852 G -> E (IN AS; JUVENILE TYPE). FT /FTId=VAR_008005. FT VARIANT 852 852 G -> R (IN AS). FT /FTId=VAR_001951. FT VARIANT 864 875 MISSING (IN AS). FT /FTId=VAR_011257. FT VARIANT 866 866 G -> E (IN AS; ADULT TYPE). FT /FTId=VAR_001952. FT VARIANT 869 869 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_001953. FT VARIANT 872 872 G -> R (IN AS). FT /FTId=VAR_001954. FT VARIANT 878 878 G -> R (IN AS). FT /FTId=VAR_008006. FT VARIANT 898 898 M -> V (IN AS; MILD PHENOTYPE). FT /FTId=VAR_011258. FT VARIANT 902 902 G -> V (IN AS; JUVENILE TYPE). FT /FTId=VAR_011259. FT VARIANT 911 911 G -> E (IN AS). FT /FTId=VAR_011260. FT VARIANT 941 941 G -> C (IN AS). FT /FTId=VAR_011261. FT VARIANT 942 942 MISSING (IN AS). FT /FTId=VAR_001955. FT VARIANT 947 947 G -> D (IN AS). FT /FTId=VAR_011262. FT VARIANT 953 953 G -> V (IN AS; FOUND ON THE SAME ALLELE FT AS VARIANT E-1211). FT /FTId=VAR_011263. FT VARIANT 988 992 MISSING (IN AS; ADULT TYPE). FT /FTId=VAR_008007. FT VARIANT 1006 1006 G -> A (IN AS). FT /FTId=VAR_011264. FT VARIANT 1006 1006 G -> V (IN AS). FT /FTId=VAR_011265. FT VARIANT 1015 1015 G -> E (IN AS). FT /FTId=VAR_011266. FT VARIANT 1015 1015 G -> V (IN AS). FT /FTId=VAR_011267. FT VARIANT 1030 1030 G -> S (IN AS). FT /FTId=VAR_011268. FT VARIANT 1036 1036 G -> V (IN AS). FT /FTId=VAR_011269. FT VARIANT 1039 1039 G -> S (IN AS; JUVENILE TYPE). FT /FTId=VAR_011270. FT VARIANT 1045 1045 G -> E (IN AS). FT /FTId=VAR_011271. FT VARIANT 1066 1066 G -> R (IN AS). FT /FTId=VAR_011272. FT VARIANT 1066 1066 G -> S (IN AS). FT /FTId=VAR_011273. FT VARIANT 1086 1086 G -> D (IN AS). FT /FTId=VAR_011274. FT VARIANT 1104 1104 G -> V (IN AS). FT /FTId=VAR_001956. FT VARIANT 1107 1107 G -> R (IN AS). FT /FTId=VAR_008008. FT VARIANT 1143 1143 G -> D (IN AS; JUVENILE TYPE). FT /FTId=VAR_001957. FT VARIANT 1143 1143 G -> S (IN AS; ADULT TYPE). FT /FTId=VAR_001958. FT VARIANT 1158 1158 G -> R (IN AS). FT /FTId=VAR_011275. FT VARIANT 1161 1161 G -> R (IN AS). FT /FTId=VAR_008009. FT VARIANT 1167 1167 G -> S (IN AS). FT /FTId=VAR_011276. FT VARIANT 1170 1170 G -> S (IN AS). FT /FTId=VAR_011277. FT VARIANT 1182 1182 G -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_001959. FT VARIANT 1196 1196 G -> R (IN AS). FT /FTId=VAR_011278. FT VARIANT 1205 1205 G -> C (IN AS; JUVENILE TYPE). FT /FTId=VAR_011279. FT VARIANT 1211 1211 G -> E (IN AS; FOUND ON THE SAME ALLELE FT AS VARIANT V-953). FT /FTId=VAR_011280. FT VARIANT 1211 1211 G -> R (IN AS). FT /FTId=VAR_008010. FT VARIANT 1220 1220 G -> D (IN AS). FT /FTId=VAR_008011. FT VARIANT 1229 1229 G -> D (IN AS; ADULT TYPE). FT /FTId=VAR_011281. FT VARIANT 1241 1241 G -> C (IN AS). FT /FTId=VAR_001960. FT VARIANT 1244 1244 G -> D (IN AS). FT /FTId=VAR_011282. FT VARIANT 1252 1252 G -> S (IN AS; ADULT TYPE). FT /FTId=VAR_011283. FT VARIANT 1261 1261 G -> E (IN AS). FT /FTId=VAR_011284. FT VARIANT 1270 1270 G -> S (IN AS). FT /FTId=VAR_001961. FT VARIANT 1333 1333 G -> S (IN AS). FT /FTId=VAR_008012. FT VARIANT 1357 1357 G -> S (IN AS). FT /FTId=VAR_011285. FT VARIANT 1379 1379 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_001962. FT VARIANT 1410 1410 R -> C (IN AS; ADULT AND JUVENILE TYPES). FT /FTId=VAR_001963. FT VARIANT 1421 1421 G -> W (IN AS; ADULT TYPE). FT /FTId=VAR_001964. FT VARIANT 1422 1422 R -> C (IN AS; JUVENILE TYPE). FT /FTId=VAR_001965. FT VARIANT 1427 1427 G -> V (IN AS; ADULT TYPE). FT /FTId=VAR_008013. FT VARIANT 1428 1428 L -> M. FT /FTId=VAR_011286. FT VARIANT 1442 1442 G -> D (IN AS). FT /FTId=VAR_008014. FT VARIANT 1451 1451 G -> S (IN AS). FT /FTId=VAR_001966. FT VARIANT 1486 1486 G -> A (IN AS; ADULT TYPE). FT /FTId=VAR_008015. FT VARIANT 1488 1488 S -> F (IN AS). FT /FTId=VAR_011287. FT VARIANT 1498 1498 A -> D (IN AS). FT /FTId=VAR_001967. FT VARIANT 1511 1511 R -> H (IN AS; JUVENILE TYPE; COULD BE A FT NON PATHOGENIC VARIANT). FT /FTId=VAR_011288. FT VARIANT 1517 1517 P -> T (IN AS; JUVENILE TYPE). FT /FTId=VAR_001968. FT VARIANT 1538 1538 W -> S (IN AS; ADULT TYPE). FT /FTId=VAR_001969. FT VARIANT 1559 1559 P -> A. FT /FTId=VAR_008016. FT VARIANT 1563 1563 R -> Q (IN AS). FT /FTId=VAR_001970. FT VARIANT 1564 1564 C -> S (IN AS; ADULT TYPE). FT /FTId=VAR_001971. FT VARIANT 1567 1567 C -> R (IN AS; JUVENILE TYPE). FT /FTId=VAR_011289. FT VARIANT 1596 1596 G -> D (IN AS). FT /FTId=VAR_001972. FT VARIANT 1649 1649 L -> R (IN AS; ADULT TYPE). FT /FTId=VAR_001973. FT VARIANT 1677 1677 R -> P (IN AS). FT /FTId=VAR_011290. FT VARIANT 1677 1677 R -> Q (IN AS). FT /FTId=VAR_001974. FT VARIANT 1678 1678 C -> W (IN AS). FT /FTId=VAR_011291. FT CONFLICT 440 441 AG -> GS (IN REF. 3). FT CONFLICT 625 628 FGPP -> LALQ (IN REF. 3). FT CONFLICT 667 668 LP -> FR (IN REF. 3). FT CONFLICT 888 888 A -> R (IN REF. 3). ** ** ################# INTERNAL SECTION ################## **CL Xq22; SQ SEQUENCE 1685 AA; 161044 MW; 4450A6762F12A626 CRC64; MKLRGVSLAA GLFLLALSLW GQPAEAAACY GCSPGSKCDC SGIKGEKGER GFPGLEGHPG LPGFPGPEGP PGPRGQKGDD GIPGPPGPKG IRGPPGLPGF PGTPGLPGMP GHDGAPGPQG IPGCNGTKGE RGFPGSPGFP GLQGPPGPPG IPGMKGEPGS IIMSSLPGPK GNPGYPGPPG IQGLPGPTGI PGPIGPPGPP GLMGPPGPPG LPGPKGNMGL NFQGPKGEKG EQGLQGPPGP PGQISEQKRP IDVEFQKGDQ GLPGDRGPPG PPGIRGPPGP PGGEKGEKGE QGEPGKRGKP GKDGENGQPG IPGLPGDPGY PGEPGRDGEK GQKGDTGPPG PPGLVIPRPG TGITIGEKGN IGLPGLPGEK GERGFPGIQG PPGLPGPPGA AVMGPPGPPG FPGERGQKGD EGPPGISIPG PPGLDGQPGA PGLPGPPGPA GPHIPPSDEI CEPGPPGPPG SPGDKGLQGE QGVKGDKGDT CFNCIGTGIS GPPGQPGLPG LPGPPGSLGF PGQKGEKGQA GATGPKGLPG IPGAPGAPGF PGSKGEPGDI LTFPGMKGDK GELGSPGAPG LPGLPGTPGQ DGLPGLPGPK GEPGGITFKG ERGPPGNPGL PGLPGNIGPM GPPGFGPPGP VGEKGIQGVA GNPGQPGIPG PKGDPGQTIT QPGKPGLPGN PGRDGDVGLP GDPGLPGQPG LPGIPGSKGE PGIPGIGLPG PPGPKGFPGI PGPPGAPGTP GRIGLEGPPG PPGFPGPKGE PGFALPGPPG PPGLPGFKGA LGPKGDRGFP GPPGPPGRTG LDGLPGPKGD VGPNGQPGPM GPPGLPGIGV QGPPGPPGIP GPIGQPGLHG IPGEKGDPGP PGLDVPGPPG ERGSPGIPGA PGPIGPPGSP GLPGKAGASG FPGTKGEMGM MGPPGPPGPL GIPGRSGVPG LKGDDGLQGQ PGLPGPTGEK GSKGEPGLPG PPGPMDPNLL GSKGEKGEPG LPGIPGVSGP KGYQGLPGDP GQPGLSGQPG LPGPPGPKGN PGLPGQPGLI GPPGLKGTIG DMGFPGPQGV EGPPGPSGVP GQPGSPGLPG QKGDKGDPGI SSIGLPGLPG PKGEPGLPGY PGNPGIKGSV GDPGLPGLPG TPGAKGQPGL PGFPGTPGPP GPKGISGPPG NPGLPGEPGP VGGGGHPGQP GPPGEKGKPG QDGIPGPAGQ KGEPGQPGFG NPGPPGLPGL SGQKGDGGLP GIPGNPGLPG PKGEPGFHGF PGVQGPPGPP GSPGPALEGP KGNPGPQGPP GRPGLPGPEG PPGLPGNGGI KGEKGNPGQP GLPGLPGLKG DQGPPGLQGN PGRPGLNGMK GDPGLPGVPG FPGMKGPSGV PGSAGPEGEP GLIGPPGPPG LPGPSGQSII IKGDAGPPGI PGQPGLKGLP GPQGPQGLPG PTGPPGDPGR NGLPGFDGAG GRKGDPGLPG QPGTRGLDGP PGPDGLQGPP GPPGTSSVAH GFLITRHSQT TDAPQCPQGT LQVYEGFSLL YVQGNKRAHG QDLGTAGSCL RRFSTMPFMF CNINNVCNFA SRNDYSYWLS TPEPMPMSMQ PLKGQSIQPF ISRCAVCEAP AVVIAVHSQT IQIPHCPQGW DSLWIGYSFM MHTSAGAEGS GQALASPGSC LEEFRSAPFI ECHGRGTCNY YANSYSFWLA TVDVSDMFSK PQSETLKAGD LRTRISRCQV CMKRT // ID O21165 PRELIMINARY; PRT; 262 AA. AC O21165; DT 01-JAN-1998 (TrEMBLrel. 05, Created) DT 01-JAN-1998 (TrEMBLrel. 05, Last sequence update) DT 01-JUN-2002 (TrEMBLrel. 21, Last annotation update) DE Putative reverse transcriptase (Fragment){EI2}. GN RT{EI2}. OS Fusarium oxysporum. OG Mitochondrion{EI2}. OG Plasmid pFOXC1{EI2}. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreales; mitosporic Hypocreales; Fusarium. OX NCBI_TaxID=5507{EP3}; RN [1]{EI2} RP SEQUENCE FROM N.A. RC TISSUE=Liver{EI2}, and Kidney{EI2}; RX MEDLINE=97394960; PubMed=9251222; RA Kistler H.C., Benny U., Powell W.A.; RT "Linear mitochondrial plasmids of Fusarium oxysporum contain genes RT with sequence similarity to genes encoding a reverse transcriptase RT from Neurospora spp."; RL Appl. Environ. Microbiol. 63:3311-3313(1997). DR EMBL; AF005240; AAD12231.1; -.{EI2} DR InterPro; IPR000477; RVTse. DR Pfam; PF00078; rvt; 1. KW Plasmid{EP3}; RNA-directed DNA polymerase{EP3,EA1}. FT NON_TER 1 1 {EI2} FT NON_TER 262 262 {EI2} ** ** ################# SOURCE SECTION ################## ** Fusarium oxysporum plasmid pFOXC1 putative reverse transcriptase (RT) gene, ** mitochondrial plasmid gene, partial cds. ** [1] ** 1-785 ** MEDLINE; 97394960. ** Kistler H.C., Benny U., Powell W.A.; ** "Linear mitochondrial plasmids of Fusarium oxysporum contain genes with ** sequence similarity to genes encoding a reverse transcriptase from ** Neurospora spp"; ** Appl. Environ. Microbiol. 63(8):3311-3313(1997). ** [2] ** 1-785 ** Kistler H.C., Benny U., Powell W.A.; ** ; ** Submitted (23-MAY-1997) to the EMBL/GenBank/DDBJ databases. ** Plant Pathology, University of Florida, PO Box 110680, Gainesville, FL ** 32611-0680, USA ** SPTREMBL; O21165; O21165. ** source 1..785 ** /db_xref="taxon:5507" ** /organelle="mitochondrion" ** /organism="Fusarium oxysporum" ** /plasmid="pFOXC1" ** CDS complement(<1..>785) ** /codon_start=1 ** /evidence=NOT_EXPERIMENTAL ** /transl_table=4 ** /gene="RT" ** /product="putative reverse transcriptase" ** /protein_id="AAD12231.1" ** CDS_IN_EMBL_ENTRY 1 ** 03-MAR-2000 (Rel. 62, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **EV EP3; TrEMBL; -; AAD12231.1; 30-SEP-2001. **EV EA1; Rulebase; -; RU000322; 30-JAN-2002. **EV EI2; EMBL; -; AAD12231.1; 30-SEP-2001. **ID XXXX_FUSOX **PM Pfam; PF00078; rvt; 12; 241; T; 18-MAR-2002; SQ SEQUENCE 262 AA; 30050 MW; 00F0D8B1DAA6A0F4 CRC64; RSELIEIMNQ CRAFRLTMDL KRYYLTKPNG KYRPIGSPTL GSKVISKALT DIWTTIADKR RGVMQHAFRP KLGVWSAAFA VCQKLRSRKP SDVIIEFDLK GFFNTIKRNS VQEAANRFSL LLGNCVRHII DNTRYVFEEL KPETELHIIN DYTHHKYKRA IPIYRTGVPQ GLPLSPVAAT IALENEVNMP EMVMYADDGI LIGGKEKFAE FVKKAIRVGA EVAPEKTREV TKEFKFLGLT FNLEKETVSN GDSYRFWNDK DL // ID NUCA_SERMA STANDARD; PRT; 266 AA. AC P13717; DT 01-JAN-1990 (Rel. 13, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Nuclease precursor (EC 3.1.30.2) (Endonuclease). GN NUCA OR NUC. OS Serratia marcescens. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Serratia. OX NCBI_TaxID=615; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=W225; RX MEDLINE=88084425; PubMed=3319779; RA Ball T.K., Saurugger P.N., Benedick M.J.; RT "The extracellular nuclease gene of Serratia marcescens and its RT secretion from Escherichia coli."; RL Gene 57:183-192(1987). RN [2] RP REVISIONS TO 7-11. RC STRAIN=W225; RA Benedick M.J.; RL Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 21-266, AND DISULFIDE BONDS. RC STRAIN=B10M1; RX MEDLINE=93385170; PubMed=8373817; RA Pedersen J., Filimonova M.N., Roepstorff P., Biedermann K.; RT "Characterization of Serratia marcescens nuclease isoforms by plasma RT desorption mass spectrometry."; RL Biochim. Biophys. Acta 1202:13-21(1993). RN [4] RP PARTIAL SEQUENCE, AND DISULFIDE BONDS. RX MEDLINE=89322554; PubMed=2665765; RA Biedermann K., Jepsen P.K., Riise E., Svendsen I.; RT "Purification and characterization of a Serratia marcescens nuclease RT produced by Escherichia coli."; RL Carlsberg Res. Commun. 54:17-27(1989). RN [5] RP ACTIVE SITE. RX MEDLINE=94359798; PubMed=8078761; RA Friedhoof P., Gimadutdinow O., Pingoud A.; RT "Identification of catalytically relevant amino acids of the RT extracellular Serratia marcescens endonuclease by alignment-guided RT mutagenesis."; RL Nucleic Acids Res. 22:3280-3287(1994). RN [6] RP KINETIC STUDIES. RX MEDLINE=95102530; PubMed=7804150; RA Filimonova M.N., Krause K.L., Benedik M.J.; RT "Kinetic studies of the Serratia marcescens extracellular nuclease RT isoforms."; RL Biochem. Mol. Biol. Int. 33:1229-1236(1994). RN [7] RP MUTAGENESIS. RX MEDLINE=96313223; PubMed=8758988; RA Firedhoff P., Kolmes B., Gimadutdinow O., Wende W., Krause K.L., RA Pingoud A.; RT "Analysis of the mechanism of the Serratia nuclease using RT site-directed mutagenesis."; RL Nucleic Acids Res. 24:2632-2639(1996). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX MEDLINE=95393180; PubMed=7664065; RA Miller M.D., Tanner J., Alpaugh M., Benedik M.J., Krause K.L.; RT "2.1-A structure of Serratia endonuclease suggests a mechanism for RT binding to double-stranded DNA."; RL Nat. Struct. Biol. 1:461-468(1994). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX MEDLINE=97400229; PubMed=9257723; RA Lunin V.Y., Levdikov V.M., Shlyapnikov S.V., Blagova E.V., Lunin V.V., RA Wilson K.S., Mikhailov A.M.; RT "Three-dimensional structure of Serratia marcescens nuclease at 1.7-A RT resolution and mechanism of its action."; RL FEBS Lett. 412:217-220(1997). CC -!- FUNCTION: CATALYZES THE HYDROLYSIS OF BOTH DNA AND RNA, DOUBLE- CC OR SINGLE-STRANDED, AT THE 3'POSITION OF THE PHOSPHODIESTER BOND CC TO PRODUCE 5'-PHOSPHORYLATED MONO-, DI-, TRI- AND CC TETRANUCLEOTIDES. DNA IS A SLIGHTLY BETTER SUBSTRATE THAN RNA. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomononucleotide and 5'-phosphooligonucleotide end-products. CC -!- COFACTOR: MAGNESIUM IS IMPORTANT FOR ACTIVITY; IN ITS ABSENCE CC NUCLEASE ACTIVITY IS SIGNIFICANTLY REDUCED. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: BELONGS TO THE DNA/RNA NON-SPECIFIC ENDONUCLEASES CC FAMILY. DR EMBL; M19495; AAA26560.1; -. DR PIR; A27356; A27356. DR PDB; 1SMN; 29-JAN-96. DR InterPro; IPR001604; Endonuclease. DR Pfam; PF01223; Endonuclease; 1. DR SMART; SM00477; NUC; 1. DR PROSITE; PS01070; NUCLEASE_NON_SPEC; 1. KW Hydrolase; Nuclease; Endonuclease; Magnesium; Signal; 3D-structure. FT SIGNAL 1 20 FT CHAIN 21 266 NUCLEASE, ISOFORM SM2. FT CHAIN 22 266 NUCLEASE, ISOFORM SM3. FT CHAIN 24 266 NUCLEASE, ISOFORM SM1. FT ACT_SITE 110 110 FT DISULFID 30 34 FT DISULFID 222 264 ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 266 AA; 28944 MW; A0FF0C1430677B9E CRC64; MRFNNKMLAL AALLFAAQAS ADTLESIDNC AVGCPTGGSS NVSIVRHAYT LNNNSTTKFA NWVAYHITKD TPASGKTRNW KTDPALNPAD TLAPADYTGA NAALKVDRGH QAPLASLAGV SDWESLNYLS NITPQKSDLN QGAWARLEDQ ERKLIDRADI SSVYTVTGPL YERDMGKLPG TQKAHTIPSA YWKVIFINNS PAVNHYAAFL FDQNTPKGAD FCQFRVTVDE IEKRTGLIIW AGLPDDVQAS LKSKPGVLPE LMGCKN // ID CLP1_AGRT5 STANDARD; PRT; 202 AA. AC Q8UEX6; DT 15-JUN-2002 (Rel. 41, Created) DT 15-JUN-2002 (Rel. 41, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE ATP-dependent Clp protease proteolytic subunit 1 (EC 3.4.21.92) DE (Endopeptidase Clp 1). GN CLPP1 OR ATU1627 OR AGR_C_3003. OS Agrobacterium tumefaciens (strain C58 / ATCC 33970). OC Bacteria; Proteobacteria; alpha subdivision; Rhizobiaceae group; OC Rhizobiaceae; Rhizobium. OX NCBI_TaxID=176299; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=21608550; PubMed=11743193; RA Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., RA Okura V.K., Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., RA Chen Y., Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., RA Chapman P., Clendenning J., Deatherage G., Gillet W., Grant C., RA Kutyavin T., Levy R., Li M.-J., McClelland E., Palmieri A., RA Raymond C., Rouse G., Saenphimmachak C., Wu Z., Romero P., Gordon D., RA Zhang S., Yoo H., Tao Y., Biddle P., Jung M., Krespan W., Perry M., RA Gordon-Kamm B., Liao L., Kim S., Hendrick C., Zhao Z.-Y., Dolan M., RA Chumley F., Tingey S.V., Tomb J.-F., Gordon M.P., Olson M.V., RA Nester E.W.; RT "The genome of the natural genetic engineer Agrobacterium tumefaciens RT C58."; RL Science 294:2317-2323(2001). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=21608551; DOI=10.1002; PubMed=11743194; RA Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., RA Qurollo B., Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., RA Houmiel K., Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., RA Wollam C., Allinger M., Doughty D., Scott C., Lappas C., Markelz B., RA Flanagan C., Crowell C., Gurson J., Lomo C., Sear C., Strub G., RA Cielo C., Slater S.; RT "Genome sequence of the plant pathogen and biotechnology agent RT Agrobacterium tumefaciens C58."; RL Science 294:2323-2328(2001). CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins to small peptides in CC the presence of ATP and magnesium. Alpha-casein is the usual test CC substrate. In the absence of ATP, only oligopeptides shorter than CC five residues are cleaved (such as succinyl-Leu-Tyr-|-NHMEC; and CC Leu-|-Tyr-Trp, in which the cleavage of the -Tyr-|-Leu- CC bond also occurs). CC -!- CATALYTIC ACTIVITY: Cleaves Leu-|- CC bonds and disulfide- CC bonds. CC -!- RNA EDITING: Modified_positions=Not_applicable; CC Note=a. CC -!- RNA EDITING: Modified_positions=Undetermined. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; CC Comment=This is just a test; CC Name=1; CC IsoId=Q8UEX6-1; Sequence=Displayed; DR EMBL; AE009120; AAL42629.1; -. DR EMBL; AE008085; AAK87406.1; -. DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1. DR PROSITE; PS00381; CLP_PROTEASE_SER; FALSE_NEG. KW Hydrolase; Serine protease; Complete proteome. FT ACT_SITE 102 102 BY SIMILARITY. FT ACT_SITE 127 127 Performs a certain function (By FT similarity). ** ** ################# INTERNAL SECTION ################## **HA SAM; Annotated by PicoHamap 1.56; MF_00444.2; 21-JUN-2002. **HF HAMAP; MF_00444; 1. **NI CLPP1 SQ SEQUENCE 202 AA; 22834 MW; 754E1B1D1A82C36C CRC64; MRETMQLVPM VVEQSSRGER SFDIYSRLLR ERIIFLNGEV DDTVSALVCA QLLFLEAENP KKPIHLYINS PGGMVTSGFA MYDTMRYIRA PVHTLCMGTA RSMGSFLLMA GEPGTRAALP NASILIHQPS GGFQGQASDM LIHAEEIRQT KHRMTRLYAE HCGRSYEEFE TAMDRDRFMT VQEALEWGLI DRILEVREDA AA // ID CPB2_STRPN STANDARD; PRT; 243 AA. AC Q54518; O08049; O08278; O52232; DT 28-FEB-2003 (Rel. 41, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 15-SEP-2003 (Rel. 42, Last annotation update) DE Protein-tyrosine phosphatase cpsB (EC 3.1.3.48). GN CPSB OR CPS19FB OR CAP1B. OS Streptococcus pneumoniae. OC Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1313; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NCTC 11906 / Serotype 19F, SP-496 / Serotype 19F, SP-VA92 / RC Serotype 19F, SP-GA71 / Serotype 19F, PO-329 / Serotype 19F, and RC SP-VA96 / Serotype 19F; RC TISSUE=Adrenal, Adrenal gland, Carcinoma, Femoral artery, Pancreatic RC acinar, and Pituitary; RX MEDLINE=98125733; PubMed=9466257; RA Coffey T.J., Enright M.C., Daniels M., Morona J.K., Morona R., RA Hryniewicz W., Paton J.C., Spratt B.G.; RT "Recombinational exchanges at the capsular polysaccharide RT biosynthetic locus lead to frequent serotype changes among natural RT isolates of Streptococcus pneumoniae."; RL Mol. Microbiol. 27:73-83(1998). CC -!- FUNCTION: Dephosphorylates cpsD. Involved in the regulation of CC capsular polysaccharide biosynthesis. CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- COFACTOR: Manganese. CC -!- PATHWAY: Capsular polysaccharide (CPS) biosynthesis. CC -!- RNA EDITING: Modified_positions=1306; Note=Partially edited. A CC stop codon is created at this position. CC -!- RNA EDITING: Modified_positions=; Note=. CC -!- SIMILARITY: BELONGS TO THE CPSB/CAPC FAMILY. DR EMBL; U09239; AAC44959.1; -. DR EMBL; Z83335; CAB05935.1; -. DR EMBL; AF030367; AAC38717.1; -. DR EMBL; AF030368; AAC38722.1; -. DR EMBL; AF030369; AAC38727.1; -. DR EMBL; AF030370; AAC38731.1; -. DR EMBL; AF030371; AAC38736.1; -. DR EMBL; AF030372; AAC38741.1; -. DR EMBL; AF106137; AAD17985.1; -. DR InterPro; IPR004013; PHP_C. DR Pfam; PF02811; PHP_C; 1. KW Exopolysaccharide synthesis; Hydrolase; Manganese; Bacterial capsule. FT VARIANT 226 226 A -> V (IN STRAIN NCTC 11906). FT MUTAGEN 199 199 D->N: LOSS OF ACTIVITY; WHEN ASSOCIATED FT WITH Q-201. FT MUTAGEN 201 201 H->Q: LOSS OF ACTIVITY; WHEN ASSOCIATED FT WITH N-199. ** ** ################# INTERNAL SECTION ################## **NI CPSB2 **ZA CAR, 22-JAN-2003; SQ SEQUENCE 243 AA; 28353 MW; 810A4C802EC43079 CRC64; MIDIHSHIVF DVDDGPKSRE ESKALLAESY RQGVRTIVST SHRRKGMFET PEEKIAENFL QVREIAKEVA DDLVIAYGAE IYYTLDALEK LEKKEIPTLN DSRYALIEFS MHTSYRQIHT GLSNILMLGI TPVIAHIERY DALENNEKRV RELIDMGCYT QINSYHVSKP KFFGEKYKFM KKRARYFLER DLVHVVASDM HNLDSRPPYM QQAYDIIAKK YGAKKAKELF VDNPRKIIMD QLI // ID ATL_STAAU STANDARD; PRT; 1256 AA. AC P52081; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Bifunctional autolysin precursor [Includes: N-acetylmuramoyl-L-alanine DE amidase (EC 3.5.1.28); Mannosyl-glycoprotein endo-beta-N- DE acetylglucosamidase (EC 3.2.1.96)]. GN ATL. OS Staphylococcus aureus. OC Bacteria; Firmicutes; Bacillales; Staphylococcus. OX NCBI_TaxID=1280; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 205-214 AND 776-792. RC STRAIN=RN450; RX MEDLINE=95116542; PubMed=7816834; RX DOI=10.1002/1615-9861(200212)2:12<1682::AID-PROT1682>3.0.COAID-PROT1682>3.0.CO;2-Y; RA Oshida T., Sugai M., Komatsuzawa H., Hong Y.-M., Suginaka H., RA Tomasz A.; RT "A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L- RT alanine amidase domain and an endo-beta-N-acetylglucosaminidase RT domain: cloning, sequence analysis, and characterization."; RL Proc. Natl. Acad. Sci. U.S.A. 92:285-289(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=NCTC 8325-4; RA Foster S.J.; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 1-28. RX MEDLINE=81090973; PubMed=6108877; RA Bennett C.D.; ** /NO TITLE. RL Unpublished results, cited by: RL Norton T.R.; RL Fed. Proc. 40:21-25(1981). CC -!- FUNCTION: ENDOHYDROLYSIS OF THE DI-N-ACETYLCHITOBIOSYL UNIT IN CC HIGH-MANNOSE GLYCOPEPTIDES AND GLYCOPROTEINS CONTAINING THE CC -[(MAN)5(GLCNAC)2]-ASN STRUCTURE. ONE N-ACETYL-D-GLUCOSAMINE CC RESIDUE REMAINS ATTACHED TO THE PROTEIN; THE REST OF THE CC OLIGOSACCHARIDE IS RELEASED INTACT. CC -!- CATALYTIC ACTIVITY: Hydrolyzes the link between N-acetylmuramoyl CC residues and L-amino acid residues in certain bacterial cell-wall CC glycopeptides. CC -!- CATALYTIC ACTIVITY: Endohydrolysis of the di-N-acetylchitobiosyl CC unit in high-mannose glycopeptides and glycoproteins containing CC the -[Man(GlcNAc)2]Asn-structure. One N-acetyl-D-glucosamine CC residue remains attached to the protein; the rest of the CC oligosaccharide is released intact. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- PTM: Undergoes proteolytic processing to generate the two CC extracellular lytic enzymes. CC -!- SIMILARITY: IN THE N-TERMINAL SECTION; BELONGS TO THE N- CC ACETYLMURAMOYL-L-ALANINE AMIDASE FAMILY 2. CC -!- SIMILARITY: IN THE C-TERMINAL SECTION; BELONGS TO FAMILY 73 OF CC GLYCOSYL HYDROLASES. DR EMBL; D17366; BAA04185.1; -. DR EMBL; L41499; AAA99982.1; -. DR InterPro; IPR002502; Amidase_2. DR InterPro; IPR002901; Amidase_4. DR Pfam; PF01510; Amidase_2; 1. DR Pfam; PF01832; Amidase_4; 1. DR SMART; SM00644; Ami_2; 1. DR SMART; SM00047; LYZ2; 1. KW Cell wall; Hydrolase; Signal; Multifunctional enzyme; Repeat. FT SIGNAL 1 29 Potential. FT CHAIN 30 1256 Bifunctional autolysin. FT DOMAIN 199 775 N-acetylmuramoyl-L-alanine amidase. FT DOMAIN 776 1256 ENDO-BETA-N-ACETYLGLUCOSAMIDASE. FT REPEAT 425 589 1. FT REPEAT 596 758 2. FT REPEAT 770 932 3. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 1256 AA; 137384 MW; 2BB76CAA292FDD20 CRC64; MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA TTEQAKAEVK NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ VNGDTRANQS ATTNNTQPVA KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE NQINPELIKS AAKPAALETQ YKTAAPKAAT TSAPKAKTEA TPKVTTFSAS AQPRSVAATP KTSLPKYKPQ VNSSINDYIC KNNLKAPKIE EDYTSYFPKY AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ YYGLKPDSAE YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY DLINEKYLIK MGKVAPWGTQ STTTPTTPSK PTTPSKPSTG KLTVAANNGV AQIKPTNSGL YTTVYDKTGK ATNEVQKTFA VSKTATLGNQ KFYLVQDYNS GNKFGWVKEG DVVYNTAKSP VNVNQSYSIK PGTKLYTVPW GTSKQVAGSV SGSGNQTFKA SKQQQIDKSI YLYGSVNGKS GWVSKAYLVD TAKPTPTPTP KPSTPTTNNK LTVSSLNGVA QINAKNNGLF TTVYDKTGKP TKEVQKTFAV TKEASLGGNK FYLVKDYNSP TLIGWVKQGD VIYNNAKSPV NVMQTYTVKP GTKLYSVPWG TYKQEAGAVS GTGNQTFKAT KQQQIDKSIY LFGTVNGKSG WVSKAYLAVP AAPKKAVAQP KTAVKAYTVT KPQTTQTVSK IAQVKPNNTG IRASVYEKTA KNGAKYADRT FYVTKERAHG NETYVLLNNT SHNIPLGWFN VKDLNVQNLG KEVKTTQKYT VNKSNNGLSM VPWGTKNQVI LTGNNIAQGT FNATKQVSVG KDVYLYGTIN NRTGWVNAKD LTAPTAVKPT TSAAKDYNYT YVIKNGNGYY YVTPNSDTAK YSLKAFNEQP FAVVKEQVIN GQTWYYGKLS NGKLAWIKST DLAKELIKYN QTGMTLNQVA QIQAGLQYKP QVQRVPGKWT DAKFNDVKHA MDTKRLAQDP ALKYQFLRLD QPQNISIDKI NQFLKGKGVL ENQGAAFNKA AQMYGINEVY LISHALLETG NGTSQLAKGA DVVNNKVVTN SNTKYHNVFG IAAYDNDPLR EGIKYAKQAG WDTVSKAIVG GAKFIGNSYV KAGQNTLYKM RWNPAHPGTH QYATDVDWAN INAKIIKGYY DKIGEVGKYF DIPQYK // ID ALBU_BOVIN STANDARD; PRT; 607 AA. AC P02769; O02787; DT 21-JUL-1986 (Rel. 01, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 10-OCT-2003 (Rel. 42, Last annotation update) DE Serum albumin precursor (Allergen Bos d 6). GN Name=ALB; Synonyms=ALB1, aal, abl; OrderedLocusNames=, ; ORFNames= ; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RA Holowachuk E.W., Stoltenborg J.K., Reed R.G., Peters T. Jr.; RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A., AND VARIANT THR-214. RC TISSUE=Liver; RA Barry T., Power S., Gannon F.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Liver; RA Hilger C., Grigioni F., de Beaufort C., Michel G., Hentges F.; RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A., AND VARIANT THR-214. RA Wu H.T., Huang M.C.; RT "The complete cDNA sequence of bovine serum albumin."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 1-32. RX MEDLINE=80024278; PubMed=488109; RA McGillivray R.T.A., Chung D.W., Davie E.W.; RT "Biosynthesis of bovine plasma proteins in a cell-free system. Amino- RT terminal sequence of preproalbumin."; RL Eur. J. Biochem. 98:477-485(1979). RN [6] RP SEQUENCE OF 25-424 AND 429-607, AND VARIANT THR-214. ** MEDLINE=None; PubMed=None; RA Brown J.R.; RT "Structure of bovine serum albumin."; RL Fed. Proc. 34:591-591(1975). RN [7] RP REVISIONS TO 190-195. RA Brown J.R.; RL Submitted (APR-1975) to the PIR data bank. RN [8] RP SEQUENCE OF 402-433. RX MEDLINE=82023364; PubMed=7283978; RA Reed R.G., Putnam F.W., Peters T. Jr.; RT "Sequence of residues 400-403 of bovine serum albumin."; RL Biochem. J. 191:867-868(1980). RN [9] RP SEQUENCE OF 19-28. RX MEDLINE=77134075; PubMed=843354; RA Patterson J.E., Geller D.M.; RT "Bovine microsomal albumin: amino terminal sequence of bovine RT proalbumin."; RL Biochem. Biophys. Res. Commun. 74:1220-1226(1977). RN [10] RP SEQUENCE, AND REVISIONS TO 118-119 AND 180. RX MEDLINE=91083649; PubMed=2260975; RA Hirayama K., Akashi S., Furuya M., Fukuhara K.-I.; RT "Rapid confirmation and revision of the primary structure of bovine RT serum albumin by ESIMS and Frit-FAB LC/MS."; RL Biochem. Biophys. Res. Commun. 173:639-646(1990). RN [11] RP SEQUENCE OF 25-41. RX MEDLINE=88267456; PubMed=3389500; RA Hsieh J.C., Lin F.P., Tam M.F.; RT "Electroblotting onto glass-fiber filter from an analytical RT isoelectrofocusing gel: a preparative method for isolating proteins RT for N-terminal microsequencing."; RL Anal. Biochem. 170:1-8(1988). RN [12] RP SEQUENCE OF 437-451. RA Vilbois F.; RL Submitted (AUG-1998) to Swiss-Prot. RN [13] RP DISULFIDE BONDS. ** MEDLINE=None; PubMed=None; RA Brown J.R.; RT "Structure of serum albumin: disulfide bridges."; RL Fed. Proc. 33:1389-1389(1974). CC -!- FUNCTION: Serum albumin, the main protein of plasma, has a good CC binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, CC hormones, bilirubin and drugs. Its main function is the regulation CC of the colloidal osmotic pressure of blood. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Plasma. CC -!- ALLERGEN: Causes an allergic reaction in human. CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. CC -!- SIMILARITY: Contains 3 albumin domains. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q92482-1; Sequence=Displayed; CC Name=2; Synonyms=delta5; CC IsoId=Q92482-2, Q92482-3; Sequence=VSP_003229, VSP_003230, VSP_003229, VSP_003230, VSP_003229, VSP_003230; CC Note=Due to a polymorphism at the 5'-splice donor site of intron CC 5, leading to exon 5 skipping and premature termination of CC translation. This is the molecular basis of the GIL blood group; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: KM=62 mM for glucose{EA1} ; CC Vmax=0.11 mmol/min/mg enzyme when maltose is used as the CC substrate; CC KM=90 mM for maltose{EP1}; Vmax=0.20 mmol/min/mg enzyme when glucose is used as CC the substrate; CC Note=Acetylates glucose, maltose, mannose, galactose, and CC fructose with a decreasing relative rate of 1, 0.55, 0.20, 0.07, CC 0.04; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: KM= ; CC Vmax=; CC KM=; CC Note=; CC -!- TOXIC DOSE: LD(50) of the glycosylated and non-glycosylated forms CC are 13.4 +/- 0.7 and 5.8 +/- 0.3 nmol/g by intra-abdominal CC injection into the cricket G.assimilis, respectively. LD(50) of CC the glycosylated and non-glycosylated forms are 15 +/- 1 and 0.16 +/- CC 0.01 uM for human HL-60 cells, respectively. CC -!- INTERACTION: CC P38936:CDKN1A; NbExp=1; IntAct=EBI-374862, EBI-375077; CC P42771:CDKN2A; NbExp=1; IntAct=EBI-374862, EBI-375053; CC Q9H211:CDT1; NbExp=1; IntAct=EBI-374862, EBI-456953; CC Q96H67:cdt1; NbExp=1; IntAct=EBI-374862, EBI-371677; CC Q7L590:MCM10; NbExp=1; IntAct=EBI-374862, EBI-374912; CC P49736:MCM2; NbExp=1; IntAct=EBI-374862, EBI-374819; CC P25205:MCM3; NbExp=1; IntAct=EBI-374862, EBI-355153; CC Q13415:ORC1L; NbExp=1; IntAct=EBI-374862, EBI-374847; CC Q13416:ORC2L; NbExp=1; IntAct=EBI-374862, EBI-374957; CC Q9UBD5:ORC3L; NbExp=1; IntAct=EBI-374862, EBI-374916; CC O43913:ORC5L; NbExp=1; IntAct=EBI-374862, EBI-374928; CC Q9Y5N6:ORC6L; NbExp=1; IntAct=EBI-374862, EBI-374840; CC P62988:RPS27A; NbExp=1; IntAct=EBI-374862, EBI-413034; DR EMBL; M73993; AAA51411.1; -. DR EMBL; X58989; CAA41735.1; -. DR EMBL; Y17769; CAA76847.1; -. DR EMBL; AF542068; AAN17824.1; -. DR HSSP; P02768; 1HK1. DR InterPro; IPR000264; Serum_albumin. DR Pfam; PF00273; Serum_albumin; 3. DR PRINTS; PR00802; SERUMALBUMIN. DR ProDom; PD002486; Serum_albumin; 1. DR SMART; SM00103; ALBUMIN; 3. DR PROSITE; PS00212; ALBUMIN; 3. KW Metal-binding; Lipid-binding; Repeat; Signal; Copper; Allergen; KW Polymorphism. FT SIGNAL 1 18 FT PROPEP 19 24 FT CHAIN 25 607 Serum albumin. FT DOMAIN 25 204 Albumin 1. FT DOMAIN 211 396 Albumin 2. FT DOMAIN 403 594 Albumin 3. FT METAL 27 27 Copper (By similarity). FT DISULFID 77 86 FT DISULFID 99 115 FT DISULFID 114 125 FT DISULFID 147 192 FT DISULFID 191 200 FT DISULFID 223 269 FT DISULFID 268 276 FT DISULFID 288 302 FT DISULFID 301 312 FT DISULFID 339 384 FT DISULFID 383 392 FT DISULFID 415 461 FT DISULFID 460 471 FT DISULFID 484 500 FT DISULFID 499 510 FT DISULFID 537 582 FT DISULFID 581 590 FT MUTAGEN 398 429 KRSRSDRAVTGPSAQQSFEVRVPEQRDALHLPLSWRVKRP FT ->TA: Complete loss of HR activity. FT MUTAGEN 399 429 TYEGKHNHHLLLSPPSSSTLPFNSPQLSKQTI->SLQPTRV FT NIIIICS: In ttg2-2; defects in trichome FT development, seed coat color and mucilage FT production. FT VARIANT 214 214 A -> T. FT CONFLICT 302 302 C -> K (in Ref. 6). FT CONFLICT 304 305 KP -> PC (in Ref. 6). FT CONFLICT 324 324 N -> D (in Ref. 6). FT CONFLICT 394 395 ST -> TS (in Ref. 6). FT CONFLICT 437 437 K -> R (in Ref. 12). FT CONFLICT 493 494 SE -> ES (in Ref. 6). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 607 AA; 69293 MW; 39167DFE768585D4 CRC64; MKWVTFISLL LLFSSAYSRG VFRRDTHKSE IAHRFKDLGE EHFKGLVLIA FSQYLQQCPF DEHVKLVNEL TEFAKTCVAD ESHAGCEKSL HTLFGDELCK VASLRETYGD MADCCEKQEP ERNECFLSHK DDSPDLPKLK PDPNTLCDEF KADEKKFWGK YLYEIARRHP YFYAPELLYY ANKYNGVFQE CCQAEDKGAC LLPKIETMRE KVLASSARQR LRCASIQKFG ERALKAWSVA RLSQKFPKAE FVEVTKLVTD LTKVHKECCH GDLLECADDR ADLAKYICDN QDTISSKLKE CCDKPLLEKS HCIAEVEKDA IPENLPPLTA DFAEDKDVCK NYQEAKDAFL GSFLYEYSRR HPEYAVSVLL RLAKEYEATL EECCAKDDPH ACYSTVFDKL KHLVDEPQNL IKQNCDQFEK LGEYGFQNAL IVRYTRKVPQ VSTPTLVEVS RSLGKVGTRC CTKPESERMP CTEDYLSLIL NRLCVLHEKT PVSEKVTKCC TESLVNRRPC FSALTPDETY VPKAFDEKLF TFHADICTLP DTEKQIKKQT ALVELLKHKP KATEEQLKTV MENFVAFVDK CCAADDKEAC FAVEGPKLVV STQTALA // Swissknife_1.75/t/DEs.txl0000644005110600510130000004202010357506347015530 0ustar ecastroSwissProtID PYR5_DROME STANDARD; PRT; 493 AA. AC Q01637; Q24221; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 30-MAY-2000, entry version 1. DE URIDINE 5'-MONOPHOSPHATE SYNTHASE (UMP SYNTHASE) (RUDIMENTARY-LIKE- DE PROTEIN) [INCLUDES: OROTATE PHOSPHORIBOSYLTRANSFERASE (EC 2.4.2.10) DE (OPRTASE); OROTIDINE 5'-PHOSPHATE DECARBOXYLASE (EC 4.1.1.23) DE (OMPDECASE)] (Fragments). GN R-L. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Eisenberg M.T., Kirkpatrick R., Rawls J.; RL Submitted (XXX-1992) to the EMBL/GenBank/DDBJ databases. SQ SEQUENCE 493 AA; 53327 MW; 56479CDAB1F6A308 CRC64; MVAQNSDKMR ALALKLFEIN AFKFGDFKMK VGINSPVYFD LRVIVSLGLP QQTVSDLLVE HIKDKQLSAK HVCGVPYTAL PRATIVSVQQ GTPMLVRRKE AKAYGTKKLV EGIFNAGDTC LIVEDVVTSG SSILDTVRDL QGEGIVVTDA VVVVDREQGG VANIAKHGVR MHSLFTLSFL LNTLHEAGRI EKSTVEAVAK YIAAVQINSD GTFVGGDKVT FPAANDLQRT KLTYESRANL AKSAVAKRLF NLIASKQTNL CLAADLTHAD EILDVADKCG PYICLLKTHV DIVEDFSDKF IADLQALAQR HNFLLMEDRK FADIGNTVSL QYGKGIYKIS SWADLVTAHT LPGRSILQGL KAGLGEGGAG KERGVFLLAE MSASGNLIDA KYKENSNKIA TEGADVDFVA GVVCQSSDAF AFPGLLQLTP GVKIDEGVDQ LGQQYQSPEH VVKERGADIG VVGRGILKAS SPKQAAQTYR DRLWAAYQDR VAK // ID 25AA_MOUSE STANDARD; PRT; 367 AA. AC P11928; Q64440; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 30-MAY-2000, entry version 1. DE (2'-5')OLIGOADENYLATE SYNTHETASE 1A (EC 2.7.7.-) ((2-5')OLIGO(A) DE SYNTHETASE 1A) (2-5A SYNTHETASE 1A). GN OAS1A OR OIAS1. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87117515; PubMed=3808949; RT "Mouse 2-5A synthetase cDNA: nucleotide sequence and comparison to RT human 2-5A synthetase."; RL Nucleic Acids Res. 14:10117-10117(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91021025; PubMed=2171206; RA Coccia E.M., Romeo G., Nissim A., Marziali G., Albertini R., RA Affabris E., Battistini A., Fiorucci G., Orsatti R., Rossi G.B., RA Chebath J.; RT "A full-length murine 2-5A synthetase cDNA transfected in NIH-3T3 RT cells impairs EMCV but not VSV replication."; RL Virology 179:228-233(1990). RN [3] RP SEQUENCE OF 14-367 FROM N.A. RX MEDLINE=91232962; PubMed=1709495; RA Rutherford M.N., Kumar A., Nissim A., Chebath J., Williams B.R.G.; RT "The murine 2-5A synthetase locus: three distinct transcripts from RT two linked genes."; RL Nucleic Acids Res. 19:1917-1924(1991). CC -!- CATALYTIC ACTIVITY: BINDS DOUBLE-STRANDED RNA AND POLYMERIZES ATP CC INTO PPP(A2'P5'A)N OLIGOMERS, WHICH ACTIVATE THE LATENT RNASE L CC THAT, WHEN ACTIVATED, CLEAVES SINGLE-STRANDED RNAS. CC -!- INDUCTION: BY INTERFERONS. CC -!- SIMILARITY: BELONGS TO THE 2-5A SYNTHETASE FAMILY. DR EMBL; X04958; CAA28620.1; -. DR EMBL; M33863; AAA37116.1; -. DR EMBL; X58077; CAA41105.1; -. DR PIR; A24725; SYMSO1. DR MGI; MGI:97429; OAS1A. DR INTERPRO; IPR001797; -. DR PROSITE; PS00832; 25A_SYNTH_1; 1. DR PROSITE; PS00833; 25A_SYNTH_2; 1. KW RNA-binding; Transferase; Nucleotidyltransferase; KW Interferon induction; Multigene family. SQ SEQUENCE 367 AA; 42456 MW; 3A4D145FA582A976 CRC64; MEHGLRSIPA WTLDKFIEDY LLPDTTFGAD VKSAVNVVCD FLKERCFQGA AHPVRVSKVV KGGSSGKGTT LKGRSDADLV VFLNNLTSFE DQLNRRGEFI KEIKKQLYEV QHERRFRVKF EVQSSWWPNA RSLSFKLSAP HLHQEVEFDV LPAFDVLGHV NTSSKPDPRI YAILIEECTS LGKDGEFSTC FTELQRNFLK QRPTKLKSLI RLVKHWYQLC KEKLGKPLPP QYALELLTVF AWEQGNGCYE FNTAQGFRTV LELVINYQHL RIYWTKYYDF QHQEVSKYLH RQLRKARPVI LDPADPTGNV AGGNPEGWRR LAEEADVWLW YPCFIKKDGS RVSSWDVPTV VPVPFEQVEE NWTCILL // ID ARGJ_BACST STANDARD; PRT; 410 AA. AC Q07908; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Arginine biosynthesis bifunctional protein argJ [Includes: Glutamate- DE and N-acetyltransferase (EC 2.3.1.35) (Ornithine acetyltransferase) DE (Ornithine transacetylase) (OATASE); Amino-acid acetyltransferase DE (EC 2.3.1.1) (N-acetylglutamate synthase) (AGS)] [Contains: Arginine DE biosynthesis bifunctional protein alpha chain; Arginine biosynthesis DE bifunctional protein beta chain]. GN ARGJ. OS Bacillus stearothermophilus. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Bacillales; OC Geobacillus. OX NCBI_TaxID=1422; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NCIB 8224; RX MEDLINE=93232760; PubMed=8473852; RA Sakanyan V., Charlier D.R.M., Legrain C., Kochikyan A., Mett I., RA Pierard P., Glansdorff N.; RT "Primary structure, partial purification and regulation of key RT enzymes of the acetyl cycle of arginine biosynthesis in Bacillus RT stearothermophilus: dual function of ornithine acetyltransferase."; RL J. Gen. Microbiol. 139:393-402(1993). RN [2] RP CHARACTERIZATION, AND MUTAGENESIS OF THR-197. RX PubMed=11320085; RA Marc F., Weigel P., Legrain C., Glansdorff N., Sakanyan V.; RT "An invariant threonine is involved in self-catalyzed cleavage of the RT precursor protein for ornithine acetyltransferase."; RL J. Biol. Chem. 276:25404-25410(2001). CC -!- FUNCTION: Catalyzes two activities which are involved in the CC cyclic version of arginine biosynthesis: the synthesis of CC acetlyglutamate from glutamate and acetyl-CoA, and of ornithine by CC transacetylation between acetylornithine and glutamate. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L- CC ornithine + N-acetyl-L-glutamate. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + L-glutamate = CoA + N-acetyl-L- CC glutamate. CC -!- ENZYME REGULATION: Feedback inhibition by L-arginine. CC -!- PATHWAY: Arginine biosynthesis; first and fifth steps. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. CC -!- MISCELLANEOUS: Independently synthesized alpha and beta subunits CC do not reconstitute a functional protein. Self-catalyzed precursor CC cleavage is a necessary step to form an active enzyme, probably by CC directing appropriate folding and/or topological organization of CC the active site. CC -!- SUBCELLULAR LOCATION: Cytoplasmic (Probable). CC -!- SIMILARITY: BELONGS TO THE ARGJ FAMILY. DR EMBL; L06036; AAA22197.1; -. DR InterPro; IPR002813; ArgJ. DR Pfam; PF01960; ArgJ; 1. DR ProDom; PD004193; ArgJ; 1. DR TIGRFAMs; TIGR00120; ArgJ; 1. KW Arginine biosynthesis; Multifunctional enzyme; Transferase; KW Acyltransferase. FT CHAIN 1 196 ARGININE BIOSYNTHESIS BIFUNCTIONAL FT PROTEIN ARGJ ALPHA CHAIN. FT CHAIN 197 410 ARGININE BIOSYNTHESIS BIFUNCTIONAL FT PROTEIN ARGJ BETA CHAIN. FT SITE 196 197 CLEAVAGE (NONHYDROLYTIC). FT MUTAGEN 197 197 T->G: NO AUTOPROTEOLYSIS; LOSS OF FT ACTIVITY. FT MUTAGEN 197 197 T->S,C: LOW RATE OF INTRAMOLECULAR FT CLEAVAGE; LOSS OF ACTIVITY. ** to be added: **HF HAMAP; MF_01106; 1. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 410 AA; 43377 MW; 00E948D64E8A8913 CRC64; MTITKQTGQV TAVADGTVVT PEGFQAAGVN AGLRYSKNDL GVILCDVPAS AAAVYTQSHF QAAPLKVTQA SLAVEQKLQA VIVNRPCANA CTGAQGLKDA YEMRELCAKQ FGLALHHVAV ASTGVIGEYL PMEKIRAGIK QLVPGVTMAD AEAFQTAILT TDTVMKRACY QTTIDGKTVT VGGAAKGSGM IHPNMATMLA FITTDANVSS PVLHAALRSI TDVSFNQITV DGDTSTNDMV VVMASGLAGN DELTPDHPDW ENFYEALRKT CEDLAKQIAK DGEGATKLIE VRVRGAKTDE EAKKIAKQIV GSNLVKTAVY GADANWGRII GAIGYSDAEV NPDNVDVAIG PMVMLKGSEP QPFSEEEAAA YLQQETVVIE VDLHIGDGVG VAWGCDLTYD YVKINASYRT // ID ANGT_HUMAN STANDARD; PRT; 485 AA. AC P01019; Q16358; Q16359; Q96F91; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Angiotensinogen precursor [Contains: Angiotensin I (Ang I); DE Angiotensin II (Ang II); Angiotensin III (Ang III) (Des-Asp[1]- DE angiotensin II)]. GN AGT OR SERPINA8. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89170129; PubMed=2924688; RA Gaillard I., Clauser E., Corvol P.; RT "Structure of human angiotensinogen gene."; RL DNA 8:87-99(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85000455; PubMed=6089875; RA Kageyama R., Ohkubo H., Nakanishi S.; RT "Primary structure of human preangiotensinogen deduced from the RT cloned cDNA sequence."; RL Biochemistry 23:3603-3609(1984). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=90237063; PubMed=1692023; RA Fukamizu A., Takahashi S., Seo M.S., Tada M., Tanimoto K., Uehara S., RA Murakami K.; RT "Structure and expression of the human angiotensinogen gene. RT Identification of a unique and highly active promoter."; RL J. Biol. Chem. 265:7576-7582(1990). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RA Strausberg R.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 1-338 FROM N.A. RX MEDLINE=87244745; PubMed=2885106; RA Kunapuli S.P., Kumar A.; RT "Molecular cloning of human angiotensinogen cDNA and evidence for the RT presence of its mRNA in rat heart."; RL Circ. Res. 60:786-790(1987). RN [6] RP SEQUENCE OF 34-45, AND SUBUNITS. RC TISSUE=Serum; RX MEDLINE=95293954; PubMed=7539791; RA Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., RA Stigbrand T., Gleich G.J., Sottrup-Jensen L.; RT "Identification of angiotensinogen and complement C3dg as novel RT proteins binding the proform of eosinophil major basic protein in RT human pregnancy serum and plasma."; RL J. Biol. Chem. 270:13645-13651(1995). RN [7] RP SEQUENCE OF 34-43. RX MEDLINE=69014170; PubMed=4300938; RA Arakawa K., Minohara A., Yamada J., Nakamura M.; RT "Enzymatic degradation and electrophoresis of human angiotensin I."; RL Biochim. Biophys. Acta 168:106-112(1968). RN [8] RP CARBOHYDRATE-LINKAGE SITES. RX MEDLINE=86056581; PubMed=3934016; RA Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P.; RT "Processing of rat and human angiotensinogen precursors by microsomal RT membranes."; RL Mol. Cell. Endocrinol. 43:31-40(1985). RN [9] RP FUNCTION OF ANGIOTENSIN III. RX MEDLINE=75166949; PubMed=1132082; RA Goodfriend T.L., Peach M.J.; RT "Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and RT speculation for its role as an important agonist in the renin - RT angiotensin system."; RL Circ. Res. 36:38-48(1975). RN [10] RP STRUCTURE BY NMR OF ANGIOTENSIN II. RX MEDLINE=98151281; PubMed=9492317; RA Carpenter K.A., Wilkes B.C., Schiller P.W.; RT "The octapeptide angiotensin II adopts a well-defined structure in a RT phospholipid environment."; RL Eur. J. Biochem. 251:448-453(1998). RN [11] RP VARIANTS MET-207; THR-268 AND CYS-281. RX MEDLINE=93008239; PubMed=1394429; RA Jeunemaitre X., Soubrier F., Kotelevtsev Y.V., Lifton R.P., RA Williams C.S., Charru A., Hunt S.C., Hopkins P.N., Williams R.R., RA Lalouel J.-M., Corvol P.; RT "Molecular basis of human hypertension: role of angiotensinogen."; RL Cell 71:169-180(1992). RN [12] RP VARIANT THR-268. RX MEDLINE=93291876; PubMed=8513325; RA Ward K., Hata A., Jeunemaitre X., Helin C., Nelson L., Namikawa C., RA Farrington P.F., Ogasawara M., Suzumori K., Tomoda S., Berrebi S., RA Sasaki M., Corvol P., Lifton R.P., Lalouel J.-M.; RT "A molecular variant of angiotensinogen associated with RT preeclampsia."; RL Nat. Genet. 4:59-61(1993). RN [13] RP VARIANTS ILE-242; ARG-244 AND CYS-281. RX MEDLINE=95331754; PubMed=7607642; RA Hixson J.E., Powers P.K.; RT "Detection and characterization of new mutations in the human RT angiotensinogen gene (AGT)."; RL Hum. Genet. 96:110-112(1995). RN [14] RP CHARACTERIZATION OF VARIANT CYS-281. RX MEDLINE=96199253; PubMed=8621667; RA Gimenez-Roqueplo A.P., Leconte I., Cohen P., Simon D., Guyene T.T., RA Celerier J., Pau B., Corvol P., Clauser E., Jeunemaitre X.; RT "The natural mutation Y248C of human angiotensinogen leads to abnormal RT glycosylation and altered immunological recognition of the protein."; RL J. Biol. Chem. 271:9838-9844(1996). CC -!- FUNCTION: IN RESPONSE TO LOWERED BLOOD PRESSURE, THE ENZYME RENIN CC CLEAVES ANGIOTENSIN I, FROM ANGIOTENSINOGEN. ACE (ANGIOTENSIN CC CONVERTING ENZYME) THEN REMOVES A DIPEPTIDE TO YIELD THE CC PHYSIOLOGICALLY ACTIVE PEPTIDE ANGIOTENSIN II, THE MOST POTENT CC PRESSOR SUBSTANCE KNOWN, WHICH HELPS REGULATE VOLUME AND MINERAL CC BALANCE OF BODY FLUIDS. CC -!- FUNCTION: Angiotensin III stimulates aldosterone release. CC -!- SUBUNIT: During pregnancy, exists as a disulfide-linked 2:2 CC heterotetramer with the proform of PRG2 and as a complex (probably CC a 2:2:2 heterohexamer) with pro-PRG2 and C3dg. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Synthesized by the liver and secreted in the CC plasma. CC -!- DISEASE: AGT SEEMS TO BE ASSOCIATED WITH A PREDISPOSITION TO CC ESSENTIAL HYPERTENSION AS WELL AS PREGNANCY-INDUCED HYPERTENSION CC (PIH) (PREECLAMPSIA). CC -!- SIMILARITY: BELONGS TO THE SERPIN FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-10 IS THE INITIATOR. DR EMBL; K02215; AAA51731.1; -. DR EMBL; M24689; AAA51679.1; -. DR EMBL; M24686; AAA51679.1; JOINED. DR EMBL; M24687; AAA51679.1; JOINED. DR EMBL; M24688; AAA51679.1; JOINED. DR EMBL; X15324; CAA33385.1; -. DR EMBL; X15325; CAA33385.1; JOINED. DR EMBL; X15326; CAA33385.1; JOINED. DR EMBL; X15327; CAA33385.1; JOINED. DR EMBL; M69110; AAA52282.1; -. DR EMBL; BC011519; AAH11519.1; -. DR EMBL; S78529; AAD14287.1; -. DR EMBL; S78530; AAD14288.1; -. DR PIR; A01249; ANHU. DR PIR; A31362; A31362. DR PIR; A35203; A35203. DR SWISS-2DPAGE; P01019; HUMAN. DR Genew; HGNC:333; AGT. DR MIM; 106150; -. DR GO; GO:0005625; C:soluble fraction; TAS. DR GO; GO:0004867; F:serine protease inhibitor activity; TAS. DR GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS. DR GO; GO:0007267; P:cell-cell signaling; TAS. DR GO; GO:0007565; P:pregnancy; TAS. DR GO; GO:0008217; P:regulation of blood pressure; TAS. DR InterPro; IPR000227; Angiotensngn. DR InterPro; IPR000215; Serpin. DR Pfam; PF00079; serpin; 1. DR PRINTS; PR00654; ANGIOTENSNGN. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Vasoconstrictor; Glycoprotein; Plasma; Serpin; Signal; KW Disease mutation; Polymorphism. FT SIGNAL 1 33 FT CHAIN 34 485 ANGIOTENSINOGEN. FT PEPTIDE 34 43 ANGIOTENSIN I. FT PEPTIDE 34 41 ANGIOTENSIN II. FT PEPTIDE 35 41 ANGIOTENSIN III. FT CARBOHYD 47 47 N-LINKED (GLCNAC...). FT CARBOHYD 170 170 N-LINKED (GLCNAC...). FT CARBOHYD 304 304 N-LINKED (GLCNAC...). FT CARBOHYD 328 328 N-LINKED (GLCNAC...). FT VARIANT 207 207 T -> M (IN dbSNP:4762). FT /FTId=VAR_007093. FT VARIANT 242 242 T -> I (IN HYPERTENSION). FT /FTId=VAR_007094. FT VARIANT 244 244 L -> R (IN HYPERTENSION). FT /FTId=VAR_007095. FT VARIANT 268 268 M -> T (IN HYPERTENSION; dbSNP:699). FT /FTId=VAR_007096. FT VARIANT 281 281 Y -> C (IN HYPERTENSION; ALTERS THE FT STRUCTURE, GLYCOSYLATION AND SECRETION OF FT ANGIOTENSINOGEN). FT /FTId=VAR_007097. FT VARIANT 392 392 L -> M (IN dbSNP:1805090). FT /FTId=VAR_014573. FT CONFLICT 333 333 Q -> E (IN REF. 1). FT CONFLICT 335 335 P -> S (IN REF. 4). ** ** ################# INTERNAL SECTION ################## **CL 1q42-q43; SQ SEQUENCE 485 AA; 53154 MW; 5026C2DFB2DD236E CRC64; MRKRAPQSEM APAGVSLRAT ILCLLAWAGL AAGDRVYIHP FHLVIHNEST CEQLAKANAG KPKDPTFIPA PIQAKTSPVD EKALQDQLVL VAAKLDTEDK LRAAMVGMLA NFLGFRIYGM HSELWGVVHG ATVLSPTAVF GTLASLYLGA LDHTADRLQA ILGVPWKDKN CTSRLDAHKV LSALQAVQGL LVAQGRADSQ AQLLLSTVVG VFTAPGLHLK QPFVQGLALY TPVVLPRSLD FTELDVAAEK IDRFMQAVTG WKTGCSLMGA SVDSTLAFNT YVHFQGKMKG FSLLAEPQEF WVDNSTSVSV PMLSGMGTFQ HWSDIQDNFS VTQVPFTESA CLLLIQPHYA SDLDKVEGLT FQQNSLNWMK KLSPRTIHLT MPQLVLQGSY DLQDLLAQAE LPAILHTELN LQKLSNDRIR VGEVLNSIFF ELEADEREPT ESTQQLNKPE VLEVTLNRPF LFAVYDQSAT ALHFLGRVAN PLSTA // Swissknife_1.75/t/GNs.txl.expected0000644005110600510130000000135510001532100017316 0ustar ecastroSwissProtGN (A{EA1} OR B{EI2}) And C. GN (A{EA2} OR B{EI3}) And C. GN (A{EA2} or B{EI3}) and C. GN A{EA1} or B{EA2}. GN Timeo danaos, et dona ferentes. GN A{EA2} and C. GN C. (Nothing) (Nothing) GN Wallace OR Gromit. GN (Wallace OR Gromit) And GN (So long vict OR ious, happy 'n gl OR ious, long to reign over us). GN Foobar And (Wallace OR Gromit) And GN (So long vict OR ious, happy 'n gl OR ious, long to reign over us). GN Name=Foobar; GN and GN Name=Wallace; Synonyms=Gromit; GN and GN Name=So long vict; GN Synonyms=ious, happy 'n gl, ious, long to reign over us; GN Name=Foobar; GN and GN Name=Wallace; Synonyms=Gromit; GN and GN Name=So long vict; Synonyms=happy 'n gl, ious, long to reign over us; Swissknife_1.75/t/formatProblems.t0000644005110600510130000000470210331445707017504 0ustar ecastroSwissProt# Swissknife Test Harness Script for fullparse # # Purpose: # Check if a set of tricky entries are correctly (re-)formatted. # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 1; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}formatProblems.txl"; my $testout = "${where}formatProblems.txl.out"; my $expectedout = "${where}formatProblems.txl.expected"; open (IN, $testin); open (OUT, ">$testout"); use SWISS::Entry; # Read an entire record at a time $/ = "\/\/\n"; while (){ # Read the entry $entry = SWISS::Entry->fromText($_, 1); $entry->reformat; #the following three lines give duplicate **\n and **...INTERNAL SECTION #lines in Swissknife 1.1 $entry->toText; $entry->Stars->update; # check that adding non-existing synonyms to alternative products lines # does not produce blank events where the comment/name does not exist foreach $CC ($entry -> CCs -> elements()) { if ($CC -> topic eq 'ALTERNATIVE PRODUCTS') { $CC -> addEvidenceTag('EP1', "Alternative splicing", "Name", "E"); $CC -> addEvidenceTag('EP1', "Alternative splicing", "Name", "Wrong"); my @events = $CC -> getEventNames(); foreach $event (@events) { if ($event eq "Alternative splicing") { # check that a synonym lists and sequence lists are wrapped # sucessfully my @synonyms = ("Alice", "Barbara", "Chloe", "Deborah", "Emily", "Frida"); $CC -> setSynonyms("Alternative splicing", "E", \@synonyms); my @sequences = ("VSP_02391", "VSP_02392", "VSP_02393", "VSP_02394", "VSP_02395"); $CC -> setFeatIds( "Alternative splicing", "E", \@sequences); } } } } $entry->toText(); $entry->update(1); $entry->CCs->sort; $entry->CCs->unique; $entry->DRs->del('PROSITE','PS01117'); map {$_->rc_sort; $_->reformat} $entry->Refs->elements; map {$_->rc_sort; $_->reformat} $entry->Refs->elements; print OUT $entry->toText; print OUT $entry->isCurated(), "\n"; } close IN; close OUT; print "checking expected output...\n"; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; Swissknife_1.75/t/crc64.t0000644005110600510130000000200710366115237015425 0ustar ecastroSwissProt# Swissknife Test Harness Script for fullparse # # Purpose: # After a full parse, the output file should be identical # to the input. # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}identity.txl"; my $testout = "${where}identity.txl.out"; my $expectedout = "${where}identity.txl.expected"; open (IN, $testin); open (OUT, ">$testout"); use SWISS::Entry; # Read an entire record at a time $/ = "\/\/\n"; while (){ # Read the entry $entry = SWISS::Entry->fromText($_); $entry->reformat; $entry->DRs->update(); $entry->SQs->update(); print OUT $entry->toText; } close IN; close OUT; print "checking expected output...\n"; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; Swissknife_1.75/t/annot.t0000644005110600510130000000241410225167417015626 0ustar ecastroSwissProt# Swissknife Test Harness Script for annotators jobs # # Purpose: # Check if the parsing of wild ** comments and indented # lines is performed correctly. use Carp; # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}annot.txl"; my $testout = "${where}annot.txl.out"; my $expectedout = "${where}annot.txl.expected"; open (IN, $testin); open (OUT, ">$testout"); use SWISS::Entry; use Data::Dumper; # Read an entire record at a time $/ = "\/\/\n"; while (){ # Read the entry $entry = SWISS::Entry->fromText($_, 1, 1); $entry->GNs->set(); #perturbate the entry $entry->CCs->del("MISCELLANEOUS"); #perturbate the entry $entry->update(1); $entry->FTs($entry->FTs->copy); $entry->DRs($entry->DRs->copy); print OUT $entry->toText(); #no indented / wild ** lines print OUT $entry->toText(1);#add indented / wild ** lines } close IN; close OUT; print "checking expected output...\n"; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; Swissknife_1.75/t/fasta.txl0000644005110600510130000000542111551045077016152 0ustar ecastroSwissProtID DCTQ_RHOSH Unreviewed; 227 AA. AC Q9LBD9; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE Putative small C4-dicarboxylate integral membrane transport protein (Yadda). GN DCTQ. OS Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1063; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=4P1; RA Omrani M.D.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR C4-DICARBOXYLATE TRANSPORT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (BY SIMILARITY). SQ SEQUENCE 227 AA; 24991 MW; 2208AD920C1230DA CRC64; MMRLLDRLEE TLIASLIAAA TGLIFVSVVQ RYSLGLLADG VAFFRGHDMP ELSAMMRSAY LGLREFNLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINKLDERK RGFFILLGLG AGALFTGIIA TLGGNFVWHM AQTSAISPDL ELPMWLVYLA IPLGSALMCF RFLQVAVIFA RTGELAHHDH GHVEGVDTED EGIDVLGSTF LKSPLTPRDL VEKPKDE // ID DCTQ_RHOSH Unreviewed; 227 AA. AC Q9LBD9; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE Putative small C4-dicarboxylate integral membrane transport protein DE with a very very very very very very very very very very very very DE very very very very very very very very very very very very very DE very very very very very very very very very very very long name (Fragment). OS Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1063; SQ SEQUENCE 227 AA; 24991 MW; 2208AD920C1230DA CRC64; MMRLLDRLEE TLIASLIAAA TGLIFVSVVQ RYSLGLLADG VAFFRGHDMP ELSAMMRSAY LGLREFNLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINKLDERK RGFFILLGLG AGALFTGIIA TLGGNFVWHM AQTSAISPDL ELPMWLVYLA IPLGSALMCF RFLQVAVIFA RTGELAHHDH GHVEGVDTED EGIDVLGSTF LKSPLTPRDL VEKPKDE // ID 3MGH_SYNJB Reviewed; 192 AA. AC Q2JI31; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 08-FEB-2011, entry version 31. DE RecName: Full=Putative 3-methyladenine DNA glycosylase; DE EC=3.2.2.-; GN OrderedLocusNames=CYB_2817; OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium OS Yellowstone B-Prime). SQ SEQUENCE 192 AA; 21330 MW; 71CAF20F5D810045 CRC64; MEWLSQPAPL VAPALLGMVL VRQFADGLQV RAQIVETEAY TAGDPACHAY RRKTQRNQVM FGPPGHLYIY RIYGLYHCLN IVTEPEGIPA AVLIRAAQLD RLPDWIPANK QNQPARAAAG PGLLCQALRI DGSHNGWRLE RAEAGQEGIW LEGSPSWQTQ LSIVQTTRIG ITQGAEIPWR WYIGGHPAVS RY // Swissknife_1.75/t/test.pl0000644005110600510130000000072310366115237015636 0ustar ecastroSwissProt#!/bin/env perl # ************************************************************* # # Purpose: # Run tests on Swissknife # # Usage: # test.pl list_of_test_scripts # # ************************************************************* # BEGIN { unless(grep /blib/, @INC) { chdir 't' if -d 't'; unshift @INC, '../lib' if -d '../lib'; } } use Test::Harness; print STDERR "*** Swissknife test suite ***\n\n"; @ARGV = sort <*.t> unless @ARGV; runtests(@ARGV); Swissknife_1.75/t/fasta.t0000644005110600510130000000152310500233441015570 0ustar ecastroSwissProt# Test for FASTA output use Carp; # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END { print "not ok 1\n" unless $loaded; } $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}fasta.txl"; my $testout = "${where}fasta.txl.out"; my $expectedout = "${where}fasta.txl.expected"; open (IN, $testin); open (OUT, ">$testout"); use SWISS::Entry; use Data::Dumper; # Read an entire record at a time $/ = "\/\/\n"; while (){ $entry = SWISS::Entry->fromText($_); print OUT $entry->toFasta(); } close IN; close OUT; print "checking expected output...\n"; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; Swissknife_1.75/t/identity.txl.expected0000644005110600510130000313713313133402155020506 0ustar ecastroSwissProtID O43499 Unreviewed; 480 AA. AC O43499; O08291; O08202; O08292; O08203; O08293; O08204; O08294; AC O08205; O08295; O08206; O08296; O08207; O08297; O08208; O08298; AC O08209; O08299; O08210; O08300; O08211; O08301; O08212; O08302; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE HTGN51. GN TGN. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=126566, 55{E2}; RN [1] RP SEQUENCE FROM N.A. RA Kain R., Angata K., Kerjaschki D., Fukuda M.; RL J. Biol. Chem. 273:0-0(1998). DR EMBL; AF029316; AAB96908.1; -. DR EMBL; AF029313; AAB96908.1; JOINED. DR EMBL; AF029314; AAB96908.1; JOINED. DR EMBL; AF029315; AAB96908.1; JOINED. KW Zinc-finger; Receptor; Transcription regulation; DNA-binding; KW Nuclear protein. ** ** ################# SOURCE SECTION ################## ** Homo sapiens trans-golgi network glycoprotein (TGN) gene, exon 4, ** and complete cds. ** [1] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** "Molecular Cloning and Expression of a Novel Human Trans-Golgi Network ** Glycoprotein, TGN51, that Contains Multiple Tyrosine-containing ** Motifs"; ** J. Biol. Chem. 273:0-0(1998). ** [2] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** ; ** Submitted (09-OCT-1997) to the EMBL/GenBank/DDBJ databases. ** Glycobiology Program, The Burnham Institute, 10901 N. Torrey Pines Rd, ** La Jolla, CA 92037, USA ** source 1..2563 ** /organism="Homo sapiens" ** /chromosome="2" ** /note="sequence from P1 plasmid 10508" ** /map="2p11.2" ** CDS ** join(AF029313:63..108,AF029314:1..1178,AF029315:278..361, ** 210..344) ** /codon_start=1 ** /db_xref="PID:g2772928" ** /note="trans-golgi network glycoprotein" ** /gene="TGN" ** /product="hTGN51" ** CDS_IN_EMBL_ENTRY 3 ** 20-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 480 AA; 50993 MW; 8CAE4EE663B7225D CRC64; MRFVVALVLV NVAAAGAVPL LATESVKQEE AGVRPSAGNV STHPSLSQRP GGSTKSHPEP QTPKDSPSKS SAEAQTPEDT PNKSGGEAKT LKDSSNKSGA EAQTPKGSTS KSGSEAQTTK DSTSKSHPEL QTPKDSTGKS GAEAQTPEDS PNRSGAEPKT QKDSPSKSGS EAQTTKDVPN KSGADGQTPK DGSSKSGAED QTPKDVPNKS GAEKQTPKDG SNKSGAEEQG PIDGPSKSGA EEQTSKDSPN KVVPEQPSRK DHSKPISNPS DNKELPKADT NQLADKGKLS PHAFKTESGE ETDLISPPQE EVKSSEPTED VGPKEAEDDD TGPEEGSPPK EEKEKMSGSA SSENREGTLS DSTGSEKDDL YPNGSGNGSA ESSHFFAYLV TAAILVAVLY IAHHNKRKII AFVLEGKRSK VTRRPKASDY QRLDQKYVLI LNVFPAPPKR SFLPQVLTEW YIPLEKDERH QWIVLLSFQL // ID O43500 PRELIMINARY; PRT; 437 AA. AC O43500; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE HTGN46. GN TGN. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Kain R., Angata K., Kerjaschki D., Fukuda M.; RL J. Biol. Chem. 273:0-0(1998). DR EMBL; AF029316; AAB96906.1; -. DR EMBL; AF029313; AAB96906.1; JOINED. DR EMBL; AF029314; AAB96906.1; JOINED. DR EMBL; AF029315; AAB96906.1; JOINED. ** ** ################# SOURCE SECTION ################## ** Homo sapiens trans-golgi network glycoprotein (TGN) gene, exon 4, ** and complete cds. ** [1] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** "Molecular Cloning and Expression of a Novel Human Trans-Golgi Network ** Glycoprotein, TGN51, that Contains Multiple Tyrosine-containing ** Motifs"; ** J. Biol. Chem. 273:0-0(1998). ** [2] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** ; ** Submitted (09-OCT-1997) to the EMBL/GenBank/DDBJ databases. ** Glycobiology Program, The Burnham Institute, 10901 N. Torrey Pines Rd, ** La Jolla, CA 92037, USA ** source 1..2563 ** /organism="Homo sapiens" ** /chromosome="2" ** /note="sequence from P1 plasmid 10508" ** /map="2p11.2" ** CDS ** join(AF029313:63..108,AF029314:1..1178,AF029315:278..361, ** 268..273) ** /codon_start=1 ** /db_xref="PID:g2772926" ** /note="trans-golgi network glycoprotein" ** /gene="TGN" ** /product="hTGN46" ** CDS_IN_EMBL_ENTRY 3 ** 20-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 437 AA; 45759 MW; 14B21554256E983B CRC64; MRFVVALVLV NVAAAGAVPL LATESVKQEE AGVRPSAGNV STHPSLSQRP GGSTKSHPEP QTPKDSPSKS SAEAQTPEDT PNKSGGEAKT LKDSSNKSGA EAQTPKGSTS KSGSEAQTTK DSTSKSHPEL QTPKDSTGKS GAEAQTPEDS PNRSGAEPKT QKDSPSKSGS EAQTTKDVPN KSGADGQTPK DGSSKSGAED QTPKDVPNKS GAEKQTPKDG SNKSGAEEQG PIDGPSKSGA EEQTSKDSPN KVVPEQPSRK DHSKPISNPS DNKELPKADT NQLADKGKLS PHAFKTESGE ETDLISPPQE EVKSSEPTED VGPKEAEDDD TGPEEGSPPK EEKEKMSGSA SSENREGTLS DSTGSEKDDL YPNGSGNGSA ESSHFFAYLV TAAILVAVLY IAHHNKRKII AFVLEGKRSK VTRRPKASDY QRLDQKS // ID O43501 PRELIMINARY; PRT; 453 AA. AC O43501; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE HTGN48. GN TGN. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Kain R., Angata K., Kerjaschki D., Fukuda M.; RL J. Biol. Chem. 273:0-0(1998). DR EMBL; AF029316; AAB96907.1; -. DR EMBL; AF029313; AAB96907.1; JOINED. DR EMBL; AF029314; AAB96907.1; JOINED. DR EMBL; AF029315; AAB96907.1; JOINED. ** ** ################# SOURCE SECTION ################## ** Homo sapiens trans-golgi network glycoprotein (TGN) gene, exon 4, ** and complete cds. ** [1] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** "Molecular Cloning and Expression of a Novel Human Trans-Golgi Network ** Glycoprotein, TGN51, that Contains Multiple Tyrosine-containing ** Motifs"; ** J. Biol. Chem. 273:0-0(1998). ** [2] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** ; ** Submitted (09-OCT-1997) to the EMBL/GenBank/DDBJ databases. ** Glycobiology Program, The Burnham Institute, 10901 N. Torrey Pines Rd, ** La Jolla, CA 92037, USA ** source 1..2563 ** /organism="Homo sapiens" ** /chromosome="2" ** /note="sequence from P1 plasmid 10508" ** /map="2p11.2" ** CDS ** join(AF029313:63..108,AF029314:1..1178,AF029315:278..361, ** 251..304) ** /codon_start=1 ** /db_xref="PID:g2772927" ** /note="trans-golgi network glycoprotein" ** /gene="TGN" ** /product="hTGN48" ** CDS_IN_EMBL_ENTRY 3 ** 20-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 453 AA; 47578 MW; 13F70172177BFE82 CRC64; MRFVVALVLV NVAAAGAVPL LATESVKQEE AGVRPSAGNV STHPSLSQRP GGSTKSHPEP QTPKDSPSKS SAEAQTPEDT PNKSGGEAKT LKDSSNKSGA EAQTPKGSTS KSGSEAQTTK DSTSKSHPEL QTPKDSTGKS GAEAQTPEDS PNRSGAEPKT QKDSPSKSGS EAQTTKDVPN KSGADGQTPK DGSSKSGAED QTPKDVPNKS GAEKQTPKDG SNKSGAEEQG PIDGPSKSGA EEQTSKDSPN KVVPEQPSRK DHSKPISNPS DNKELPKADT NQLADKGKLS PHAFKTESGE ETDLISPPQE EVKSSEPTED VGPKEAEDDD TGPEEGSPPK EEKEKMSGSA SSENREGTLS DSTGSEKDDL YPNGSGNGSA ESSHFFAYLV TAAILVAVLY IAHHNKRKII AFVLEGKRSK VTRRPKASDY QRLDQKIFSP PSPNRMVYSS GKR // ID O43530 PRELIMINARY; PRT; 456 AA. AC O43530; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE NBMPR-INSENSITIVE NUCLEOSIDE TRANSPORTER EI. GN ENT2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Crawford C.R., Patel D.H., Naeve C.W., Belt J.A.; RL J. Biol. Chem. 273:0-0(1998). DR EMBL; AF034102; AAB97834.1; -. DR InterPro; IPR002259; -. DR PFAM; PF01733; Nucleoside_tran; 1. DR PRINTS; PR01130; DERENTRNSPRT. DR PRODOM; PD005103; -; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens NBMPR-insensitive nucleoside transporter ei (ENT2) ** mRNA, complete cds. ** [1] ** 1-2522 ** Crawford C.R., Patel D.H., Naeve C.W., Belt J.A.; ** "Cloning of the Human Equilibrative, Nitrobenzylmercaptopurineriboside ** (NBMPR)-Insensitive Nucleoside Transporter ei by Functional Expression ** in a Transport-Deficient Cell Line"; ** J. Biol. Chem. 273:0-0(1998). ** [2] ** 1-2522 ** Crawford C.R., Naeve C.W., Belt J.A.; ** ; ** Submitted (11-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Molecular Pharmacology, St. Jude Children's Research Hospital, 332 N. ** Lauderdale, Memphis, TN 38105, USA ** for description of the isolation and properties of the cDNA, see ** Crawford, et al, Proc. Annu. Meet. Am. Assoc. Cancer Res., 38:A406, ** 1997 (abstract). ** source 1..2522 ** /organism="Homo sapiens" ** /cell_line="HeLa S3; ATCC CCL2.2" ** /clone_lib="Clonetech HL1152y" ** CDS 238..1608 ** /codon_start=1 ** /db_xref="PID:g2811137" ** /note="plasma membrane transport protein" ** /gene="ENT2" ** /function="mediates equilibrative transport of purine ** and ** pyrimidine nucleosides, and the purine base ** hypoxanthine" ** /product="NBMPR-insensitive nucleoside transporter ei" ** CDS_IN_EMBL_ENTRY 1 ** 28-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PRODOM; PD005103; PD005103; 131; 456; T; 19-JUN-2000; **PM PFAM; PF01733; Nucleoside_tran; 131; 454; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 137; 159; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 165; 185; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 191; 214; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 301; 318; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 333; 354; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 361; 378; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 393; 409; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 412; 428; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 430; 454; T; 19-JUN-2000; SQ SEQUENCE 456 AA; 50113 MW; ABCBD244306708E1 CRC64; MARGDAPRDS YHLVGISFFI LGLGTLLPWN FFITAIPYFQ ARLAGAGNST ARILSTNHTG PEDAFNFNNW VTLLSQLPLL LFTLLNSFLY QCVPETVRIL GSLLAILLLF ALTAALVKVD MSPGPFFSIT MASVCFINSF SAVLQGSLFG QLGTMPSTYS TLFLSGQGLA GIFAALAMLL SMASGVDAET SALGYFITPC VGILMSIVCY LSLPHLKFAR YYLANKSSQA QAQELETKAE LLQSDENGIP SSPQKVALTL DLDLEKEPES EPDEPQKPGK PSVFTVFQKI WLTALCLVLV FTVTLSVFPA ITAMVTSSTS PGKWSQFFNP ICCFLLFNIM DWLGRSLTSY FLWPDEDSRL LPLLVCLRFL FVPLFMLCHV PQRSRLPILF PQDAYFITFM LLFAVSNGYL VSLTMCLAPR QVLPHEREVA GALMTFFLAL GLSCGASLSF LFKALL // ID O43534 PRELIMINARY; PRT; 377 AA. AC O43534; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE NATURAL KILLER CELL INHIBITORY RECEPTOR. GN KIR2DL4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Valiant N.M., Uhrberg M., Shilling H.G., Lienert-Weidenbach K., RA Arnett K.L., D'Andrea A., Phillips J.H., Lanier L.L., Parham P.; RL Immunity 0:0-0(1997). RN [2] RP SEQUENCE FROM N.A. RA Uhrberg M., Valiant N.M., Shum B., Shilling H.G., RA Lienert-Weidenbach K., Corliss B., Tyan D., Lanier L.L., Parham P.; RL Immunity 0:0-0(1998). DR EMBL; AF034773; AAB95166.1; -. DR InterPro; IPR003006; -. DR Pfam; PF00047; ig; 2. DR HSSP; P43626; 1NKR. ** ** ################# SOURCE SECTION ################## ** Homo sapiens natural killer cell inhibitory receptor (KIR2DL4) ** mRNA, variant 3, complete cds. ** [1] ** 1-1179 ** Valiant N.M., Uhrberg M., Shilling H.G., Lienert-Weidenbach K., ** Arnett K.L., D'Andrea A., Phillips J.H., Lanier L.L., Parham P.; ** "Functionally and Structurally Distinct NK Cell Receptor Repertoires ** in ** the Peripheral Blood of Two Human Donors"; ** Immunity 0:0-0(1997). ** [2] ** 1-1179 ** Uhrberg M., Valiant N.M., Shum B., Shilling H.G., Lienert-Weidenbach ** K., ** Corliss B., Tyan D., Lanier L.L., Parham P.; ** "Human Diversity in Killer Cell Inhibitory Receptor (KIR) Genes"; ** Immunity 0:0-0(1998). ** [3] ** 1-1179 ** Shilling H.G.; ** ; ** Submitted (17-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Structural Biology, Stanford University, Sherman Fairchild Building, ** Stanford University School of Medicine, Stanford, CA 94305-5400, USA ** source 1..1179 ** /organism="Homo sapiens" ** /cell_type="peripheral blood" ** CDS 7..1140 ** /codon_start=1 ** /db_xref="PID:g2739182" ** /gene="KIR2DL4" ** /product="natural killer cell inhibitory receptor" ** CDS_IN_EMBL_ENTRY 1 ** 09-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00047; ig; 44; 99; T; 19-JUN-2000; **PM PFAM; PF00047; ig; 139; 197; T; 19-JUN-2000; SQ SEQUENCE 377 AA; 41426 MW; 969DA8DB9872F4B6 CRC64; MSMSPTVIIL ACLGFFLDQS VWAHVGGQDK PFCSAWPSAV VPQGGHVTLR CHCRRGFNIF TLYKKDGVPV PELYNRIFWN SFLISPVTPA HAGTYRCRGF HPHSPTEWSA PSNPLVIMVT GLYEKPSLTA RPGPTVRAGE NVTLSCSSQS SFDIYHLSRE GEAHELRLPA VPSINGTFQA DFPLGPATHG ETYRCFGSFH GSPYEWSDPS DPLPVSVTGN PSSSWPSPTE PSFKTGIARH LHAVIRYSVA IILFTILPFF LLHRWCSKKK NAAVMNQEPA GHRTVNREDS DEQDPQEVTY AQLDHCIFTQ RKITGPSQRS KRPSTDTSVC IELPNAEPRA LSPAHEHHSQ ALMGSSRETT ALSQTQLASS NVPAAGI // ID O43538 PRELIMINARY; PRT; 653 AA. AC O43538; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE AMPHIPHYSIN I. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BREAST; RA Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., RA Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.; RL Mol. Med. (Camb. Mass.) 0:0-0(1998). DR EMBL; AF034996; AAC02977.1; -. DR INTERPRO; IPR001452; -. DR INTERPRO; IPR003005; -. DR INTERPRO; IPR003017; -. DR PFAM; PF00018; SH3; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01252; AMPHIPHYSIN1. DR PRINTS; PR00452; SH3DOMAIN. DR PROSITE; PS50002; SH3; 1. DR HSSP; P29355; 2SEM. ** ** ################# SOURCE SECTION ################## ** Homo sapiens amphiphysin I mRNA, alternative splice isoform, ** complete cds. ** [1] ** 1-3161 ** Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., ** Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.; ** "Expression of amphiphysin I, an autoantigen of paraneoplastic ** neurological syndromes, in breast cancer"; ** Mol. Med. (Camb. Mass.) 0:0-0(1998). ** [2] ** 1-3161 ** Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., ** Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.; ** ; ** Submitted (18-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Cell Biology, Yale University, 295 Congress Avenue, New Haven, CT ** 06510, ** USA ** source 1..3161 ** /organism="Homo sapiens" ** /cell_line="Hs578T" ** /tissue_type="breast" ** CDS 70..2031 ** /codon_start=1 ** /db_xref="PID:g2895528" ** /note="alternative splice isoform" ** /product="amphiphysin I" ** CDS_IN_EMBL_ENTRY 1 ** 20-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00018; SH3; 583; 652; T; 19-JUN-2000; **PM PRINTS; PR00452; SH3DOMAIN; 583; 593; T; 19-JUN-2000; **PM PRINTS; PR00452; SH3DOMAIN; 597; 612; T; 19-JUN-2000; **PM PRINTS; PR00452; SH3DOMAIN; 619; 628; T; 19-JUN-2000; **PM PRINTS; PR00452; SH3DOMAIN; 640; 652; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 23; 40; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 51; 61; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 83; 95; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 118; 132; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 140; 151; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 175; 184; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 186; 196; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 576; 585; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 597; 611; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 3; 11; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 93; 104; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 220; 234; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 235; 246; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 247; 258; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 386; 396; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 632; 643; T; 19-JUN-2000; **PM PROSITE; PS50002; SH3; 580; 653; T; 19-JUN-2000; SQ SEQUENCE 653 AA; 71929 MW; 44C1115E3E70B6A9 CRC64; MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF EEFNVDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD KAFTIQGAPS DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPAR PRSPSQTRKG PPVPPLPKVT PTKELQQENI ISFFEDNFVP EISVTTPSQN EVPEVKKEET LLDLDFDPFK PEVTPAGSAG VTHSPMSQTL PWDLWTTSTD LVQPASGGSF NGFTQPQDTS LFTMQTDQSM ICNLIIPGAD ADAAVGTLVS AAEGAPGEEA EAEKATVPAG EGVSLEEAKI GTETTEGAES AQPEAEELEA TVPQEKVIPS VVIEPASNHE EEGENEITIG AEPKETTEDA APPGPTSETP ELATEQKPIQ DPQPTPSAPA MGAADQLASA REASQELPPG FLYKVETLHD FEAANSDELT LQRGDVVLVV PSDSEADQDA GWLVGVKESD WLQYRDLATY KGLFPENFTR RLD // ID O43541 PRELIMINARY; PRT; 496 AA. AC O43541; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE SMAD6. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Hata A., Lagna G., Massague J., Hemmati-Brivanlou A.; RL Genes Dev. 0:0-0(1997). DR EMBL; AF035528; AAB94137.1; -. DR INTERPRO; IPR001132; -. DR PFAM; PF00968; Dwarfin; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens Smad6 mRNA, complete cds. ** [1] ** 1-2887 ** Hata A., Lagna G., Massague J., Hemmati-Brivanlou A.; ** "Smad6 inhibits BMP/Smad1 signaling by specifically competing with the ** Smad4 tumor suppressor"; ** Genes Dev. 0:0-0(1997). ** [2] ** 1-2887 ** Hata A., Lagna G., Massague J., Hemmati-Brivanlou A.; ** ; ** Submitted (21-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Laboratory of Molecular Embryology, The Rockefeller University, 1230 ** York Avenue, New York, NY 10021, USA ** source 1..2887 ** /organism="Homo sapiens" ** /cell_line="Jurkat T-cell" ** CDS 937..2427 ** /codon_start=1 ** /db_xref="PID:g2736316" ** /note="SMAD family member" ** /function="inhibitor of BMP signaling" ** /product="Smad6" ** CDS_IN_EMBL_ENTRY 1 ** 07-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00968; Dwarfin; 132; 495; T; 19-JUN-2000; SQ SEQUENCE 496 AA; 53496 MW; 4D50B634D8911B37 CRC64; MFRSKRSGLV RRLWRSRVVP NREEGGSGGG GGGDEDGSLG SRAEPAPRAR EGGGCGRSEV RPVAPRRPRD AVGQRGAQGA GRRRRAGGPP RPMSEPGAGA GSSLLDVAEP GGPGWLPESD CETVTCCLFS ERDAAGAPRD ASDPLAGAAL EPAGGGRSRE ARSRLLLLEQ ELKTVTYSLL KRLKERSLDT LLEAVESRGG VPGGCVLVPR ADLRLGGQPA PPQLLLGRLF RWPDLQHAVE LKPLCGCHSF AAAADGPTVC CNPYHFSRLC GPESPPPPYS RLSPRDEYKP LDLSDSTLSY TETEATNSLI TAPGEFSDAS MSPDATKPSH WCSVAYWEHR TRVGRLYAVY DQAVSIFYDL PQGSGFCLGQ LNLEQRSESV RRTRSKIGFG ILLSKEPDGV WAYNRGEHPI FVNSPTLDAP GGRALVVRKV PPGYSIKVFD FERSGLQHAP EPDAADGPYD PNSVRISFAK GWGPCYSRQF ITSCPCWLEI LLNNPR // ID O43545 PRELIMINARY; PRT; 179 AA. AC O43545; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE MESODERM-SPECIFIC BASIC-HELIX-LOOP-HELIX PROTEIN. GN POD1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Quaggin S.E., Vanden Heuvel G.B., Igarashi P.; RL Mech. Dev. 0:0-0(1997). DR EMBL; AF035718; AAC62514.1; -. DR INTERPRO; IPR001092; -. DR INTERPRO; IPR003015; -. DR PFAM; PF00010; HLH; 1. DR PROSITE; PS00038; HELIX_LOOP_HELIX; UNKNOWN_1. DR HSSP; P10085; 1MDY. ** ** ################# SOURCE SECTION ################## ** Homo sapiens mesoderm-specific basic-helix-loop-helix protein ** (POD1) mRNA, complete cds. ** [1] ** 1-1254 ** Quaggin S.E., Vanden Heuvel G.B., Igarashi P.; ** "Pod-1, A Mesoderm-Specific Basic-Helix-Loop-Helix Protein Expressed ** in ** Mesenchymal and Glomerular Epithelial Cells in the Developing Kidney"; ** Mech. Dev. 0:0-0(1997). ** [2] ** 1-1254 ** Quaggin S.E., Vanden Heuvel G.B., Igarashi P.; ** ; ** Submitted (24-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Internal Medicine, Yale University, 333 Cedar Street, New Haven, CT ** 06520-8029, USA ** source 1..1254 ** /organism="Homo sapiens" ** /chromosome="6" ** CDS 261..800 ** /codon_start=1 ** /db_xref="PID:g2745887" ** /note="Pod-1" ** /gene="POD1" ** /product="mesoderm-specific basic-helix-loop-helix ** protein" ** misc_feature 492..653 ** /note="encodes basic-helix-loop-helix domain" ** /gene="POD1" ** AA 78 -> 131 ** CDS_IN_EMBL_ENTRY 1 ** 08-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00010; HLH; 80; 132; T; 19-JUN-2000; **PM PROSITE; PS00038; HELIX_LOOP_HELIX; 116; 131; ?; 19-JUN-2000; **PM PROSITE; PS50037; HELIX_LOOP_HELIX_2; 89; 129; T; 19-JUN-2000; SQ SEQUENCE 179 AA; 19743 MW; 9B6F496C4A6B658A CRC64; MSTGSLSDVE DLQEVEMLEC DGLKMDSNKE FVTSNESTEE SSNCENGSPQ KGRGGLGKRR RAPTKKSPLS GVSQEGKQVQ RNAANARERA RMRVLSKAFS RLKTTLPWVP PDTKLSKLDT LRLASSYIAH LRQILANDKY ENGYIHPVNL TWPFMVAGKP ESDLKEVVTA SRLCGTTAS // ID O43547 PRELIMINARY; PRT; 232 AA. AC O43547; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE VESICLE SOLUBLE NSF ATTACHMENT PROTEIN RECEPTOR. GN VTI1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98112804; PubMed=9446565; RA Fischer von Mollard G., Stevens T.H.; RT "A human homolog can functionally replace the yeast vesicle-associated RT SNARE Vti1p in two vesicle transport pathways."; RL J. Biol. Chem. 273:2624-2630(1998). DR EMBL; AF035824; AAC52016.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens vesicle soluble NSF attachment protein receptor (VTI1) ** mRNA, complete cds. ** [1] ** 1-935 ** Fischer von Mollard G., Stevens T.H.; ** "A human homolog can functionally replace the yeast v-SNARE Vti1p in ** two ** vesicle transport pathways"; ** J. Biol. Chem. 273:2624-2630(1998). ** [2] ** 1-935 ** Fischer von Mollard G., Stevens T.H.; ** ; ** Submitted (25-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Institute of Molecular Biology, University of Oregon, Eugene, OR ** 97403, ** USA ** source 1..935 ** /organism="Homo sapiens" ** CDS 72..770 ** /codon_start=1 ** /db_xref="PID:g2687400" ** /note="Vti1; v-SNARE" ** /gene="VTI1" ** /product="vesicle soluble NSF attachment protein ** receptor" ** CDS_IN_EMBL_ENTRY 1 ** 05-FEB-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 232 AA; 26687 MW; E34B62215F5F1EDC CRC64; MASSAASSEH FEKLHEIFRG LHENLQGVPE RLLGTAGTEE KKKLIRDFDE KQQEANETLA EMEEELRYAP LSFRNPMMSK LRNYRKDLAK LHREVRSTPL TATPGGRGDM KYGIYAVENE HMNRLQSQRA MLLQGTESLN RATQSIERSH RIATETDQIG SEIIEELGEQ RDQLERTKSR LVNTSENLSK SRKILRSMSR KVTTNKLLLS IIILLELAIL GGLVYYKFFR SH // ID O43557 PRELIMINARY; PRT; 240 AA. AC O43557; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE TUMOR NECROSIS FACTOR SUPERFAMILY MEMBER LIGHT. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98122340; PubMed=9462508; RA Mauri D.N., Ebner R., Montgomery R.I., Kochel K.D., Cheung T.C., RA Yu G.-L., Ruben S., Murphy M., Eisenberg R.J., Cohen G.H., Spear P.G., RA Ware C.F.; RT "LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha are RT ligands for herpesvirus entry mediator."; RL Immunity 8:21-30(1998). DR EMBL; AF036581; AAC39563.1; -. DR INTERPRO; IPR000478; -. DR PFAM; PF00229; TNF; 1. DR PROSITE; PS50049; TNF_2; 1. DR HSSP; P01375; 4TSV. ** ** ################# SOURCE SECTION ################## ** Homo sapiens tumor necrosis factor superfamily member LIGHT mRNA, ** complete cds. ** [1] ** 1-1169 ** Mauri D.N., Ebner R., Montgomery R.I., Kochel K.D., Cheung T.C., ** Yu G.-L., Ruben S., Murphy M., Eisenberg R.J., Cohen G.H., Spear P.G., ** Ware C.F.; ** "LIGHT, a new member of the TNF superfamily, and lymphotoxin (LT)a are ** ligands for herpesvirus entry mediator (HVEM)"; ** Immunity 8:21-30(1998). ** [2] ** 1-1169 ** Ebner R., Kochel K.D., Ware C.F.; ** ; ** Submitted (02-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Division of Molecular Immunology, La Jolla Institute for Allergy and ** Immunology, 10355 Science Center Drive, San Diego, CA 92121, USA ** source 1..1169 ** /organism="Homo sapiens" ** /chromosome="16" ** /cell_type="peripheral blood mononuclear cells ** activated ** with phorbol ester and phytohemagglutinin for 12 hr" ** CDS 49..771 ** /codon_start=1 ** /db_xref="PID:g2815624" ** /function="ligand for herpesvirus entry mediator ** (HVEM) and ** lymphotoxin-beta receptor (LTbR)" ** /product="tumor necrosis factor superfamily member ** LIGHT" ** CDS_IN_EMBL_ENTRY 1 ** 31-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00229; TNF; 93; 240; T; 19-JUN-2000; **PM PROSITE; PS50049; TNF_2; 95; 240; T; 19-JUN-2000; SQ SEQUENCE 240 AA; 26351 MW; 49D0BF67E1390B39 CRC64; MEESVVRPSV FVVDGQTDIP FTRLGRSHRR QSCSVARVGL GLLLLLMGAG LAVQGWFLLQ LHWRLGEMVT RLPDGPAGSW EQLIQERRSH EVNPAAHLTG ANSSLTGSGG PLLWETQLGL AFLRGLSYHD GALVVTKAGY YYIYSKVQLG GVGCPLGLAS TITHGLYKRT PRYPEELELL VSQQSPCGRA TSSSRVWWDS SFLGGVVHLE AGEEVVVRVL DERLVRLRDG TRSYFGAFMV // ID O43561 PRELIMINARY; PRT; 262 AA. AC O43561; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE LINKER FOR ACTIVATION OF T CELLS (LAT). GN LAT. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; RL Cell 0:0-0(1997). DR EMBL; AF036906; AAC39637.1; -. DR INTERPRO; IPR000345; -. DR PROSITE; PS00190; CYTOCHROME_C; UNKNOWN_1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens linker for activation of T cells (LAT) mRNA, ** alternatively spliced form, complete cds. ** [1] ** 1-1460 ** Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; ** "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor ** to ** cellular activation"; ** Cell 0:0-0(1997). ** [2] ** 1-1460 ** Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; ** ; ** Submitted (05-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Cell Biology and Metabolism Branch, National Institute of Child Health ** and Development, National Institute of Health, 9000 Rockville Pike, ** Bethesda, MD 20892, USA ** LAT is a highly tyrosine phosphorylated protein, previously ** described as p36-38, and it associates with many signaling ** molecules, such as Grb2, PLC-gamma1, PI-3 kinase, cbl, Vav, and ** SLP-76, either directly or indirectly upon T cell activation. It is ** a potential type III transmembrane protein. ** source 1..1460 ** /organism="Homo sapiens" ** /cell_line="Jurkat T cells" ** CDS 79..867 ** /codon_start=1 ** /db_xref="PID:g2828026" ** /note="tyrosine kinase substrate; This a alternatively ** spliced form of LAT" ** /gene="LAT" ** /product="LAT" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS00190; CYTOCHROME_C; 26; 31; ?; 19-JUN-2000; SQ SEQUENCE 262 AA; 27930 MW; BCD80AE7DCA64153 CRC64; MEEAILVPCV LGLLLLPILA MLMALCVHCH RLPGSYDSTS SDSLYPRGIQ FKRPHTVAPW PPAYPPVTSY PPLSQPDLLP IPRSPQPLGG SHRTPSSRRD SDGANSVASY ENEGASGIRG AQAGWGVWGP SWTRLTPVSL PPEPACEDAD EDEDDYHNPG YLVVLPDSTP ATSTAAPSAP ALSTPGIRDS AFSMESIDDY VNVPESGESA EASLDGSREY VNVSQELHPG AAKTEPAALS SQEAEEVEEE GAPDYENLQE LN // ID O43562 PRELIMINARY; PRT; 424 AA. AC O43562; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE ORGANIC CATION TRANSPORTER-LIKE PROTEIN 2. GN ORCTL2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Cooper P.R., Smilinich N.J., Day C.D., Nowak N.J., Reid L.H., RA Pearsall R.S., Reece M., Prawitt D., Landers J., Housman D.E., RA Winterpacht A., Zabel B.U., Pelletier J., Weissman B.E., Shows T.B., RA Higgins M.J.; RL Genomics 0:0-0(1998). DR EMBL; AF037064; AAC04787.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens organic cation transporter-like protein 2 (ORCTL2) ** mRNA, complete cds. ** [1] ** 1-1535 ** Cooper P.R., Smilinich N.J., Day C.D., Nowak N.J., Reid L.H., ** Pearsall R.S., Reece M., Prawitt D., Landers J., Housman D.E., ** Winterpacht A., Zabel B.U., Pelletier J., Weissman B.E., Shows T.B., ** Higgins M.J.; ** "Divergently transcribed overlapping genes expressed in liver and ** kidney ** and located in the 11p15.5 imprinted domain"; ** Genomics 0:0-0(1998). ** [2] ** 1-1535 ** Cooper P.R., Shows T.B., Pelletier J., Landers J., Higgins M.J.; ** ; ** Submitted (08-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Human Genetics, Roswell Park Cancer Institute, Elm and Carlton ** Streets, ** Buffalo, NY 14263, USA ** source 1..1535 ** /organism="Homo sapiens" ** /chromosome="11" ** /map="11p15.5" ** CDS 203..1477 ** /codon_start=1 ** /db_xref="PID:g2921449" ** /note="predicted integral membrane protein functioning ** in ** organic cation transport. A second in frame ATG is ** present ** at position 251. In the mouse gene, the corresponding ** ATG ** is contained within a better translational context ** suggesting that translation may start at the second ** ATG in ** both cases" ** /gene="ORCTL2" ** /product="organic cation transporter-like protein 2" ** CDS_IN_EMBL_ENTRY 1 ** 10-MAR-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 424 AA; 44864 MW; 6EFD5F912A7761F5 CRC64; MQGARAPRDQ GRSPGRMSAL GRSSVILLTY VLAATELTCL FMQFSIVPYL SRKLGLDSIA FGYLQTTFGV LQLLGGPVFG RFADQRGARA ALTLSFLAAL ALYLLLAAAS SPALPGVYLL FASRLPGALM HTLPAAQMVI TDLSAPEERP AALGRLGLCF GVGVILGSLL GGTLVSAYGI QCPAILAALA TLLGAVLSFT CIPASTKGAK TDAQAPLPGG PRASVFDLKA IASLLRLPDV PRIFLVKVAS NCPTGLFMVM FSIISMDFFQ LEAAQAGYLM SFFGLLQMVT QGLVIGQLSS HFSEEVMLRA SVLVFIVVGL AMAWMSSVFH FCLLVPGLVF SLCTLNVVTD SMLIKAVSTS DTGTMLGLCA SVQPLLRTLG PTVGGLLYRS FGVPVFGHVQ VAINTLVLLV LWRKPMPQRK DKVR // ID O43568 PRELIMINARY; PRT; 346 AA. AC O43568; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE XRCC3. GN XRCC3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Liu N., Lamerdin J.E., Tebbs R.S., Schild D., Tucker J.D., Shen R., RA Brookman K.W., Siciliano M.J., Walter C.A., Fan W., Narayana L.S., RA Zhou Z.-Q., Adamson A.W., Sorenson K.J., Chen D.J., Jones N.J., RA Thompson L.H.; RL Mol. Cell 0:0-0(1998). DR EMBL; AF037222; AAC04805.1; -. DR INTERPRO; IPR001553; -. ** ** ################# SOURCE SECTION ################## ** Human DNA from chromosome 14-specific cosmid containing XRCC3 DNA ** repair gene, genomic sequence, complete sequence. ** [1] ** 1-36628 ** Liu N., Lamerdin J.E., Tebbs R.S., Schild D., Tucker J.D., Shen R., ** Brookman K.W., Siciliano M.J., Walter C.A., Fan W., Narayana L.S., ** Zhou Z.-Q., Adamson A.W., Sorenson K.J., Chen D.J., Jones N.J., ** Thompson L.H.; ** "XRCC2 and XRCC3, New Members of the Rad51 Family, Promote Chromosome ** Stability and Protect Against DNA Damages"; ** Mol. Cell 0:0-0(1998). ** [2] ** 1-36628 ** Lamerdin J.E.; ** ; ** Submitted (08-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Human Genome Center, Lawrence Livermore National Laboratory, 7000 East ** Ave., Livermore, CA 94551, USA ** source 1..36628 ** /organism="Homo sapiens" ** /chromosome="14" ** /note="cosmid from library constructed at LANL from ** flow-sorted material containing chromosome 14 as the ** only ** human chromosome" ** /clone="hsXRCC3GEN" ** /map="14q32.3" ** CDS join(6396..6450,8824..8961,10268..10480,14156..14310, ** 17907..18119,18304..18350,18465..18684) ** /codon_start=1 ** /db_xref="PID:g2921500" ** /note="DNA repair protein" ** /gene="XRCC3" ** /product="XRCC3" ** CDS_IN_EMBL_ENTRY 1 ** 10-MAR-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS50162; RECA_1; 78; 263; T; 19-JUN-2000; SQ SEQUENCE 346 AA; 37880 MW; C531EAE5F307C0E3 CRC64; MDLDLLDLNP RIIAAIKKAK LKSVKEVLHF SGPDLKRLTN LSSPEVWHLL RTASLHLRGS SILTALQLHQ QKERFPTQHQ RLSLGCPVLD ALLRGGLPLD GITELAGRSS AGKTQLALQL CLAVQFPRQH GGLEAGAVYI CTEDAFPHKR LQQLMAQQPR LRTDVPGELL QKLRFGSQIF IEHVADVDTL LECVNKKVPV LLSRGMARLV VIDSVAAPFR CEFDSQASAP RARHLQSLGA MLRELSSAFQ SPVLCINQVT EAMEEQGAAH GPLGFWDERV SPALGITWAN QLLVRLLADR LREEEAALGC PARTLRVLSA PHLPPSSCSY TISAEGVRGT PGTQSH // ID O43574 PRELIMINARY; PRT; 777 AA. AC O43574; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE BRCA1-ASSOCIATED RING DOMAIN PROTEIN. GN BARD1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Thai T.H., Du F., Tsan J.T., Jin Y., Phung A., Spillman M.A., RA Massa H.F., Muller C.Y., Ashfaq R., Mathis J.M., Miller D.S., RA Trask B.J., Baer R., Bowcock A.M.; RL Hum. Mol. Genet. 0:0-0(1998). CC -!- SIMILARITY: CONTAINS A C3HC4-CLASS ZINC FINGER. DR EMBL; AF038042; AAB99978.1; -. DR EMBL; AF038034; AAB99978.1; JOINED. DR EMBL; AF038035; AAB99978.1; JOINED. DR EMBL; AF038036; AAB99978.1; JOINED. DR EMBL; AF038037; AAB99978.1; JOINED. DR EMBL; AF038038; AAB99978.1; JOINED. DR EMBL; AF038039; AAB99978.1; JOINED. DR EMBL; AF038040; AAB99978.1; JOINED. DR EMBL; AF038041; AAB99978.1; JOINED. DR INTERPRO; IPR001357; -. DR INTERPRO; IPR001841; -. DR INTERPRO; IPR002110; -. DR PFAM; PF00023; ank; 3. DR PROSITE; PS00518; ZINC_FINGER_C3HC4; 1. DR HSSP; P25963; 1IKN. KW Zinc-finger. ** ** ################# SOURCE SECTION ################## ** Homo sapiens BRCA1-associated RING domain protein (BARD1) gene, ** exons 10, 11 and complete cds. ** [1] ** 1-4334 ** Thai T.H., Du F., Tsan J.T., Jin Y., Phung A., Spillman M.A., ** Massa H.F., Muller C.Y., Ashfaq R., Mathis J.M., Miller D.S., ** Trask B.J., Baer R., Bowcock A.M.; ** "Mutations in the BRCA1-associated RING domain (BARD1) gene in primary ** breast, ovarian and uterine cancers"; ** Hum. Mol. Genet. 0:0-0(1998). ** [2] ** 1-4334 ** Thai T.H., Du F., Tsan J.T., Jin Y., Phung A., Spillman M.A., ** Massa H.F., Muller C.Y., Ashfaq R., Mathis J.M., Miller D.S., ** Trask B.J., Baer R., Bowcock A.M.; ** ; ** Submitted (11-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Microbiology, UT Southwestern Medical Center, 6000 Harry Hines Blvd., ** Dallas, TX 75235, USA ** source 1..4334 ** /organism="Homo sapiens" ** /chromosome="2" ** /map="2q34-2q35" ** CDS join(AF038034:174..331,AF038035:2614..2670, ** AF038035:7289..7437,AF038036:621..1570,AF038037:451..531, ** AF038038:508..680,AF038039:548..656,AF038040:566..698, ** AF038041:226..318,519..616,2019..2351) ** /codon_start=1 ** /db_xref="PID:g2828068" ** /gene="BARD1" ** /product="BRCA1-associated RING domain protein" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00023; ank; 427; 459; T; 19-JUN-2000; **PM PFAM; PF00023; ank; 460; 492; T; 19-JUN-2000; **PM PFAM; PF00023; ank; 493; 525; T; 19-JUN-2000; **PM PROSITE; PS00518; ZINC_FINGER_C3HC4; 66; 75; T; 19-JUN-2000; **PM PROSITE; PS50088; ANK_REP; 427; 459; T; 19-JUN-2000; **PM PROSITE; PS50088; ANK_REP; 460; 492; T; 19-JUN-2000; **PM PROSITE; PS50088; ANK_REP; 493; 525; T; 19-JUN-2000; **PM PROSITE; PS50089; ZF_RING; 50; 86; T; 19-JUN-2000; **PM PROSITE; PS50172; BRCT_DOMAIN; 570; 653; T; 19-JUN-2000; **PM PROSITE; PS50172; BRCT_DOMAIN; 667; 777; T; 19-JUN-2000; **PM PROSITE; PS50297; ANK_REP_REGION; 427; 525; T; 19-JUN-2000; **RU RU000251; 22-JAN-1998. SQ SEQUENCE 777 AA; 86579 MW; 51DCB76574015D4D CRC64; MPDNRQPRNR QPRIRSGNEP RSAPAMEPDG RGAWAHSRAA LDRLEKLLRC SRCTNILREP VCLGGCEHIF CSNCVSDCIG TGCPVCYTPA WIQDLKINRQ LDSMIQLCSK LRNLLHDNEL SDLKEDKPRK SLFNDAGNKK NSIKMWFSPR SKKVRYVVSK ASVQTQPAIK KDASAQQDSY EFVSPSPPAD VSERAKKASA RSGKKQKKKT LAEINQKWNL EAEKEDGEFD SKEESKQKLV SFCSQPSVIS SPQINGEIDL LASGSLTESE CFGSLTEVSL PLAEQIESPD TKSRNEVVTP EKVCKNYLTS KKSLPLENNG KRGHHNRLSS PISKRCRTSI LSTSGDFVKQ TVPSENIPLP ECSSPPSCKR KVGGTSGSKN SNMSDEFISL SPGTPPSTLS SSSYRRVMSS PSAMKLLPNM AVKRNHRGET LLHIASIKGD IPSVEYLLQN GSDPNVKDHA GWTPLHEACN HGHLKVVELL LQHKALVNTT GYQNDSPLHD AAKNGHVDIV KLLLSYGASR NAVNIFGLRP VDYTDDESMK SLLLLPEKNE SSSASHCSVM NTGQRRDGPL VLIGSGLSSE QQKMLSELAV ILKAKKYTEF DSTVTHVVVP GDAVQSTLKC MLGILNGCWI LKFEWVKACL RRKVCEQEEK YEIPEGPRRS RLNREQLLPK LFDGCYFYLW GTFKHHPKDN LIKLVTAGGG QILSRKPKPD SDVTQTINTV AYHARPDSDQ RFCTQYIIYE DLCNYHPERV RQGKVWKAPS SWFIDCVMSF ELLPLDS // ID O43588 PRELIMINARY; PRT; 978 AA. AC O43588; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE GENERAL TRANSCRIPTION FACTOR 2-I. GN GTF2I. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., RA Francke U.; RL Hum. Mol. Genet. 0:0-0(1998). DR EMBL; AF038967; AAC08313.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens general transcription factor 2-I (GTF2I) mRNA, ** alternatively spliced product, complete cds. ** [1] ** 1-4423 ** Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., ** Francke U.; ** "A duplicated gene in the breakpoint regions of the 7q11.23 ** Williams-Beuren syndrome deletion encodes the initiator binding ** protein ** TFII-I and BAP-135, a phosphorylation target of Btk"; ** Hum. Mol. Genet. 0:0-0(1998). ** [2] ** 1-4423 ** Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., ** Francke U.; ** ; ** Submitted (18-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Howard Hughes Medical Institute, Stanford Medical Center, Beckman ** Center ** B201, Stanford, CA 94305, USA ** source 1..4423 ** /organism="Homo sapiens" ** /chromosome="7" ** /map="7q11.23" ** CDS 317..3253 ** /codon_start=1 ** /db_xref="PID:g2827203" ** /note="alternatively spliced" ** /gene="GTF2I" ** /product="general transcription factor 2-I" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 978 AA; 110280 MW; 1F006D480F0BE702 CRC64; MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ YNIQGSHHSS EGNEGTEMEV PAEDSTQHVP SETSEDPEVE VTIEDDDYSP PSKRPKANEL PQPPVPEPAN AGKRKVREFN FEKWNARITD LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE GLPEGIPFRR PSTYGIPRLE RILLAKERIR FVIKKHELLN STREDLQLDK PASGVKEEWY ARITKLRKMV DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR PELLTHSTTE VTQPRTNTPV KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK FVVKKPELVI SYLPPGMASK INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNNNPQTSA VRTPTQTNGS NVPFKPRGRE FSFEAWNAKI TDLKQKVENL FNEKCGEALG LKQAVKVPFA LFESFPEDFY VEGLPEGVPF RRPSTFGIPR LEKILRNKAK IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG VEDLNIIQVT IPDDDNERLS KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN PGCVVVDGMP PGVSFKAPSY LEISSMRRIL DSAEFIKFTV IRPFPGLVIN NQLVDQSESE GPVIQESAEP SQLEVPATEE IKETDGSSQI KQEPDPTW // ID O43589 PRELIMINARY; PRT; 977 AA. AC O43589; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE GENERAL TRANSCRIPTION FACTOR 2-I. GN GTF2I. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., RA Francke U.; RL Hum. Mol. Genet. 0:0-0(1998). DR EMBL; AF038968; AAC08314.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens general transcription factor 2-I (GTF2I) mRNA, ** alternatively spliced product, complete cds. ** [1] ** 1-4420 ** Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., ** Francke U.; ** "A duplicated gene in the breakpoint regions of the 7q11.23 ** Williams-Beuren syndrome deletion encodes the initiator binding ** protein ** TFII-I and BAP-135, a phosphorylation target of Btk"; ** Hum. Mol. Genet. 0:0-0(1998). ** [2] ** 1-4420 ** Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., ** Francke U.; ** ; ** Submitted (18-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Howard Hughes Medical Institute, Stanford Medical Center, Beckman ** Center ** B201, Stanford, CA 94305, USA ** source 1..4420 ** /organism="Homo sapiens" ** /chromosome="7" ** /map="7q11.23" ** CDS 317..3250 ** /codon_start=1 ** /db_xref="PID:g2827205" ** /note="alternatively spliced" ** /gene="GTF2I" ** /product="general transcription factor 2-I" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 977 AA; 110106 MW; 418D59EC623E6141 CRC64; MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDDDYSPP SKRPKANELP QPPVPEPANA GKRKVREFNF EKWNARITDL RKQVEELFER KYAQAIKAKG PVTIPYPLFQ SHVEDLYVEG LPEGIPFRRP STYGIPRLER ILLAKERIRF VIKKHELLNS TREDLQLDKP ASGVKEEWYA RITKLRKMVD QLFCKKFAEA LGSTEAKAVP YQKFEAHPND LYVEGLPENI PFRSPSWYGI PRLEKIIQVG NRIKFVIKRP ELLTHSTTEV TQPRTNTPVK EDWNVRITKL RKQVEEIFNL KFAQALGLTE AVKVPYPVFE SNPEFLYVEG LPEGIPFRSP TWFGIPRLER IVRGSNKIKF VVKKPELVIS YLPPGMASKI NTKALQSPKR PRSPGSNSKV PEIEVTVEGP NNNNPQTSAV RTPTQTNGSN VPFKPRGREF SFEAWNAKIT DLKQKVENLF NEKCGEALGL KQAVKVPFAL FESFPEDFYV EGLPEGVPFR RPSTFGIPRL EKILRNKAKI KFIIKKPEMF ETAIKESTSS KSPPRKINSS PNVNTTASGV EDLNIIQVTI PDDDNERLSK VEKARQLREQ VNDLFSRKFG EAIGMGFPVK VPYRKITINP GCVVVDGMPP GVSFKAPSYL EISSMRRILD SAEFIKFTVI RPFPGLVINN QLVDQSESEG PVIQESAEPS QLEVPATEEI KETDGSSQIK QEPDPTW // ID O43592 PRELIMINARY; PRT; 962 AA. AC O43592; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE EXPORTIN T. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Kutay U., Lipowsky G., Izaurralde E., Schwarzmaier P., Hartmann E., RA Goerlich D.; RL Mol. Cell 0:0-0(1998). DR EMBL; AF039022; AAC39793.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens exportin t mRNA, complete cds. ** [1] ** 1-2889 ** Kutay U., Lipowsky G., Izaurralde E., Schwarzmaier P., Hartmann E., ** Goerlich D.; ** "Identification of a t-RNA-specific nuclear export receptor"; ** Mol. Cell 0:0-0(1998). ** [2] ** 1-2889 ** Goerlich D., Hartmann E.; ** ; ** Submitted (17-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Zellbiologie, MDC Berlin, Robert-Roessle-Str. 10, Berlin 13125, ** Deutschland ** source 1..2889 ** /organism="Homo sapiens" ** CDS 1..2889 ** /codon_start=1 ** /db_xref="PID:g2873377" ** /function="nuclear export factor involved in tRNA ** export" ** /function="binds to Ran-GTP" ** /product="exportin t" ** CDS_IN_EMBL_ENTRY 1 ** 16-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 962 AA; 109992 MW; 317F7FB8186A58F1 CRC64; MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQRTYSDD HVKFFCFQVL EHQVKYKYSE LTTVQQQLIR ETLISWLQAQ MLNPQPEKTF IRNKAAQVFA LLFVTEYLTK WPKFFFDILS VVDLNPRGVD LYLRILMAID SELVDRDVVH TSEEARRNTL IKDTMREQCI PNLVESWYQI LQNYQFTNSE VTCQCLEVVG AYVSWIDLSL IANDRFINML LGHMSIEVLR EEACDCLFEV VNKGMDPVDK MKLVESLCQV LQSAGFFSID QEEDVDFLAR FSKLVNGMGQ SLIVSWSKLI KNGDIKNAQE ALQAIETKVA LMLQLLIHED DDISSNIIGF CYDYLHILKR LTVLSDQQKA NVEAIMLAVM KKLTYDEEYN FENEGEDEAM FVEYRKQLKL LLDRLAQVSP ELLLASVRRV FSSTLQNWQT TRFMEVEVAI RLLYMLAEAL PVSHGAHFSG DVSKASALQD MMRTLVTSGV SSYQHTSVTL EFFETVVRYE KFFTVEPQHI PCVLMAFLDH RGLRHSSAKV RSRTAYLFSR FVKSLNKQMN PFIEDILNRI QDLLELSPPE NGHQSLLSSD DQLFIYETAG VLIVNSEYPA ERKQALMRNL LTPLMEKFKI LLEKLMLAQD EERQASLADC LNHAVGFASR TSKAFSNKQT VKQCGCSEVY LDCLQTFLPA LSCPLQKDIL RSGVRTFLHR MIICLEEEVL PFIPSASEHM LKDCEAKDLQ EFIPLINQIT AKFKIQVSPF LQQMFMPLLH AIFEVLLRPA EENDQSAALE KQMLRRSYFA FLQTVTGSGM SEVIANQGAE NVERVLVTVI QGAVEYPDPI AQKTCFIILS KLVELWGGKD GPVGFADFVY KHIVPACFLA PLKQTFDLAD AQTVLALSEC AVTLKTIHLK RGPECVQYLQ QEYLPSLQVA PEIIQEFCQA LQQPDAKVFK NYLKVFFQRA KP // ID O43629 PRELIMINARY; PRT; 194 AA. AC O43629; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE OLFACTORY RECEPTOR-LIKE PROTEIN (FRAGMENT). GN OLFR42A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Gallinaro H.; RL Immunogenetics 0:0-0(1998). DR EMBL; AF042078; AAC00184.1; -. DR INTERPRO; IPR000276; -. DR PFAM; PF00001; 7tm_1; 1. DR PROSITE; PS00237; G_PROTEIN_RECEPTOR; UNKNOWN_1. FT NON_TER 1 1 FT NON_TER 194 194 ** ** ################# SOURCE SECTION ################## ** Homo sapiens olfactory receptor-like protein (OLFR42A) gene, ** OLFR42A-9026.2 allele, partial cds. ** [1] ** 1-583 ** Gallinaro H.; ** "Olfactory receptor gene cluster in man and mouse major ** histocompatibility complex"; ** Immunogenetics 0:0-0(1998). ** [2] ** 1-583 ** Gallinaro H.; ** ; ** Submitted (09-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, CIGH-CNRS, 1 Avenue de Grande Bretagne, Toulouse ** 31300, France ** source 1..583 ** /organism="Homo sapiens" ** /chromosome="6" ** /map="6p21.3" ** /cell_line="12th IHW # 9026" ** CDS <1..>583 ** /codon_start=1 ** /db_xref="PID:g2828682" ** /gene="OLFR42A" ** /product="olfactory receptor-like protein" ** CDS_IN_EMBL_ENTRY 1 ** 05-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00001; 7tm_1; 1; 189; T; 19-JUN-2000; **PM PROSITE; PS00237; G_PROTEIN_RECEPTOR; 51; 67; ?; 19-JUN-2000; **PM PROSITE; PS50262; G_PROTEIN_RECEPTOR_2; 1; 194; T; 19-JUN-2000; SQ SEQUENCE 194 AA; 21527 MW; 6A23FBF2FDCACEAF CRC64; YFFLSNLSFL DLCFTTSCVP QMLVNLWGPK KTISFLGCSV QLFIFLSLGT TECILLTVMA FDRYVAVCQP LHYATIIHPR LCWQLASVAW VMSLVQSIVQ TPSTLHLPFC PHQQIDDFLC EVPSLIRLSC GDTSYNEIQL AVSSVIFVVV PLSLILASYG ATAQAVLRIN SATAWRKAFG TCSSHLTVVT LFYS // ID O43636 PRELIMINARY; PRT; 1245 AA. AC O43636; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE ROD PHOTORECEPTOR CNG-CHANNEL BETA SUBUNIT. GN RCNC2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Grunwald M.E., Yu W.P., Yu H.H., Yau K.W.; RL J. Biol. Chem. 0:0-0(1998). DR EMBL; AF042498; AAC04830.1; -. DR INTERPRO; IPR000595; -. DR INTERPRO; IPR001622; -. DR INTERPRO; IPR002025; -. DR PFAM; PF00914; CNG_membrane; 1. DR PFAM; PF00027; cNMP_binding; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 1. DR PROSITE; PS00889; CNMP_BINDING_2; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens rod photoreceptor CNG-channel beta subunit (RCNC2) ** mRNA, complete cds. ** [1] ** 1-4382 ** Grunwald M.E., Yu W.P., Yu H.H., Yau K.W.; ** "Identification of a domain on the beta subunit of the rod cGMP-gated ** cation channel that mediates inhibition by calcium-calmodulin"; ** J. Biol. Chem. 0:0-0(1998). ** [2] ** 1-4382 ** Grunwald M.E., Yu W.P., Yu H.H., Yau K.W.; ** ; ** Submitted (12-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Neuroscience, Johns Hopkins University School of Medicine, 725 N. ** Wolfe ** St., Baltimore, MD 21205, USA ** source 1..4382 ** /organism="Homo sapiens" ** CDS 71..3808 ** /codon_start=1 ** /db_xref="PID:g2921583" ** /note="cyclic nucleotide-gated cation channel beta ** subunit" ** /gene="RCNC2" ** /product="rod photoreceptor CNG-channel beta subunit" ** CDS_IN_EMBL_ENTRY 1 ** 10-MAR-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00027; cNMP_binding; 971; 1065; T; 19-JUN-2000; **PM PFAM; PF00914; CNG_membrane; 726; 942; T; 19-JUN-2000; **PM PROSITE; PS00888; CNMP_BINDING_1; 983; 999; T; 19-JUN-2000; **PM PROSITE; PS00889; CNMP_BINDING_2; 1022; 1042; T; 19-JUN-2000; **PM PROSITE; PS50042; CNMP_BINDING_3; 956; 1060; T; 19-JUN-2000; **PM PROSITE; PS50265; CHANNEL_PORE_K; 825; 877; T; 19-JUN-2000; SQ SEQUENCE 1245 AA; 139160 MW; 40C4860BFCF86126 CRC64; MLGWVQRVLP QPPGTPRKTK MQEEEEVEPE PEMEAEVEPE PNPEEAETES ESMPPEESFK EEEVAVADPS PQETKEAALT STISLRAQGA EISEMNSPSH RVLTWLMKGV EKVIPQPVHS ITEDPAQILG HGSTGDTGCT DEPNEALEAQ DTRPGLRLLL WLEQNLERVL PQPPKSSEVW RDEPAVATAP PGRPQEMGPK LQARETPSLP TPIPLQPKEE PKEAPAPEPQ PGSQAQTSSL PPTRDPARLV AWVLHRLEMA LPQPVLHGKI GEQEPDSPGI CDVQTISILP GGQVEPDLVL EEVEPPWEDA HQDVSTSPQG TEVVPAYEEE NKAVEKMPRE LSRIEEEKED EEEEEEEEEE EEEEEVTEVL LDSCVVSQVG VGQSEEDGTR PQSTSDQKLW EEVGEEAKKE AEEKAKEEAE EVAEEEAEKE PQDWAETKEE PEAEAEAASS GVPATKQHPE VQVEDTDADS CPLMAEENPP STVLPPPSPA KSDTLIVPSS ASGTHRKKLP SEDDEAEELK ALSPAESPVV AWSDPTTPKD TDGQDRAAST ASTNSAIIND RLQELVKLFK ERTEKVKEKL IDPDVTSDEE SPKPSPAKKA PEPAPDTKPA EAEPVEEEHY CDMLCCKFKH RPWKKYQFPQ SIDPLTNLMY VLWLFFVVMA WNWNCWLIPV RWAFPYQTPD NIHHWLLMDY LCDLIYFLDI TVFQTRLQFV RGGDIITDKK DMRNNYLKSR RFKMDLLSLL PLDFLYLKVG VNPLLRLPRC LKYMAFFEFN SRLESILSKA YVYRVIRTTA YLLYSLHLNS CLYYWASAYQ GLGSTHWVYD GVGNSYIRCY YFAVKTLITI GGLPDPKTLF EIVFQLLNYF TGVFAFSVMI GQMRDVVGAA TAGQTYYRSC MDSTVKYMNF YKIPKSVQNR VKTWYEYTWH SQGMLDESEL MVQLPDKMRL DLAIDVNYNI VSKVALFQGC DRQMIFDMLK RLRSVVYLPN DYVCKKGEIG REMYIIQAGQ VQVLGGPDGK SVLVTLKAGS VFGEISLLAV GGGNRRTANV VAHGFTNLFI LDKKDLNEIL VHYPESQKLL RKKARRMLRS NNKPKEEKSV LILPPRAGTP KLFNAALAMT GKMGGKGAKG GKLAHLRARL KELAALEAAA KQQELVEQAK SSQDVKGEEG SAAPDQHTHP KEAATDPPAP RTPPEPPGSP PSSPPPASLG RPEGEEEGPA EPEEHSVRIC MSPGPEPGEQ ILSVKMPEER EEKAE // ID O43707 PRELIMINARY; PRT; 884 AA. AC O43707; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE ALPHA ACTININ 4. GN HACTN4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Honda K., Yamada T., Endo R., Ino Y., Gotoh M., Tsuda H., Yamada Y., RA Chiba H., Hirohashi S.; RL J. Cell Biol. 0:0-0(1998). DR EMBL; D89980; BAA24447.1; -. DR INTERPRO; IPR001589; -. DR INTERPRO; IPR001715; -. DR INTERPRO; IPR002017; -. DR INTERPRO; IPR002048; -. DR PFAM; PF00307; CH; 2. DR PFAM; PF00036; efhand; 2. DR PFAM; PF00435; spectrin; 4. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. DR PROSITE; PS00018; EF_HAND; UNKNOWN_1. DR HSSP; Q01082; 1AA2. ** ** ################# SOURCE SECTION ################## ** Homo sapiens mRNA for alpha actinin 4, complete cds. ** [1] ** 1-2873 ** Honda K.; ** ; ** Submitted (20-DEC-1996) to the EMBL/GenBank/DDBJ databases. ** Kazufumi Honda, National Cancer Center Research Institute, Pathology ** Division; 1-1 Tsukiji 5-chome, Chuo-ku, Tokyo 104, Japan ** (E-mail:tyamada@gan2.ncc.go.jp, Tel:+81-3-3542-2511, ** Fax:+81-3-3248-2737) ** [2] ** Honda K., Yamada T., Endo R., Ino Y., Gotoh M., Tsuda H., Yamada Y., ** Chiba H., Hirohashi S.; ** "Actinin-4, a novel actin-bundling protein associated with cell ** motility ** and cancer invasion"; ** J. Cell Biol. 0:0-0(1998). ** source 1..2873 ** /organism="Homo sapiens" ** /sequenced_mol="cDNA to mRNA" ** /cell_line="NCC-MS-1 CDDP" ** CDS 89..2743 ** /codon_start=1 ** /db_xref="PID:d1025362" ** /transl_table=1 ** /gene="HACTN4" ** /product="alpha actinin 4" ** CDS_IN_EMBL_ENTRY 1 ** 26-FEB-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00036; efhand; 742; 770; T; 19-JUN-2000; **PM PFAM; PF00036; efhand; 783; 811; T; 19-JUN-2000; **PM PFAM; PF00307; CH; 23; 127; T; 19-JUN-2000; **PM PFAM; PF00307; CH; 136; 242; T; 19-JUN-2000; **PM PFAM; PF00435; spectrin; 266; 376; T; 19-JUN-2000; **PM PFAM; PF00435; spectrin; 386; 491; T; 19-JUN-2000; **PM PFAM; PF00435; spectrin; 501; 612; T; 19-JUN-2000; **PM PFAM; PF00435; spectrin; 622; 725; T; 19-JUN-2000; **PM PROSITE; PS00018; EF_HAND; 751; 763; ?; 19-JUN-2000; **PM PROSITE; PS00019; ACTININ_1; 25; 34; T; 19-JUN-2000; **PM PROSITE; PS00020; ACTININ_2; 99; 123; T; 19-JUN-2000; **PM PROSITE; PS50021; CH_DOMAIN; 23; 127; T; 19-JUN-2000; **PM PROSITE; PS50021; CH_DOMAIN; 136; 239; T; 19-JUN-2000; **PM PROSITE; PS50083; SPEC_REPEAT; 353; 455; T; 19-JUN-2000; **PM PROSITE; PS50083; SPEC_REPEAT; 464; 575; T; 19-JUN-2000; **PM PROSITE; PS50083; SPEC_REPEAT; 592; 691; T; 19-JUN-2000; **PM PROSITE; PS50222; EF_HAND_2; 734; 808; T; 19-JUN-2000; SQ SEQUENCE 884 AA; 102268 MW; 0B5D0C6B614E424C CRC64; MGDYMAQEDD WDRDLLLDPA WEKQQRKTFT AWCNSHLRKA GTQIENIDED FRDGLKLMLL LEVISGERLP KPERGKMRVH KINNVNKALD FIASKGVKLV SIGAEEIVDG NAKMTLGMIW TIILRFAIQD ISVEETSAKE GLLLWCQRKT APYKNVNVQN FHISWKDGLA FNALIHRHRP ELIEYDKLRK DDPVTNLNNA FEVAEKYLDI PKMLDAEDIV NTARPDEKAI MTYVSSFYHA FSGAQKAETA ANRICKVLAV NQENEHLMED YEKLASDLLE WIRRTIPWLE DRVPQKTIQE MQQKLEDFRD YRRVHKPPKV QEKCQLEINF NTLQTKLRLS NRPAFMPSEG KMVSDINNGW QHLEQAEKGY EEWLLNEIRR LERLDHLAEK FRQKASIHEA WTDGKEAMLK HRDYETATLS DIKALIRKHE AFESDLAAHQ DRVEQIAAIA QELNELDYYD SHNVNTRCQK ICDQWDALGS LTHSRREALE KTEKQLEAID QLHLEYAKRA APFNNWMESA MEDLQDMFIV HTIEEIEGLI SAHDQFKSTL PDADREREAI LAIHKEAQRI AESNHIKLSG SNPYTTVTPQ IINSKWEKVQ QLVPKRDHAL LEEQSKQQSN EHLRRQFASQ ANVVGPWIQT KMEEIGRISI EMNGTLEDQL SHLKQYERSI VDYKPNLDLL EQQHQLIQEA LIFDNKHTNY TMEHIRVGWE QLLTTIARTI NEVENQILTR DAKGISQEQM QEFRASFNHF DKDHGGALGP EEFKACLISL GYDVENDRQG EAEFNRIMSL VDPNHSGLVT FQAFIDFMSR ETTDTDTADQ VIASFKVLAG DKNFITAEEL RRELPPDQAE YCIARMAPYQ GPDAVPGALD YKSFSTALYG ESDL // ID O43721 PRELIMINARY; PRT; 220 AA. AC O43721; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE HYPOTHETICAL 24.5 kDa PROTEIN. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=FETAL HEART; RX MEDLINE=98153806; PubMed=9480850; RA Vidal-Taboada J.M., Bergonon S., Sanchez M., Lopez-Acedo C., Groet J., RA Nizetic D., Egeo A., Scartezzini P., Katsanis N., Fisher E.M.C., RA Delabar J.M., Oliva R.; RT "High resolution physical mapping and identification of transcribed RT sequences in the Down syndrome region-2."; RL Biochem. Biophys. Res. Commun. 243:572-578(1998). DR EMBL; AJ222636; CAA10896.1; -. KW Hypothetical protein. ** ** ################# SOURCE SECTION ################## ** Homo sapiens partial human cDNA (660 bp) ** [1] ** 1-660 ** Scartezzini P.; ** ; ** Submitted (27-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Scartezzini P., Pediatrics, E/O Ospedali Galliera, Via Mura delle ** capuccine 14, 16128 Genova, ITALY. ** [3] ** Vidal-Taboada J.M., Bergonon S., Sanchez M., Lopez-Acedo C., Groet J., ** Nizetic D., Egeo A., Scartezzini P., Katsanis N., Fisher E.M.C., ** Delabar J.M., Oliva R.; ** "High resolution physical mapping and identification of transcribed ** sequences in the down syndrome region-2"; ** Biochem. Biophys. Res. Commun. 243:572-578(1998). ** source 1..660 ** /organism="Homo sapiens" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="fetal heart" ** CDS 1..660 ** /codon_start=1 ** /db_xref="PID:e1254889" ** /product="hypothetical protein" ** Warning: illegal start codon ** CDS_IN_EMBL_ENTRY 1 ** 03-MAR-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 220 AA; 24455 MW; 4B795D89F191ECDF CRC64; GTRRSGLSRS SNLRVTRTRA AQRKTGPVSL ANGCGRKATR KRVYLSDSDN NSLETGEILK ARAGNNRKVL RKCAAVAANK IKLMSDVEEN SSSESVCSGR KLPHRNASAV ARKKLLHNSE DEQSLKSEIE EEELKDENQP LPVSSSHTAQ SNVDESENRD SESESDLRVA RKNWHANGYK SHTPAPSKTK FLKIESSEED SKVMIQIMHV QNCWPINVCQ // ID O43919 PRELIMINARY; PRT; 233 AA. AC O43919; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE LINKER FOR ACTIVATION OF T CELLS (LAT). GN LAT OR PP36. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; RL Cell 0:0-0(1997). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=THYMUS; RA Weber J.R., Orstavik S., Torgersen K.M., Danbolt N.C., Berg S.F., RA Tasken K., Imboden J.B., Vaage J.T.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. DR EMBL; AF036905; AAC39636.1; -. DR EMBL; AJ223280; CAA11218.1; -. DR INTERPRO; IPR000345; -. DR PROSITE; PS00190; CYTOCHROME_C; UNKNOWN_1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens linker for activation of T cells (LAT) mRNA, complete ** cds. ** [1] ** 1-1060 ** Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; ** "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor ** to ** cellular activation"; ** Cell 0:0-0(1997). ** [2] ** 1-1060 ** Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; ** ; ** Submitted (05-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Cell Biology and Metabolism Branch, National Institute of Child Health ** and Development, National Institute of Health, 9000 Rockville Pike, ** Bethesda, MD 20892, USA ** LAT is a highly tyrosine phosphorylated protein, previously ** described as p36-38, and it associates with many signaling ** molecules, such as Grb2, PLC-gamma1, PI-3 kinase, cbl, Vav, and ** SLP-76, either directly or indirectly upon T cell activation. It is ** a potential type III transmembrane protein. ** [1] ** 1-1616 ** Orstavik S.; ** ; ** Submitted (09-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Orstavik S., Institute of Medical Biochemistry, University of Oslo, BP ** 1112, Blindern, N-0317 Oslo, NORWAY. ** [2] ** Weber J.R., Orstavik S., Torgersen K.M., Danbolt N.C., Berg S.F., ** Tasken K., Imboden J.B., Vaage J.T.; ** "Cloning of pp36, a tyrosine-phosphorylated adaptor protein ** specifically ** expressed in T and NK cells."; ** Unpublished. ** source 1..1060 ** /organism="Homo sapiens" ** /cell_line="Jurkat T cells" ** CDS 58..759 ** /codon_start=1 ** /db_xref="PID:g2828024" ** /note="tyrosine kinase substrate" ** /gene="LAT" ** /product="LAT" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** source 1..1616 ** /organism="Homo sapiens" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="thymus" ** CDS 323..1024 ** /codon_start=1 ** /db_xref="PID:e1234817" ** /gene="pp36" ** /product="36 kDa phosphothyrosine protein" ** CDS_IN_EMBL_ENTRY 1 ** 13-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS00190; CYTOCHROME_C; 26; 31; ?; 19-JUN-2000; SQ SEQUENCE 233 AA; 24985 MW; 0832E2D2B4220BC6 CRC64; MEEAILVPCV LGLLLLPILA MLMALCVHCH RLPGSYDSTS SDSLYPRGIQ FKRPHTVAPW PPAYPPVTSY PPLSQPDLLP IPRSPQPLGG SHRTPSSRRD SDGANSVASY ENEEPACEDA DEDEDDYHNP GYLVVLPDST PATSTAAPSA PALSTPGIRD SAFSMESIDD YVNVPESGES AEASLDGSRE YVNVSQELHP GAAKTEPAAL SSQEAEEVEE EGAPDYENLQ ELN // ID O43923 PRELIMINARY; PRT; 183 AA. AC O43923; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE METALLOPROTEINASE. GN MMP20. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Bernot A., Heilig R., Clepet C., Smaoui N., Delpech M., da Silva C., RA Devaud C., Petit J.L., Chiannilkulchai N., Fizames C., Samson D., RA Cruaud C., Caloustian C., Gyapay G., Weissenbach J.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. DR EMBL; AJ003147; CAA05902.1; -. DR EMBL; AJ003144; CAA05900.1; -. DR INTERPRO; IPR001818; -. DR PFAM; PF00413; Peptidase_M10; 1. DR HSSP; P09237; 1MMP. ** ** ################# SOURCE SECTION ################## ** Homo sapiens complete genomic sequence between D16S3070 and ** D16S3275, containing Familial Mediterranean Fever gene disease ** [1] ** Bernot A., Heilig R., Clepet C., Smaoui N., Delpech M., da Silva C., ** Devaud C., Petit J.L., Chiannilkulchai N., Fizames C., Samson D., ** Cruaud C., Caloustian C., Gyapay G., Weissenbach J.; ** "A transcriptional map of the FMF region"; ** Unpublished. ** [2] ** 1-239566 ** Bernot A.; ** ; ** Submitted (07-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** GENOSCOPE - Centre National de Sequencage, 2 rue Gaston Cremieux, EVRY ** BP191, FRANCE. ** [2] ** 1-627 ** Bernot A.; ** ; ** Submitted (07-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** GENOSCOPE - Centre National de Sequencage, 2 rue Gaston Cremieux, EVRY ** BP191, FRANCE. ** [3] ** Bernot A., Heilig R., Clepet C., Smaoui N., Delpech M., da Silva C., ** Devaud C., Petit J.L., Chiannilkulchai N., Fizames C., Samson D., ** Cruaud C., Caloustian C., Gyapay G., Weissenbach J.; ** "A transcriptional map of the FMF region"; ** Unpublished. ** source 179596..222837 ** /organism="Homo sapiens" ** /chromosome="16" ** /map="p13.3" ** /clone="YAC 26fe7" ** /sub_clone="30e10" ** CDS join(6772..6775,9222..9357,9467..9758,15042..15161) ** /db_xref="PID:e1246030" ** /gene="mmp20" ** /product="metalloproteinase" ** CDS_IN_EMBL_ENTRY 5 ** 22-JAN-1998 (Rel. 54, Last updated, Version 1) ** source 1..627 ** /organism="Homo sapiens" ** /chromosome="16" ** /map="p13.3" ** CDS 14..565 ** /codon_start=1 ** /db_xref="PID:e1245446" ** /gene="MMP20" ** /product="metalloproteinase" ** CDS_IN_EMBL_ENTRY 1 ** 22-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00413; Peptidase_M10; 1; 140; T; 19-JUN-2000; SQ SEQUENCE 183 AA; 20354 MW; 2F844C2B8338787B CRC64; MDPGTVATMR KPRCSLPDVL GVAGLVRRRR RYALSGSVWK KRTLTWRVRS FPQSSQLSQE TVRVLMSYAL MAWGMESGLT FHEVDSPQGQ EPDILIDFAR AFHQDSYPFD GLGGTLAHAF FPGEHPISGD THFDDEETWT FGSKASQQLE QELAGGSPVD EELGFSRGWR VNPLGPGSPE RLS // ID C2F_HUMAN PRELIMINARY; PRT; 151 AA. AC Q92979; O00726; O00675; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE C2F PROTEIN. GN C2F. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.; RL Genome Res. 7:268-280(1997). CC -!- SIMILARITY: TO YEAST L9470.5 AND SPAC18G6.07C. DR EMBL; U72514; AAC51641.1; ALT_INIT. DR EMBL; U47924; CAB35662.1; -. KW Hypothetical protein. ** ** ################# SOURCE SECTION ################## ** Human C2f mRNA, complete cds. ** [1] ** 1-886 ** Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.; ** "Large scale sequencing in human chromosome 12p13: experimental and ** computational gene structure determination"; ** Genome Res. 7:268-280(1997). ** [2] ** 1-886 ** Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.; ** ; ** Submitted (24-SEP-1996) to the EMBL/GenBank/DDBJ databases. ** Molecular and Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** [3] ** 1-886 ** Ansari-Lari M.A. PhD, Shen Y., Muzzny D.M., Lee W., Gibbs R.A. PhD.; ** ; ** Submitted (24-JUL-1997) to the EMBL/GenBank/DDBJ databases. ** Department of Moelcular and Human Genetics, Baylor College of ** Medicine, ** One Baylor Plaza, Houston, TX 77030, USA ** source 1..886 ** /organism="Homo sapiens" ** /chromosome="12" ** /map="12p13" ** CDS <1..721 ** /codon_start=2 ** /db_xref="PID:g2276396" ** /evidence=EXPERIMENTAL ** /note="similar to EST with GenBank Accession Number ** R64505; ** similar to S. cerevisiae hypothetical protein L9470.5 ** encoded by GenBank Accession Number S51431, and to S. ** pombe ** hypothetical 34.9 KD protein encoded by GenBank ** Accession ** Number Z68198; see corresponding genomic sequence in ** GenBank Accession Number U72506" ** /gene="C2f" ** /product="C2f" ** CDS_IN_EMBL_ENTRY 1 ** 26-JUL-1997 (Rel. 52, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **ZZ CREATED AND FINISHED BY FIONA. **ZZ UPDATED BY FIONA. **ZZ CURATED. SQ SEQUENCE 151 AA; 16611 MW; 2D0090A2429296DB CRC64; MLMDSPLNRA GLLQVYIHTQ KNVLIEVNPQ TRIPRTFDRF CGLMVQLLHK LSVRAADGPQ KLLKVIKNPV SDHFPVGCMK VGTSFSIPVV SDVRELVPSS DPIVFVVGAF AHGKVSVEYT EKMVSISNYP LSAALTCAKL TTAFEEVWGV I // ID Q12757 PRELIMINARY; PRT; 171 AA. AC Q12757; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE MUCIN (FRAGMENT). GN B1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=COLON; RA Walter A.O., Schwoeble W., Dippold W.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; X83412; CAA58319.1; -. FT VAR_SEQ 358 383 ETNWPRELKDGNGQESLSMSSSSSPA -> DPGSPKKCRAR FT FGLNQQTDWCGPCRRKKKCIRYLPGEGRCPSPVPSDDSALG FT CPGSPAPQDSPSYHLLPRFPTELLTSPAERHLHPQVSPLLS FT ASQPQGPHRPPAAPCRAHRYSNRNLRDRWPSRHRTPGRLQE FT PTP (in isoform 1L and isoform 1S). FT /FTId=VSP_006960. FT VAR_SEQ 358 383 ETNWPRELKDGNGQESLSMSSSSSPA -> GGKRNAFGTYP FT EKAAAPAPFLPMTVL (in isoform 2L and FT isoform 2S). FT /FTId=VSP_002191. FT VAR_SEQ 358 383 ETNWPRELKDGNGQESLSMSSSSSPA -> DPGSPKKCRAR FT FGLNQQTDWCGPCR (in isoform 3L and isoform FT 3S). FT /FTId=VSP_002192. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens B1 mRNA for mucin ** [1] ** Walter A.O., Schwoeble W., Dippold W.; ** "Cloning and expression of the carboxy terminus of a novel mucin"; ** Unpublished. ** [2] ** 1-798 ** Walter A.O.; ** ; ** Submitted (13-DEC-1994) to the EMBL/GenBank/DDBJ databases. ** A.O. Walter, I. Medical Clinic & Univ. of Mainz, ** Verfuegungsgebaeude, Obere Zahlbacherstr. 63, 55101 Mainz, FRG ** source 1..798 ** /organism="Homo sapiens" ** /tissue_type="colon" ** /cell_line="T84" ** /clone_lib="lambda ZapXR" ** /chromosome="7" ** CDS <1..516 ** /partial ** /codon_start=1 ** /gene="B1" ** /product="mucin" ** /db_xref="PID:g853956" ** CDS_1_OUT_OF_1 ** 01-JUN-1995 (Rel. 44, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 171 AA; 17863 MW; 3F249989A6FA501D CRC64; AREKRKPQQP QRRPAGGTGQ RRGSGYSPSA DQQGAQDREE EAAAAPAPTS SGHRTEKRKR LQLQCQPAGG TGQRRGSGQG PSARPAAFTG QRRGSRSSPS ADQQRAQDRE EEAARPQRRP AAGTGQRRGS AAAPVPTSSG TGQRRGSAAA PAPTSSGTGQ RRGSEEMEEE G // ID Q12814 PRELIMINARY; PRT; 47 AA. AC Q12814; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE CEA FAMILY MEMBER (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Mclenachan P.A., Rutherfurd K.J., Beggs K.T., Sims S., Mansfield B.C.; RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; U04433; AAA18341.1; -. FT NON_TER 1 1 FT NON_TER 47 47 ** ** ################# SOURCE SECTION ################## ** Human CEA family member gene, BI-like domain, partial cds. ** [1] ** 1-384 ** McLenachan P.A., Rutherfurd K.J., Beggs K.T., Sims S., ** Mansfield B.C.; ** "Characterization of the PSG11 Gene"; ** Unpublished. ** [2] ** 1-384 ** Mansfield B.C.; ** ; ** Submitted (15-DEC-1993) to the EMBL/GenBank/DDBJ databases. ** Brian C. Mansfield, Massey University, Microbiology and Genetics, ** Palmerston North, New Zealand ** NCBI gi: 436166 ** source 1..384 ** /clone="C20.5" ** /clone_lib="CVOO1K" ** /organism="Homo sapiens" ** /cell_type="leukocyte" ** CDS <244..>384 ** /standard_name="CEA family member gene, BI-like ** domain" ** /note="NCBI gi: 436167" ** /codon_start=2 ** /db_xref="PID:g436167" ** CDS_1_OUT_OF_1 ** 26-MAY-1994 (Rel. 39, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 47 AA; 5415 MW; 832E3F1A03BC0913 CRC64; WLGHPFTPVI SYELGANLRL FIHVASNPPS PYFWRVMETF CNTCKSS // ID Q12833 PRELIMINARY; PRT; 58 AA. AC Q12833; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE FIBROMODULIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=CARTILAGE; RA Sztrolovics R., Chen X.N., Grover J., Roughley P.J., Korenberg J.R.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U05291; AAA16153.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human fibromodulin mRNA, partial cds. ** [1] ** 1-1892 ** Sztrolovics R., Chen X.N., Grover J., Roughley P.J., ** Korenberg J.R.; ** "Localization of the human fibromodulin gene to chromosome 1q32 ** and completion of the cDNA sequence"; ** Unpublished. ** [2] ** 1-1892 ** Sztrolovics R.; ** ; ** Submitted (12-JAN-1994) to the EMBL/GenBank/DDBJ databases. ** Robert Sztrolovics, Department of Surgery, McGill University, ** Genetics Unit, Shriners Hospital for Crippled Children, 1529 Cedar ** Avenue, Montreal, Quebec, H3G 1A6, Canada ** source 1..1892 ** /isolate="patient A10/03/93" ** /clone="pHFM-3'UT" ** /clone_lib="PCR product" ** /organism="Homo sapiens" ** /sex="female" ** /cell_type="chondrocyte" ** /tissue_type="cartilage" ** /dev_stage="neonate" ** /map="1q32" ** /chromosome="1" ** CDS <1..178 ** /note="Encodes only the most carboxy terminal 58 amino ** acids of fibromodulin" ** /product="fibromodulin" ** /codon_start=2 ** /db_xref="PID:g450855" ** CDS_1_OUT_OF_1 ** 29-JAN-1994 (Rel. 38, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 58 AA; 6470 MW; 822B24A3ACDD4D80 CRC64; YLQGNRINEF SISSFCTVVD VVNFSKLQVL RLDGNEIKRS AMPADAPLCL RLASLIEI // ID Q12914 PRELIMINARY; PRT; 1692 AA. AC Q12914; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE G2 PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE OF 1-564 FROM N.A. RC TISSUE=KIDNEY; RA Foord O., Rose E.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U10991; AAA21253.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human G2 protein mRNA, partial cds. ** [1] ** 1-1694 ** Foord O., Rose E.; ** "Transposon-based mapping and sequencing of a novel transcript ** within the WAGR region of human chromosome 11p13"; ** Unpublished. ** [2] ** 1-6868 ** Foord O.; ** ; ** Submitted (17-JUN-1994) to the EMBL/GenBank/DDBJ databases. ** Orit Foord, Advanced Center for Genetic Technology, Applied ** Biosystems Division, Perkin-Elmer Corporation, 850 Lincoln Centre ** Drive, Foster City, CA 94404, USA ** NCBI gi: 533094 ** source 1..6868 ** /clone="pG2-6.9" ** /clone_lib="lambda gt11 cDNA library from embroyonic ** kidney" ** /chromosome="11" ** /organism="Homo sapiens" ** /map="11p13" ** /tissue_type="kidney" ** /dev_stage="embryo" ** CDS <3..5081 ** /note="NCBI gi: 533095" ** /codon_start=1 ** /product="G2" ** /db_xref="PID:g533095" ** CDS_1_OUT_OF_1 ** 08-SEP-1994 (Rel. 40, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 1692 AA; 183170 MW; C5A975AF1485B51A CRC64; IPEGRLSAEH TSSLVPSLHI TTLGQEQAIL SGAVPASPST GTADFPSILT FLQPTENHAS PSPVPEMPTL PAEGSDGSPP ATRDLLLSSK VPNLLSTSWT FPRWKKDSVT AILGKNEEAN VTIPLQGFPR KEVLSLHTVN GFVSDFSTGS VSSPIITAPR TNPLSSGPPL PSILSIQATQ TVFPSLLAFS STKPEVYAAA VDHSGLPASA PKQVRASPSS MDVYDSLTIG DMKKPATTDV FWSSLSAETG SLSTESIISG LQQQTNYDLN GHTISTTSWE THLAPTAPPN GLTSAADAIK SQDFKDTAGH SVTAEGFSIQ DLVLGTSIEQ PVQQSDMTMV GSHIDLWPTS NNNHSRDFQT AEVAYYSPTT RHSVSHPQLQ LPNQPAHPLL LTSPGPTSTG SLQEMLSDGT DTGSEISSDI NSSPERNAST PFQNILGYHS AAESSISTSV FPRTSSRVLR ASQHPKKWTA DTVSSKVQPT AAAAVTLFLR KSSPPALSAA LVAKGTSSSP LAVASGPAKS SSMTTLAKNV TNKAASGPKR TPGAVHTAFP FTPTYMYART GHTTSTHTAI ARKHGHCLWP VVYNLPPPGK PQAMHTGLPN PTNLEMPRAS TPRPLTVTAA LTSITASVKA TRLPPLRAEN TDAVLPAASA AVVTTGKMAS NLECQMSSKL LVKTVLFLTQ RRVQISESLK FSIAKGLTQA LRKAFHQNDV SAHVDILEYS HNVTVGYYAT KGKLVYLPAV VIEMLGVYGV SNVTADLKQH TPHLQSVAVL ASPWNPQPAG YFQLKTVLQF VSQADNIQSC KFAQTMEQRL QKAFQDAERK VLNTKSNLTI QIVSTSNASQ AVTLVYVVGN QSTFLNGTVA SSLLSQLSAE LVGFYLTYPP LTIAEPLEYP NLDISETTRD YWVITVLQGV DNSLVGLHNQ SFARVMEQRL AQLFMMSQQQ GRRFKRATTL GSYTVQMVKM QRVPGPKDPA ELTYYTLYNG KPLLGTVAAK ILSTIDSQRM ALTLHHVVLL QADPVVKNPP NNLWIIAAVL APIAVVTVII IIITAVLCRK NKNDFKPDTM INLPQRAKPV QGFDYAKQHL GQQGADEEVI PVTQETVVLP LPIRDAPQER DVAQDGSTIK TAKSTETRKS RSPSENGSVI SNESGKPSSG RRSPQNVMAQ QKVTKEEARK RNVPASDEEE GAVLFDNSSK VAAEPFDTSS GSVQLIAIKP TALPMVPPTS DRSQESSAVL NGEVNKALKQ KSDIEHYRNK LRLKAKRKGY YDFPAVETSK GLTERKKMYE KAPKEMEHVL DPDSELCAPF TESKNRQQMK NSVYRSRQSL NSPSPGETEM DLLVTRERPR RGIRNSGYDT EPEIIEETNI DRVPEPRGYS RSRQVKGHSE TSTLSSQPSI DEVRQQMHML LEEAFSLASA GHAGQSRHQE AYGSAQHLPY SEVVTSAPGT MTRPRAGVQW VPTYRPEMYQ YSLPRPAYRF SQLPEMVMGS PPPPVPPRTG PVAVASLRRS TSDIGSKTRM AESTGPEPAQ LHDSASFTQM SRGPVSVTQL DQSALNYSGN TVPAVFAIPA ANRPGFTGYF IPTPPSSYRN QAWMSYAGEN ELPSQWADSV PLPGYIEAYP RSRYPQSSPS RLPRQYSQPA NLHPSLEQAP APSTAASQQS LAENDPSDAP LTNISTAALV KAIREEVAKL AKKQTDMFEF QV // ID Q12915 PRELIMINARY; PRT; 204 AA. AC Q12915; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE IBD1 (FRAGMENT). GN IBD1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=HEMATOPOIETIC; RA Appierto V., Pergolizzi R., Spurr N., Biunno I.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U11036; AAA67652.1; -. FT NON_TER 1 1 FT NON_TER 204 204 ** ** ################# SOURCE SECTION ################## ** Human Ibd1 mRNA, partial cds. ** [1] ** 1-613 ** Appierto V., Pergolizzi R., Spurr N., Biunno I.; ** "Identification and chromosomal localization of two new genes"; ** Unpublished. ** [2] ** 1-613 ** Biunno I.; ** ; ** Submitted (20-JUN-1994) to the EMBL/GenBank/DDBJ databases. ** Ida Biunno, CNR, ITBA, Via Ampere 56, Milano, 20131, Italy ** NCBI gi: 836882 ** source 1..613 ** /clone_lib="Clontech T lymphocytes cDNA library" ** /organism="Homo sapiens" ** /cell_type="T-lymophocyte" ** /tissue_type="hematopoietic" ** /chromosome="18" ** CDS <1..>612 ** /gene="Ibd1" ** /note="NCBI gi: 836883" ** /codon_start=1 ** /function="unknown" ** /db_xref="PID:g836883" ** CDS_1_OUT_OF_1 ** 04-JUN-1995 (Rel. 44, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 204 AA; 22095 MW; 5ADAE93D3744E581 CRC64; VSGIRGAGSG CTRQTFPMAS VTRAVFGELP SGGGTVEKFQ LQSDLLRVDI ISWGCTITAL EVKDRQGRAS DVVLGFAELE GYLQKQPYFG AVIGRVANRI AKGTFKVDGK EYHLAITRNP TVCTGRSQQG FDKVLWTLGA VKCVQFSRIS PDGEEGYPGE LKVWVTYTLD GGELHSATTE HKPVQATPVN LTTILTSTWQ ATRI // ID Q12925 PRELIMINARY; PRT; 113 AA. AC Q12925; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HYPOTHETICAL PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Lamartine J., Wang Q., Kaneko K., Tsuji S., Mattei M., Lenoir G., RA Sylla B.S.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U12206; AAA62165.1; -. KW Hypothetical protein. FT NON_TER 113 113 ** ** ################# SOURCE SECTION ################## ** Human clone pL713 hypothetical protein mRNA, partial cds. ** [1] ** 1-766 ** Lamartine J., Wang Q., Kaneko K., Tsuji S., Mattei M., Lenoir G., ** Sylla B.S.; ** "Cloning, sequencing, and chromosomal assignment of a new cDNA ** clone to Xq12-q13 and 14q11"; ** Unpublished. ** [2] ** 1-766 ** Sylla B.S.; ** ; ** Submitted (12-JUL-1994) to the EMBL/GenBank/DDBJ databases. ** Bakary S. Sylla, International Agency for Research on Cancer, ** MCA/VHC, 150 Cours Albert Thomas, Lyon, 69372 Cedex O8, France ** NCBI gi: 662789 ** source 1..766 ** /clone="pL713" ** /clone_lib="human placental cDNA library" ** /organism="Homo sapiens" ** /chromosome="Xq12-q13 and 14q11" ** CDS 428..>766 ** /note="ORF1; NCBI gi: 662790" ** /codon_start=1 ** /product="unknown" ** /db_xref="PID:g662790" ** CDS_1_OUT_OF_1 ** 04-MAR-1995 (Rel. 42, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 113 AA; 11385 MW; F93B6A01C558A7B2 CRC64; MEPASAHLLL NDMIAGQHCL EVTIFICFST SFCSSFSFSA SSSISLTLDS SASGPQWRVP VTSTSPAPPP PLGCRGSRTS PGPGAPGGRG AGAAPLRARA PARAPAARPQ APP // ID Q12928 PRELIMINARY; PRT; 48 AA. AC Q12928; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE THROMBOSPONDIN-P50 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Dimitry J.M., Sheibani N., Finn M., Boak B.M., Paul L.L., RA Frazier W.A.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U12471; AAA21126.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human thrombospondin-1 gene, partial cds. ** [1] ** 1-1966 ** Dimitry J.M., Sheibani N., Finn M., Boak B.M., Paul L.L., ** Frazier W.A.; ** "Identification of a human thrombospondin-1 isoform generated by ** alternative splicing"; ** Unpublished. ** [2] ** 1-1966 ** Frazier W.A.; ** ; ** Submitted (20-JUL-1994) to the EMBL/GenBank/DDBJ databases. ** William A. Frazier, Biochemistry and Molecular Biophysics, ** Washington University Medical School, 660 South Euclid Avenue, St. ** Louis, MO 63110, USA ** NCBI gi: 532687 ** source 1..1966 ** /chromosome="15" ** /map="15q21" ** /organism="Homo sapiens" ** /cell_type="leukocyte" ** CDS join(<1..31,961..1076) ** /note="NCBI gi: 532688" ** /codon_start=1 ** /product="thrombospondin-p50" ** /db_xref="PID:g532688" ** CDS_1_OUT_OF_2 ** 08-SEP-1994 (Rel. 40, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 48 AA; 5132 MW; 728FC778BD079EDF CRC64; PDGECCPRCW PRCDCSRGAW ADGKETCCPL MTICAEKAPN AGVRGTTN // ID Q13058 PRELIMINARY; PRT; 109 AA. AC Q13058; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HYPOTHETICAL PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=OVARY; RA Montagna M., Serova O., Sylla B.S., Feunten J., Lenoir G.M.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U18920; AAA69700.1; -. KW Hypothetical protein. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human chromosome 17q12-21 mRNA, clone pOV-3, partial cds. ** [1] ** Montagna M., Serova O., Sylla B.S., Feunten J., Lenoir G.M.; ** "100 kb physical map around the EDH17B2 gene: identification of ** three new genes and a pseudogene of a human homologue of the rat ** PRL-1 tyrosine phosphatase"; ** Unpublished. ** [2] ** 1-861 ** Lenoir G.M.; ** ; ** Submitted (20-DEC-1994) to the EMBL/GenBank/DDBJ databases. ** Gilbert M. Lenoir, International Agency for Research on Cancer, ** VHC/MCA, 150 Cours Albert Thomas, 69372 Lyon CEDEX 08, France ** NCBI gi: 894179 ** source 1..861 ** /clone="pOV-3" ** /clone_lib="Human ovarian cDNA library (Stratagene)" ** /organism="Homo sapiens" ** /sex="female" ** /tissue_type="ovary" ** /dev_stage="adult" ** /map="17q12-21" ** /chromosome="17" ** /note="similar to ESTs, GenBank Accession Numbers ** Z38537 ** and M62002" ** CDS <1..331 ** /note="NCBI gi: 894180" ** /codon_start=2 ** /product="unknown" ** /db_xref="PID:g894180" ** CDS_1_OUT_OF_1 ** 13-JUL-1995 (Rel. 44, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 109 AA; 11583 MW; 6440B7B6E992044F CRC64; GYLHRLSDPT LHSHPFLSPR SCPALHSTAG MLGTEALAAP QCTGLPSLGV GFFPGLAWAL PTSTPSGRGC RLMLFPDETL RSSPPPIMMS SVWDWGPLGS ACMPAWLRP // ID Q13079 PRELIMINARY; PRT; 344 AA. AC Q13079; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE VT4 PROTEIN (VT) (FRAGMENT). GN VT. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Tesmer V., Babin J., Rajadhyaksha A., Bina M.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U19346; AAA64188.1; -. FT NON_TER 1 1 FT NON_TER 344 344 ** ** ################# SOURCE SECTION ################## ** Human VT4 protein (VT) mRNA, partial cds. ** [1] ** 1-1032 ** Tesmer V., Babin J., Rajadhyaksha A., Bina M.; ** ; ** Unpublished. ** [2] ** 1-1032 ** Bina M.; ** ; ** Submitted (30-DEC-1994) to the EMBL/GenBank/DDBJ databases. ** Minou Bina, Department of Chemistry, Purdue University, 1393 Brown ** Blg., W. Lafayette, IN 47907, USA ** NCBI gi: 726043 ** source 1..1032 ** /organism="Homo sapiens" ** /cell_line="Hela" ** CDS <1..>1032 ** /gene="VT" ** /note="NCBI gi: 726044" ** /codon_start=1 ** /product="VT4" ** /db_xref="PID:g726044" ** CDS_1_OUT_OF_1 ** 13-APR-1995 (Rel. 43, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 344 AA; 38166 MW; D9BCC309953FB987 CRC64; RQPSSLPEGL PAPLEKRVKE LAQAARAAEG ESRQKFFTQD INGILLDIEA QTRELSSQVR SGVYAYLASF LPCSKDALLK RARKLHLYEQ GGRLKEPLQK LKEAIGRAMP EQMAKYQDEC QAHTQAKVAK MLEEEKDKEQ RDRICSDEEE DEEKGGRRIM GPRKKFQWND EIRELLCQVV KIKLESQDLE RNNKAQAWED CVKGFLDAEV KPLWPKGWMQ ARTLFKESRR GHGHLTSILA KKKVMAPSKI KVKESSTKPD KKVSVPSGQI GGPIALPSDH QTGGLSIGAS SRELPSQASG GLANPPPVNL EDSLDEDLIR NPASSVEAVS KELAALNSRA AGNS // ID Q13116 PRELIMINARY; PRT; 353 AA. AC Q13116; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE MEMBRANE PROTEIN-LIKE PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., RA Anzevino R., Velona I., Brahe C., Scheffer H., Van Ommen G.J.B., RA Buys C.H.C.M.; RL Eur. J. Hum. Genet. 0:0-0(0). DR EMBL; U21556; AAA69956.1; -. FT NON_TER 1 1 FT NON_TER 353 353 ** ** ################# SOURCE SECTION ################## ** Human membrane protein-like protein mRNA, partial cds. ** [1] ** der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., ** Anzevino R., VELONA I., Brahe C., Scheffer H., van Ommen G.J.B., ** Buys C.H.C.M.; ** "A provisional transcript map of the spinal muscular atrophy (SMA) ** critical region"; ** Unpublished. ** [2] ** 1-1263 ** der Steege G.; ** ; ** Submitted (23-FEB-1995) to the EMBL/GenBank/DDBJ databases. ** Gerrit Van der Steege, University of Groningen, Department of ** Medical Genetics, Antonius Deusinglaan 4, Groningen, 9713 AW, The ** Netherlands ** NCBI gi: 899492 ** source 1..1263 ** /clone="5G5" ** /clone_lib="library of A. Bernards" ** /organism="Homo sapiens" ** /map="5q13.1 and 5p" ** /chromosome="5" ** /cell_type="pre-B-cells" ** CDS <204..>1263 ** /note="similar to rat integral membrane glycoprotein, ** PIR ** Accession Number A40670; NCBI gi: 899493" ** /codon_start=1 ** /db_xref="PID:g899493" ** CDS_1_OUT_OF_1 ** 19-JUL-1995 (Rel. 44, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 353 AA; 36932 MW; 431ADAB38FD2CA6E CRC64; SQNGPRGHRG CTVCILALRX NGGLSPFVPR PGPLQTDLHA QSSEIRYNQT SQTSWTSSST KRNAISSSYS STGGLPGLKQ RRGPASSRCQ LTLSYSKTVS EDGPQAVSSR HTRCEKADTA PGQTLAPRGG SPRSQASRPR RRKIPLLPRR RGEPLMLPPP LELGYRVTAE DLHLEKETAL QRINSALHVE DKATSDCRPS RPSHTLSSLA TGASGGPPVS KAPTMDAQPD KLKSQDCLGL VAALASATEV SSTAPMSGKK HRPPGPLFSS SDPLPATSSH SQDSAQVTSM IPAPFTAASR DASMRRTRPG TSAPAXAAAA PPPSTLNPTS GSLLNAVDEG PSHFLASATA AAR // ID Q13119 PRELIMINARY; PRT; 293 AA. AC Q13119; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE DUPLICATE SPINAL MUSCULAR ATROPHY (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., RA Anzevino R., Velona I., Brahe C., Scheffer H., Van Ommen G.J.B., RA Buys C.H.C.M.; RL Eur. J. Hum. Genet. 0:0-0(0). DR EMBL; U21914; AAA64505.1; -. DR INTERPRO; IPR002999; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human duplicate spinal muscular atrophy mRNA, clone 5G7, partial ** cds. ** [1] ** der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., ** Anzevino R., VELONA I., Brahe C., Scheffer H., van Ommen G.J.B., ** Buys C.H.C.M.; ** "A provisional transcript map of the spinal muscular atrophy (SMA) ** critical region"; ** Unpublished. ** [2] ** 1-1466 ** der Steege G.; ** ; ** Submitted (28-FEB-1995) to the EMBL/GenBank/DDBJ databases. ** Gerrit Van der Steege, University of Groningen, Department of ** Medical Genetics, Antonius Deusinglaan 4, Groningen, 9713 AW, The ** Netherlands ** NCBI gi: 736410 ** source 1..1466 ** /clone="5G7" ** /clone_lib="library of A. Bernards" ** /organism="Homo sapiens" ** /map="5q13.1" ** /chromosome="5" ** /cell_type="pre-B-cells" ** CDS <1..882 ** /note="putative open reading frame; duplicate of the ** functional spinal muscular atrophy gene, cDNA clone ** BCD514, ** GenBank Accession Number U18423; it is not known if ** this ** copy of the gene is actually translated; NCBI gi: ** 736411" ** /codon_start=1 ** /db_xref="PID:g736411" ** CDS_1_OUT_OF_1 ** 23-MAY-1995 (Rel. 43, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS50304; TUDOR; 90; 150; T; 19-JUN-2000; SQ SEQUENCE 293 AA; 31718 MW; FEF4B81E12040F24 CRC64; AMSSGGSGGG VPEQEDSVLF RRGTGQSDDS DIWDDTALIK AYDKAVASFK HALKNGDICE TSGKPKTTPK RKPAKKNKSQ KKNTAASLQQ WKVGDKCSAI WSEDGCIYPA TIASIDFKRE TCVVVYTGYG NREEQNLSDL LSPICEVANN IEQNAQENEN ESQVSTDESE NSRSPGNKSD NIKPKSAPWN SFLPPPPPMP GPRLGPGKPG LKFNGPPPPP PPPPPHLLSC WLPPFPSGPP IIPPPPPICP DSLDDADALG SMLISWYMSG YHTGYYMGFR QNQKEGRCSH SLN // ID Q13222 PRELIMINARY; PRT; 203 AA. AC Q13222; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1999 (TrEMBLrel. 12, Last annotation update) DE GATA-4 (FRAGMENT). GN GATA-4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Wood S., Yaremko M.L., Schertzer M.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U28835; AAA70335.1; -. DR HSSP; P04002; 1WFA. FT NON_TER 203 203 ** ** ################# SOURCE SECTION ################## ** Human GATA-4 gene, partial cds. ** [1] ** 1-855 ** Wood S., Yaremko M.L., Schertzer M.; ** "Localization of human GATA4 to 8p23 maps chromosomal breakpoints ** disrupting synteny between human 8p and mouse 14 to the Clu-Gata4 ** interval"; ** Unpublished. ** [2] ** 1-855 ** Wood S.; ** ; ** Submitted (09-JUN-1995) to the EMBL/GenBank/DDBJ databases. ** Stephen Wood, Medical Genetics, University of British Columbia, ** 6174 University Blvd., Vancouver, B.C. V6T 1Z3, Canada ** NCBI gi: 903937 ** source 1..855 ** /organism="Homo sapiens" ** /clone_lib="LA08NC01, Wood et al. Cytogenet. Cell ** Genet. ** 59:243-247, 1992" ** /clone="161F5" ** /chromosome="8" ** /map="8p" ** CDS 61..>669 ** /gene="GATA-4" ** /note="similar to human GATA-4 cDNA sequence, GenBank ** Accession Number L34357; NCBI gi: 903938" ** /codon_start=1 ** /db_xref="PID:g903938" ** CDS_1_OUT_OF_1 ** 26-JUL-1995 (Rel. 44, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 203 AA; 20104 MW; 7C238D931655F208 CRC64; MYQSLPWPPT TGRPPVPTRR AAPAPSCXXX APRPRQSTCP PAGALLRAGP VLPPGRRRGL CVRRRLGRSS GGAASGAGPG TQQGSPGWSQ AGADGAAYTP PPVSPRFSFP GPTGSLAAAA AAAAAREAAA YSSGGGAAGA GLAGREQYGR AXFAGSYSSX YPAYMADVGA SWAAAAAASA GPFDSPVLHS LPGRANPXXH PNL // ID Q13306 PRELIMINARY; PRT; 71 AA. AC Q13306; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE THYROID TRANSCRIPTION FACTOR-1 (FRAGMENT). GN TTF-1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Hamdan H., Liu H., Jones C., Delemos R., Minoo P.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U33627; AAA83233.1; -. FT NON_TER 71 71 ** ** ################# SOURCE SECTION ################## ** Human thyroid transcription factor-1 (TTF-1) gene, partial cds. ** [1] ** 1-1062 ** Hamdan H., Liu H., Jones C., deLemos R., Minoo P.; ** "Characterization of TTF-1 transcripts in human lung identifies an ** additional exon"; ** Unpublished. ** [2] ** 1-1062 ** Hamdan H.; ** ; ** Submitted (10-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** Hasnah Hamdan, University of Southern California, Pediatrics, ** Division of Basic Research, 1801 E. Marengo, Rm 1G-1, Los Angeles, ** CA 90033, USA ** NCBI gi: 1113816 ** source 1..1062 ** /clone="pHGX4" ** /clone_lib="Lambda EMBLT3 SP6/T7 library of Clontech, ** Palo ** Alto, CA." ** /organism="Homo sapiens" ** /cell_type="leukocyte" ** CDS join(164..240,927..>1062) ** /gene="TTF-1" ** /codon_start=1 ** /product="thyroid transcription factor-1" ** /db_xref="PID:g1113817" ** CDS_1_OUT_OF_1 ** 13-DEC-1995 (Rel. 46, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 71 AA; 7425 MW; 7ABFD04CD963A711 CRC64; MWSGGSGKAR GWEAAAGGRS SPGRLSRRRI MSMSPKHTTP FSVSDILSPL EESYKKVGME GGGLGAPLAA Y // ID Q13548 PRELIMINARY; PRT; 36 AA. AC Q13548; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE P38-2G4 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Greco N.J., Rao P., Modeli R., Jamieson G.A.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U50137; AAA91484.1; -. FT NON_TER 36 36 ** ** ################# SOURCE SECTION ################## ** Human p38-2G4 mRNA, partial cds. ** [1] ** 1-172 ** Greco N.J., Rao P., Modeli R., Jamieson G.A.; ** ; ** Submitted (27-FEB-1996) to the EMBL/GenBank/DDBJ databases. ** Nicholas J. Greco, Platelet Biology, American Red Cross, 15601 ** Crabbs Branch Way, Rockville, MD 20855, USA ** NCBI gi: 1216525 ** source 1..172 ** /organism="Homo sapiens" ** /cell_type="platelets and CMK 11-5 cells" ** CDS 65..>172 ** /note="similar to Mus musculus p38-2G4 encoded by ** GenBank ** Accession Number X84789; NCBI gi: 1216526" ** /codon_start=1 ** /product="p38-2G4" ** /db_xref="PID:g1216526" ** CDS_1_OUT_OF_1 ** 08-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 36 AA; 4117 MW; 7C2D4C3BCE49FC53 CRC64; MIMEETGKIF KKEKEMKKGI AFPTSISVNN CVCHFP // ID Q13552 PRELIMINARY; PRT; 31 AA. AC Q13552; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE SUPPRESSOR ELEMENT ISHMAEL UPPER CP1 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=MAMMARY; RA DeBlasio T.R., Moasser M.M., Mendelsohn J.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U50277; AAA92144.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human breast cancer suppressor element Ishmael Upper CP1 mRNA, ** partial cds. ** [1] ** 1-132 ** DeBlasio T.R., Moasser M.M., Mendelsohn J.; ** ; ** Submitted (29-FEB-1996) to the EMBL/GenBank/DDBJ databases. ** Tony R. DeBlasio, Medicine, Memorial Sloan-Kettering Cancer Center, ** 430 E. 67 St. RRL 727, New York City, N.Y. 10021, USA ** NCBI gi: 1224126 ** source 1..132 ** /organism="Homo sapiens" ** /clone="Ishmael" ** /cell_type="epithelial" ** /tissue_type="mammary" ** /cell_line="MCF-7" ** CDS <1..96 ** /codon_start=1 ** /product="suppressor element Ishmael Upper CP1" ** /db_xref="PID:g1224127" ** CDS_1_OUT_OF_1 ** 14-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 31 AA; 4015 MW; 45566C06AF4812E1 CRC64; YLKEGDKKYV WHRLGRKREL SDHFLKWKIQ R // ID Q13559 PRELIMINARY; PRT; 34 AA. AC Q13559; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE BREAST CANCER SUPPRESSOR ELEMENT ISHMAEL UPPER RP2 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=MAMMARY; RA DeBlasio T.R., Moasser M.M., Mendelsohn J.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U50403; AAA92145.1; -. FT NON_TER 1 1 FT NON_TER 34 34 ** ** ################# SOURCE SECTION ################## ** Human breast cancer suppressor element Ishmael Upper RP2 mRNA, ** partial cds. ** [1] ** 1-103 ** DeBlasio T.R., Moasser M.M., Mendelsohn J.; ** ; ** Submitted (01-MAR-1996) to the EMBL/GenBank/DDBJ databases. ** Tony R. DeBlasio, Medicine, Memorial Sloan-Kettering Cancer Center, ** 430 E. 67 St. RRL 727, New York City, N.Y. 10021, USA ** NCBI gi: 1224130 ** source 1..103 ** /organism="Homo sapiens" ** /cell_line="MCF-7 human mammary" ** /tissue_type="mammary" ** /cell_type="epithelial" ** /clone="Ishmael" ** CDS <1..>103 ** /codon_start=3 ** /product="breast cancer suppressor element Ishmael ** Upper ** RP2" ** /db_xref="PID:g1224131" ** CDS_1_OUT_OF_1 ** 14-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 34 AA; 3726 MW; EB286FD9128FBBA8 CRC64; LLWSTLVSWG CWLTPVIPTL WEAKAGGSPE PRSS // ID Q13581 PRELIMINARY; PRT; 84 AA. AC Q13581; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE KR-ZNF2 (FRAGMENT). GN KR-ZNF2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Sancho E., Gonzalez-Lamuno D., Thomson T.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U52097; AAA97913.1; -. FT NON_TER 1 1 FT NON_TER 84 84 ** ** ################# SOURCE SECTION ################## ** Human zinc finger protein (kr-znf2) mRNA, partial cds. ** [1] ** 1-253 ** Sancho E., Gonzalez-Lamuno D., Thomson T.; ** "Three novel Zn finger proteins"; ** Unpublished. ** [2] ** 1-253 ** Sancho E.; ** ; ** Submitted (22-MAR-1996) to the EMBL/GenBank/DDBJ databases. ** Elena Sancho, Biologia Celular y Molecular, Instituto Municipal de ** Investigacion Medica, c/ Dr Aiguader 80, Barcelona 08003, Spain ** NCBI gi: 1277184 ** source 1..253 ** /organism="Homo sapiens" ** /cell_type="HT-29 colon cancer cells" ** CDS <1..>253 ** /gene="kr-znf2" ** /note="zinc finger protein; NCBI gi: 1277185" ** /codon_start=1 ** /product="KR-ZNF2" ** /db_xref="PID:g1277185" ** CDS_1_OUT_OF_1 ** 26-APR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 84 AA; 9733 MW; FAD9F3A6EEE965F6 CRC64; PVLSTSPPNL FKKIIYTGEK FYKCEEYGKA FNQSSTLTRI KNSYCTETLT RVKNMAKPLT SPQFLTDITQ YTLERNTRQT TKDL // ID Q13599 PRELIMINARY; PRT; 58 AA. AC Q13599; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE TRANSCRIPTION ELONGATION INHIBITOR PVHL (FRAGMENT). GN VHL. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=CLEAR-CELL RENAL CELL CARCINOMA; RA Wenzel M.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U54612; AAA98614.1; -. DR INTERPRO; IPR002714; -. DR PFAM; PF01847; VHL; 1. FT NON_TER 1 1 FT NON_TER 58 58 ** ** ################# SOURCE SECTION ################## ** Human von Hippel-Lindau tumor suppressor (vhl) gene, exon 3, ** partial cds. ** [1] ** 1-176 ** Wenzel M.; ** ; ** Submitted (10-APR-1996) to the EMBL/GenBank/DDBJ databases. ** Michael Wenzel, KMS-registry, University of Duesseldorf, Moorenstr. ** 5, Duesseldorf 40225, FRG ** NCBI gi: 1293146 ** source 1..176 ** /organism="Homo sapiens" ** /tissue_type="clear-cell renal cell carcinoma" ** /chromosome="3" ** /map="3p25-26" ** CDS <1..>176 ** /gene="vhl" ** /note="Description: von Hippel-Lindau tumor ** suppressor; ** transcription elongation inhibitor; NCBI gi: 1293147" ** /codon_start=3 ** /product="pVHL" ** /db_xref="PID:g1293147" ** CDS_1_OUT_OF_1 ** 04-MAY-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01847; VHL; 1; 58; T; 19-JUN-2000; SQ SEQUENCE 58 AA; 7051 MW; 2AA043F064D06238 CRC64; YTLKERCPQV VRSLVKPENY RRLDIVRSLY EDLEDHPNVQ KDLERLTQER IAHQRMGD // ID Q13600 PRELIMINARY; PRT; 350 AA. AC Q13600; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE TOPOISOMERASE IIB (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Yuwen H.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U54831; AAB01982.1; -. KW Isomerase. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human topoisomerase IIb mRNA, partial cds. ** [1] ** 1-1388 ** Yuwen H.; ** "Binding of wild-type p53 by topoisomerase II and overexpression ** of topoisomerase II in human hepatocellular carcinoma"; ** Unpublished. ** [2] ** 1-1388 ** Yuwen H.; ** ; ** Submitted (12-APR-1996) to the EMBL/GenBank/DDBJ databases. ** H. Yuwen, CBER/DTTD/LH HFM-310, FDA, 1401 Rockville Pike, ** Rockville, MD 20852-1448, USA ** source 1..1388 ** /organism="Homo sapiens" ** CDS <1..1053 ** /note="p53 binding protein" ** /codon_start=1 ** /product="topoisomerase IIb" ** /db_xref="PID:g1354507" ** CDS_1_OUT_OF_1 ** 08-JUN-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 350 AA; 38567 MW; 55E6A5693B1C16CC CRC64; EFSGAPVEGA GEEALTPSVP INKGPKPKRE KKEPGTRVRK TPTSSGKPSA KKVKKRNPWS DDESKSESDL EETEPVVIPR DSLLRRAAAE RPKYTFDFSE EEDDDADDDD DDNNDLEELK VKASPITNDG EDEFVPSDGL DKDEYTFSPG KSKATPEKSL HDKKSQDFGN LFSFPSYSQK SEDDSAKFDS NEEDSASVFS PSFGLKQTDK VPSKTVAAKK GKPSSDTVPK PKRAPKQKKV VEAVNSDSDS EFGIPKKTTT PKGKGRGAKK RKASGSENEG DYNPGRKTSK TTSKKPKKTS FDQDSDVDIF PSDFPTEPPS LPRTGRARKE VKYFAESDEE EDDVDFAMFN // ID Q13681 PRELIMINARY; PRT; 146 AA. AC Q13681; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE ALPHA 3 TYPE IX COLLAGEN (FRAGMENT). GN HUMCOL9A3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=HYALINE CARTILAGE; RX MEDLINE=97293217; PubMed=9164858; RA Peraelae M., Savontaus M., Metsaeranta M., Vuorio E.; RT "Developmental regulation of mRNA species for types II, IX and XI RT collagens during mouse embryogenesis."; RL Biochem. J. 324:209-216(1997). DR EMBL; X91013; CAA62495.1; -. DR INTERPRO; IPR000087; -. DR PFAM; PF01391; Collagen; 2. KW Extracellular matrix. FT NON_TER 1 1 FT NON_TER 146 146 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for alpha 3 type IX collagen ** [1] ** Peraelae M.; ** ; ** Unpublished. ** [2] ** 1-438 ** Peraelae M.P.; ** ; ** Submitted (21-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** M.P. Peraelae, Dept. of Medical Biochemistry, Univ. of Turku, ** Kiinamyllynkatu 10, 20520 Turku, FINLAND ** source 1..438 ** /organism="Homo sapiens" ** /dev_stage="fetal" ** /tissue_type="hyaline cartilage" ** CDS <1..>438 ** /partial ** /codon_start=1 ** /gene="humcol9a3" ** /product="alpha 3 type IX collagen" ** /db_xref="PID:g975657" ** misc_feature 1..87 ** /note="NC2 domain" ** AA 1 -> 29 ** misc_feature 88..423 ** /note="COL1 domain" ** AA 30 -> 141 ** misc_feature 424..438 ** /note="NC1 domain" ** AA 142 -> 146 ** CDS_1_OUT_OF_1 ** 05-SEP-1995 (Rel. 45, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01391; Collagen; 28; 86; T; 19-JUN-2000; **PM PFAM; PF01391; Collagen; 87; 144; T; 19-JUN-2000; **PM PROSITE; PS50288; COLLAGEN_REP; 29; 87; T; 19-JUN-2000; **PM PROSITE; PS50288; COLLAGEN_REP; 112; 139; T; 19-JUN-2000; SQ SEQUENCE 146 AA; 13913 MW; 99F402AF2683D517 CRC64; EQHIRELCGG MISEQIAQLA AHLRKPLAPG SIGRPGPAGP PGPPGPPGSI GHPGTRGPPG YRGPTGELGD PGPRGNQGDR GDKGAAGAGL DGPEGDQGPQ GPQGVPGTSK DGQDGAPGEP GPPGDPGLPG AIGAQGTPGI CDTSAC // ID Q13727 PRELIMINARY; PRT; 534 AA. AC Q13727; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE AHNAK-RELATED PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=CERVIX; RA Kilwinski J.; RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; X74818; CAA52817.1; -. FT NON_TER 1 1 FT NON_TER 534 534 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA of AHNAK-related sequence ** [1] ** 1-1601 ** Kilwinski J.; ** ; ** Submitted (11-AUG-1993) to the EMBL/GenBank/DDBJ databases. ** J. Kilwinski, Univ. Konstanz, Fakultaet fuer Biologie, D-78434 ** Konstanz, FRG ** [2] ** Kilwinski J.; ** ; ** Unpublished. ** source 1..1601 ** /organism="Homo sapiens" ** /cell_line="HeLa S3" ** /clone_lib="lambda gt11" ** /clone="MB 41" ** /dev_stage="carcinoma" ** /haplotype="aneuploid" ** /tissue_type="cervix" ** /cell_type="epithelial" ** CDS <1..>1601 ** /codon_start=1 ** /product="AHNAK-related protein" ** /db_xref="PID:g535177" ** CDS_1_OUT_OF_1 ** 03-SEP-1994 (Rel. 40, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 534 AA; 57740 MW; D9E5251D1AF639D7 CRC64; KGPKFKMPDL HLKAPKISMP EVDLNLKGPK MKGDVDVSLP KVEGDLKGPE VDVKGPKVDI DVPDVDVQGP DWHLKMPKVK MPKFSMPGFK GEGPDVDVNL PKADLDVSGP KVDIDVPDVN IEGPDAKLKG PKFKMPEMNI KAPKISMPDF DLHLKGPKVK GDVDVSLPKV EGDLKGPEVD IKGPKVDIDA PDVDVHGPDW HLKMPKVKMP KFSMPGFKGE GPDVDVTLPK ADIEISGPKV DIDAPDVSIE GPDAKLKGPK FKMPEMNIKA PKISMPDIDF NLKGPKVKGD VDVSLPKVEG DLKGPEIDIK GPSLDIDTPD VNIEGPEGKL KGPKFKMPEM NIKAPKISMP DFDLHLKGPK VKGDVDVSLP KVESDLKGPE VDIEGPEGKL KGPKFKMPDV HFKSPQISMS DIDLNLKGPK IKGDMDISVP KLEGDLKGPK VDVKGPKVGI DTPDIDIHGP EGKLKGPKFK MPDLHLKAPK ISMPEVDLNL KGPKVKGDMD ISLPKVEGDL KGPEVDIRDP KVDIDVPDVD VQGP // ID Q13791 PRELIMINARY; PRT; 40 AA. AC Q13791; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1999 (TrEMBLrel. 12, Last annotation update) DE APOLIPOPROTEIN E3 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Bohnet K.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; X92000; CAA63051.1; -. DR HSSP; P02649; 1LE2. KW Lipoprotein. FT VARIANT 20 20 C -> G. FT NON_TER 1 1 FT NON_TER 40 40 ** ** ################# SOURCE SECTION ################## ** H.sapiens apolipoprotein E3 gene ** [1] ** Bohnet K.; ** ; ** Unpublished. ** [2] ** 1-121 ** Bohnet K.; ** ; ** Submitted (05-OCT-1995) to the EMBL/GenBank/DDBJ databases. ** K. Bohnet, Centre de Medecine Preventive, 2 Ave. Doyen Jacques ** Parisot, F-54501, Vandoeuvre les Nancy, CEDEX, FRANCE ** Related sequences: M10065, ** SC.Rall Jr, J. Biol. Chem., 257, 4171-4178, 1982 ** P.de Knijff et al, Hum. Mutat.,4, 178-194, 1994 ** source 1..121 ** /organism="Homo sapiens" ** /cell_type="leucocytes" ** /chromosome="19" ** /map="q13.2" ** CDS <1..>121 ** /partial ** /codon_start=1 ** /product="apolipoprotein E3" ** /db_xref="PID:e205282" ** variation replace(58,"g") ** /note="point mutation" ** CDS_1_OUT_OF_1 ** 01-AUG-1996 (Rel. 48, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 40 AA; 4697 MW; B7F2E3E935CDA52C CRC64; QYRGEVQAML GQSTEELRVC LASHLRKLRK RLLRDADDLQ // ID Q13830 PRELIMINARY; PRT; 144 AA. AC Q13830; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE PREGNANCY-SPECIFIC BETA-1 GLYCOPROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Bocco J.; RL Submitted (NOV-1991) to the EMBL/GenBank/DDBJ databases. DR EMBL; X63203; CAA44885.1; -. KW Pregnancy. FT NON_TER 144 144 ** ** ################# SOURCE SECTION ################## ** H.sapiens gene for pregnancy specific beta-1 glycoprotein ** [1] ** 1-3036 ** Bocco J.; ** ; ** Submitted (05-NOV-1991) to the EMBL/GenBank/DDBJ databases. ** J. Bocco, LGME du CNRS - INSERM U184, 11 Rue Humann, Strasbourg, ** 67085 Cedex, FRANCE ** [2] ** 1-3036 ** Bocco J.; ** "Nucleotide sequence of a pregnancy-specific beta-1 glycopotein ** gene family member"; ** Unpublished. ** CPGISLE; HSB1GP; Release 3.0. ** source 1..3036 ** /organism="Homo sapiens" ** /dev_stage="embryo" ** /tissue_type="placenta" ** /cell_type="trophoblast" ** /sex="Female" ** CDS join(1191..1254,2492..>2858) ** /product="pregnancy-specific beta-1 glycoprotein" ** /partial ** /db_xref="PID:g29196" ** CDS_1_OUT_OF_1 ** 07-MAY-1992 (Rel. 31, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 144 AA; 16193 MW; 6871647785F0C63C CRC64; MGPLSAPPCT QHITWKGVLL TASLLNFWNL PITAQVTIEA LPPKVSEGKD VLLLVHNLPQ NLAGYIWYKG QLMDLYHYIT SYVVDGQINI YGPAYTGRET VYSNASLLIQ NVTREDAGSY TLHIIKRGDR TRGVTGYFTF NLYR // ID Q13831 PRELIMINARY; PRT; 93 AA. AC Q13831; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE B1 MUCIN-LIKE ANTIGEN (FRAGMENT). GN B1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=KIDNEY; RA Walter A.O., Dippold W.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; X84838; CAA59277.1; -. FT NON_TER 93 93 ** ** ################# SOURCE SECTION ################## ** H.sapiens B1 mRNA for mucin-like antigen ** [1] ** Walter A.O., Dippold W.; ** "Cloning and expression of a novel mucin-like antigen"; ** Unpublished. ** [2] ** 1-854 ** Walter A.O.; ** ; ** Submitted (15-FEB-1995) to the EMBL/GenBank/DDBJ databases. ** A.O. Walter, Medical Clinic, University of Mainz, Obere ** Zahlbacherstr. 63, 55101 Mainz, FRG ** Related sequence: X83412 (C-terminus) ** source 1..854 ** /organism="Homo sapiens" ** /tissue_type="kidney" ** /clone_lib="lambda MAX1" ** /chromosome="7" ** CDS 577..>854 ** /partial ** /gene="B1" ** /db_xref="PID:g974822" ** CDS_1_OUT_OF_1 ** 01-SEP-1995 (Rel. 45, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 93 AA; 10471 MW; 85A604F02DE1BBCE CRC64; MKPRQKEQDT RLRKLRESSE GDQWLENEKT KPLRPQQQPQ RRPAGGTGQR RGSGSSPSAD QQRAQDREEE AAAAPVPNQQ RAQDREEEAA AAP // ID Q13981 PRELIMINARY; PRT; 86 AA. AC Q13981; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE CARCINOEMBRYONIC ANTIGEN SUBDOMAIN B (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTAL; RA Oikawa S.; RL Submitted (SEP-1989) to the EMBL/GenBank/DDBJ databases. DR EMBL; X16454; CAA34473.1; -. KW Cell adhesion. FT NON_TER 86 86 ** ** ################# SOURCE SECTION ################## ** Human gene for carcinoembryonic antigen subdomains A and B. ** [1] ** 1-1092 ** Oikawa S.; ** ; ** Submitted (02-SEP-1989) to the EMBL/GenBank/DDBJ databases. ** Oikawa S., Suntory Institute for Biomedical Research, 1-1-1 ** Wakayamadai, Shimamoto-cho, Mishima-gun Osaka 618, Japan. ** source 1..1092 ** /organism="Homo sapiens" ** /clone="36" ** /tissue_type="placental" ** /clone_lib="genomic" ** CDS 715..973 ** /product="carcinoembryonic antigen subdomain B" ** /partial ** /db_xref="PID:g296641" ** CDS_1_OUT_OF_1 ** 24-APR-1993 (Rel. 35, Last updated, Version 5) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 86 AA; 9321 MW; 5C76C55FA3E00840 CRC64; MDRAFPPFPP QTPITIQGQI STSPATWPLT HLHSTPGLSV ECSSNTHKSS LSPTSQWIRV DPMLASPITQ PLASVQSQSR QSQSLL // ID Q14083 PRELIMINARY; PRT; 136 AA. AC Q14083; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE C219-REACTIVE PEPTIDE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LEUKEMIA CELL; RA Norris M.D., Gilbert J., Madafiglio J., Haber M.; RL Gene 0:0-0(0). DR EMBL; L34688; AAB00324.1; -. FT NON_TER 1 1 FT NON_TER 136 136 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone D320) C219-reactive peptide mRNA, partial cds. ** [1] ** 1-409 ** Norris M.D., Gilbert J., Madafiglio J., Haber M.; ** "Analysis of a novel cDNA encoding a C219-reactive peptide ** isolated from methotrexate-selected multidrug-resistant human ** leukemic cells"; ** Unpublished. ** source 1..409 ** /organism="Homo sapiens" ** /cell_line="CCRF-CEM" ** /cell_type="T-cell" ** /tissue_type="leukemia cell" ** /tissue_lib="lambda gt11" ** CDS <1..>409 ** /codon_start=3 ** /product="C219-reactive peptide" ** /db_xref="PID:g511639" ** CDS_1_OUT_OF_1 ** 21-MAY-1996 (Rel. 47, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 136 AA; 15343 MW; 98DAFBC8F58C28E1 CRC64; ENKKSIEKLK DVISMNASEF SEVQIALNEA KLSEEKVKSE CHRVQEENAR LKKKKEQLQQ EIEDWSKLHA ELSEQIKSFE KSQKDLEVAL THKDDNINAL TNCITQLNLL ECESESEGQN KGGNDSDELA NGEVGG // ID Q14402 PRELIMINARY; PRT; 25 AA. AC Q14402; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE GAMMA-G GLOBIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RA Vladimir V., Kavsan V.M.; RL Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RA Dmitrenko V.V., Kavsan V.M.; RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases. DR EMBL; X55657; CAA39190.1; -. DR INTERPRO; IPR000971; -. DR PFAM; PF00042; globin; 1. DR PROSITE; PS01033; GLOBIN; 1. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for gamma-G globin (clone pHG18) ** [1] ** 1-166 ** Vladimir V., Kavsan V.M.; ** ; ** Submitted (18-SEP-1990) to the EMBL/GenBank/DDBJ databases. ** Vladimir V., Kavsan V.M., Institute of Molecular Biology and ** Genetics Ukr.SSR Acad. of Sci., Zabolotnogo str. 150, Kiev 252627, ** USSR. ** [2] ** Dmitrenko V.V., Kavsan V.M.; ** "Nucleotide sequence of mitochondrial cytochrome C oxydase II from ** human fetal liver"; ** Unpublished. ** source 1..166 ** /organism="Homo sapiens" ** /dev_stage="embryonal" ** /tissue_type="liver" ** /cell_type="hepatocytes" ** CDS <1..80 ** /product="gamma-G globin" ** /codon_start=3 ** /db_xref="PID:g31723" ** CDS_1_OUT_OF_1 ** 11-MAY-1992 (Rel. 31, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00042; globin; 1; 25; T; 19-JUN-2000; **PM PROSITE; PS01033; GLOBIN; 1; 25; T; 19-JUN-2000; SQ SEQUENCE 25 AA; 2781 MW; C7BE9A334CD66D91 CRC64; FTPEVQASWQ KMVTGVASAL SSRYH // ID Q14441 PRELIMINARY; PRT; 52 AA. AC Q14441; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE GLYCOPROTEIN IB ALPHA (FRAGMENT). GN GPIB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Ishida F.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; L39103; AAA69491.1; -. FT NON_TER 1 1 FT NON_TER 52 52 ** ** ################# SOURCE SECTION ################## ** Homo sapiens glycoprotein Ib alpha (GPIb) gene, partial cds. ** [1] ** 1-424 ** Ishida F.; ** "Submission"; ** Unpublished. ** NCBI gi: 886281 ** source 1..424 ** /organism="Homo sapiens" ** /sequenced_mol="DNA" ** CDS <105..>260 ** /gene="GPIb" ** /note="isoform A; putative; NCBI gi: 886282" ** /codon_start=1 ** /product="glycoprotein Ib alpha" ** /db_xref="PID:g886282" ** CDS_1_OUT_OF_1 ** 05-JUL-1995 (Rel. 44, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 52 AA; 5187 MW; 829FBEB4792EA30F CRC64; SEPAPSPTTP EPTSEPAPSP TTPEPTSEPA PSPTTPEPTS EPAPSPTTPE PT // ID Q14489 PRELIMINARY; PRT; 58 AA. AC Q14489; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE RIBOSOMAL PROTEIN S10 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RA Dmitrenko V.V., Garifulin O.M., Shostak K.A., Smikodub A.I., RA Kavsan V.M.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; Z70761; CAA94807.1; -. KW Ribosomal protein. FT NON_TER 1 1 FT NON_TER 58 58 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for ribosomal protein S10 ** [1] ** 1-174 ** Dmitrenko V.V., Garifulin O.M., Shostak K.A., Smikodub A.I., ** Kavsan V.M.; ** "Characterization of different mRNA types expressed in human ** brain"; ** Unpublished. ** [2] ** 1-174 ** Dmitrenko V.V.; ** ; ** Submitted (12-APR-1996) to the EMBL/GenBank/DDBJ databases. ** Dmitrenko V. V., Institute of Molecular Biology and Genetics, ** Biosynthesis of Nucleic Acids, Zabolotnogo 150, Kiev, Ukraine, ** 252627 ** source 1..174 ** /organism="Homo sapiens" ** /clone="ICRFp507K114" ** /dev_stage="fetus" ** /tissue_type="brain" ** /clone_lib="S. Meier-Ewert's cDNA library no. 507" ** CDS <1..>174 ** /codon_start=1 ** /product="ribosomal protein S10" ** /db_xref="PID:e236293" ** CDS_1_OUT_OF_1 ** 15-APR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 58 AA; 6281 MW; CB8CCC9198F69FDB CRC64; KGLEGERPAR LTRGEADRDT YRRSAVPPGA DKKAEAGLGQ QPEFQFRGGF GRGRGQPP // ID Q14497 PRELIMINARY; PRT; 25 AA. AC Q14497; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE CCAAT BINDING FACTOR SUBUNIT C (FRAGMENT). GN HCBF-C. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RA Dmitrenko V.V., Garifulin O.M., Shostak K.A., Smikodub A.I., RA Kavsan V.M.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; Z70024; CAA93846.1; -. FT NON_TER 25 25 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for CCAAT binding factor subunit gamma ** [1] ** Dmitrenko V.V., Garifulin O.M., Shostak K.A., Smikodub A.I., ** Kavsan V.M.; ** "Characterization of different mRNA types expressed in human ** brain"; ** Unpublished. ** [2] ** 1-270 ** Dmitrenko V.V.; ** ; ** Submitted (07-MAR-1996) to the EMBL/GenBank/DDBJ databases. ** Dmitrenko V. V., Institute of Molecular Biology and Genetics, ** Biosynthesis of Nucleic Acids, Zabolotnogo 150, Kiev, Ukraine, ** 252627 ** source 1..270 ** /organism="Homo sapiens" ** /clone="ICRFp507N0593" ** /dev_stage="fetus" ** /tissue_type="brain" ** /clone_lib="S. Meier-Ewert's cDNA library no.507" ** CDS 196..>270 ** /product="CCAAT binding factor subunit C" ** /function="transcription factor" ** /gene="hCBF-C" ** /note="homologous to rat CCAAT binding factor subunit ** C ** (rCBF-C)" ** /db_xref="PID:e226027" ** CDS_1_OUT_OF_1 ** 08-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 25 AA; 2649 MW; 12DE150C48C31875 CRC64; MSTEGGFGGT SSSDAQQSLQ SFWPR // ID Q14551 PRELIMINARY; PRT; 39 AA. AC Q14551; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE ALBUMIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RA Dmitrenko V.V., Kavsan V.M.; RL Submitted (JAN-1990) to the EMBL/GenBank/DDBJ databases. DR EMBL; X51365; CAA35749.1; -. FT NON_TER 1 1 FT NON_TER 39 39 ** ** ################# SOURCE SECTION ################## ** Human mRNA for albumin (clone pHA19) ** [1] ** 1-124 ** Dmitrenko V.V., Kavasan V.M.; ** ; ** Submitted (04-JAN-1990) to the EMBL/GenBank/DDBJ databases. ** Dmitrenko V.V., Kavasan V.M., Institute of Molecular Biology and ** Genetics, Acad. Sci. Ukr. SSR, 252627 Kiev, Zabolotnogo Str. 150, ** USSR. ** [2] ** 1-124 ** Dmitrenko V.V., Kavsan V.M.; ** ; ** Unpublished. ** For clones pHA1,pHA12 and pHA8,25 see and . ** Data kindly reviewed (18-SEP-1990) by Dmitrenko V.V. ** source 1..117 ** /organism="Homo sapiens" ** /dev_stage="embryo" ** /tissue_type="liver" ** /cell_type="hepatocyte" ** CDS <1..>117 ** /codon_start=1 ** /product="albumin" ** /db_xref="PID:g930070" ** CDS_1_OUT_OF_1 ** 05-AUG-1995 (Rel. 44, Last updated, Version 4) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 39 AA; 4619 MW; ED477E0AD309370B CRC64; QLIHLFFFFV GVKPTPCLKN INFFNHFASF LCASINKKW // ID Q14579 PRELIMINARY; PRT; 30 AA. AC Q14579; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HUMER (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Oberbaeumer I.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; X85129; CAA59443.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for humer ** [1] ** Oberbaeumer I.; ** ; ** Submitted (06-MAR-1995) to the EMBL/GenBank/DDBJ databases. ** I. Oberbaeumer, Max-Planck-Institut fuer Biochemie, Am Klopferspitz ** 18a, D-82152 Martinsried, FRG ** [2] ** 1-643 ** Oberbaeumer I.; ** "A new member of the highly conserved multigene family of ** thiol-specific antioxidant proteins (TSA) of mouse with ** wide-spread occurrence in adherent cell lines: defining ** orthologous mRNAs by their 3' untranslated regions."; ** Unpublished. ** Related sequence: T10952; T10244 ** source 1..643 ** /organism="Homo sapiens" ** /cell_line="HT 1080 (fibrosarcoma, ATCC CCL 1212)" ** /clone_lib="RT-PCR" ** /clone="14" ** CDS <1..93 ** /partial ** /codon_start=1 ** /product="humer" ** /note="equivalent of mouse mer5 gene" ** /db_xref="PID:g854126" ** CDS_1_OUT_OF_1 ** 31-MAY-1995 (Rel. 43, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 30 AA; 3334 MW; 5713AF472692E46E CRC64; EVCPANWTPD SPTIKPSPAA SKEYFQKVNQ // ID Q14759 PRELIMINARY; PRT; 11 AA. AC Q14759; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE LYMPHOCYTE CYTOSOLIC PROTEIN 2 (FRAGMENT). GN LCP2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Sunden S.L.F., Carr L.L., Clements J.L., Motto D.G., Koretzky G.A.; RL Genomics 0:0-0(0). DR EMBL; U44065; AAA93308.1; -. FT NON_TER 1 1 FT NON_TER 11 11 ** ** ################# SOURCE SECTION ################## ** Human lymphocyte cytosolic protein 2 (LCP2) gene, partial cds, ** partial intron. ** [1] ** 1-500 ** Sunden S.L.F., Carr L.L., Clements J.L., Motto D.G., Koretzky G.A.; ** "Polymorphism in and localization of the gene encoding the 76 kDa ** SH2 domain-containing Leukocyte Protein (SLP-76) to chromosome ** 5q33.1-qter"; ** Unpublished. ** [2] ** 1-500 ** Clements J.L., Sunden S.L.F., Motto D.G., Koretzky G.A.; ** ; ** Submitted (29-DEC-1995) to the EMBL/GenBank/DDBJ databases. ** J.L. Clements, Pediatrics, University of Iowa, 440G EMRB, Iowa ** City, IA 52242, USA ** NCBI gi: 1203823 ** source 1..500 ** /organism="Homo sapiens" ** /chromosome="5" ** /map="5q33.1-qter" ** CDS <1..>34 ** /gene="LCP2" ** /note="SLP-76; 76 kDa SH2 domain-containing leukocyte ** protein; NCBI gi: 1203827" ** /codon_start=2 ** /product="lymphocyte cytosolic protein 2" ** /db_xref="PID:g1203827" ** CDS_1_OUT_OF_1 ** 08-APR-1996 (Rel. 47, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 11 AA; 1242 MW; D695104224072DDD CRC64; EAEAALRKIN Q // ID Q14760 PRELIMINARY; PRT; 25 AA. AC Q14760; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE LYMPHOCYTE CYTOSOLIC PROTEIN 2 (FRAGMENT). GN LCP2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Sunden S.L.F., Carr L.L., Clements J.L., Motto D.G., Koretzky G.A.; RL Genomics 0:0-0(0). DR EMBL; U44067; AAA93309.1; -. DR EMBL; U44066; AAA93309.1; JOINED. FT NON_TER 1 1 FT NON_TER 25 25 ** ** ################# SOURCE SECTION ################## ** Human lymphocyte cytosolic protein 2 (LCP2) gene, partial cds, ** partial intron. ** [1] ** 1-361 ** Sunden S.L.F., Carr L.L., Clements J.L., Motto D.G., Koretzky G.A.; ** "Polymorphism in and localization of the gene encoding the 76 kDa ** SH2 domain-containing Leukocyte Protein (SLP-76) to chromosome ** 5q33.1-qter"; ** Unpublished. ** [2] ** 1-361 ** Clements J.L., Sunden S.L.F., Motto D.G., Koretzky G.A.; ** ; ** Submitted (29-DEC-1995) to the EMBL/GenBank/DDBJ databases. ** J.L. Clements, Pediatrics, University of Iowa, 440G EMRB, Iowa ** City, IA 52242, USA ** NCBI gi: 1203825 ** source 1..361 ** /organism="Homo sapiens" ** /chromosome="5" ** /map="5q33.1-qter" ** CDS join(U44066:<1..36,322..>361) ** /gene="LCP2" ** /note="SLP-76; 76 kDa SH2 domain-containing leukocyte ** protein; NCBI gi: 1203828" ** /codon_start=1 ** /product="lymphocyte cytosolic protein 2" ** /db_xref="PID:g1203828" ** CDS_1_OUT_OF_1 ** 08-APR-1996 (Rel. 47, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 25 AA; 2808 MW; 8B7E8429F398865E CRC64; FYXXGTGLRG KEDXLSVXXI XDXFX // ID Q14864 PRELIMINARY; PRT; 109 AA. AC Q14864; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE MPS1 PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTAL; RA Spilsbury K., O'Mara M.A., Wu W., Rowe P.B., Symonds G., Takayama Y.; RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; L20314; AAA36324.1; -. FT NON_TER 1 1 FT NON_TER 109 109 ** ** ################# SOURCE SECTION ################## ** Human MPS1 gene, partial cds. ** [1] ** 1-328 ** Spilsbury K., O'Mara M.A., Wu W., Rowe P.B., Symonds G., ** Takayama Y.; ** "MPS1,a novel macrophage expressed gene isolated by differential ** cDNA analysis"; ** Unpublished. ** source 1..328 ** /organism="Homo sapiens" ** /sequenced_mol="DNA" ** /tissue_type="placental" ** CDS <1..>328 ** /note="partial protein" ** /product="MPS1 protein" ** /codon_start=1 ** /db_xref="PID:g553591" ** CDS_1_OUT_OF_1 ** 05-DEC-1993 (Rel. 38, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 109 AA; 12462 MW; A5205A8C4E70E893 CRC64; PVLEVLPGGG WDNLRNVDMG RVMELTYSNC RTTEDGQYII PDEIFTIPQK QSNLEMNSEI LESWANYQSS TSYSINTELS LFSKVNGKFS TDFQRMKTLQ VKDQAITTR // ID Q14865 PRELIMINARY; PRT; 246 AA. AC Q14865; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE MODULATOR RECOGNITION FACTOR 2 (FRAGMENT). GN MRF-2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=FORESKIN; RA Merrills B.W., Huang T.H., Oka T., LeBon T.R., Gertson P.N., RA Itakura K.; RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases. DR EMBL; M73837; AAA59870.1; -. DR INTERPRO; IPR001606; -. DR PFAM; PF01388; ARID; 1. FT NON_TER 1 1 FT NON_TER 246 246 ** ** ################# SOURCE SECTION ################## ** Human modulator recognition factor 2 (MRF-2) mRNA, complete cds. ** [1] ** 1-740 ** Merrills B.W., Huang T.H., Oka T., LeBon T.R., Gertson P.N., ** Itakura K.; ** "A new family of DNA binding factors contain a member responsive ** to retinoic acid"; ** Unpublished. ** NCBI gi: 188685 ** source 1..740 ** /organism="Homo sapiens" ** /cell_type="fibroblast (not transformed)" ** /haplotype="NA" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="foreskin" ** /tissue_lib="lambda gt11" ** CDS <1..>740 ** /gene="MRF-2" ** /note="NCBI gi: 553592" ** /codon_start=1 ** /product="modulator recognition factor 2" ** /db_xref="PID:g553592" ** CDS_1_OUT_OF_1 ** 18-JAN-1995 (Rel. 42, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01388; ARID; 14; 125; T; 19-JUN-2000; SQ SEQUENCE 246 AA; 27862 MW; 2AD44181EAFD476C CRC64; KVSNEEKPKV AIGEECRADE QAFLVALYKY MKERKTPIER IPYLGFKQIN LWTMFQAAQK LGGYETITAR RQWKHIYDEL GGNPGSTSAA TCTRRHYERL ILPYERFIKG EEDKPLPPIK PRKQENSSQE NENKTKVSGT KRIKHEIPKS KKEKENAPKP QDAAEVSSEQ EKEQETLISQ KSIPEPLPAA DMKKKIEGYQ EFSAKPLASR VDPEKDNETD QGSNSEKVAE EAGEKGPTPP LPSAPL // ID Q14880 PRELIMINARY; PRT; 187 AA. AC Q14880; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE MUCIN (FRAGMENT). GN MUC5B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=TRACHEOBRONCHIAL MUCOSA; RA Aubert J.; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; X74954; CAA52909.1; -. FT NON_TER 1 1 FT NON_TER 187 187 ** ** ################# SOURCE SECTION ################## ** H.sapiens MUC5B mRNA (clone JER28) for mucin (partial) ** [1] ** 1-561 ** Aubert J.; ** ; ** Submitted (07-SEP-1993) to the EMBL/GenBank/DDBJ databases. ** J. Aubert, Unite Inserm 16, Place de Verdun, 59045 Lille cedex, ** FRANCE ** source 1..561 ** /organism="Homo sapiens" ** /tissue_type="tracheobronchial mucosa" ** /chromosome="11" ** /map="11p15" ** /clone="JER28" ** CDS <1..>561 ** /gene="MUC5B" ** /product="mucin" ** /partial ** /codon_start=1 ** /db_xref="PID:g407070" ** CDS_1_OUT_OF_1 ** 08-OCT-1993 (Rel. 37, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 187 AA; 18993 MW; 8F89B7AA6C2F890E CRC64; SSTPGTTWIL TEPSTTATVT GPTGSTATAS STQATAGTPH VSTTATTPTV TSSKATPFSS PGTATALPAL RSTATTPTAT SFTAIPLSWA PTGPLSQTTT PRPPCPQPHP PPLQRLSTPP PVLTTTPPPT GHRLCGHPLL HPSNSSHYQS ADYHNHGFTA TPSSSPGTAR TLPVWISTTT TPTTRGS // ID Q14881 PRELIMINARY; PRT; 622 AA. AC Q14881; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE MUCIN (FRAGMENT). GN MUC5B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=TRACHEOBRONCHIAL MUCOSA; RA Desseyn J.L., Guyonnet-Duperat V., Porchet N., Aubert J.P., Laine A.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; X74955; CAA52910.1; -. FT NON_TER 1 1 FT NON_TER 622 622 ** ** ################# SOURCE SECTION ################## ** H.sapiens MUC5B mRNA (clone JER57) for mucin (partial) ** [1] ** Aubert J.; ** ; ** Submitted (07-SEP-1993) to the EMBL/GenBank/DDBJ databases. ** J. Aubert, Unite Inserm 16, Place de Verdun, 59045 Lille cedex, ** FRANCE ** [2] ** 1-1866 ** Desseyn J.L., Guyonnet-Duperat V., Porchet N., Aubert J.P., ** Laine A.; ** "Human mucin gene MUC5B: the 10.7 kb large central exon encodes ** various alternate subdomains resulting in a super repeat"; ** Unpublished. ** [3] ** 1-1866 ** Laine A.; ** ; ** Submitted (12-JUN-1996) to the EMBL/GenBank/DDBJ databases. ** A. Laine, Inserm U377, Place de Verdun, 59045 Lille cedex, FRANCE ** source 1..1866 ** /organism="Homo sapiens" ** /tissue_type="tracheobronchial mucosa" ** /chromosome="11" ** /map="11p15" ** /clone="JER57" ** /germline ** CDS <1..>1866 ** /gene="MUC5B" ** /product="mucin" ** /partial ** /codon_start=1 ** /db_xref="PID:e248524" ** CDS_1_OUT_OF_1 ** 12-JUN-1996 (Rel. 48, Last updated, Version 11) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 622 AA; 61787 MW; 4FC85A52F50D57E5 CRC64; LGLECRAQAQ PGVPLGELGQ VVECSLDFGL VCRNREQVGK FKMCFNYEIR VFCCNYGHCP STPATSSTAM PSSTPGTTWI LTELTTTATT TASTGSTATP SSTPGTAPPP KVLTSPATTP TATSSKATSS SSPRTATTLP VLTTTATKST ATSVTPIPSS TLGTTGTLPE QTTTPVATMS TIHPSSTPET THTSTVLTTK ATTTRATSST STPSSTPGTT WILTELTTAA TTTAGTGPTA TPSSTPGTTW ILTELTTTAT TTASTGSTAT LSSTPGTTWI LTEPSTTATV TVPTGSTATA SSTQATAGTP HVSTTATTPT VTSSKATPSS SPGTATALPA LRSTATTPTA TSFTAIPSSS LGTTWTRLSQ TTTPTATMST ATPSSTPETV HTSTVLTATA TTTGATGSVA TPSSTPGTAH TTKVPTTTTT GFTATPSSSP GTALTPPVWI STTTTPTTTT PTTSGSTVTP SSIPGTTHTA RVLTTTTTTV ATGSMATPSS STQTSGTPPS LTTTATTITA TGSTTNPSST PGTTPIPPVL TSTATTPAAT SSKATSSSSP RTATTLPVLT STATKSTATS FTPIPSSTLW TTWTVPAQTT TPMSTMSTIH TSSTPETTHT ST // ID Q14882 PRELIMINARY; PRT; 330 AA. AC Q14882; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE MUCIN (FRAGMENT). GN MUC5B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=TRACHEOBRONCHIAL MUCOSA; RA Aubert J.; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; X74956; CAA52911.1; -. FT NON_TER 1 1 FT NON_TER 330 330 ** ** ################# SOURCE SECTION ################## ** H.sapiens MUC5B mRNA (clone JUL10) for mucin (partial) ** [1] ** 1-991 ** Aubert J.; ** ; ** Submitted (07-SEP-1993) to the EMBL/GenBank/DDBJ databases. ** J. Aubert, Unite Inserm 16, Place de Verdun, 59045 Lille cedex, ** FRANCE ** source 1..991 ** /organism="Homo sapiens" ** /tissue_type="tracheobronchial mucosa" ** /chromosome="11" ** /map="11p15" ** /clone="JUL10" ** CDS <1..>991 ** /gene="MUC5B" ** /product="mucin" ** /partial ** /codon_start=1 ** /db_xref="PID:g407053" ** CDS_1_OUT_OF_1 ** 08-OCT-1993 (Rel. 37, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 330 AA; 35556 MW; 97892E19FFC4FA50 CRC64; PTKATTTRAT SSMSTPSSTP GMTWILTELT TAATTTAATA PHCDPVLHPR DHLDPHRAQH YSTVTVPTGS QPTASSTRGT AGTLKVLTSD HHTHSHQLQS HSLLQSRDCN RPSSTEKHSH HTHSYQRYSH PLFLPGTAWT RLSQTTTPTA TMSTATPSST PETVHTSTVL TTTATTTRAT ALWPPPPPPQ EQLTLPKCRL PQPRLHSYPL LQPRDGTHAS SVDQHNHHTH NQRLHGDPLL HPGTTHTATV LTTTTTTVPL VLWQHPPLAH RPVVLPPSLT TTATTITATG STTNPSSTPG TTPIPPVLTT TANHTCSHQQ HSDSLLCPRE // ID Q14913 PRELIMINARY; PRT; 40 AA. AC Q14913; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE NA+/CA2+ EXCHANGER (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=AIRWAY SMOOTH MUSCLE; RA Pitt A., Knox A.J.; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; X91815; CAA62923.1; -. FT NON_TER 1 1 FT NON_TER 40 40 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for Na+/Ca2+ exchanger isoform ** [1] ** Pitt A., Knox A.J.; ** "Molecular characterization of thr Na+/Ca2+ exchanger isoform ** expressed in human airway smooth muscle."; ** Unpublished. ** [2] ** 1-122 ** Pitt A.; ** ; ** Submitted (07-SEP-1995) to the EMBL/GenBank/DDBJ databases. ** A. Pitt, Nottingham University, Respiratory Medicine, City ** Hospital, Hucknall Road, Nottingham, NG5 1PB, UK ** source 1..122 ** /organism="Homo sapiens" ** /dev_stage="adult" ** /tissue_type="airway smooth muscle" ** CDS join(<1..104,105..>122) ** /partial ** /codon_start=2 ** /product="Na+/Ca2+ exchanger" ** /note="alternatively spliced isoform variable region" ** /db_xref="PID:g1008973" ** CDS_1_OUT_OF_1 ** 04-OCT-1995 (Rel. 45, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 40 AA; 4787 MW; C9126B9105B01AC2 CRC64; KIITIRIFDR EEYEKECSLS LVLEEPKWIR RGMKGGFTIT // ID Q14928 PRELIMINARY; PRT; 41 AA. AC Q14928; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE KRUEPPEL-TYPE ZINC FINGER PROTEIN (FRAGMENT). GN ZNF169. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Dean M., Chidambaram A., Gerrard B.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U28322; AAA70187.1; -. DR INTERPRO; IPR001909; -. DR PFAM; PF01352; KRAB; 1. FT NON_TER 1 1 FT NON_TER 41 41 ** ** ################# SOURCE SECTION ################## ** Human Krueppel-type zinc finger protein (ZNF169) gene, partial cds. ** [1] ** 1-444 ** Dean M., Chidambaram A., Gerrard B.; ** ; ** Submitted (02-JUN-1995) to the EMBL/GenBank/DDBJ databases. ** Michael Dean, LVC, NCI-FCRDC, P.O. Box B, Frederick, MD 21702, USA ** NCBI gi: 903595 ** source 1..444 ** /organism="Homo sapiens" ** /map="9q22-31" ** /chromosome="9" ** CDS <59..>184 ** /gene="ZNF169" ** /note="NCBI gi: 903598" ** /codon_start=3 ** /product="Krueppel-type zinc finger protein" ** /db_xref="PID:g903598" ** CDS_1_OUT_OF_1 ** 26-JUL-1995 (Rel. 44, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01352; KRAB; 4; 41; T; 19-JUN-2000; SQ SEQUENCE 41 AA; 4816 MW; 653EF5ADE02B70AF CRC64; IDGFRDVAVA FTQKEWKLLS SAQRTLYREV MLENYSHLVS L // ID Q15175 PRELIMINARY; PRT; 535 AA. AC Q15175; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE PARANEOPLASTIC ANTIGEN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Fathallah-Shaykh H.M., Finizio J., Ho A., Rosenblum M., Posner J.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; L02867; AAA91850.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Homo sapiens 62 kDa paraneoplastic antigen mRNA, 3' end. ** [1] ** 1-2750 ** Fathallah-Shaykh H.M., Finizio J., Ho A., Rosenblum M., Posner J.; ** "Cloning and characterization of a second leucine zipper protein ** recognized by the sera of the patients with antibody associated ** paraneoplastic cerebellar degeneration"; ** Unpublished. ** NCBI gi: 1220352 ** source 1..2750 ** /organism="Homo sapiens" ** /cell_line="HeLa" ** /tissue_lib="1-ZapII" ** CDS <1..1608 ** /note="62 kDa; NCBI gi: 1220353" ** /codon_start=1 ** /product="paraneoplastic antigen" ** /db_xref="PID:g1220353" ** CDS_1_OUT_OF_1 ** 12-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 535 AA; 58014 MW; 6C80A459E888A1DA CRC64; YRIPGGGTWQ SARPRVGSRR AVDGEGARRG LCSPSSRRWR PGPPQPHCPG PRAPALSCAA AAPARRPRGH AESRRDGGLG SAEEEESWYD QQDLEQDLHL AAELGKTLLE RNKELEGSLQ QMYSTNEEQV QEIEYLTKQL DTLRHVNEQH AKVYEQLDLT ARDLELTNHR LVLESKAAQQ KIHGLTETIE RLQAQVEELQ AQVEQLRGLE QLRVLREKRE RRRTIHTFPC LKELCTSPRC KDAFRLHSSS LELPAAPGAG ERAAADPGGG AALPGEPGAA AQGAGGARVH RGAAGVLGAG APAVRDGGLS PACAGAGGRA AGAAADEAGQ DLPTGSGTTT WPRPCSHPSR RPLRPTIPSP AAGTTWAPRT GSPHRQPLQA TWCARAAATL RSTPSWPKTQ PAGTRATSHC TPTALRKRGM SILREVDEQY HALLEKYEEL LSKCRQHGAG VRDAGVQTSR PISRDSSWRD LRGGEEGQGE VKAGEKSLSQ HVEAVDKRLE QSQPEYKALF KEIFSRIQKT KADINATKVK THSSK // ID Q15371 PRELIMINARY; PRT; 150 AA. AC Q15371; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE RIBOSOMAL PROTEIN L18A HOMOLOGUE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Zenz K.I.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; X80821; CAA56787.1; -. KW Ribosomal protein. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for ribosomal protein L18a homologue ** [1] ** Zenz K.I.; ** ; ** Unpublished. ** [2] ** 1-660 ** Zenz K.I.; ** ; ** Submitted (02-AUG-1994) to the EMBL/GenBank/DDBJ databases. ** K.I. Zenz, Institute of Immunology, Christian-Albrechts University, ** Kiel, Michaelisstr. 5, 24105 Kiel, FRG ** source 1..660 ** /organism="Homo sapiens" ** /cell_type="lymphocyte" ** /cell_line="human periferal lymphocytes" ** CDS <200..652 ** /partial ** /codon_start=1 ** /product="ribosomal protein L18a homologue" ** /db_xref="PID:g527580" ** CDS_1_OUT_OF_1 ** 05-AUG-1994 (Rel. 40, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 150 AA; 18050 MW; 4E5E933C97FA075F CRC64; TEDLFLNMEH ESLTLEKKSK LEKNIKDDKS TKEKHVSKER NFKEERDKIK KESENLLLWG MSAIEESIGL HLVEKEIDIE KQEKHIKESK EKPEKRSQIK EKDIEKMERK TFDKGQAYIR ITQTKWPYKK GEKEQKYCCL LKKPDGQREK // ID Q15489 PRELIMINARY; PRT; 55 AA. AC Q15489; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE MYELIN ASSOCIATED GLYCOPROTEIN (FRAGMENT). GN S-MAG. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RX MEDLINE=98154940; PubMed=9495552; RA Miescher G., Luetzelschwab R., Erne B., Ferracin F., Huber S., RA Stack A.J.; RT "Reciprocal expression of myelin-associated glycoprotein splice RT variants in the adult human peripheral and central nervous systems."; RL Brain Res. Mol. Brain Res. 52:308-315(1997). DR EMBL; X98405; CAA67055.1; -. KW Myelin. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for myelin associated glycoprotein, S-MAG ** [1] ** Miescher G., Luetzelschwab R., Huber S., Ferracin F., Erne B., ** Stack A.J.; ** "Differential expression of human MAG isoforms in brain and ** nerve"; ** Unpublished. ** [2] ** 1-446 ** Miescher G.C.; ** ; ** Submitted (15-MAY-1996) to the EMBL/GenBank/DDBJ databases. ** G.C. Miescher, University Hospitals Basel, Neurobiology Lab. ** Department of Research, Hebelstrasse 20, Kantonsspital Basel, ** Basel, 4031, Switzerland ** source 1..446 ** /organism="Homo sapiens" ** /chromosome="19" ** /map="q13.1" ** /dev_stage="adult" ** /lab_host="E.coli" ** /isolate="pMAG-PCRII#11" ** /tissue_type="brain" ** CDS <1..169 ** /codon_start=2 ** /gene="S-MAG" ** /product="myelin associated glycoprotein" ** /db_xref="PID:e248458" ** misc_feature 137..181 ** /note="alternative splice from exon 12" ** CDS_1_OUT_OF_1 ** 11-JUN-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 55 AA; 6106 MW; 34D851778133F87F CRC64; AIVCYITQTR RKKNVTESPS FSAGDNPPVL FSSDFRISGA PEKYESKEVS TLESH // ID Q15559 PRELIMINARY; PRT; 102 AA. AC Q15559; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE (CLONE TEC14) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Piek E., Mosselman S.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; L32558; AAA36727.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone tec14) mRNA, partial cds. ** [1] ** 1-320 ** Piek E., Mosselman S.; ** ; ** Unpublished. ** NCBI gi: 483354 ** source 1..320 ** /organism="Homo sapiens" ** /cell_line="Tera-2 (EC)" ** /sequenced_mol="cDNA to mRNA" ** /tissue_lib="lambda GEM2" ** CDS <1..311 ** /note="(embryonal carcinoma) cells. The sequence may ** contain mismatches (one strand sequenced only once). ** 97% ** identical in 320 bp overlap with human 54 kDA prot; ** ORF. ** sequence is expressed in human Tera-2 clone 13; NCBI ** gi: ** 483355." ** /codon_start=3 ** /db_xref="PID:g483355" ** CDS_1_OUT_OF_1 ** 19-MAY-1994 (Rel. 39, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 102 AA; 11659 MW; B447711590819F74 CRC64; IQANVHKGHR QRTYGSVIPH ILPLHVLKKT FSLRDFHFSV SLKKNLVLTC LDLFLGVRTP RNDPFVSMML LFTRFLDRPS TILGTGLLYT EGLTVALRLR LS // ID Q15570 PRELIMINARY; PRT; 130 AA. AC Q15570; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE BTF2P44 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., RA Anzevino R., Velona I., Brahe C., Scheffer H., Van Ommen G.J.B., RA Buys C.H.C.M.; RL Eur. J. Hum. Genet. 0:0-0(0). DR EMBL; U21911; AAA64502.1; -. FT NON_TER 130 130 ** ** ################# SOURCE SECTION ################## ** Human basic transcription factor BTF2p44 mRNA, 5' end, partial cds. ** [1] ** der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., ** Anzevino R., VELONA I., Brahe C., Scheffer H., van Ommen G.J.B., ** Buys C.H.C.M.; ** "A provisional transcript map of the spinal muscular atrophy (SMA) ** critical region"; ** Unpublished. ** [2] ** 1-548 ** der Steege G.; ** ; ** Submitted (28-FEB-1995) to the EMBL/GenBank/DDBJ databases. ** Gerrit Van der Steege, University of Groningen, Department of ** Medical Genetics, Antonius Deusinglaan 4, Groningen, 9713 AW, The ** Netherlands ** NCBI gi: 736401 ** source 1..548 ** /clone="5G3 5'-end" ** /clone_lib="library of A. Bernards" ** /organism="Homo sapiens" ** /chromosome="5" ** /map="5q13.1" ** /cell_type="pre-B-cells" ** CDS 157..>548 ** /note="basic transcription factor 2, 44 kDa subunit; ** NCBI ** gi: 736404" ** /codon_start=1 ** /product="BTF2p44" ** /db_xref="PID:g736404" ** CDS_1_OUT_OF_1 ** 23-MAY-1995 (Rel. 43, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 130 AA; 15286 MW; C681910BD2069D13 CRC64; MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH GQVRLGMMRH LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP ISQIGIIVTK SKRAEKLTEL SGNPRKXISS // ID Q15597 PRELIMINARY; PRT; 699 AA. AC Q15597; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE TRANSLATION INITIATIONFACTOR EIF-4GAMMA (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=OVARY; RA Klaudiny J.J., von der Kammer H.H., Scheit K.K.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; Z34918; CAA84397.1; -. DR PFAM; PF02020; IF5_eIF4_eIF2; 1. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for translation initiation factor eIF-4gamma ** (partial) ** [1] ** 1-2124 ** Klaudiny J.J., von der Kammer H.H., Scheit K.K.; ** "Characterization of secretory proteins of human ovarian follicle ** cells by cDNA cloning"; ** Unpublished. ** [2] ** 1-2124 ** von der Kammer H.; ** ; ** Submitted (30-JUN-1994) to the EMBL/GenBank/DDBJ databases. ** Heinz von der Kammer, Abteilung fuer Molekulare Biologie, ** Max-Planck-Institut fuer Biophysikalische Chemie, Am Fassberg 11, ** Goettingen, D-37077, Germany ** source 1..2124 ** /organism="Homo sapiens" ** /dev_stage="adult" ** /tissue_type="ovary" ** CDS <1..2100 ** /note="putative" ** /codon_start=1 ** /note="homologue" ** /product="translation initiationfactor eIF-4gamma" ** /db_xref="PID:g510307" ** CDS_1_OUT_OF_1 ** 04-JUL-1994 (Rel. 40, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF02020; IF5_eIF4_eIF2; 618; 699; T; 19-JUN-2000; SQ SEQUENCE 699 AA; 79421 MW; DC65F87073258175 CRC64; RRSIGNIKFI GELFKLKMLT EAIMHDCVVK LLKNHDEESL ECLCRLLTTI GKDLDFEKAK PRMDQYFNQM EKIVKERKTS SRIRFMLQDV IDLRLCNWVS RRADQGPKTI EQIHKEAKIE EQEEQRKVQQ LMTKEKRRPG VQRVDEGGWN TVQGAKNSRV LDPSKFLKIT KPTIDEKIQL VPKAQLGSWG KGSSGGAKAS ETDALRSSAS SLNRFSALQP PAPSGSTPST PVEFDSRRTL TSRGSMGREK NDKPLPSATA RPNTFMRGGS SKDLLDNQSQ EEQRREMLET VKQLTGGVDV ERNSTEAERN KTRESAKPEI SAMSAHDKAA LSEEELERKS KSIIDEFLHI NDFKEAMQCV EELNAQGLLH VFVRVGVEST LERSQITRDH MGQLLYQLVQ SEKLSKQDFF KGFSETLELA DDMAIDIPHI WLYLAELVTP MLKEGGISMR ELTIEFSKPL LPVGRAGVLL SEILHLLCKQ MSHKKVGALW READLSWKDF LPEGEDVHNF LLEQKLDFIE SDSPCSSEAL SKKELSAEEL YKRLEKLIIE DKANDEQIFD WVEANLDEIQ MSSPTFLRAL MTAVCKAAII ADSSTFRVDT AVIKQRVPIL LKYLDSDTEK ELQALYALQA SIVKLDQPAN LLRMFFDCLY DEEVISEDAF YKWESSKDPA EQNGKGVALK SVTAFFTWLR EAEEESEDN // ID Q15636 PRELIMINARY; PRT; 450 AA. AC Q15636; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE TRANSCRIPTION FACTOR (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Lania L.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; L32162; AAA36767.1; -. DR INTERPRO; IPR001909; -. DR PFAM; PF01352; KRAB; 1. DR PFAM; PF02023; SCAN; 1. FT NON_TER 450 450 ** ** ################# SOURCE SECTION ################## ** Homo sapiens transcription factor mRNA, 5' end. ** [1] ** 1-1520 ** Lania L.; ** "Positional cloning of cDNAs from the human chromosome 3p21-22 ** region identifies a clustered organization of ZNF genes"; ** Unpublished. ** NCBI gi: 487835 ** source 1..1520 ** /organism="Homo sapiens" ** /sequenced_mol="cDNA to mRNA" ** CDS 171..>1520 ** /map="3p21-22" ** /note="NCBI gi: 487836" ** /product="transcription factor" ** /codon_start=1 ** /db_xref="PID:g487836" ** CDS_1_OUT_OF_1 ** 18-MAY-1994 (Rel. 39, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01352; KRAB; 232; 293; T; 19-JUN-2000; **PM PFAM; PF02023; SCAN; 48; 153; T; 19-JUN-2000; SQ SEQUENCE 450 AA; 50359 MW; A2CC962BAD05C5C2 CRC64; MPPGRWHAAI SSGPVFEGAR ALQTVKKEEE DESYTPVQAR RPQTLNRPGQ ELFRQLFRQL RYHESSGPLE TLSRLRELCR WWLRPDVLSK AQILELLVLE QFLSILPGEL RVWVQLHNPE SGEELWPCWR SCRGTLMGHP GGTRALPEPR CALDGYRSLR SAQIWSLASP LRSSSALGDH LEPPYEIEAR DFLAGQSDTP AAQMPALFPR EGCPGDQVTP TRSLTAQLQE TMTFKDVEVT FSQDEWGWLD SAQRNLYRDV MLENYRNMAS LVGPFTKPAL ISWLEAREPW GLNMQAAQPK GNPVAAPTGD DLQSKTNKFI LNQEPLEEAE TLAVSSGCPA TSVSEGIDRS ILRESFQQNQ SRDKMRDLRE GQMEPPKSEL IGWGGGETSR WVRGGASPPP ALSPLFRITW SGHKDLKDLK VRGLRGLEAP RVNVWETEAN QAASTPGPPA // ID Q15662 PRELIMINARY; PRT; 368 AA. AC Q15662; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE TRANSFORMATION-RELATED PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=EPITHELIUM; RA Shen H., Steinberg M.L.; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; L24521; AAA36776.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human transformation-related protein mRNA, 3' end. ** [1] ** 1-1240 ** Shen H., Steinberg M.L.; ** ; ** Unpublished. ** source 1..1240 ** /organism="Homo sapiens" ** /cell_type="SV40-transformed keratinocyte" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="epithelium" ** CDS <1..1109 ** /product="transformation-related protein" ** /codon_start=3 ** /db_xref="PID:g403460" ** repeat_region 1..283 ** /rpt_family="Alu" ** /note="Alu-like repeat" ** AA 1 -> 95 ** CDS_1_OUT_OF_1 ** 28-SEP-1993 (Rel. 37, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 368 AA; 42029 MW; A8B79E59EBBBA2B0 CRC64; DRLSLLSPRL ECNGMILAHC KLRLPGFKRF SCLSLPSSWD YRHVPPRQVH FVFSVETGFH RAGQAGLELL TSSVPPTSAF PKCWDYRRDD QAWPTLSSFR GLNKFAFLPK FFAHPISQFQ RVECNVGCPI LLAMKYLAYS SLPGADTMLY FYFYEQEASL AVCNICRQKF HWVLYQISHL YRGVIVDNFL LHPDGRFTWT IFFLSWVKQN SLVDFFFGTE SRSVALLPRL ECSGAMSTLH TVLRPAYSHI YHPDVKEKTH FLGNVFNKRK LQKKILKTPN PLCALHSAPS PSLPPFLRCT GRLPFYLGLD DFLFVAGALM FLPVSFLNPH TLTWPPQCCT RSDCNPLRGQ REISALSHSL PTGLSMPL // ID Q15706 PRELIMINARY; PRT; 112 AA. AC Q15706; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE 13 kDa DIFFERENTIATION-ASSOCIATED PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LUNG ADENOCARCINOMA; RA Wu M., Li B., Wang Z., Cai Y.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U34343; AAB03380.1; -. FT NON_TER 112 112 ** ** ################# SOURCE SECTION ################## ** Human 13kD differentiation-associated protein mRNA, partial cds. ** [1] ** 1-681 ** Wu M., Li B., Wang Z., Cai Y.; ** "Molecular cloning of differentiation associated gene from human ** lung adenocarcinoma cell line treated with all-trans retinoic ** acid"; ** Unpublished. ** [2] ** 1-681 ** Wu M.; ** ; ** Submitted (20-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** Min Wu, Department of Cell Biology, Cancer Institute, Chinese ** Academy of Medical Sciences, Panjiayuan, Chaoyang District, ** Beijing, 100021, China ** source 1..681 ** /organism="Homo sapiens" ** /clone="RA42" ** /sex="female" ** /cell_line="GLC-82" ** /tissue_type="lung adenocarcinoma" ** CDS 345..>681 ** /codon_start=1 ** /product="13kD differentiation-associated protein" ** /db_xref="PID:g995939" ** CDS_1_OUT_OF_1 ** 08-JUL-1996 (Rel. 48, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 112 AA; 13217 MW; 7751BF462C419080 CRC64; MGKNTFWDVE GSMVPPEWHR WLHSMTDDPP TTKPLTARKF IWTNHNFNVT GPQNNMYLIL PLERRFRSGS HLQHLTSKDN EEQLKHAKYG AFHVITLLLF TIHYNSQLKL CD // ID Q15734 PRELIMINARY; PRT; 232 AA. AC Q15734; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE PHOSPHATIDYLINOSITOL (4,5) BISPHOSPHATE 5-PHOSPHATASE HOMOLOG DE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Nussbaum R.L.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U45974; AAB03215.1; -. DR INTERPRO; IPR000300; -. DR PFAM; PF00783; IPPc; 1. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human phosphatidylinositol (4,5) bisphosphate 5-phosphatase homolog ** mRNA, partial cds. ** [1] ** 1-1616 ** Nussbaum R.L.; ** ; ** Submitted (11-JAN-1996) to the EMBL/GenBank/DDBJ databases. ** Robert L. Nussbaum, NCHGR, NIH, 49 Convent Drive, Bethesda, MD ** 20892, USA ** source 1..1616 ** /organism="Homo sapiens" ** /note="derived using EST HSC39F111, GenBank Accession ** Number F12413, and 5'RACE procedure" ** CDS <1..699 ** /note="phosphatidylinositol (4,5) bisphosphate ** 5-phosphatase homolog" ** /codon_start=1 ** /db_xref="PID:g1399103" ** CDS_1_OUT_OF_1 ** 08-JUL-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00783; IPPc; 2; 138; T; 19-JUN-2000; SQ SEQUENCE 232 AA; 26172 MW; 6C7B868147F97E75 CRC64; RQAWHEGFDE VFWFGDFNFR LSGGRTVVDA LLCQGLVVDV PALLQHDQLI REMRKGSIFK GFQEPDIHFL PSYKFDIGKD TYDSTSKQRT PSYTDRVLYR SRHKGDICPV SYSSCPGIKT SDHRPVYGLF RVKVRPGRDN IPLAAGKFDR ELYLLGIKRR ISKEIQRQQA LQSQNSSTIC SVFAERGLTA ATWGDCIDQN PLGRTKSLPP FGDPRDCGDR ASVPASQEGS QP // ID Q15735 PRELIMINARY; PRT; 397 AA. AC Q15735; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE PHOSPHATIDYLINOSITOL (4,5)BISPHOSPHATE 5-PHOSPHATASE HOMOLOG DE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RA Nussbaum R.L.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U45975; AAB03216.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human phosphatidylinositol (4,5)bisphosphate 5-phosphatase homolog ** mRNA, partial cds. ** [1] ** 1-1496 ** Nussbaum R.L.; ** ; ** Submitted (11-JAN-1996) to the EMBL/GenBank/DDBJ databases. ** Robert L. Nussbaum, NCHGR, NIH, 49 Convent Drive, Bethesda, MD ** 20892, USA ** source 1..1496 ** /organism="Homo sapiens" ** /note="derived using ESTs, GenBank Accession Number ** R13943 ** and R15390" ** /tissue_type="brain" ** /dev_stage="neonatal infant" ** CDS <1..1194 ** /note="phosphatidylinositol (4,5)bisphosphate ** 5-phosphatase ** homolog" ** /codon_start=1 ** /db_xref="PID:g1399105" ** CDS_1_OUT_OF_1 ** 08-JUL-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 397 AA; 43893 MW; 71418E311E24FBFA CRC64; ARGLHFVKFA IDSDQLHQLW EKDQLNMAKN TWPILKGFQE GPLNFAPTFK FDVGTNKYDT SAKKRKPAWT DRILWKVKAP GGGPSPSGRK SHRLQVTQHS YRSHMEYTVS DHKPVAAQFL LQFAFRDDMP LVRLEVADEW VRPEQAVVRY RMETVFARSS WDWIGLYRVG FRHCKDYVAY VWAKHEDVDG NTYQVTFSEE SLPKGHGDFI LGYYSHNHSI LIGITEPFQI SLPSSELASS STDSSGTSSE GEDDSTLELL APKSRSPSPG KSKRHRSRSP GLARFPGLAL RPSSRERRGA SRSPSPQSRR LSRVAPDRSS NGSSRGSSEE GPSGLPGPWA FPPAVPRSLG LLPALRLETV DPGGGGSWGP DREALAPNSL SPSPQGHRGL EEGGLGP // ID Q15752 PRELIMINARY; PRT; 73 AA. AC Q15752; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE RETINOBLASTOMA BINDING PROTEIN 3 (FRAGMENT). GN RBBP3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Vogt T., Welsh J., Stolz W., Kullmann F., Zamudio J., McClelland M.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U50848; AAB86738.1; -. FT NON_TER 1 1 FT NON_TER 73 73 ** ** ################# SOURCE SECTION ################## ** Human retinoblastoma binding protein 3 mRNA, partial cds. ** [1] ** 1-220 ** Vogt T., Welsh J., Stolz W., Kullmann F., McClelland M.; ** ; ** Submitted (06-MAR-1996) to the EMBL/GenBank/DDBJ databases. ** Thomas Vogt, Molecular Science, Sidney Kimmel Cancer Center, 11099 ** North Torrey Pines Road, San Diego, CA 92037, USA ** source 1..220 ** /organism="Homo sapiens" ** /dev_stage="newborn" ** /cell_type="melanocytes" ** CDS <1..>220 ** /gene="RBBP3" ** /note="mRNA is differentially regulated in TPA treated ** cells, i.e., upregulated; sequence has potential to ** form a ** zinc finger motif; new member of the RBBP familiy" ** /codon_start=3 ** /product="retinoblastoma binding protein 3" ** /db_xref="PID:g1480479" ** CDS_1_OUT_OF_1 ** 10-AUG-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 73 AA; 8363 MW; DC60BF32D7943E3A CRC64; GDSYHTFXXI PPLHDVPKGD WRCPKCLAQE CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM VPL // ID Q15810 PRELIMINARY; PRT; 77 AA. AC Q15810; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE CLONE 137308 ORF1 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Sampson M., McClendon D., Barlow C., Wiley K.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RA Hamilton R.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U60873; AAB05597.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human clone 137308 mRNA, partial cds. ** [1] ** 1-601 ** Sampson M., McClendon D., Barlow C., Wiley K.; ** "Human cDNA clone 137308"; ** Unpublished. ** [2] ** 1-601 ** Hamilton R.; ** ; ** Submitted (14-JUN-1996) to the EMBL/GenBank/DDBJ databases. ** Biological Sciences, Mississippi College, 200 South Capitol Street, ** Clinton, MS 39058, USA ** source 1..601 ** /organism="Homo sapiens" ** /clone="137308" ** CDS <1..235 ** /note="orf1 protein." ** /codon_start=2 ** /db_xref="PID:g1478282" ** CDS_1_OUT_OF_1 ** 03-AUG-1996 (Rel. 48, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 77 AA; 8689 MW; 0B3EBD4DF30BA6C2 CRC64; ARVQEGRPWR REPASIDACR LNFQRLRRRK FSNVLFPGLA QEALYSGGYH LKFADELMGG NLKKSTADAS GSRGHQL // ID Q15888 PRELIMINARY; PRT; 8 AA. AC Q15888; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP15H8A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32069; AAA73878.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP15H8A) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557141 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP15H8A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="chromosome X" ** /note="ORF; NCBI gi: 558107" ** /codon_start=2 ** /db_xref="PID:g558107" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 1068 MW; 0315A37EAB5B0763 CRC64; KPEYCWSR // ID Q15889 PRELIMINARY; PRT; 8 AA. AC Q15889; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP15H8B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32070; AAA73879.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP15H8B) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557142 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP15H8B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="chromosome X" ** /note="ORF; NCBI gi: 558108" ** /codon_start=1 ** /db_xref="PID:g558108" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 865 MW; 0474472325A761E7 CRC64; LHPSKLNG // ID Q15890 PRELIMINARY; PRT; 8 AA. AC Q15890; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP19G12A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32083; AAA73880.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP19G12A) mRNA, partial cds. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557146 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP19G12A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xp11.1-q11" ** /note="ORF; NCBI gi: 558109" ** /codon_start=1 ** /db_xref="PID:g558109" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 975 MW; 605EA6C5BEA5A2D3 CRC64; WVSCSQCY // ID Q15891 PRELIMINARY; PRT; 9 AA. AC Q15891; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP2E8B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32131; AAA73881.1; -. FT NON_TER 1 1 FT NON_TER 9 9 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP2E8B) mRNA, partial cds. ** [1] ** 1-26 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557154 ** source 1..26 ** /organism="Homo sapiens" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>26 ** /map="chromosome 17" ** /note="ORF; NCBI gi: 557735" ** /codon_start=1 ** /db_xref="PID:g557735" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 7) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 9 AA; 1030 MW; E56635A1A33686D1 CRC64; EHQMKTSLG // ID Q15892 PRELIMINARY; PRT; 9 AA. AC Q15892; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP3B4A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32071; AAA73882.1; -. FT NON_TER 1 1 FT NON_TER 9 9 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP3B4A) mRNA, partial EST. ** [1] ** 1-26 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557159 ** source 1..26 ** /organism="Homo sapiens" ** /clone="XP3B4A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>26 ** /map="Xq24" ** /note="ORF; NCBI gi: 558110" ** /codon_start=1 ** /db_xref="PID:g558110" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 9 AA; 971 MW; 49B22732CDC40B17 CRC64; ALERAVLLS // ID Q15893 PRELIMINARY; PRT; 8 AA. AC Q15893; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP587A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32073; AAA73883.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP587A) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557169 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP587A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq22" ** /note="ORF; NCBI gi: 558111" ** /codon_start=1 ** /db_xref="PID:g558111" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 874 MW; DAA1B6D7376456C5 CRC64; SQNPLQTS // ID Q15894 PRELIMINARY; PRT; 8 AA. AC Q15894; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP587B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32074; AAA73884.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP587B) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557170 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP587B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq22" ** /note="ORF; NCBI gi: 558112" ** /codon_start=1 ** /db_xref="PID:g558112" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 952 MW; EBC735B1E1F1B6D6 CRC64; MQTHHSLV // ID Q15895 PRELIMINARY; PRT; 8 AA. AC Q15895; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP6A10A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32075; AAA73885.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP6A10A) mRNA, partial EST. ** [1] ** 1-25 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557173 ** source 1..25 ** /organism="Homo sapiens" ** /clone="XP6A10A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>25 ** /map="Xq21.3-q22" ** /note="ORF; NCBI gi: 558113" ** /codon_start=1 ** /db_xref="PID:g558113" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 921 MW; C6C735B33686C1AA CRC64; DTQMKSLV // ID Q15896 PRELIMINARY; PRT; 9 AA. AC Q15896; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP6A10B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32076; AAA73886.1; -. FT NON_TER 1 1 FT NON_TER 9 9 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP6A10B) mRNA, partial EST. ** [1] ** 1-28 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557174 ** source 1..28 ** /organism="Homo sapiens" ** /clone="XP6A10B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>28 ** /map="Xq21.3-q22" ** /note="ORF; NCBI gi: 558114" ** /codon_start=1 ** /db_xref="PID:g558114" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 9 AA; 1047 MW; 11D15731B2C9C054 CRC64; ENIFVTLIV // ID Q15897 PRELIMINARY; PRT; 7 AA. AC Q15897; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP6A11A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32077; AAA73887.1; -. FT NON_TER 1 1 FT NON_TER 7 7 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP6A11A) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557175 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP6A11A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq22" ** /note="ORF; NCBI gi: 558115" ** /codon_start=3 ** /db_xref="PID:g558115" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 7 AA; 814 MW; 672B1DD3372046B0 CRC64; QILKAEL // ID Q15898 PRELIMINARY; PRT; 8 AA. AC Q15898; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP6A11B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32078; AAA73888.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP6A11B) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557176 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP6A11B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq22" ** /note="ORF; NCBI gi: 558116" ** /codon_start=1 ** /db_xref="PID:g558116" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 938 MW; 34A415B0477B45BB CRC64; ESYPISRS // ID Q15900 PRELIMINARY; PRT; 8 AA. AC Q15900; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP7B11A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32079; AAA73890.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP7B11A) mRNA, partial EST. ** [1] ** 1-25 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557179 ** source 1..25 ** /organism="Homo sapiens" ** /clone="XP7B11A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>25 ** /map="Xq27.3-q28,2,3,16" ** /note="ORF; NCBI gi: 558117" ** /codon_start=2 ** /db_xref="PID:g558117" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 931 MW; B5DDC403369AAEB1 CRC64; HCDMKRAA // ID Q15901 PRELIMINARY; PRT; 8 AA. AC Q15901; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP7B11B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32080; AAA73891.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP7B11B) mRNA, partial EST. ** [1] ** 1-25 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557180 ** source 1..25 ** /organism="Homo sapiens" ** /clone="XP7B11B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>25 ** /map="Xq27.3-q28, 2, 3, 16" ** /note="ORF; NCBI gi: 558118" ** /codon_start=1 ** /db_xref="PID:g558118" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 860 MW; 37D72878676729CB CRC64; EFLPGGLQ // ID Q15902 PRELIMINARY; PRT; 8 AA. AC Q15902; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP7E7A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32081; AAA73892.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP7E7A) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557183 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP7E7A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq24" ** /note="ORF; NCBI gi: 558119" ** /codon_start=2 ** /db_xref="PID:g558119" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 931 MW; 83D699CAB1B1B2C9 CRC64; FVTTDFMA // ID Q15903 PRELIMINARY; PRT; 7 AA. AC Q15903; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP7E7B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32082; AAA73893.1; -. FT NON_TER 1 1 FT NON_TER 7 7 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP7E7B) mRNA, partial cds. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557184 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP7E7B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq24" ** /note="ORF; NCBI gi: 558120" ** /codon_start=3 ** /db_xref="PID:g558120" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 7 AA; 849 MW; 6B040339CDD33DB0 CRC64; AKAFKRE // ID Q16467 PRELIMINARY; PRT; 43 AA. AC Q16467; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE PROTON ATPASE HOMOLOGUE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Bhat K.S.; RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases. DR EMBL; L05089; AAC15853.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human proton ATPase homologue mRNA, 3' end. ** [1] ** 1-373 ** Bhat K.S.; ** "Expressed sequence tags from a human cell line"; ** Unpublished. ** source 1..373 ** /organism="Homo sapiens" ** CDS 1..132 ** /note="Expressed Sequence Tag; amino acid sequence ** shows ** homology with carboxy end of yeast proton ATPase ** proteolipid chain (PIR:A34633)" ** /note="putative" ** /codon_start=1 ** /citation=[1] ** /partial ** /db_xref="PID:g190378" ** CDS_1_OUT_OF_1 ** 08-DEC-1992 (Rel. 34, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 43 AA; 4393 MW; 6E7292577E46BDB3 CRC64; VGSGAALADA QNPSLFVKIL IVEIFGSALA SLGSSSQFFR PPE // ID Q16779 PRELIMINARY; PRT; 51 AA. AC Q16779; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HEXOKINASE III (EC 2.7.1.1) (GLUCOKINASE) (HEXOKINASE TYPE IV) DE (FRAGMENT). GN HK3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Colosimo A., Calabrese G., Gennarelli M., Ruzzo A., Sangiuolo F., RA Magnani M., Palka G., Novelli G., DallaPiccola B.; RL Cytogenet. Cell Genet. 0:0-0(0). CC -!- CATALYTIC ACTIVITY: ATP + D-HEXOSE = ADP + D-HEXOSE 6-PHOSPHATE. DR EMBL; L37749; AAB03512.1; -. KW Transferase. FT NON_TER 1 1 FT NON_TER 51 51 ** ** ################# SOURCE SECTION ################## ** Human hexokinase III (HK3) gene, partial cds. ** [1] ** 1-245 ** Colosimo A., Calabrese G., Gennarelli M., Ruzzo A., Sangiuolo F., ** Magnani M., Palka G., Novelli G., Dallapiccola B.; ** "Assignment of the hexokinase type 3 (HK3) gene to human ** chromosome band 5q35.3 by somatic cell hybrids and in situ ** hybridization"; ** Unpublished. ** [2] ** 1-245 ** Colosimo A.; ** ; ** Submitted (11-NOV-1994) to the EMBL/GenBank/DDBJ databases. ** Sanita' Pubblica e Biologia Cellulare, Cattedra di Genetica Umana ** Universita, Via di Tor Vergata, 135, Rome 00133, Italy ** source 1..245 ** /organism="Homo sapiens" ** /clone="pHKIII" ** /map="5q35.3" ** /chromosome="5" ** CDS join(<1..103,197..>245) ** /gene="HK3" ** /EC_number="2.7.1.1" ** /codon_start=1 ** /product="hexokinase III" ** /db_xref="PID:g1402644" ** CDS_1_OUT_OF_1 ** 09-JUL-1996 (Rel. 48, Last updated, Version 4) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 51 AA; 5505 MW; 52380713EE23C165 CRC64; TWSGGPLGTM ALWPCSAPAL MQVWTRRPST PASRGLKRWS AACTWVKSSA T // ID Q92484 PRELIMINARY; PRT; 177 AA. AC Q92484; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-FEB-1997 (TrEMBLrel. 02, Last annotation update) DE ACID SPHINGOMYELINASE-LIKE PHOSPHODIESTERASE (FRAGMENT). GN ASML3A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Hofmann K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; Y08136; CAA69330.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for ASM-like phosphodiesterase 3a ** [1] ** Hofmann K.; ** "Acid Sphingomyelinase is a member of a multi-gene family and ** shares motifs with a large family of metallo-phosphoesterases"; ** Unpublished. ** [2] ** 1-863 ** Hofmann K.; ** ; ** Submitted (17-SEP-1996) to the EMBL/GenBank/DDBJ databases. ** K. Hofmann, Isrec (Swiss Inst. F. Exp. Canc. Res.), Bioinformatics ** Group, Chemin Des Boveresses 155, Ch/1066 Epalinges S/Lausanne, ** SWITZERLAND ** source 1..863 ** /organism="Homo sapiens" ** CDS <1..536 ** /codon_start=3 ** /gene="ASML3a" ** /product="acid sphingomyelinase-like ** phosphodiesterase" ** /note="putative" ** /db_xref="PID:e266650" ** CDS_1_OUT_OF_1 ** 19-SEP-1996 (Rel. 49, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 177 AA; 20634 MW; CA38DDAE817B87EC CRC64; DIFQKYSDVI AGQFYGHTHR DSIMVLSDKK GSPVNSLFVA PAVTPVKSVL EKQTNNPGIR LFQYDPRDYK LLDMLQYYLN LTEANLKGES IWKLEYILTQ TYDIEDLQPE SLYGLAKQFT ILDSKQFIKY YNYFFVSYDS SVTCDKTCKA FQICAIMNLD NISYADCLKQ LYIKHKY // ID Q92485 PRELIMINARY; PRT; 465 AA. AC Q92485; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE ACID SPHINGOMYELINASE-LIKE PHOSPHODIESTERASE. GN ASML3B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Hofmann K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; Y08134; CAA69328.1; -. DR INTERPRO; IPR000934; -. ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for ASM-like phosphodiesterase 3b ** [1] ** Hofmann K.; ** "Acid Sphingomyelinase is a member of a multi-gene family and ** shares motifs with a large family of metallo-phosphoesterases"; ** Unpublished. ** [2] ** 1-1610 ** Hofmann K.; ** ; ** Submitted (17-SEP-1996) to the EMBL/GenBank/DDBJ databases. ** K. Hofmann, Isrec (Swiss Inst. F. Exp. Canc. Res.), Bioinformatics ** Group, Chemin Des Boveresses 155, Ch/1066 Epalinges S/Lausanne, ** SWITZERLAND ** source 1..1610 ** /organism="Homo sapiens" ** CDS 122..1519 ** /gene="ASML3b" ** /product="acid sphingomyelinase-like ** phosphodiesterase" ** /note="putative" ** /db_xref="PID:e266651" ** CDS_1_OUT_OF_1 ** 19-SEP-1996 (Rel. 49, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS50185; PHOSPHO_ESTER; 21; 284; T; 19-JUN-2000; SQ SEQUENCE 465 AA; 51895 MW; AE9FBF92A2C1ED32 CRC64; MRLLAWLIFL ANWGGARAEP GKFWHIADLH LDPDYKVSKD PFQVCPSAGS QPVPDAGPWG DYLCDSPWAL INSSIYAMKE IEPEPDFILW TGDDTPHVPD EKLGEAAVLE IVERLTKLIR EVFPDTKVYA ALGNHDFHPK NQFPAGSNNI YNQIAELWKP WLSNESIALF KKGAFYCEKL PGPSGAGRIV VLNTNLYYTS NALTADMADP GQQFQWLEDV LTDASKAGDM VYIVGHVPPG FFEKTQNKAW FREGFNEKYL KVVRKHHRVI AGQFFGHHHT DSFRMLYDDA GVPISAMFIT PGVTPWKTTL PGVVNGANNP AIRVFEYDRA TLSLXDMVTY FMNLSQANAQ GTPRWELEYQ LTEAYGVPDA SAHSIDTVLD RIAGDQSTLQ RYYVYNSVSY SAGVCDEACS MQHVCAMRQV DIDAYTTCLY ASGTTPVPQL PXLLMALLGL CTTRAVTCQA HHSSW // ID Q92661 PRELIMINARY; PRT; 55 AA. AC Q92661; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE UV-B REPRESSED SEQUENCE, HUR 7 (FRAGMENT). GN HUR 7. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Abts H.F., Breuhahn K., Michel G., Esser P., Ruzicka T.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; X98307; CAA66951.1; -. DR INTERPRO; IPR000215; -. DR PFAM; PF00079; serpin; 1. DR HSSP; P05619; 1HLE. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for UV-B repressed sequence, HUR 7 ** [1] ** Abts H.F., Breuhahn K., Michel G., Esser P., Ruzicka T.; ** "Analysis of UV-B modulated gene expression in human keratinocytes ** by mRNA differential display PCR (DD-PCR)"; ** Unpublished. ** [2] ** 1-405 ** Abts H.F.; ** ; ** Submitted (22-MAY-1996) to the EMBL/GenBank/DDBJ databases. ** H.F. Abts, Heinrich-Heine-Universitaet Duesseldorf, Dermatologie, ** Cytokinlabor, Geb.11.80, Moorenstrasse 5, 40225 Duesseldorf, FRG ** source 1..405 ** /organism="Homo sapiens" ** /cell_line="HaCaT" ** /cell_type="keratinocyte" ** CDS <1..170 ** /codon_start=3 ** /gene="HUR 7" ** /db_xref="PID:e260052" ** CDS_1_OUT_OF_1 ** 01-SEP-1996 (Rel. 49, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00079; serpin; 2; 34; T; 19-JUN-2000; SQ SEQUENCE 55 AA; 6224 MW; 107A694FEA43F7E6 CRC64; LEDLQAKILG IPYKNNDLSM FVLLPNDIDG LEKVNAYTSL FFLSFPKAFC LRASE // ID Q92771 PRELIMINARY; PRT; 734 AA. AC Q92771; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HELICASE (FRAGMENT). GN CHLR2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Amann J.M., Kidd V.J., Lahti J.M.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U33834; AAB06963.1; -. KW Helicase. FT NON_TER 1 1 FT NON_TER 734 734 ** ** ################# SOURCE SECTION ################## ** Human CHL1-related helicase (CHLR2) mRNA, partial cds. ** [1] ** 1-2202 ** Amann J.M., Kidd V.J., Lahti J.M.; ** "Isolation and characterization of a human gene related to the ** yeast chromosome transmission fidelity gene, CHL1"; ** Unpublished. ** [2] ** 1-2202 ** Lahti J.M.; ** ; ** Submitted (11-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** Jill M. Lahti, St. Jude Children's Research Hospital, Tumor Cell ** Biology, 332 N. Lauderdale St., Memphis, TN 38105, USA, 38105 ** source 1..2202 ** /organism="Homo sapiens" ** /clone="human CHL-Related 2" ** /clone_lib="HeLa cDNA, K562 cDNA, human fetal liver ** cDNA" ** CDS <1..>2202 ** /gene="CHLR2" ** /codon_start=1 ** /product="helicase" ** /db_xref="PID:g1517818" ** CDS_1_OUT_OF_1 ** 01-SEP-1996 (Rel. 49, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 734 AA; 82439 MW; FBAC66E4801D5F73 CRC64; HRVQLKYAAK RLRQEEEERE NLLRLSREML ETGPEAEWLE QLESGEEELV LAEYESDEEK KVASGVDEDE DDLEEEHITK IYYCSRTHSQ LAQFVHEVKK SPFGKDVRLV SLGSQQNLCV NEDVRSLGSV QLINDRCVDM QRSRHEKKKG AEEEKPKRRR QEKQAACPFY NHEQMGLLRD EALAEVKDME QLLALGKEAR ACPYYRSRLA IPAAQLVVLS YQMLLHAATR QAAGIRLQDQ VVIIDEAHNL IDTITGMHSV EVSGSQLCQA HSQLLQYMER YGKRLKAKNL MYLKQILYLL EKFVAVLGGN IKQNPNTQSL SQTGMELKTI NDFLFQSQID NINLFKVQRY CEKSMISRKL FGFTERYGAV FSSREQPKLA GFQQFLQSLQ PRTTEALAAP ADESQASVPQ PASPLMHIEG FLAALTTANQ DGRVILSRQG SLSQSTLKFL LLNPAVHFAQ VVKECRAVVI AGGTMQPVSD FRQQLLACAG VEAERVVEFS CGHVIPPDNI LPLVICIGVS NQPLEFTFQK RDLPQMMDEV GRILCNLCSV VSGGVVCFFP SYEYLRQVHA HWEKGGLLGH LAARKKIFQE PKSAHQVEQV LLAYSRCIQA CGQERGPVTG ALLLSVVGGK MSEGINFSDN LGRCVVMVGM PFPNIRSAEL QEKMAYLDQT LPRAPGQAPP GKALVENLCM KAVNQSIGRA IRHQKDFASI VLLDQRYARP PVLAKLPAWI RARV // ID Q92792 PRELIMINARY; PRT; 177 AA. AC Q92792; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-FEB-1997 (TrEMBLrel. 02, Last annotation update) DE D13S824E LOCUS (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BONE MARROW; RA Still I.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U47635; AAB18856.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human D13S824E locus mRNA, complete cds. ** [1] ** 1-2486 ** Still I.; ** ; ** Submitted (29-JAN-1996) to the EMBL/GenBank/DDBJ databases. ** Ivan Still, Neurosciences, Cleveland Clinic Foundation, 9500 Euclid ** Avenue, Cleveland, Ohio 44195, USA ** Auffray, C. et al (1995). IMAGE: Integration molecular analysis of ** the human genome and its expression. C.R. Acad. Sci. Paris 318: ** 263-272. ** source 1..2486 ** /organism="Homo sapiens" ** /chromosome="13" ** /tissue_type="bone marrow" ** /cell_type="HeLa" ** /clone_lib="Clontech catolog HL5005a; Stratagene ** catalog ** 936201" ** CDS <1..534 ** /note="DSEG number: D13S824E; orf" ** /codon_start=1 ** /db_xref="PID:g1669391" ** CDS_1_OUT_OF_1 ** 15-NOV-1996 (Rel. 49, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 177 AA; 20647 MW; 9005F0FE031F92B5 CRC64; KRRAQVEGED LFPVAISFGR PKEYFPPLYS SESHRFTVLE PNTVSFNFKF WRNMYHQFDR TLHPRQSVFN IIMNMNEQNK QLEKDIKDLE SKIKQRKNKQ TDGILTKELL HSVHPESPNL KTSLCFKEQT LLPVNDALRT IEGSSPADNR YSEYAEEFSK SEPAVVSLEY GVARMTC // ID O54521 PRELIMINARY; PRT; 144 AA. AC O54521; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE SLYA. GN SLYA. OS Salmonella enterica serovar Typhi (made up common name to get long OS OS line){EI3}. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Salmonella. OX NCBI_TaxID=90370, 119912; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=TY2, RF-1; RA Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., RA Nonaka T., Matsui H., Kawahara K., Danbara H.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. DR EMBL; AB010777; BAA24582.1; -. DR EMBL; AB010776; BAA24581.1; -. DR InterPro; IPR001835; A_TESTDOMAIN. DR InterPro; IPR000835; B_TESTDOMAIN. DR Pfam; PF01047; MarR; 1. DR PRINTS; PR00598; HTHMARR. DR SMART; SM1234; Smarty. DR PROSITE; PS01117; HTH_MARR_FAMILY; 1. ** ** ################# SOURCE SECTION ################## ** Salmonella choleraesuis serovar Typhi gene for SlyA, complete cds. ** [1] ** 1-636 ** Okada N.; ** ; ** Submitted (27-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Nobuhiko Okada, Kitasato University, School of Pharmaceutical ** Sciences, ** Department of Microbiology; 5-9-1 Shirokane, Minato, Tokyo 108-8641, ** Japan (E-mail:okadan@platinum.pharm.kitasato-u.ac.j p, ** Tel:03-3444-6161, ** Fax:03-3444-4831) ** [2] ** Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., Nonaka ** T., ** Matsui H., Kawahara K., Danbara H.; ** "Identification of TTG initiation codon in slyA of Salmonella, a gene ** required for survival within macrophages"; ** Unpublished. ** [1] ** 1-636 ** Okada N.; ** ; ** Submitted (27-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Nobuhiko Okada, Kitasato University, School of Pharmaceutical ** Sciences, ** Department of Microbiology; 5-9-1 Shirokane, Minato, Tokyo 108-8641, ** Japan (E-mail:okadan@platinum.pharm.kitasato-u.ac.j p, ** Tel:03-3444-6161, ** Fax:03-3444-4831) ** [2] ** Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., Nonaka ** T., ** Matsui H., Kawahara K., Danbara H.; ** "Identification of TTG initiation codon in slyA of Salmonella, a gene ** required for survival within macrophages"; ** Unpublished. ** source 1..636 ** /organism="Salmonella choleraesuis serovar Typhi" ** /sequenced_mol="DNA" ** /strain="Ty2" ** CDS 154..588 ** /codon_start=1 ** /db_xref="PID:d1025502" ** /transl_table=11 ** /gene="slyA" ** /product="SlyA" ** CDS_IN_EMBL_ENTRY 1 ** ORGANISM DOESN'T EXIST IN SP ** 11-FEB-1998 (Rel. 54, Last updated, Version 2) ** source 1..636 ** /organism="Salmonella choleraesuis choleraesuis" ** /sequenced_mol="DNA" ** /strain="RF-1" ** CDS 154..588 ** /codon_start=1 ** /db_xref="PID:d1025501" ** /transl_table=11 ** /gene="slyA" ** /product="SlyA" ** CDS_IN_EMBL_ENTRY 1 ** ORGANISM DOESN'T EXIST IN SP ** 11-FEB-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **PM PFAM; PF01047; MarR; 29; 133; T; 19-JUN-2000; **PM PRINTS; PR00598; HTHMARR; 47; 63; T; 19-JUN-2000; **PM PRINTS; PR00598; HTHMARR; 64; 79; T; 19-JUN-2000; **PM PRINTS; PR00598; HTHMARR; 83; 99; T; 19-JUN-2000; **PM PRINTS; PR00598; HTHMARR; 113; 133; T; 19-JUN-2000; **PM PROSITE; PS01117; HTH_MARR_FAMILY; 62; 96; T; 19-JUN-2000; SQ SEQUENCE 144 AA; 16448 MW; 4647F7704F2D78DE CRC64; MESPLGSDLA RLVRIWRALI DHRLKPLELT QTHWVTLHNI HQLPPDQSQI QLAKAIGIEQ PSLVRTLDQL EDKGLISRQT CASDRRAKRI KLTEKAEPLI AEMEEVIHKT RGEILAGISS EEIELLIKLV AKLEHNIMEL HSHD // ID TRA9_MYCTU STANDARD; PRT; 278 AA. AC P19774; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE PUTATIVE TRANSPOSASE FOR INSERTION SEQUENCE ELEMENT IS986/IS6110 DE (ORFB). GN (RV0796 OR MTV042.06) AND (RV2106 OR MTCY261.02) AND GN (RV2279 OR MTCY339.31C) AND (RV2355 OR MTCY98.24) AND GN (RV2814C OR MTCY16B7.29) AND (RV3185 OR MTV014.29) AND GN (RV3187 OR MTV014.31) AND (RV3326 OR MTV016.26). OS Mycobacterium tuberculosis. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1773; KW Transposable element; Transposition; DNA-binding; DNA recombination. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 278 AA; 31369 MW; E4D33328228D7676 CRC64; MPIAPSTYYD HINREPSRRE LRDGELKEHI SRVHAANYGV YGARKVWLTL NREGIEVARC TVERLMTKLG LSGTTRGKAR RTTIADPATA RPADLVQRRF GPPAPNRLWV ADLTYVSTWA GFAYVAFVTD AYARRILGWR VASTMATSMV LDAIEQAIWT RQQEGVLDLK DVIHHTDRGS QYTSIRFSER LAEAGIQPSV GAVGSSYDNA LAETINGLYK TELIKPGKPW RSIEDVELAT ARWVDWFNHR RLYQYCGDVP PVELEAAYYA QRQRPAAG // ID Q9ZQ91 PRELIMINARY; PRT; 312 AA. AC Q9ZQ91; DT 01-MAY-1999 (TrEMBLrel. 10, Created) DT 01-MAY-1999 (TrEMBLrel. 10, Last sequence update) DT 01-JUN-2001 (TrEMBLrel. 17, Last annotation update) DE PUTATIVE HYDROLASE (CONTAINS AN ESTERASE/LIPASE/THIOESTERASE ACTIVE DE SITE SERINE DOMAIN (PROSITE: PS50187). GN T4M8.1. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; eudicotyledons; core eudicots; Rosidae; eurosids II; OC Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Lin X., Kaul S., Shea T.P., Fujii C.Y., Shen M., VanAken S.E., RA Barnstead M.E., Mason T.M., Bowman C.L., Ronning C.M., Benito M., RA Carrera A.J., Creasy T.H., Buell C.R., Town C.D., Nierman W.C., RA Fraser C.M., Venter J.C.; RT "Arabidopsis thaliana chromosome II BAC T4M8 genomic sequence."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. DR EMBL; AC006284; AAD17422.1; -. DR InterPro; IPR000379; Est_lip_thioest_actsite. KW Hydrolase. ** ** ################# SOURCE SECTION ################## ** Arabidopsis thaliana chromosome II BAC T4M8 genomic sequence, ** complete sequence. ** [1] ** 1-89137 ** Lin X., Kaul S., Shea T.P., Fujii C.Y., Shen M., VanAken S.E., ** Barnstead M.E., Mason T.M., Bowman C.L., Ronning C.M., Benito M., ** Carrera A.J., Creasy T.H., Buell C.R., Town C.D., Nierman W.C., ** Fraser C.M., Venter J.C.; ** "Arabidopsis thaliana chromosome II BAC T4M8 genomic sequence"; ** Unpublished. ** [2] ** 1-89137 ** Lin X., Kaul S.; ** ; ** Submitted (05-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** The Institute for Genomic Research, 9712 Medical Center Dr, Rockville, ** MD 20850, USA, xlin@tigr.org ** [3] ** 1-89137 ** Lin X.; ** ; ** Submitted (04-MAR-1999) to the EMBL/GenBank/DDBJ databases. ** The Institute for Genomic Research, 9712 Medical Center Dr., Rockville, ** MD 20850, USA ** On Mar 4, 1999 this sequence version replaced gi:4156124. ** Address all correspondence to: ** Xiaoying Lin ** The Institute for Genomic Research ** 9712 Medical Center Dr. ** Rockville, MD 20850, USA ** e-mail: xlin@tigr.org ** BAC clone T4M8 is from Arabidopsis chromosome II and is contained ** in the YAC clone CIC11A04. ** The orientation of the sequence is from SP6 to T7 end of the BAC ** clone. ** Genes were identified by a combination of three methods: Gene ** prediction programs including GRAIL (available by anonymous ftp ** from arthur.epm.ornl.gov), Genefinder (Phil Green, University of ** Washington), Genscan (Chris Burge, ** http://gnomic.stanford.edu/~chris/GENSCANW.html), and NetPlantGene ** (http://www.cbs.dtu.dk/netpgene/cbsnetpgene.html), searches of the ** complete sequence against a peptide database and the Arabidopsis ** EST database at TIGR (http://www.tigr.org/tdb/at/at.html). ** Annotated genes are named to indicate the level of evidence for ** their annotation. Genes with similarity to other proteins are named ** after the database hits. Genes without significant peptide ** similarity but with EST similarity are named as 'unknown' proteins. ** Genes without protein or EST similarity, that are predicted by more ** than two gene prediction programs over most of their length are ** annotated as 'hypothetical' proteins. Genes encoding tRNAs are ** predicted by tRNAscan-SE (Sean Eddy, ** http://genome.wustl.edu/eddy/tRNAscan-SE/). Simple repeats are ** identified by repeatmasker (Arian Smit, ** http://ftp.genome.washington.edu/RM/RepeatMasker.html). Regions of ** genomic sequence that are not annotated as genes but have predicted ** exons by GRAIL are annotated as misc features. ** source 1..89137 ** /organism="Arabidopsis thaliana" ** /chromosome="II" ** /db_xref="taxon:3702" ** /cultivar="Columbia" ** /map="CIC11A04" ** /clone="T4M8" ** CDS complement(1731..2669) ** /codon_start=1 ** /db_xref="PID:g4335745" ** /gene="T4M8.1" ** /product="putative hydrolase (contains an ** esterase/lipase/thioesterase active site serine domain ** (prosite: PS50187)" ** /protein_id="AAD17422.1" ** CDS_IN_EMBL_ENTRY 30 ** 12-MAR-1999 (Rel. 59, Last updated, Version 4) ** ################# INTERNAL SECTION ################## **ID XXXX_ARATH **PM PROSITE; PS50187; ESTERASE; 69; 174; T; 28-JAN-2000; SQ SEQUENCE 312 AA; 34750 MW; 1D9B933F2BE9DD78 CRC64; MDSVIAFDRS PMFRVYKSGR IERLLGETTV PPSLTPQNGV VSKDIIHSPE KNLSLRIYLP EKVTVKKLPI LIYFHGGGFI IETAFSPPYH TFLTSAVAAA NCLAISVNYR RAPEFPVPIP YEDSWDSLKW VLTHITGTGP ETWINKHGDF GKVFLAGDSA GGNISHHLTM RAKKEKLCDS LISGIILIHP YFWSKTPIDE FEVRDVGKTK GVEGSWRVAS PNSKQGVDDP WLNVVGSDPS GLGCGRVLVM VAGDDLFVRQ GWCYAEKLKK SGWEGEVEVM ETKNEGHVFH LKNPNSDNAR QVVKKLEEFI NK // ID Q9JSZ7 PRELIMINARY; PRT; 355 AA. AC Q9JSZ7; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE UDP-N-acetylglucosamine--N-acetylmuramyl-(pentape pyrophosphoryl- DE undecaprenol N-acetylglucosamine transferase (EC 2.4.1.){EI1}. GN MURG OR NMA2062{EP4}. OS Neisseria meningitidis (serogroup A){EP3}. OC Bacteria; Proteobacteria; beta subdivision; Neisseriaceae; Neisseria. OX NCBI_TaxID=65699; RN [1]{EP3} RP SEQUENCE FROM N.A. RC STRAIN=Z2491 / SEROGROUP A / SEROTYPE 4A; RX MEDLINE=20222556; PubMed=10761919; RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C., RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., RA Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., RA Jagels K., Leather S., Moule S., Mungall K., Quail M.A., RA Rajandream M.A., Rutherford K.M., Simmonds M., Skelton J., RA Whitehead S., Spratt B.G., Barrell B.G.; RT "Complete DNA sequence of a serogroup A strain of Neisseria RT menigitidis Z2491."; RL Nature 404:502-506(2000). DR EMBL; AL162758; CAB85280.1; -.{EI1} KW Transferase{EP2}; Glycosyltransferase{EP2}; Complete proteome{EP5}. ** ** ################# SOURCE SECTION ################## ** Neisseria meningitidis serogroup A strain Z2491 complete genome; segment ** 7/7 ** [1] ** 1-195767 ** Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C., Klee S.R., ** Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., ** Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S., ** Moule S., Mungall K., Quail M.A., Rajandream M.A., Rutherford K.M., ** Simmonds M., Skelton J., Whitehead S., Spratt B.G., Barrell B.G.; ** "Complete DNA sequence of a serogroup A strain of Neisseria menigitidis ** Z2491"; ** Nature 404:502-506(2000). ** [2] ** 1-195767 ** Parkhill J.; ** ; ** Submitted (30-MAR-2000) to the EMBL/GenBank/DDBJ databases. ** Submitted on behalf of the Neisseria sequencing team, Sanger Centre, ** Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA E-mail: ** parkhill@sanger.ac.uk ** Notes: ** ** Details of N. meningitidis sequencing at the Sanger Centre ** are available on the World Wide Web. ** (URL, http://www.sanger.ac.uk/Projects/N_meningitidis/) ** ** source 1..195767 ** /db_xref="taxon:487" ** /note="serogroup: A" ** /organism="Neisseria meningitidis" ** /strain="Z2491" ** CDS complement(21643..22710) ** /note="NMA2062, murG, ** UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) ** pyrophosphoryl-undecaprenol N-acetylglucosamine ** transferase, len: 355aa; similar to many eg. SW:P17443 ** (MURG_ECOLI) murG, ** UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) ** pyrophosphoryl-undecaprenol N-acetylglucosamine transferase ** from Escherichia coli (354 aa) fasta scores; E(): 0, 46.2% ** identity in 346 aa overlap." ** /transl_table=11 ** /gene="murG" ** /product="UDP-N-acetylglucosamine--N-acetylmuramyl-(pentape ** pyrophosphoryl-undecaprenol N-acetylglucosamine ** transferase" ** /EC_number="2.4.1.-" ** /protein_id="CAB85280.1" ** misc_feature complement(22163..22172) ** /label=DUS ** /note="Core DNA uptake sequence: gccgtctgaa" ** AA 181 -> 183 ** CDS_IN_EMBL_ENTRY 179 ** 30-MAR-2000 (Rel. 63, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **CP 65699; Chromosome; 2011349; -1065; ATG; ; AL157959.1. **EV EI1; EMBL; -; CAB85280.1; 21-AUG-2000. **EV EP2; TREMBL; -; CAB85280.1; 21-AUG-2000. **EV EP3; RefFix; -; -; 20-SEP-2000. **EV EP4; GenFix; -; v1.2; 20-SEP-2000. **EV EP5; ProtChange; -; addKW; 01-MAY-2001. **ID XXXX_NEIME SQ SEQUENCE 355 AA; 38056 MW; DD93836BB897C401 CRC64; MGGKTFMLMA GGTGGHIFPA LAVADSLRAR GHHVIWLGSK DSMEERIVPQ YDILLETLAI KGVRGNGIKR KLMLPFTLYQ TVREAQQIIR KHRVECVIGF GGFVTFPGGL AAKLLGVPIV IHEQNAVAGL SNRHLSRWAK RVLYAFPKAF SHEGGLVGNP VRADISNLPV PAERFQGREG RLKILVVGGS LGADVLNKTV PQALALLPDN ARPQMYHQSG RGKLGSLQAD YDALGVQAEC VEFITDMVSA YRDADLVICR AGALTIAELT AAGLGALLVP YPHAVDDHQT ANARFMVQAE AGLLLPQTQL TAEKLAEILG GLNREKCLKW AENARTLALP HSADDVAEAA IACAA // ID ALYS_MYCPH STANDARD; PRT; 17 AA. AC P81528; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Autolysin (EC 3.5.1.28) (N-acetylmuramoyl-L-alanine amidase) DE (Peptidoglycan hydrolase) (Fragment). GN LYTA. OS Mycobacterium phlei. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1771; RN [1] RP SEQUENCE. RC STRAIN=425; RX MEDLINE=99140149; PubMed=10206696; RA Li Z.S., Beveridge T.J., Betts J., Clarke A.J.; RT "Partial characterization of a major autolysin from Mycobacterium RT phlei."; RL Microbiology 145:169-176(1999). CC -!- CATALYTIC ACTIVITY: HYDROLYZES THE LINK BETWEEN N-ACETYLMURAMOYL CC RESIDUES AND L-AMINO ACID RESIDUES IN CERTAIN BACTERIAL CELL-WALL CC GLYCOPEPTIDES. CC -!- MISCELLANEOUS: THE OPTIMUM PH OF THIS ENZYME IS 7.5. KW Hydrolase; Cell wall. FT VARIANT 1 1 V -> I OR L. FT VARIANT 2 2 A -> G. FT VARIANT 14 14 I -> L. FT NON_TER 1 1 FT NON_TER 17 17 ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 17 AA; 1817 MW; 1FACA3240F5C4EC5 CRC64; VAVKATTTEE ETEIPAK // ID GAG_HV1MN STANDARD; PRT; 506 AA. AC P05888; DT 01-NOV-1988 (Rel. 09, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE GAG POLYPROTEIN [Contains: CORE PROTEINS P17, P24, P2, P7, P1, P6]. GN GAG. OS Human immunodeficiency virus type 1 (MN isolate) (HIV-1). OC Viruses; Retroid viruses; Retroviridae; Lentivirus. OX NCBI_TaxID=11696; RN [1] RP SEQUENCE, AND POST-TRANSLATIONAL MODIFICATIONS. RX MEDLINE=92194415; PubMed=1548743; RA Henderson L.E., Bowers M.A., Sowder R.C. II, Serabyn S.A., RA Johnson D.G., Bess J.W. Jr., Arthur L.O., Bryant D.K., Fenselau C.; RT "Gag proteins of the highly replicative MN strain of human RT immunodeficiency virus type 1: posttranslational modifications, RT proteolytic processings, and complete amino acid sequences."; RL J. Virol. 66:1856-1865(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88219542; PubMed=3369091; RA Gurgo C., Guo H.-G., Franchini G., Aldovini A., Collalti E., RA Farrell K., Wong-Staal F., Gallo R.C., Reitz M.S. Jr.; RT "Envelope sequences of two new United States HIV-1 isolates."; RL Virology 164:531-536(1988). RN [3] RP STRUCTURE BY NMR OF 380-434. RX MEDLINE=93278285; PubMed=1304355; RA Summers M.F., Henderson L.E., Chance M.R., Bess J.W. Jr., South T.L., RA Blake P.R., Sagi I., Perez-Alvarado G., Sowder R.C. III, Hare D.R., RA Arthur L.O.; RT "Nucleocapsid zinc fingers detected in retroviruses: EXAFS studies of RT intact viruses and the solution-state structure of the nucleocapsid RT protein from HIV-1."; RL Protein Sci. 1:563-574(1992). CC -!- FUNCTION: PERFORMS HIGHLY COMPLEX ORCHESTRATED TASKS DURING THE CC ASSEMBLY, BUDDING, MATURATION, AND INFECTION STAGES OF THE VIRAL CC REPLICATION CYCLE. DURING VIRAL ASSEMBLY, THE PROTEINS FORM CC MEMBRANE ASSOCIATIONS AND SELF-ASSOCIATIONS THAT ULTIMATELY RESULT CC IN BUDDING OF AN IMMATURE VIRION FROM THE INFECTED CELL. GAG CC PRECURSORS ALSO FUNCTION DURING VIRAL ASSEMBLY TO SELECTIVELY BIND CC AND PACKAGE TWO PLUS STRANDS OF GENOMIC RNA. CC -!- PTM: THE P24 PROTEIN IS PHOSPHORYLATED. CC -!- MISCELLANEOUS: THE MN ISOLATE WAS TAKEN FROM A PEDIATRIC AIDS CC PATIENT IN 1984. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M17449; AAA44853.1; -. DR PIR; A38068; A38068. DR PDB; 1AAF; 31-JAN-94. DR InterPro; IPR000721; Gag_p24. DR InterPro; IPR000071; Retroviral_gag_p17. DR InterPro; IPR001878; Znf_CCHC. DR Pfam; PF00540; gag_p17; 1. DR Pfam; PF00607; gag_p24; 1. DR Pfam; PF00098; zf-CCHC; 2. DR PRINTS; PR00939; C2HCZNFINGER. DR PRINTS; PR00234; HIV1MATRIX. DR SMART; SM00343; ZnF_C2HC; 2. DR HIV; M17449; GAG$MN. KW AIDS; Core protein; Polyprotein; Myristate; Phosphorylation; KW Zinc-finger; 3D-structure. FT INIT_MET 0 0 FT CHAIN 1 134 CORE PROTEIN P17 (MATRIX ANTIGEN). FT CHAIN 135 365 CORE PROTEIN P24 (CORE ANTIGEN). FT CHAIN 366 379 CORE PROTEIN P2. FT CHAIN 380 434 CORE PROTEIN P7 (NUCLEOCAPSID PROTEIN). FT CHAIN 435 450 CORE PROTEIN P1. FT CHAIN 451 506 CORE PROTEIN P6. FT ZN_FING 394 407 C2HC-TYPE. FT LIPID 1 1 MYRISTATE. FT VARIANT 34 34 V -> I. FT VARIANT 45 45 I -> V. FT VARIANT 74 74 R -> L OR S OR N. FT VARIANT 92 92 K -> E. FT CONFLICT 17 17 K -> N (IN REF. 2). FT CONFLICT 141 141 Q -> E (IN REF. 2). FT CONFLICT 220 220 A -> V (IN REF. 2). FT CONFLICT 226 226 A -> T (IN REF. 2). FT CONFLICT 318 319 WM -> RT (IN REF. 2). FT CONFLICT 447 448 PG -> R (IN REF. 2). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 506 AA; 56630 MW; AC6F3CEB691C4726 CRC64; GARASVLSGG ELDRWEKIRL RPGGKKKYKL KHVVWASREL ERFAINPGLL ETSEGCRQIL GQLQPSLQTG SEERKSLYNT VATLYCVHQK IKIKDTKEAL EKIEEEQNKS KKKAQQAAAD TGNRGNSSQV SQNYPIVQNI QGQMVHQAIS PRTLNAWVKV VEEKAFSPEV IPMFSALSEG ATPQDLNTML NTVGGHQAAM QMLKETINEE AAEWDRLHPA HAGPIAPGQM REPRGSDIAG TTSTLQEQIG WMTNNPPIPV GEIYKRWIIL GLNKIVRMYS PSSILDIRQG PKEPFRDYVD RFYKTLRAEQ ASQEVKNWMT ETLLVQNANP DCKTILKALG PAATLEEMMT ACQGVGGPGH KARVLAEAMS QVTNSATIMM QRGNFRNQRK IIKCFNCGKE GHIAKNCRAP RKRGCWKCGK EGHQMKDCTE RQANFLGKIW PSCKGRPGNF PQSRTEPTAP PEESFRFGEE TTTPYQKQEK KQETIDKDLY PLASLKSLFG NDPLSQ // ID LDLR_HUMAN STANDARD; PRT; 860 AA. AC P01130; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE Low-density lipoprotein receptor precursor (LDL receptor). GN LDLR. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; FT VARIANT 667 667 C -> Y (IN FRENCH CANADIAN-2; 5% OF FT FRENCH CANADIANS). FT /FTId=VAR_005407. FT VARIANT 685 685 P -> L (IN GUJERAT/ZAMBIA/BELGIAN/DUTCH/ FT SWEDEN/JAPAN). ** ** ################# INTERNAL SECTION ################## **CL 19p13.3; SQ SEQUENCE 860 AA; 95376 MW; A4C28E9B8BADAD5E CRC64; MGPWGWKLRW TVALLLAAAG TAVGDRCERN EFQCQDGKCI SYKWVCDGSA ECQDGSDESQ ETCLSVTCKS GDFSCGGRVN RCIPQFWRCD GQVDCDNGSD EQGCPPKTCS QDEFRCHDGK CISRQFVCDS DRDCLDGSDE ASCPVLTCGP ASFQCNSSTC IPQLWACDND PDCEDGSDEW PQRCRGLYVF QGDSSPCSAF EFHCLSGECI HSSWRCDGGP DCKDKSDEEN CAVATCRPDE FQCSDGNCIH GSRQCDREYD CKDMSDEVGC VNVTLCEGPN KFKCHSGECI TLDKVCNMAR DCRDWSDEPI KECGTNECLD NNGGCSHVCN DLKIGYECLC PDGFQLVAQR RCEDIDECQD PDTCSQLCVN LEGGYKCQCE EGFQLDPHTK ACKAVGSIAY LFFTNRHEVR KMTLDRSEYT SLIPNLRNVV ALDTEVASNR IYWSDLSQRM ICSTQLDRAH GVSSYDTVIS RDIQAPDGLA VDWIHSNIYW TDSVLGTVSV ADTKGVKRKT LFRENGSKPR AIVVDPVHGF MYWTDWGTPA KIKKGGLNGV DIYSLVTENI QWPNGITLDL LSGRLYWVDS KLHSISSIDV NGGNRKTILE DEKRLAHPFS LAVFEDKVFW TDIINEAIFS ANRLTGSDVN LLAENLLSPE DMVLFHNLTQ PRGVNWCERT TLSNGGCQYL CLPAPQINPH SPKFTCACPD GMLLARDMRS CLTEAEAAVA TQETSTVRLK VSSTAVRTQH TTTRPVPDTS RLPGATPGLT TVEIVTMSHQ ALGDVAGRGN EKKPSSVRAL SIVLPIVLLV FLCLGVFLLW KNWRLKNINS INFDNPVYQK TTEDEVHICH NQDGYSYPSR QMVSLEDDVA // ID H13_RABIT STANDARD; PRT; 213 AA. AC P02251; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Histone H1.3. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE. RA Hsiang M., Largman C.R., Cole R.D.; ** /NO TITLE. RL Unpublished results, cited by: RL Cole R.D.; RL (In) Ts'o P.O.P. (eds.); RL The molecular biology of the mammalian genetic apparatus, pp.1:93-104, RL Elsevier, Amsterdam (1977). RN [2] RP SEQUENCE OF 1-72. RX MEDLINE=72068710; PubMed=5167020; RA Rall S.C., Cole R.D.; RT "Amino acid sequence and sequence variability of the amino-terminal RT regions of lysine-rich histones."; RL J. Biol. Chem. 246:7175-7190(1971). RN [3] RP SEQUENCE OF 73-107. RX MEDLINE=74143498; PubMed=4822503; RA Jones G.M.T., Rall S.C., Cole R.D.; RT "Extension of the amino acid sequence of a lysine-rich histone."; RL J. Biol. Chem. 249:2548-2553(1974). CC -!- FUNCTION: HISTONES H1 ARE NECESSARY FOR THE CONDENSATION OF CC NUCLEOSOME CHAINS INTO HIGHER ORDER STRUCTURES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE HISTONE H1/H5 FAMILY. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=1; CC Comment=This is just a test; CC Name=VI; CC IsoId=P02251-1; Sequence=Displayed; DR PIR; A02578; HSRB13. DR InterPro; IPR001386; Linker_histone. DR Pfam; PF00538; linker_histone; 1. DR SMART; SM00526; H15; 1. DR HSSP; P08287; 1GHC. KW Chromosomal protein; Nuclear protein; DNA-binding; Multigene family; KW Acetylation. FT DOMAIN 37 110 GLOBULAR. FT MOD_RES 1 1 ACETYLATION. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 213 AA; 21423 MW; 21DE34BBD10D894E CRC64; SEAPAETAAP APAEKSPAKK KKAAKKPGAG AAKRKAAGPP VSELITKAVA ASKERNGLSL AALKKALAAG GYDVEKNNSR IKLGLKSLVS KGTLVETKGT GASGSFKLDK KAASGEAKPK PKKAGAAKPK KPAGATPKKP KKAAGAKKAV KKTPKKAPKP KAAAKPKVAK PKSPAKVAKS PKKAKAVKPK AAKPKAPKPK AAKAKKTAAK KKK // ID ANGT_HUMAN STANDARD; PRT; 485 AA. AC P01019; Q16358; Q16359; Q96F91; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Angiotensinogen precursor [Contains: Angiotensin I (Ang I); DE Angiotensin II (Ang II); Angiotensin III (Ang III) (Des-Asp[1]- DE angiotensin II)]. GN AGT OR SERPINA8. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89170129; PubMed=2924688; RA Gaillard I., Clauser E., Corvol P.; RT "Structure of human angiotensinogen gene."; RL DNA 8:87-99(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85000455; PubMed=6089875; RA Kageyama R., Ohkubo H., Nakanishi S.; RT "Primary structure of human preangiotensinogen deduced from the cloned RT cDNA sequence."; RL Biochemistry 23:3603-3609(1984). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=90237063; PubMed=1692023; RA Fukamizu A., Takahashi S., Seo M.S., Tada M., Tanimoto K., Uehara S., RA Murakami K.; RT "Structure and expression of the human angiotensinogen gene. RT Identification of a unique and highly active promoter."; RL J. Biol. Chem. 265:7576-7582(1990). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RA Strausberg R.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 1-338 FROM N.A. RX MEDLINE=87244745; PubMed=2885106; RA Kunapuli S.P., Kumar A.; RT "Molecular cloning of human angiotensinogen cDNA and evidence for the RT presence of its mRNA in rat heart."; RL Circ. Res. 60:786-790(1987). RN [6] RP SEQUENCE OF 34-45, AND SUBUNITS. RC TISSUE=Serum; RX MEDLINE=95293954; PubMed=7539791; RA Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., RA Stigbrand T., Gleich G.J., Sottrup-Jensen L.; RT "Identification of angiotensinogen and complement C3dg as novel RT proteins binding the proform of eosinophil major basic protein in RT human pregnancy serum and plasma."; RL J. Biol. Chem. 270:13645-13651(1995). RN [7] RP SEQUENCE OF 34-43. RX MEDLINE=69014170; PubMed=4300938; RA Arakawa K., Minohara A., Yamada J., Nakamura M.; RT "Enzymatic degradation and electrophoresis of human angiotensin I."; RL Biochim. Biophys. Acta 168:106-112(1968). RN [8] RP CARBOHYDRATE-LINKAGE SITES. RX MEDLINE=86056581; PubMed=3934016; RA Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P.; RT "Processing of rat and human angiotensinogen precursors by microsomal RT membranes."; RL Mol. Cell. Endocrinol. 43:31-40(1985). RN [9] RP FUNCTION OF ANGIOTENSIN III. RX MEDLINE=75166949; PubMed=1132082; RA Goodfriend T.L., Peach M.J.; RT "Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and RT speculation for its role as an important agonist in the renin RT - angiotensin system."; RL Circ. Res. 36:38-48(1975). RN [10] RP STRUCTURE BY NMR OF ANGIOTENSIN II. RX MEDLINE=98151281; PubMed=9492317; RA Carpenter K.A., Wilkes B.C., Schiller P.W.; RT "The octapeptide angiotensin II adopts a well-defined structure in a RT phospholipid environment."; RL Eur. J. Biochem. 251:448-453(1998). RN [11] RP VARIANTS MET-207; THR-268 AND CYS-281. RX MEDLINE=93008239; PubMed=1394429; RA Jeunemaitre X., Soubrier F., Kotelevtsev Y.V., Lifton R.P., RA Williams C.S., Charru A., Hunt S.C., Hopkins P.N., Williams R.R., RA Lalouel J.-M., Corvol P.; RT "Molecular basis of human hypertension: role of angiotensinogen."; RL Cell 71:169-180(1992). RN [12] RP VARIANT THR-268. RX MEDLINE=93291876; PubMed=8513325; RA Ward K., Hata A., Jeunemaitre X., Helin C., Nelson L., Namikawa C., RA Farrington P.F., Ogasawara M., Suzumori K., Tomoda S., Berrebi S., RA Sasaki M., Corvol P., Lifton R.P., Lalouel J.-M.; RT "A molecular variant of angiotensinogen associated with RT preeclampsia."; RL Nat. Genet. 4:59-61(1993). RN [13] RP VARIANTS ILE-242; ARG-244 AND CYS-281. RX MEDLINE=95331754; PubMed=7607642; RA Hixson J.E., Powers P.K.; RT "Detection and characterization of new mutations in the human RT angiotensinogen gene (AGT)."; RL Hum. Genet. 96:110-112(1995). RN [14] RP CHARACTERIZATION OF VARIANT CYS-281. RX MEDLINE=96199253; PubMed=8621667; RA Gimenez-Roqueplo A.P., Leconte I., Cohen P., Simon D., Guyene T.T., RA Celerier J., Pau B., Corvol P., Clauser E., Jeunemaitre X.; RT "The natural mutation Y248C of human angiotensinogen leads to abnormal RT glycosylation and altered immunological recognition of the protein."; RL J. Biol. Chem. 271:9838-9844(1996). CC -!- FUNCTION: IN RESPONSE TO LOWERED BLOOD PRESSURE, THE ENZYME RENIN CC CLEAVES ANGIOTENSIN I, FROM ANGIOTENSINOGEN. ACE (ANGIOTENSIN CC CONVERTING ENZYME) THEN REMOVES A DIPEPTIDE TO YIELD THE CC PHYSIOLOGICALLY ACTIVE PEPTIDE ANGIOTENSIN II, THE MOST POTENT CC PRESSOR SUBSTANCE KNOWN, WHICH HELPS REGULATE VOLUME AND MINERAL CC BALANCE OF BODY FLUIDS. CC -!- FUNCTION: Angiotensin III stimulates aldosterone release. CC -!- SUBUNIT: During pregnancy, exists as a disulfide-linked 2:2 CC heterotetramer with the proform of PRG2 and as a complex (probably CC a 2:2:2 heterohexamer) with pro-PRG2 and C3dg. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Synthesized by the liver and secreted in the CC plasma. CC -!- DISEASE: AGT SEEMS TO BE ASSOCIATED WITH A PREDISPOSITION TO CC ESSENTIAL HYPERTENSION AS WELL AS PREGNANCY-INDUCED HYPERTENSION CC (PIH) (PREECLAMPSIA). CC -!- SIMILARITY: BELONGS TO THE SERPIN FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-10 IS THE INITIATOR. DR EMBL; K02215; AAA51731.1; -. DR EMBL; M24689; AAA51679.1; -. DR EMBL; M24686; AAA51679.1; JOINED. DR EMBL; M24687; AAA51679.1; JOINED. DR EMBL; M24688; AAA51679.1; JOINED. DR EMBL; X15324; CAA33385.1; -. DR EMBL; X15325; CAA33385.1; JOINED. DR EMBL; X15326; CAA33385.1; JOINED. DR EMBL; X15327; CAA33385.1; JOINED. DR EMBL; M69110; AAA52282.1; -. DR EMBL; BC011519; AAH11519.1; -. DR EMBL; S78529; AAD14287.1; -. DR EMBL; S78530; AAD14288.1; -. DR PIR; A01249; ANHU. DR PIR; A31362; A31362. DR PIR; A35203; A35203. DR SWISS-2DPAGE; P01019; HUMAN. DR HGNC; HGNC:333; AGT. DR MIM; 106150; -. DR GO; GO:0005625; C:soluble fraction; TAS. DR GO; GO:0004867; F:serine protease inhibitor activity; TAS. DR GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS. DR GO; GO:0007267; P:cell-cell signaling; TAS. DR GO; GO:0007565; P:pregnancy; TAS. DR GO; GO:0008217; P:regulation of blood pressure; TAS. DR InterPro; IPR000227; Angiotensngn. DR InterPro; IPR000215; Serpin. DR Pfam; PF00079; serpin; 1. DR PRINTS; PR00654; ANGIOTENSNGN. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Vasoconstrictor; Glycoprotein; Plasma; Serpin; Signal; KW Disease mutation; Polymorphism. FT SIGNAL 1 33 FT CHAIN 34 485 ANGIOTENSINOGEN. FT PEPTIDE 34 43 ANGIOTENSIN I. FT PEPTIDE 34 41 ANGIOTENSIN II. FT PEPTIDE 35 41 ANGIOTENSIN III. FT CARBOHYD 47 47 N-LINKED (GLCNAC...). FT CARBOHYD 170 170 N-LINKED (GLCNAC...). FT CARBOHYD 304 304 N-LINKED (GLCNAC...). FT CARBOHYD 328 328 N-LINKED (GLCNAC...). FT VARIANT 207 207 T -> M (IN dbSNP:4762). FT /FTId=VAR_007093. FT VARIANT 242 242 T -> I (IN HYPERTENSION). FT /FTId=VAR_007094. FT VARIANT 244 244 L -> R (IN HYPERTENSION). FT /FTId=VAR_007095. FT VARIANT 268 268 M -> T (IN HYPERTENSION; dbSNP:699). FT /FTId=VAR_007096. FT VARIANT 281 281 Y -> C (IN HYPERTENSION; ALTERS THE FT STRUCTURE, GLYCOSYLATION AND SECRETION OF FT ANGIOTENSINOGEN). FT /FTId=VAR_007097. FT VARIANT 392 392 L -> M (IN dbSNP:1805090). FT /FTId=VAR_014573. FT CONFLICT 333 333 Q -> E (IN REF. 1). FT CONFLICT 335 335 P -> S (IN REF. 4). ** ** ################# INTERNAL SECTION ################## **CL 1q42-q43; SQ SEQUENCE 485 AA; 53154 MW; 5026C2DFB2DD236E CRC64; MRKRAPQSEM APAGVSLRAT ILCLLAWAGL AAGDRVYIHP FHLVIHNEST CEQLAKANAG KPKDPTFIPA PIQAKTSPVD EKALQDQLVL VAAKLDTEDK LRAAMVGMLA NFLGFRIYGM HSELWGVVHG ATVLSPTAVF GTLASLYLGA LDHTADRLQA ILGVPWKDKN CTSRLDAHKV LSALQAVQGL LVAQGRADSQ AQLLLSTVVG VFTAPGLHLK QPFVQGLALY TPVVLPRSLD FTELDVAAEK IDRFMQAVTG WKTGCSLMGA SVDSTLAFNT YVHFQGKMKG FSLLAEPQEF WVDNSTSVSV PMLSGMGTFQ HWSDIQDNFS VTQVPFTESA CLLLIQPHYA SDLDKVEGLT FQQNSLNWMK KLSPRTIHLT MPQLVLQGSY DLQDLLAQAE LPAILHTELN LQKLSNDRIR VGEVLNSIFF ELEADEREPT ESTQQLNKPE VLEVTLNRPF LFAVYDQSAT ALHFLGRVAN PLSTA // ID NRTC_SYNY3 STANDARD; PRT; 670 AA. AC P73450; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Nitrate transport ATP-binding protein nrtC. GN NRTC OR SLL1452. OS Synechocystis sp. (strain PCC 6803). OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. OX NCBI_TaxID=1148; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97061201; PubMed=8905231; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: PROBABLY PART OF A HIGH-AFFINITY BINDING-PROTEIN- CC DEPENDENT TRANSPORT SYSTEM FOR NITRATE. PROBABLY RESPONSIBLE FOR CC ENERGY COUPLING TO THE TRANSPORT SYSTEM. CC -!- SUBCELLULAR LOCATION: Membrane-associated (Potential). CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. CC -!- SIMILARITY: SOME, IN THE C-TERMINAL DOMAIN TO NRTA. DR EMBL; D90906; BAA17490.1; -. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transporter. DR InterPro; IPR005890; NtrCD. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01184; ntrCD; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. KW Transport; ATP-binding; Membrane; Nitrate assimilation; KW Complete proteome. FT DOMAIN 1 254 ABC TRANSPORTER. FT DOMAIN 240 250 INTERNAL. FT DOMAIN 255 278 LINKER. FT DOMAIN 279 670 NTRA-LIKE. FT NP_BIND 42 49 ATP (POTENTIAL). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 670 AA; 75101 MW; 03B47E6C7918AD14 CRC64; MMPFIEIDHV DRIFPLPDGG RYIALKNIEL KISQGEFISL IGHSGCGKST LLNMISGLDK PTFGGVIMEG KEITEPGPER MVVFQNYSLL PWLTVRQNIA LAVNRVLRDL PKPEQEKIID DNIALVGLQR AAHKRPGELS GGMKQRVAIA RALSTRPKVL LLDEPFGALD ALTRGNLQER LMEIVQESGV TCIMVTHDVD EALLLSDRVV MLTTGPEAHI GQILEVPIPR PRHRLEVVNH PSYYALRGEM VYFLNQQKRA KKVGAVSQFA EAMGGNGLEK INLDLGFIPL TDCAPLVVAK EKGFFQKHGL EQVNLVKEPS WQAIADGIRE RRLDGAQMVA GMPLALTLGM GGKTPLPMVT AMVMSRNGNA ITLSKKFAEA GVKTLEDLRL KLAETPDQVS TLGMVHPASM QNLLLRYWLA SGSIDPDQDI NLMRLPPPQM VSNLEAGNID GFCVGEPWNS YAVKQNLGYV IATDLDIWNG HPEKVLGMRE EWVNKYPATH LALVKALLEA CEYCDDRRHR QEILDYLALP QYVGTSTEYI SPGFLTEYDQ GNDAEAEMLL DFNQFYVKQS NYPSRSEGLW ILTQLARWGY IDFPKNWVEI IERVRRPDLF GEACRHLGWP DLEGDHHNVS LFDGMVFTPN DPLGYIKRFT IHRDIQVTEI LIDQIDQVNQ // ID FAS2_PENPA STANDARD; PRT; 1857 AA. AC P15368; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl DE carrier; 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) DE (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier protein] synthase DE (EC 2.3.1.41) (Beta-ketoacyl synthase)]. GN FAS2. OS Penicillium patulum (Penicillium griseofulvum). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Penicillium. OX NCBI_TaxID=5078; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89030697; PubMed=3053172; RA Wiesner P., Beck J., Beck K.-F., Ripka S., Mueller G., Luecke S., RA Schweizer E.; RT "Isolation and sequence analysis of the fatty acid synthetase FAS2 RT gene from Penicillium patulum."; RL Eur. J. Biochem. 177:69-79(1988). CC -!- FUNCTION: FATTY ACID SYNTHETASE CATALYZES THE FORMATION OF LONG- CC CHAIN FATTY ACIDS FROM ACETYL-COA, MALONYL-COA AND NADPH. THE CC ALPHA SUBUNIT CONTAINS DOMAINS FOR: ACYL CARRIER PROTEIN, 3- CC OXOACYL-[ACYL-CARRIER PROTEIN] REDUCTASE, AND 3-OXOACYL-[ACYL- CC CARRIER-PROTEIN] SYNTHASE. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + N malonyl-CoA + 2N NADPH = a CC long-chain acyl-CoA + N CoA + N CO(2) + 2N NADP(+). CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier protein] + malonyl-[acyl- CC carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO(2) + CC [acyl-carrier protein]. CC -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier protein] + CC NADP(+) = 3-oxoacyl-[acyl-carrier protein] + NADPH. CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional CC subunits (alpha and beta). CC -!- SIMILARITY: TO THE FATTY ACID SYNTHETASE, SUBUNIT ALPHA FROM OTHER CC FUNGI. DR EMBL; M37461; AAA33695.1; -. DR PIR; S01787; S01787. DR InterPro; IPR000794; Ketoacyl-synt. DR InterPro; IPR004568; Pantethn_trn. DR InterPro; IPR006162; Ppantne_attach. DR Pfam; PF01648; ACPS; 1. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; ketoacyl-synt_C; 1. DR ProDom; PD004282; ACPS; 1. DR TIGRFAMs; TIGR00556; pantethn_trn; 1. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. KW Fatty acid biosynthesis; Multifunctional enzyme; Oxidoreductase; KW Transferase; NADP; Phosphopantetheine. FT DOMAIN 1 ? ACYL CARRIER (ACP). FT DOMAIN 648 845 BETA-KETOACYL REDUCTASE. FT DOMAIN ? 1857 BETA-KETOACYL SYNTHASE. FT ACT_SITE 1275 1275 BETA-KETOACYL SYNTHASE (BY SIMILARITY). FT BINDING 174 174 PHOSPHOPANTETHEINE (BY SIMILARITY). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 1857 AA; 204466 MW; 34BAFD547D93FEE6 CRC64; MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVILAEQR TERIVEIGPA DTLGGMARRT LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEEPE ATEPAPSATP AAPAAAPAAG APPPPPSAGP AASVEDIPVT AVDILRTLVA QKLKKSLADV PLSKAIKDLV GGKSTLQNEI LGDLGKEFGS TPEKPEDVPL DELGASMQAT FNGQLGKQSS SLIARMVSSK MPGGFNITSV RKYLETRWGL GSGRQDGVLL LALTMEPAAR LGSEVDAKAY LDDVTNKYAA SAGVNLSAPV AGGDSGGAGG GMVMDPAAID ALTKDQRALF KQQLEIIARY LKMDLRGGEK AHVISQETQK ALQAQLDLWQ AEHGDFYASG IEPSFDQLKA RVYDSSWNWA RQDALSMYYD IIFGRLQVVD REIVSQCIRI MNRSNPLLLD FMQYHIDNCP TERGETYQLA KELGQQLIEN CREVLEVAPV YKDVAVPTGP QTTIDARGNI SYKETPRTSA RKLEHYVKHM AEGGPISEYS NRTKVQNDLK SVYKLIRKQH RLSKSSQLQF DALYKDVVHA LGMNESQIIP QENGHSKKGG RSAAKRNTPT RPGKVETIPF LHLKKKTEHG WDYNKKLTGI YLNVTESAAK DGLSFQGKNV LMTGAGAGSI GAEVLQGLIS GGAQVIVTTS RFSREVTEYY QAMYARYGAR GSQLVVVPFN QGSKQDVEAL VEYIYDTKKG LGWDLDFVVP FAAIPENGRE IDSIDSKSEL AHRIMLTNLL RLLGSVKTQK QAHGFETRPA QVILPLSPNH GTFGNDGLYS ESKLALETLF NRWYSENWGH YLTICGAVIG WTRGTGLMSG NNMVAEGVEK LGVRTFSQQE MAFNLLGLMS PAIVNLCQLD PVFADLNGGL QFIPDLKGLM TKLRTDIMET SDVRQAVMKE TAIEHNIVNG EDSGVLYKKV IAEPRANIKF EFPNLPDWEK EVKPLNENLK GMVNLDKVVV VTGFSEVGPW GNSRTRWEME SKGKFSLEGC VEMAWIMGLI KHHNGPLKGQ AYSGWVDAKT GEPVDDKDVK PKYEKHILEH TGIRLIEPEL FKGYDPKKKQ LLQEIVIQED LEPFEASKET AEEFKREHGD KVEIFEIPES GEYTVRLCKG ATMLIPKALQ FDRLVAGQVP TGWDASRYGI PDDIISQVDP VTLFVLVCTA EAMLSAGVTD PYEFYKYVHL SEVGNCIGSG IGGTHRLRGM YKDRFLDKPL QKDILQESFI NTMSAWVNML LLSSTGPIKT PVGCCATAVE SVDIGYETIV EGKARVCFVG GFDDFQEEGS YEFANMKATS NAEDEFAHGR TPQEMSRPTT TTRAGFMESQ GCGMQLIMTA QLALDMGVPI HGIIALTTTA TDKIGRSVRS VPAPGQGVLT TARENPGKFP SPLLDIKYRR RQLDLRKKQI NEWQEAELLY LQEEAEAMKA QSDETFNEAE YMQERAQHIE REAIRQEKDA QYSLGNNFWK QDSRIAPLRG AMATWGLTVD DIDVASFHGT STVANDKNES DVICQQMKHL GRSKGNAVMG IFQKYLTGHP KGAAGAWMFN GCLQVLDSGL VPGNRNADNV DKVMEKFDYI VYPSRSIQTD GVKAFSVTSF GFGQKGAQVI GIHPKYLYAT LDQAQYEAYK TKVEARQKKA YRYFHNGLIN NSIFVAKSKA PYEDEQQSKV FLNPDYRVSV DKKTSELKFS TTAPEAKQSE STRQTLESLA KANATENSKI GVDVEHIDSV NIENETFVER NFTQSEQDYC RKAASPQSSF AGRWSAKEAV FKSLGVSSKG AGAALKDIEI GVDANGAPVV NLHGAAAAAA KQAGVKQVSV SISHSDSQAV AVAVSQF // ID UKA1_HUMAN STANDARD; PRT; 19 AA. AC P31940; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Unknown protein from 2D-page of epidermal keratinocytes (Spot 1118) DE (Fragments). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE. RC TISSUE=Keratinocytes; RX MEDLINE=93162043; PubMed=1286667; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 7.24, ITS MW IS: 23.5 kDa. DR Aarhus/Ghent-2DPAGE; 1118; IEF. FT UNSURE 6 6 FT UNSURE 17 17 FT NON_CONS 6 7 FT NON_CONS 12 13 FT NON_TER 1 1 FT NON_TER 19 19 ** ** ################# INTERNAL SECTION ################## **CL ?; SQ SEQUENCE 19 AA; 2087 MW; EF7515F79D50DE12 CRC64; HIGLVRLTPT EVQEPIITA // ID A4_MOUSE STANDARD; PRT; 770 AA. AC P12023; DT 01-OCT-1989 (Rel. 12, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Alzheimer's disease amyloid A4 protein homolog precursor DE (Amyloidogenic glycoprotein) (AG). GN APP. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE OF 1-289 AND 365-770 FROM N.A. RC STRAIN=BALB/c; TISSUE=Brain; RX MEDLINE=92096458; PubMed=1756177; RA de Strooper B., van Leuven F., van den Berghe H.; RT "The amyloid beta protein precursor or proteinase nexin II from mouse RT is closer related to its human homolog than previously reported."; RL Biochim. Biophys. Acta 1129:141-143(1991). RN [2] RP SEQUENCE OF 1-289 AND 365-770 FROM N.A. RC TISSUE=Brain; RX MEDLINE=88106489; PubMed=3322280; RA Yamada T., Sasaki H., Furuya H., Miyata T., Goto I., Sakaki Y.; RT "Complementary DNA for the mouse homolog of the human amyloid beta RT protein precursor."; RL Biochem. Biophys. Res. Commun. 149:665-671(1987). RN [3] RP REVISIONS. RA Yamada T.; RL Submitted (MAR-1988) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 289-364 FROM N.A. RC STRAIN=CD-1; TISSUE=Placenta; RX MEDLINE=89345111; PubMed=2569710; RA Fukuchi K., Martin G.M., Deeb S.S.; RT "Sequence of the protease inhibitor domain of the A4 amyloid protein RT precursor of Mus domesticus."; RL Nucleic Acids Res. 17:5396-5396(1989). RN [5] RP SEQUENCE OF 1-19 FROM N.A. RX MEDLINE=92209998; PubMed=1555768; RA Izumi R., Yamada T., Yoshikai S.I., Sasaki H., Hattori M., Sakai Y.; RT "Positive and negative regulatory elements for the expression of the RT Alzheimer's disease amyloid precursor-encoding gene in mouse."; RL Gene 112:189-195(1992). RN [6] RP SEQUENCE OF 281-380 FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Brain, and Kidney; RX MEDLINE=89149813; PubMed=2493250; RA Yamada T., Sasaki H., Dohura K., Goto I., Sakaki Y.; RT "Structure and expression of the alternatively-spliced forms of mRNA RT for the mouse homolog of Alzheimer's disease amyloid beta protein RT precursor."; RL Biochem. Biophys. Res. Commun. 158:906-912(1989). RN [7] RP PHOSPHORYLATION. RX MEDLINE=22028091; PubMed=11912189; RA Taru H., Iijima K.-I., Hase M., Kirino Y., Yagi Y., Suzuki T.; RT "Interaction of Alzheimer's beta-amyloid precursor family proteins RT with scaffold proteins of the JNK signaling cascade."; RL J. Biol. Chem. 277:20070-20078(2002). CC -!- SUBCELLULAR LOCATION: Type I membrane protein. Mature, CC phosphorylated APP is largely located on the plasma membrane of CC cell bodies and the growth cones of neurites of mature neurons (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=APP(770); CC IsoId=P12023-1; Sequence=Displayed; CC Name=APP(395); CC IsoId=P12023-4; Sequence=Not described; CC Name=APP(563); CC IsoId=P12023-5; Sequence=Not described; CC Name=APP(695); CC IsoId=P12023-2; Sequence=VSP_000012, VSP_000013; CC Name=APP(751); CC IsoId=P12023-3; Sequence=VSP_000014; CC -!- TISSUE SPECIFICITY: Isoform APP(770) is expressed in kidney. CC Isoform APP(751) is widely expressed. Isoform APP(695) is CC expressed in brain, kidney and liver. CC -!- DOMAIN: The clathrin-binding site is essential for its association CC with X11-alpha, -beta, and -gamma. The sequence specific CC recognition extends to peptide residues that are C-terminal to the CC NPXY motif. This interaction appears to be independent of CC phosphorylation. Binds to Jip1 which may result in the CC phosphorylation of App by members of the JNK-signaling cascade. CC Cytoplasmic domain binds Apbb1, phosphorylation within this domain CC results in a conformational change which prevents protein binding CC (By similarity). CC -!- SIMILARITY: BELONGS TO THE APP FAMILY. CC -!- SIMILARITY: Contains 1 BPTI/Kunitz inhibitor domain. DR EMBL; X59379; -; NOT_ANNOTATED_CDS. DR EMBL; M18373; AAA37139.1; -. DR EMBL; X15210; CAA33280.1; -. DR EMBL; D10603; BAA01456.1; -. DR EMBL; M24397; AAA39929.1; -. DR PIR; A27485; A27485. DR PIR; S04855; S04855. DR PIR; S19727; S19727. DR MGI; MGI:88059; App. DR InterPro; IPR001868; A4_APP. DR InterPro; IPR001255; Beta-APP. DR InterPro; IPR002223; Kunitz_BPTI. DR Pfam; PF02177; A4_EXTRA; 1. DR Pfam; PF03494; Beta-APP; 1. DR Pfam; PF00014; Kunitz_BPTI; 1. DR PRINTS; PR00203; AMYLOIDA4. DR PRINTS; PR00759; BASICPTASE. DR ProDom; PD000222; Kunitz_BPTI; 1. DR SMART; SM00006; A4_EXTRA; 1. DR SMART; SM00131; KU; 1. DR PROSITE; PS00319; A4_EXTRA; 1. DR PROSITE; PS00320; A4_INTRA; 1. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. DR HSSP; P05067; 1AAP. KW Glycoprotein; Amyloid; Neurone; Transmembrane; Signal; KW Alternative splicing; Serine protease inhibitor; Phosphorylation. FT SIGNAL 1 17 BY SIMILARITY. FT CHAIN 18 770 ALZHEIMER'S DISEASE AMYLOID A4 PROTEIN FT HOMOLOG. FT TOPO_DOM 18 699 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 700 723 POTENTIAL. FT TOPO_DOM 724 770 CYTOPLASMIC (POTENTIAL). FT DOMAIN 287 345 BPTI/KUNITZ INHIBITOR. FT DOMAIN 673 715 EQUIVALENT OF BETA-AMYLOID PROTEIN. FT SITE 759 762 CLATHRIN-BINDING (BY SIMILARITY). FT MOD_RES 743 743 PHOSPHORYLATION. FT CARBOHYD 542 542 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 571 571 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 291 341 BY SIMILARITY. FT DISULFID 300 324 BY SIMILARITY. FT DISULFID 316 337 BY SIMILARITY. FT VAR_SEQ 289 289 E -> V (in isoform APP(695)). FT /FTId=VSP_000012. FT VAR_SEQ 290 364 Missing (in isoform APP(695)). FT /FTId=VSP_000013. FT VAR_SEQ 346 380 Missing (in isoform APP(751)). FT /FTId=VSP_000014. ** ** ################# INTERNAL SECTION ################## **IS P12023-6 **ZB SAO, 16-SEP-2002; SQ SEQUENCE 770 AA; 86752 MW; 26C50DE0890CAF7A CRC64; MLPSLALLLL AAWTVRALEV PTDGNAGLLA EPQIAMFCGK LNMHMNVQNG KWESDPSGTK TCIGTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHTH IVIPYRCLVG EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR GVEFVCCPLA EESDSVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVADVEEE EADDDEDVED GDEVEEEAEE PYEEATERTT STATTTTTTT ESVEEVVREV CSEQAETGPC RAMISRWYFD VTEGKCVPFF YGGCGGNRNN FDTEEYCMAV CGSVSTQSLL KTTSEPLPQD PDKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL QAVPPRPHHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET KTTVELLPVN GEFSLDDLQP WHPFGVDSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN IKTEEISEVK MDAEFGHDSG FEVRHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN // ID WASL_RAT STANDARD; PRT; 501 AA. AC O08816; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Neural Wiskott-Aldrich syndrome protein (N-WASP). GN WASL. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97464048; PubMed=9322739; RA Fukuoka M., Miki H., Takenawa T.; RT "Identification of N-WASP homologs in human and rat brain."; RL Gene 196:43-48(1997). CC -!- FUNCTION: REGULATES ACTIN POLYMERIZATION BY STIMULATING THE ACTIN- CC NUCLEATING ACTIVITY OF THE ACTIN-RELATED PROTEIN 2/3 (ARP2/3) CC COMPLEX (BY SIMILARITY). CC -!- SUBUNIT: BINDS ACTIN AND ARP2/3 COMPLEX; INTERACTS WITH CDC42 CC BINDS TO SH3 DOMAINS OF ASH/GRB2 (BY SIMILARITY). CC -!- SIMILARITY: Contains 1 CRIB domain. CC -!- SIMILARITY: Contains 1 WH1 domain. CC -!- SIMILARITY: Contains 2 WH2 domains. DR EMBL; D88461; BAA21534.1; -. DR InterPro; IPR000697; EVH1. DR InterPro; IPR000095; PAKbox/Rhobndng. DR InterPro; IPR001960; WH1. DR InterPro; IPR003124; WH2. DR Pfam; PF00786; PBD; 1. DR Pfam; PF00568; WH1; 1. DR Pfam; PF02205; WH2; 2. ** PRINTS; PR01217; PRICHEXTENSN; FALSE_POS_1. DR SMART; SM00285; PBD; 1. DR SMART; SM00461; WH1; 1. DR SMART; SM00246; WH2; 2. DR PROSITE; PS50108; CRIB; 1. KW Actin-binding; Repeat. FT DOMAIN 31 135 WH1. FT DOMAIN 200 213 CRIB. FT DOMAIN 401 418 WH2 1. FT DOMAIN 429 446 WH2 2. FT COMPBIAS 274 385 PRO-RICH. FT COMPBIAS 482 501 ASP-RICH. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 501 AA; 54325 MW; 480E21F26F7FC77E CRC64; MSSGQQPPRR VTNVGSLLLT PQENESLFSF LGKKCVTMSS AVVQLYAADR NCMWSKKCSG VACLVKDNPQ RSYFLRIFDI KDGKLLWEQE LYNNFVYNSP RGYFHTFAGD TCQVALNFAN EEEAKKFRKA VTDLLGRRQR KSEKRRDAPN GPNLPMATVD IKNPEITTNR FYSSQVNNIS HTKEKKKGKA KKKRLTKADI GTPSNFQHIG HVGWDPNTGF DLNNLDPELK NLFDMCGISE AQLKDRETSK VIYDFIEKTG GVEAVKNELR RQAPPPPPPS RGGPPPPPPP PHSSGPPPPP ARGRGAPPPP PSRAPTAAPP PPPPSRPGVV VPPPPPNRMY PPPPPALPSS APSGPPPPPP LSMAGSTAPP PPPPPPPPPG PPPPPGLPSD GDHQVPASSG NKAALLDQIR EGAQLKKVEQ NSRPVSCSGR DALLDQIRQG IQLKSVSDGQ ESTPPTPAPT SGIVGALMEV MQKRSKAIHS SDEDEDDDDE EDFQDDDEWE D // ID Q9B1S6 PRELIMINARY; PRT; 260 AA. AC Q9B1S6; DT 01-JUN-2001 (TrEMBLrel. 17, Created) DT 01-JUN-2001 (TrEMBLrel. 17, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Cytochrome c oxidase subunit III (EC 1.9.3.1) (Cytochrome co oxidase DE subunit III) (Cytochrome c oxidase polypeptide III) (Cytochrome DE oxidase subunit III){EP249}. GN COX3{EI2}. OS Homo sapiens (Human). OG Mitochondrion{EI3}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606{EP248}; RN [1]{EI3} RP SEQUENCE FROM N.A. RX MEDLINE=21012010; PubMed=11130070; RA Ingman M., Kaessmann H., Paabo S., Gyllensten U.; RT "Mitochondrial genome variation and the origin of modern humans."; RL Nature 408:708-713(2000). RN [2]{EI3} RP SEQUENCE FROM N.A. RX MEDLINE=21176314; PubMed=11279504; RA Ingman M., Kaessmann H., Paabo S., Gyllensten U.; RT "correction: Mitochondrial genome variation and the origin of modern RT humans."; RL Nature 410:611-611(2001). RN [3]{EI3} RP SEQUENCE FROM N.A. RA Ingman M., Kaessmann H., Paabo S., Gyllensten U.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [4]{EI2} RP SEQUENCE FROM N.A. RX PubMed=11553319; RA Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; RT "Major genomic mitochondrial lineages delineate early human RT expansions."; RL BMC Genet. 2:13-13(2001). RN [5]{EI2} RP SEQUENCE FROM N.A. RA Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [6]{EI79} RP SEQUENCE FROM N.A. RX MEDLINE=22062553; PubMed=12022039; RA Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., RA Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., RA Barbosa M., Paco-Larson M.L., Petzl-Erler M.L., Valente V., RA Santos S.E., Zago M.A.; RT "Mitochondrial genome diversity of Native Americans supports a single RT early entry of founder populations into America."; RL Am. J. Hum. Genet. 71:187-192(2002). RN [7]{EI118} RP SEQUENCE FROM N.A. RX MEDLINE=22406325; PubMed=12509511; RA Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., RA Hosseini S., Brandon M., Easley K., Chen E., Brown M.D., RA Sukernik R.I., Olckers A., Wallace D.C.; RT "Natural selection shaped regional mtDNA variation in humans."; RL Proc. Natl. Acad. Sci. U.S.A. 100:171-176(2003). RN [8]{EI157} RP SEQUENCE FROM N.A. RC STRAIN=GD7812, LN7550, LN7589, SD10313, XJ8426, EWK28, QD8141, GD7834, RC Miao271, DW48, WH6954, WH6967, Mg246, LN7595, GD7817, WH6958, GD7829, RC SD10352, XJ8420, SD10334, WH6979, SD10324, XJ8416, LN7711, QD8166, RC GD7837n, QD8168, GD7811, GD7830, WH6980, XJ8451, GD7809, YN289, RC GD7813, SD10362, GD7825, XJ8435, GD7824, LN7710, QD8167, YN163, RC WH6973, and QD8147; RA Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; RT "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from RT Complete Sequences."; RL Am. J. Hum. Genet. 0:0-0(2003). RN [9]{EI200} RP SEQUENCE FROM N.A. RC STRAIN=Aus14, Aus15, Aus16, Aus17, Aus20, Aus21, Aus22, Aus23, B2, B4, RC B6, E4, E9, F5, Y6, Y7, C1112, C1190, CAM, T1331, K11b, M306, 961, RC 100, CP8, GP4, WE16, WE18, WE23, WE4, WE7, 36, NG12, NG29, SH10, SH17, RC SH19, SH23, SH29, SH33, S1216, S1220, 496, 513, DCH002, Sb13, and RC Sb29; RX MEDLINE=22723755; PubMed=12840039; RA Ingman M., Gyllensten U.; RT "Mitochondrial genome variation and evolutionary history of Australian RT and new guinean aborigines."; RL Genome Res. 13:1600-1606(2003). CC -!- FUNCTION: Subunits I, II and III form the functional core of the CC enzyme complex (By similarity){EA1}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) = 4 ferricytochrome CC c + 2 H(2)O{EA1}. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME C OXIDASE SUBUNIT 3 CC FAMILY{EA1}. DR EMBL; AF347015; AAK17889.2; -.{EI3} DR EMBL; AF346963; AAK17213.1; -.{EI4} DR EMBL; AF346964; AAK17226.2; -.{EI5} DR EMBL; AF346966; AAK17252.1; -.{EI6} DR EMBL; AF346967; AAK17265.2; -.{EI7} DR EMBL; AF346968; AAK17278.2; -.{EI8} DR EMBL; AF346969; AAK17291.2; -.{EI9} DR EMBL; AF346970; AAK17304.2; -.{EI10} DR EMBL; AF346971; AAK17317.2; -.{EI11} DR EMBL; AF346972; AAK17330.2; -.{EI12} DR EMBL; AF346973; AAK17343.2; -.{EI13} DR EMBL; AF346974; AAK17356.2; -.{EI14} DR EMBL; AF346975; AAK17369.2; -.{EI15} DR EMBL; AF346976; AAK17382.1; -.{EI16} DR EMBL; AF346977; AAK17395.1; -.{EI17} DR EMBL; AF346978; AAK17408.1; -.{EI18} DR EMBL; AF346979; AAK17421.1; -.{EI19} DR EMBL; AF346980; AAK17434.2; -.{EI20} DR EMBL; AF346981; AAK17447.2; -.{EI21} DR EMBL; AF346982; AAK17460.1; -.{EI22} DR EMBL; AF346983; AAK17473.1; -.{EI23} DR EMBL; AF346984; AAK17486.2; -.{EI24} DR EMBL; AF346985; AAK17499.2; -.{EI25} DR EMBL; AF346986; AAK17512.2; -.{EI26} DR EMBL; AF346987; AAK17525.2; -.{EI27} DR EMBL; AF346990; AAK17564.1; -.{EI28} DR EMBL; AF346991; AAK17577.2; -.{EI29} DR EMBL; AF346992; AAK17590.2; -.{EI30} DR EMBL; AF346993; AAK17603.2; -.{EI31} DR EMBL; AF346994; AAK17616.2; -.{EI32} DR EMBL; AF346995; AAK17629.2; -.{EI33} DR EMBL; AF346996; AAK17642.2; -.{EI34} DR EMBL; AF346997; AAK17655.2; -.{EI35} DR EMBL; AF346998; AAK17668.2; -.{EI36} DR EMBL; AF346999; AAK17681.2; -.{EI37} DR EMBL; AF347000; AAK17694.1; -.{EI38} DR EMBL; AF347001; AAK17707.2; -.{EI39} DR EMBL; AF347002; AAK17720.2; -.{EI40} DR EMBL; AF347003; AAK17733.2; -.{EI41} DR EMBL; AF347004; AAK17746.2; -.{EI42} DR EMBL; AF347005; AAK17759.2; -.{EI43} DR EMBL; AF347006; AAK17772.2; -.{EI44} DR EMBL; AF347007; AAK17785.2; -.{EI45} DR EMBL; AF347008; AAK17798.2; -.{EI46} DR EMBL; AF347009; AAK17811.2; -.{EI47} DR EMBL; AF347011; AAK17837.2; -.{EI48} DR EMBL; AF347014; AAK17876.2; -.{EI49} DR EMBL; AF382013; AAL54806.1; -.{EI2} DR EMBL; AF381981; AAL54393.1; -.{EI50} DR EMBL; AF381982; AAL54403.1; -.{EI51} DR EMBL; AF381983; AAL54416.1; -.{EI52} DR EMBL; AF381984; AAL54429.1; -.{EI53} DR EMBL; AF381985; AAL54442.1; -.{EI54} DR EMBL; AF381986; AAL54455.1; -.{EI55} DR EMBL; AF381987; AAL54468.1; -.{EI56} DR EMBL; AF381988; AAL54481.1; -.{EI57} DR EMBL; AF381990; AAL54507.1; -.{EI58} DR EMBL; AF381991; AAL54520.1; -.{EI59} DR EMBL; AF381993; AAL54546.1; -.{EI60} DR EMBL; AF381994; AAL54559.1; -.{EI61} DR EMBL; AF381995; AAL54572.1; -.{EI62} DR EMBL; AF381996; AAL54585.1; -.{EI63} DR EMBL; AF381998; AAL54611.1; -.{EI64} DR EMBL; AF381999; AAL54624.1; -.{EI65} DR EMBL; AF382000; AAL54637.1; -.{EI66} DR EMBL; AF382001; AAL54650.1; -.{EI67} DR EMBL; AF382002; AAL54663.1; -.{EI68} DR EMBL; AF382003; AAL54676.1; -.{EI69} DR EMBL; AF382004; AAL54689.1; -.{EI70} DR EMBL; AF382005; AAL54702.1; -.{EI71} DR EMBL; AF382006; AAL54715.1; -.{EI72} DR EMBL; AF382007; AAL54728.1; -.{EI73} DR EMBL; AF382008; AAL54741.1; -.{EI74} DR EMBL; AF382009; AAL54754.1; -.{EI75} DR EMBL; AF382010; AAL54767.1; -.{EI76} DR EMBL; AF382011; AAL54780.1; -.{EI77} DR EMBL; AF382012; AAL54793.1; -.{EI78} DR EMBL; AF465941; AAN14542.1; -.{EI79} DR EMBL; AF465942; AAN14553.1; -.{EI80} DR EMBL; AF465943; AAN14564.1; -.{EI81} DR EMBL; AF465944; AAN14575.1; -.{EI82} DR EMBL; AF465945; AAN14586.1; -.{EI83} DR EMBL; AF465946; AAN14597.1; -.{EI84} DR EMBL; AF465947; AAN14608.1; -.{EI85} DR EMBL; AF465948; AAN14619.1; -.{EI86} DR EMBL; AF465949; AAN14630.1; -.{EI87} DR EMBL; AF465950; AAN14641.1; -.{EI88} DR EMBL; AF465951; AAN14652.1; -.{EI89} DR EMBL; AF465952; AAN14663.1; -.{EI90} DR EMBL; AF465953; AAN14674.1; -.{EI91} DR EMBL; AF465954; AAN14685.1; -.{EI92} DR EMBL; AF465955; AAN14696.1; -.{EI93} DR EMBL; AF465956; AAN14707.1; -.{EI94} DR EMBL; AF465958; AAN14729.1; -.{EI95} DR EMBL; AF465959; AAN14740.1; -.{EI96} DR EMBL; AF465960; AAN14751.1; -.{EI97} DR EMBL; AF465961; AAN14762.1; -.{EI98} DR EMBL; AF465962; AAN14773.1; -.{EI99} DR EMBL; AF465963; AAN14784.1; -.{EI100} DR EMBL; AF465964; AAN14795.1; -.{EI101} DR EMBL; AF465965; AAN14806.1; -.{EI102} DR EMBL; AF465966; AAN14817.1; -.{EI103} DR EMBL; AF465967; AAN14828.1; -.{EI104} DR EMBL; AF465968; AAN14839.1; -.{EI105} DR EMBL; AF465969; AAN14850.1; -.{EI106} DR EMBL; AF465970; AAN14861.1; -.{EI107} DR EMBL; AF465971; AAN14872.1; -.{EI108} DR EMBL; AF465972; AAN14883.1; -.{EI109} DR EMBL; AF465973; AAN14894.1; -.{EI110} DR EMBL; AF465974; AAN14905.1; -.{EI111} DR EMBL; AF465975; AAN14916.1; -.{EI112} DR EMBL; AF465976; AAN14927.1; -.{EI113} DR EMBL; AF465977; AAN14938.1; -.{EI114} DR EMBL; AF465978; AAN14949.1; -.{EI115} DR EMBL; AF465979; AAN14960.1; -.{EI116} DR EMBL; AF465980; AAN14971.1; -.{EI117} DR EMBL; AY195745; AAO88286.1; -.{EI118} DR EMBL; AY195747; AAO88312.1; -.{EI119} DR EMBL; AY195750; AAO88351.1; -.{EI120} DR EMBL; AY195751; AAO88364.1; -.{EI121} DR EMBL; AY195752; AAO88377.1; -.{EI122} DR EMBL; AY195754; AAO88403.1; -.{EI123} DR EMBL; AY195755; AAO88416.1; -.{EI124} DR EMBL; AY195757; AAO88442.1; -.{EI125} DR EMBL; AY195758; AAO88455.1; -.{EI126} DR EMBL; AY195759; AAO88468.1; -.{EI127} DR EMBL; AY195760; AAO88481.1; -.{EI128} DR EMBL; AY195761; AAO88494.1; -.{EI129} DR EMBL; AY195762; AAO88507.1; -.{EI130} DR EMBL; AY195763; AAO88520.1; -.{EI131} DR EMBL; AY195764; AAO88533.1; -.{EI132} DR EMBL; AY195765; AAO88546.1; -.{EI133} DR EMBL; AY195766; AAO88559.1; -.{EI134} DR EMBL; AY195767; AAO88572.1; -.{EI135} DR EMBL; AY195768; AAO88585.1; -.{EI136} DR EMBL; AY195771; AAO88624.1; -.{EI137} DR EMBL; AY195772; AAO88637.1; -.{EI138} DR EMBL; AY195773; AAO88650.1; -.{EI139} DR EMBL; AY195774; AAO88663.1; -.{EI140} DR EMBL; AY195775; AAO88676.1; -.{EI141} DR EMBL; AY195776; AAO88689.1; -.{EI142} DR EMBL; AY195777; AAO88702.1; -.{EI143} DR EMBL; AY195778; AAO88715.1; -.{EI144} DR EMBL; AY195779; AAO88728.1; -.{EI145} DR EMBL; AY195780; AAO88741.1; -.{EI146} DR EMBL; AY195781; AAO88754.1; -.{EI147} DR EMBL; AY195782; AAO88767.1; -.{EI148} DR EMBL; AY195783; AAO88780.1; -.{EI149} DR EMBL; AY195784; AAO88793.1; -.{EI150} DR EMBL; AY195786; AAO88819.1; -.{EI151} DR EMBL; AY195787; AAO88832.1; -.{EI152} DR EMBL; AY195788; AAO88845.1; -.{EI153} DR EMBL; AY195790; AAO88871.1; -.{EI154} DR EMBL; AY195791; AAO88884.1; -.{EI155} DR EMBL; AY195792; AAO88897.1; -.{EI156} DR EMBL; AY255133; AAO66624.1; -.{EI157} DR EMBL; AY255134; AAO66637.1; -.{EI158} DR EMBL; AY255135; AAO66650.1; -.{EI159} DR EMBL; AY255136; AAO66663.1; -.{EI160} DR EMBL; AY255138; AAO66689.1; -.{EI161} DR EMBL; AY255139; AAO66702.1; -.{EI162} DR EMBL; AY255140; AAO66715.1; -.{EI163} DR EMBL; AY255141; AAO66728.1; -.{EI164} DR EMBL; AY255142; AAO66741.1; -.{EI165} DR EMBL; AY255143; AAO66754.1; -.{EI166} DR EMBL; AY255144; AAO66767.1; -.{EI167} DR EMBL; AY255145; AAO66780.1; -.{EI168} DR EMBL; AY255146; AAO66793.1; -.{EI169} DR EMBL; AY255147; AAO66806.1; -.{EI170} DR EMBL; AY255148; AAO66819.1; -.{EI171} DR EMBL; AY255150; AAO66845.1; -.{EI172} DR EMBL; AY255151; AAO66858.1; -.{EI173} DR EMBL; AY255152; AAO66871.1; -.{EI174} DR EMBL; AY255153; AAO66884.1; -.{EI175} DR EMBL; AY255154; AAO66897.1; -.{EI176} DR EMBL; AY255155; AAO66910.1; -.{EI177} DR EMBL; AY255156; AAO66923.1; -.{EI178} DR EMBL; AY255157; AAO66936.1; -.{EI179} DR EMBL; AY255158; AAO66949.1; -.{EI180} DR EMBL; AY255160; AAO66975.1; -.{EI181} DR EMBL; AY255162; AAO67001.1; -.{EI182} DR EMBL; AY255163; AAO67014.1; -.{EI183} DR EMBL; AY255164; AAO67027.1; -.{EI184} DR EMBL; AY255165; AAO67040.1; -.{EI185} DR EMBL; AY255166; AAO67053.1; -.{EI186} DR EMBL; AY255167; AAO67066.1; -.{EI187} DR EMBL; AY255168; AAO67079.1; -.{EI188} DR EMBL; AY255169; AAO67091.1; -.{EI189} DR EMBL; AY255170; AAO67104.1; -.{EI190} DR EMBL; AY255171; AAO67117.1; -.{EI191} DR EMBL; AY255172; AAO67130.1; -.{EI192} DR EMBL; AY255174; AAO67156.1; -.{EI193} DR EMBL; AY255175; AAO67169.1; -.{EI194} DR EMBL; AY255176; AAO67182.1; -.{EI195} DR EMBL; AY255177; AAO67195.1; -.{EI196} DR EMBL; AY255178; AAO67208.1; -.{EI197} DR EMBL; AY255179; AAO67221.1; -.{EI198} DR EMBL; AY255180; AAO67234.1; -.{EI199} DR EMBL; AY289052; AAP47899.1; -.{EI200} DR EMBL; AY289053; AAP47912.1; -.{EI201} DR EMBL; AY289054; AAP47925.1; -.{EI202} DR EMBL; AY289055; AAP47938.1; -.{EI203} DR EMBL; AY289056; AAP47951.1; -.{EI204} DR EMBL; AY289057; AAP47964.1; -.{EI205} DR EMBL; AY289058; AAP47977.1; -.{EI206} DR EMBL; AY289059; AAP47990.1; -.{EI207} DR EMBL; AY289060; AAP48003.1; -.{EI208} DR EMBL; AY289061; AAP48016.1; -.{EI209} DR EMBL; AY289062; AAP48029.1; -.{EI210} DR EMBL; AY289063; AAP48042.1; -.{EI211} DR EMBL; AY289064; AAP48055.1; -.{EI212} DR EMBL; AY289065; AAP48068.1; -.{EI213} DR EMBL; AY289066; AAP48081.1; -.{EI214} DR EMBL; AY289067; AAP48094.1; -.{EI215} DR EMBL; AY289068; AAP48107.1; -.{EI216} DR EMBL; AY289069; AAP48120.1; -.{EI217} DR EMBL; AY289070; AAP48133.1; -.{EI218} DR EMBL; AY289071; AAP48146.1; -.{EI219} DR EMBL; AY289072; AAP48159.1; -.{EI220} DR EMBL; AY289074; AAP48185.1; -.{EI221} DR EMBL; AY289075; AAP48198.1; -.{EI222} DR EMBL; AY289076; AAP48211.1; -.{EI223} DR EMBL; AY289077; AAP48224.1; -.{EI224} DR EMBL; AY289078; AAP48237.1; -.{EI225} DR EMBL; AY289079; AAP48250.1; -.{EI226} DR EMBL; AY289080; AAP48263.1; -.{EI227} DR EMBL; AY289081; AAP48276.1; -.{EI228} DR EMBL; AY289082; AAP48289.1; -.{EI229} DR EMBL; AY289083; AAP48302.1; -.{EI230} DR EMBL; AY289084; AAP48315.1; -.{EI231} DR EMBL; AY289085; AAP48328.1; -.{EI232} DR EMBL; AY289086; AAP48341.1; -.{EI233} DR EMBL; AY289087; AAP48354.1; -.{EI234} DR EMBL; AY289088; AAP48367.1; -.{EI235} DR EMBL; AY289089; AAP48380.1; -.{EI236} DR EMBL; AY289090; AAP48393.1; -.{EI237} DR EMBL; AY289091; AAP48406.1; -.{EI238} DR EMBL; AY289092; AAP48419.1; -.{EI239} DR EMBL; AY289093; AAP48431.1; -.{EI240} DR EMBL; AY289094; AAP48444.1; -.{EI241} DR EMBL; AY289095; AAP48457.1; -.{EI242} DR EMBL; AY289096; AAP48470.1; -.{EI243} DR EMBL; AY289099; AAP48509.1; -.{EI244} DR EMBL; AY289100; AAP48522.1; -.{EI245} DR EMBL; AY289101; AAP48535.1; -.{EI246} DR EMBL; AY289102; AAP48548.1; -.{EI247} DR GO; GO:0016021; C:integral to membrane; IEA. DR GO; GO:0005739; C:mitochondrion; IEA. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA. DR GO; GO:0016491; F:oxidoreductase activity; IEA. DR GO; GO:0006118; P:electron transport; IEA. DR InterPro; IPR000298; CytC_oxdse_III. DR Pfam; PF00510; COX3; 1. DR ProDom; PD000382; CytC_oxdse_III; 1. DR TIGRFAMs; TIGR01732; tiny_TM_bacill; 1. DR PROSITE; PS50253; COX3; 1. KW Oxidoreductase{EA1}; Transmembrane{EA1}; Mitochondrion{EA1,EP248}. ** ** ################# SOURCE SECTION ################## ** Homo sapiens mitochondrion, complete genome. ** [1] ** 1-16571 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16571 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16571 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16574 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16574 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16574 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16571 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16571 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16566 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16566 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16566 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16571 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16571 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16558 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16558 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16558 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16568 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16568 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16568 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16566 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16566 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16566 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16561 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16561 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16562 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16562 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16562 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16561 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16561 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16572 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16572 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16572 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16572 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16572 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16572 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16568 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16568 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16568 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16560 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16560 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16562 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16562 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16562 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16568 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16568 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16570 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16570 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16570 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16570 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16571 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16571 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16568 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16568 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16570 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16570 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16572 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16572 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16570 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16570 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16560 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16560 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16564 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16564 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16568 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16568 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16568 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16568 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-8828 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8828 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8827 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8827 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8828 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8828 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8820 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8820 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8820 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8820 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16566 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16566 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16565 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16565 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16572 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16572 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16567 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16567 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16557 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16557 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16567 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16567 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16565 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16565 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16566 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16566 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16566 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16566 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16567 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16567 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16556 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16556 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16492 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16492 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16562 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16562 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16486 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16486 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16571 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16571 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16561 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16561 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16558 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16558 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16574 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16574 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16579 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16579 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16576 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16576 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16575 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16575 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16566 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16566 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16558 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16558 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16566 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16566 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16562 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16562 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16576 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16576 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16559 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16559 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16571 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16575 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16575 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16573 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16573 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16559 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16559 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16560 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16567 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16568 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16568 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16571 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16560 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16568 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16568 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16571 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16574 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16574 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16560 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16560 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** source 1..16571 ** /db_xref="taxon:9606" ** /note="from African (Yoruba) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17889.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /country="Australia" ** /db_xref="taxon:9606" ** /note="from Aborigine" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17213.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16574 ** /country="Australia" ** /db_xref="taxon:9606" ** /note="from Aborigine" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9212..9992 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17226.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from Asian Indian" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17252.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Bamileke)" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17265.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 4) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Biaka)" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17278.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Biaka)" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17291.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from Buriat individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17304.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from Chukchi individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17317.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17330.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17343.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16571 ** /db_xref="taxon:9606" ** /note="from Crimean Tatar individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17356.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from Dutch individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17369.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from African (Effik) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17382.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from African (Effik) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17395.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from English individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17408.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from Evenki individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17421.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from African (Ewondo) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17434.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from French individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17447.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from Georgian individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17460.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from German individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17473.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from South American Indian (Guarani) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17486.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Hausa) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17499.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Ibo) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17512.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16566 ** /db_xref="taxon:9606" ** /note="from African (Ibo) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17525.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from Japanese individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17564.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from Khirgiz individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17577.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16571 ** /db_xref="taxon:9606" ** /note="from African (Kikuyu) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17590.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16558 ** /db_xref="taxon:9606" ** /note="from Korean individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9196..9976 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17603.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from African (Lisongo) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17616.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16568 ** /db_xref="taxon:9606" ** /note="from African (Mandenka) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17629.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16566 ** /db_xref="taxon:9606" ** /note="from African (Mbenzele) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17642.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Mbenzele) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17655.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16561 ** /db_xref="taxon:9606" ** /note="from African (Mbuti) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9199..9979 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17668.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16562 ** /db_xref="taxon:9606" ** /note="from African (Mbuti) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9200..9980 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17681.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from African (Mkamba) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17694.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16561 ** /db_xref="taxon:9606" ** /note="from North American Indian (Piman) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9199..9979 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17707.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16572 ** /db_xref="taxon:9606" ** /note="from PNG (Coast) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17720.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from PNG (Coast) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17733.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16572 ** /db_xref="taxon:9606" ** /note="from PNG (Highland) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17746.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16572 ** /db_xref="taxon:9606" ** /note="from PNG (Highland) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17759.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16568 ** /db_xref="taxon:9606" ** /note="from Saami individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17772.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16560 ** /db_xref="taxon:9606" ** /note="from Samoan individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17785.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from African (San) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17798.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (San) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17811.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16562 ** /db_xref="taxon:9606" ** /note="from Uzbek individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9200..9980 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17837.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Yoruba) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17876.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /country="India" ** /db_xref="taxon:9606" ** /haplotype="M*2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="2619" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54806.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16568 ** /country="Mauritania" ** /db_xref="taxon:9606" ** /haplotype="L2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="441" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome co oxidase subunit III" ** /protein_id="AAL54393.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Spain: Canary Islands, Tenerife" ** /db_xref="taxon:9606" ** /haplotype="U31" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="117" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54403.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="U32" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="249" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54416.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16570 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="M11" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="250" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54429.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16570 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="T5" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="252" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54442.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="X" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="255" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54455.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="J1b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="268" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54468.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="L1a" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="271" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54481.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Morocco: Berber" ** /db_xref="taxon:9606" ** /haplotype="V" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="364" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54507.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Mauritania" ** /db_xref="taxon:9606" ** /haplotype="L3b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="430" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54520.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Mauritania" ** /db_xref="taxon:9606" ** /haplotype="H1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="446" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54546.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Mauritania" ** /db_xref="taxon:9606" ** /haplotype="L1b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="451" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54559.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="U21" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="766" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54572.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16571 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="M12" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="771" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54585.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="L3d" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="800" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54611.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="N1b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="832" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54624.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="U2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="842" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54637.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16568 ** /country="Spain: Maragato" ** /db_xref="taxon:9606" ** /haplotype="J2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M26" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54650.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16570 ** /country="Spain: Maragato" ** /db_xref="taxon:9606" ** /haplotype="H2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M27" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54663.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Spain: Maragato" ** /db_xref="taxon:9606" ** /haplotype="W" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M47" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54676.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Spain: Leon" ** /db_xref="taxon:9606" ** /haplotype="U22" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M68" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54689.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16572 ** /country="Spain: Leon" ** /db_xref="taxon:9606" ** /haplotype="K" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M72" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54702.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16570 ** /country="Spain: Leon" ** /db_xref="taxon:9606" ** /haplotype="T1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M78" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54715.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16560 ** /country="Spain: Leon" ** /db_xref="taxon:9606" ** /haplotype="I" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M90" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54728.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="U6" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="279" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54741.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16564 ** /country="Spain: Canary Islands, Tenerife" ** /db_xref="taxon:9606" ** /haplotype="C" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="4" ** CDS 9202..9982 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54754.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16568 ** /country="Spain: Canary Islands, Hierro" ** /db_xref="taxon:9606" ** /haplotype="A" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="248" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54767.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16568 ** /country="Spain: Andalusia" ** /db_xref="taxon:9606" ** /haplotype="U7" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="1646" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54780.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Philippines" ** /db_xref="taxon:9606" ** /haplotype="M*1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="2601" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54793.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..8828 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="African" ** /clone="NGR0524" ** CDS 2059..2839 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14542.1" ** CDS_IN_EMBL_ENTRY 10 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8827 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="African" ** /clone="NGR0522" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14553.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="African" ** /clone="NGR0475" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14564.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="African" ** /clone="NGR0510" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14575.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="ARL0058" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14586.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Japanese" ** /clone="JAP1043" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14597.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Japanese" ** /clone="JAP1045" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14608.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8828 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Japanese" ** /clone="JAP1044" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14619.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="GRC0149" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14630.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KCR0029" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14641.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KRC0033" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14652.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="GRC0131" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14663.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="GRC0169" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14674.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KTN0018" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14685.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KTN0209" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14696.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KTN0130" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14707.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8820 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KPO0001" ** CDS 2051..2831 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14729.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8820 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KPO0039" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14740.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KPO0023" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14751.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="PTJ0068" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14762.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="PTJ0003" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14773.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="PTJ0001" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14784.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Peru" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1876" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14795.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Peru" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1881" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14806.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Peru" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1875" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14817.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Peru" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1878" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14828.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1880" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14839.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="TYR0004" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14850.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="TYR0016" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14861.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Caucasian" ** /clone="WTE1145" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14872.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Caucasian" ** /clone="WTE1182" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14883.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Caucasian" ** /clone="WTE1150" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14894.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="WPI0167" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14905.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0623" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14916.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0665" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14927.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0669" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14938.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0591" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14949.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0650" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14960.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0637" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14971.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E12T" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="T haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88286.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="E4H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88312.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E17V" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="V haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88351.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16566 ** /db_xref="taxon:9606" ** /haplotype="E2H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9984,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88364.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E7H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88377.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E9J" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="J haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88403.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="As11G" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="G haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88416.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E6H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88442.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E5H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88455.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16565 ** /db_xref="taxon:9606" ** /haplotype="Na4C" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Native American" ** /isolation_source="C haplogroup Native American" ** CDS 9203..9983 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9983,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88468.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="As1A" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="A haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88481.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="As12Z" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Z Haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88494.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="As7G" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="G Halogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88507.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /haplotype="As4C" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Asian" ** /isolation_source="C Haplogroup Asian" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88520.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E19U" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="U haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88533.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="E13K" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="K haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88546.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16567 ** /db_xref="taxon:9606" ** /haplotype="A11L2b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L2b haplogroup" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88559.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E11T" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="T haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88572.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E15W" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="W haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88585.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="As2A" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Asian" ** /isolation_source="A haplogroup Asian" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88624.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="As5C" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Asian" ** /isolation_source="C haplogroup Asian" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88637.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="E18X" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="European" ** /isolation_source="X haplogroup European" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88650.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="E10J" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="J haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88663.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="E1H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88676.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="A9L2a" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L2a haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88689.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16557 ** /db_xref="taxon:9606" ** /haplotype="A10L1A2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L1A2 haplogroup" ** CDS 9195..9975 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9975,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88702.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="E8J" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="J haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88715.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E14W" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="W haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88728.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16567 ** /db_xref="taxon:9606" ** /haplotype="A2L1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L1a haplogroup" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88741.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E16V" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="V haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88754.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="A7NL" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L3 haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88767.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16565 ** /db_xref="taxon:9606" ** /haplotype="A4L1B2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L1B2 haplogroup" ** CDS 9203..9983 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9983,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88780.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16566 ** /db_xref="taxon:9606" ** /haplotype="A8NL" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L3 haplogroup" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88793.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16566 ** /db_xref="taxon:9606" ** /haplotype="Na5A" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Native American" ** /isolation_source="A haplogroup Native American" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9984,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88819.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="Na3X" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Native American" ** /isolation_source="X haplogroup Native American" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88832.1" ** 11-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="A5L2A1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L2A1 haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88845.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="As8D" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Asian" ** /isolation_source="D haplogroup Asian" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88871.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16567 ** /db_xref="taxon:9606" ** /haplotype="As10F" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="F haplogroup" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88884.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="As9Y" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Y haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88897.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16556 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7812" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9195..9975 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9975,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66624.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16492 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7550" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9130..9910 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9910,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66637.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16562 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7589" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9200..9980 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9980,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66650.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16486 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10313" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9124..9904 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9904,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66663.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16571 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8426" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9989,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66689.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="EWK28" ** /isolation_source="Ewenki from Inner Mongolia" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66702.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8141" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9199..9979 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9979,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66715.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7834" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66728.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Miao271" ** /isolation_source="Miao from Fenghuang, Hunan" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66741.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="DW48" ** /isolation_source="Daur from Inner Mongolia" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66754.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6954" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66767.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16558 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6967" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9196..9976 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9976,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66780.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Mg246" ** /isolation_source="Mongolian from Inner Mongolia" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66793.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16574 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7595" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9212..9992 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9992,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66806.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7817" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66819.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16579 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6958" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9217..9997 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9997,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66845.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7829" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66858.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10352" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66871.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8420" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66884.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16576 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10334" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9214..9994 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9994,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66897.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6979" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66910.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10324" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66923.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8416" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66936.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7711" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66949.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8166" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66975.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7837n" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67001.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16575 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8168" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9213..9993 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9993,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67014.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16566 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7811" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9984,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67027.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16558 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7830" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9196..9976 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9976,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67040.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16566 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6980" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9984,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67053.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8451" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67066.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7809" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67079.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="YN289" ** /isolation_source="Han from Kunming, Yunnan" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67091.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16562 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7813" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9200..9980 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9980,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67104.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10362" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67117.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7825" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67130.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8435" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67156.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7824" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67169.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7710" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67182.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8167" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67195.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16576 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="YN163" ** /isolation_source="Han from Kunming, Yunnan" ** CDS 9214..9994 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9994,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67208.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16559 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6973" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9197..9977 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9977,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67221.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8147" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67234.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus14" ** /isolation_source="Australian Aborigine" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47899.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16571 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus15" ** /isolation_source="Australian Aborigine" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9989,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47912.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus16" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47925.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus17" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47938.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus20" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47951.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus21" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47964.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus22" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47977.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16575 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus23" ** /isolation_source="Australian Aborigine" ** CDS 9212..9992 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9992,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47990.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="B2" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48003.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="B4" ** /isolation_source="Australian Aborigine" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48016.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="B6" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48029.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="E4" ** /isolation_source="Australian Aborigine" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48042.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="E9" ** /isolation_source="Australian Aborigine" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48055.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="F5" ** /isolation_source="Australian Aborigine" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48068.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16573 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Y6" ** /isolation_source="Australian Aborigine" ** CDS 9211..9991 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9991,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48081.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Y7" ** /isolation_source="Australian Aborigine" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48094.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16559 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="C1112" ** /isolation_source="Cook Islander" ** CDS 9197..9977 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9977,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48107.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16560 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="C1190" ** /isolation_source="Cook Islander" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48120.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="CAM" ** /isolation_source="Filipino" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48133.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="T1331" ** /isolation_source="Southern Indian (Kannada)" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48146.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="K11b" ** /isolation_source="Southern Indian (Koraga)" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48159.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M306" ** /isolation_source="Southern Indian (Mullukurunan)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48185.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16571 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="961" ** /isolation_source="Nasioi" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9989,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48198.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16560 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="100" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9197..9977 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9977,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48211.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="CP8" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48224.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GP4" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48237.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE16" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48250.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE18" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48263.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE23" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48276.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE4" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48289.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE7" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48302.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="36" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48315.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="NG12" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48328.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="NG29" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48341.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH10" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48354.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH17" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48367.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH19" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48380.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH23" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48393.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16571 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH29" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9989,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48406.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH33" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48419.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="S1216" ** /isolation_source="Samoan" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48431.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="S1220" ** /isolation_source="Samoan" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48444.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16574 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="496" ** /isolation_source="Taiwanese Indian" ** CDS 9212..9992 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9992,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48457.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="513" ** /isolation_source="Taiwanese Indian" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48470.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="DCH002" ** /isolation_source="Thai" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48509.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Sb13" ** /isolation_source="Thai" ** CDS 9199..9979 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9979,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48522.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16560 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Sb29" ** /isolation_source="Thai" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48535.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16560 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Tongan" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48548.1" ** 08-JUL-2003 Last updated, EMBL entry ** ################# INTERNAL SECTION ################## **EV EA1; Rulebase; -; RU003375V0.42; 18-NOV-2002. **EV EI2; EMBL; -; AAL54806.1; 07-FEB-2002. **EV EI3; EMBL; -; AAK17889.2; 26-APR-2001. **EV EI4; EMBL; -; AAK17213.1; 26-APR-2001. **EV EI5; EMBL; -; AAK17226.2; 26-APR-2001. **EV EI6; EMBL; -; AAK17252.1; 26-APR-2001. **EV EI7; EMBL; -; AAK17265.2; 26-APR-2001. **EV EI8; EMBL; -; AAK17278.2; 26-APR-2001. **EV EI9; EMBL; -; AAK17291.2; 26-APR-2001. **EV EI10; EMBL; -; AAK17304.2; 26-APR-2001. **EV EI11; EMBL; -; AAK17317.2; 26-APR-2001. **EV EI12; EMBL; -; AAK17330.2; 26-APR-2001. **EV EI13; EMBL; -; AAK17343.2; 26-APR-2001. **EV EI14; EMBL; -; AAK17356.2; 26-APR-2001. **EV EI15; EMBL; -; AAK17369.2; 26-APR-2001. **EV EI16; EMBL; -; AAK17382.1; 26-APR-2001. **EV EI17; EMBL; -; AAK17395.1; 26-APR-2001. **EV EI18; EMBL; -; AAK17408.1; 26-APR-2001. **EV EI19; EMBL; -; AAK17421.1; 26-APR-2001. **EV EI20; EMBL; -; AAK17434.2; 26-APR-2001. **EV EI21; EMBL; -; AAK17447.2; 26-APR-2001. **EV EI22; EMBL; -; AAK17460.1; 26-APR-2001. **EV EI23; EMBL; -; AAK17473.1; 26-APR-2001. **EV EI24; EMBL; -; AAK17486.2; 26-APR-2001. **EV EI25; EMBL; -; AAK17499.2; 26-APR-2001. **EV EI26; EMBL; -; AAK17512.2; 26-APR-2001. **EV EI27; EMBL; -; AAK17525.2; 26-APR-2001. **EV EI28; EMBL; -; AAK17564.1; 26-APR-2001. **EV EI29; EMBL; -; AAK17577.2; 26-APR-2001. **EV EI30; EMBL; -; AAK17590.2; 26-APR-2001. **EV EI31; EMBL; -; AAK17603.2; 26-APR-2001. **EV EI32; EMBL; -; AAK17616.2; 26-APR-2001. **EV EI33; EMBL; -; AAK17629.2; 26-APR-2001. **EV EI34; EMBL; -; AAK17642.2; 26-APR-2001. **EV EI35; EMBL; -; AAK17655.2; 26-APR-2001. **EV EI36; EMBL; -; AAK17668.2; 26-APR-2001. **EV EI37; EMBL; -; AAK17681.2; 26-APR-2001. **EV EI38; EMBL; -; AAK17694.1; 26-APR-2001. **EV EI39; EMBL; -; AAK17707.2; 26-APR-2001. **EV EI40; EMBL; -; AAK17720.2; 26-APR-2001. **EV EI41; EMBL; -; AAK17733.2; 26-APR-2001. **EV EI42; EMBL; -; AAK17746.2; 26-APR-2001. **EV EI43; EMBL; -; AAK17759.2; 26-APR-2001. **EV EI44; EMBL; -; AAK17772.2; 26-APR-2001. **EV EI45; EMBL; -; AAK17785.2; 26-APR-2001. **EV EI46; EMBL; -; AAK17798.2; 26-APR-2001. **EV EI47; EMBL; -; AAK17811.2; 26-APR-2001. **EV EI48; EMBL; -; AAK17837.2; 26-APR-2001. **EV EI49; EMBL; -; AAK17876.2; 26-APR-2001. **EV EI50; EMBL; -; AAL54393.1; 07-FEB-2002. **EV EI51; EMBL; -; AAL54403.1; 07-FEB-2002. **EV EI52; EMBL; -; AAL54416.1; 07-FEB-2002. **EV EI53; EMBL; -; AAL54429.1; 07-FEB-2002. **EV EI54; EMBL; -; AAL54442.1; 07-FEB-2002. **EV EI55; EMBL; -; AAL54455.1; 07-FEB-2002. **EV EI56; EMBL; -; AAL54468.1; 07-FEB-2002. **EV EI57; EMBL; -; AAL54481.1; 07-FEB-2002. **EV EI58; EMBL; -; AAL54507.1; 07-FEB-2002. **EV EI59; EMBL; -; AAL54520.1; 07-FEB-2002. **EV EI60; EMBL; -; AAL54546.1; 07-FEB-2002. **EV EI61; EMBL; -; AAL54559.1; 07-FEB-2002. **EV EI62; EMBL; -; AAL54572.1; 07-FEB-2002. **EV EI63; EMBL; -; AAL54585.1; 07-FEB-2002. **EV EI64; EMBL; -; AAL54611.1; 07-FEB-2002. **EV EI65; EMBL; -; AAL54624.1; 07-FEB-2002. **EV EI66; EMBL; -; AAL54637.1; 07-FEB-2002. **EV EI67; EMBL; -; AAL54650.1; 07-FEB-2002. **EV EI68; EMBL; -; AAL54663.1; 07-FEB-2002. **EV EI69; EMBL; -; AAL54676.1; 07-FEB-2002. **EV EI70; EMBL; -; AAL54689.1; 07-FEB-2002. **EV EI71; EMBL; -; AAL54702.1; 07-FEB-2002. **EV EI72; EMBL; -; AAL54715.1; 07-FEB-2002. **EV EI73; EMBL; -; AAL54728.1; 07-FEB-2002. **EV EI74; EMBL; -; AAL54741.1; 07-FEB-2002. **EV EI75; EMBL; -; AAL54754.1; 07-FEB-2002. **EV EI76; EMBL; -; AAL54767.1; 07-FEB-2002. **EV EI77; EMBL; -; AAL54780.1; 07-FEB-2002. **EV EI78; EMBL; -; AAL54793.1; 07-FEB-2002. **EV EI79; EMBL; -; AAN14542.1; 12-DEC-2002. **EV EI80; EMBL; -; AAN14553.1; 12-DEC-2002. **EV EI81; EMBL; -; AAN14564.1; 12-DEC-2002. **EV EI82; EMBL; -; AAN14575.1; 12-DEC-2002. **EV EI83; EMBL; -; AAN14586.1; 12-DEC-2002. **EV EI84; EMBL; -; AAN14597.1; 12-DEC-2002. **EV EI85; EMBL; -; AAN14608.1; 12-DEC-2002. **EV EI86; EMBL; -; AAN14619.1; 12-DEC-2002. **EV EI87; EMBL; -; AAN14630.1; 12-DEC-2002. **EV EI88; EMBL; -; AAN14641.1; 12-DEC-2002. **EV EI89; EMBL; -; AAN14652.1; 12-DEC-2002. **EV EI90; EMBL; -; AAN14663.1; 12-DEC-2002. **EV EI91; EMBL; -; AAN14674.1; 12-DEC-2002. **EV EI92; EMBL; -; AAN14685.1; 12-DEC-2002. **EV EI93; EMBL; -; AAN14696.1; 12-DEC-2002. **EV EI94; EMBL; -; AAN14707.1; 12-DEC-2002. **EV EI95; EMBL; -; AAN14729.1; 12-DEC-2002. **EV EI96; EMBL; -; AAN14740.1; 12-DEC-2002. **EV EI97; EMBL; -; AAN14751.1; 12-DEC-2002. **EV EI98; EMBL; -; AAN14762.1; 12-DEC-2002. **EV EI99; EMBL; -; AAN14773.1; 12-DEC-2002. **EV EI100; EMBL; -; AAN14784.1; 12-DEC-2002. **EV EI101; EMBL; -; AAN14795.1; 12-DEC-2002. **EV EI102; EMBL; -; AAN14806.1; 12-DEC-2002. **EV EI103; EMBL; -; AAN14817.1; 12-DEC-2002. **EV EI104; EMBL; -; AAN14828.1; 12-DEC-2002. **EV EI105; EMBL; -; AAN14839.1; 12-DEC-2002. **EV EI106; EMBL; -; AAN14850.1; 12-DEC-2002. **EV EI107; EMBL; -; AAN14861.1; 12-DEC-2002. **EV EI108; EMBL; -; AAN14872.1; 12-DEC-2002. **EV EI109; EMBL; -; AAN14883.1; 12-DEC-2002. **EV EI110; EMBL; -; AAN14894.1; 12-DEC-2002. **EV EI111; EMBL; -; AAN14905.1; 12-DEC-2002. **EV EI112; EMBL; -; AAN14916.1; 12-DEC-2002. **EV EI113; EMBL; -; AAN14927.1; 12-DEC-2002. **EV EI114; EMBL; -; AAN14938.1; 12-DEC-2002. **EV EI115; EMBL; -; AAN14949.1; 12-DEC-2002. **EV EI116; EMBL; -; AAN14960.1; 12-DEC-2002. **EV EI117; EMBL; -; AAN14971.1; 12-DEC-2002. **EV EI118; EMBL; -; AAO88286.1; 14-APR-2003. **EV EI119; EMBL; -; AAO88312.1; 14-APR-2003. **EV EI120; EMBL; -; AAO88351.1; 14-APR-2003. **EV EI121; EMBL; -; AAO88364.1; 14-APR-2003. **EV EI122; EMBL; -; AAO88377.1; 14-APR-2003. **EV EI123; EMBL; -; AAO88403.1; 14-APR-2003. **EV EI124; EMBL; -; AAO88416.1; 14-APR-2003. **EV EI125; EMBL; -; AAO88442.1; 14-APR-2003. **EV EI126; EMBL; -; AAO88455.1; 14-APR-2003. **EV EI127; EMBL; -; AAO88468.1; 14-APR-2003. **EV EI128; EMBL; -; AAO88481.1; 14-APR-2003. **EV EI129; EMBL; -; AAO88494.1; 14-APR-2003. **EV EI130; EMBL; -; AAO88507.1; 14-APR-2003. **EV EI131; EMBL; -; AAO88520.1; 14-APR-2003. **EV EI132; EMBL; -; AAO88533.1; 14-APR-2003. **EV EI133; EMBL; -; AAO88546.1; 14-APR-2003. **EV EI134; EMBL; -; AAO88559.1; 14-APR-2003. **EV EI135; EMBL; -; AAO88572.1; 14-APR-2003. **EV EI136; EMBL; -; AAO88585.1; 14-APR-2003. **EV EI137; EMBL; -; AAO88624.1; 14-APR-2003. **EV EI138; EMBL; -; AAO88637.1; 14-APR-2003. **EV EI139; EMBL; -; AAO88650.1; 14-APR-2003. **EV EI140; EMBL; -; AAO88663.1; 14-APR-2003. **EV EI141; EMBL; -; AAO88676.1; 14-APR-2003. **EV EI142; EMBL; -; AAO88689.1; 14-APR-2003. **EV EI143; EMBL; -; AAO88702.1; 14-APR-2003. **EV EI144; EMBL; -; AAO88715.1; 14-APR-2003. **EV EI145; EMBL; -; AAO88728.1; 14-APR-2003. **EV EI146; EMBL; -; AAO88741.1; 14-APR-2003. **EV EI147; EMBL; -; AAO88754.1; 14-APR-2003. **EV EI148; EMBL; -; AAO88767.1; 14-APR-2003. **EV EI149; EMBL; -; AAO88780.1; 14-APR-2003. **EV EI150; EMBL; -; AAO88793.1; 14-APR-2003. **EV EI151; EMBL; -; AAO88819.1; 14-APR-2003. **EV EI152; EMBL; -; AAO88832.1; 14-APR-2003. **EV EI153; EMBL; -; AAO88845.1; 14-APR-2003. **EV EI154; EMBL; -; AAO88871.1; 14-APR-2003. **EV EI155; EMBL; -; AAO88884.1; 14-APR-2003. **EV EI156; EMBL; -; AAO88897.1; 14-APR-2003. **EV EI157; EMBL; -; AAO66624.1; 23-JUL-2003. **EV EI158; EMBL; -; AAO66637.1; 23-JUL-2003. **EV EI159; EMBL; -; AAO66650.1; 23-JUL-2003. **EV EI160; EMBL; -; AAO66663.1; 23-JUL-2003. **EV EI161; EMBL; -; AAO66689.1; 23-JUL-2003. **EV EI162; EMBL; -; AAO66702.1; 23-JUL-2003. **EV EI163; EMBL; -; AAO66715.1; 23-JUL-2003. **EV EI164; EMBL; -; AAO66728.1; 23-JUL-2003. **EV EI165; EMBL; -; AAO66741.1; 23-JUL-2003. **EV EI166; EMBL; -; AAO66754.1; 23-JUL-2003. **EV EI167; EMBL; -; AAO66767.1; 23-JUL-2003. **EV EI168; EMBL; -; AAO66780.1; 23-JUL-2003. **EV EI169; EMBL; -; AAO66793.1; 23-JUL-2003. **EV EI170; EMBL; -; AAO66806.1; 23-JUL-2003. **EV EI171; EMBL; -; AAO66819.1; 23-JUL-2003. **EV EI172; EMBL; -; AAO66845.1; 23-JUL-2003. **EV EI173; EMBL; -; AAO66858.1; 23-JUL-2003. **EV EI174; EMBL; -; AAO66871.1; 23-JUL-2003. **EV EI175; EMBL; -; AAO66884.1; 23-JUL-2003. **EV EI176; EMBL; -; AAO66897.1; 23-JUL-2003. **EV EI177; EMBL; -; AAO66910.1; 23-JUL-2003. **EV EI178; EMBL; -; AAO66923.1; 23-JUL-2003. **EV EI179; EMBL; -; AAO66936.1; 23-JUL-2003. **EV EI180; EMBL; -; AAO66949.1; 23-JUL-2003. **EV EI181; EMBL; -; AAO66975.1; 23-JUL-2003. **EV EI182; EMBL; -; AAO67001.1; 23-JUL-2003. **EV EI183; EMBL; -; AAO67014.1; 23-JUL-2003. **EV EI184; EMBL; -; AAO67027.1; 23-JUL-2003. **EV EI185; EMBL; -; AAO67040.1; 23-JUL-2003. **EV EI186; EMBL; -; AAO67053.1; 23-JUL-2003. **EV EI187; EMBL; -; AAO67066.1; 23-JUL-2003. **EV EI188; EMBL; -; AAO67079.1; 23-JUL-2003. **EV EI189; EMBL; -; AAO67091.1; 23-JUL-2003. **EV EI190; EMBL; -; AAO67104.1; 23-JUL-2003. **EV EI191; EMBL; -; AAO67117.1; 23-JUL-2003. **EV EI192; EMBL; -; AAO67130.1; 23-JUL-2003. **EV EI193; EMBL; -; AAO67156.1; 23-JUL-2003. **EV EI194; EMBL; -; AAO67169.1; 23-JUL-2003. **EV EI195; EMBL; -; AAO67182.1; 23-JUL-2003. **EV EI196; EMBL; -; AAO67195.1; 23-JUL-2003. **EV EI197; EMBL; -; AAO67208.1; 23-JUL-2003. **EV EI198; EMBL; -; AAO67221.1; 23-JUL-2003. **EV EI199; EMBL; -; AAO67234.1; 23-JUL-2003. **EV EI200; EMBL; -; AAP47899.1; 14-JUL-2003. **EV EI201; EMBL; -; AAP47912.1; 14-JUL-2003. **EV EI202; EMBL; -; AAP47925.1; 14-JUL-2003. **EV EI203; EMBL; -; AAP47938.1; 14-JUL-2003. **EV EI204; EMBL; -; AAP47951.1; 14-JUL-2003. **EV EI205; EMBL; -; AAP47964.1; 14-JUL-2003. **EV EI206; EMBL; -; AAP47977.1; 14-JUL-2003. **EV EI207; EMBL; -; AAP47990.1; 14-JUL-2003. **EV EI208; EMBL; -; AAP48003.1; 14-JUL-2003. **EV EI209; EMBL; -; AAP48016.1; 14-JUL-2003. **EV EI210; EMBL; -; AAP48029.1; 14-JUL-2003. **EV EI211; EMBL; -; AAP48042.1; 14-JUL-2003. **EV EI212; EMBL; -; AAP48055.1; 14-JUL-2003. **EV EI213; EMBL; -; AAP48068.1; 14-JUL-2003. **EV EI214; EMBL; -; AAP48081.1; 14-JUL-2003. **EV EI215; EMBL; -; AAP48094.1; 14-JUL-2003. **EV EI216; EMBL; -; AAP48107.1; 14-JUL-2003. **EV EI217; EMBL; -; AAP48120.1; 14-JUL-2003. **EV EI218; EMBL; -; AAP48133.1; 14-JUL-2003. **EV EI219; EMBL; -; AAP48146.1; 14-JUL-2003. **EV EI220; EMBL; -; AAP48159.1; 14-JUL-2003. **EV EI221; EMBL; -; AAP48185.1; 14-JUL-2003. **EV EI222; EMBL; -; AAP48198.1; 14-JUL-2003. **EV EI223; EMBL; -; AAP48211.1; 14-JUL-2003. **EV EI224; EMBL; -; AAP48224.1; 14-JUL-2003. **EV EI225; EMBL; -; AAP48237.1; 14-JUL-2003. **EV EI226; EMBL; -; AAP48250.1; 14-JUL-2003. **EV EI227; EMBL; -; AAP48263.1; 14-JUL-2003. **EV EI228; EMBL; -; AAP48276.1; 14-JUL-2003. **EV EI229; EMBL; -; AAP48289.1; 14-JUL-2003. **EV EI230; EMBL; -; AAP48302.1; 14-JUL-2003. **EV EI231; EMBL; -; AAP48315.1; 14-JUL-2003. **EV EI232; EMBL; -; AAP48328.1; 14-JUL-2003. **EV EI233; EMBL; -; AAP48341.1; 14-JUL-2003. **EV EI234; EMBL; -; AAP48354.1; 14-JUL-2003. **EV EI235; EMBL; -; AAP48367.1; 14-JUL-2003. **EV EI236; EMBL; -; AAP48380.1; 14-JUL-2003. **EV EI237; EMBL; -; AAP48393.1; 14-JUL-2003. **EV EI238; EMBL; -; AAP48406.1; 14-JUL-2003. **EV EI239; EMBL; -; AAP48419.1; 14-JUL-2003. **EV EI240; EMBL; -; AAP48431.1; 14-JUL-2003. **EV EI241; EMBL; -; AAP48444.1; 14-JUL-2003. **EV EI242; EMBL; -; AAP48457.1; 14-JUL-2003. **EV EI243; EMBL; -; AAP48470.1; 14-JUL-2003. **EV EI244; EMBL; -; AAP48509.1; 14-JUL-2003. **EV EI245; EMBL; -; AAP48522.1; 14-JUL-2003. **EV EI246; EMBL; -; AAP48535.1; 14-JUL-2003. **EV EI247; EMBL; -; AAP48548.1; 14-JUL-2003. **EV EP248; TrEMBL; -; AAK17889.2; 26-APR-2001. **EV EP249; Merge; -; -; 18-JUN-2003. **ID XXXX_HUMAN **PM ProDom; PD000382; CytC_oxdse_III; 6; 260; T; 14-APR-2003; **PM Pfam; PF00510; COX3; 6; 260; T; 06-NOV-2003; **PM PROSITE; PS50253; COX3; 4; 260; T; 07-NOV-2003; **PM TIGRFAMs; TIGR01732; tiny_TM_bacill; 190; 215; T; 23-OCT-2003; SQ SEQUENCE 260 AA; 29864 MW; 1385EF748B7C1488 CRC64; MTHQSHAYHM VKPSPWPLTG ALSALLMTSG LAMWFHFHSM TLLMLGLLTN TLTMYQWWRD VTRESTYQGH HTPPVQKGLR YGMILFITSE VFFFAGFFWA FYHSSLAPTP QLGGHWPPTG ITPLNPLEVP LLNTSVLLAS GVSITWAHHS LMENNRNQMI QALLITILLG LYFTLLQASE YFESPFTISD GIYGSTFFVA TGFHGLHVII GSTFLTICFI RQLMFHFTSK HHFGFEAAAW YWHFVDVVWL FLYVSIYWWG // ID 3BHS_BOVIN STANDARD; PRT; 372 AA. AC P14893; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE 3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase (3Beta-HSD) DE [Includes: 3-beta-hydroxy-delta(5)-steroid dehydrogenase (EC DE 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) (Progesterone DE reductase); Steroid delta-isomerase (EC 5.3.3.1) (Delta-5-3- DE ketosteroid isomerase)]. GN HSD3B. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=90092517; PubMed=2599102; RA Zhao H.-F., Simard J., Labrie C., Breton N., Rheaume E., Luu-The V., RA Labrie F.; RT "Molecular cloning, cDNA structure and predicted amino acid sequence RT of bovine 3 beta-hydroxy-5-ene steroid dehydrogenase/delta 5-delta 4 RT isomerase."; RL FEBS Lett. 259:153-157(1989). RN [2] RP PARTIAL SEQUENCE, AND CD STUDIES. RC TISSUE=Adrenal gland; RX MEDLINE=91329389; PubMed=1868086; RA Rutherfurd K.J., Chen S., Shively J.E.; RT "Isolation and amino acid sequence analysis of bovine adrenal 3 beta- RT hydroxysteroid dehydrogenase/steroid isomerase."; RL Biochemistry 30:8108-8116(1991). CC -!- FUNCTION: 3beta-HSD is a bifunctional enzyme, that catalyzes the CC oxidative conversion of delta(5)-ene-3-beta-hydroxy steroid, and CC the oxidative conversion of ketosteroids. The 3beta-HSD enzymatic CC system plays a crucial role in the biosynthesis of all classes of CC hormonal steroids. CC -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-delta(5)-steroid + NAD(+) = 3- CC oxo-delta(5)-steroid + NADH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-delta(5)-steroid = a 3-oxo-delta(4)- CC steroid. CC -!- PATHWAY: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum and mitochondrial CC membrane-bound protein. CC -!- SIMILARITY: Belongs to the 3beta-HSD family. DR EMBL; X17614; CAA35615.1; -. DR PIR; S07102; DEBOHS. DR InterPro; IPR002225; 3Beta_HSD. DR Pfam; PF01073; 3Beta_HSD; 1. KW Steroidogenesis; Oxidoreductase; NAD; Isomerase; Mitochondrion; KW Multifunctional enzyme; Transmembrane; Endoplasmic reticulum; KW Direct protein sequencing. FT INIT_MET 0 0 FT TRANSMEM 74 91 0 (Potential). FT TRANSMEM 287 305 Potential. FT NP_BIND 5 36 NAD (Potential). FT CONFLICT 141 219 AKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVE FT IQPRANIQLDFPELKPYKQVKQIAPAELEGLLDLERVI -> FT CLNCVKSWLKLLKLERQFPSKLLWSIRLSMAIALMLHMLKS FT KFNQELTFNWTSQNRNHTNRLNKLLPLSLRVCWIWKELF FT (in Ref. 1). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 372 AA; 42088 MW; 5B8481DEEA5807BC CRC64; AGWSCLVTGG GGFLGQRIIC LLVEEKDLQE IRVLDKVFRP EVREEFSKLQ SKIKLTLLEG DILDEQCLKG ACQGTSVVIH TASVIDVRNA VPRETIMNVN VKGTQLLLEA CVQASVPVFI HTSTIEVAGP NSYREIIQDG REEEHHESAW SSPYPYSKKL AEKAVLGANG WALKNGGTLY TCALRPMYIY GEGSPFLSAY MHGALNNNGI LTNHCKFSRV NPVYVGNVAW AHILALRALR DPKKVPNIQG QFYYISDDTP HQSYDDLNYT LSKEWGFCLD SRMSLPISLQ YWLAFLLEIV SFLLSPIYKY NPCFNRHLVT LSNSVFTFSY KKAQRDLGYE PLYTWEEAKQ KTKEWIGSLV KQHKETLKTK IH // ID CBP1_HORVU STANDARD; PRT; 499 AA. AC P07519; P07520; DT 01-APR-1988 (Rel. 07, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Serine carboxypeptidase I precursor (EC 3.4.16.5) (Carboxypeptidase C) DE (CP-MI). GN Name=CBP1; Synonyms=CXP;1; OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; Pooideae; OC Triticeae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Aleurone; RA Rocher A., Lok F., Cameron-Mills V., von Wettstein D.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 88-499 FROM N.A. RX MEDLINE=88298749; PubMed=3403516; RA Doan N.P., Fincher G.B.; RT "The A- and B-chains of carboxypeptidase I from germinated barley RT originate from a single precursor polypeptide."; RL J. Biol. Chem. 263:11106-11110(1988). RN [3] RP SEQUENCE OF 31-296 AND 352-499. ** MEDLINE=None; PubMed=None; RA Soerensen S.B., Breddam K., Svendsen I.; RT "Primary structure of carboxypeptidase I from malted barley."; RL Carlsberg Res. Commun. 51:475-485(1986). CC -!- FUNCTION: May be involved in the degradation of small peptides (2- CC 5 residues) or in the degradation of storage proteins in the CC embryo. CC -!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with a CC broad specificity. CC -!- SUBUNIT: Carboxypeptidase I is a dimer, where each monomer is CC composed of two chains linked by disulfide bonds. CC -!- SUBCELLULAR LOCATION: Secreted into the endosperm. CC -!- DEVELOPMENTAL STAGE: After one day of germination, mainly found in CC the scutellum of the developing grain; barely detectable after CC four days, and absent from the mature grain. A lower level of CC expression is seen in the aleurone both during development and CC germination. CC -!- PTM: Three disulfide bonds are present. CC -!- PTM: The linker peptide is endoproteolytically excised during CC enzyme maturation. CC -!- SIMILARITY: Belongs to peptidase family S10. DR EMBL; Y09603; CAA70816.1; -. DR EMBL; J03897; AAA32940.1; -. DR PIR; T05367; CPBHS. DR MEROPS; S10.004; -. DR InterPro; IPR001563; Peptidase_S10. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR ProDom; PD001189; Serine_carbpept; 2. DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. DR HSSP; P08819; 1WHT. KW Hydrolase; Carboxypeptidase; Glycoprotein; Zymogen; Signal; KW Direct protein sequencing. FT SIGNAL 1 30 Potential. FT CHAIN 31 296 Serine carboxypeptidase I chain A. FT PROPEP 297 351 Linker peptide. FT CHAIN 352 499 Serine carboxypeptidase I chain B. FT ACT_SITE 188 188 By similarity. FT ACT_SITE 423 423 By similarity. FT ACT_SITE 476 476 By similarity. FT SITE 497 499 Microbody targeting signal (Potential). FT CARBOHYD 148 148 N-linked (GlcNAc...). FT CARBOHYD 262 262 N-linked (GlcNAc...). FT CARBOHYD 407 407 N-linked (GlcNAc...). FT CONFLICT 102 102 H -> P (in Ref. 3). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 499 AA; 54096 MW; 9C6674B14D9DB9BF CRC64; MARCRRRSGC TAGAALLLLL ALALSGGGGA APQGAEVTGL PGFDGALPSK HYAGYVTVDE GHGRNLFYYV VESERDPGKD PVVLWLNGGP GCSSFDGFVY EHGPFNFESG GSVKSLPKLH LNPYAWSKVS TMIYLDSPAG VGLSYSKNVS DYETGDLKTA TDSHTFLLKW FQLYPEFLSN PFYIAGESYA GVYVPTLSHE VVKGIQGGAK PTINFKGYMV GNGVCDTIFD GNALVPFAHG MGLISDEIYQ QASTSCHGNY WNATDGKCDT AISKIESLIS GLNIYDILEP CYHSRSIKEV NLQNSKLPQS FKDLGTTNKP FPVRTRMLGR AWPLRAPVKA GRVPSWQEVA SGVPCMSDEV ATAWLDNAAV RSAIHAQSVS AIGPWLLCTD KLYFVHDAGS MIAYHKNLTS QGYRAIIFSG DHDMCVPFTG SEAWTKSLGY GVVDSWRPWI TNGQVSGYTE GYEHGLTFAT IKGAGHTVPE YKPQEAFAFY SRWLAGSKL // ID YCXD_CYAPA STANDARD; PRT; 244 AA. AC P48334; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Probable ABC transporter ATP-binding protein in ycf23-apcF intergenic DE region (ORF244). OS Cyanophora paradoxa. OG Cyanelle. OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora. OX NCBI_TaxID=2762; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=UTEX LB 555 / Pringsheim; ** MEDLINE=None; PubMed=None; RA Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J., RA Bryant D.A.; RT "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa."; RL Plant Mol. Biol. Rep. 13:327-332(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=UTEX LB 555 / Pringsheim; RA Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M., RA Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., RA Steiner J.M., Jakowitsch J., Bohnert H.J., Bryant D.A.; RT "The complete sequence of the cyanelle genome of Cyanophora paradoxa: RT the genetic complexity of a primitive plastid."; RL (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., RL Schwemmler W. (eds.); RL Eukaryotism and Symbiosis, pp.40-48, Springer-Verlag, Heidelberg RL (1997). CC -!- SUBCELLULAR LOCATION: Cyanelle. CC -!- SIMILARITY: Belongs to the ABC transporter family. DR EMBL; U30821; AAA81304.1; -. DR PIR; T06961; T06961. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transporter. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR HSSP; P58301; 1F2T. KW Hypothetical protein; ATP-binding; Transport; Cyanelle. FT NP_BIND 41 48 ATP (Potential). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 244 AA; 27747 MW; 4C5B357FF9C55D3B CRC64; MFYTLPKQLE INNLTVSYPH GTVLQNIFLT IESGKLIGII GPNGAGKSTL LKTIIEQIKP ISGEIFYQGA PLKNQRARIG YVPQRAQVDW DFPINVWDVV MMARLKKIGW FSSYSKKSYE CVKAALEKVD MLKYKDRNIR ELSGGQQQRV FLARLLAQEA DLLLLDEPFT GVDFQTQKII FSLLKEQIAS NKIVIVIHHD LGESIINFDE LILLNKKIIS HDLTTKILNS KKLSTLFGEH IYAN // ID CYC_ARUMA STANDARD; PRT; 111 AA. AC P00065; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Cytochrome c. OS Arum maculatum (Cuckoo-pint). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Araceae; Arum. OX NCBI_TaxID=4458; RN [1] RP SEQUENCE. RA Boulter D.; ** /NO TITLE. RL Unpublished results, cited by: RL Dickerson R.E., Timkovich R.; RL (In) Boyer P.D. (eds.); RL The enzymes (3rd ed.), pp.11:397-547, Academic Press, New York (1975). CC -!- FUNCTION: Electron carrier protein. The oxidized form of the CC cytochrome c heme group can accept an electron from the heme group CC of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c CC then transfers this electron to the cytochrome oxidase complex, CC the final protein carrier in the mitochondrial electron-transport CC chain. CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix. CC -!- PTM: Binds 1 heme group per subunit. CC -!- SIMILARITY: Belongs to the cytochrome c family. DR PIR; A00057; CCRM. DR InterPro; IPR003088; Cyt_CI. DR InterPro; IPR002327; Cyt_CIAB. DR InterPro; IPR000345; CytC_heme_BS. DR InterPro; IPR009056; Cytochrome_c. DR Pfam; PF00034; Cytochrom_C; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR ProDom; PD000375; Cyt_CIAB; 1. DR PROSITE; PS00190; CYTOCHROME_C; 1. DR HSSP; P00055; 1CCR. KW Mitochondrion; Electron transport; Respiratory chain; Heme; KW Acetylation; Direct protein sequencing. FT METAL 26 26 Iron (heme axial ligand). FT METAL 88 88 Iron (heme axial ligand). FT BINDING 22 22 Heme (covalent). FT BINDING 25 25 Heme (covalent). FT MOD_RES 1 1 N-acetylalanine. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 111 AA; 12005 MW; 6F7C201451D52E47 CRC64; ASFAEAPPGN PKAGEKIFKT KCAQCHTVEK GAGHKQGPNL NGLFGRQSGT TAGYSYSAAN KNMAVIWEES TLYDYLLNPX KYIPGTKMVF PGLXKPQERA DLIAYLKEST A // ID TAP2_HUMAN STANDARD; PRT; 686 AA. AC Q03519; Q9UQ83; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Antigen peptide transporter 2 (APT2) (Peptide transporter TAP2) DE (Peptide transporter PSF2) (Peptide supply factor 2) (PSF-2) (Peptide DE transporter involved in antigen processing 2). GN Name=TAP2; Synonyms=ABCB3, PSF2, RING11, Y1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (TAP2*0101). RX MEDLINE=93085727; PubMed=1453454; RA Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., RA Trowsdale J.; RT "DNA sequence analysis of 66 kb of the human MHC class II region RT encoding a cluster of genes for antigen processing."; RL J. Mol. Biol. 228:433-441(1992). RN [2] RP SEQUENCE FROM N.A. (TAP2*0101/TAP2*0201). RX MEDLINE=92159069; PubMed=1741401; RA Powis S.H., Mockridge I., Kelly A., Kerr L.-A., Glynne R.J., RA Gileadi U., Beck S., Trowsdale J.; RT "Polymorphism in a second ABC transporter gene located within the RT class II region of the human major histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 89:1463-1467(1992). RN [3] RP SEQUENCE FROM N.A. (TAP2*0201). RX MEDLINE=92052217; PubMed=1946428; RA Bahram S., Arnold D., Bresnahan M., Strominger J.L., Spies T.; RT "Two putative subunits of a peptide pump encoded in the human major RT histocompatibility complex class II region."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10094-10098(1991). RN [4] RP SEQUENCE FROM N.A. (TAP2*0102). RX MEDLINE=93154779; PubMed=8428770; RA Powis S.H., Tonks S., Mockridge I., Kelly A.P., Bodmer J.G., RA Trowsdale J.; RT "Alleles and haplotypes of the MHC-encoded ABC transporters TAP1 and RT TAP2."; RL Immunogenetics 37:373-380(1993). RN [5] RP SEQUENCE FROM N.A. (TAP2*0101). RX MEDLINE=96144827; PubMed=8568858; RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., RA Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., RA Radley E., Thorpe K.L., Trowsdale J.; RT "Evolutionary dynamics of non-coding sequences within the class II RT region of the human MHC."; RL J. Mol. Biol. 255:1-13(1996). RN [6] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [7] RP SEQUENCE OF 65-686 FROM N.A. (TAP2*0103). RC TISSUE=Blood; RX MEDLINE=95313033; PubMed=7792761; RA Cano P., Baxter-Lowe L.A.; RT "Novel human TAP2*103 allele shows further polymorphism in the ATP- RT binding domain."; RL Tissue Antigens 45:139-142(1995). RN [8] RP SEQUENCE OF 204-686 FROM N.A., AND VARIANTS THR-374 AND ILE-467. RA Tang J., Allen S., Karita E., Musonda R., Kaslow R.A.; RT "New TAP2 polymorphisms in Africans."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP SEQUENCE OF 517-645 FROM N.A. (TAP2*0101/TAP2*0102). RA Singal D.P., Ye M., D'Souza M.; RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases. RN [10] RP SEQUENCE OF 517-645 FROM N.A. (TAP2*0101/TAP2*0102). RX MEDLINE=94215245; PubMed=8162639; RA Singal D.P., Ye M., Qiu X., D'Souza M.; RT "Polymorphisms in the TAP2 gene and their association with rheumatoid RT arthritis."; RL Clin. Exp. Rheumatol. 12:29-33(1994). RN [11] RP PEPTIDE-BINDING SITE. RX PubMed=8955196; RA Nijenhuis M., Hammerling G.J.; RT "Multiple regions of the transporter associated with antigen RT processing (TAP) contribute to its peptide binding site."; RL J. Immunol. 157:5467-5477(1996). RN [12] RP INHIBITION BY ICP47. RX PubMed=8670825; RA Ahn K., Meyer T.H., Uebel S., Sempe P., Djaballah H., Yang Y., RA Peterson P.A., Frueh K., Tampe R.; RT "Molecular mechanism and species specificity of TAP inhibition by RT herpes simplex virus ICP47."; RL EMBO J. 15:3247-3255(1996). RN [13] RP INHIBITION BY US6 GLYCOPROTEIN. RX PubMed=9175839; RA Ahn K., Gruhler A., Galocha B., Jones T.R., Wiertz E.J.H.J., RA Ploegh H.L., Peterson P.A., Yang Y., Frueh K.; RT "The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide RT translocation by TAP."; RL Immunity 6:613-621(1997). RN [14] RP INHIBITION BY US6 GLYCOPROTEIN. RX PubMed=11157746; RA Hewitt E.W., Gupta S.S., Lehner P.J.; RT "The human cytomegalovirus gene product US6 inhibits ATP binding by RT TAP."; RL EMBO J. 20:387-396(2001). RN [15] RP INHIBITION BY E3-19K GLYCOPROTEIN. RX PubMed=10227971; RA Bennett E.M., Bennink J.R., Yewdell J.W., Brodsky F.M.; RT "Cutting edge: adenovirus E19 has two mechanisms for affecting class I RT MHC expression."; RL J. Immunol. 162:5049-5052(1999). RN [16] RP VARIANTS ILE-379 AND ALA-665. RX MEDLINE=92237283; PubMed=1570316; RA Colonna M., Bresnahan M., Bahram S., Strominger J.L., Spies T.; RT "Allelic variants of the human putative peptide transporter involved RT in antigen processing."; RL Proc. Natl. Acad. Sci. U.S.A. 89:3932-3936(1992). RN [17] RP VARIANT TAP2*BKY2 VAL-577. RX MEDLINE=97464203; PubMed=9324024; RA Kumagai S., Kanagawa S., Morinobu A., Takada M., Nakamura K., RA Sugai S., Maruya E., Saji H.; RT "Association of a new allele of the TAP2 gene, TAP2*Bky2 (Val577), RT with susceptibility to Sjogren's syndrome."; RL Arthritis Rheum. 40:1685-1692(1997). RN [18] RP VARIANTS THR-374; ILE-379; ILE-467; SER-513 THR-565; CYS-651; ALA-665 RP AND GLN-GLU-GLY-GLN-ASP-LEU-TYR-SER-ARG-LEU-VAL-GLN-GLN-ARG-LEU-MET- RP ASP-686 INS, AND DEFINITION OF ALLELES. RX MEDLINE=21190086; PubMed=11294565; DOI=10.1038/sj/gene/6363731; RA Tang J., Freedman D.O., Allen S., Karita E., Musonda R., Braga C., RA Jamieson B.D., Louie L., Kaslow R.A.; RT "Genotyping TAP2 variants in North American Caucasians, Brazilians, RT and Africans."; RL Genes Immun. 2:32-40(2001). CC -!- FUNCTION: Involved in the transport of antigens from the cytoplasm CC to the endoplasmic reticulum for association with MHC class I CC molecules. Also acts as a molecular scaffold for the final stage CC of MHC class I folding, namely the binding of peptide. Nascent MHC CC class I molecules associate with TAP via tapasin. Inhibited by the CC covalent attachment of herpes simplex virus ICP47 protein, which CC blocks the peptide-binding site of TAP. Inhibited by human CC cytomegalovirus US6 glycoprotein, which binds to the lumenal side CC of the TAP complex and inhibits peptide translocation by CC specifically blocking ATP-binding to TAP1 and prevents the CC conformational rearrangement of TAP induced by peptide binding. CC Inhibited by human adenovirus E3-19K glycoprotein, which binds the CC TAP complex and acts as a tapasin inhibitor, preventing MHC class CC I/TAP association. CC -!- SUBUNIT: Heterodimer of TAP1 and TAP2. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Endoplasmic CC reticulum. The transmembrane segments seem to form a pore in the CC membrane. CC -!- INDUCTION: By interferon gamma. CC -!- DOMAIN: The peptide-binding site is shared between the cytoplasmic CC loops of TAP1 and TAP2. CC -!- POLYMORPHISM: 4 common alleles are officially recognized: CC TAP2*0101 (TAP2A or PSF2A or RING11A), TAP2*0102 (TAP2E), CC TAP2*0103 (TAP2F), and TAP2*0201 (TAP2B or PSF2B or RING11B). CC Other relatively common alleles have been identified: TAP2*01D, CC TAP2*01E, TAP2*01F, TAP2*01G, TAP2*01H, TAP2*02B, TAP2*02C CC (TAP2*0202), TAP2*02D, TAP2*02E, TAP2*02F, TAP2*03A and TAP2*04A. CC The sequence shown is that of TAP2*0101. CC -!- POLYMORPHISM: The allele TAP2*Bky2 is commonly found only in the CC Japanese population. It may be associated with susceptibility to CC Sjoegren's syndrome, an autoimmune disorder characterized by CC abnormal dryness of the conjunctiva, cornea and mouth due to CC exocrine glands dysfunction. CC -!- SIMILARITY: Belongs to the ABC transporter family. MDR subfamily. DR EMBL; X66401; CAA47027.1; -. DR EMBL; M84748; -; NOT_ANNOTATED_CDS. DR EMBL; M74447; AAA59841.1; -. DR EMBL; Z22935; CAA80522.1; -. DR EMBL; Z22936; CAA80523.1; -. DR EMBL; X87344; CAA60788.1; -. DR EMBL; U07844; AAA79901.1; -. DR EMBL; BC002751; AAH02751.1; -. DR EMBL; AF100418; AAD23381.1; -. DR EMBL; AF100415; AAD23381.1; JOINED. DR EMBL; AF100416; AAD23381.1; JOINED. DR EMBL; AF100417; AAD23381.1; JOINED. DR EMBL; L09191; AAA58648.1; -. DR EMBL; L10287; AAA58649.1; -. DR PIR; B41538; B41538. DR HGNC; HGNC:44; TAP2. DR MIM; 170261; -. DR GO; GO:0005829; C:cytosol; NAS. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IMP. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0042825; C:TAP complex; NAS. DR GO; GO:0005524; F:ATP binding; NAS. DR GO; GO:0004409; F:homoaconitate hydratase activity; NAS. DR GO; GO:0042288; F:MHC class I protein binding; NAS. DR GO; GO:0042605; F:peptide antigen binding; NAS. DR GO; GO:0015433; F:peptide antigen transporter activity; NAS. DR GO; GO:0042301; F:phosphate binding; NAS. DR GO; GO:0046982; F:protein heterodimerization activity; IPI. DR GO; GO:0046980; F:tapasin binding; IPI. DR GO; GO:0048004; P:antigen presentation, endogenous peptide an...; NAS. DR GO; GO:0019885; P:antigen processing, endogenous antigen via ...; NAS. DR GO; GO:0046967; P:cytosol to ER transport; NAS. DR GO; GO:0006886; P:intracellular protein transport; IMP. DR GO; GO:0015833; P:peptide transport; NAS. DR GO; GO:0006461; P:protein complex assembly; NAS. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR001140; ABC_TM_transpt. DR InterPro; IPR003439; ABC_transporter. DR InterPro; IPR005293; Ag_transporter2. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR00958; 3a01208; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR HSSP; Q03518; 1JJ7. KW Immune response; Transport; Peptide transport; Endoplasmic reticulum; KW ATP-binding; Transmembrane; Polymorphism. FT TOPO_DOM 1 6 Lumenal (Potential). FT TRANSMEM 7 27 1 (Potential). FT TOPO_DOM 28 56 Cytoplasmic (Potential). FT TRANSMEM 57 77 2 (Potential). FT TOPO_DOM 78 98 Lumenal (Potential). FT TRANSMEM 99 119 3 (Potential). FT TOPO_DOM 120 148 Cytoplasmic (Potential). FT TRANSMEM 149 169 4 (Potential). FT TOPO_DOM 170 187 Lumenal (Potential). FT TRANSMEM 188 208 5 (Potential). FT TOPO_DOM 209 266 Cytoplasmic (Potential). FT TRANSMEM 267 287 6 (Potential). FT TOPO_DOM 288 293 Lumenal (Potential). FT TRANSMEM 294 314 7 (Potential). FT TOPO_DOM 315 374 Cytoplasmic (Potential). FT TRANSMEM 375 395 8 (Potential). FT TOPO_DOM 396 408 Lumenal (Potential). FT TRANSMEM 409 429 9 (Potential). FT TOPO_DOM 430 686 Cytoplasmic (Potential). FT NP_BIND 503 510 ATP (Potential). FT REGION 301 389 Involved in peptide-binding site. FT REGION 414 433 Involved in peptide-binding site. FT REGION 468 686 ABC transporter. FT VARIANT 374 374 A -> T (in allele TAP2*01F, allele FT TAP2*01G, allele TAP2*01H, allele FT TAP2*02B and allele TAP2*02D). FT /FTId=VAR_014997. FT VARIANT 379 379 V -> I (in allele TAP2*01D, allele FT TAP2*01E, allele TAP2*01G, allele FT TAP2*02C and allele TAP2*02F; FT dbSNP:1800454). FT /FTId=VAR_000094. FT VARIANT 467 467 V -> I (in allele TAP2*01F and allele FT TAP2*02D). FT /FTId=VAR_014998. FT VARIANT 513 513 A -> S (rare polymorphism). FT /FTId=VAR_014999. FT VARIANT 565 565 A -> T (in allele TAP2*0102, allele FT TAP2*01D, allele TAP2*02E and allele FT TAP2*02F). FT /FTId=VAR_000095. FT VARIANT 577 577 M -> V (in allele TAP2*BKY2). FT /FTId=VAR_015000. FT VARIANT 651 651 R -> C (in allele TAP2*0103 and allele FT TAP2*01G). FT /FTId=VAR_000096. FT VARIANT 665 665 T -> A (in allele TAP2*0201, allele FT TAP2*02B, allele TAP2*02C, allele FT TAP2*02D, allele TAP2*02E, allele FT TAP2*02F, allele TAP2*04A and allele FT TAP2*Bky2; dbSNP:241447). FT /FTId=VAR_000097. FT VARIANT 686 686 L -> LQEGQDLYSRLVQQRLMD (in allele FT TAP2*0201, allele TAP2*02B, allele FT TAP2*02C, allele TAP2*02D, allele FT TAP2*02E, allele TAP2*02F, allele FT TAP2*03A and allele TAP2*Bky2). FT /FTId=VAR_000098. ** ** ################# INTERNAL SECTION ################## **CL 6p21.3; **ZB CHH, 8-JAN-2004; SQ SEQUENCE 686 AA; 75664 MW; E7E4A7F6A2A3B48B CRC64; MRLPDLRPWT SLLLVDAALL WLLQGPLGTL LPQGLPGLWL EGTLRLGGLW GLLKLRGLLG FVGTLLLPLC LATPLTVSLR ALVAGASRAP PARVASAPWS WLLVGYGAAG LSWSLWAVLS PPGAQEKEQD QVNNKVLMWR LLKLSRPDLP LLVAAFFFLV LAVLGETLIP HYSGRVIDIL GGDFDPHAFA SAIFFMCLFS FGSSLSAGCR GGCFTYTMSR INLRIREQLF SSLLRQDLGF FQETKTGELN SRLSSDTTLM SNWLPLNANV LLRSLVKVVG LYGFMLSISP RLTLLSLLHM PFTIAAEKVY NTRHQEVLRE IQDAVARAGQ VVREAVGGLQ TVRSFGAEEH EVCRYKEALE QCRQLYWRRD LERALYLLVR RVLHLGVQML MLSCGLQQMQ DGELTQGSLL SFMIYQESVG SYVQTLVYIY GDMLSNVGAA EKVFSYMDRQ PNLPSPGTLA PTTLQGVVKF QDVSFAYPNR PDRPVLKGLT FTLRPGEVTA LVGPNGSGKS TVAALLQNLY QPTGGQVLLD EKPISQYEHC YLHSQVVSVG QEPVLFSGSV RNNIAYGLQS CEDDKVMAAA QAAHADDFIQ EMEHGIYTDV GEKGSQLAAG QKQRLAIARA LVRDPRVLIL DEATSALDVQ CEQALQDWNS RGDRTVLVIA HRLQTVQRAH QILVLQEGKL QKLAQL // ID CIN5_HUMAN STANDARD; PRT; 2016 AA. AC Q14524; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Sodium channel protein type V alpha subunit (Voltage-gated sodium DE channel alpha subunit Nav1.5) (Sodium channel protein, cardiac muscle DE alpha-subunit) (HH1). GN Name=SCN5A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Heart; RX MEDLINE=92115699; PubMed=1309946; RA Gellens M.E., George A.L. Jr., Chen L.Q., Chahine M., Horn R., RA Barchi R.L., Kallen R.G.; RT "Primary structure and functional expression of the human cardiac RT tetrodotoxin-insensitive voltage-dependent sodium channel."; RL Proc. Natl. Acad. Sci. U.S.A. 89:554-558(1992). RN [2] RP VARIANTS LQT3. RX MEDLINE=95196273; PubMed=7889574; RA Wang Q., Shen J., Splawski I., Atkinson D., Li Z., Robinson J.L., RA Moss A.J., Towbin J.A., Keating M.T.; RT "SCN5A mutations associated with an inherited cardiac arrhythmia, long RT QT syndrome."; RL Cell 80:805-811(1995). RN [3] RP VARIANTS LQT3. RX MEDLINE=96081224; PubMed=8541846; RA Wang Q., Shen J., Li Z., Timothy K.W., Vincent G.M., Priori S.G., RA Schwartz P.J., Keating M.T.; RT "Cardiac sodium channel mutations in patients with long QT syndrome, RT an inherited cardiac arrhythmia."; RL Hum. Mol. Genet. 4:1603-1607(1995). RN [4] RP VARIANT LQT3 1505-LYS--GLN-1507 DEL. RX MEDLINE=95379949; PubMed=7651517; RA Bennett P.B., Yazawa K., Makita N., George A.L. Jr.; RT "Molecular mechanism for an inherited cardiac arrhythmia."; RL Nature 376:683-685(1995). RN [5] RP VARIANT LQT3 GLY-1790. RX MEDLINE=98349542; PubMed=9686753; RA An R.H., Wang X.L., Kerem B., Benhorin J., Medina A., Goldmit M., RA Kass R.S.; RT "Novel LQT-3 mutation affects Na+ channel activity through RT interactions between alpha- and beta1-subunits."; RL Circ. Res. 83:141-146(1998). RN [6] RP VARIANT LQT3 GLN-1623. RX MEDLINE=98165676; PubMed=9506831; RA Makita N., Shirai N., Nagashima M., Matsuoka R., Yamada Y., Tohse N., RA Kitabatake A.; RT "A de novo missense mutation of human cardiac Na(+) channel exhibiting RT novel molecular mechanisms of long QT syndrome."; RL FEBS Lett. 423:5-9(1998). RN [7] RP VARIANT LQT3 GLY-1839. ** MEDLINE=None; PubMed=None; RA Benhorin J., Goldmit M., Maccluer J.W., Blangero J., Goffen R., RA Leibovitch A., Rahat A., Wang Q., Medina A., Towbin J.A., Kerem B.; RT "Identification of a new SCN5A mutation, D1840G, associated with the RT long QT syndrome."; RL Hum. Mutat. 12:72-72(1998). RN [8] RP VARIANT LQT3 GLN-1623. ** MEDLINE=None; PubMed=None; RA Yamagishi H., Furutani M., Kamisago M., Morikawa Y., Kojima Y., RA Hino Y., Furutani Y., Kimura M., Imamura S.-I., Takao A., Momma K., RA Matsuoka R.; RT "A De Novo missense mutation (R1623Q) of the SCN5A gene in a Japanese RT girl with sporadic long QT syndrome."; RL Hum. Mutat. 12:481-481(1998). RN [9] RP VARIANTS BRUGADA SYNDROME TRP-1232 AND MET-1620. RX PubMed=9521325; DOI=10.1038/32675; RA Chen Q., Kirsch G.E., Zhang D., Brugada R., Brugada J., Brugada P., RA Potenza D., Moya A., Borggrefe M., Breithardt G., Ortiz-Lopez R., RA Wang Z., Antzelevitch C., O'Brien R.E., Schulze-Bahr E., Keating M.T., RA Towbin J.A., Wang Q.; RT "Genetic basis and molecular mechanism for idiopathic ventricular RT fibrillation."; RL Nature 392:293-296(1998). RN [10] RP VARIANTS LQT3 MET-1304 AND MET-1645, AND VARIANT ASN-1500. RX MEDLINE=99439526; PubMed=10508990; RA Wattanasirichaigoon D., Vesely M.R., Duggal P., Levine J.C., RA Blume E.D., Wolff G.S., Edwards S.B., Beggs A.H.; RT "Sodium channel abnormalities are infrequent in patients with long QT RT syndrome: identification of two novel SCN5A mutations."; RL Am. J. Med. Genet. 86:470-476(1999). RN [11] RP CHARATERIZATION OF VARIANTS BRUGADA SYNDROME TRP-1512 AND THR-1924. RX PubMed=10690282; RA Rook M.B., Bezzina Alshinawi C., Groenewegen W.A., van Gelder I.C., RA van Ginneken A.C.G., Jongsma H.J., Mannens M.M.A.M., Wilde A.A.M.; RT "Human SCN5A gene mutations alter cardiac sodium channel kinetics and RT are associated with the Brugada syndrome."; RL Cardiovasc. Res. 44:507-517(1999). RN [12] RP VARIANT LQT3 LYS-1784. RX MEDLINE=99307063; PubMed=10377081; RA Wei J., Wang D.W., Alings M., Fish F., Wathen M., Roden D.M., RA George A.L. Jr.; RT "Congenital long-QT syndrome caused by a novel mutation in a conserved RT acidic domain of the cardiac Na+ channel."; RL Circulation 99:3165-3171(1999). RN [13] RP CHARACTERIZATION OF VARIANT BRUGADA SYNDROME MET-1620. RX PubMed=10532948; RA Dumaine R., Towbin J.A., Brugada P., Vatta M., Nesterenko D.V., RA Nesterenko V.V., Brugada J., Brugada R., Antzelevitch C.; RT "Ionic mechanisms responsible for the electrocardiographic phenotype RT of the Brugada syndrome are temperature dependent."; RL Circ. Res. 85:803-809(1999). RN [14] RP CHARACTERIZATION OF VARIANT LQT3/BRUGADA SYNDROME ASP-1795 INS. RX PubMed=10590249; RA Bezzina C.R., Veldkamp M.W., van Den Berg M.P., Postma A.V., RA Rook M.B., Viersma J.-W., van Langen I.M., Tan-Sindhunata G., RA Bink-Boelkens M.T.E., van Der Hout A.H., Mannens M.M.A.M., RA Wilde A.A.M.; RT "A single Na(+) channel mutation causing both long-QT and Brugada RT syndromes."; RL Circ. Res. 85:1206-1213(1999). RN [15] RP DISEASE. RX PubMed=10471492; DOI=10.1038/12618; RA Schott J.-J., Alshinawi C., Kyndt F., Probst V., Hoorntje T.M., RA Hulsbeek M., Wilde A.A.M., Escande D., Mannens M.M.A.M., Le Marec H.; RT "Cardiac conduction defects associate with mutations in SCN5A."; RL Nat. Genet. 23:20-21(1999). RN [16] RP CHARACTERIZATION OF VARIANT BRUGADA SYNDROME MET-1620. RX PubMed=10618304; RA Makita N., Shirai N., Wang D.W., Sasaki K., George A.L. Jr., Kanno M., RA Kitabatake A.; RT "Cardiac Na(+) channel dysfunction in Brugada syndrome is aggravated RT by beta(1)-subunit."; RL Circulation 101:54-60(2000). RN [17] RP VARIANTS LQT3 ASN-1114; VAL-1501; LEU-1623; HIS-1644 AND ASN-1787. RX MEDLINE=20432616; PubMed=10973849; RA Splawski I., Shen J., Timothy K.W., Lehmann M.H., Priori S., RA Robinson J.L., Moss A.J., Schwartz P.J., Towbin J.A., Vincent G.M., RA Keating M.T.; RT "Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, RT KCNE1, and KCNE2."; RL Circulation 102:1178-1185(2000). RN [18] RP VARIANT IVF LEU-1710. RX PubMed=10940383; RA Akai J., Makita N., Sakurada H., Shirai N., Ueda K., Kitabatake A., RA Nakazawa K., Kimura A., Hiraoka M.; RT "A novel SCN5A mutation associated with idiopathic ventricular RT fibrillation without typical ECG findings of Brugada syndrome."; RL FEBS Lett. 479:29-34(2000). RN [19] RP VARIANT LQT3 ASN-941. RX PubMed=10911008; RA Schwartz P.J., Priori S.G., Dumaine R., Napolitano C., RA Antzelevitch C., Stramba-Badiale M., Richard T.A., Berti M.R., RA Bloise R.; RT "A molecular link between the sudden infant death syndrome and the RT long-QT syndrome."; RL N. Engl. J. Med. 343:262-267(2000). RN [20] RP CHARACTERIZATION OF VARIANTS LQT3 CYS-1795 AND BRUGADA SYNDROME RP HIS-1795. RX PubMed=11410597; DOI=10.1074/jbc.M104471200; RA Rivolta I., Abriel H., Tateyama M., Liu H., Memmi M., Vardas P., RA Napolitano C., Priori S.G., Kass R.S.; RT "Inherited Brugada and long QT-3 syndrome mutations of a single RT residue of the cardiac sodium channel confer distinct channel and RT clinical phenotypes."; RL J. Biol. Chem. 276:30623-30630(2001). RN [21] RP VARIANT SSS1/BRUGADA SYNDROME ARG-1408. RX PubMed=11748104; RA Kyndt F., Probst V., Potet F., Demolombe S., Chevallier J.-C., RA Baro I., Moisan J.-P., Boisseau P., Schott J.-J., Escande D., RA Le Marec H.; RT "Novel SCN5A mutation leading either to isolated cardiac conduction RT defect or Brugada syndrome in a large French family."; RL Circulation 104:3081-3086(2001). RN [22] RP CHARACTERIZATION OF VARIANTS LQT3 SER-997 AND HIS-1826. RX PubMed=11710892; RA Ackerman M.J., Siu B.L., Sturner W.Q., Tester D.J., Valdivia C.R., RA Makielski J.C., Towbin J.A.; RT "Postmortem molecular analysis of SCN5A defects in sudden infant death RT syndrome."; RL JAMA 286:2264-2269(2001). RN [23] RP CHARACTERIZATION OF VARIANT CARDIAC CONDUCTION DEFECT CYS-514. RX PubMed=11234013; DOI=10.1038/35059090; RA Tan H.L., Bink-Boelkens M.T.E., Bezzina C.R., Viswanathan P.C., RA Beaufort-Krol G.C.M., van Tintelen P.J., van den Berg M.P., RA Wilde A.A.M., Balser J.R.; RT "A sodium-channel mutation causes isolated cardiac conduction RT disease."; RL Nature 409:1043-1047(2001). RN [24] RP CHARATCTERIZATION OF VARIANTS PROGRESSIVE FAMILIAL HEART BLOCK TYPE I RP SER-298 AND ASN-1595. RX PubMed=11804990; RA Wang D.W., Viswanathan P.C., Balser J.R., George A.L. Jr., RA Benson D.W.; RT "Clinical, genetic and biophysical characterisation of SCN5A mutations RT associated with atrioventricular block."; RL Circulation 105:341-346(2002). RN [25] RP VIRTUAL MODELING OF VARIANT LQT3/BRUGADA SYNDROME ASP-1795 INS. RX PubMed=11889015; RA Clancy C.E., Rudy Y.; RT "Na(+) channel mutation that causes both Brugada and long-QT syndrome RT phenotypes: a simulation study of mechanism."; RL Circulation 105:1208-1213(2002). RN [26] RP CHARACTERIZATION OF VARIANTS BRUGADA SYNDROME HIS-367; VAL-735 AND RP GLN-1193. RX PubMed=11823453; RA Vatta M., Dumaine R., Varghese G., Richard T.A., Shimizu W., RA Aihara N., Nademanee K., Brugada R., Brugada J., Veerakul G., Li H., RA Bowles N.E., Brugada P., Antzelevitch C., Towbin J.A.; RT "Genetic and biophysical basis of sudden unexplained nocturnal death RT syndrome (SUNDS), a disease allelic to Brugada syndrome."; RL Hum. Mol. Genet. 11:337-345(2002). RN [27] RP VARIANT ACQUIRED ARRHYTHMIA TYR-1103. RX PubMed=12471205; RA Chen S., Chung M.K., Martin D., Rozich R., Tchou P.J., Wang Q.; RT "SNP S1103Y in the cardiac sodium channel gene SCN5A is associated RT with cardiac arrhythmias and sudden death in a white family."; RL J. Med. Genet. 39:913-915(2002). RN [28] RP VARIANT ACQUIRED ARRHYTHMIA TYR-1103. RX PubMed=12193783; DOI=10.1126/science.1073569; RA Splawski I., Timothy K.W., Tateyama M., Clancy C.E., Malhotra A., RA Beggs A.H., Cappuccio F.P., Sagnella G.A., Kass R.S., Keating M.T.; RT "Variant of SCN5A sodium channel implicated in risk of cardiac RT arrhythmia."; RL Science 297:1333-1336(2002). RN [29] RP VARIANT LQT3 PHE-619. RX MEDLINE=22560398; PubMed=12673799; DOI=10.1002/humu.9136; RA Wehrens X.H., Rossenbacker T., Jongbloed R.J., Gewillig M., RA Heidbuchel H., Doevendans P.A., Vos M.A., Wellens H.J., Kass R.S.; RT "A novel mutation L619F in the cardiac Na+ channel SCN5A associated RT with long-QT syndrome (LQT3): a role for the I-II linker in RT inactivation gating."; RL Hum. Mutat. 21:552-552(2003). RN [30] RP VARIANTS SSS1 ILE-220; LEU-1298 AND ARG-1408. RX PubMed=14523039; DOI=10.1172/JCI200318062; RA Benson D.W., Wang D.W., Dyment M., Knilans T.K., Fish F.A., RA Strieper M.J., Rhodes T.H., George A.L. Jr.; RT "Congenital sick sinus syndrome caused by recessive mutations in the RT cardiac sodium channel gene (SCN5A)."; RL J. Clin. Invest. 112:1019-1028(2003). CC -!- FUNCTION: This protein mediates the voltage-dependent sodium ion CC permeability of excitable membranes. Assuming opened or closed CC conformations in response to the voltage difference across the CC membrane, the protein forms a sodium-selective channel through CC which Na+ ions may pass in accordance with their electrochemical CC gradient. It is a tetrodotoxin-resistant Na+ channel isoform. This CC channel is responsible for the initial upstroke of the action CC potential in the electrocardiogram. CC -!- SUBUNIT: Interacts with the PDZ domain of the syntrophin SNTA1, CC SNTB1 and SNTB2 (By similarity). CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in human atrial and ventricular CC cardiac muscle but not in adult skeletal muscle, brain, CC myometrium, liver, or spleen. CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5 CC hydrophobic segments (S1,S2,S3,S5,S6) and one positively charged CC segment (S4). Segments S4 are probably the voltage-sensors and are CC characterized by a series of positively charged amino acids at CC every third position. CC -!- DISEASE: Defects in SCN5A are a cause of progressive familial CC heart block type I (PFHBI) [MIM:113900]; also known as Lenegre-Lev CC disease or progressive cardiac conduction defect (PCCD). PFHBI is CC characterized by progressive alteration of cardiac conduction CC through the His-Purkinje system with right or left bundle branch CC block and widening of QRS complexes, leading to complete atrio- CC ventricular block and causing syncope and sudden death. PFHBI CC inheritance is autosomal dominant. CC -!- DISEASE: Defects in SCN5A are the cause of long QT syndrome type 3 CC (LQT3) [MIM:603830]. LQT3 is an autosomal dominant cardiac disease CC characterized by prolonged QT interval on electrocardiogram, CC recurrent syncope and sudden cardiac death. CC -!- DISEASE: Defects in SCN5A are the cause of Brugada syndrome CC [MIM:601144]. Brugada syndrome is an autosomal dominant inherited CC arrhythmia that causes the ventricles to beat so fast that they CC can prevent the blood from circulating efficiently in the body. CC When this situation occurs (called ventricular fibrillation), the CC individual will faint and may die in a few minutes if the heart is CC not reset. Brugada syndrome is an idiopathic ventricular CC fibrillation (IVF) syndrome characterized by right bundle branch CC block and ST elevation on an electrocardiogram (ECG). While CC Brugada syndrome is a disease that usually affects people in their CC 30's, it has actually been described at all ages. CC -!- DISEASE: Defects in SCN5A are the cause of autosomal recessive CC sick sinus syndrome 1 (SSS1) [MIM:608567]. The term 'sick sinus CC syndrome' encompasses a variety of conditions caused by sinus node CC dysfunction. The most common clinical manifestations are syncope, CC presyncope, dizziness, and fatigue. Electrocardiogram typically CC shows sinus bradycardia, sinus arrest, and/or sinoatrial block. CC Episodes of atrial tachycardias coexisting with sinus bradycardia CC ('tachycardia-bradycardia syndrome') are also common in this CC disorder. SSS occurs most often in the elderly associated with CC underlying heart disease or previous cardiac surgery, but can also CC occur in the fetus, infant, or child without heart disease or CC other contributing factors, in which case it is considered to be a CC congenital disorder. CC -!- DISEASE: Defects in SCN5A are a cause of idiopathic ventricular CC fibrillation (IVF) [MIM:603829]; also called paroxysmal familial CC ventricular fibrillation. IVF is a self originated, of unknown CC causation, ventricular fibrillation that causes the ventricles to CC beat so fast that they can prevent the blood from circulating CC efficiently in the body. This disorder is not truly idiopathic in CC many cases but can be caused by specific mutations such as those CC in the SCN5A gene. IVF is said to cause more than 300,000 sudden CC deaths each year in the United States alone. In approximately 5 to CC 12% of cases, there are no demonstrable cardiac or noncardiac CC causes to account for the episode, which is therefore classified CC as idiopathic ventricular fibrillation. CC -!- DISEASE: Defects in SCN5A are a cause of sudden infant death CC syndrome (SIDS) [MIM:272120]. SIDS remains elusive in its causes CC and devastating in its consequences. Despite the impressive CC decline in the incidence of SIDS since the recommendation to avoid CC the prone sleep position, SIDS remains a leading cause of death in CC the first year of life. CC -!- MISCELLANEOUS: Na+ channels in mammalian cardiac membrane have CC functional properties quite distinct from Na+ channels in nerve CC and skeletal muscle. CC -!- SIMILARITY: Belongs to the sodium channel family. CC -!- SIMILARITY: Contains 1 IQ domain. CC -!- WEB RESOURCE: Name=LQTSdb; Note=SCN5A mutations page; CC URL="http://www.ssi.dk/en/forskning/lqtsdb/scn5a.htm"; CC -!- WEB RESOURCE: Name=CaBP; Note=Calpain; CC URL="http://structbio.vanderbilt.edu/cabp_database/general/prot_pages/calpain.html"; DR EMBL; M77235; AAA58644.1; -. DR PIR; A38195; A38195. DR HGNC; HGNC:10593; SCN5A. DR MIM; 113900; -. DR MIM; 272120; -. DR MIM; 600163; -. DR MIM; 601144; -. DR MIM; 603829; -. DR MIM; 603830; -. DR MIM; 608567; -. DR GO; GO:0005248; F:voltage-gated sodium channel activity; TAS. DR GO; GO:0006936; P:muscle contraction; TAS. DR GO; GO:0008016; P:regulation of heart rate; TAS. DR GO; GO:0006814; P:sodium ion transport; TAS. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR000048; IQ_region. DR InterPro; IPR005820; M+channel_nlg. DR InterPro; IPR001696; Na_channel. DR InterPro; IPR008053; Na_channel5. DR InterPro; IPR010526; Na_trans_assoc. DR Pfam; PF00520; Ion_trans; 4. DR Pfam; PF00612; IQ; 1. DR Pfam; PF06512; Na_trans_assoc; 1. DR PRINTS; PR00170; NACHANNEL. DR PRINTS; PR01666; NACHANNEL5. DR PROSITE; PS50096; IQ; FALSE_NEG. DR HSSP; P04775; 1BYY. KW Ionic channel; Transmembrane; Ion transport; Voltage-gated channel; KW Glycoprotein; Repeat; Multigene family; Phosphorylation; Polymorphism; KW Disease mutation; Long QT syndrome; Sodium channel. FT TRANSMEM 127 150 S1 of repeat I (Potential). FT TRANSMEM 159 178 S2 of repeat I (Potential). FT TRANSMEM 192 210 S3 of repeat I (Potential). FT TRANSMEM 217 236 S4 of repeat I (Potential). FT TRANSMEM 253 276 S5 of repeat I (Potential). FT TRANSMEM 390 415 S6 of repeat I (Potential). FT TRANSMEM 712 736 S1 of repeat II (Potential). FT TRANSMEM 748 771 S2 of repeat II (Potential). FT TRANSMEM 780 799 S3 of repeat II (Potential). FT TRANSMEM 806 825 S4 of repeat II (Potential). FT TRANSMEM 842 862 S5 of repeat II (Potential). FT TRANSMEM 914 939 S6 of repeat II (Potential). FT TRANSMEM 1201 1224 S1 of repeat III (Potential). FT TRANSMEM 1238 1263 S2 of repeat III (Potential). FT TRANSMEM 1270 1291 S3 of repeat III (Potential). FT TRANSMEM 1296 1317 S4 of repeat III (Potential). FT TRANSMEM 1337 1359 S5 of repeat III (Potential). FT TRANSMEM 1444 1470 S6 of repeat III (Potential). FT TRANSMEM 1524 1547 S1 of repeat IV (Potential). FT TRANSMEM 1559 1582 S2 of repeat IV (Potential). FT TRANSMEM 1589 1612 S3 of repeat IV (Potential). FT TRANSMEM 1623 1644 S4 of repeat IV (Potential). FT TRANSMEM 1660 1682 S5 of repeat IV (Potential). FT TRANSMEM 1748 1772 S6 of repeat IV (Potential). FT CARBOHYD 214 214 N-linked (GlcNAc...) (Potential). FT CARBOHYD 283 283 N-linked (GlcNAc...) (Potential). FT CARBOHYD 288 288 N-linked (GlcNAc...) (Potential). FT CARBOHYD 291 291 N-linked (GlcNAc...) (Potential). FT CARBOHYD 318 318 N-linked (GlcNAc...) (Potential). FT CARBOHYD 328 328 N-linked (GlcNAc...) (Potential). FT CARBOHYD 548 548 N-linked (GlcNAc...) (Potential). FT CARBOHYD 592 592 N-linked (GlcNAc...) (Potential). FT CARBOHYD 740 740 N-linked (GlcNAc...) (Potential). FT CARBOHYD 803 803 N-linked (GlcNAc...) (Potential). FT CARBOHYD 841 841 N-linked (GlcNAc...) (Potential). FT CARBOHYD 864 864 N-linked (GlcNAc...) (Potential). FT CARBOHYD 946 946 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1365 1365 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1374 1374 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1380 1380 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1388 1388 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1736 1736 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1774 1774 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1955 1955 N-linked (GlcNAc...) (Potential). FT VARIANT 220 220 T -> I (in SSS1). FT /FTId=VAR_017670. FT VARIANT 298 298 G -> S (in progressive familial heart FT block type I; significant defect in the FT kinetics of fast-channel inactivation FT distinct from mutations reported in FT LQT3). FT /FTId=VAR_017671. FT VARIANT 367 367 R -> H (in Brugada syndrome; express no FT current). FT /FTId=VAR_017672. FT VARIANT 425 425 R -> H (in AT-III deficiency; type-II; FT Glasgow/Sheffield/Chicago/Avranches/ FT Kumamoto-2; increases affinity for FT heparin). FT /FTId=VAR_007074. FT VARIANT 514 514 G -> C (in cardiac conduction defect). FT /FTId=VAR_017673. FT VARIANT 558 558 H -> R (in dbSNP:1805124). FT /FTId=VAR_008955. FT VARIANT 619 619 L -> F (in LQT3). FT /FTId=VAR_015682. FT VARIANT 735 735 A -> V (in Brugada syndrome; expresses FT currents with steady state activation FT voltage shifted to more positive FT potentials and exhibit reduced sodium FT channel current at the end of phase I of FT the action potential). FT /FTId=VAR_017674. FT VARIANT 941 941 S -> N (in LQT3; also in SIDS). FT /FTId=VAR_017675. FT VARIANT 997 997 A -> S (in LQT3; sodium current FT characterized by slower decay and a 2- to FT 3-fold increase in late sodium current). FT /FTId=VAR_017676. FT VARIANT 1090 1090 P -> L (in dbSNP:1805125). FT /FTId=VAR_014464. FT VARIANT 1103 1103 S -> Y (in acquired arrhythmia; FT susceptibility to). FT /FTId=VAR_017677. FT VARIANT 1114 1114 D -> N (in LQT3). FT /FTId=VAR_009935. FT VARIANT 1193 1193 R -> Q (in Brugada syndrome; accelerates FT the inactivation of the sodium channel FT current and exhibit reduced sodium FT channel current at the end of phase I of FT the action potential). FT /FTId=VAR_017678. FT VARIANT 1232 1232 R -> W (in Brugada syndrome; could be a FT rare polymorphism). FT /FTId=VAR_017679. FT VARIANT 1298 1298 P -> L (in SSS1). FT /FTId=VAR_017680. FT VARIANT 1304 1304 T -> M (in LQT3). FT /FTId=VAR_008956. FT VARIANT 1325 1325 N -> S (in LQT3). FT /FTId=VAR_001577. FT VARIANT 1408 1408 G -> R (in SSS1 and Brugada syndrome; FT also in cardiac conduction defect). FT /FTId=VAR_017681. FT VARIANT 1500 1500 K -> N. FT /FTId=VAR_008957. FT VARIANT 1501 1501 L -> V (in LQT3). FT /FTId=VAR_009936. FT VARIANT 1505 1507 Missing (in LQT3). FT /FTId=VAR_001576. FT VARIANT 1512 1512 R -> W (in Brugada syndrome; FT significantly affects cardiac sodium FT channel characteristics; associated with FT an increase in inward sodium current FT during the action potential upstroke). FT /FTId=VAR_017682. FT VARIANT 1595 1595 D -> N (in progressive familial heart FT block type I; significant defect in the FT kinetics of fast-channel inactivation FT distinct from mutations reported in FT LQT3). FT /FTId=VAR_017683. FT VARIANT 1620 1620 T -> M (in Brugada syndrome; FT arrhythmogenicity revealed only at FT temperatures approaching the physiologic FT range). FT /FTId=VAR_017684. FT VARIANT 1623 1623 R -> L (in LQT3). FT /FTId=VAR_009937. FT VARIANT 1623 1623 R -> Q (in LQT3). FT /FTId=VAR_001578. FT VARIANT 1644 1644 R -> H (in LQT3). FT /FTId=VAR_001579. FT VARIANT 1645 1645 T -> M (in LQT3). FT /FTId=VAR_008958. FT VARIANT 1710 1710 S -> L (in IVF). FT /FTId=VAR_017685. FT VARIANT 1784 1784 E -> K (in LQT3). FT /FTId=VAR_008959. FT VARIANT 1787 1787 S -> N (in LQT3). FT /FTId=VAR_009938. FT VARIANT 1790 1790 D -> G (in LQT3). FT /FTId=VAR_001580. FT VARIANT 1795 1795 Y -> C (in LQT3; slows the onset of FT activation, but does not cause a marked FT negative shift in the voltage dependence FT of inactivation or affect the kinetics of FT the recovery from inactivation; increases FT the expression of sustained Na(+) channel FT activity and promotes entrance into an FT intermediate or slowly developing FT inactivated state). FT /FTId=VAR_019123. FT VARIANT 1795 1795 Y -> H (in Brugada syndrome; accelerates FT the onset of activation and causes a FT marked negative shift in the voltage FT dependence of inactivation; does not FT affect the kinetics of the recovery from FT inactivation; increases the expression of FT sustained Na(+) channel activity and FT promotes entrance into an intermediate or FT slowly developing inactivated state). FT /FTId=VAR_019124. FT VARIANT 1795 1795 Y -> YD (in LQT3 and Brugada syndrome; FT 7.3-mV negative shift of the steady-state FT inactivation curve and 8.1-mV positive FT shift of the steady-state activation FT curve; may reduced sodium current during FT the upstroke of the action potential). FT /FTId=VAR_017686. FT VARIANT 1826 1826 R -> H (in LQT3; sodium current FT characterized by slower decay and a 2- to FT 3-fold increase in late sodium current). FT /FTId=VAR_017687. FT VARIANT 1839 1839 D -> G (in LQT3). FT /FTId=VAR_001581. FT VARIANT 1924 1924 A -> T (in Brugada syndrome; FT significantly affect cardiac sodium FT channel characteristics; associated with FT an increase in inward sodium current FT during the action potential upstroke). FT /FTId=VAR_017688. ** ** ################# INTERNAL SECTION ################## **CL 3p21; **ZB SYP, 23-JUL-2002; SQ SEQUENCE 2016 AA; 227162 MW; ED97598D215E349E CRC64; MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSTTLQ ESREGLPEEE APRPQLDLQA SKKLPDLYGN PPQELIGEPL EDLDPFYSTQ KTFIVLNKGK TIFRFSATNA LYVLSPFHPV RRAAVKILVH SLFNMLIMCT ILTNCVFMAQ HDPPPWTKYV EYTFTAIYTF ESLVKILARA FCLHAFTFLR DPWNWLDFSV IIMAYTTEFV DLGNVSALRT FRVLRALKTI SVISGLKTIV GALIQSVKKL ADVMVLTVFC LSVFALIGLQ LFMGNLRHKC VRNFTALNGT NGSVEADGLV WESLDLYLSD PENYLLKNGT SDVLLCGNSS DAGTCPEGYR CLKAGENPDH GYTSFDSFAW AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG SFYLVNLILA VVAMAYEEQN QATIAETEEK EKRFQEAMEM LKKEHEALTI RGVDTVSRSS LEMSPLAPVN SHERRSKRRK RMSSGTEECG EDRLPKSDSE DGPRAMNHLS LTRGLSRTSM KPRSSRGSIF TFRRRDLGSE ADFADDENST ARESESHHTS LLVPWPLRRT SAQGQPSPGT SAPGHALHGK KNSTVDCNGV VSLLGAGDPE ATSPGSHLLR PVMLEHPPDT TTPSEEPGGP QMLTSQAPCV DGFEEPGARQ RALSAVSVLT SALEELEESR HKCPPCWNRL AQRYLIWECC PLWMSIKQGV KLVVMDPFTD LTITMCIVLN TLFMALEHYN MTSEFEEMLQ VGNLVFTGIF TAEMTFKIIA LDPYYYFQQG WNIFDSIIVI LSLMELGLSR MSNLSVLRSF RLLRVFKLAK SWPTLNTLIK IIGNSVGALG NLTLVLAIIV FIFAVVGMQL FGKNYSELRD SDSGLLPRWH MMDFFHAFLI IFRILCGEWI ETMWDCMEVS GQSLCLLVFL LVMVIGNLVV LNLFLALLLS SFSADNLTAP DEDREMNNLQ LALARIQRGL RFVKRTTWDF CCGLLRHRPQ KPAALAAQGQ LPSCIATPYS PPPPETEKVP PTRKETQFEE GEQPGQGTPG DPEPVCVPIA VAESDTDDQE EDEENSLGTE EESSKQQESQ PVSGWPRGPP DSRTWSQVSA TASSEAEASA SQADWRQQWK AEPQAPGCGE TPEDSCSEGS TADMTNTAEL LEQIPDLGQD VKDPEDCFTE GCVRRCPCCA VDTTQAPGKV WWRLRKTCYH IVEHSWFETF IIFMILLSSG ALAFEDIYLE ERKTIKVLLE YADKMFTYVF VLEMLLKWVA YGFKKYFTNA WCWLDFLIVD VSLVSLVANT LGFAEMGPIK SLRTLRALRP LRALSRFEGM RVVVNALVGA IPSIMNVLLV CLIFWLIFSI MGVNLFAGKF GRCINQTEGD LPLNYTIVNN KSQCESLNLT GELYWTKVKV NFDNVGAGYL ALLQVATFKG WMDIMYAAVD SRGYEEQPQW EYNLYMYIYF VIFIIFGSFF TLNLFIGVII DNFNQQKKKL GGQDIFMTEE QKKYYNAMKK LGSKKPQKPI PRPLNKYQGF IFDIVTKQAF DVTIMFLICL NMVTMMVETD DQSPEKINIL AKINLLFVAI FTGECIVKLA ALRHYYFTNS WNIFDFVVVI LSIVGTVLSD IIQKYFFSPT LFRVIRLARI GRILRLIRGA KGIRTLLFAL MMSLPALFNI GLLLFLVMFI YSIFGMANFA YVKWEAGIDD MFNFQTFANS MLCLFQITTS AGWDGLLSPI LNTGPPYCDP TLPNSNGSRG DCGSPAVGIL FFTTYIIISF LIVVNMYIAI ILENFSVATE ESTEPLSEDD FDMFYEIWEK FDPEATQFIE YSVLSDFADA LSEPLRIAKP NQISLINMDL PMVSGDRIHC MDILFAFTKR VLGESGEMDA LKIQMEEKFM AANPSKISYE PITTTLRRKH EEVSAMVIQR AFRRHLLQRS LKHASFLFRQ QAGSGLSEED APEREGLIAY VMSENFSRPL GPPSSSSISS TSFPPSYDSV TRATSDNLQV RGSDYSHSED LADFPPSPDR DRESIV // ID Q9DIX3 PRELIMINARY; PRT; 56 AA. AC Q9DIX3; DT 01-MAR-2001 (TrEMBLrel. 16, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE VP1 capsid protein and P2A protease (Fragment){EI4}. GN Name=VP1 and P2A{EI4}; OS Hepatitis A virus. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornaviridae; OC Hepatovirus. OX NCBI_TaxID=12092{EI4}; RN [1]{EI4} RP SEQUENCE FROM N.A. RX MEDLINE=21259955; PubMed=11360240; RA Diaz B.I., Sariol C.A., Normann A., Rodriguez L.A., Flehmig B.; RT "Genetic relatedness of Cuban HAV wild-type isolates."; RL J. Med. Virol. 64:96-103(2001). DR EMBL; AJ245534; CAC17887.1; -.{EI4} DR PIR; PQ0427; PQ0427. DR PIR; PQ0428; PQ0428. DR GO; GO:0008233; F:peptidase activity; IEA. DR InterPro; IPR000886; ER_target_S. DR PROSITE; PS00014; ER_TARGET; UNKNOWN_1. KW Protease{EP2}. FT NON_TER 1 1 {EI4} FT NON_TER 56 56 {EI4} ** ** ################# INTERNAL SECTION ################## **EV EI4; EMBL; -; CAC17887.1; 11-MAY-2004. **EV EP2; TrEMBL; -; CAC17887.1; 11-MAY-2004. **PM PROSITE; PS00014; ER_TARGET; 53; 56; ?; 27-APR-2004; SQ SEQUENCE 56 AA; 6628 MW; 465CF4B35C1EF4BC CRC64; ESMMSRIAAG DLESSVDDPR SDEDRRFESH IECRKPYKEL RLEVGKQRLK YAQEEL // ID Q27383 PRELIMINARY; PRT; 378 AA. AC Q27383; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Hypothetical 40.7 kDa protein R09F10.2 in chromosome X precursor. GN Name=R09F10.2; GN and GN Name=abu-9{EI1}; ORFNames=R09F10.2{EI1}, R09F10.7{EI2}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Couch J.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP REVISIONS TO C-TERMINUS. ** MEDLINE=None; PubMed=None; RA Ambler R.P.; ** /NO TITLE. RL Unpublished results, cited by: RL McGinnis J., Sinclair-day J.D., Sykes A.G., Powls R., Moore J., RL Wright P.D.; RL Inorg. Chem. 27:2306-2312(1988). RN [3] RP SEQUENCE. RC TISSUE=Plasma; RA Moorad D.R., Luo C., Garcia G.E., Doctor B.P.; RT "Amino acid sequence of horse serum butyrycholinesterase."; RL (In) Doctor B.P., Taylor P., Quinn D.M., Rotundo R.L., Gentry M.K. RL (eds.); RL Structure and function of cholinesterases and related proteins, RL pp.145-146, Plenum Press, New York and London (1998). CC -!- WEB RESOURCE: Name=Androgen receptor gene mutations database; CC URL="http://www.mcgill.ca/androgendb/"; CC -!- SIMILARITY: BELONGS TO FAMILY UPF. DR EMBL; U64859; AAC69090.1; -. DR PIR; B89588; B89588. DR WormBase; R09F10.2; CE07436. DR WormBase; R09F10.7; CE07436. DR InterPro; IPR009475; DUF1096. DR InterPro; IPR003341; DUF139. DR Pfam; PF02363; C_tripleX; 9. DR Pfam; PF06493; DUF1096; 1. KW Hypothetical protein; Signal. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 378 HYPOTHETICAL PROTEIN R09F10.2. ** ** ################# SOURCE SECTION ################## ** Caenorhabditis elegans cosmid R09F10. ** [1] ** 1-31934 ** MEDLINE; 94150718. ** Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield ** J., ** Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., ** Dear S., Du Z., Durbin R., Favello A., Fulton L., Gardner A., Green ** P., ** Hawkins T., Hillier L., Jier M., Johnston L., Jones M., Kershaw J., ** Kirsten J., Laister N., Latreille P., Lightning J., Lloyd C., ** McMurray A., Mortimore B., O'Callaghan M., Parsons J., Percy C., ** Rifken L., Roopra A., Saunders D., Shownkeen R., Smaldon N., Smith A., ** Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., ** Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., ** Wilkinson-Sproat J., Wohldman P.; ** "2.2 Mb of contiguous nucleotide sequence from chromosome III of C. ** elegans"; ** Nature 368:32-38(1994). ** [2] ** 1-31934 ** Couch J.; ** "The sequence of C. elegans cosmid R09F10"; ** Unpublished. ** [3] ** 1-31934 ** Waterston R.; ** ; ** Submitted (22-JUL-1996) to the EMBL/GenBank/DDBJ databases. ** Genome Sequencing Center Department of Genetics, Washington ** University, ** St. Louis, MO 63110, USA, and Sanger Centre, Hinxton Hall Cambridge ** CB10 ** IRQ, England e-mail: rw@nematode.wustl.edu and jes@sanger.ac.uk ** Submitted by: Genome Sequencing Center Department of Genetics, ** Washington University, St. Louis, MO 63110, USA, and Sanger Centre, ** Hinxton Hall Cambridge CB10 IRQ, England e-mail: ** rw@nematode.wustl.edu and jes@sanger.ac.uk NEIGHBORING COSMID ** INFORMATION: The 5' cosmid is F13B9, 600 bp overlap;3' cosmid is ** F55E10, 200 bp overlap. Actual start of this cosmid is at base ** position 595 of CELR09F10; actual end is at 7938 of CELF55E10 ** NOTES: Coding sequences below are predicted from computer analysis, ** using the program Genefinder(P. Green and L. Hillier, ms in ** preparation). ** source 1..31934 ** /organism="Caenorhabditis elegans" ** /chromosome="X" ** /strain="Bristol N2" ** /clone="R09F10" ** CDS join(complement(26227..26277),complement(26009. ** .26179), ** complement(25045..25959)) ** /codon_start=1 ** /db_xref="PID:g1465855" ** /evidence=NOT_EXPERIMENTAL ** /note="glutamine-rich protein" ** /gene="R09f10.7" ** CDS_IN_EMBL_ENTRY 8 ** 01-OCT-1996 (Rel. 49, Last updated, Version 5) ** Caenorhabditis elegans cosmid R09F10. ** [1] ** 1-31934 ** MEDLINE; 94150718. ** Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield ** J., ** Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., ** Dear S., Du Z., Durbin R., Favello A., Fulton L., Gardner A., Green ** P., ** Hawkins T., Hillier L., Jier M., Johnston L., Jones M., Kershaw J., ** Kirsten J., Laister N., Latreille P., Lightning J., Lloyd C., ** McMurray A., Mortimore B., O'Callaghan M., Parsons J., Percy C., ** Rifken L., Roopra A., Saunders D., Shownkeen R., Smaldon N., Smith A., ** Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., ** Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., ** Wilkinson-Sproat J., Wohldman P.; ** "2.2 Mb of contiguous nucleotide sequence from chromosome III of C. ** elegans"; ** Nature 368:32-38(1994). ** [2] ** 1-31934 ** Couch J.; ** "The sequence of C. elegans cosmid R09F10"; ** Unpublished. ** [3] ** 1-31934 ** Waterston R.; ** ; ** Submitted (22-JUL-1996) to the EMBL/GenBank/DDBJ databases. ** Genome Sequencing Center Department of Genetics, Washington ** University, ** St. Louis, MO 63110, USA, and Sanger Centre, Hinxton Hall Cambridge ** CB10 ** IRQ, England e-mail: rw@nematode.wustl.edu and jes@sanger.ac.uk ** Submitted by: Genome Sequencing Center Department of Genetics, ** Washington University, St. Louis, MO 63110, USA, and Sanger Centre, ** Hinxton Hall Cambridge CB10 IRQ, England e-mail: ** rw@nematode.wustl.edu and jes@sanger.ac.uk NEIGHBORING COSMID ** INFORMATION: The 5' cosmid is F13B9, 600 bp overlap;3' cosmid is ** F55E10, 200 bp overlap. Actual start of this cosmid is at base ** position 595 of CELR09F10; actual end is at 7938 of CELF55E10 ** NOTES: Coding sequences below are predicted from computer analysis, ** using the program Genefinder(P. Green and L. Hillier, ms in ** preparation). ** source 1..31934 ** /organism="Caenorhabditis elegans" ** /chromosome="X" ** /strain="Bristol N2" ** /clone="R09F10" ** CDS join(27488..27538,27586..27756,27806..28720) ** /codon_start=1 ** /db_xref="PID:g1465856" ** /evidence=NOT_EXPERIMENTAL ** /note="glutamine-rich protein" ** /gene="R09f10.2" ** CDS_IN_EMBL_ENTRY 8 ** 01-OCT-1996 (Rel. 49, Last updated, Version 5) ** FAMILY UPF CONSISTS OF Q17400, Q17401, Q19919, Q19594 AND Q27383. ** FOR THIS ENTRY AMOS, THERE ARE TWO CDS IN THE SAME COSMID WHICH ** ENCODE IDENTICAL PROTEINS AND SO I HAVE MERGED. I HAVE USED THE ** FIRST CDS FOR NOMENCLATURE. ** ################# INTERNAL SECTION ################## **EV EI1; WormBase_ADD; -; R09F10.2; 23-MAY-2004. **EV EI2; WormBase_ADD; -; R09F10.7; 23-MAY-2004. **ID XXXX_CAEEL **PM Pfam; PF02363; C_tripleX; 131; 147; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 153; 169; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 191; 207; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 213; 229; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 259; 275; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 305; 321; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 327; 343; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 78; 94; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 99; 115; T; 06-MAY-2004; **PM Pfam; PF06493; DUF1096; 3; 65; T; 06-MAY-2004; **ZZ CREATED AND FINISHED BY CLAIRE. SQ SEQUENCE 378 AA; 40683 MW; E58B416BFE3A7610 CRC64; MRFITLAVFF ACALVASSSV LREKRHCGCA QPQQSQCSCQ QVQQTQSCSC QSAPVQQQAP SCSCAQPQQT QTVQVQSTQC APACQQSCRQ QCQSAPAVSQ CQPMCQQQCQ SQCTPMYNPP ATTTTTPAPV VQCQPMCQQQ CQSTCVQQQQ PVSQCQPQCQ QQCNVACDAT TTTTSAPQVI HIQLEIQQAQ VQCQPACQQQ CQSSCVQQQQ PAKQCASSCN TQCTNACQQT AQATQQVIYG QNSNTQMYDP YNNQQQQQAN CAPACQPACD NSCIQQTAAP IYNPTTTSAP QVVQIVLQAS VAQSSQCAPQ CEQSCQQQCV QQQQPVAQCQ SACQSSCSSS CQAAQPATVA CQQAPQSNQC SCQSNYSPCG QGQCCRRK // ID TAU_HUMAN STANDARD; PRT; 757 AA. AC P10636; P18518; Q14799; Q15549; Q15550; Q15551; Q9UDJ3; Q9UMH0; AC Q9UQ96; DT 01-JUL-1989 (Rel. 11, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE Microtubule-associated protein tau (Neurofibrillary tangle protein) DE (Paired helical filament-tau) (PHF-tau). GN Name=MAPT; Synonyms=MTBT1, TAU; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS PNS-TAU; TAU-A AND TAU-F). RA Andreadis A.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. (ISOFORM TAU-A). RC TISSUE=Brain; RX MEDLINE=88234557; PubMed=3131773; RA Goedert M., Wischik C., Crowther R., Walker J., Klug A.; RT "Cloning and sequencing of the cDNA encoding a core protein of the RT paired helical filament of Alzheimer disease: identification as the RT microtubule-associated protein tau."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4051-4055(1988). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS TAU-B; TAU-C; TAU-E AND TAU-F). RC TISSUE=Brain; RX MEDLINE=90380393; PubMed=2484340; RA Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A.; RT "Multiple isoforms of human microtubule-associated protein tau: RT sequences and localization in neurofibrillary tangles of Alzheimer's RT disease."; RL Neuron 3:519-526(1989). RN [4] RP SEQUENCE FROM N.A. (ISOFORM TAU-D). RC TISSUE=Brain; RX MEDLINE=89251564; PubMed=2498079; RA Goedert M., Spillantini M.G., Potier M.C., Ulrich J., Crowther R.A.; RT "Cloning and sequencing of the cDNA encoding an isoform of RT microtubule-associated protein tau containing four tandem repeats: RT differential expression of tau protein mRNAs in human brain."; RL EMBO J. 8:393-399(1989). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS TAU-A AND FETAL-TAU). RC TISSUE=Fetal brain; RX MEDLINE=90180482; PubMed=2516729; RA Lee G., Neve R.L., Kosik K.S.; RT "The microtubule binding domain of tau protein."; RL Neuron 2:1615-1624(1989). RN [6] RP SEQUENCE FROM N.A. (ISOFORM TAU-F), AND ALTERNATIVE SPLICING. RX MEDLINE=93041757; PubMed=1420178; RA Andreadis A., Brown W.M., Kosik K.S.; RT "Structure and novel exons of the human tau gene."; RL Biochemistry 31:10626-10633(1992). RN [7] RP SEQUENCE FROM N.A. (ISOFORM TAU-A). RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [8] RP SEQUENCE OF 591-621 FROM N.A. RC TISSUE=Brain; RX MEDLINE=89193714; PubMed=2495000; RA Mori H., Hamada Y., Kawaguchi M., Honda T., Kondo J., Ihara Y.; RT "A distinct form of tau is selectively incorporated into Alzheimer's RT paired helical filaments."; RL Biochem. Biophys. Res. Commun. 159:1221-1226(1989). RN [9] RP SEQUENCE OF 1-72; 102-380; 467-496; 507-570; 576-582; 591-606; RP 615-633; 638-656; 660-663; 670-699 AND 702-757. RC TISSUE=Brain; RX MEDLINE=92381012; PubMed=1512244; RA Hasegawa M., Morishima-Kawashima M., Takio K., Suzuki M., Titani K., RA Ihara Y.; RT "Protein sequence and mass spectrometric analyses of tau in the RT Alzheimer's disease brain."; RL J. Biol. Chem. 267:17047-17054(1992). RN [10] RP SEQUENCE OF 576-583; 607-610; 615-627; 638-647 AND 670-685, RP PHOSPHORYLATION, AND MUTAGENESIS. RX MEDLINE=95221434; PubMed=7706316; RA Drewes G., Trinczek B., Illenberger S., Biernat J., Schmitt-Ulms G., RA Meyer H.E., Mandelkow E.-M., Mandelkow E.; RT "Microtubule-associated protein/microtubule affinity-regulating kinase RT (p110mark). A novel protein kinase that regulates tau-microtubule RT interactions and dynamic instability by phosphorylation at the RT Alzheimer-specific site serine 262."; RL J. Biol. Chem. 270:7679-7688(1995). RN [11] RP REVIEW. RX MEDLINE=91320377; PubMed=1713721; DOI=10.1016/0166-2236(91)90105-4; RA Goedert M., Crowther R.A., Garner C.C.; RT "Molecular characterization of microtubule-associated proteins tau and RT MAP2."; RL Trends Neurosci. 14:193-199(1991). RN [12] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX MEDLINE=20283597; PubMed=10747907; DOI=10.1074/jbc.M000389200; RA Maas T., Eidenmueller J., Brandt R.; RT "Interaction of tau with the neural membrane cortex is regulated by RT phosphorylation at sites that are modified in paired helical RT filaments."; RL J. Biol. Chem. 275:15733-15740(2000). RN [13] RP PHOSPHORYLATION, AND MUTAGENESIS. RX MEDLINE=98413833; PubMed=9735171; RA Sengupta A., Kabat J., Novak M., Wu Q., Grundke-Iqbal I., Iqbal K.; RT "Phosphorylation of tau at both Thr 231 and Ser 262 is required for RT maximal inhibition of its binding to microtubules."; RL Arch. Biochem. Biophys. 357:299-309(1998). RN [14] RP PHOSPHORYLATION, AND MUTAGENESIS. RX MEDLINE=98278959; PubMed=9614189; RA Illenberger S., Zheng-Fischhofer Q., Preuss U., Stamer K., Baumann K., RA Trinczek B., Biernat J., Godemann R., Mandelkow E.-M., Mandelkow E.; RT "The endogenous and cell cycle-dependent phosphorylation of tau RT protein in living cells: implications for Alzheimer's disease."; RL Mol. Biol. Cell 9:1495-1512(1998). RN [15] RP GLYCATION. RX MEDLINE=97465580; PubMed=9326300; RA Nacharaju P., Ko L., Yen S.H.; RT "Characterization of in vitro glycation sites of tau."; RL J. Neurochem. 69:1709-1719(1997). RN [16] RP REVIEW ON VARIANTS. RX MEDLINE=20437008; PubMed=10899436; DOI=10.1016/S0925-4439(00)00037-5; RA Goedert M., Spillantini M.G.; RT "Tau mutations in frontotemporal dementia FTDP-17 and their relevance RT for Alzheimer's disease."; RL Biochim. Biophys. Acta 1502:110-121(2000). RN [17] RP VARIANT FTDP17 MET-653, AND VARIANTS ASN-284; ALA-288; TYR-440 AND RP PRO-446. RX MEDLINE=98291804; PubMed=9629852; RA Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., RA Anderson L., Andreadis A., Wiederholt W.C., Raskind M., RA Schellenberg G.D.; RT "Tau is a candidate gene for chromosome 17 frontotemporal dementia."; RL Ann. Neurol. 43:815-825(1998). RN [18] RP ERRATUM. ** MEDLINE=None; PubMed=None; RA Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., RA Anderson L., Andreadis A., Wiederholt W.C., Raskind M., RA Schellenberg G.D.; ** /NO TITLE. RL Ann. Neurol. 44:428-428(1998). RN [19] RP VARIANT FTDP17 LEU-617. RX MEDLINE=98409513; PubMed=9736786; RA Dumanchin C., Camuzat A., Campion D., Verpillat P., Hannequin D., RA Dubois B., Saugier-Veber P., Martin C., Penet C., Charbonnier F., RA Agid Y., Frebourg T., Brice A.; RT "Segregation of a missense mutation in the microtubule-associated RT protein tau gene with familial frontotemporal dementia and RT parkinsonism."; RL Hum. Mol. Genet. 7:1825-1829(1998). RN [20] RP VARIANTS FTDP17 VAL-588; LEU-617 AND TRP-722. RX MEDLINE=98303385; PubMed=9641683; DOI=10.1038/31508; RA Hutton M., Lendon C.L., Rizzu P., Baker M., Froelich S., Houlden H., RA Pickering-Brown S., Chakraverty S., Isaacs A., Grover A., Hackett J., RA Adamson J., Lincoln S., Dickson D., Davies P., Petersen R.C., RA Stevens M., de Graaff E., Wauters E., van Baren J., Hillebrand M., RA Joosse M., Kwon J.M., Nowotny P., Che L.K., Norton J., Morris J.C., RA Reed L.A., Trojanowski J., Basun H., Lannfelt L., Neystat M., Fahn S., RA Dark F., Tannenberg T., Dodd P.R., Hayward N., Kwok J.B.J., RA Schofield P.R., Andreadis A., Snowden J., Craufurd D., Neary D., RA Owen F., Oostra B.A., Hardy J., Goate A., van Swieten J., Mann D., RA Lynch T., Heutink P.; RT "Association of missense and 5'-splice-site mutations in tau with the RT inherited dementia FTDP-17."; RL Nature 393:702-705(1998). RN [21] RP VARIANT PPND LYS-595, AND VARIANT FTDP17 LEU-617. RX MEDLINE=99007274; PubMed=9789048; RA Clark L.N., Poorkaj P., Wszolek Z., Geschwind D.H., Nasreddine Z.S., RA Miller B., Li D., Payami H., Awert F., Markopoulou K., Andreadis A., RA D'Souza I., Lee V.M.-Y., Reed L., Trojanowski J.Q., Zhukareva V., RA Bird T., Schellenberg G., Wilhelmsen K.C.; RT "Pathogenic implications of mutations in the tau gene in pallido- RT ponto-nigral degeneration and related neurodegenerative disorders RT linked to chromosome 17."; RL Proc. Natl. Acad. Sci. U.S.A. 95:13103-13107(1998). RN [22] RP VARIANTS FTDP17 VAL-588; LYS-596 DEL; LEU-617 AND TRP-722. RX MEDLINE=99138654; PubMed=9973279; RA Rizzu P., Van Swieten J.C., Joosse M., Hasegawa M., Stevens M., RA Tibben A., Niermeijer M.F., Hillebrand M., Ravid R., Oostra B.A., RA Goedert M., van Duijn C.M., Heutink P.; RT "High prevalence of mutations in the microtubule-associated protein RT tau in a population study of frontotemporal dementia in the RT Netherlands."; RL Am. J. Hum. Genet. 64:414-421(1999). RN [23] RP VARIANTS FTDP17 LEU-617; MET-653 AND TRP-722. RX MEDLINE=99229757; PubMed=10214944; RA Nacharaju P., Lewis J., Easson C., Yen S., Hackett J., Hutton M., RA Yen S.H.; RT "Accelerated filament formation from tau protein with specific FTDP-17 RT missense mutations."; RL FEBS Lett. 447:195-199(1999). RN [24] RP VARIANT FTDP17/CBD SER-617. RX MEDLINE=99301293; PubMed=10374757; RA Bugiani O., Murrell J.R., Giaccone G., Hasegawa M., Ghigo G., RA Tabaton M., Morbin M., Primavera A., Carella F., Solaro C., RA Grisoli M., Savoiardo M., Spillantini M.G., Tagliavini F., Goedert M., RA Ghetti B.; RT "Frontotemporal dementia and corticobasal degeneration in a family RT with a P301S mutation in tau."; RL J. Neuropathol. Exp. Neurol. 58:667-677(1999). RN [25] RP VARIANT DEMENTIA ARG-705. RX MEDLINE=20068246; PubMed=10604746; RA Murrell J.R., Spillantini M.G., Zolo P., Guazzelli M., Smith M.J., RA Hasegawa M., Redi F., Crowther R.A., Pietrini P., Ghetti B., RA Goedert M.; RT "Tau gene mutation G389R causes a tauopathy with abundant pick body- RT like inclusions and axonal deposits."; RL J. Neuropathol. Exp. Neurol. 58:1207-1226(1999). RN [26] RP VARIANTS PSP ASN-284 AND ALA-288. RX MEDLINE=20001812; PubMed=10534245; RA Higgins J.J., Adler R.L., Loveless J.M.; RT "Mutational analysis of the tau gene in progressive supranuclear RT palsy."; RL Neurology 53:1421-1424(1999). RN [27] RP VARIANT FTDP17 ASN-621. RX MEDLINE=99223277; PubMed=10208578; RA Iijima M., Tabira T., Poorkaj P., Schellenberg G.D., Trojanowski J.Q., RA Lee V.M.-Y., Schmidt M.L., Takahashi K., Nabika T., Matsumoto T., RA Yamashita Y., Yoshioka S., Ishino H.; RT "A distinct familial presenile dementia with a novel missense mutation RT in the tau gene."; RL NeuroReport 10:497-501(1999). RN [28] RP VARIANT DEMENTIA THR-573. RX MEDLINE=20539309; PubMed=11089577; RA Rizzini C., Goedert M., Hodges J.R., Smith M.J., Jakes R., Hills R., RA Xuereb J.H., Crowther R.A., Spillantini M.G.; RT "Tau gene mutation K257T causes a tauopathy similar to Pick's RT disease."; RL J. Neuropathol. Exp. Neurol. 59:990-1001(2000). CC -!- FUNCTION: Promotes microtubule assembly and stability, and might CC be involved in the establishment and maintenance of neuronal CC polarity. The C-terminus binds axonal microtubules while the N- CC terminus binds neural plasma membrane components, suggesting that CC tau functions as a linker protein between both. Axonal polarity is CC predetermined by tau localization (in the neuronal cell) in the CC domain of the cell body defined by the centrosome. The short CC isoforms allow plasticity of the cytoskeleton whereas the longer CC isoforms may preferentially play a role in its stabilization. CC -!- SUBCELLULAR LOCATION: Mostly found in the axons of neurons, in the CC cytosol and in association with plasma membrane components. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Comment=Additional isoforms seem to exist. Isoforms differ from CC each other by the presence or absence of up to 5 of the 15 CC exons. One of these optional exons contains the additional CC tau/MAP repeat; CC Name=PNS-tau; CC IsoId=P10636-1; Sequence=Displayed; CC Name=Fetal-tau; CC IsoId=P10636-2; Sequence=VSP_003175, VSP_003176, VSP_003177, CC VSP_003178, VSP_003179, VSP_003180, CC VSP_003181; CC Name=Tau-A; CC IsoId=P10636-3; Sequence=VSP_003176, VSP_003177, VSP_003179, CC VSP_003180, VSP_003181; CC Name=Tau-B; CC IsoId=P10636-4; Sequence=VSP_003177, VSP_003179, VSP_003180, CC VSP_003181; CC Name=Tau-C; Synonyms=Tau-3; CC IsoId=P10636-5; Sequence=VSP_003179, VSP_003180, VSP_003181; CC Name=Tau-D; CC IsoId=P10636-6; Sequence=VSP_003176, VSP_003177, VSP_003179, CC VSP_003180; CC Name=Tau-E; CC IsoId=P10636-7; Sequence=VSP_003177, VSP_003179, VSP_003180; CC Name=Tau-F; Synonyms=Tau-4; CC IsoId=P10636-8; Sequence=VSP_003179, VSP_003180; CC -!- TISSUE SPECIFICITY: Expressed in neurons. PNS-tau is expressed in CC the peripheral nervous system while the others are expressed in CC the central nervous system. CC -!- DEVELOPMENTAL STAGE: Four-repeat (type II) tau is expressed in an CC adult-specific manner and is not found in fetal brain, whereas CC three-repeat (type I) tau is found in both adult and fetal brain. CC -!- DOMAIN: The tau/MAP repeat binds to tubulin. Type I isoforms CC contain 3 repeats while type II isoforms contain 4 repeats. CC -!- PTM: Phosphorylation at serine and threonine residues in S-P or T- CC P motifs by proline-directed protein kinases (PDPK: CDC2, CDK5, CC GSK-3, MAPK) (only 2-3 sites per protein in interphase, seven-fold CC increase in mitosis, and in PHF-tau), and at serine residues in K- CC X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK) CC in Alzheimer's diseased brains. Phosphorylation decreases with CC age. Phosphorylation within tau's repeat domain or in flanking CC regions seems to reduce tau's interaction with, respectively, CC microtubules or plasma membrane components. CC -!- PTM: Glycation of PHF-tau, but not normal brain tau. Glycation is CC a non-enzymatic posttranslational modification that involves a CC covalent linkage between a sugar and an amino group of a protein CC molecule forming ketoamine. Subsequent oxidation, fragmentation CC and/or crosslinking of ketoamine leads to the production of CC advanced glycation endproducts (AGES). Glycation may play a role CC in stabilizing PHF aggregation leading to tangle formation in AD. CC -!- PTM: Phosphorylation on Ser-609, Ser-621, Ser-640 and Ser-672 in CC several isoforms during mitosis. CC -!- DISEASE: In Alzheimer disease, the neuronal cytoskeleton in the CC brain is progressively disrupted and replaced by tangles of paired CC helical filaments (PHF) and straight filaments, mainly composed of CC hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU). CC -!- DISEASE: Defects in MAPT are a cause of frontotemporal dementia CC and parkinsonism linked to chromosome 17 (FTDP17) [MIM:600274]; CC also historically termed Pick's disease. This form of CC frontotemporal dementia is characterized by presenile dementia CC with behavioral changes, deterioration of cognitive capacities and CC loss of memory. In some cases, parkinsonian symptoms are CC prominent. Neuropathological changes include frontotemporal CC atrophy often associated with atrophy of the basal ganglia, CC substantia nigra, amygdala. In most cases, protein tau deposits CC are found in glial cells and/or neurons. CC -!- DISEASE: Defects in MAPT are a cause of pallido-ponto-nigral CC degeneration (PPND) [MIM:168610]. The clinical features include CC ocular motility abnormalities, dystonia and urinary incontinence, CC beside progressive parkinsonism and dementia. CC -!- DISEASE: Defects in MAPT are a cause of corticobasal degeneration CC (CBD). It is marked by extrapyramidal signs and apraxia and can be CC associated with memory loss. Neuropathologic features may overlap CC Alzheimer's disease, progressive supranuclear palsy, and CC Parkinson's disease. CC -!- DISEASE: Defects in MAPT may predispose to progressive CC supranuclear palsy (PSP) [MIM:601104]; also known as steele- CC richardson-olszewski syndrome. It is characterized by akinetic- CC rigid syndrome, supranuclear gaze palsy, pyramidal tract CC dysfunction, pseudobulbar signs and cognitive capacities CC deterioration. Neurofibrillary tangles and gliosis but no amyloid CC plaques are found in diseased brains. CC -!- DISEASE: Defects in MAPT may be a cause of hereditary dysphasic CC disinhibition dementia (HDDD) [MIM:607485], a frontotemporal CC dementia characterized by progressive cognitive deficits with CC memory loss and personality changes, severe dysphasic disturbances CC leading to mutism, and hyperphagia. CC -!- SIMILARITY: Contains 4 Tau/MAP repeats. CC -!- WEB RESOURCE: Name=HotMolecBase; Note=Tau entry; CC URL="http://bioinformatics.weizmann.ac.il/hotmolecbase/entries/tau.htm"; CC -!- WEB RESOURCE: Name=Alzheimer Research Forum; Note=Tau mutations; CC URL="http://www.alzforum.org/res/com/mut/tau/default.asp"; CC -!- 100% SWISS-PROT IDENTITY: Q8X251. CC -!- INTERACTION: CC Q9H074:dkfzp586c051; NbExp=3; IntAct=EBI-81531, EBI-81519; CC Q04637:EIF4G1; NbExp=1; IntAct=EBI-81531, EBI-73711; CC -!- INTERACTION: CC Q8NI08:-; NbExp=1; IntAct=EBI-80809, EBI-80799; CC Q9Y618:ncor2; NbExp=1; IntAct=EBI-80809, EBI-80830; CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-123485, EBI-123485; CC Q9W158:cg4612; NbExp=1; IntAct=EBI-123485, EBI-89895; CC Q9VYI0:fne; NbExp=1; IntAct=EBI-123485, EBI-126770; CC -!- INTERACTION: CC Q8C1S0:2410018m14rik (xeno); NbExp=1; IntAct=EBI-394562, EBI-398761; CC Q15528:surf5; NbExp=1; IntAct=EBI-394562, EBI-394687; CC Q9CQI9:thrap6 (xeno); NbExp=1; IntAct=EBI-394562, EBI-309220; CC -!- INTERACTION: CC P13607:atp-alpha; NbExp=1; IntAct=EBI-126914, EBI-213208; CC P11450:fcp3c; NbExp=1; IntAct=EBI-126914, EBI-159556; DR EMBL; AF047863; AAC04277.1; -. DR EMBL; AF027491; AAC04277.1; JOINED. DR EMBL; AF047856; AAC04277.1; JOINED. DR EMBL; AF047857; AAC04277.1; JOINED. DR EMBL; AF027492; AAC04277.1; JOINED. DR EMBL; AF047858; AAC04277.1; JOINED. DR EMBL; AF027493; AAC04277.1; JOINED. DR EMBL; AF047859; AAC04277.1; JOINED. DR EMBL; AF047860; AAC04277.1; JOINED. DR EMBL; AF047862; AAC04277.1; JOINED. DR EMBL; AF027494; AAC04277.1; JOINED. DR EMBL; AF027495; AAC04277.1; JOINED. DR EMBL; AF027496; AAC04277.1; JOINED. DR EMBL; J03778; AAA60615.1; -. DR EMBL; X14474; CAA32636.1; -. DR EMBL; AF027491; AAC04279.1; -. DR EMBL; AF047856; AAC04279.1; JOINED. DR EMBL; AF047857; AAC04279.1; JOINED. DR EMBL; AF027492; AAC04279.1; JOINED. DR EMBL; AF027493; AAC04279.1; JOINED. DR EMBL; AF047860; AAC04279.1; JOINED. DR EMBL; AF047862; AAC04279.1; JOINED. DR EMBL; AF027494; AAC04279.1; JOINED. DR EMBL; AF027495; AAC04279.1; JOINED. DR EMBL; AF027496; AAC04279.1; JOINED. DR EMBL; AF047863; AAC04279.1; JOINED. DR EMBL; AF027491; AAC04278.1; -. DR EMBL; AF027492; AAC04278.1; JOINED. DR EMBL; AF027493; AAC04278.1; JOINED. DR EMBL; AF047860; AAC04278.1; JOINED. DR EMBL; AF047862; AAC04278.1; JOINED. DR EMBL; AF027495; AAC04278.1; JOINED. DR EMBL; AF027496; AAC04278.1; JOINED. DR EMBL; AF047863; AAC04278.1; JOINED. DR EMBL; BC000558; AAH00558.1; -. DR EMBL; M25298; AAA57264.1; -. DR PIR; I52232; I52232. DR PIR; JS0370; QRHUT1. DR PDB; 1I8H; NMR; A=541-553. DR HGNC; HGNC:6893; MAPT. DR MIM; 157140; -. DR MIM; 168610; -. DR MIM; 172700; -. DR MIM; 600274; -. DR MIM; 601104; -. DR MIM; 607485; -. DR GO; GO:0030424; C:axon; NAS. DR GO; GO:0005829; C:cytosol; TAS. DR GO; GO:0005875; C:microtubule associated complex; TAS. DR GO; GO:0005886; C:plasma membrane; TAS. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS. DR GO; GO:0007026; P:microtubule stabilization; NAS. DR InterPro; IPR002955; Tau_protein. DR InterPro; IPR001084; Tubulin_Tau. DR Pfam; PF00418; Tubulin-binding; 4. DR PRINTS; PR01261; TAUPROTEIN. ** PRINTS; PR01217; PRICHEXTENSN; FALSE_POS_1. DR PROSITE; PS00229; TAU_MAP; 4. KW 3D-structure; Acetylation; Alternative splicing; Alzheimer's disease; KW Cytoskeleton; Direct protein sequencing; Disease mutation; KW Glycoprotein; Microtubule; Phosphorylation; Polymorphism; Repeat. FT INIT_MET 0 0 FT REPEAT 560 590 Tau/MAP motif 1. FT REPEAT 591 621 Tau/MAP motif 2. FT REPEAT 622 652 Tau/MAP motif 3. FT REPEAT 653 684 Tau/MAP motif 4. FT MOD_RES 1 1 N-acetylalanine. FT MOD_RES 45 45 Phosphoserine (by PDPK) (partial). FT MOD_RES 49 49 Phosphothreonine (by PDPK) (partial). FT MOD_RES 469 469 Phosphothreonine (by PDPK) (partial). FT MOD_RES 483 483 Deamidated asparagine (in form Tau and FT form PHF-Tau) (partial). FT MOD_RES 491 491 Phosphothreonine (by PDPK) (partial). FT MOD_RES 497 497 Phosphothreonine (by PDPK) (partial). FT MOD_RES 514 514 Phosphoserine (by PDPK) (partial). FT MOD_RES 515 515 Phosphoserine (by PDPK) (partial). FT MOD_RES 518 518 Phosphoserine (by PDPK) (partial). FT MOD_RES 521 521 Phosphothreonine (by PDPK) (partial). FT MOD_RES 528 528 Phosphothreonine (by PDPK) (partial). FT MOD_RES 530 530 Phosphoserine (by PKA) (partial). FT MOD_RES 533 533 Phosphothreonine (by PDPK) (partial). FT MOD_RES 547 547 Phosphothreonine (by PDPK) (partial). FT MOD_RES 551 551 Phosphoserine (by PDPK) (partial). FT MOD_RES 578 578 Phosphoserine (by MARK1). FT MOD_RES 595 595 Deamidated asparagine (in form Tau and FT form PHF-Tau) (partial). FT MOD_RES 609 609 Phosphoserine (by MARK1) (in PHF-tau). FT MOD_RES 621 621 Phosphoserine (by MARK1) (in PHF-tau). FT MOD_RES 640 640 Phosphoserine (by MARK1) (in PHF-tau). FT MOD_RES 672 672 Phosphoserine (by MARK1) (in PHF-tau). FT MOD_RES 712 712 Phosphoserine (by PDPK) (partial). FT MOD_RES 720 720 Phosphoserine (by PDPK) (partial). FT MOD_RES 725 725 Phosphoserine (Potential). FT MOD_RES 729 729 Phosphoserine (Potential). FT MOD_RES 732 732 Phosphoserine (by CaMK2). FT MOD_RES 738 738 Phosphoserine (by PDPK) (partial). FT CARBOHYD 86 86 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 382 382 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 466 466 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 479 479 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 490 490 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 541 541 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 550 550 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 575 575 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 596 596 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 597 597 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 663 663 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 669 669 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 685 685 N-linked (Glc) (glycation); in PHF-tau. FT DISULFID 607 638 By similarity. FT VAR_SEQ 1 43 AEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAG FT LK -> LRALQQRKR (in isoform Fetal-tau). FT /FTId=VSP_003175. FT VAR_SEQ 44 72 Missing (in isoform Tau-A, isoform Tau-D FT and isoform Fetal-tau). FT /FTId=VSP_003176. FT VAR_SEQ 73 101 Missing (in isoform Tau-A, isoform Tau-B, FT isoform Tau-D, isoform Tau-E and isoform FT Fetal-tau). FT /FTId=VSP_003177. FT VAR_SEQ 102 103 Missing (in isoform Fetal-tau). FT /FTId=VSP_003178. FT VAR_SEQ 124 374 Missing (in isoform Tau-A, isoform Tau-B, FT isoform Tau-C, isoform Tau-D, isoform FT Tau-E, isoform Tau-F and isoform Fetal- FT tau). FT /FTId=VSP_003179. FT VAR_SEQ 394 459 Missing (in isoform Tau-A, isoform Tau-B, FT isoform Tau-C, isoform Tau-D, isoform FT Tau-E, isoform Tau-F and isoform Fetal- FT tau). FT /FTId=VSP_003180. FT VAR_SEQ 591 621 Missing (in isoform Tau-A, isoform Tau-B, FT isoform Tau-C and isoform Fetal-tau). FT /FTId=VSP_003181. FT VARIANT 284 284 D -> N (risk factor for progressive FT supranuclear palsy). FT /FTId=VAR_010340. FT VARIANT 288 288 V -> A (risk factor for progressive FT supranuclear palsy). FT /FTId=VAR_010341. FT VARIANT 440 440 H -> Y. FT /FTId=VAR_010342. FT VARIANT 446 446 S -> P. FT /FTId=VAR_010343. FT VARIANT 573 573 K -> T (in a dementia resembling Pick's FT disease). FT /FTId=VAR_010344. FT VARIANT 588 588 G -> V (in FTDP17). FT /FTId=VAR_010345. FT VARIANT 595 595 N -> K (in PPND). FT /FTId=VAR_010346. FT VARIANT 596 596 Missing (in FTDP17). FT /FTId=VAR_010347. FT VARIANT 617 617 P -> L (in FTDP17; most common mutation; FT reduction in the ability to promote FT microtubule assembly; accelerated FT aggregation of Tau into filaments). FT /FTId=VAR_010348. FT VARIANT 617 617 P -> S (in FTDP17 and in CBD; reduction FT in the ability to promote microtubule FT assembly). FT /FTId=VAR_010349. FT VARIANT 621 621 S -> N (in FTDP17; minimal parkinsonism; FT very early age of onset). FT /FTId=VAR_010350. FT VARIANT 653 653 V -> M (in FTDP17; ultrastructural and FT biochemical characteristics FT indistinguishable from Alzheimer's FT disease; accelerated aggregation of Tau FT into filaments). FT /FTId=VAR_010351. FT VARIANT 705 705 G -> R (in FTDP17; in a dementia FT resembling Pick's disease). FT /FTId=VAR_010352. FT VARIANT 722 722 R -> W (in FTDP17; accelerated FT aggregation of Tau into filaments). FT /FTId=VAR_010353. FT MUTAGEN 514 514 S->E: No association with plasma FT membrane. FT MUTAGEN 515 515 S->E: No association with plasma FT membrane. FT MUTAGEN 518 518 S->E: No association with plasma FT membrane. FT MUTAGEN 530 530 S->A: No decrease in microtubule-binding FT and nucleation activity after in vitro FT phosphorylation of mutant protein. FT MUTAGEN 547 547 T->A: 50% Decrease in microtubule-binding FT after in vitro phosphorylation of mutant FT protein. FT MUTAGEN 547 547 T->E: No association with plasma FT membrane. FT MUTAGEN 551 551 S->A: 70% decrease in microtubule-binding FT after in vitro phosphorylation of mutant FT protein. FT MUTAGEN 551 551 S->E: No association with plasma FT membrane. FT MUTAGEN 573 573 K->T: Reduced ability to promote FT microtubule assembly. FT MUTAGEN 578 578 S->A: 8% decrease in microtubule-binding FT after in vitro phosphorylation of mutant FT protein. FT MUTAGEN 712 712 S->E: No association with plasma FT membrane. FT MUTAGEN 720 720 S->E: No association with plasma FT membrane. FT MUTAGEN 725 725 S->E: No association with plasma FT membrane. FT MUTAGEN 729 729 S->E: No association with plasma FT membrane. FT MUTAGEN 738 738 S->E: No association with plasma FT membrane. ** ** ################# INTERNAL SECTION ################## **CL 17q21.1; **IS P10636-9 **ZC EMBL; BC000558; AAH00558.1; -. 11-05-2003 SQ SEQUENCE 757 AA; 78746 MW; 1426CEB011C1CC73 CRC64; AEPRQEFEVM EDHAGTYGLG DRKDQGGYTM HQDQEGDTDA GLKESPLQTP TEDGSEEPGS ETSDAKSTPT AEDVTAPLVD EGAPGKQAAA QPHTEIPEGT TAEEAGIGDT PSLEDEAAGH VTQEPESGKV VQEGFLREPG PPGLSHQLMS GMPGAPLLPE GPREATRQPS GTGPEDTEGG RHAPELLKHQ LLGDLHQEGP PLKGAGGKER PGSKEEVDED RDVDESSPQD SPPSKASPAQ DGRPPQTAAR EATSIPGFPA EGAIPLPVDF LSKVSTEIPA SEPDGPSVGR AKGQDAPLEF TFHVEITPNV QKEQAHSEEH LGRAAFPGAP GEGPEARGPS LGEDTKEADL PEPSEKQPAA APRGKPVSRV PQLKARMVSK SKDGTGSDDK KAKTSTRSSA KTLKNRPCLS PKLPTPGSSD PLIQPSSPAV CPEPPSSPKH VSSVTSRTGS SGAKEMKLKG ADGKTKIATP RGAAPPGQKG QANATRIPAK TPPAPKTPPS SGEPPKSGDR SGYSSPGSPG TPGSRSRTPS LPTPPTREPK KVAVVRTPPK SPSSAKSRLQ TAPVPMPDLK NVKSKIGSTE NLKHQPGGGK VQIINKKLDL SNVQSKCGSK DNIKHVPGGG SVQIVYKPVD LSKVTSKCGS LGNIHHKPGG GQVEVKSEKL DFKDRVQSKI GSLDNITHVP GGGNKKIETH KLTFRENAKA KTDHGAEIVY KSPVVSGDTS PRHLSNVSST GSIDMVDSPQ LATLADEVSA SLAKQGL // ID ZEA1_MAIZE STANDARD; PRT; 234 AA. AC P02859; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone A30). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=82081837; PubMed=6895552; RA Geraghty D., Peifer M.A., Rubenstein I., Messing J.; RT "The primary structure of a plant storage protein: zein."; RL Nucleic Acids Res. 9:5163-5174(1981). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=84207882; PubMed=6233138; RA Hu N.T., Peifer M.A., Heidecker G., Messing J., Rubenstein I.; RT "Primary structure of a genomic zein sequence of maize."; RL EMBO J. 1:1337-1342(1982). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 19 kDa and 19 kDa zeins are composed CC of nine adjacent, topologically antiparallel helices clustered CC within a distorted cylinder. CC -!- SIMILARITY: Belongs to the zein family. DR EMBL; V01481; CAA24728.1; -; mRNA. DR EMBL; V01481; CAA24728.1; -; mRNA.{EP1} DR PIR; A90967; ZIZM3. DR MaizeGDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Multigene family; Repeat; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 21 FT CHAIN 22 234 Zein-alpha. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 234 AA; 25404 MW; 502A99D438CA5DAA CRC64; MAAKIFCLLM LLGLSASAAT ATIFPQCSQA PIASLLPPYL SPAVSSVCEN PILQPYRIQQ AIAAGILPLS PLFLQQSSAL LQQLPLVHLL AQNIRAQQLQ QLVLANLAAY SQQQQFLPFN QLAALNSASY LQQQQLPFSQ LPAAYPQQFL PFNQLAALNS PAYLQQQQLL PFSQLAGVSP ATFLTQPQLL PFYQHAAPNA GTLLQLQQLL PFNQLALTNL AAFYQQPIIG GALF // ID ENTK_HUMAN Reviewed; 1019 AA. AC P98073; Q2NKL7; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 22-JUL-2008, entry version 94. DE RecName: Full=Enteropeptidase; DE EC=3.4.21.9; DE AltName: Full=Enterokinase; DE AltName: Full=Serine protease 7; DE Contains: DE RecName: Full=Enteropeptidase non-catalytic heavy chain; DE Contains: DE RecName: Full=Enteropeptidase catalytic light chain; DE Flags: Precursor; GN Name=PRSS7; Synonyms=ENTK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Duodenum; RX MEDLINE=95234679; PubMed=7718557; DOI=10.1021/bi00014a008; RA Kitamoto Y., Veile R.A., Donis-Keller H., Sadler J.E.; RT "cDNA sequence and chromosomal localization of human enterokinase, the RT proteolytic activator of trypsinogen."; RL Biochemistry 34:4562-4568(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN ENTEROKINASE RP DEFICIENCY. RX MEDLINE=21606074; PubMed=11719902; DOI=10.1086/338456; RA Holzinger A., Maier E.M., Buck C., Mayerhofer P.U., Kappler M., RA Haworth J.C., Moroz S.P., Hadorn H.-B., Sadler J.E., Roscher A.A.; RT "Mutations in the proenteropeptidase gene are the molecular cause of RT congenital enteropeptidase deficiency."; RL Am. J. Hum. Genet. 70:20-25(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-134 RP AND PRO-732. RX MEDLINE=20289799; PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., RA Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 749-1019. RC TISSUE=Duodenum; RX MEDLINE=94329561; PubMed=8052624; RA Kitamoto Y., Yuan X., Wu Q., McCourt D.W., Sadler J.E.; RT "Enterokinase, the initiator of intestinal digestion, is a mosaic RT protease composed of a distinctive assortment of domains."; RL Proc. Natl. Acad. Sci. U.S.A. 91:7588-7592(1994). CC -!- FUNCTION: Responsible for initiating activation of pancreatic CC proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase CC A). It catalyzes the conversion of trypsinogen to trypsin which in CC turn activates other proenzymes including chymotrypsinogen, CC procarboxypeptidases, and proelastases. CC -!- CATALYTIC ACTIVITY: Activation of trypsinogen by selective CC cleavage of 6-Lys-|-Ile-7 bond. CC -!- SUBUNIT: Heterodimer of a catalytic (light) chain and a CC multidomain (heavy) chain linked by a disulfide bond. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (Probable). CC -!- TISSUE SPECIFICITY: Intestinal brush border. CC -!- PTM: The chains are derived from a single precursor that is CC cleaved by a trypsin-like protease. CC -!- DISEASE: Defects in PRSS7 are a cause of enterokinase deficiency CC [MIM:226200]; a life-threatening intestinal malabsorption disorder CC characterized by diarrhea and failure to thrive. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC -!- SIMILARITY: Contains 2 CUB domains. CC -!- SIMILARITY: Contains 2 LDL-receptor class A domains. CC -!- SIMILARITY: Contains 1 MAM domain. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC -!- SIMILARITY: Contains 1 SEA domain. CC -!- SIMILARITY: Contains 1 SRCR domain. DR EMBL; U09860; AAC50138.1; -; mRNA. DR EMBL; Y19124; CAB65555.1; -; Genomic_DNA. DR EMBL; Y19125; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19126; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19127; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19128; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19129; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19130; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19131; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19132; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19133; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19134; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19135; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19136; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19137; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19138; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19139; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19140; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19141; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19142; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19143; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; AL163218; CAB90392.1; -; Genomic_DNA. DR EMBL; AL163217; CAB90389.1; -; Genomic_DNA. DR EMBL; BC111749; AAI11750.1; -; mRNA. DR PIR; A56318; A56318. DR RefSeq; NP_002763.1; -. DR UniGene; Hs.149473; -. DR SMR; P98073; 785-1019. DR MEROPS; S01.156; -. DR Ensembl; ENSG00000154646; Homo sapiens. DR GeneID; 5651; -. DR KEGG; hsa:5651; -. DR H-InvDB; HIX0040924; -. DR HGNC; HGNC:9490; PRSS7. DR HPA; HPA015611; -. DR MIM; 226200; phenotype. DR MIM; 606635; gene. DR PharmGKB; PA33839; -. DR HOGENOM; P98073; -. DR HOVERGEN; P98073; -. DR CleanEx; HS_PRSS7; -. DR GO; GO:0005903; C:brush border; TAS:ProtInc. DR Gene3D; G3DSA:2.60.120.290; CUB; 2. DR Gene3D; G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 1. DR InterPro; IPR000859; CUB. DR InterPro; IPR002172; LDL_rcpt_classA_cys-rich. DR InterPro; IPR000998; MAM. DR InterPro; IPR011163; Pept_S1A_enterop. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR000082; SEA. DR InterPro; IPR001190; Srcr_rcpt. DR InterPro; IPR017448; Srcr_rcpt-rel. DR Pfam; PF00431; CUB; 2. DR Pfam; PF00057; Ldl_recept_a; 2. DR Pfam; PF00629; MAM; 1. DR Pfam; PF01390; SEA; 1. DR Pfam; PF00530; SRCR; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001138; Enteropeptidase; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00261; LDLRECEPTOR. DR PRINTS; PR00020; MAMDOMAIN. DR SMART; SM00042; CUB; 2. DR SMART; SM00192; LDLa; 2. DR SMART; SM00137; MAM; 1. DR SMART; SM00200; SEA; 1. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS01180; CUB; 2. DR PROSITE; PS01209; LDLRA_1; 2. DR PROSITE; PS50068; LDLRA_2; 2. DR PROSITE; PS00740; MAM_1; 1. DR PROSITE; PS50060; MAM_2; 1. DR PROSITE; PS50024; SEA; 1. DR PROSITE; PS00420; SRCR_1; FALSE_NEG. DR PROSITE; PS50287; SRCR_2; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. DR HSSP; P98072; 1EKB. DR LinkHub; P98073; -. DR ArrayExpress; P98073; -. DR GermOnline; ENSG00000154646; Homo sapiens. PE 2: Evidence at transcript level; KW Glycoprotein; Hydrolase; Lipoprotein; Membrane; Myristate; KW Polymorphism; Protease; Repeat; Serine protease; Signal-anchor; KW Transmembrane; Zymogen. FT CHAIN 1 784 Enteropeptidase non-catalytic heavy FT chain. FT /FTId=PRO_0000027719. FT CHAIN 785 1019 Enteropeptidase catalytic light chain. FT /FTId=PRO_0000027720. FT TOPO_DOM 1 18 Cytoplasmic (Potential). FT TRANSMEM 19 47 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 48 1019 Extracellular (Potential). FT DOMAIN 52 169 SEA. FT DOMAIN 182 223 LDL-receptor class A 1. FT DOMAIN 225 334 CUB 1. FT DOMAIN 342 504 MAM. FT DOMAIN 524 634 CUB 2. FT DOMAIN 641 679 LDL-receptor class A 2. FT DOMAIN 678 771 SRCR. FT DOMAIN 785 1019 Peptidase S1. FT ACT_SITE 825 825 Charge relay system (By similarity). FT ACT_SITE 876 876 Charge relay system (By similarity). FT ACT_SITE 971 971 Charge relay system (By similarity). FT LIPID 2 2 N-myristoyl glycine (Potential). FT CARBOHYD 116 116 N-linked (GlcNAc...) (Potential). FT CARBOHYD 147 147 N-linked (GlcNAc...) (Potential). FT CARBOHYD 179 179 N-linked (GlcNAc...) (Potential). FT CARBOHYD 328 328 N-linked (GlcNAc...) (Potential). FT CARBOHYD 335 335 N-linked (GlcNAc...) (Potential). FT CARBOHYD 388 388 N-linked (GlcNAc...) (Potential). FT CARBOHYD 440 440 N-linked (GlcNAc...) (Potential). FT CARBOHYD 470 470 N-linked (GlcNAc...) (Potential). FT CARBOHYD 503 503 N-linked (GlcNAc...) (Potential). FT CARBOHYD 534 534 N-linked (GlcNAc...) (Potential). FT CARBOHYD 630 630 N-linked (GlcNAc...) (Potential). FT CARBOHYD 682 682 N-linked (GlcNAc...) (Potential). FT CARBOHYD 706 706 N-linked (GlcNAc...) (Potential). FT CARBOHYD 725 725 N-linked (GlcNAc...) (Potential). FT CARBOHYD 848 848 N-linked (GlcNAc...) (Potential). FT CARBOHYD 887 887 N-linked (GlcNAc...) (Potential). FT CARBOHYD 909 909 N-linked (GlcNAc...) (Potential). FT CARBOHYD 949 949 N-linked (GlcNAc...) (Potential). FT DISULFID 184 197 By similarity. FT DISULFID 191 210 By similarity. FT DISULFID 204 221 By similarity. FT DISULFID 225 253 By similarity. FT DISULFID 524 552 By similarity. FT DISULFID 643 655 By similarity. FT DISULFID 650 668 By similarity. FT DISULFID 662 677 By similarity. FT DISULFID 757 767 By similarity. FT DISULFID 772 896 Interchain (between heavy and light FT chains) (By similarity). FT DISULFID 810 826 By similarity. FT DISULFID 910 977 By similarity. FT DISULFID 941 956 By similarity. FT DISULFID 967 995 By similarity. FT VARIANT 65 65 T -> I (in dbSNP:rs35987974). FT /FTId=VAR_031686. FT VARIANT 77 77 K -> R (in dbSNP:rs2824804). FT /FTId=VAR_021940. FT VARIANT 134 134 Q -> E (in dbSNP:rs2824790). FT /FTId=VAR_031687. FT VARIANT 545 545 S -> C (in dbSNP:rs8134187). FT /FTId=VAR_031688. FT VARIANT 641 641 E -> K (in dbSNP:rs2273204). FT /FTId=VAR_020175. FT VARIANT 660 660 N -> H (in dbSNP:rs11088674). FT /FTId=VAR_024292. FT VARIANT 732 732 S -> P (in dbSNP:rs2824721). FT /FTId=VAR_031689. FT VARIANT 828 828 Y -> C (in dbSNP:rs8130110). FT /FTId=VAR_031690. FT CONFLICT 754 771 SQQCLQDSLIRLQCNHKS -> RRNAKNEIDALSPIILIA FT (in Ref. 3; CAB90389). ** ** ################# INTERNAL SECTION ################## **CL 21q21.1; **YY VAR_031687: AA shown in Swiss-Prot is the most frequent; 19-MAR-2007. **YY VAR_031688: AA shown in Swiss-Prot is the most frequent; 19-MAR-2007. **ZB NAG, 23-Mar-2007; SQ SEQUENCE 1019 AA; 112924 MW; B6AAA245F6D4A563 CRC64; MGSKRGISSR HHSLSSYEIM FAALFAILVV LCAGLIAVSC LTIKESQRGA ALGQSHEARA TFKITSGVTY NPNLQDKLSV DFKVLAFDLQ QMIDEIFLSS NLKNEYKNSR VLQFENGSII VVFDLFFAQW VSDQNVKEEL IQGLEANKSS QLVTFHIDLN SVDILDKLTT TSHLATPGNV SIECLPGSSP CTDALTCIKA DLFCDGEVNC PDGSDEDNKM CATVCDGRFL LTGSSGSFQA THYPKPSETS VVCQWIIRVN QGLSIKLSFD DFNTYYTDIL DIYEGVGSSK ILRASIWETN PGTIRIFSNQ VTATFLIESD ESDYVGFNAT YTAFNSSELN NYEKINCNFE DGFCFWVQDL NDDNEWERIQ GSTFSPFTGP NFDHTFGNAS GFYISTPTGP GGRQERVGLL SLPLDPTLEP ACLSFWYHMY GENVHKLSIN ISNDQNMEKT VFQKEGNYGD NWNYGQVTLN ETVKFKVAFN AFKNKILSDI ALDDISLTYG ICNGSLYPEP TLVPTPPPEL PTDCGGPFEL WEPNTTFSST NFPNSYPNLA FCVWILNAQK GKNIQLHFQE FDLENINDVV EIRDGEEADS LLLAVYTGPG PVKDVFSTTN RMTVLLITND VLARGGFKAN FTTGYHLGIP EPCKADHFQC KNGECVPLVN LCDGHLHCED GSDEADCVRF FNGTTNNNGL VRFRIQSIWH TACAENWTTQ ISNDVCQLLG LGSGNSSKPI FSTDGGPFVK LNTAPDGHLI LTPSQQCLQD SLIRLQCNHK SCGKKLAAQD ITPKIVGGSN AKEGAWPWVV GLYYGGRLLC GASLVSSDWL VSAAHCVYGR NLEPSKWTAI LGLHMKSNLT SPQTVPRLID EIVINPHYNR RRKDNDIAMM HLEFKVNYTD YIQPICLPEE NQVFPPGRNC SIAGWGTVVY QGTTANILQE ADVPLLSNER CQQQMPEYNI TENMICAGYE EGGIDSCQGD SGGPLMCQEN NRWFLAGVTS FGYKCALPNR PGVYARVSRF TEWIQSFLH // ID Q27861_9HYMN Unreviewed; 41 AA. AC Q27861; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 22-JUL-2008, entry version 32. DE SubName: Full=Histone H3{EI1}; DE EC=3.4.21.9; DE AltName: Full=Enterokinase{EI5}; DE Flags: Precursor{EI7}; Fragment{EI8}; GN Name=histone H3II{EI1}; OS Tetrahymena hegewischi. OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae; OC Tetrahymena. OX NCBI_TaxID=5923{EI1}; RN [1]{EI1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KP7{EI1}; RX MEDLINE=92203991; PubMed=1552842; RA Sadler L.A., Brunk C.F.; RT "Phylogenetic relationships and unusual diversity in histone H4 RT proteins within the Tetrahymena pyriformis complex."; RL Mol. Biol. Evol. 9:70-84(1992). CC -!- SIMILARITY: Belongs to the histone H3 family{EA4}. DR EMBL; M73210; AAA75643.1; -; Genomic_DNA.{EI1} DR GO; GO:0000786; C:nucleosome; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro. DR Gene3D; G3DSA:1.10.20.10; Histone-fold; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR000164; Histone_H3. DR PANTHER; PTHR11426; Histone_H3; 1. DR PRINTS; PR00622; HISTONEH3. DR PROSITE; PS00322; HISTONE_H3_1; UNKNOWN_1. PE 3: Inferred from homology; FT NON_TER 41 41 {EI1} ** ** ################# INTERNAL SECTION ################## **EV EA4; Rulebase; TREMBL; RU004194V0.230S0031185; 11-MAR-2008. **EV EI1; EMBL; -; AAA75643.1; 23-APR-2004. **PM Gene3D; G3DSA:1.10.20.10; Histone-fold; 2; 40; T; 16-NOV-2006; **PM PANTHER; PTHR11426; Histone_H3; 1; 40; T; 27-APR-2007; **PM PRINTS; PR00622; HISTONEH3; 17; 31; T; 30-SEP-2005; **PM PRINTS; PR00622; HISTONEH3; 34; 41; T; 30-SEP-2005; **PM PRINTS; PR00622; HISTONEH3; 3; 17; T; 30-SEP-2005; **PM PROSITE; PS00322; HISTONE_H3_1; 15; 21; ?; 07-OCT-2007; SQ SEQUENCE 41 AA; 4316 MW; E343DF37507B58D9 CRC64; MARTKQTARK STGAKAPRKQ LASKAARKSA PATGGIKKPH E // ID CAPSD_PCV2 Reviewed; 233 AA. AC O56129; Q8BB11; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 05-APR-2011, entry version 41. DE RecName: Full=Capsid protein; GN Name=Cap; ORFNames=ORF2; OS Porcine circovirus 2 (PCV2). OC Viruses; ssDNA viruses; Circoviridae; Circovirus. OX NCBI_TaxID=85708; OH NCBI_TaxID=9823; Sus scrofa (Pig). DR EMBL; AF027217; AAC59463.1; -; Genomic_DNA. DR EMBL; AY094619; AAM21849.1; -; Genomic_DNA. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW. DR InterPro; IPR003383; Circovirus_ORF2_capsid. DR Pfam; PF02443; Circo_capsid; 1. PE 1: Evidence at protein level; KW Capsid protein; KW Clathrin- and caveolin-independent endocytosis of virus by host; KW Complete proteome; DNA-binding; Host nucleus; Host-virus interaction; KW Initiation of viral infection; T=1 icosahedral capsid protein; KW Viral attachment to host cell; Viral penetration into host cytoplasm; KW Viral penetration into host nucleus; Virion; KW Virus endocytosis by host. FT CHAIN 1 233 Capsid protein. FT /FTId=PRO_0000133085. ** ** ################# INTERNAL SECTION ################## **ZA PHL, 07-SEP-2005; **ZB CHH, 25-MAY-2009; CHH, 25-JAN-2011; CHH, 14-MAR-2011; SQ SEQUENCE 233 AA; 27897 MW; 3C664C4B4E83AB58 CRC64; MTYPRRRYRR RRHRPRSHLG QILRRRPWLV HPRHRYRWRR KNGIFNTRLS RTFGYTVKAT TVRTPSWAVD MMRFNIDDFV PPGGGTNKIS IPFEYYRIRK VKVEFWPCSP ITQGDRGVGS TAVILDDNFV TKATALTYDP YVNYSSRHTI PQPFSYHSRY FTPKPVLDST IDYFQPNNKR TQLWLRLQTS RNVDHVGLGT AFENSIYDQD YNIRVTMYVQ FREFNLKDPP LKP // ID PCLO_RAT Reviewed; 1380 AA. AC Q9JKS6; Q9JLT1; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 108. DE RecName: Full=Protein piccolo {ECO:0000269|PubMed:11285225}; DE AltName: Full=Aczonin; DE AltName: Full=Multidomain presynaptic cytomatrix protein; GN Name=vcp {ECO:0000313|EMBL:AAH50488.1, GN ECO:0000313|ZFIN:ZDB-GENE-030131-5408}; Synonyms=cdc48; GN ORFNames=si:ch211-113n10.2; OG Plasmid pCP301 {ECO:0000313|EMBL:AAH50488.1, OG ECO:0000269|PubMed:11285225}, Plasmid pWR100, Plasmid pINV_F6_M1382, OG and Plasmid pSF5; Chloroplast. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] {ECO:0000269|PubMed:11285225} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH RABAC1. RX PubMed=10707984; DOI=10.1016/S0896-6273(00)80883-1; RA Fenster S.D., Chung W.J., Zhai R., Cases-Langhoff C., Voss B., RA Garner A.M., Kaempf U., Kindler S., Gundelfinger E.D., Garner C.C.; RT "Piccolo, a presynaptic zinc finger protein structurally related to RT bassoon."; RL Neuron 25:203-214(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Fenster S.D., Cases-Langhoff C., Gundelfinger E.D., Garner C.C.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May act as a scaffolding protein involved in the CC organization of synaptic active zones and in synaptic vesicle CC trafficking (By similarity). {ECO:0000250|UniProtKB:Q9QYX7}. CC -!- SUBUNIT: Interacts with RABAC1/PRA1, RIMS2 and profilin (By CC similarity). {ECO:0000269|PubMed:10707984}. CC -!- INTERACTION: CC Q920M9:Siah1; NbExp=2; IntAct=EBI-2271602, EBI-957514; CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- SUBCELLULAR LOCATION: Cell junction, synapse. Note=Concentrated at CC presynaptic side of synaptic junctions. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane CC {ECO:0000269|PubMed:12766230, ECO:0000269|Ref.11}; Peripheral CC membrane protein {ECO:0000269|PubMed:12766230, CC ECO:0000269|PubMed:18431481}. Plastid, chloroplast stroma. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9JKS6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9JKS6-2; Sequence=VSP_003930, VSP_003931; CC Name=3; CC IsoId=Q9JKS6-3; Sequence=VSP_018194; CC -!- RNA EDITING: Modified_positions=1, 4, 18, 33 CC {ECO:0000269|PubMed:10707984, ECO:0000269|PubMed:11285225}, 34, CC 72, 80, 86, 95, 121, 123, 154, 155, 156, 163, 169, 193, 196, 233, CC 295, 346; Note=The initiator methionine is created by RNA editing. CC The nonsense codons at positions 72, 121, 169, 193 and 346 are CC modified to sense codons. {ECO:0000269|PubMed:10707984}; CC -!- RNA EDITING: Modified_positions=Not_applicable; Note=a; CC -!- DOMAIN: C2 domain 1 is involved in binding calcium and CC phospholipids. Calcium binds with low affinity but with high CC specificity and induces a large conformational change. CC {ECO:0000269|PubMed:11285225}. CC -!- DISEASE: Spastic paraplegia 4, autosomal dominant (SPG4) CC [MIM:182601]: A form of spastic paraplegia, a neurodegenerative CC disorder characterized by a slow, gradual, progressive weakness CC and spasticity of the lower limbs. Rate of progression and the CC severity of symptoms are quite variable. Initial symptoms may CC include difficulty with balance, weakness and stiffness in the CC legs, muscle spasms, and dragging the toes when walking. In some CC forms of the disorder, bladder symptoms (such as incontinence) may CC appear, or the weakness and stiffness may spread to other parts of CC the body. {ECO:0000269|PubMed:10610178, CC ECO:0000269|PubMed:10699187, ECO:0000269|PubMed:11015453, CC ECO:0000269|PubMed:11039577, ECO:0000269|PubMed:11087788, CC ECO:0000269|PubMed:11309678, ECO:0000269|PubMed:11843700, CC ECO:0000269|PubMed:11985387, ECO:0000269|PubMed:12124993, CC ECO:0000269|PubMed:12161613, ECO:0000269|PubMed:12163196, CC ECO:0000269|PubMed:12202986, ECO:0000269|PubMed:12460147, CC ECO:0000269|PubMed:12552568, ECO:0000269|PubMed:12939659, CC ECO:0000269|PubMed:14732620, ECO:0000269|PubMed:15159500, CC ECO:0000269|PubMed:15210521, ECO:0000269|PubMed:15248095, CC ECO:0000269|PubMed:15326248, ECO:0000269|PubMed:15482961, CC ECO:0000269|PubMed:16682546, ECO:0000269|PubMed:16684598, CC ECO:0000269|PubMed:17594340, ECO:0000269|PubMed:20214791, CC ECO:0000269|PubMed:20550563, ECO:0000269|PubMed:20562464, CC ECO:0000269|PubMed:20718791, ECO:0000269|PubMed:20932283}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.45 mM for ATP {ECO:0000269|PubMed:15716377, CC ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:22637577}; CC Vmax=1.2 nmol/min/ug enzyme {ECO:0000269|PubMed:15716377, CC ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:22637577}; CC Note=Kinetic parameters shown are for full length enzyme. N- CC terminally truncated spastin (residues 228-616), which has been CC shown to exhibit full severing activity, shows a basal ATP CC turnover rate of 0.78 sec(-1) in the absence of microtubules, a CC KM of 0.16 mM for ATP, and the ATP turnover rate is extrapolated CC to 3.83 sec(-1) in the presence of microtubules. ATPase activity CC shows non-Michaelis-Menten kinetics in the presence of CC microtubules, but is close to non-cooperative behavior in their CC absence (PubMed:22637577). {ECO:0000269|PubMed:15716377, CC ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:22637577}; CC -!- SIMILARITY: Contains 2 C2 domains. {ECO:0000269|PubMed:11285225}. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=This alternative splicing is restricted to C4 species of CC Flaveria. {ECO:0000269|PubMed:7550380, CC ECO:0000269|PubMed:8771790, ECO:0000269|Ref.3}; CC Name=1; Synonyms=Long, Long variant 1; CC IsoId=Q9UBP0-1; Sequence=Displayed; CC Note=No experimental confirmation available. {ECO:0000305}; CC Name=2; Synonyms=Long variant 2; CC IsoId=Q9UBP0-2; Sequence=VSP_000024; CC -!- SEQUENCE CAUTION: CC Sequence=AAH52843.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAI06097.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAC33868.1; Type=Frameshift; Positions=1759; CC -!- RNA EDITING: Modified_positions=207 {ECO:0000269|PubMed:17018572, CC ECO:0000269|Ref.6}; Note=Partially edited. Target of Adar; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Pfam; PF00168; C2; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF05715; zf-piccolo; 2. DR SMART; SM00239; C2; 2. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF49562; SSF49562; 2. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF57903; SSF57903; 2. DR PROSITE; PS50004; C2; 2. DR PROSITE; PS50106; PDZ; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; KW Calcium/phospholipid-binding; Cell junction; Complete proteome; KW Glycoprotein; Metal-binding; Phosphoprotein; Reference proteome; KW Repeat; Synapse; Zinc; Zinc-finger. FT CHAIN 1 5085 Protein piccolo. FT /FTId=PRO_0000058252. FT TRANSIT 1 29 MITOCHONDRION{EC2}. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:22814378}. FT DOMAIN 4442 4536 PDZ.{ECO:0000269|PubMed:11285225}. FT DOMAIN 4653 4752 C2 1. {ECO:0000269|PubMed:11285225}. FT DOMAIN 4968 5059 C2 2. {ECO:0000269|PubMed:11285225}. FT ZN_FING 523 547 C4-type (Potential). FT {ECO:0000269|PubMed:10707984}. FT ZN_FING 1010 1033 C4-type (Potential). FT {ECO:0000269|PubMed:10707984}. FT REGION 372 491 12 X 10 AA tandem approximate repeats of FT P-A-K-P-Q-P-Q-Q-P-X. FT COMPBIAS 2351 2362 Poly-Pro. {ECO:0000269|PubMed:11285225}. FT MOD_RES 3 3 Phosphoserine. FT MOD_RES 1778 1778 Phosphoserine (By similarity). FT MOD_RES 3374 3374 Phosphoserine (By similarity). FT MOD_RES 3392 3392 Phosphothreonine (By similarity). FT CARBOHYD 2702 2702 O-linked (GlcNAc) (By similarity). FT CARBOHYD 2976 2976 O-linked (GlcNAc) (By similarity). FT VAR_SEQ 4687 4695 Missing (in isoform 3). FT /FTId=VSP_018194. FT VAR_SEQ 4876 4880 TKPTN -> SKRRK (in isoform 2). FT {ECO:0000269|PubMed:11285225}. FT /FTId=VSP_003930. FT VAR_SEQ 4881 5085 Missing (in isoform 2). FT {ECO:0000269|PubMed:11285225}. FT /FTId=VSP_003931. FT VARIANT 3 3 A -> L{EC2}. FT /FTId=VAR_000001. FT VARIANT 3 3 A -> LFSJFSHLJSDHFLSJLFHSJLLSJKDHFLSKJFHJ FT . FT VARIANT 23 23 Missing. {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8906617, FT ECO:0000269|PubMed:9009220, FT ECO:0000269|PubMed:9921897}. FT VARIANT 386 386 N -> S (in SPG4). FT MUTAGEN 4668 4668 D->A: Complete loss of calcium-binding FT and calcium-dependent phospholipid FT binding activity. FT {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4674 4674 D->A: Complete loss of calcium-binding FT and calcium-dependent phospholipid FT binding activity. FT {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4688 4689 VM->SS: 10-fold increase in affinity for FT calcium. {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4688 4688 V->S: Small increase in affinity for FT calcium. {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4689 4689 M->S: Increased affinity for calcium. FT {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4690 4691 VV->SS: 10-fold increase in affinity for FT calcium. {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4692 4693 QN->AA: Moderate increase in affinity for FT calcium. {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4694 4694 A->S: No effect on calcium-binding FT activity. {ECO:0000269|PubMed:11285225}. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 1380 AA; 144367 MW; 13497D39F4CE32B8 CRC64; MGNEASLEGE GLPEGLAAAA GAGGSGSALH PGIPAGMEAD LSQLSEEERR QIAAVMSRAQ GLPKGSVPPA AAESPSMHRK QELDSSQAPQ QPGKPPDPGR PTQPGLSKSR TTDTFRSEQK LPGRSPSTIS LKESKSRTDF KEEYKSSMMP GFFSDVNPLS AVSSVVNKFN PFDLISDSEA SQEETTKKQK VVQKEQGKSE GMAKPPLQQP SPKPIPKQQG QVKEVIQQDS SPKSVSSQQA EKVKPQAPGT GKPSQQSPAQ TPAQQASPGK PVAQQPGSAK ATVQQPGPAK SPAQPAGTGK SPAQPPAKTP GQQAGLEKTS SSQQPGPKSL AQTPGHGKFP LGPVKSPAQQ PGTAKHPAQQ PGPQTAAKVP GPTKTPAQQS GPGKTPAQQP GPTKPSPQQP IPAKPQPQQP VATKTQPQQS APAKPQPQQP APAKPQPQQP TPAKPQPQPP TPAKPQPQPP TATKPQPQPP TATKPHHQQP GLAKPSAQQP TKSISQTVTG RPLQPPPTSA AQTPAQGLSK TICPLCNTTE LLLHIPEKAN FNTCTECQST VCSLCGFNPN PHLTEIKEWL CLNCQMQRAL GGDLAAAIPS SPQPTPKAAT APTATASKSP VPSQQASPKK EPPSKQDSPK ALESKKPPEP KKPPEPKKPP EPKKPPPLVK QPTLHGPTPA TAPQLPVAEA LPEPAPPKEP SGPLPEQAKA PVGDVEPKQP KMTETRADIQ SSSTTKPDIL SSQVQSQAQV KTASPLKTDS AKPSQSFPPT GEKTTPLDSK AMPRPASDSK IISQPGPGSE SKDPKHIDPI QKKDEPKKAQ PKGSPKPETK PVPKGSPTPS GTRPTAGQAA PPSQQPPKPQ EQSRRFSLNL GGITDAPKSQ PTTPQETVTG KLFGFGASIF SQASNLISTA GQQGPHPQTG PAAPSKQAPT PSQSPAAQGP AKSTGQLPPA PAKATAVKKE AKAAAAENLE SKPEQAPTAK KTEKDKKPPP AKVGKPPPSE PEKAVPAHKP DKTTKPKPAC PLCRTELNLG SQEPPNFNTC TECKNQVCNL CGFNPTPHLT EIQEWLCLNC QTQRAISGQL GDMGKMPPAP SGPKASPMPA PAEPSSQKTP TGTQVKGKKK EAEGKTEAEK PVPEKETASI EKTPPMVTTD QKLEESEGKK SKVSALPEKK PSEEEKAISA DKKERKPPAE EKPPLEEKKP IPVDKKLPPE AKPLSSEGEE KHEILKAHVQ IPEEEPTGKV AAKAGEEEQQ PDSRPEALPG ATPLTLPKAG EKERAVAQPQ AEGSSKDGQG ERSKEKTEKE EDKSDTSSSQ QPKSPQGLSD TGYSSDGISG SLGEIPSLIP SDEKDLLKGL KKDSFSQESS PSSPSDLAKL ESTVLSILEA QASTLVGEKA // ID RIBA1_ARATH Reviewed; 543 AA. AC P47924; Q9SBA8; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2003, sequence version 2. DT 24-JUN-2015, entry version 119. DE RecName: Full=Bifunctional riboflavin biosynthesis protein RIBA 1, chloroplastic; DE Short=AtRIBA1; DE Includes: DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase; DE Short=DHBP synthase; DE EC=4.1.99.12; DE Flags: Precursor; GN Name=RIBA1; Synonyms=RIBBA; OrderedLocusNames=At5g64300; GN ORFNames=MSJ1.14; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10783978; DOI=10.1016/S0031-9422(00)00013-3; RA Herz S.W., Eberhardt S., Bacher A.; RT "Biosynthesis of riboflavin in plants. The ribA gene of Arabidopsis RT thaliana specifies a bifunctional GTP cyclohydrolase II/3,4-dihydroxy- RT 2-butanone 4-phosphate synthase."; RL Phytochemistry 53:723-731(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9501997; DOI=10.1093/dnares/4.6.401; RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. RT Sequence features of the regions of 1,191,918 bp covered by seventeen RT physically assigned P1 clones."; RL DNA Res. 4:401-414(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 279-543. RX PubMed=7642114; DOI=10.1016/0378-1119(95)00246-3; RA Kobayashi M., Sugiyama M., Yamamoto K.; RT "Isolation of cDNAs encoding GTP cyclohydrolase II from Arabidopsis RT thaliana."; RL Gene 160:303-304(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=10835424; DOI=10.1074/jbc.M003127200; RA Turk E., Kim O., Le Coutre J., Whitelegge J.P., Eskandari S., RA Lam J.T., Kreman M., Zampighi G., Faull K.F., Wright E.M.; RT "Molecular characterization of Vibrio parahaemolyticus vSGLT: a model RT for sodium-coupled sugar cotransporters."; RL J. Biol. Chem. 275:25711-25716(2000). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19376835; DOI=10.1104/pp.109.138677; RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., RA Grossmann J., Gruissem W., Baginsky S.; RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel RT chloroplast kinase substrates and phosphorylation networks."; RL Plant Physiol. 150:889-903(2009). RN [7] RP VARIANT GLN-229 (ISOFORM 2). RX PubMed=18514161; DOI=10.1016/j.ajhg.2008.04.020; RA Tanaka M., Olsen R.W., Medina M.T., Schwartz E., Alonso M.E., RA Duron R.M., Castro-Ortega R., Martinez-Juarez I.E., RA Pascual-Castroviejo I., Machado-Salas J., Silva R., Bailey J.N., RA Bai D., Ochoa A., Jara-Prado A., Pineda G., Macdonald R.L., RA Delgado-Escueta A.V.; RT "Hyperglycosylation and reduced GABA currents of mutated GABRB3 RT polypeptide in remitting childhood absence epilepsy."; RL Am. J. Hum. Genet. 82:1249-1261(2008). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RX PubMed=23203051; DOI=10.3390/ijms131114086; RA Hiltunen H.M., Illarionov B., Hedtke B., Fischer M., Grimm B.; RT "Arabidopsis RIBA Proteins: two out of three isoforms have lost their RT bifunctional activity in riboflavin biosynthesis."; RL Int. J. Mol. Sci. 13:14086-14105(2012). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22081402; DOI=10.1007/s11103-011-9846-1; RA Hedtke B., Alawady A., Albacete A., Kobayashi K., Melzer M., RA Roitsch T., Masuda T., Grimm B.; RT "Deficiency in riboflavin biosynthesis affects tetrapyrrole RT biosynthesis in etiolated Arabidopsis tissue."; RL Plant Mol. Biol. 78:77-93(2012). RN [10] RP DISRUPTION PHENOTYPE. RX PubMed=19797057; DOI=10.1074/jbc.M109.030247; RA Nagy R., Grob H., Weder B., Green P., Klein M., Frelet-Barrand A., RA Schjoerring J.K., Brearley C., Martinoia E.; RT "The Arabidopsis ATP-binding cassette protein AtMRP5/AtABCC5 is a high RT affinity inositol hexakisphosphate transporter involved in guard cell RT signaling and phytate storage."; RL J. Biol. Chem. 284:33614-33622(2009). RN [11] RP ALLERGEN. RX PubMed=21848516; DOI=10.1111/j.1398-9995.2011.02683.x; RA An S., Ma D., Wei J.F., Yang X., Yang H.W., Yang H., Xu X., He S., RA Lai R.; RT "A novel allergen Tab y 1 with inhibitory activity of platelet RT aggregation from salivary glands of horseflies."; RL Allergy 66:1420-1427(2011). RN [12] RP ALLERGEN. RX PubMed=12100054; DOI=10.1046/j.1365-2222.2002.01411.x; RA Codina R., Ardusso L., Lockey R.F., Crisci C.D., Jaen C., RA Bertoya N.H.; RT "Identification of the soybean hull allergens involved in RT sensitization to soybean dust in a rural population from Argentina and RT N-terminal sequence of a major 50 KD allergen."; RL Clin. Exp. Allergy 32:1059-1063(2002). RN [13] RP SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DOMAIN. RX PubMed=24389466; DOI=10.1038/nsmb.2740; RA Boel G., Smith P.C., Ning W., Englander M.T., Chen B., Hashem Y., RA Testa A.J., Fischer J.J., Wieden H.J., Frank J., Gonzalez R.L. Jr., RA Hunt J.F.; RT "The ABC-F protein EttA gates ribosome entry into the translation RT elongation cycle."; RL Nat. Struct. Mol. Biol. 21:143-151(2014). RN [14] RP SUBUNIT, AND DOMAIN. RX PubMed=24389465; DOI=10.1038/nsmb.2741; RA Chen B., Boel G., Hashem Y., Ning W., Fei J., Wang C., RA Gonzalez R.L. Jr., Hunt J.F., Frank J.; RT "EttA regulates translation by binding the ribosomal E site and RT restricting ribosome-tRNA dynamics."; RL Nat. Struct. Mol. Biol. 21:152-159(2014). RN [15] RP INDUCTION. RX PubMed=21094157; DOI=10.1016/j.febslet.2010.11.025; RA Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.; RT "14-3-3 proteins fine-tune plant nutrient metabolism."; RL FEBS Lett. 585:143-147(2011). RN [16] RP COFACTOR, AND BIOTECHNOLOGY. RX PubMed=23269834; DOI=10.1073/pnas.1214159110; RA Kim S., Yamaoka Y., Ono H., Kim H., Shim D., Maeshima M., RA Martinoia E., Cahoon E.B., Nishida I., Lee Y.; RT "AtABCA9 transporter supplies fatty acids for lipid synthesis to the RT endoplasmic reticulum."; RL Proc. Natl. Acad. Sci. U.S.A. 110:773-778(2013). RN [17] RP BIOTECHNOLOGY. RX PubMed=16244144; DOI=10.1104/pp.105.068684; RA Van Hoewyk D., Garifullina G.F., Ackley A.R., Abdel-Ghany S.E., RA Marcus M.A., Fakra S., Ishiyama K., Inoue E., Pilon M., Takahashi H., RA Pilon-Smits E.A.; RT "Overexpression of AtCpNifS enhances selenium tolerance and RT accumulation in Arabidopsis."; RL Plant Physiol. 139:1518-1528(2005). RN [18] RP DEVELOPMENTAL STAGE. RX PubMed=9675899; DOI=10.1046/j.1365-313X.1998.00151.x; RA Hirner B., Fischer W.-N., Rentsch D., Kwart M., Frommer W.B.; RT "Developmental control of H+/amino acid permease gene expression RT during seed development of Arabidopsis."; RL Plant J. 14:535-544(1998). RN [19] RP DEVELOPMENTAL STAGE. RX PubMed=12376641; DOI=10.1104/pp.008110; RA Fatland B.L., Ke J., Anderson M.D., Mentzen W.I., Cui L.W., RA Allred C.C., Johnston J.L., Nikolau B.J., Wurtele E.S.; RT "Molecular characterization of a heteromeric ATP-citrate lyase that RT generates cytosolic acetyl-coenzyme A in Arabidopsis."; RL Plant Physiol. 130:740-756(2002). RN [20] RP DISEASE. RX PubMed=17315199; DOI=10.1002/hipo.20268; RA Almgren M., Persson A.S., Fenghua C., Witgen B.M., Schalling M., RA Nyengaard J.R., Lavebratt C.; RT "Lack of potassium channel induces proliferation and survival causing RT increased neurogenesis and two-fold hippocampus enlargement."; RL Hippocampus 17:292-304(2007). RN [21] RP DISEASE. RX PubMed=8995755; DOI=10.1007/s003359900259; RA Donahue L.R., Cook S.A., Johnson K.R., Bronson R.T., Davisson M.T.; RT "Megencephaly: a new mouse mutation on chromosome 6 that causes RT hypertrophy of the brain."; RL Mamm. Genome 7:871-876(1996). RN [22] RP DISEASE. RX PubMed=21966978; DOI=10.1111/j.1460-9568.2011.07834.x; RA Fisahn A., Lavebratt C., Canlon B.; RT "Acoustic startle hypersensitivity in Mceph mice and its effect on RT hippocampal excitability."; RL Eur. J. Neurosci. 34:1121-1130(2011). RN [23] RP ENZYME REGULATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=6750031; RA Ogrydziak D.M., Scharf S.J.; RT "Alkaline extracellular protease produced by Saccharomycopsis RT lipolytica CX161-1B."; RL J. Gen. Microbiol. 128:1225-1234(1982). RN [24] RP ENZYME REGULATION, CATALYTIC ACTIVITY, AND PROTEOLYTIC PROCESSING. RX PubMed=2649495; RA Matoba S., Ogrydziak D.M.; RT "A novel location for dipeptidyl aminopeptidase processing sites in RT the alkaline extracellular protease of Yarrowia lipolytica."; RL J. Biol. Chem. 264:6037-6043(1989). RN [25] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17432872; DOI=10.1021/jf0633894; RA Poza M., Sestelo A.B., Ageitos J.M., Vallejo J.A., Veiga-Crespo P., RA Villa T.G.; RT "Cloning and expression of the XPR2 gene from Yarrowia lipolytica in RT Pichia pastoris."; RL J. Agric. Food Chem. 55:3944-3948(2007). RN [26] RP PROTEOLYTIC PROCESSING. RX PubMed=9353927; RA Matoba S., Morano K.A., Klionsky D.J., Kim K., Ogrydziak D.M.; RT "Dipeptidyl aminopeptidase processing and biosynthesis of alkaline RT extracellular protease from Yarrowia lipolytica."; RL Microbiology 143:3263-3272(1997). RN [27] RP PHARMACEUTICAL. RX PubMed=21949405; DOI=10.1073/pnas.1108495108; RA Crawford M.A., Lowe D.E., Fisher D.J., Stibitz S., Plaut R.D., RA Beaber J.W., Zemansky J., Mehrad B., Glomski I.J., Strieter R.M., RA Hughes M.A.; RT "Identification of the bacterial protein FtsX as a unique target of RT chemokine-mediated antimicrobial activity against Bacillus RT anthracis."; RL Proc. Natl. Acad. Sci. U.S.A. 108:17159-17164(2011). RN [28] RP PHARMACEUTICAL. RX PubMed=16632613; DOI=10.1073/pnas.0509392103; RA Rutten L., Geurtsen J., Lambert W., Smolenaers J.J., Bonvin A.M., RA de Haan A., van der Ley P., Egmond M.R., Gros P., Tommassen J.; RT "Crystal structure and catalytic mechanism of the LPS 3-O-deacylase RT PagL from Pseudomonas aeruginosa."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7071-7076(2006). RN [29] RP INVOLVEMENT IN ASTHMA RESPONSE TO GLUCOCORTICOID TREATMENT, AND TISSUE RP SPECIFICITY. RX PubMed=21991891; DOI=10.1056/NEJMoa0911353; RA Tantisira K.G., Lasky-Su J., Harada M., Murphy A., Litonjua A.A., RA Himes B.E., Lange C., Lazarus R., Sylvia J., Klanderman B., Duan Q.L., RA Qiu W., Hirota T., Martinez F.D., Mauger D., Sorkness C., Szefler S., RA Lazarus S.C., Lemanske R.F. Jr., Peters S.P., Lima J.J., Nakamura Y., RA Tamari M., Weiss S.T.; RT "Genomewide association between GLCCI1 and response to glucocorticoid RT therapy in asthma."; RL N. Engl. J. Med. 365:1173-1183(2011). RN [30] RP INVOLVEMENT IN CHRONIC OBSTRUCTIVE PULMONARY DISEASE RESPONSE TO RP GLUCOCORTICOID TREATMENT. RX PubMed=22187997; DOI=10.1056/NEJMc1112547#SA2; RA Van den Berge M., Hiemstra P.S., Postma D.S.; RT "Genetics of glucocorticoids in asthma."; RL N. Engl. J. Med. 365:2434-2435(2011). RN [31] RP RNA EDITING, AND SUBCELLULAR LOCATION. RC TISSUE=Ehrlich ascites tumor cell; RX PubMed=9372446; RA Petzelt C., Joswig G., Mincheva A., Lichter P., Stammer H., Werner D.; RT "The centrosomal protein centrosomin A and the nuclear protein RT centrosomin B derive from one gene by post-transcriptional processes RT involving RNA editing."; RL J. Cell Sci. 110:2573-2578(1997). RN [32] {ECO:0000305} RP RNA EDITING. RX PubMed=17018572; DOI=10.1261/rna.254306; RA Stapleton M., Carlson J.W., Celniker S.E.; RT "RNA editing in Drosophila melanogaster: new targets and functional RT consequences."; RL RNA 12:1922-1932(2006). RN [33] RP TOXIC DOSE. RC TISSUE=Venom; RX PubMed=3075905; RA Masci P.P., Whitaker A.N., de Jersey J.; RT "Purification and characterization of a prothrombin activator from the RT venom of the Australian brown snake, Pseudonaja textilis textilis."; RL Biochem. Int. 17:825-835(1988). RN [34] RP TOXIC DOSE. RC TISSUE=Venom gland; RX PubMed=15351847; DOI=10.1267/THRO04090509; RA Rao V.S., Swarup S., Kini R.M.; RT "The catalytic subunit of pseutarin C, a group C prothrombin activator RT from the venom of Pseudonaja textilis, is structurally similar to RT mammalian blood coagulation factor Xa."; RL Thromb. Haemost. 92:509-521(2004). RN [35] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12111146; DOI=10.1007/s00253-002-1012-x; RA Kiiskinen L.-L., Viikari L., Kruus K.; RT "Purification and characterisation of a novel laccase from the RT ascomycete Melanocarpus albomyces."; RL Appl. Microbiol. Biotechnol. 59:198-204(2002). RN [36] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12118243; DOI=10.1038/nsb823; RA Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A., RA Koivula A., Rouvinen J.; RT "Crystal structure of a laccase from Melanocarpus albomyces with an RT intact trinuclear copper site."; RL Nat. Struct. Biol. 9:601-605(2002). RN [37] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=21592966; DOI=10.1074/jbc.M110.212183; RA Kilmartin J.R., Maher M.J., Krusong K., Noble C.J., Hanson G.R., RA Bernhardt P.V., Riley M.J., Kappler U.; RT "Insights into structure and function of the active site of SoxAX RT cytochromes."; RL J. Biol. Chem. 286:24872-24881(2011). RN [38] {ECO:0000305} RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18552405; DOI=10.1074/jbc.M800315200; RA Kappler U., Bernhardt P.V., Kilmartin J., Riley M.J., Teschner J., RA McKenzie K.J., Hanson G.R.; RT "SoxAX cytochromes, a new type of heme copper protein involved in RT bacterial energy generation from sulfur compounds."; RL J. Biol. Chem. 283:22206-22214(2008). RN [39] RP MASS SPECTROMETRY OF FORMYLATED FORM. RX PubMed=10757971; DOI=10.1021/bi000150m; RA le Coutre J., Whitelegge J.P., Gross A., Turk E., Wright E.M., RA Kaback H.R., Faull K.F.; RT "Proteomics on full-length membrane proteins using mass RT spectrometry."; RL Biochemistry 39:4237-4242(2000). CC -!- FUNCTION: Involved in the retrieval of endoplasmic reticulum CC membrane proteins from the early Golgi compartment. Required for CC correct localization of SEC12, SEC71 and SEC63 in the endoplasmic CC reticulum (By similarity). {ECO:0000250}. RIBA2 and RIBA3 together CC are not able to complement the loss of function of RIBA1. CC {ECO:0000269|PubMed:22081402}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. {ECO:0000269|PubMed:17432872, CC ECO:0000269|PubMed:23203051}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity CC for peptide bonds, and a preference for a large uncharged residue CC in P1. {ECO:0000269|PubMed:6750031}. Hydrolyzes peptide amides. CC {ECO:0000269|PubMed:2649495}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:23203051, CC ECO:0000269|PubMed:23269834}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23269834}. CC The purified enzyme contains a mixture of Fe(2+) and Zn(2+) bound CC in the active site, and a single equivalent of metal is required CC for full catalytic activity. {ECO:0000269|PubMed:23203051}; CC -!- ENZYME REGULATION: The protease activity is completely inhibited CC by the serine inhibitor PMSF but is not affected by thiol group CC inhibitors and in the presence of dithiothreitol. In the presence CC of high concentrations of o-phenanthroline the protease activity CC is only partially inhibited. {ECO:0000269|PubMed:6750031}. The CC pro-region plays an inhibitory role and may provide a mechanism CC for preventing premature activation in the secretory pathway. CC {ECO:0000269|PubMed:2649495}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=~280 nm {ECO:0000269|PubMed:12111146, CC ECO:0000269|PubMed:12118243}; CC Note=Exhibits a shoulder at 360 nm, a smaller absorption peak at CC 450 nm, and a second, larger peak at 590 nm. CC {ECO:0000269|PubMed:12118243}. Absorption peak at 450 nm CC disappears at high pH. {ECO:0000269|PubMed:12111146}; CC Kinetic parameters: CC KM=0.49 mM for glutathione (at pH 6.0) CC {ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; CC KM=0.19 mM for glutathione (at pH 7.0) CC {ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; CC Vmax=0.124 uM/min/mg enzyme (copper-free) at pH 6.2 CC {ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; CC Vmax=1.54 uM/min/mg enzyme (copper-loaded) at pH 6.2 CC {ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; CC Note=kcat is 8.72 s(-1) and 5.7 s(-1) for glutathione at pH 6.0 CC and pH 7.0, respectively. {ECO:0000269|PubMed:18552405}. Vmax CC decreases a lot at pH 7.0. {ECO:0000269|PubMed:21592966}; CC pH dependence: CC Optimum pH is 9.0-10.0. {ECO:0000269|PubMed:6750031}. Inactive CC when pH is greater than 8.0. {ECO:0000269|PubMed:17432872}; CC Redox potential: CC E(0) is -479 mV for heme at pH 8.0. CC {ECO:0000269|PubMed:21592966}. E(0) is -430 mV for heme at pH 6 CC with copper-loaded SoxAX, -455 mV for heme at pH 7 with copper- CC loaded SoxAX, -486 mV for heme at pH 8 with copper-loaded SoxAX, CC -424 mV for heme at pH 6 with copper-free SoxAX, -479 mV for CC heme at pH 7 with copper-free SoxAX, -507 mV for heme at pH 8 CC with copper-free SoxAX and -196 mV for copper center. CC {ECO:0000269|PubMed:18552405}. The Fe (III/II) potentials are CC +133 mV at pH 6.0, +104 mV at pH 7.0, +49 at pH 7.9 and +10 mV CC at pH 8.7. {ECO:0000269|PubMed:18552405, CC ECO:0000269|PubMed:21592966}; CC Temperature dependence: CC Optimum temperature is 40 degrees Celsius. CC {ECO:0000269|PubMed:6750031}. Inactive when temperature drops CC below 20 degrees Celsius. {ECO:0000269|PubMed:17432872}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2- CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step CC 1/1. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 1/4. CC -!- SUBUNIT: Interacts with AXL1, AXL2, IQG1 and SEC3. CC {ECO:0000269|PubMed:24389465}. Probably contacts ribosomal CC proteins L1, L5, L33 and S7, the 16S and 23S rRNA and the P site CC containing tRNA(fMet). {ECO:0000269|PubMed:24389466}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP- CC Rule:MF_03000}. Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:23203051}. Nucleus CC {ECO:0000269|PubMed:9372446}. Note=Centrosomin-A is found in the CC centrosome. {ECO:0000269|PubMed:23203051}. Centrosomin-B is found CC in the nucleus. {ECO:0000269|PubMed:9372446}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms may be produced by alternative CC initiation, both from non-canonical start codons upstream of the CC initiator methionine displayed and from other canonical start CC codons downstream of that displayed. CC {ECO:0000303|PubMed:10835424}. The precise sites of translation CC initiation have not been unambiguously identified. CC {ECO:0000269|PubMed:10835424}; CC Name=1; CC IsoId=P47924-1; Sequence=Displayed; CC Name=2; CC IsoId=P47924-2; Sequence=VSP_002721; CC Note=Most abundantly expressed isoform, at mRNA level. CC {ECO:0000269|PubMed:10835424}. Contains a phosphothreonine at CC position 214. {ECO:0000269|PubMed:10835424}. Ref.5 (AAF80602) CC sequence is in conflict in position: 223:K->E. {ECO:0000305}. CC Variant in position: 229:P->Q (in dbSNP:rs1141138). CC {ECO:0000269|PubMed:18514161}. Ref.5 (AAF80602) sequence differs CC from that shown due to several frameshifts. {ECO:0000305}; CC -!- TISSUE SPECIFICITY: Expressed in leaves, shoots, roots, flowers CC and siliques. {ECO:0000269|PubMed:23203051}. Predominantly CC expressed in lung, spleen, thymus and testis and, at lower levels, CC in brain, bone marrow, peripheral leukocytes, skin and trachea. CC {ECO:0000269|PubMed:21991891}. CC -!- DEVELOPMENTAL STAGE: Expressed in endosperm during early stages of CC seed development. Strongly induced at heart stage of CC embryogenesis. {ECO:0000269|PubMed:9675899}. Expressed in flower CC buds at stage 6 of development in tapetal cells and at stage 10 in CC the epidermal cells of growing petals and ovaries. In young CC siliques, expressed transiently in the inner integument of the CC ovules just prior to testal deposition. CC {ECO:0000269|PubMed:12376641}. CC -!- INDUCTION: Constitutively expressed, increases in stationary phase CC (at protein level). {ECO:0000269|PubMed:24389466}. Induced by CC nitrogen (N) and phosphate (P) deprivation in leaves, but CC repressed by potassium (K) and N deprivation in roots. CC {ECO:0000269|PubMed:21094157}. CC -!- DOMAIN: The arm domain (residues 95-139) is inserted in the first CC ABC transporter domain. Its deletion abrogates the growth arrest CC and translation inhibition effect of the double Q-188/Q-470 CC mutation. When deleted impairs fitness in long-term (up to 6 days) CC growth in stationary phase. {ECO:0000269|PubMed:24389466}. CC Probably contacts ribosomal protein L1. CC {ECO:0000269|PubMed:24389465}. CC -!- PTM: The 10 consecutive -X-Ala- or -X-Pro- dipeptides located over CC 100 amino acids upstream of the N-terminal of mature XPR2 are CC subject to dipeptidyl aminopeptidase (DPAPase)-processing. CC {ECO:0000269|PubMed:9353927}. DPAPase activity is not necessary CC for XPR6 cleavage and for secretion of mature active XPR2. CC {ECO:0000269|PubMed:2649495}. CC -!- RNA EDITING: Modified_positions=Not_applicable; Note=Some CC positions are modified by RNA editing via nucleotide deletion, up CC to position 787. The unedited version gives rise to centrosomin-B CC (shown here). The fully edited version gives rise to centrosomin- CC A, in which the C-terminal sequence is replaced up to position 787 CC by Ser-Ile-Val-Ala-STOP. A combination of alternative splicing and CC RNA editing resulting in this template G deletion could also CC explain the generation of centrosomin-A mRNA. CC {ECO:0000269|PubMed:9372446}. Target of Adar. CC {ECO:0000269|PubMed:17018572}; CC -!- MASS SPECTROMETRY: Mass=60680; Method=Electrospray; Range=1-543; CC Note=Formylated form.; Evidence={ECO:0000269|PubMed:10757971}; CC -!- POLYMORPHISM: Polymorphisms dbSNP:rs37972 and dbSNP:rs37973, CC located in GLCCI1 promoter region, are associated with a decreased CC response to glucorticoid treatment [MIM:614400] in asthma CC patients. {ECO:0000269|PubMed:21991891}. Same observations have CC been found in chronic obstructive pulmonary disease patients. CC {ECO:0000269|PubMed:22187997}. The mean increase in forced CC expiratory volume in 1 second in glucorticoid treated subjects who CC are homozygous for the mutant (G) rs37973 allele is only about CC one-third of that seen in similarly treated subjects who are CC homozygous for the wild-type allele (A). CC {ECO:0000269|PubMed:21991891}. These polymorphisms affect GLCCI1 CC transcription level. {ECO:0000269|PubMed:21991891, CC ECO:0000269|PubMed:22187997}. CC -!- DISEASE: Note=A spontaneous mutation leading to a frameshift and CC truncation of Kcna2 causes megencephaly with a 25% increase of CC brain weight relative to wild-type. Especially the hippocampus CC shows increased proliferation of neurons and astrocytes, leading CC to increased brain volume. {ECO:0000269|PubMed:17315199}. Mutant CC mice appear normal at birth. After 3-4 weeks, they display low CC body weight, a subtle shakiness in their gait, a preference for a CC strange sitting position that is maintained for periods ranging CC from 30 seconds to several minutes, excessive lacrimation and CC acoustic startle hypersensitivity. {ECO:0000269|PubMed:21966978, CC ECO:0000269|PubMed:8995755}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype when heterozygous. CC Bleached phenotype and no viable seeds produced when homozygous. CC {ECO:0000269|PubMed:22081402}. Low phytic acid levels in seed CC tissue. {ECO:0000269|PubMed:19797057}. CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. CC {ECO:0000269|PubMed:21848516}. Sensitization is common in subjects CC who are repeatedly exposed to G.max dust. Common symptoms are CC bronchial asthma and allergic rhinitis. CC {ECO:0000269|PubMed:12100054}. CC -!- TOXIC DOSE: Intravenous injection (23 ug/kg bodyweight) of the CC group C prothrombin activator causes death in rats through CC disseminated intravascular coagulopathy. CC {ECO:0000269|PubMed:3075905}. To the contrary, pseutarin-C is not CC lethal even at 10 mg/kg in mice when injected intraperitoneally. CC {ECO:0000269|PubMed:15351847}. CC -!- BIOTECHNOLOGY: Overexpression of ABCA9 increases seed oil content. CC {ECO:0000269|PubMed:23269834}. NFS2-overexpressing transgenic CC plants have enhanced ability to tolerate and accumulate Se and may CC be used in phytoremediation. {ECO:0000269|PubMed:16244144}. CC -!- PHARMACEUTICAL: Potential therapeutic target of chemokine-mediated CC antimicrobial activity against B.anthracis to treat infection. CC {ECO:0000269|PubMed:21949405}. Might be useful for the development CC of new vaccines or adjuvants because of its LPS-modifying CC properties. May be used for the design of inhibitors with possible CC therapeutic value. {ECO:0000303|PubMed:16632613}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HNH domain. {ECO:0000305}. CC -!- SIMILARITY: To phage T4 mobB and mobD. {ECO:0000305}. CC -!- CAUTION: The active site cysteine and glutamate residues are not CC conserved in this protein. Its activity is therefore unsure. CC {ECO:0000305}. Dermonecrotic toxins were previously known as CC sphingomyelin phosphodiesterase D based on their ability to CC hydrolyze sphingomyelin into choline and acylsphingosine CC phosphate. Based on additional biochemical analysis, the enzymes CC have been renamed phospholipase D to represent a more accurate and CC broader denomination. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA08113.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; DR EMBL; AJ000053; CAA03884.1; -; Genomic_DNA. DR EMBL; AB008268; BAB09861.1; -; Genomic_DNA. DR EMBL; CP002688; AED97867.1; -; Genomic_DNA. DR EMBL; D45165; BAA08113.1; ALT_INIT; mRNA. DR EMBL; AF255301; AAF80602.1; -; mRNA. DR PIR; JC4209; JC4209. DR RefSeq; NP_201235.4; NM_125826.4. DR UniGene; At.49217; -. DR ProteinModelPortal; P47924; -. DR SMR; P47924; 125-502. DR MINT; MINT-8063173; -. DR STRING; 3702.AT5G64300.1; -. DR PaxDb; P47924; -. DR PRIDE; P47924; -. DR EnsemblPlants; AT5G64300.1; AT5G64300.1; AT5G64300. DR GeneID; 836551; -. DR KEGG; ath:AT5G64300; -. DR GeneFarm; 2299; 254. DR TAIR; AT5G64300; -. DR eggNOG; COG0108; -. DR HOGENOM; HOG000115440; -. DR InParanoid; P47924; -. DR KO; K14652; -. DR OMA; LMVDRNT; -. DR PhylomeDB; P47924; -. DR BioCyc; ARA:AT5G64300-MONOMER; -. DR BioCyc; MetaCyc:AT5G64300-MONOMER; -. DR BRENDA; 4.1.99.12; 399. DR UniPathway; UPA00275; UER00399. DR UniPathway; UPA00275; UER00400. DR PRO; PR:P47924; -. DR Proteomes; UP000006548; Chromosome 5. DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB. DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR. DR GO; GO:0016020; C:membrane; IDA:TAIR. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IMP:UniProtKB. DR Gene3D; 3.90.870.10; -; 1. DR HAMAP; MF_00179; RibA; 1. DR HAMAP; MF_00180; RibB; 1. DR HAMAP; MF_01283; RibBA; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR000422; DHBP_synthase_RibB. DR InterPro; IPR000926; GTP_CycHdrlaseII_RibA. DR InterPro; IPR016299; Riboflavin_synth_RibBA. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00505; ribA; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 1: Evidence at protein level; KW Allergen; Alternative splicing; Chloroplast; Complete proteome; KW Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase; Lyase; Magnesium; KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Nucleus; Pharmaceutical; Plastid; Reference proteome; KW Riboflavin biosynthesis; Transit peptide; Zinc. FT TRANSIT 1 56 Chloroplast. {ECO:0000255|HAMAP- FT Rule:MF_03000}. FT CHAIN 57 543 Bifunctional riboflavin biosynthesis FT protein RIBA 1, chloroplastic. FT /FTId=PRO_0000030436. FT NP_BIND 379 383 GTP. {ECO:0000250}. FT NP_BIND 423 425 GTP. {ECO:0000250}. FT REGION 57 328 DHBP synthase. FT REGION 152 153 D-ribulose 5-phosphate binding. FT {ECO:0000250}. FT REGION 267 271 D-ribulose 5-phosphate binding. FT {ECO:0000250}. FT REGION 329 543 GTP cyclohydrolase II. FT COMPBIAS 7 10 Poly-Ser. FT COMPBIAS 144 147 Poly-Val. FT ACT_SITE 457 457 Proton acceptor; for GTP cyclohydrolase FT activity. {ECO:0000255}. FT ACT_SITE 459 459 Nucleophile; for GTP cyclohydrolase FT activity. {ECO:0000250}. FT METAL 153 153 Magnesium or manganese 1. {ECO:0000250}. FT METAL 153 153 Magnesium or manganese 2. {ECO:0000250}. FT METAL 270 270 Magnesium or manganese 2. {ECO:0000250}. FT METAL 384 384 Zinc; catalytic. {ECO:0000250}. FT METAL 395 395 Zinc; catalytic. {ECO:0000250}. FT METAL 397 397 Zinc; catalytic. {ECO:0000250}. FT BINDING 157 157 D-ribulose 5-phosphate. {ECO:0000250}. FT BINDING 291 291 D-ribulose 5-phosphate. {ECO:0000250}. FT BINDING 400 400 GTP. {ECO:0000250}. FT BINDING 445 445 GTP. {ECO:0000250}. FT BINDING 480 480 GTP. {ECO:0000250}. FT BINDING 485 485 GTP. {ECO:0000250}. FT SITE 253 253 Essential for DHBP synthase activity. FT {ECO:0000250}. FT SITE 291 291 Essential for DHBP synthase activity. FT {ECO:0000250}. FT VAR_SEQ 203 203 E -> ETYMAVSFIGGTDGWFAGVSKMVDAAPGHFEMILDQ FT SNPQYMNLPGIAVLIGGLWVANLYYWGFNQYIIQRTLAAK FT (in isoform 2). FT /FTId=VSP_002721. ** ** ################# INTERNAL SECTION ################## **DR TAIR-CDS; AT5G64300.1; TAIR10; P47924-1. **EV ECO:0000250; -; XXX; 01-JAN-1900. **EV ECO:0000255; -; XXX; 01-JAN-1900. **EV ECO:0000255; HAMAP-Rule:MF_03000; SEG; 30-JUN-2015. **EV ECO:0000269; PubMed:10757971; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:10835424; SEG; 30-JUN-2015. **EV ECO:0000269; PubMed:12100054; EMB; 09-APR-2013. **EV ECO:0000269; PubMed:12111146; JUJ; 19-APR-2006. **EV ECO:0000269; PubMed:12118243; JUJ; 19-APR-2006. **EV ECO:0000269; PubMed:12376641; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:15351847; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:16244144; MIS; 14-JAN-2015. **EV ECO:0000269; PubMed:17018572; ELS; 27-MAR-2008. **EV ECO:0000269; PubMed:17315199; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:17432872; SEG; 29-JUN-2015. **EV ECO:0000269; PubMed:18514161; SEG; 30-JUN-2015. **EV ECO:0000269; PubMed:18552405; KAL; 17-JUN-2013. **EV ECO:0000269; PubMed:19797057; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:21094157; MAF; 23-APR-2015. **EV ECO:0000269; PubMed:21592966; KAL; 13-JUN-2013. **EV ECO:0000269; PubMed:21848516; MNS; 14-OCT-2011. **EV ECO:0000269; PubMed:21949405; KAL; 09-JAN-2013. **EV ECO:0000269; PubMed:21966978; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:21991891; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:22081402; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:22187997; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:23203051; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:23269834; MIT; 19-JUN-2010. **EV ECO:0000269; PubMed:24389465; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:24389466; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:2649495; MAF; 23-APR-2015. **EV ECO:0000269; PubMed:3075905; SEG; 30-JUN-2015. **EV ECO:0000269; PubMed:6750031; MAF; 23-APR-2015. **EV ECO:0000269; PubMed:8995755; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:9353927; SEG; 29-JUN-2015. **EV ECO:0000269; PubMed:9372446; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:9675899; XXX; 01-JAN-1900. **EV ECO:0000303; PubMed:10835424; SEG; 30-JUN-2015. **EV ECO:0000303; PubMed:16632613; KAL; 30-APR-2013. **EV ECO:0000305; -; SEG; 30-JUN-2015. **IS P47924-3 **ZB MIT, 21-JUL-2004; ELC, 15-NOV-2007; MIS, 02-MAY-2013; SQ SEQUENCE 543 AA; 59056 MW; 31D89A500E42BF81 CRC64; MSSINLSSSS PSTISLSRSR LSQSSTTLLH GLHRVTLPSN HPLSTFSIKT NTGKVKAAVI SREDDLLSFT NGNTPLSNGS LIDDRTEEPL EADSVSLGTL AADSAPAPAN GFVAEDDDFE LDLPTPGFSS IPEAIEDIRQ GKLVVVVDDE DRENEGDLVM AAQLATPEAM AFIVRHGTGI VCVSMKEDDL ERLHLPLMVN QKENEEKLST AFTVTVDAKH GTTTGVSARD RATTILSLAS RDSKPEDFNR PGHIFPLKYR EGGVLKRAGH TEASVDLTVL AGLDPVGVLC EIVDDDGSMA RLPKLREFAA ENNLKVVSIA DLIRYRRKRD KLVERASAAR IPTMWGPFTA YCYRSILDGI EHIAMVKGEI GDGQDILVRV HSECLTGDIF GSARCDCGNQ LALSMQQIEA TGRGVLVYLR GHEGRGIGLG HKLRAYNLQD AGRDTVEANE ELGLPVDSRE YGIGAQIIRD LGVRTMKLMT NNPAKYVGLK GYGLAIVGRV PLLSLITKEN KRYLETKRTK MGHMYGLKFK GDVVEKIESE SES // Swissknife_1.75/t/identity.txl0000644005110600510130000313673312573305310016715 0ustar ecastroSwissProtID O43499 Unreviewed; 480 AA. AC O43499; O08291; O08202; O08292; O08203; O08293; O08204; O08294; AC O08205; O08295; O08206; O08296; O08207; O08297; O08208; O08298; AC O08209; O08299; O08210; O08300; O08211; O08301; O08212; O08302; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE HTGN51. GN TGN. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=126566, 55{E2}; RN [1] RP SEQUENCE FROM N.A. RA Kain R., Angata K., Kerjaschki D., Fukuda M.; RL J. Biol. Chem. 273:0-0(1998). DR EMBL; AF029316; AAB96908.1; -. DR EMBL; AF029313; AAB96908.1; JOINED. DR EMBL; AF029314; AAB96908.1; JOINED. DR EMBL; AF029315; AAB96908.1; JOINED. KW Zinc-finger; Receptor; Transcription regulation; DNA-binding; KW Nuclear protein. ** ** ################# SOURCE SECTION ################## ** Homo sapiens trans-golgi network glycoprotein (TGN) gene, exon 4, ** and complete cds. ** [1] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** "Molecular Cloning and Expression of a Novel Human Trans-Golgi Network ** Glycoprotein, TGN51, that Contains Multiple Tyrosine-containing ** Motifs"; ** J. Biol. Chem. 273:0-0(1998). ** [2] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** ; ** Submitted (09-OCT-1997) to the EMBL/GenBank/DDBJ databases. ** Glycobiology Program, The Burnham Institute, 10901 N. Torrey Pines Rd, ** La Jolla, CA 92037, USA ** source 1..2563 ** /organism="Homo sapiens" ** /chromosome="2" ** /note="sequence from P1 plasmid 10508" ** /map="2p11.2" ** CDS ** join(AF029313:63..108,AF029314:1..1178,AF029315:278..361, ** 210..344) ** /codon_start=1 ** /db_xref="PID:g2772928" ** /note="trans-golgi network glycoprotein" ** /gene="TGN" ** /product="hTGN51" ** CDS_IN_EMBL_ENTRY 3 ** 20-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 480 AA; 50993 MW; 8CAE4EE663B7225D CRC64; MRFVVALVLV NVAAAGAVPL LATESVKQEE AGVRPSAGNV STHPSLSQRP GGSTKSHPEP QTPKDSPSKS SAEAQTPEDT PNKSGGEAKT LKDSSNKSGA EAQTPKGSTS KSGSEAQTTK DSTSKSHPEL QTPKDSTGKS GAEAQTPEDS PNRSGAEPKT QKDSPSKSGS EAQTTKDVPN KSGADGQTPK DGSSKSGAED QTPKDVPNKS GAEKQTPKDG SNKSGAEEQG PIDGPSKSGA EEQTSKDSPN KVVPEQPSRK DHSKPISNPS DNKELPKADT NQLADKGKLS PHAFKTESGE ETDLISPPQE EVKSSEPTED VGPKEAEDDD TGPEEGSPPK EEKEKMSGSA SSENREGTLS DSTGSEKDDL YPNGSGNGSA ESSHFFAYLV TAAILVAVLY IAHHNKRKII AFVLEGKRSK VTRRPKASDY QRLDQKYVLI LNVFPAPPKR SFLPQVLTEW YIPLEKDERH QWIVLLSFQL // ID O43500 PRELIMINARY; PRT; 437 AA. AC O43500; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE HTGN46. GN TGN. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Kain R., Angata K., Kerjaschki D., Fukuda M.; RL J. Biol. Chem. 273:0-0(1998). DR EMBL; AF029316; AAB96906.1; -. DR EMBL; AF029313; AAB96906.1; JOINED. DR EMBL; AF029314; AAB96906.1; JOINED. DR EMBL; AF029315; AAB96906.1; JOINED. ** ** ################# SOURCE SECTION ################## ** Homo sapiens trans-golgi network glycoprotein (TGN) gene, exon 4, ** and complete cds. ** [1] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** "Molecular Cloning and Expression of a Novel Human Trans-Golgi Network ** Glycoprotein, TGN51, that Contains Multiple Tyrosine-containing ** Motifs"; ** J. Biol. Chem. 273:0-0(1998). ** [2] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** ; ** Submitted (09-OCT-1997) to the EMBL/GenBank/DDBJ databases. ** Glycobiology Program, The Burnham Institute, 10901 N. Torrey Pines Rd, ** La Jolla, CA 92037, USA ** source 1..2563 ** /organism="Homo sapiens" ** /chromosome="2" ** /note="sequence from P1 plasmid 10508" ** /map="2p11.2" ** CDS ** join(AF029313:63..108,AF029314:1..1178,AF029315:278..361, ** 268..273) ** /codon_start=1 ** /db_xref="PID:g2772926" ** /note="trans-golgi network glycoprotein" ** /gene="TGN" ** /product="hTGN46" ** CDS_IN_EMBL_ENTRY 3 ** 20-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 437 AA; 45759 MW; 14B21554256E983B CRC64; MRFVVALVLV NVAAAGAVPL LATESVKQEE AGVRPSAGNV STHPSLSQRP GGSTKSHPEP QTPKDSPSKS SAEAQTPEDT PNKSGGEAKT LKDSSNKSGA EAQTPKGSTS KSGSEAQTTK DSTSKSHPEL QTPKDSTGKS GAEAQTPEDS PNRSGAEPKT QKDSPSKSGS EAQTTKDVPN KSGADGQTPK DGSSKSGAED QTPKDVPNKS GAEKQTPKDG SNKSGAEEQG PIDGPSKSGA EEQTSKDSPN KVVPEQPSRK DHSKPISNPS DNKELPKADT NQLADKGKLS PHAFKTESGE ETDLISPPQE EVKSSEPTED VGPKEAEDDD TGPEEGSPPK EEKEKMSGSA SSENREGTLS DSTGSEKDDL YPNGSGNGSA ESSHFFAYLV TAAILVAVLY IAHHNKRKII AFVLEGKRSK VTRRPKASDY QRLDQKS // ID O43501 PRELIMINARY; PRT; 453 AA. AC O43501; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE HTGN48. GN TGN. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Kain R., Angata K., Kerjaschki D., Fukuda M.; RL J. Biol. Chem. 273:0-0(1998). DR EMBL; AF029316; AAB96907.1; -. DR EMBL; AF029313; AAB96907.1; JOINED. DR EMBL; AF029314; AAB96907.1; JOINED. DR EMBL; AF029315; AAB96907.1; JOINED. ** ** ################# SOURCE SECTION ################## ** Homo sapiens trans-golgi network glycoprotein (TGN) gene, exon 4, ** and complete cds. ** [1] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** "Molecular Cloning and Expression of a Novel Human Trans-Golgi Network ** Glycoprotein, TGN51, that Contains Multiple Tyrosine-containing ** Motifs"; ** J. Biol. Chem. 273:0-0(1998). ** [2] ** 1-2563 ** Kain R., Angata K., Kerjaschki D., Fukuda M.; ** ; ** Submitted (09-OCT-1997) to the EMBL/GenBank/DDBJ databases. ** Glycobiology Program, The Burnham Institute, 10901 N. Torrey Pines Rd, ** La Jolla, CA 92037, USA ** source 1..2563 ** /organism="Homo sapiens" ** /chromosome="2" ** /note="sequence from P1 plasmid 10508" ** /map="2p11.2" ** CDS ** join(AF029313:63..108,AF029314:1..1178,AF029315:278..361, ** 251..304) ** /codon_start=1 ** /db_xref="PID:g2772927" ** /note="trans-golgi network glycoprotein" ** /gene="TGN" ** /product="hTGN48" ** CDS_IN_EMBL_ENTRY 3 ** 20-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 453 AA; 47578 MW; 13F70172177BFE82 CRC64; MRFVVALVLV NVAAAGAVPL LATESVKQEE AGVRPSAGNV STHPSLSQRP GGSTKSHPEP QTPKDSPSKS SAEAQTPEDT PNKSGGEAKT LKDSSNKSGA EAQTPKGSTS KSGSEAQTTK DSTSKSHPEL QTPKDSTGKS GAEAQTPEDS PNRSGAEPKT QKDSPSKSGS EAQTTKDVPN KSGADGQTPK DGSSKSGAED QTPKDVPNKS GAEKQTPKDG SNKSGAEEQG PIDGPSKSGA EEQTSKDSPN KVVPEQPSRK DHSKPISNPS DNKELPKADT NQLADKGKLS PHAFKTESGE ETDLISPPQE EVKSSEPTED VGPKEAEDDD TGPEEGSPPK EEKEKMSGSA SSENREGTLS DSTGSEKDDL YPNGSGNGSA ESSHFFAYLV TAAILVAVLY IAHHNKRKII AFVLEGKRSK VTRRPKASDY QRLDQKIFSP PSPNRMVYSS GKR // ID O43530 PRELIMINARY; PRT; 456 AA. AC O43530; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE NBMPR-INSENSITIVE NUCLEOSIDE TRANSPORTER EI. GN ENT2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Crawford C.R., Patel D.H., Naeve C.W., Belt J.A.; RL J. Biol. Chem. 273:0-0(1998). DR EMBL; AF034102; AAB97834.1; -. DR InterPro; IPR002259; -. DR PFAM; PF01733; Nucleoside_tran; 1. DR PRINTS; PR01130; DERENTRNSPRT. DR PRODOM; PD005103; -; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens NBMPR-insensitive nucleoside transporter ei (ENT2) ** mRNA, complete cds. ** [1] ** 1-2522 ** Crawford C.R., Patel D.H., Naeve C.W., Belt J.A.; ** "Cloning of the Human Equilibrative, Nitrobenzylmercaptopurineriboside ** (NBMPR)-Insensitive Nucleoside Transporter ei by Functional Expression ** in a Transport-Deficient Cell Line"; ** J. Biol. Chem. 273:0-0(1998). ** [2] ** 1-2522 ** Crawford C.R., Naeve C.W., Belt J.A.; ** ; ** Submitted (11-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Molecular Pharmacology, St. Jude Children's Research Hospital, 332 N. ** Lauderdale, Memphis, TN 38105, USA ** for description of the isolation and properties of the cDNA, see ** Crawford, et al, Proc. Annu. Meet. Am. Assoc. Cancer Res., 38:A406, ** 1997 (abstract). ** source 1..2522 ** /organism="Homo sapiens" ** /cell_line="HeLa S3; ATCC CCL2.2" ** /clone_lib="Clonetech HL1152y" ** CDS 238..1608 ** /codon_start=1 ** /db_xref="PID:g2811137" ** /note="plasma membrane transport protein" ** /gene="ENT2" ** /function="mediates equilibrative transport of purine ** and ** pyrimidine nucleosides, and the purine base ** hypoxanthine" ** /product="NBMPR-insensitive nucleoside transporter ei" ** CDS_IN_EMBL_ENTRY 1 ** 28-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PRODOM; PD005103; PD005103; 131; 456; T; 19-JUN-2000; **PM PFAM; PF01733; Nucleoside_tran; 131; 454; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 137; 159; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 165; 185; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 191; 214; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 301; 318; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 333; 354; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 361; 378; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 393; 409; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 412; 428; T; 19-JUN-2000; **PM PRINTS; PR01130; DERENTRNSPRT; 430; 454; T; 19-JUN-2000; SQ SEQUENCE 456 AA; 50113 MW; ABCBD244306708E1 CRC64; MARGDAPRDS YHLVGISFFI LGLGTLLPWN FFITAIPYFQ ARLAGAGNST ARILSTNHTG PEDAFNFNNW VTLLSQLPLL LFTLLNSFLY QCVPETVRIL GSLLAILLLF ALTAALVKVD MSPGPFFSIT MASVCFINSF SAVLQGSLFG QLGTMPSTYS TLFLSGQGLA GIFAALAMLL SMASGVDAET SALGYFITPC VGILMSIVCY LSLPHLKFAR YYLANKSSQA QAQELETKAE LLQSDENGIP SSPQKVALTL DLDLEKEPES EPDEPQKPGK PSVFTVFQKI WLTALCLVLV FTVTLSVFPA ITAMVTSSTS PGKWSQFFNP ICCFLLFNIM DWLGRSLTSY FLWPDEDSRL LPLLVCLRFL FVPLFMLCHV PQRSRLPILF PQDAYFITFM LLFAVSNGYL VSLTMCLAPR QVLPHEREVA GALMTFFLAL GLSCGASLSF LFKALL // ID O43534 PRELIMINARY; PRT; 377 AA. AC O43534; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE NATURAL KILLER CELL INHIBITORY RECEPTOR. GN KIR2DL4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Valiant N.M., Uhrberg M., Shilling H.G., Lienert-Weidenbach K., RA Arnett K.L., D'Andrea A., Phillips J.H., Lanier L.L., Parham P.; RL Immunity 0:0-0(1997). RN [2] RP SEQUENCE FROM N.A. RA Uhrberg M., Valiant N.M., Shum B., Shilling H.G., RA Lienert-Weidenbach K., Corliss B., Tyan D., Lanier L.L., Parham P.; RL Immunity 0:0-0(1998). DR EMBL; AF034773; AAB95166.1; -. DR HSSP; P43626; 1NKR. DR InterPro; IPR003006; -. DR Pfam; PF00047; ig; 2. ** ** ################# SOURCE SECTION ################## ** Homo sapiens natural killer cell inhibitory receptor (KIR2DL4) ** mRNA, variant 3, complete cds. ** [1] ** 1-1179 ** Valiant N.M., Uhrberg M., Shilling H.G., Lienert-Weidenbach K., ** Arnett K.L., D'Andrea A., Phillips J.H., Lanier L.L., Parham P.; ** "Functionally and Structurally Distinct NK Cell Receptor Repertoires ** in ** the Peripheral Blood of Two Human Donors"; ** Immunity 0:0-0(1997). ** [2] ** 1-1179 ** Uhrberg M., Valiant N.M., Shum B., Shilling H.G., Lienert-Weidenbach ** K., ** Corliss B., Tyan D., Lanier L.L., Parham P.; ** "Human Diversity in Killer Cell Inhibitory Receptor (KIR) Genes"; ** Immunity 0:0-0(1998). ** [3] ** 1-1179 ** Shilling H.G.; ** ; ** Submitted (17-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Structural Biology, Stanford University, Sherman Fairchild Building, ** Stanford University School of Medicine, Stanford, CA 94305-5400, USA ** source 1..1179 ** /organism="Homo sapiens" ** /cell_type="peripheral blood" ** CDS 7..1140 ** /codon_start=1 ** /db_xref="PID:g2739182" ** /gene="KIR2DL4" ** /product="natural killer cell inhibitory receptor" ** CDS_IN_EMBL_ENTRY 1 ** 09-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00047; ig; 44; 99; T; 19-JUN-2000; **PM PFAM; PF00047; ig; 139; 197; T; 19-JUN-2000; SQ SEQUENCE 377 AA; 41426 MW; 969DA8DB9872F4B6 CRC64; MSMSPTVIIL ACLGFFLDQS VWAHVGGQDK PFCSAWPSAV VPQGGHVTLR CHCRRGFNIF TLYKKDGVPV PELYNRIFWN SFLISPVTPA HAGTYRCRGF HPHSPTEWSA PSNPLVIMVT GLYEKPSLTA RPGPTVRAGE NVTLSCSSQS SFDIYHLSRE GEAHELRLPA VPSINGTFQA DFPLGPATHG ETYRCFGSFH GSPYEWSDPS DPLPVSVTGN PSSSWPSPTE PSFKTGIARH LHAVIRYSVA IILFTILPFF LLHRWCSKKK NAAVMNQEPA GHRTVNREDS DEQDPQEVTY AQLDHCIFTQ RKITGPSQRS KRPSTDTSVC IELPNAEPRA LSPAHEHHSQ ALMGSSRETT ALSQTQLASS NVPAAGI // ID O43538 PRELIMINARY; PRT; 653 AA. AC O43538; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE AMPHIPHYSIN I. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BREAST; RA Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., RA Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.; RL Mol. Med. (Camb. Mass.) 0:0-0(1998). DR EMBL; AF034996; AAC02977.1; -. DR HSSP; P29355; 2SEM. DR INTERPRO; IPR001452; -. DR INTERPRO; IPR003005; -. DR INTERPRO; IPR003017; -. DR PFAM; PF00018; SH3; 1. DR PRINTS; PR00452; SH3DOMAIN. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01252; AMPHIPHYSIN1. DR PROSITE; PS50002; SH3; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens amphiphysin I mRNA, alternative splice isoform, ** complete cds. ** [1] ** 1-3161 ** Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., ** Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.; ** "Expression of amphiphysin I, an autoantigen of paraneoplastic ** neurological syndromes, in breast cancer"; ** Mol. Med. (Camb. Mass.) 0:0-0(1998). ** [2] ** 1-3161 ** Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., ** Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.; ** ; ** Submitted (18-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Cell Biology, Yale University, 295 Congress Avenue, New Haven, CT ** 06510, ** USA ** source 1..3161 ** /organism="Homo sapiens" ** /cell_line="Hs578T" ** /tissue_type="breast" ** CDS 70..2031 ** /codon_start=1 ** /db_xref="PID:g2895528" ** /note="alternative splice isoform" ** /product="amphiphysin I" ** CDS_IN_EMBL_ENTRY 1 ** 20-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00018; SH3; 583; 652; T; 19-JUN-2000; **PM PRINTS; PR00452; SH3DOMAIN; 583; 593; T; 19-JUN-2000; **PM PRINTS; PR00452; SH3DOMAIN; 597; 612; T; 19-JUN-2000; **PM PRINTS; PR00452; SH3DOMAIN; 619; 628; T; 19-JUN-2000; **PM PRINTS; PR00452; SH3DOMAIN; 640; 652; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 23; 40; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 51; 61; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 83; 95; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 118; 132; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 140; 151; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 175; 184; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 186; 196; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 576; 585; T; 19-JUN-2000; **PM PRINTS; PR01251; AMPHIPHYSIN; 597; 611; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 3; 11; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 93; 104; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 220; 234; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 235; 246; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 247; 258; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 386; 396; T; 19-JUN-2000; **PM PRINTS; PR01252; AMPHIPHYSIN1; 632; 643; T; 19-JUN-2000; **PM PROSITE; PS50002; SH3; 580; 653; T; 19-JUN-2000; SQ SEQUENCE 653 AA; 71929 MW; 44C1115E3E70B6A9 CRC64; MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF EEFNVDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD KAFTIQGAPS DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPAR PRSPSQTRKG PPVPPLPKVT PTKELQQENI ISFFEDNFVP EISVTTPSQN EVPEVKKEET LLDLDFDPFK PEVTPAGSAG VTHSPMSQTL PWDLWTTSTD LVQPASGGSF NGFTQPQDTS LFTMQTDQSM ICNLIIPGAD ADAAVGTLVS AAEGAPGEEA EAEKATVPAG EGVSLEEAKI GTETTEGAES AQPEAEELEA TVPQEKVIPS VVIEPASNHE EEGENEITIG AEPKETTEDA APPGPTSETP ELATEQKPIQ DPQPTPSAPA MGAADQLASA REASQELPPG FLYKVETLHD FEAANSDELT LQRGDVVLVV PSDSEADQDA GWLVGVKESD WLQYRDLATY KGLFPENFTR RLD // ID O43541 PRELIMINARY; PRT; 496 AA. AC O43541; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE SMAD6. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Hata A., Lagna G., Massague J., Hemmati-Brivanlou A.; RL Genes Dev. 0:0-0(1997). DR EMBL; AF035528; AAB94137.1; -. DR INTERPRO; IPR001132; -. DR PFAM; PF00968; Dwarfin; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens Smad6 mRNA, complete cds. ** [1] ** 1-2887 ** Hata A., Lagna G., Massague J., Hemmati-Brivanlou A.; ** "Smad6 inhibits BMP/Smad1 signaling by specifically competing with the ** Smad4 tumor suppressor"; ** Genes Dev. 0:0-0(1997). ** [2] ** 1-2887 ** Hata A., Lagna G., Massague J., Hemmati-Brivanlou A.; ** ; ** Submitted (21-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Laboratory of Molecular Embryology, The Rockefeller University, 1230 ** York Avenue, New York, NY 10021, USA ** source 1..2887 ** /organism="Homo sapiens" ** /cell_line="Jurkat T-cell" ** CDS 937..2427 ** /codon_start=1 ** /db_xref="PID:g2736316" ** /note="SMAD family member" ** /function="inhibitor of BMP signaling" ** /product="Smad6" ** CDS_IN_EMBL_ENTRY 1 ** 07-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00968; Dwarfin; 132; 495; T; 19-JUN-2000; SQ SEQUENCE 496 AA; 53496 MW; 4D50B634D8911B37 CRC64; MFRSKRSGLV RRLWRSRVVP NREEGGSGGG GGGDEDGSLG SRAEPAPRAR EGGGCGRSEV RPVAPRRPRD AVGQRGAQGA GRRRRAGGPP RPMSEPGAGA GSSLLDVAEP GGPGWLPESD CETVTCCLFS ERDAAGAPRD ASDPLAGAAL EPAGGGRSRE ARSRLLLLEQ ELKTVTYSLL KRLKERSLDT LLEAVESRGG VPGGCVLVPR ADLRLGGQPA PPQLLLGRLF RWPDLQHAVE LKPLCGCHSF AAAADGPTVC CNPYHFSRLC GPESPPPPYS RLSPRDEYKP LDLSDSTLSY TETEATNSLI TAPGEFSDAS MSPDATKPSH WCSVAYWEHR TRVGRLYAVY DQAVSIFYDL PQGSGFCLGQ LNLEQRSESV RRTRSKIGFG ILLSKEPDGV WAYNRGEHPI FVNSPTLDAP GGRALVVRKV PPGYSIKVFD FERSGLQHAP EPDAADGPYD PNSVRISFAK GWGPCYSRQF ITSCPCWLEI LLNNPR // ID O43545 PRELIMINARY; PRT; 179 AA. AC O43545; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE MESODERM-SPECIFIC BASIC-HELIX-LOOP-HELIX PROTEIN. GN POD1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Quaggin S.E., Vanden Heuvel G.B., Igarashi P.; RL Mech. Dev. 0:0-0(1997). DR EMBL; AF035718; AAC62514.1; -. DR HSSP; P10085; 1MDY. DR INTERPRO; IPR001092; -. DR INTERPRO; IPR003015; -. DR PFAM; PF00010; HLH; 1. DR PROSITE; PS00038; HELIX_LOOP_HELIX; UNKNOWN_1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens mesoderm-specific basic-helix-loop-helix protein ** (POD1) mRNA, complete cds. ** [1] ** 1-1254 ** Quaggin S.E., Vanden Heuvel G.B., Igarashi P.; ** "Pod-1, A Mesoderm-Specific Basic-Helix-Loop-Helix Protein Expressed ** in ** Mesenchymal and Glomerular Epithelial Cells in the Developing Kidney"; ** Mech. Dev. 0:0-0(1997). ** [2] ** 1-1254 ** Quaggin S.E., Vanden Heuvel G.B., Igarashi P.; ** ; ** Submitted (24-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Internal Medicine, Yale University, 333 Cedar Street, New Haven, CT ** 06520-8029, USA ** source 1..1254 ** /organism="Homo sapiens" ** /chromosome="6" ** CDS 261..800 ** /codon_start=1 ** /db_xref="PID:g2745887" ** /note="Pod-1" ** /gene="POD1" ** /product="mesoderm-specific basic-helix-loop-helix ** protein" ** misc_feature 492..653 ** /note="encodes basic-helix-loop-helix domain" ** /gene="POD1" ** AA 78 -> 131 ** CDS_IN_EMBL_ENTRY 1 ** 08-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00010; HLH; 80; 132; T; 19-JUN-2000; **PM PROSITE; PS00038; HELIX_LOOP_HELIX; 116; 131; ?; 19-JUN-2000; **PM PROSITE; PS50037; HELIX_LOOP_HELIX_2; 89; 129; T; 19-JUN-2000; SQ SEQUENCE 179 AA; 19743 MW; 9B6F496C4A6B658A CRC64; MSTGSLSDVE DLQEVEMLEC DGLKMDSNKE FVTSNESTEE SSNCENGSPQ KGRGGLGKRR RAPTKKSPLS GVSQEGKQVQ RNAANARERA RMRVLSKAFS RLKTTLPWVP PDTKLSKLDT LRLASSYIAH LRQILANDKY ENGYIHPVNL TWPFMVAGKP ESDLKEVVTA SRLCGTTAS // ID O43547 PRELIMINARY; PRT; 232 AA. AC O43547; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE VESICLE SOLUBLE NSF ATTACHMENT PROTEIN RECEPTOR. GN VTI1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98112804; PubMed=9446565; RA Fischer von Mollard G., Stevens T.H.; RT "A human homolog can functionally replace the yeast vesicle-associated RT SNARE Vti1p in two vesicle transport pathways."; RL J. Biol. Chem. 273:2624-2630(1998). DR EMBL; AF035824; AAC52016.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens vesicle soluble NSF attachment protein receptor (VTI1) ** mRNA, complete cds. ** [1] ** 1-935 ** Fischer von Mollard G., Stevens T.H.; ** "A human homolog can functionally replace the yeast v-SNARE Vti1p in ** two ** vesicle transport pathways"; ** J. Biol. Chem. 273:2624-2630(1998). ** [2] ** 1-935 ** Fischer von Mollard G., Stevens T.H.; ** ; ** Submitted (25-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Institute of Molecular Biology, University of Oregon, Eugene, OR ** 97403, ** USA ** source 1..935 ** /organism="Homo sapiens" ** CDS 72..770 ** /codon_start=1 ** /db_xref="PID:g2687400" ** /note="Vti1; v-SNARE" ** /gene="VTI1" ** /product="vesicle soluble NSF attachment protein ** receptor" ** CDS_IN_EMBL_ENTRY 1 ** 05-FEB-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 232 AA; 26687 MW; E34B62215F5F1EDC CRC64; MASSAASSEH FEKLHEIFRG LHENLQGVPE RLLGTAGTEE KKKLIRDFDE KQQEANETLA EMEEELRYAP LSFRNPMMSK LRNYRKDLAK LHREVRSTPL TATPGGRGDM KYGIYAVENE HMNRLQSQRA MLLQGTESLN RATQSIERSH RIATETDQIG SEIIEELGEQ RDQLERTKSR LVNTSENLSK SRKILRSMSR KVTTNKLLLS IIILLELAIL GGLVYYKFFR SH // ID O43557 PRELIMINARY; PRT; 240 AA. AC O43557; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE TUMOR NECROSIS FACTOR SUPERFAMILY MEMBER LIGHT. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98122340; PubMed=9462508; RA Mauri D.N., Ebner R., Montgomery R.I., Kochel K.D., Cheung T.C., RA Yu G.-L., Ruben S., Murphy M., Eisenberg R.J., Cohen G.H., Spear P.G., RA Ware C.F.; RT "LIGHT, a new member of the TNF superfamily, and lymphotoxin alpha are RT ligands for herpesvirus entry mediator."; RL Immunity 8:21-30(1998). DR EMBL; AF036581; AAC39563.1; -. DR HSSP; P01375; 4TSV. DR INTERPRO; IPR000478; -. DR PFAM; PF00229; TNF; 1. DR PROSITE; PS50049; TNF_2; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens tumor necrosis factor superfamily member LIGHT mRNA, ** complete cds. ** [1] ** 1-1169 ** Mauri D.N., Ebner R., Montgomery R.I., Kochel K.D., Cheung T.C., ** Yu G.-L., Ruben S., Murphy M., Eisenberg R.J., Cohen G.H., Spear P.G., ** Ware C.F.; ** "LIGHT, a new member of the TNF superfamily, and lymphotoxin (LT)a are ** ligands for herpesvirus entry mediator (HVEM)"; ** Immunity 8:21-30(1998). ** [2] ** 1-1169 ** Ebner R., Kochel K.D., Ware C.F.; ** ; ** Submitted (02-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Division of Molecular Immunology, La Jolla Institute for Allergy and ** Immunology, 10355 Science Center Drive, San Diego, CA 92121, USA ** source 1..1169 ** /organism="Homo sapiens" ** /chromosome="16" ** /cell_type="peripheral blood mononuclear cells ** activated ** with phorbol ester and phytohemagglutinin for 12 hr" ** CDS 49..771 ** /codon_start=1 ** /db_xref="PID:g2815624" ** /function="ligand for herpesvirus entry mediator ** (HVEM) and ** lymphotoxin-beta receptor (LTbR)" ** /product="tumor necrosis factor superfamily member ** LIGHT" ** CDS_IN_EMBL_ENTRY 1 ** 31-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00229; TNF; 93; 240; T; 19-JUN-2000; **PM PROSITE; PS50049; TNF_2; 95; 240; T; 19-JUN-2000; SQ SEQUENCE 240 AA; 26351 MW; 49D0BF67E1390B39 CRC64; MEESVVRPSV FVVDGQTDIP FTRLGRSHRR QSCSVARVGL GLLLLLMGAG LAVQGWFLLQ LHWRLGEMVT RLPDGPAGSW EQLIQERRSH EVNPAAHLTG ANSSLTGSGG PLLWETQLGL AFLRGLSYHD GALVVTKAGY YYIYSKVQLG GVGCPLGLAS TITHGLYKRT PRYPEELELL VSQQSPCGRA TSSSRVWWDS SFLGGVVHLE AGEEVVVRVL DERLVRLRDG TRSYFGAFMV // ID O43561 PRELIMINARY; PRT; 262 AA. AC O43561; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE LINKER FOR ACTIVATION OF T CELLS (LAT). GN LAT. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; RL Cell 0:0-0(1997). DR EMBL; AF036906; AAC39637.1; -. DR INTERPRO; IPR000345; -. DR PROSITE; PS00190; CYTOCHROME_C; UNKNOWN_1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens linker for activation of T cells (LAT) mRNA, ** alternatively spliced form, complete cds. ** [1] ** 1-1460 ** Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; ** "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor ** to ** cellular activation"; ** Cell 0:0-0(1997). ** [2] ** 1-1460 ** Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; ** ; ** Submitted (05-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Cell Biology and Metabolism Branch, National Institute of Child Health ** and Development, National Institute of Health, 9000 Rockville Pike, ** Bethesda, MD 20892, USA ** LAT is a highly tyrosine phosphorylated protein, previously ** described as p36-38, and it associates with many signaling ** molecules, such as Grb2, PLC-gamma1, PI-3 kinase, cbl, Vav, and ** SLP-76, either directly or indirectly upon T cell activation. It is ** a potential type III transmembrane protein. ** source 1..1460 ** /organism="Homo sapiens" ** /cell_line="Jurkat T cells" ** CDS 79..867 ** /codon_start=1 ** /db_xref="PID:g2828026" ** /note="tyrosine kinase substrate; This a alternatively ** spliced form of LAT" ** /gene="LAT" ** /product="LAT" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS00190; CYTOCHROME_C; 26; 31; ?; 19-JUN-2000; SQ SEQUENCE 262 AA; 27930 MW; BCD80AE7DCA64153 CRC64; MEEAILVPCV LGLLLLPILA MLMALCVHCH RLPGSYDSTS SDSLYPRGIQ FKRPHTVAPW PPAYPPVTSY PPLSQPDLLP IPRSPQPLGG SHRTPSSRRD SDGANSVASY ENEGASGIRG AQAGWGVWGP SWTRLTPVSL PPEPACEDAD EDEDDYHNPG YLVVLPDSTP ATSTAAPSAP ALSTPGIRDS AFSMESIDDY VNVPESGESA EASLDGSREY VNVSQELHPG AAKTEPAALS SQEAEEVEEE GAPDYENLQE LN // ID O43562 PRELIMINARY; PRT; 424 AA. AC O43562; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE ORGANIC CATION TRANSPORTER-LIKE PROTEIN 2. GN ORCTL2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Cooper P.R., Smilinich N.J., Day C.D., Nowak N.J., Reid L.H., RA Pearsall R.S., Reece M., Prawitt D., Landers J., Housman D.E., RA Winterpacht A., Zabel B.U., Pelletier J., Weissman B.E., Shows T.B., RA Higgins M.J.; RL Genomics 0:0-0(1998). DR EMBL; AF037064; AAC04787.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens organic cation transporter-like protein 2 (ORCTL2) ** mRNA, complete cds. ** [1] ** 1-1535 ** Cooper P.R., Smilinich N.J., Day C.D., Nowak N.J., Reid L.H., ** Pearsall R.S., Reece M., Prawitt D., Landers J., Housman D.E., ** Winterpacht A., Zabel B.U., Pelletier J., Weissman B.E., Shows T.B., ** Higgins M.J.; ** "Divergently transcribed overlapping genes expressed in liver and ** kidney ** and located in the 11p15.5 imprinted domain"; ** Genomics 0:0-0(1998). ** [2] ** 1-1535 ** Cooper P.R., Shows T.B., Pelletier J., Landers J., Higgins M.J.; ** ; ** Submitted (08-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Human Genetics, Roswell Park Cancer Institute, Elm and Carlton ** Streets, ** Buffalo, NY 14263, USA ** source 1..1535 ** /organism="Homo sapiens" ** /chromosome="11" ** /map="11p15.5" ** CDS 203..1477 ** /codon_start=1 ** /db_xref="PID:g2921449" ** /note="predicted integral membrane protein functioning ** in ** organic cation transport. A second in frame ATG is ** present ** at position 251. In the mouse gene, the corresponding ** ATG ** is contained within a better translational context ** suggesting that translation may start at the second ** ATG in ** both cases" ** /gene="ORCTL2" ** /product="organic cation transporter-like protein 2" ** CDS_IN_EMBL_ENTRY 1 ** 10-MAR-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 424 AA; 44864 MW; 6EFD5F912A7761F5 CRC64; MQGARAPRDQ GRSPGRMSAL GRSSVILLTY VLAATELTCL FMQFSIVPYL SRKLGLDSIA FGYLQTTFGV LQLLGGPVFG RFADQRGARA ALTLSFLAAL ALYLLLAAAS SPALPGVYLL FASRLPGALM HTLPAAQMVI TDLSAPEERP AALGRLGLCF GVGVILGSLL GGTLVSAYGI QCPAILAALA TLLGAVLSFT CIPASTKGAK TDAQAPLPGG PRASVFDLKA IASLLRLPDV PRIFLVKVAS NCPTGLFMVM FSIISMDFFQ LEAAQAGYLM SFFGLLQMVT QGLVIGQLSS HFSEEVMLRA SVLVFIVVGL AMAWMSSVFH FCLLVPGLVF SLCTLNVVTD SMLIKAVSTS DTGTMLGLCA SVQPLLRTLG PTVGGLLYRS FGVPVFGHVQ VAINTLVLLV LWRKPMPQRK DKVR // ID O43568 PRELIMINARY; PRT; 346 AA. AC O43568; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE XRCC3. GN XRCC3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Liu N., Lamerdin J.E., Tebbs R.S., Schild D., Tucker J.D., Shen R., RA Brookman K.W., Siciliano M.J., Walter C.A., Fan W., Narayana L.S., RA Zhou Z.-Q., Adamson A.W., Sorenson K.J., Chen D.J., Jones N.J., RA Thompson L.H.; RL Mol. Cell 0:0-0(1998). DR EMBL; AF037222; AAC04805.1; -. DR INTERPRO; IPR001553; -. ** ** ################# SOURCE SECTION ################## ** Human DNA from chromosome 14-specific cosmid containing XRCC3 DNA ** repair gene, genomic sequence, complete sequence. ** [1] ** 1-36628 ** Liu N., Lamerdin J.E., Tebbs R.S., Schild D., Tucker J.D., Shen R., ** Brookman K.W., Siciliano M.J., Walter C.A., Fan W., Narayana L.S., ** Zhou Z.-Q., Adamson A.W., Sorenson K.J., Chen D.J., Jones N.J., ** Thompson L.H.; ** "XRCC2 and XRCC3, New Members of the Rad51 Family, Promote Chromosome ** Stability and Protect Against DNA Damages"; ** Mol. Cell 0:0-0(1998). ** [2] ** 1-36628 ** Lamerdin J.E.; ** ; ** Submitted (08-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Human Genome Center, Lawrence Livermore National Laboratory, 7000 East ** Ave., Livermore, CA 94551, USA ** source 1..36628 ** /organism="Homo sapiens" ** /chromosome="14" ** /note="cosmid from library constructed at LANL from ** flow-sorted material containing chromosome 14 as the ** only ** human chromosome" ** /clone="hsXRCC3GEN" ** /map="14q32.3" ** CDS join(6396..6450,8824..8961,10268..10480,14156..14310, ** 17907..18119,18304..18350,18465..18684) ** /codon_start=1 ** /db_xref="PID:g2921500" ** /note="DNA repair protein" ** /gene="XRCC3" ** /product="XRCC3" ** CDS_IN_EMBL_ENTRY 1 ** 10-MAR-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS50162; RECA_1; 78; 263; T; 19-JUN-2000; SQ SEQUENCE 346 AA; 37880 MW; C531EAE5F307C0E3 CRC64; MDLDLLDLNP RIIAAIKKAK LKSVKEVLHF SGPDLKRLTN LSSPEVWHLL RTASLHLRGS SILTALQLHQ QKERFPTQHQ RLSLGCPVLD ALLRGGLPLD GITELAGRSS AGKTQLALQL CLAVQFPRQH GGLEAGAVYI CTEDAFPHKR LQQLMAQQPR LRTDVPGELL QKLRFGSQIF IEHVADVDTL LECVNKKVPV LLSRGMARLV VIDSVAAPFR CEFDSQASAP RARHLQSLGA MLRELSSAFQ SPVLCINQVT EAMEEQGAAH GPLGFWDERV SPALGITWAN QLLVRLLADR LREEEAALGC PARTLRVLSA PHLPPSSCSY TISAEGVRGT PGTQSH // ID O43574 PRELIMINARY; PRT; 777 AA. AC O43574; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE BRCA1-ASSOCIATED RING DOMAIN PROTEIN. GN BARD1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Thai T.H., Du F., Tsan J.T., Jin Y., Phung A., Spillman M.A., RA Massa H.F., Muller C.Y., Ashfaq R., Mathis J.M., Miller D.S., RA Trask B.J., Baer R., Bowcock A.M.; RL Hum. Mol. Genet. 0:0-0(1998). CC -!- SIMILARITY: CONTAINS A C3HC4-CLASS ZINC FINGER. DR EMBL; AF038042; AAB99978.1; -. DR EMBL; AF038034; AAB99978.1; JOINED. DR EMBL; AF038035; AAB99978.1; JOINED. DR EMBL; AF038036; AAB99978.1; JOINED. DR EMBL; AF038037; AAB99978.1; JOINED. DR EMBL; AF038038; AAB99978.1; JOINED. DR EMBL; AF038039; AAB99978.1; JOINED. DR EMBL; AF038040; AAB99978.1; JOINED. DR EMBL; AF038041; AAB99978.1; JOINED. DR HSSP; P25963; 1IKN. DR INTERPRO; IPR001357; -. DR INTERPRO; IPR001841; -. DR INTERPRO; IPR002110; -. DR PFAM; PF00023; ank; 3. DR PROSITE; PS00518; ZINC_FINGER_C3HC4; 1. KW Zinc-finger. ** ** ################# SOURCE SECTION ################## ** Homo sapiens BRCA1-associated RING domain protein (BARD1) gene, ** exons 10, 11 and complete cds. ** [1] ** 1-4334 ** Thai T.H., Du F., Tsan J.T., Jin Y., Phung A., Spillman M.A., ** Massa H.F., Muller C.Y., Ashfaq R., Mathis J.M., Miller D.S., ** Trask B.J., Baer R., Bowcock A.M.; ** "Mutations in the BRCA1-associated RING domain (BARD1) gene in primary ** breast, ovarian and uterine cancers"; ** Hum. Mol. Genet. 0:0-0(1998). ** [2] ** 1-4334 ** Thai T.H., Du F., Tsan J.T., Jin Y., Phung A., Spillman M.A., ** Massa H.F., Muller C.Y., Ashfaq R., Mathis J.M., Miller D.S., ** Trask B.J., Baer R., Bowcock A.M.; ** ; ** Submitted (11-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Microbiology, UT Southwestern Medical Center, 6000 Harry Hines Blvd., ** Dallas, TX 75235, USA ** source 1..4334 ** /organism="Homo sapiens" ** /chromosome="2" ** /map="2q34-2q35" ** CDS join(AF038034:174..331,AF038035:2614..2670, ** AF038035:7289..7437,AF038036:621..1570,AF038037:451..531, ** AF038038:508..680,AF038039:548..656,AF038040:566..698, ** AF038041:226..318,519..616,2019..2351) ** /codon_start=1 ** /db_xref="PID:g2828068" ** /gene="BARD1" ** /product="BRCA1-associated RING domain protein" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00023; ank; 427; 459; T; 19-JUN-2000; **PM PFAM; PF00023; ank; 460; 492; T; 19-JUN-2000; **PM PFAM; PF00023; ank; 493; 525; T; 19-JUN-2000; **PM PROSITE; PS00518; ZINC_FINGER_C3HC4; 66; 75; T; 19-JUN-2000; **PM PROSITE; PS50088; ANK_REP; 427; 459; T; 19-JUN-2000; **PM PROSITE; PS50088; ANK_REP; 460; 492; T; 19-JUN-2000; **PM PROSITE; PS50088; ANK_REP; 493; 525; T; 19-JUN-2000; **PM PROSITE; PS50089; ZF_RING; 50; 86; T; 19-JUN-2000; **PM PROSITE; PS50172; BRCT_DOMAIN; 570; 653; T; 19-JUN-2000; **PM PROSITE; PS50172; BRCT_DOMAIN; 667; 777; T; 19-JUN-2000; **PM PROSITE; PS50297; ANK_REP_REGION; 427; 525; T; 19-JUN-2000; **RU RU000251; 22-JAN-1998. SQ SEQUENCE 777 AA; 86579 MW; 51DCB76574015D4D CRC64; MPDNRQPRNR QPRIRSGNEP RSAPAMEPDG RGAWAHSRAA LDRLEKLLRC SRCTNILREP VCLGGCEHIF CSNCVSDCIG TGCPVCYTPA WIQDLKINRQ LDSMIQLCSK LRNLLHDNEL SDLKEDKPRK SLFNDAGNKK NSIKMWFSPR SKKVRYVVSK ASVQTQPAIK KDASAQQDSY EFVSPSPPAD VSERAKKASA RSGKKQKKKT LAEINQKWNL EAEKEDGEFD SKEESKQKLV SFCSQPSVIS SPQINGEIDL LASGSLTESE CFGSLTEVSL PLAEQIESPD TKSRNEVVTP EKVCKNYLTS KKSLPLENNG KRGHHNRLSS PISKRCRTSI LSTSGDFVKQ TVPSENIPLP ECSSPPSCKR KVGGTSGSKN SNMSDEFISL SPGTPPSTLS SSSYRRVMSS PSAMKLLPNM AVKRNHRGET LLHIASIKGD IPSVEYLLQN GSDPNVKDHA GWTPLHEACN HGHLKVVELL LQHKALVNTT GYQNDSPLHD AAKNGHVDIV KLLLSYGASR NAVNIFGLRP VDYTDDESMK SLLLLPEKNE SSSASHCSVM NTGQRRDGPL VLIGSGLSSE QQKMLSELAV ILKAKKYTEF DSTVTHVVVP GDAVQSTLKC MLGILNGCWI LKFEWVKACL RRKVCEQEEK YEIPEGPRRS RLNREQLLPK LFDGCYFYLW GTFKHHPKDN LIKLVTAGGG QILSRKPKPD SDVTQTINTV AYHARPDSDQ RFCTQYIIYE DLCNYHPERV RQGKVWKAPS SWFIDCVMSF ELLPLDS // ID O43588 PRELIMINARY; PRT; 978 AA. AC O43588; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE GENERAL TRANSCRIPTION FACTOR 2-I. GN GTF2I. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., RA Francke U.; RL Hum. Mol. Genet. 0:0-0(1998). DR EMBL; AF038967; AAC08313.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens general transcription factor 2-I (GTF2I) mRNA, ** alternatively spliced product, complete cds. ** [1] ** 1-4423 ** Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., ** Francke U.; ** "A duplicated gene in the breakpoint regions of the 7q11.23 ** Williams-Beuren syndrome deletion encodes the initiator binding ** protein ** TFII-I and BAP-135, a phosphorylation target of Btk"; ** Hum. Mol. Genet. 0:0-0(1998). ** [2] ** 1-4423 ** Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., ** Francke U.; ** ; ** Submitted (18-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Howard Hughes Medical Institute, Stanford Medical Center, Beckman ** Center ** B201, Stanford, CA 94305, USA ** source 1..4423 ** /organism="Homo sapiens" ** /chromosome="7" ** /map="7q11.23" ** CDS 317..3253 ** /codon_start=1 ** /db_xref="PID:g2827203" ** /note="alternatively spliced" ** /gene="GTF2I" ** /product="general transcription factor 2-I" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 978 AA; 110280 MW; 1F006D480F0BE702 CRC64; MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ YNIQGSHHSS EGNEGTEMEV PAEDSTQHVP SETSEDPEVE VTIEDDDYSP PSKRPKANEL PQPPVPEPAN AGKRKVREFN FEKWNARITD LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE GLPEGIPFRR PSTYGIPRLE RILLAKERIR FVIKKHELLN STREDLQLDK PASGVKEEWY ARITKLRKMV DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR PELLTHSTTE VTQPRTNTPV KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK FVVKKPELVI SYLPPGMASK INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNNNPQTSA VRTPTQTNGS NVPFKPRGRE FSFEAWNAKI TDLKQKVENL FNEKCGEALG LKQAVKVPFA LFESFPEDFY VEGLPEGVPF RRPSTFGIPR LEKILRNKAK IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG VEDLNIIQVT IPDDDNERLS KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN PGCVVVDGMP PGVSFKAPSY LEISSMRRIL DSAEFIKFTV IRPFPGLVIN NQLVDQSESE GPVIQESAEP SQLEVPATEE IKETDGSSQI KQEPDPTW // ID O43589 PRELIMINARY; PRT; 977 AA. AC O43589; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE GENERAL TRANSCRIPTION FACTOR 2-I. GN GTF2I. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., RA Francke U.; RL Hum. Mol. Genet. 0:0-0(1998). DR EMBL; AF038968; AAC08314.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens general transcription factor 2-I (GTF2I) mRNA, ** alternatively spliced product, complete cds. ** [1] ** 1-4420 ** Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., ** Francke U.; ** "A duplicated gene in the breakpoint regions of the 7q11.23 ** Williams-Beuren syndrome deletion encodes the initiator binding ** protein ** TFII-I and BAP-135, a phosphorylation target of Btk"; ** Hum. Mol. Genet. 0:0-0(1998). ** [2] ** 1-4420 ** Perez-Jurado L.A., Wang Y.K., Peoples R., Coloma A., Cruces J., ** Francke U.; ** ; ** Submitted (18-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Howard Hughes Medical Institute, Stanford Medical Center, Beckman ** Center ** B201, Stanford, CA 94305, USA ** source 1..4420 ** /organism="Homo sapiens" ** /chromosome="7" ** /map="7q11.23" ** CDS 317..3250 ** /codon_start=1 ** /db_xref="PID:g2827205" ** /note="alternatively spliced" ** /gene="GTF2I" ** /product="general transcription factor 2-I" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 977 AA; 110106 MW; 418D59EC623E6141 CRC64; MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDDDYSPP SKRPKANELP QPPVPEPANA GKRKVREFNF EKWNARITDL RKQVEELFER KYAQAIKAKG PVTIPYPLFQ SHVEDLYVEG LPEGIPFRRP STYGIPRLER ILLAKERIRF VIKKHELLNS TREDLQLDKP ASGVKEEWYA RITKLRKMVD QLFCKKFAEA LGSTEAKAVP YQKFEAHPND LYVEGLPENI PFRSPSWYGI PRLEKIIQVG NRIKFVIKRP ELLTHSTTEV TQPRTNTPVK EDWNVRITKL RKQVEEIFNL KFAQALGLTE AVKVPYPVFE SNPEFLYVEG LPEGIPFRSP TWFGIPRLER IVRGSNKIKF VVKKPELVIS YLPPGMASKI NTKALQSPKR PRSPGSNSKV PEIEVTVEGP NNNNPQTSAV RTPTQTNGSN VPFKPRGREF SFEAWNAKIT DLKQKVENLF NEKCGEALGL KQAVKVPFAL FESFPEDFYV EGLPEGVPFR RPSTFGIPRL EKILRNKAKI KFIIKKPEMF ETAIKESTSS KSPPRKINSS PNVNTTASGV EDLNIIQVTI PDDDNERLSK VEKARQLREQ VNDLFSRKFG EAIGMGFPVK VPYRKITINP GCVVVDGMPP GVSFKAPSYL EISSMRRILD SAEFIKFTVI RPFPGLVINN QLVDQSESEG PVIQESAEPS QLEVPATEEI KETDGSSQIK QEPDPTW // ID O43592 PRELIMINARY; PRT; 962 AA. AC O43592; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE EXPORTIN T. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Kutay U., Lipowsky G., Izaurralde E., Schwarzmaier P., Hartmann E., RA Goerlich D.; RL Mol. Cell 0:0-0(1998). DR EMBL; AF039022; AAC39793.1; -. ** ** ################# SOURCE SECTION ################## ** Homo sapiens exportin t mRNA, complete cds. ** [1] ** 1-2889 ** Kutay U., Lipowsky G., Izaurralde E., Schwarzmaier P., Hartmann E., ** Goerlich D.; ** "Identification of a t-RNA-specific nuclear export receptor"; ** Mol. Cell 0:0-0(1998). ** [2] ** 1-2889 ** Goerlich D., Hartmann E.; ** ; ** Submitted (17-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Zellbiologie, MDC Berlin, Robert-Roessle-Str. 10, Berlin 13125, ** Deutschland ** source 1..2889 ** /organism="Homo sapiens" ** CDS 1..2889 ** /codon_start=1 ** /db_xref="PID:g2873377" ** /function="nuclear export factor involved in tRNA ** export" ** /function="binds to Ran-GTP" ** /product="exportin t" ** CDS_IN_EMBL_ENTRY 1 ** 16-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 962 AA; 109992 MW; 317F7FB8186A58F1 CRC64; MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQRTYSDD HVKFFCFQVL EHQVKYKYSE LTTVQQQLIR ETLISWLQAQ MLNPQPEKTF IRNKAAQVFA LLFVTEYLTK WPKFFFDILS VVDLNPRGVD LYLRILMAID SELVDRDVVH TSEEARRNTL IKDTMREQCI PNLVESWYQI LQNYQFTNSE VTCQCLEVVG AYVSWIDLSL IANDRFINML LGHMSIEVLR EEACDCLFEV VNKGMDPVDK MKLVESLCQV LQSAGFFSID QEEDVDFLAR FSKLVNGMGQ SLIVSWSKLI KNGDIKNAQE ALQAIETKVA LMLQLLIHED DDISSNIIGF CYDYLHILKR LTVLSDQQKA NVEAIMLAVM KKLTYDEEYN FENEGEDEAM FVEYRKQLKL LLDRLAQVSP ELLLASVRRV FSSTLQNWQT TRFMEVEVAI RLLYMLAEAL PVSHGAHFSG DVSKASALQD MMRTLVTSGV SSYQHTSVTL EFFETVVRYE KFFTVEPQHI PCVLMAFLDH RGLRHSSAKV RSRTAYLFSR FVKSLNKQMN PFIEDILNRI QDLLELSPPE NGHQSLLSSD DQLFIYETAG VLIVNSEYPA ERKQALMRNL LTPLMEKFKI LLEKLMLAQD EERQASLADC LNHAVGFASR TSKAFSNKQT VKQCGCSEVY LDCLQTFLPA LSCPLQKDIL RSGVRTFLHR MIICLEEEVL PFIPSASEHM LKDCEAKDLQ EFIPLINQIT AKFKIQVSPF LQQMFMPLLH AIFEVLLRPA EENDQSAALE KQMLRRSYFA FLQTVTGSGM SEVIANQGAE NVERVLVTVI QGAVEYPDPI AQKTCFIILS KLVELWGGKD GPVGFADFVY KHIVPACFLA PLKQTFDLAD AQTVLALSEC AVTLKTIHLK RGPECVQYLQ QEYLPSLQVA PEIIQEFCQA LQQPDAKVFK NYLKVFFQRA KP // ID O43629 PRELIMINARY; PRT; 194 AA. AC O43629; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE OLFACTORY RECEPTOR-LIKE PROTEIN (FRAGMENT). GN OLFR42A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Gallinaro H.; RL Immunogenetics 0:0-0(1998). DR EMBL; AF042078; AAC00184.1; -. DR INTERPRO; IPR000276; -. DR PFAM; PF00001; 7tm_1; 1. DR PROSITE; PS00237; G_PROTEIN_RECEPTOR; UNKNOWN_1. FT NON_TER 1 1 FT NON_TER 194 194 ** ** ################# SOURCE SECTION ################## ** Homo sapiens olfactory receptor-like protein (OLFR42A) gene, ** OLFR42A-9026.2 allele, partial cds. ** [1] ** 1-583 ** Gallinaro H.; ** "Olfactory receptor gene cluster in man and mouse major ** histocompatibility complex"; ** Immunogenetics 0:0-0(1998). ** [2] ** 1-583 ** Gallinaro H.; ** ; ** Submitted (09-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, CIGH-CNRS, 1 Avenue de Grande Bretagne, Toulouse ** 31300, France ** source 1..583 ** /organism="Homo sapiens" ** /chromosome="6" ** /map="6p21.3" ** /cell_line="12th IHW # 9026" ** CDS <1..>583 ** /codon_start=1 ** /db_xref="PID:g2828682" ** /gene="OLFR42A" ** /product="olfactory receptor-like protein" ** CDS_IN_EMBL_ENTRY 1 ** 05-FEB-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00001; 7tm_1; 1; 189; T; 19-JUN-2000; **PM PROSITE; PS00237; G_PROTEIN_RECEPTOR; 51; 67; ?; 19-JUN-2000; **PM PROSITE; PS50262; G_PROTEIN_RECEPTOR_2; 1; 194; T; 19-JUN-2000; SQ SEQUENCE 194 AA; 21527 MW; 6A23FBF2FDCACEAF CRC64; YFFLSNLSFL DLCFTTSCVP QMLVNLWGPK KTISFLGCSV QLFIFLSLGT TECILLTVMA FDRYVAVCQP LHYATIIHPR LCWQLASVAW VMSLVQSIVQ TPSTLHLPFC PHQQIDDFLC EVPSLIRLSC GDTSYNEIQL AVSSVIFVVV PLSLILASYG ATAQAVLRIN SATAWRKAFG TCSSHLTVVT LFYS // ID O43636 PRELIMINARY; PRT; 1245 AA. AC O43636; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE ROD PHOTORECEPTOR CNG-CHANNEL BETA SUBUNIT. GN RCNC2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Grunwald M.E., Yu W.P., Yu H.H., Yau K.W.; RL J. Biol. Chem. 0:0-0(1998). DR EMBL; AF042498; AAC04830.1; -. DR INTERPRO; IPR000595; -. DR INTERPRO; IPR001622; -. DR INTERPRO; IPR002025; -. DR PFAM; PF00027; cNMP_binding; 1. DR PFAM; PF00914; CNG_membrane; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 1. DR PROSITE; PS00889; CNMP_BINDING_2; 1. DR PROSITE; PS50042; CNMP_BINDING_3; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens rod photoreceptor CNG-channel beta subunit (RCNC2) ** mRNA, complete cds. ** [1] ** 1-4382 ** Grunwald M.E., Yu W.P., Yu H.H., Yau K.W.; ** "Identification of a domain on the beta subunit of the rod cGMP-gated ** cation channel that mediates inhibition by calcium-calmodulin"; ** J. Biol. Chem. 0:0-0(1998). ** [2] ** 1-4382 ** Grunwald M.E., Yu W.P., Yu H.H., Yau K.W.; ** ; ** Submitted (12-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Neuroscience, Johns Hopkins University School of Medicine, 725 N. ** Wolfe ** St., Baltimore, MD 21205, USA ** source 1..4382 ** /organism="Homo sapiens" ** CDS 71..3808 ** /codon_start=1 ** /db_xref="PID:g2921583" ** /note="cyclic nucleotide-gated cation channel beta ** subunit" ** /gene="RCNC2" ** /product="rod photoreceptor CNG-channel beta subunit" ** CDS_IN_EMBL_ENTRY 1 ** 10-MAR-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00027; cNMP_binding; 971; 1065; T; 19-JUN-2000; **PM PFAM; PF00914; CNG_membrane; 726; 942; T; 19-JUN-2000; **PM PROSITE; PS00888; CNMP_BINDING_1; 983; 999; T; 19-JUN-2000; **PM PROSITE; PS00889; CNMP_BINDING_2; 1022; 1042; T; 19-JUN-2000; **PM PROSITE; PS50042; CNMP_BINDING_3; 956; 1060; T; 19-JUN-2000; **PM PROSITE; PS50265; CHANNEL_PORE_K; 825; 877; T; 19-JUN-2000; SQ SEQUENCE 1245 AA; 139160 MW; 40C4860BFCF86126 CRC64; MLGWVQRVLP QPPGTPRKTK MQEEEEVEPE PEMEAEVEPE PNPEEAETES ESMPPEESFK EEEVAVADPS PQETKEAALT STISLRAQGA EISEMNSPSH RVLTWLMKGV EKVIPQPVHS ITEDPAQILG HGSTGDTGCT DEPNEALEAQ DTRPGLRLLL WLEQNLERVL PQPPKSSEVW RDEPAVATAP PGRPQEMGPK LQARETPSLP TPIPLQPKEE PKEAPAPEPQ PGSQAQTSSL PPTRDPARLV AWVLHRLEMA LPQPVLHGKI GEQEPDSPGI CDVQTISILP GGQVEPDLVL EEVEPPWEDA HQDVSTSPQG TEVVPAYEEE NKAVEKMPRE LSRIEEEKED EEEEEEEEEE EEEEEVTEVL LDSCVVSQVG VGQSEEDGTR PQSTSDQKLW EEVGEEAKKE AEEKAKEEAE EVAEEEAEKE PQDWAETKEE PEAEAEAASS GVPATKQHPE VQVEDTDADS CPLMAEENPP STVLPPPSPA KSDTLIVPSS ASGTHRKKLP SEDDEAEELK ALSPAESPVV AWSDPTTPKD TDGQDRAAST ASTNSAIIND RLQELVKLFK ERTEKVKEKL IDPDVTSDEE SPKPSPAKKA PEPAPDTKPA EAEPVEEEHY CDMLCCKFKH RPWKKYQFPQ SIDPLTNLMY VLWLFFVVMA WNWNCWLIPV RWAFPYQTPD NIHHWLLMDY LCDLIYFLDI TVFQTRLQFV RGGDIITDKK DMRNNYLKSR RFKMDLLSLL PLDFLYLKVG VNPLLRLPRC LKYMAFFEFN SRLESILSKA YVYRVIRTTA YLLYSLHLNS CLYYWASAYQ GLGSTHWVYD GVGNSYIRCY YFAVKTLITI GGLPDPKTLF EIVFQLLNYF TGVFAFSVMI GQMRDVVGAA TAGQTYYRSC MDSTVKYMNF YKIPKSVQNR VKTWYEYTWH SQGMLDESEL MVQLPDKMRL DLAIDVNYNI VSKVALFQGC DRQMIFDMLK RLRSVVYLPN DYVCKKGEIG REMYIIQAGQ VQVLGGPDGK SVLVTLKAGS VFGEISLLAV GGGNRRTANV VAHGFTNLFI LDKKDLNEIL VHYPESQKLL RKKARRMLRS NNKPKEEKSV LILPPRAGTP KLFNAALAMT GKMGGKGAKG GKLAHLRARL KELAALEAAA KQQELVEQAK SSQDVKGEEG SAAPDQHTHP KEAATDPPAP RTPPEPPGSP PSSPPPASLG RPEGEEEGPA EPEEHSVRIC MSPGPEPGEQ ILSVKMPEER EEKAE // ID O43707 PRELIMINARY; PRT; 884 AA. AC O43707; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE ALPHA ACTININ 4. GN HACTN4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Honda K., Yamada T., Endo R., Ino Y., Gotoh M., Tsuda H., Yamada Y., RA Chiba H., Hirohashi S.; RL J. Cell Biol. 0:0-0(1998). DR EMBL; D89980; BAA24447.1; -. DR HSSP; Q01082; 1AA2. DR INTERPRO; IPR001589; -. DR INTERPRO; IPR001715; -. DR INTERPRO; IPR002017; -. DR INTERPRO; IPR002048; -. DR PFAM; PF00036; efhand; 2. DR PFAM; PF00307; CH; 2. DR PFAM; PF00435; spectrin; 4. DR PROSITE; PS00018; EF_HAND; UNKNOWN_1. DR PROSITE; PS00019; ACTININ_1; 1. DR PROSITE; PS00020; ACTININ_2; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens mRNA for alpha actinin 4, complete cds. ** [1] ** 1-2873 ** Honda K.; ** ; ** Submitted (20-DEC-1996) to the EMBL/GenBank/DDBJ databases. ** Kazufumi Honda, National Cancer Center Research Institute, Pathology ** Division; 1-1 Tsukiji 5-chome, Chuo-ku, Tokyo 104, Japan ** (E-mail:tyamada@gan2.ncc.go.jp, Tel:+81-3-3542-2511, ** Fax:+81-3-3248-2737) ** [2] ** Honda K., Yamada T., Endo R., Ino Y., Gotoh M., Tsuda H., Yamada Y., ** Chiba H., Hirohashi S.; ** "Actinin-4, a novel actin-bundling protein associated with cell ** motility ** and cancer invasion"; ** J. Cell Biol. 0:0-0(1998). ** source 1..2873 ** /organism="Homo sapiens" ** /sequenced_mol="cDNA to mRNA" ** /cell_line="NCC-MS-1 CDDP" ** CDS 89..2743 ** /codon_start=1 ** /db_xref="PID:d1025362" ** /transl_table=1 ** /gene="HACTN4" ** /product="alpha actinin 4" ** CDS_IN_EMBL_ENTRY 1 ** 26-FEB-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00036; efhand; 742; 770; T; 19-JUN-2000; **PM PFAM; PF00036; efhand; 783; 811; T; 19-JUN-2000; **PM PFAM; PF00307; CH; 23; 127; T; 19-JUN-2000; **PM PFAM; PF00307; CH; 136; 242; T; 19-JUN-2000; **PM PFAM; PF00435; spectrin; 266; 376; T; 19-JUN-2000; **PM PFAM; PF00435; spectrin; 386; 491; T; 19-JUN-2000; **PM PFAM; PF00435; spectrin; 501; 612; T; 19-JUN-2000; **PM PFAM; PF00435; spectrin; 622; 725; T; 19-JUN-2000; **PM PROSITE; PS00018; EF_HAND; 751; 763; ?; 19-JUN-2000; **PM PROSITE; PS00019; ACTININ_1; 25; 34; T; 19-JUN-2000; **PM PROSITE; PS00020; ACTININ_2; 99; 123; T; 19-JUN-2000; **PM PROSITE; PS50021; CH_DOMAIN; 23; 127; T; 19-JUN-2000; **PM PROSITE; PS50021; CH_DOMAIN; 136; 239; T; 19-JUN-2000; **PM PROSITE; PS50083; SPEC_REPEAT; 353; 455; T; 19-JUN-2000; **PM PROSITE; PS50083; SPEC_REPEAT; 464; 575; T; 19-JUN-2000; **PM PROSITE; PS50083; SPEC_REPEAT; 592; 691; T; 19-JUN-2000; **PM PROSITE; PS50222; EF_HAND_2; 734; 808; T; 19-JUN-2000; SQ SEQUENCE 884 AA; 102268 MW; 0B5D0C6B614E424C CRC64; MGDYMAQEDD WDRDLLLDPA WEKQQRKTFT AWCNSHLRKA GTQIENIDED FRDGLKLMLL LEVISGERLP KPERGKMRVH KINNVNKALD FIASKGVKLV SIGAEEIVDG NAKMTLGMIW TIILRFAIQD ISVEETSAKE GLLLWCQRKT APYKNVNVQN FHISWKDGLA FNALIHRHRP ELIEYDKLRK DDPVTNLNNA FEVAEKYLDI PKMLDAEDIV NTARPDEKAI MTYVSSFYHA FSGAQKAETA ANRICKVLAV NQENEHLMED YEKLASDLLE WIRRTIPWLE DRVPQKTIQE MQQKLEDFRD YRRVHKPPKV QEKCQLEINF NTLQTKLRLS NRPAFMPSEG KMVSDINNGW QHLEQAEKGY EEWLLNEIRR LERLDHLAEK FRQKASIHEA WTDGKEAMLK HRDYETATLS DIKALIRKHE AFESDLAAHQ DRVEQIAAIA QELNELDYYD SHNVNTRCQK ICDQWDALGS LTHSRREALE KTEKQLEAID QLHLEYAKRA APFNNWMESA MEDLQDMFIV HTIEEIEGLI SAHDQFKSTL PDADREREAI LAIHKEAQRI AESNHIKLSG SNPYTTVTPQ IINSKWEKVQ QLVPKRDHAL LEEQSKQQSN EHLRRQFASQ ANVVGPWIQT KMEEIGRISI EMNGTLEDQL SHLKQYERSI VDYKPNLDLL EQQHQLIQEA LIFDNKHTNY TMEHIRVGWE QLLTTIARTI NEVENQILTR DAKGISQEQM QEFRASFNHF DKDHGGALGP EEFKACLISL GYDVENDRQG EAEFNRIMSL VDPNHSGLVT FQAFIDFMSR ETTDTDTADQ VIASFKVLAG DKNFITAEEL RRELPPDQAE YCIARMAPYQ GPDAVPGALD YKSFSTALYG ESDL // ID O43721 PRELIMINARY; PRT; 220 AA. AC O43721; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE HYPOTHETICAL 24.5 kDa PROTEIN. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=FETAL HEART; RX MEDLINE=98153806; PubMed=9480850; RA Vidal-Taboada J.M., Bergonon S., Sanchez M., Lopez-Acedo C., Groet J., RA Nizetic D., Egeo A., Scartezzini P., Katsanis N., Fisher E.M.C., RA Delabar J.M., Oliva R.; RT "High resolution physical mapping and identification of transcribed RT sequences in the Down syndrome region-2."; RL Biochem. Biophys. Res. Commun. 243:572-578(1998). DR EMBL; AJ222636; CAA10896.1; -. KW Hypothetical protein. ** ** ################# SOURCE SECTION ################## ** Homo sapiens partial human cDNA (660 bp) ** [1] ** 1-660 ** Scartezzini P.; ** ; ** Submitted (27-NOV-1997) to the EMBL/GenBank/DDBJ databases. ** Scartezzini P., Pediatrics, E/O Ospedali Galliera, Via Mura delle ** capuccine 14, 16128 Genova, ITALY. ** [3] ** Vidal-Taboada J.M., Bergonon S., Sanchez M., Lopez-Acedo C., Groet J., ** Nizetic D., Egeo A., Scartezzini P., Katsanis N., Fisher E.M.C., ** Delabar J.M., Oliva R.; ** "High resolution physical mapping and identification of transcribed ** sequences in the down syndrome region-2"; ** Biochem. Biophys. Res. Commun. 243:572-578(1998). ** source 1..660 ** /organism="Homo sapiens" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="fetal heart" ** CDS 1..660 ** /codon_start=1 ** /db_xref="PID:e1254889" ** /product="hypothetical protein" ** Warning: illegal start codon ** CDS_IN_EMBL_ENTRY 1 ** 03-MAR-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 220 AA; 24455 MW; 4B795D89F191ECDF CRC64; GTRRSGLSRS SNLRVTRTRA AQRKTGPVSL ANGCGRKATR KRVYLSDSDN NSLETGEILK ARAGNNRKVL RKCAAVAANK IKLMSDVEEN SSSESVCSGR KLPHRNASAV ARKKLLHNSE DEQSLKSEIE EEELKDENQP LPVSSSHTAQ SNVDESENRD SESESDLRVA RKNWHANGYK SHTPAPSKTK FLKIESSEED SKVMIQIMHV QNCWPINVCQ // ID O43919 PRELIMINARY; PRT; 233 AA. AC O43919; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE LINKER FOR ACTIVATION OF T CELLS (LAT). GN LAT OR PP36. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; RL Cell 0:0-0(1997). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=THYMUS; RA Weber J.R., Orstavik S., Torgersen K.M., Danbolt N.C., Berg S.F., RA Tasken K., Imboden J.B., Vaage J.T.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. DR EMBL; AF036905; AAC39636.1; -. DR EMBL; AJ223280; CAA11218.1; -. DR INTERPRO; IPR000345; -. DR PROSITE; PS00190; CYTOCHROME_C; UNKNOWN_1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens linker for activation of T cells (LAT) mRNA, complete ** cds. ** [1] ** 1-1060 ** Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; ** "LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor ** to ** cellular activation"; ** Cell 0:0-0(1997). ** [2] ** 1-1060 ** Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.; ** ; ** Submitted (05-DEC-1997) to the EMBL/GenBank/DDBJ databases. ** Cell Biology and Metabolism Branch, National Institute of Child Health ** and Development, National Institute of Health, 9000 Rockville Pike, ** Bethesda, MD 20892, USA ** LAT is a highly tyrosine phosphorylated protein, previously ** described as p36-38, and it associates with many signaling ** molecules, such as Grb2, PLC-gamma1, PI-3 kinase, cbl, Vav, and ** SLP-76, either directly or indirectly upon T cell activation. It is ** a potential type III transmembrane protein. ** [1] ** 1-1616 ** Orstavik S.; ** ; ** Submitted (09-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Orstavik S., Institute of Medical Biochemistry, University of Oslo, BP ** 1112, Blindern, N-0317 Oslo, NORWAY. ** [2] ** Weber J.R., Orstavik S., Torgersen K.M., Danbolt N.C., Berg S.F., ** Tasken K., Imboden J.B., Vaage J.T.; ** "Cloning of pp36, a tyrosine-phosphorylated adaptor protein ** specifically ** expressed in T and NK cells."; ** Unpublished. ** source 1..1060 ** /organism="Homo sapiens" ** /cell_line="Jurkat T cells" ** CDS 58..759 ** /codon_start=1 ** /db_xref="PID:g2828024" ** /note="tyrosine kinase substrate" ** /gene="LAT" ** /product="LAT" ** CDS_IN_EMBL_ENTRY 1 ** 03-FEB-1998 (Rel. 54, Last updated, Version 1) ** source 1..1616 ** /organism="Homo sapiens" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="thymus" ** CDS 323..1024 ** /codon_start=1 ** /db_xref="PID:e1234817" ** /gene="pp36" ** /product="36 kDa phosphothyrosine protein" ** CDS_IN_EMBL_ENTRY 1 ** 13-JAN-1998 (Rel. 54, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS00190; CYTOCHROME_C; 26; 31; ?; 19-JUN-2000; SQ SEQUENCE 233 AA; 24985 MW; 0832E2D2B4220BC6 CRC64; MEEAILVPCV LGLLLLPILA MLMALCVHCH RLPGSYDSTS SDSLYPRGIQ FKRPHTVAPW PPAYPPVTSY PPLSQPDLLP IPRSPQPLGG SHRTPSSRRD SDGANSVASY ENEEPACEDA DEDEDDYHNP GYLVVLPDST PATSTAAPSA PALSTPGIRD SAFSMESIDD YVNVPESGES AEASLDGSRE YVNVSQELHP GAAKTEPAAL SSQEAEEVEE EGAPDYENLQ ELN // ID O43923 PRELIMINARY; PRT; 183 AA. AC O43923; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE METALLOPROTEINASE. GN MMP20. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Bernot A., Heilig R., Clepet C., Smaoui N., Delpech M., da Silva C., RA Devaud C., Petit J.L., Chiannilkulchai N., Fizames C., Samson D., RA Cruaud C., Caloustian C., Gyapay G., Weissenbach J.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. DR EMBL; AJ003147; CAA05902.1; -. DR EMBL; AJ003144; CAA05900.1; -. DR HSSP; P09237; 1MMP. DR INTERPRO; IPR001818; -. DR PFAM; PF00413; Peptidase_M10; 1. ** ** ################# SOURCE SECTION ################## ** Homo sapiens complete genomic sequence between D16S3070 and ** D16S3275, containing Familial Mediterranean Fever gene disease ** [1] ** Bernot A., Heilig R., Clepet C., Smaoui N., Delpech M., da Silva C., ** Devaud C., Petit J.L., Chiannilkulchai N., Fizames C., Samson D., ** Cruaud C., Caloustian C., Gyapay G., Weissenbach J.; ** "A transcriptional map of the FMF region"; ** Unpublished. ** [2] ** 1-239566 ** Bernot A.; ** ; ** Submitted (07-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** GENOSCOPE - Centre National de Sequencage, 2 rue Gaston Cremieux, EVRY ** BP191, FRANCE. ** [2] ** 1-627 ** Bernot A.; ** ; ** Submitted (07-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** GENOSCOPE - Centre National de Sequencage, 2 rue Gaston Cremieux, EVRY ** BP191, FRANCE. ** [3] ** Bernot A., Heilig R., Clepet C., Smaoui N., Delpech M., da Silva C., ** Devaud C., Petit J.L., Chiannilkulchai N., Fizames C., Samson D., ** Cruaud C., Caloustian C., Gyapay G., Weissenbach J.; ** "A transcriptional map of the FMF region"; ** Unpublished. ** source 179596..222837 ** /organism="Homo sapiens" ** /chromosome="16" ** /map="p13.3" ** /clone="YAC 26fe7" ** /sub_clone="30e10" ** CDS join(6772..6775,9222..9357,9467..9758,15042..15161) ** /db_xref="PID:e1246030" ** /gene="mmp20" ** /product="metalloproteinase" ** CDS_IN_EMBL_ENTRY 5 ** 22-JAN-1998 (Rel. 54, Last updated, Version 1) ** source 1..627 ** /organism="Homo sapiens" ** /chromosome="16" ** /map="p13.3" ** CDS 14..565 ** /codon_start=1 ** /db_xref="PID:e1245446" ** /gene="MMP20" ** /product="metalloproteinase" ** CDS_IN_EMBL_ENTRY 1 ** 22-JAN-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00413; Peptidase_M10; 1; 140; T; 19-JUN-2000; SQ SEQUENCE 183 AA; 20354 MW; 2F844C2B8338787B CRC64; MDPGTVATMR KPRCSLPDVL GVAGLVRRRR RYALSGSVWK KRTLTWRVRS FPQSSQLSQE TVRVLMSYAL MAWGMESGLT FHEVDSPQGQ EPDILIDFAR AFHQDSYPFD GLGGTLAHAF FPGEHPISGD THFDDEETWT FGSKASQQLE QELAGGSPVD EELGFSRGWR VNPLGPGSPE RLS // ID C2F_HUMAN PRELIMINARY; PRT; 151 AA. AC Q92979; O00726; O00675; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-JUN-1998 (TrEMBLrel. 06, Last annotation update) DE C2F PROTEIN. GN C2F. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.; RL Genome Res. 7:268-280(1997). CC -!- SIMILARITY: TO YEAST L9470.5 AND SPAC18G6.07C. DR EMBL; U72514; AAC51641.1; ALT_INIT. DR EMBL; U47924; CAB35662.1; -. KW Hypothetical protein. ** ** ################# SOURCE SECTION ################## ** Human C2f mRNA, complete cds. ** [1] ** 1-886 ** Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.; ** "Large scale sequencing in human chromosome 12p13: experimental and ** computational gene structure determination"; ** Genome Res. 7:268-280(1997). ** [2] ** 1-886 ** Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.; ** ; ** Submitted (24-SEP-1996) to the EMBL/GenBank/DDBJ databases. ** Molecular and Human Genetics, Baylor College of Medicine, One Baylor ** Plaza, Houston, TX 77030, USA ** [3] ** 1-886 ** Ansari-Lari M.A. PhD, Shen Y., Muzzny D.M., Lee W., Gibbs R.A. PhD.; ** ; ** Submitted (24-JUL-1997) to the EMBL/GenBank/DDBJ databases. ** Department of Moelcular and Human Genetics, Baylor College of ** Medicine, ** One Baylor Plaza, Houston, TX 77030, USA ** source 1..886 ** /organism="Homo sapiens" ** /chromosome="12" ** /map="12p13" ** CDS <1..721 ** /codon_start=2 ** /db_xref="PID:g2276396" ** /evidence=EXPERIMENTAL ** /note="similar to EST with GenBank Accession Number ** R64505; ** similar to S. cerevisiae hypothetical protein L9470.5 ** encoded by GenBank Accession Number S51431, and to S. ** pombe ** hypothetical 34.9 KD protein encoded by GenBank ** Accession ** Number Z68198; see corresponding genomic sequence in ** GenBank Accession Number U72506" ** /gene="C2f" ** /product="C2f" ** CDS_IN_EMBL_ENTRY 1 ** 26-JUL-1997 (Rel. 52, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **ZZ CREATED AND FINISHED BY FIONA. **ZZ UPDATED BY FIONA. **ZZ CURATED. SQ SEQUENCE 151 AA; 16611 MW; 2D0090A2429296DB CRC64; MLMDSPLNRA GLLQVYIHTQ KNVLIEVNPQ TRIPRTFDRF CGLMVQLLHK LSVRAADGPQ KLLKVIKNPV SDHFPVGCMK VGTSFSIPVV SDVRELVPSS DPIVFVVGAF AHGKVSVEYT EKMVSISNYP LSAALTCAKL TTAFEEVWGV I // ID Q12757 PRELIMINARY; PRT; 171 AA. AC Q12757; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE MUCIN (FRAGMENT). GN B1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=COLON; RA Walter A.O., Schwoeble W., Dippold W.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; X83412; CAA58319.1; -. FT VAR_SEQ 358 383 ETNWPRELKDGNGQESLSMSSSSSPA -> DPGSPKKCRAR FT FGLNQQTDWCGPCRRKKKCIRYLPGEGRCPSPVPSDDSALG FT CPGSPAPQDSPSYHLLPRFPTELLTSPAERHLHPQVSPLLS FT ASQPQGPHRPPAAPCRAHRYSNRNLRDRWPSRHRTPGRLQE FT PTP (in isoform 1L and isoform 1S). FT /FTId=VSP_006960. FT VAR_SEQ 358 383 ETNWPRELKDGNGQESLSMSSSSSPA -> GGKRNAFGTYP FT EKAAAPAPFLPMTVL (in isoform 2L and FT isoform 2S). FT /FTId=VSP_002191. FT VAR_SEQ 358 383 ETNWPRELKDGNGQESLSMSSSSSPA -> DPGSPKKCRAR FT FGLNQQTDWCGPCR (in isoform 3L and isoform FT 3S). FT /FTId=VSP_002192. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens B1 mRNA for mucin ** [1] ** Walter A.O., Schwoeble W., Dippold W.; ** "Cloning and expression of the carboxy terminus of a novel mucin"; ** Unpublished. ** [2] ** 1-798 ** Walter A.O.; ** ; ** Submitted (13-DEC-1994) to the EMBL/GenBank/DDBJ databases. ** A.O. Walter, I. Medical Clinic & Univ. of Mainz, ** Verfuegungsgebaeude, Obere Zahlbacherstr. 63, 55101 Mainz, FRG ** source 1..798 ** /organism="Homo sapiens" ** /tissue_type="colon" ** /cell_line="T84" ** /clone_lib="lambda ZapXR" ** /chromosome="7" ** CDS <1..516 ** /partial ** /codon_start=1 ** /gene="B1" ** /product="mucin" ** /db_xref="PID:g853956" ** CDS_1_OUT_OF_1 ** 01-JUN-1995 (Rel. 44, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 171 AA; 17863 MW; 3F249989A6FA501D CRC64; AREKRKPQQP QRRPAGGTGQ RRGSGYSPSA DQQGAQDREE EAAAAPAPTS SGHRTEKRKR LQLQCQPAGG TGQRRGSGQG PSARPAAFTG QRRGSRSSPS ADQQRAQDRE EEAARPQRRP AAGTGQRRGS AAAPVPTSSG TGQRRGSAAA PAPTSSGTGQ RRGSEEMEEE G // ID Q12814 PRELIMINARY; PRT; 47 AA. AC Q12814; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE CEA FAMILY MEMBER (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Mclenachan P.A., Rutherfurd K.J., Beggs K.T., Sims S., Mansfield B.C.; RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; U04433; AAA18341.1; -. FT NON_TER 1 1 FT NON_TER 47 47 ** ** ################# SOURCE SECTION ################## ** Human CEA family member gene, BI-like domain, partial cds. ** [1] ** 1-384 ** McLenachan P.A., Rutherfurd K.J., Beggs K.T., Sims S., ** Mansfield B.C.; ** "Characterization of the PSG11 Gene"; ** Unpublished. ** [2] ** 1-384 ** Mansfield B.C.; ** ; ** Submitted (15-DEC-1993) to the EMBL/GenBank/DDBJ databases. ** Brian C. Mansfield, Massey University, Microbiology and Genetics, ** Palmerston North, New Zealand ** NCBI gi: 436166 ** source 1..384 ** /clone="C20.5" ** /clone_lib="CVOO1K" ** /organism="Homo sapiens" ** /cell_type="leukocyte" ** CDS <244..>384 ** /standard_name="CEA family member gene, BI-like ** domain" ** /note="NCBI gi: 436167" ** /codon_start=2 ** /db_xref="PID:g436167" ** CDS_1_OUT_OF_1 ** 26-MAY-1994 (Rel. 39, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 47 AA; 5415 MW; 832E3F1A03BC0913 CRC64; WLGHPFTPVI SYELGANLRL FIHVASNPPS PYFWRVMETF CNTCKSS // ID Q12833 PRELIMINARY; PRT; 58 AA. AC Q12833; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE FIBROMODULIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=CARTILAGE; RA Sztrolovics R., Chen X.N., Grover J., Roughley P.J., Korenberg J.R.; RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U05291; AAA16153.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human fibromodulin mRNA, partial cds. ** [1] ** 1-1892 ** Sztrolovics R., Chen X.N., Grover J., Roughley P.J., ** Korenberg J.R.; ** "Localization of the human fibromodulin gene to chromosome 1q32 ** and completion of the cDNA sequence"; ** Unpublished. ** [2] ** 1-1892 ** Sztrolovics R.; ** ; ** Submitted (12-JAN-1994) to the EMBL/GenBank/DDBJ databases. ** Robert Sztrolovics, Department of Surgery, McGill University, ** Genetics Unit, Shriners Hospital for Crippled Children, 1529 Cedar ** Avenue, Montreal, Quebec, H3G 1A6, Canada ** source 1..1892 ** /isolate="patient A10/03/93" ** /clone="pHFM-3'UT" ** /clone_lib="PCR product" ** /organism="Homo sapiens" ** /sex="female" ** /cell_type="chondrocyte" ** /tissue_type="cartilage" ** /dev_stage="neonate" ** /map="1q32" ** /chromosome="1" ** CDS <1..178 ** /note="Encodes only the most carboxy terminal 58 amino ** acids of fibromodulin" ** /product="fibromodulin" ** /codon_start=2 ** /db_xref="PID:g450855" ** CDS_1_OUT_OF_1 ** 29-JAN-1994 (Rel. 38, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 58 AA; 6470 MW; 822B24A3ACDD4D80 CRC64; YLQGNRINEF SISSFCTVVD VVNFSKLQVL RLDGNEIKRS AMPADAPLCL RLASLIEI // ID Q12914 PRELIMINARY; PRT; 1692 AA. AC Q12914; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE G2 PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE OF 1-564 FROM N.A. RC TISSUE=KIDNEY; RA Foord O., Rose E.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U10991; AAA21253.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human G2 protein mRNA, partial cds. ** [1] ** 1-1694 ** Foord O., Rose E.; ** "Transposon-based mapping and sequencing of a novel transcript ** within the WAGR region of human chromosome 11p13"; ** Unpublished. ** [2] ** 1-6868 ** Foord O.; ** ; ** Submitted (17-JUN-1994) to the EMBL/GenBank/DDBJ databases. ** Orit Foord, Advanced Center for Genetic Technology, Applied ** Biosystems Division, Perkin-Elmer Corporation, 850 Lincoln Centre ** Drive, Foster City, CA 94404, USA ** NCBI gi: 533094 ** source 1..6868 ** /clone="pG2-6.9" ** /clone_lib="lambda gt11 cDNA library from embroyonic ** kidney" ** /chromosome="11" ** /organism="Homo sapiens" ** /map="11p13" ** /tissue_type="kidney" ** /dev_stage="embryo" ** CDS <3..5081 ** /note="NCBI gi: 533095" ** /codon_start=1 ** /product="G2" ** /db_xref="PID:g533095" ** CDS_1_OUT_OF_1 ** 08-SEP-1994 (Rel. 40, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 1692 AA; 183170 MW; C5A975AF1485B51A CRC64; IPEGRLSAEH TSSLVPSLHI TTLGQEQAIL SGAVPASPST GTADFPSILT FLQPTENHAS PSPVPEMPTL PAEGSDGSPP ATRDLLLSSK VPNLLSTSWT FPRWKKDSVT AILGKNEEAN VTIPLQGFPR KEVLSLHTVN GFVSDFSTGS VSSPIITAPR TNPLSSGPPL PSILSIQATQ TVFPSLLAFS STKPEVYAAA VDHSGLPASA PKQVRASPSS MDVYDSLTIG DMKKPATTDV FWSSLSAETG SLSTESIISG LQQQTNYDLN GHTISTTSWE THLAPTAPPN GLTSAADAIK SQDFKDTAGH SVTAEGFSIQ DLVLGTSIEQ PVQQSDMTMV GSHIDLWPTS NNNHSRDFQT AEVAYYSPTT RHSVSHPQLQ LPNQPAHPLL LTSPGPTSTG SLQEMLSDGT DTGSEISSDI NSSPERNAST PFQNILGYHS AAESSISTSV FPRTSSRVLR ASQHPKKWTA DTVSSKVQPT AAAAVTLFLR KSSPPALSAA LVAKGTSSSP LAVASGPAKS SSMTTLAKNV TNKAASGPKR TPGAVHTAFP FTPTYMYART GHTTSTHTAI ARKHGHCLWP VVYNLPPPGK PQAMHTGLPN PTNLEMPRAS TPRPLTVTAA LTSITASVKA TRLPPLRAEN TDAVLPAASA AVVTTGKMAS NLECQMSSKL LVKTVLFLTQ RRVQISESLK FSIAKGLTQA LRKAFHQNDV SAHVDILEYS HNVTVGYYAT KGKLVYLPAV VIEMLGVYGV SNVTADLKQH TPHLQSVAVL ASPWNPQPAG YFQLKTVLQF VSQADNIQSC KFAQTMEQRL QKAFQDAERK VLNTKSNLTI QIVSTSNASQ AVTLVYVVGN QSTFLNGTVA SSLLSQLSAE LVGFYLTYPP LTIAEPLEYP NLDISETTRD YWVITVLQGV DNSLVGLHNQ SFARVMEQRL AQLFMMSQQQ GRRFKRATTL GSYTVQMVKM QRVPGPKDPA ELTYYTLYNG KPLLGTVAAK ILSTIDSQRM ALTLHHVVLL QADPVVKNPP NNLWIIAAVL APIAVVTVII IIITAVLCRK NKNDFKPDTM INLPQRAKPV QGFDYAKQHL GQQGADEEVI PVTQETVVLP LPIRDAPQER DVAQDGSTIK TAKSTETRKS RSPSENGSVI SNESGKPSSG RRSPQNVMAQ QKVTKEEARK RNVPASDEEE GAVLFDNSSK VAAEPFDTSS GSVQLIAIKP TALPMVPPTS DRSQESSAVL NGEVNKALKQ KSDIEHYRNK LRLKAKRKGY YDFPAVETSK GLTERKKMYE KAPKEMEHVL DPDSELCAPF TESKNRQQMK NSVYRSRQSL NSPSPGETEM DLLVTRERPR RGIRNSGYDT EPEIIEETNI DRVPEPRGYS RSRQVKGHSE TSTLSSQPSI DEVRQQMHML LEEAFSLASA GHAGQSRHQE AYGSAQHLPY SEVVTSAPGT MTRPRAGVQW VPTYRPEMYQ YSLPRPAYRF SQLPEMVMGS PPPPVPPRTG PVAVASLRRS TSDIGSKTRM AESTGPEPAQ LHDSASFTQM SRGPVSVTQL DQSALNYSGN TVPAVFAIPA ANRPGFTGYF IPTPPSSYRN QAWMSYAGEN ELPSQWADSV PLPGYIEAYP RSRYPQSSPS RLPRQYSQPA NLHPSLEQAP APSTAASQQS LAENDPSDAP LTNISTAALV KAIREEVAKL AKKQTDMFEF QV // ID Q12915 PRELIMINARY; PRT; 204 AA. AC Q12915; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE IBD1 (FRAGMENT). GN IBD1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=HEMATOPOIETIC; RA Appierto V., Pergolizzi R., Spurr N., Biunno I.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U11036; AAA67652.1; -. FT NON_TER 1 1 FT NON_TER 204 204 ** ** ################# SOURCE SECTION ################## ** Human Ibd1 mRNA, partial cds. ** [1] ** 1-613 ** Appierto V., Pergolizzi R., Spurr N., Biunno I.; ** "Identification and chromosomal localization of two new genes"; ** Unpublished. ** [2] ** 1-613 ** Biunno I.; ** ; ** Submitted (20-JUN-1994) to the EMBL/GenBank/DDBJ databases. ** Ida Biunno, CNR, ITBA, Via Ampere 56, Milano, 20131, Italy ** NCBI gi: 836882 ** source 1..613 ** /clone_lib="Clontech T lymphocytes cDNA library" ** /organism="Homo sapiens" ** /cell_type="T-lymophocyte" ** /tissue_type="hematopoietic" ** /chromosome="18" ** CDS <1..>612 ** /gene="Ibd1" ** /note="NCBI gi: 836883" ** /codon_start=1 ** /function="unknown" ** /db_xref="PID:g836883" ** CDS_1_OUT_OF_1 ** 04-JUN-1995 (Rel. 44, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 204 AA; 22095 MW; 5ADAE93D3744E581 CRC64; VSGIRGAGSG CTRQTFPMAS VTRAVFGELP SGGGTVEKFQ LQSDLLRVDI ISWGCTITAL EVKDRQGRAS DVVLGFAELE GYLQKQPYFG AVIGRVANRI AKGTFKVDGK EYHLAITRNP TVCTGRSQQG FDKVLWTLGA VKCVQFSRIS PDGEEGYPGE LKVWVTYTLD GGELHSATTE HKPVQATPVN LTTILTSTWQ ATRI // ID Q12925 PRELIMINARY; PRT; 113 AA. AC Q12925; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HYPOTHETICAL PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Lamartine J., Wang Q., Kaneko K., Tsuji S., Mattei M., Lenoir G., RA Sylla B.S.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U12206; AAA62165.1; -. KW Hypothetical protein. FT NON_TER 113 113 ** ** ################# SOURCE SECTION ################## ** Human clone pL713 hypothetical protein mRNA, partial cds. ** [1] ** 1-766 ** Lamartine J., Wang Q., Kaneko K., Tsuji S., Mattei M., Lenoir G., ** Sylla B.S.; ** "Cloning, sequencing, and chromosomal assignment of a new cDNA ** clone to Xq12-q13 and 14q11"; ** Unpublished. ** [2] ** 1-766 ** Sylla B.S.; ** ; ** Submitted (12-JUL-1994) to the EMBL/GenBank/DDBJ databases. ** Bakary S. Sylla, International Agency for Research on Cancer, ** MCA/VHC, 150 Cours Albert Thomas, Lyon, 69372 Cedex O8, France ** NCBI gi: 662789 ** source 1..766 ** /clone="pL713" ** /clone_lib="human placental cDNA library" ** /organism="Homo sapiens" ** /chromosome="Xq12-q13 and 14q11" ** CDS 428..>766 ** /note="ORF1; NCBI gi: 662790" ** /codon_start=1 ** /product="unknown" ** /db_xref="PID:g662790" ** CDS_1_OUT_OF_1 ** 04-MAR-1995 (Rel. 42, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 113 AA; 11385 MW; F93B6A01C558A7B2 CRC64; MEPASAHLLL NDMIAGQHCL EVTIFICFST SFCSSFSFSA SSSISLTLDS SASGPQWRVP VTSTSPAPPP PLGCRGSRTS PGPGAPGGRG AGAAPLRARA PARAPAARPQ APP // ID Q12928 PRELIMINARY; PRT; 48 AA. AC Q12928; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE THROMBOSPONDIN-P50 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Dimitry J.M., Sheibani N., Finn M., Boak B.M., Paul L.L., RA Frazier W.A.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U12471; AAA21126.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human thrombospondin-1 gene, partial cds. ** [1] ** 1-1966 ** Dimitry J.M., Sheibani N., Finn M., Boak B.M., Paul L.L., ** Frazier W.A.; ** "Identification of a human thrombospondin-1 isoform generated by ** alternative splicing"; ** Unpublished. ** [2] ** 1-1966 ** Frazier W.A.; ** ; ** Submitted (20-JUL-1994) to the EMBL/GenBank/DDBJ databases. ** William A. Frazier, Biochemistry and Molecular Biophysics, ** Washington University Medical School, 660 South Euclid Avenue, St. ** Louis, MO 63110, USA ** NCBI gi: 532687 ** source 1..1966 ** /chromosome="15" ** /map="15q21" ** /organism="Homo sapiens" ** /cell_type="leukocyte" ** CDS join(<1..31,961..1076) ** /note="NCBI gi: 532688" ** /codon_start=1 ** /product="thrombospondin-p50" ** /db_xref="PID:g532688" ** CDS_1_OUT_OF_2 ** 08-SEP-1994 (Rel. 40, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 48 AA; 5132 MW; 728FC778BD079EDF CRC64; PDGECCPRCW PRCDCSRGAW ADGKETCCPL MTICAEKAPN AGVRGTTN // ID Q13058 PRELIMINARY; PRT; 109 AA. AC Q13058; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HYPOTHETICAL PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=OVARY; RA Montagna M., Serova O., Sylla B.S., Feunten J., Lenoir G.M.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U18920; AAA69700.1; -. KW Hypothetical protein. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human chromosome 17q12-21 mRNA, clone pOV-3, partial cds. ** [1] ** Montagna M., Serova O., Sylla B.S., Feunten J., Lenoir G.M.; ** "100 kb physical map around the EDH17B2 gene: identification of ** three new genes and a pseudogene of a human homologue of the rat ** PRL-1 tyrosine phosphatase"; ** Unpublished. ** [2] ** 1-861 ** Lenoir G.M.; ** ; ** Submitted (20-DEC-1994) to the EMBL/GenBank/DDBJ databases. ** Gilbert M. Lenoir, International Agency for Research on Cancer, ** VHC/MCA, 150 Cours Albert Thomas, 69372 Lyon CEDEX 08, France ** NCBI gi: 894179 ** source 1..861 ** /clone="pOV-3" ** /clone_lib="Human ovarian cDNA library (Stratagene)" ** /organism="Homo sapiens" ** /sex="female" ** /tissue_type="ovary" ** /dev_stage="adult" ** /map="17q12-21" ** /chromosome="17" ** /note="similar to ESTs, GenBank Accession Numbers ** Z38537 ** and M62002" ** CDS <1..331 ** /note="NCBI gi: 894180" ** /codon_start=2 ** /product="unknown" ** /db_xref="PID:g894180" ** CDS_1_OUT_OF_1 ** 13-JUL-1995 (Rel. 44, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 109 AA; 11583 MW; 6440B7B6E992044F CRC64; GYLHRLSDPT LHSHPFLSPR SCPALHSTAG MLGTEALAAP QCTGLPSLGV GFFPGLAWAL PTSTPSGRGC RLMLFPDETL RSSPPPIMMS SVWDWGPLGS ACMPAWLRP // ID Q13079 PRELIMINARY; PRT; 344 AA. AC Q13079; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE VT4 PROTEIN (VT) (FRAGMENT). GN VT. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Tesmer V., Babin J., Rajadhyaksha A., Bina M.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; U19346; AAA64188.1; -. FT NON_TER 1 1 FT NON_TER 344 344 ** ** ################# SOURCE SECTION ################## ** Human VT4 protein (VT) mRNA, partial cds. ** [1] ** 1-1032 ** Tesmer V., Babin J., Rajadhyaksha A., Bina M.; ** ; ** Unpublished. ** [2] ** 1-1032 ** Bina M.; ** ; ** Submitted (30-DEC-1994) to the EMBL/GenBank/DDBJ databases. ** Minou Bina, Department of Chemistry, Purdue University, 1393 Brown ** Blg., W. Lafayette, IN 47907, USA ** NCBI gi: 726043 ** source 1..1032 ** /organism="Homo sapiens" ** /cell_line="Hela" ** CDS <1..>1032 ** /gene="VT" ** /note="NCBI gi: 726044" ** /codon_start=1 ** /product="VT4" ** /db_xref="PID:g726044" ** CDS_1_OUT_OF_1 ** 13-APR-1995 (Rel. 43, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 344 AA; 38166 MW; D9BCC309953FB987 CRC64; RQPSSLPEGL PAPLEKRVKE LAQAARAAEG ESRQKFFTQD INGILLDIEA QTRELSSQVR SGVYAYLASF LPCSKDALLK RARKLHLYEQ GGRLKEPLQK LKEAIGRAMP EQMAKYQDEC QAHTQAKVAK MLEEEKDKEQ RDRICSDEEE DEEKGGRRIM GPRKKFQWND EIRELLCQVV KIKLESQDLE RNNKAQAWED CVKGFLDAEV KPLWPKGWMQ ARTLFKESRR GHGHLTSILA KKKVMAPSKI KVKESSTKPD KKVSVPSGQI GGPIALPSDH QTGGLSIGAS SRELPSQASG GLANPPPVNL EDSLDEDLIR NPASSVEAVS KELAALNSRA AGNS // ID Q13116 PRELIMINARY; PRT; 353 AA. AC Q13116; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE MEMBRANE PROTEIN-LIKE PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., RA Anzevino R., Velona I., Brahe C., Scheffer H., Van Ommen G.J.B., RA Buys C.H.C.M.; RL Eur. J. Hum. Genet. 0:0-0(0). DR EMBL; U21556; AAA69956.1; -. FT NON_TER 1 1 FT NON_TER 353 353 ** ** ################# SOURCE SECTION ################## ** Human membrane protein-like protein mRNA, partial cds. ** [1] ** der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., ** Anzevino R., VELONA I., Brahe C., Scheffer H., van Ommen G.J.B., ** Buys C.H.C.M.; ** "A provisional transcript map of the spinal muscular atrophy (SMA) ** critical region"; ** Unpublished. ** [2] ** 1-1263 ** der Steege G.; ** ; ** Submitted (23-FEB-1995) to the EMBL/GenBank/DDBJ databases. ** Gerrit Van der Steege, University of Groningen, Department of ** Medical Genetics, Antonius Deusinglaan 4, Groningen, 9713 AW, The ** Netherlands ** NCBI gi: 899492 ** source 1..1263 ** /clone="5G5" ** /clone_lib="library of A. Bernards" ** /organism="Homo sapiens" ** /map="5q13.1 and 5p" ** /chromosome="5" ** /cell_type="pre-B-cells" ** CDS <204..>1263 ** /note="similar to rat integral membrane glycoprotein, ** PIR ** Accession Number A40670; NCBI gi: 899493" ** /codon_start=1 ** /db_xref="PID:g899493" ** CDS_1_OUT_OF_1 ** 19-JUL-1995 (Rel. 44, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 353 AA; 36947 MW; 431ADAB38FD2CA6E CRC64; SQNGPRGHRG CTVCILALRX NGGLSPFVPR PGPLQTDLHA QSSEIRYNQT SQTSWTSSST KRNAISSSYS STGGLPGLKQ RRGPASSRCQ LTLSYSKTVS EDGPQAVSSR HTRCEKADTA PGQTLAPRGG SPRSQASRPR RRKIPLLPRR RGEPLMLPPP LELGYRVTAE DLHLEKETAL QRINSALHVE DKATSDCRPS RPSHTLSSLA TGASGGPPVS KAPTMDAQPD KLKSQDCLGL VAALASATEV SSTAPMSGKK HRPPGPLFSS SDPLPATSSH SQDSAQVTSM IPAPFTAASR DASMRRTRPG TSAPAXAAAA PPPSTLNPTS GSLLNAVDEG PSHFLASATA AAR // ID Q13119 PRELIMINARY; PRT; 293 AA. AC Q13119; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE DUPLICATE SPINAL MUSCULAR ATROPHY (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., RA Anzevino R., Velona I., Brahe C., Scheffer H., Van Ommen G.J.B., RA Buys C.H.C.M.; RL Eur. J. Hum. Genet. 0:0-0(0). DR EMBL; U21914; AAA64505.1; -. DR INTERPRO; IPR002999; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human duplicate spinal muscular atrophy mRNA, clone 5G7, partial ** cds. ** [1] ** der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., ** Anzevino R., VELONA I., Brahe C., Scheffer H., van Ommen G.J.B., ** Buys C.H.C.M.; ** "A provisional transcript map of the spinal muscular atrophy (SMA) ** critical region"; ** Unpublished. ** [2] ** 1-1466 ** der Steege G.; ** ; ** Submitted (28-FEB-1995) to the EMBL/GenBank/DDBJ databases. ** Gerrit Van der Steege, University of Groningen, Department of ** Medical Genetics, Antonius Deusinglaan 4, Groningen, 9713 AW, The ** Netherlands ** NCBI gi: 736410 ** source 1..1466 ** /clone="5G7" ** /clone_lib="library of A. Bernards" ** /organism="Homo sapiens" ** /map="5q13.1" ** /chromosome="5" ** /cell_type="pre-B-cells" ** CDS <1..882 ** /note="putative open reading frame; duplicate of the ** functional spinal muscular atrophy gene, cDNA clone ** BCD514, ** GenBank Accession Number U18423; it is not known if ** this ** copy of the gene is actually translated; NCBI gi: ** 736411" ** /codon_start=1 ** /db_xref="PID:g736411" ** CDS_1_OUT_OF_1 ** 23-MAY-1995 (Rel. 43, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS50304; TUDOR; 90; 150; T; 19-JUN-2000; SQ SEQUENCE 293 AA; 31718 MW; FEF4B81E12040F24 CRC64; AMSSGGSGGG VPEQEDSVLF RRGTGQSDDS DIWDDTALIK AYDKAVASFK HALKNGDICE TSGKPKTTPK RKPAKKNKSQ KKNTAASLQQ WKVGDKCSAI WSEDGCIYPA TIASIDFKRE TCVVVYTGYG NREEQNLSDL LSPICEVANN IEQNAQENEN ESQVSTDESE NSRSPGNKSD NIKPKSAPWN SFLPPPPPMP GPRLGPGKPG LKFNGPPPPP PPPPPHLLSC WLPPFPSGPP IIPPPPPICP DSLDDADALG SMLISWYMSG YHTGYYMGFR QNQKEGRCSH SLN // ID Q13222 PRELIMINARY; PRT; 203 AA. AC Q13222; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1999 (TrEMBLrel. 12, Last annotation update) DE GATA-4 (FRAGMENT). GN GATA-4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Wood S., Yaremko M.L., Schertzer M.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U28835; AAA70335.1; -. DR HSSP; P04002; 1WFA. FT NON_TER 203 203 ** ** ################# SOURCE SECTION ################## ** Human GATA-4 gene, partial cds. ** [1] ** 1-855 ** Wood S., Yaremko M.L., Schertzer M.; ** "Localization of human GATA4 to 8p23 maps chromosomal breakpoints ** disrupting synteny between human 8p and mouse 14 to the Clu-Gata4 ** interval"; ** Unpublished. ** [2] ** 1-855 ** Wood S.; ** ; ** Submitted (09-JUN-1995) to the EMBL/GenBank/DDBJ databases. ** Stephen Wood, Medical Genetics, University of British Columbia, ** 6174 University Blvd., Vancouver, B.C. V6T 1Z3, Canada ** NCBI gi: 903937 ** source 1..855 ** /organism="Homo sapiens" ** /clone_lib="LA08NC01, Wood et al. Cytogenet. Cell ** Genet. ** 59:243-247, 1992" ** /clone="161F5" ** /chromosome="8" ** /map="8p" ** CDS 61..>669 ** /gene="GATA-4" ** /note="similar to human GATA-4 cDNA sequence, GenBank ** Accession Number L34357; NCBI gi: 903938" ** /codon_start=1 ** /db_xref="PID:g903938" ** CDS_1_OUT_OF_1 ** 26-JUL-1995 (Rel. 44, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 203 AA; 20157 MW; 7C238D931655F208 CRC64; MYQSLPWPPT TGRPPVPTRR AAPAPSCXXX APRPRQSTCP PAGALLRAGP VLPPGRRRGL CVRRRLGRSS GGAASGAGPG TQQGSPGWSQ AGADGAAYTP PPVSPRFSFP GPTGSLAAAA AAAAAREAAA YSSGGGAAGA GLAGREQYGR AXFAGSYSSX YPAYMADVGA SWAAAAAASA GPFDSPVLHS LPGRANPXXH PNL // ID Q13306 PRELIMINARY; PRT; 71 AA. AC Q13306; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE THYROID TRANSCRIPTION FACTOR-1 (FRAGMENT). GN TTF-1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Hamdan H., Liu H., Jones C., Delemos R., Minoo P.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U33627; AAA83233.1; -. FT NON_TER 71 71 ** ** ################# SOURCE SECTION ################## ** Human thyroid transcription factor-1 (TTF-1) gene, partial cds. ** [1] ** 1-1062 ** Hamdan H., Liu H., Jones C., deLemos R., Minoo P.; ** "Characterization of TTF-1 transcripts in human lung identifies an ** additional exon"; ** Unpublished. ** [2] ** 1-1062 ** Hamdan H.; ** ; ** Submitted (10-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** Hasnah Hamdan, University of Southern California, Pediatrics, ** Division of Basic Research, 1801 E. Marengo, Rm 1G-1, Los Angeles, ** CA 90033, USA ** NCBI gi: 1113816 ** source 1..1062 ** /clone="pHGX4" ** /clone_lib="Lambda EMBLT3 SP6/T7 library of Clontech, ** Palo ** Alto, CA." ** /organism="Homo sapiens" ** /cell_type="leukocyte" ** CDS join(164..240,927..>1062) ** /gene="TTF-1" ** /codon_start=1 ** /product="thyroid transcription factor-1" ** /db_xref="PID:g1113817" ** CDS_1_OUT_OF_1 ** 13-DEC-1995 (Rel. 46, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 71 AA; 7425 MW; 7ABFD04CD963A711 CRC64; MWSGGSGKAR GWEAAAGGRS SPGRLSRRRI MSMSPKHTTP FSVSDILSPL EESYKKVGME GGGLGAPLAA Y // ID Q13548 PRELIMINARY; PRT; 36 AA. AC Q13548; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE P38-2G4 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Greco N.J., Rao P., Modeli R., Jamieson G.A.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U50137; AAA91484.1; -. FT NON_TER 36 36 ** ** ################# SOURCE SECTION ################## ** Human p38-2G4 mRNA, partial cds. ** [1] ** 1-172 ** Greco N.J., Rao P., Modeli R., Jamieson G.A.; ** ; ** Submitted (27-FEB-1996) to the EMBL/GenBank/DDBJ databases. ** Nicholas J. Greco, Platelet Biology, American Red Cross, 15601 ** Crabbs Branch Way, Rockville, MD 20855, USA ** NCBI gi: 1216525 ** source 1..172 ** /organism="Homo sapiens" ** /cell_type="platelets and CMK 11-5 cells" ** CDS 65..>172 ** /note="similar to Mus musculus p38-2G4 encoded by ** GenBank ** Accession Number X84789; NCBI gi: 1216526" ** /codon_start=1 ** /product="p38-2G4" ** /db_xref="PID:g1216526" ** CDS_1_OUT_OF_1 ** 08-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 36 AA; 4117 MW; 7C2D4C3BCE49FC53 CRC64; MIMEETGKIF KKEKEMKKGI AFPTSISVNN CVCHFP // ID Q13552 PRELIMINARY; PRT; 31 AA. AC Q13552; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE SUPPRESSOR ELEMENT ISHMAEL UPPER CP1 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=MAMMARY; RA DeBlasio T.R., Moasser M.M., Mendelsohn J.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U50277; AAA92144.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human breast cancer suppressor element Ishmael Upper CP1 mRNA, ** partial cds. ** [1] ** 1-132 ** DeBlasio T.R., Moasser M.M., Mendelsohn J.; ** ; ** Submitted (29-FEB-1996) to the EMBL/GenBank/DDBJ databases. ** Tony R. DeBlasio, Medicine, Memorial Sloan-Kettering Cancer Center, ** 430 E. 67 St. RRL 727, New York City, N.Y. 10021, USA ** NCBI gi: 1224126 ** source 1..132 ** /organism="Homo sapiens" ** /clone="Ishmael" ** /cell_type="epithelial" ** /tissue_type="mammary" ** /cell_line="MCF-7" ** CDS <1..96 ** /codon_start=1 ** /product="suppressor element Ishmael Upper CP1" ** /db_xref="PID:g1224127" ** CDS_1_OUT_OF_1 ** 14-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 31 AA; 4015 MW; 45566C06AF4812E1 CRC64; YLKEGDKKYV WHRLGRKREL SDHFLKWKIQ R // ID Q13559 PRELIMINARY; PRT; 34 AA. AC Q13559; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE BREAST CANCER SUPPRESSOR ELEMENT ISHMAEL UPPER RP2 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=MAMMARY; RA DeBlasio T.R., Moasser M.M., Mendelsohn J.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U50403; AAA92145.1; -. FT NON_TER 1 1 FT NON_TER 34 34 ** ** ################# SOURCE SECTION ################## ** Human breast cancer suppressor element Ishmael Upper RP2 mRNA, ** partial cds. ** [1] ** 1-103 ** DeBlasio T.R., Moasser M.M., Mendelsohn J.; ** ; ** Submitted (01-MAR-1996) to the EMBL/GenBank/DDBJ databases. ** Tony R. DeBlasio, Medicine, Memorial Sloan-Kettering Cancer Center, ** 430 E. 67 St. RRL 727, New York City, N.Y. 10021, USA ** NCBI gi: 1224130 ** source 1..103 ** /organism="Homo sapiens" ** /cell_line="MCF-7 human mammary" ** /tissue_type="mammary" ** /cell_type="epithelial" ** /clone="Ishmael" ** CDS <1..>103 ** /codon_start=3 ** /product="breast cancer suppressor element Ishmael ** Upper ** RP2" ** /db_xref="PID:g1224131" ** CDS_1_OUT_OF_1 ** 14-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 34 AA; 3726 MW; EB286FD9128FBBA8 CRC64; LLWSTLVSWG CWLTPVIPTL WEAKAGGSPE PRSS // ID Q13581 PRELIMINARY; PRT; 84 AA. AC Q13581; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE KR-ZNF2 (FRAGMENT). GN KR-ZNF2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Sancho E., Gonzalez-Lamuno D., Thomson T.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U52097; AAA97913.1; -. FT NON_TER 1 1 FT NON_TER 84 84 ** ** ################# SOURCE SECTION ################## ** Human zinc finger protein (kr-znf2) mRNA, partial cds. ** [1] ** 1-253 ** Sancho E., Gonzalez-Lamuno D., Thomson T.; ** "Three novel Zn finger proteins"; ** Unpublished. ** [2] ** 1-253 ** Sancho E.; ** ; ** Submitted (22-MAR-1996) to the EMBL/GenBank/DDBJ databases. ** Elena Sancho, Biologia Celular y Molecular, Instituto Municipal de ** Investigacion Medica, c/ Dr Aiguader 80, Barcelona 08003, Spain ** NCBI gi: 1277184 ** source 1..253 ** /organism="Homo sapiens" ** /cell_type="HT-29 colon cancer cells" ** CDS <1..>253 ** /gene="kr-znf2" ** /note="zinc finger protein; NCBI gi: 1277185" ** /codon_start=1 ** /product="KR-ZNF2" ** /db_xref="PID:g1277185" ** CDS_1_OUT_OF_1 ** 26-APR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 84 AA; 9733 MW; FAD9F3A6EEE965F6 CRC64; PVLSTSPPNL FKKIIYTGEK FYKCEEYGKA FNQSSTLTRI KNSYCTETLT RVKNMAKPLT SPQFLTDITQ YTLERNTRQT TKDL // ID Q13599 PRELIMINARY; PRT; 58 AA. AC Q13599; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE TRANSCRIPTION ELONGATION INHIBITOR PVHL (FRAGMENT). GN VHL. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=CLEAR-CELL RENAL CELL CARCINOMA; RA Wenzel M.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U54612; AAA98614.1; -. DR INTERPRO; IPR002714; -. DR PFAM; PF01847; VHL; 1. FT NON_TER 1 1 FT NON_TER 58 58 ** ** ################# SOURCE SECTION ################## ** Human von Hippel-Lindau tumor suppressor (vhl) gene, exon 3, ** partial cds. ** [1] ** 1-176 ** Wenzel M.; ** ; ** Submitted (10-APR-1996) to the EMBL/GenBank/DDBJ databases. ** Michael Wenzel, KMS-registry, University of Duesseldorf, Moorenstr. ** 5, Duesseldorf 40225, FRG ** NCBI gi: 1293146 ** source 1..176 ** /organism="Homo sapiens" ** /tissue_type="clear-cell renal cell carcinoma" ** /chromosome="3" ** /map="3p25-26" ** CDS <1..>176 ** /gene="vhl" ** /note="Description: von Hippel-Lindau tumor ** suppressor; ** transcription elongation inhibitor; NCBI gi: 1293147" ** /codon_start=3 ** /product="pVHL" ** /db_xref="PID:g1293147" ** CDS_1_OUT_OF_1 ** 04-MAY-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01847; VHL; 1; 58; T; 19-JUN-2000; SQ SEQUENCE 58 AA; 7051 MW; 2AA043F064D06238 CRC64; YTLKERCPQV VRSLVKPENY RRLDIVRSLY EDLEDHPNVQ KDLERLTQER IAHQRMGD // ID Q13600 PRELIMINARY; PRT; 350 AA. AC Q13600; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE TOPOISOMERASE IIB (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Yuwen H.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U54831; AAB01982.1; -. KW Isomerase. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human topoisomerase IIb mRNA, partial cds. ** [1] ** 1-1388 ** Yuwen H.; ** "Binding of wild-type p53 by topoisomerase II and overexpression ** of topoisomerase II in human hepatocellular carcinoma"; ** Unpublished. ** [2] ** 1-1388 ** Yuwen H.; ** ; ** Submitted (12-APR-1996) to the EMBL/GenBank/DDBJ databases. ** H. Yuwen, CBER/DTTD/LH HFM-310, FDA, 1401 Rockville Pike, ** Rockville, MD 20852-1448, USA ** source 1..1388 ** /organism="Homo sapiens" ** CDS <1..1053 ** /note="p53 binding protein" ** /codon_start=1 ** /product="topoisomerase IIb" ** /db_xref="PID:g1354507" ** CDS_1_OUT_OF_1 ** 08-JUN-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 350 AA; 38567 MW; 55E6A5693B1C16CC CRC64; EFSGAPVEGA GEEALTPSVP INKGPKPKRE KKEPGTRVRK TPTSSGKPSA KKVKKRNPWS DDESKSESDL EETEPVVIPR DSLLRRAAAE RPKYTFDFSE EEDDDADDDD DDNNDLEELK VKASPITNDG EDEFVPSDGL DKDEYTFSPG KSKATPEKSL HDKKSQDFGN LFSFPSYSQK SEDDSAKFDS NEEDSASVFS PSFGLKQTDK VPSKTVAAKK GKPSSDTVPK PKRAPKQKKV VEAVNSDSDS EFGIPKKTTT PKGKGRGAKK RKASGSENEG DYNPGRKTSK TTSKKPKKTS FDQDSDVDIF PSDFPTEPPS LPRTGRARKE VKYFAESDEE EDDVDFAMFN // ID Q13681 PRELIMINARY; PRT; 146 AA. AC Q13681; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE ALPHA 3 TYPE IX COLLAGEN (FRAGMENT). GN HUMCOL9A3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=HYALINE CARTILAGE; RX MEDLINE=97293217; PubMed=9164858; RA Peraelae M., Savontaus M., Metsaeranta M., Vuorio E.; RT "Developmental regulation of mRNA species for types II, IX and XI RT collagens during mouse embryogenesis."; RL Biochem. J. 324:209-216(1997). DR EMBL; X91013; CAA62495.1; -. DR INTERPRO; IPR000087; -. DR PFAM; PF01391; Collagen; 2. KW Extracellular matrix. FT NON_TER 1 1 FT NON_TER 146 146 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for alpha 3 type IX collagen ** [1] ** Peraelae M.; ** ; ** Unpublished. ** [2] ** 1-438 ** Peraelae M.P.; ** ; ** Submitted (21-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** M.P. Peraelae, Dept. of Medical Biochemistry, Univ. of Turku, ** Kiinamyllynkatu 10, 20520 Turku, FINLAND ** source 1..438 ** /organism="Homo sapiens" ** /dev_stage="fetal" ** /tissue_type="hyaline cartilage" ** CDS <1..>438 ** /partial ** /codon_start=1 ** /gene="humcol9a3" ** /product="alpha 3 type IX collagen" ** /db_xref="PID:g975657" ** misc_feature 1..87 ** /note="NC2 domain" ** AA 1 -> 29 ** misc_feature 88..423 ** /note="COL1 domain" ** AA 30 -> 141 ** misc_feature 424..438 ** /note="NC1 domain" ** AA 142 -> 146 ** CDS_1_OUT_OF_1 ** 05-SEP-1995 (Rel. 45, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01391; Collagen; 28; 86; T; 19-JUN-2000; **PM PFAM; PF01391; Collagen; 87; 144; T; 19-JUN-2000; **PM PROSITE; PS50288; COLLAGEN_REP; 29; 87; T; 19-JUN-2000; **PM PROSITE; PS50288; COLLAGEN_REP; 112; 139; T; 19-JUN-2000; SQ SEQUENCE 146 AA; 13913 MW; 99F402AF2683D517 CRC64; EQHIRELCGG MISEQIAQLA AHLRKPLAPG SIGRPGPAGP PGPPGPPGSI GHPGTRGPPG YRGPTGELGD PGPRGNQGDR GDKGAAGAGL DGPEGDQGPQ GPQGVPGTSK DGQDGAPGEP GPPGDPGLPG AIGAQGTPGI CDTSAC // ID Q13727 PRELIMINARY; PRT; 534 AA. AC Q13727; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE AHNAK-RELATED PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=CERVIX; RA Kilwinski J.; RL Submitted (AUG-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; X74818; CAA52817.1; -. FT NON_TER 1 1 FT NON_TER 534 534 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA of AHNAK-related sequence ** [1] ** 1-1601 ** Kilwinski J.; ** ; ** Submitted (11-AUG-1993) to the EMBL/GenBank/DDBJ databases. ** J. Kilwinski, Univ. Konstanz, Fakultaet fuer Biologie, D-78434 ** Konstanz, FRG ** [2] ** Kilwinski J.; ** ; ** Unpublished. ** source 1..1601 ** /organism="Homo sapiens" ** /cell_line="HeLa S3" ** /clone_lib="lambda gt11" ** /clone="MB 41" ** /dev_stage="carcinoma" ** /haplotype="aneuploid" ** /tissue_type="cervix" ** /cell_type="epithelial" ** CDS <1..>1601 ** /codon_start=1 ** /product="AHNAK-related protein" ** /db_xref="PID:g535177" ** CDS_1_OUT_OF_1 ** 03-SEP-1994 (Rel. 40, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 534 AA; 57740 MW; D9E5251D1AF639D7 CRC64; KGPKFKMPDL HLKAPKISMP EVDLNLKGPK MKGDVDVSLP KVEGDLKGPE VDVKGPKVDI DVPDVDVQGP DWHLKMPKVK MPKFSMPGFK GEGPDVDVNL PKADLDVSGP KVDIDVPDVN IEGPDAKLKG PKFKMPEMNI KAPKISMPDF DLHLKGPKVK GDVDVSLPKV EGDLKGPEVD IKGPKVDIDA PDVDVHGPDW HLKMPKVKMP KFSMPGFKGE GPDVDVTLPK ADIEISGPKV DIDAPDVSIE GPDAKLKGPK FKMPEMNIKA PKISMPDIDF NLKGPKVKGD VDVSLPKVEG DLKGPEIDIK GPSLDIDTPD VNIEGPEGKL KGPKFKMPEM NIKAPKISMP DFDLHLKGPK VKGDVDVSLP KVESDLKGPE VDIEGPEGKL KGPKFKMPDV HFKSPQISMS DIDLNLKGPK IKGDMDISVP KLEGDLKGPK VDVKGPKVGI DTPDIDIHGP EGKLKGPKFK MPDLHLKAPK ISMPEVDLNL KGPKVKGDMD ISLPKVEGDL KGPEVDIRDP KVDIDVPDVD VQGP // ID Q13791 PRELIMINARY; PRT; 40 AA. AC Q13791; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1999 (TrEMBLrel. 12, Last annotation update) DE APOLIPOPROTEIN E3 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Bohnet K.; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; X92000; CAA63051.1; -. DR HSSP; P02649; 1LE2. KW Lipoprotein. FT VARIANT 20 20 C -> G. FT NON_TER 1 1 FT NON_TER 40 40 ** ** ################# SOURCE SECTION ################## ** H.sapiens apolipoprotein E3 gene ** [1] ** Bohnet K.; ** ; ** Unpublished. ** [2] ** 1-121 ** Bohnet K.; ** ; ** Submitted (05-OCT-1995) to the EMBL/GenBank/DDBJ databases. ** K. Bohnet, Centre de Medecine Preventive, 2 Ave. Doyen Jacques ** Parisot, F-54501, Vandoeuvre les Nancy, CEDEX, FRANCE ** Related sequences: M10065, ** SC.Rall Jr, J. Biol. Chem., 257, 4171-4178, 1982 ** P.de Knijff et al, Hum. Mutat.,4, 178-194, 1994 ** source 1..121 ** /organism="Homo sapiens" ** /cell_type="leucocytes" ** /chromosome="19" ** /map="q13.2" ** CDS <1..>121 ** /partial ** /codon_start=1 ** /product="apolipoprotein E3" ** /db_xref="PID:e205282" ** variation replace(58,"g") ** /note="point mutation" ** CDS_1_OUT_OF_1 ** 01-AUG-1996 (Rel. 48, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 40 AA; 4697 MW; B7F2E3E935CDA52C CRC64; QYRGEVQAML GQSTEELRVC LASHLRKLRK RLLRDADDLQ // ID Q13830 PRELIMINARY; PRT; 144 AA. AC Q13830; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE PREGNANCY-SPECIFIC BETA-1 GLYCOPROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Bocco J.; RL Submitted (NOV-1991) to the EMBL/GenBank/DDBJ databases. DR EMBL; X63203; CAA44885.1; -. KW Pregnancy. FT NON_TER 144 144 ** ** ################# SOURCE SECTION ################## ** H.sapiens gene for pregnancy specific beta-1 glycoprotein ** [1] ** 1-3036 ** Bocco J.; ** ; ** Submitted (05-NOV-1991) to the EMBL/GenBank/DDBJ databases. ** J. Bocco, LGME du CNRS - INSERM U184, 11 Rue Humann, Strasbourg, ** 67085 Cedex, FRANCE ** [2] ** 1-3036 ** Bocco J.; ** "Nucleotide sequence of a pregnancy-specific beta-1 glycopotein ** gene family member"; ** Unpublished. ** CPGISLE; HSB1GP; Release 3.0. ** source 1..3036 ** /organism="Homo sapiens" ** /dev_stage="embryo" ** /tissue_type="placenta" ** /cell_type="trophoblast" ** /sex="Female" ** CDS join(1191..1254,2492..>2858) ** /product="pregnancy-specific beta-1 glycoprotein" ** /partial ** /db_xref="PID:g29196" ** CDS_1_OUT_OF_1 ** 07-MAY-1992 (Rel. 31, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 144 AA; 16193 MW; 6871647785F0C63C CRC64; MGPLSAPPCT QHITWKGVLL TASLLNFWNL PITAQVTIEA LPPKVSEGKD VLLLVHNLPQ NLAGYIWYKG QLMDLYHYIT SYVVDGQINI YGPAYTGRET VYSNASLLIQ NVTREDAGSY TLHIIKRGDR TRGVTGYFTF NLYR // ID Q13831 PRELIMINARY; PRT; 93 AA. AC Q13831; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE B1 MUCIN-LIKE ANTIGEN (FRAGMENT). GN B1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=KIDNEY; RA Walter A.O., Dippold W.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; X84838; CAA59277.1; -. FT NON_TER 93 93 ** ** ################# SOURCE SECTION ################## ** H.sapiens B1 mRNA for mucin-like antigen ** [1] ** Walter A.O., Dippold W.; ** "Cloning and expression of a novel mucin-like antigen"; ** Unpublished. ** [2] ** 1-854 ** Walter A.O.; ** ; ** Submitted (15-FEB-1995) to the EMBL/GenBank/DDBJ databases. ** A.O. Walter, Medical Clinic, University of Mainz, Obere ** Zahlbacherstr. 63, 55101 Mainz, FRG ** Related sequence: X83412 (C-terminus) ** source 1..854 ** /organism="Homo sapiens" ** /tissue_type="kidney" ** /clone_lib="lambda MAX1" ** /chromosome="7" ** CDS 577..>854 ** /partial ** /gene="B1" ** /db_xref="PID:g974822" ** CDS_1_OUT_OF_1 ** 01-SEP-1995 (Rel. 45, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 93 AA; 10471 MW; 85A604F02DE1BBCE CRC64; MKPRQKEQDT RLRKLRESSE GDQWLENEKT KPLRPQQQPQ RRPAGGTGQR RGSGSSPSAD QQRAQDREEE AAAAPVPNQQ RAQDREEEAA AAP // ID Q13981 PRELIMINARY; PRT; 86 AA. AC Q13981; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE CARCINOEMBRYONIC ANTIGEN SUBDOMAIN B (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTAL; RA Oikawa S.; RL Submitted (SEP-1989) to the EMBL/GenBank/DDBJ databases. DR EMBL; X16454; CAA34473.1; -. KW Cell adhesion. FT NON_TER 86 86 ** ** ################# SOURCE SECTION ################## ** Human gene for carcinoembryonic antigen subdomains A and B. ** [1] ** 1-1092 ** Oikawa S.; ** ; ** Submitted (02-SEP-1989) to the EMBL/GenBank/DDBJ databases. ** Oikawa S., Suntory Institute for Biomedical Research, 1-1-1 ** Wakayamadai, Shimamoto-cho, Mishima-gun Osaka 618, Japan. ** source 1..1092 ** /organism="Homo sapiens" ** /clone="36" ** /tissue_type="placental" ** /clone_lib="genomic" ** CDS 715..973 ** /product="carcinoembryonic antigen subdomain B" ** /partial ** /db_xref="PID:g296641" ** CDS_1_OUT_OF_1 ** 24-APR-1993 (Rel. 35, Last updated, Version 5) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 86 AA; 9321 MW; 5C76C55FA3E00840 CRC64; MDRAFPPFPP QTPITIQGQI STSPATWPLT HLHSTPGLSV ECSSNTHKSS LSPTSQWIRV DPMLASPITQ PLASVQSQSR QSQSLL // ID Q14083 PRELIMINARY; PRT; 136 AA. AC Q14083; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE C219-REACTIVE PEPTIDE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LEUKEMIA CELL; RA Norris M.D., Gilbert J., Madafiglio J., Haber M.; RL Gene 0:0-0(0). DR EMBL; L34688; AAB00324.1; -. FT NON_TER 1 1 FT NON_TER 136 136 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone D320) C219-reactive peptide mRNA, partial cds. ** [1] ** 1-409 ** Norris M.D., Gilbert J., Madafiglio J., Haber M.; ** "Analysis of a novel cDNA encoding a C219-reactive peptide ** isolated from methotrexate-selected multidrug-resistant human ** leukemic cells"; ** Unpublished. ** source 1..409 ** /organism="Homo sapiens" ** /cell_line="CCRF-CEM" ** /cell_type="T-cell" ** /tissue_type="leukemia cell" ** /tissue_lib="lambda gt11" ** CDS <1..>409 ** /codon_start=3 ** /product="C219-reactive peptide" ** /db_xref="PID:g511639" ** CDS_1_OUT_OF_1 ** 21-MAY-1996 (Rel. 47, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 136 AA; 15343 MW; 98DAFBC8F58C28E1 CRC64; ENKKSIEKLK DVISMNASEF SEVQIALNEA KLSEEKVKSE CHRVQEENAR LKKKKEQLQQ EIEDWSKLHA ELSEQIKSFE KSQKDLEVAL THKDDNINAL TNCITQLNLL ECESESEGQN KGGNDSDELA NGEVGG // ID Q14402 PRELIMINARY; PRT; 25 AA. AC Q14402; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE GAMMA-G GLOBIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RA Vladimir V., Kavsan V.M.; RL Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RA Dmitrenko V.V., Kavsan V.M.; RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases. DR EMBL; X55657; CAA39190.1; -. DR INTERPRO; IPR000971; -. DR PFAM; PF00042; globin; 1. DR PROSITE; PS01033; GLOBIN; 1. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for gamma-G globin (clone pHG18) ** [1] ** 1-166 ** Vladimir V., Kavsan V.M.; ** ; ** Submitted (18-SEP-1990) to the EMBL/GenBank/DDBJ databases. ** Vladimir V., Kavsan V.M., Institute of Molecular Biology and ** Genetics Ukr.SSR Acad. of Sci., Zabolotnogo str. 150, Kiev 252627, ** USSR. ** [2] ** Dmitrenko V.V., Kavsan V.M.; ** "Nucleotide sequence of mitochondrial cytochrome C oxydase II from ** human fetal liver"; ** Unpublished. ** source 1..166 ** /organism="Homo sapiens" ** /dev_stage="embryonal" ** /tissue_type="liver" ** /cell_type="hepatocytes" ** CDS <1..80 ** /product="gamma-G globin" ** /codon_start=3 ** /db_xref="PID:g31723" ** CDS_1_OUT_OF_1 ** 11-MAY-1992 (Rel. 31, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00042; globin; 1; 25; T; 19-JUN-2000; **PM PROSITE; PS01033; GLOBIN; 1; 25; T; 19-JUN-2000; SQ SEQUENCE 25 AA; 2781 MW; C7BE9A334CD66D91 CRC64; FTPEVQASWQ KMVTGVASAL SSRYH // ID Q14441 PRELIMINARY; PRT; 52 AA. AC Q14441; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE GLYCOPROTEIN IB ALPHA (FRAGMENT). GN GPIB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Ishida F.; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; L39103; AAA69491.1; -. FT NON_TER 1 1 FT NON_TER 52 52 ** ** ################# SOURCE SECTION ################## ** Homo sapiens glycoprotein Ib alpha (GPIb) gene, partial cds. ** [1] ** 1-424 ** Ishida F.; ** "Submission"; ** Unpublished. ** NCBI gi: 886281 ** source 1..424 ** /organism="Homo sapiens" ** /sequenced_mol="DNA" ** CDS <105..>260 ** /gene="GPIb" ** /note="isoform A; putative; NCBI gi: 886282" ** /codon_start=1 ** /product="glycoprotein Ib alpha" ** /db_xref="PID:g886282" ** CDS_1_OUT_OF_1 ** 05-JUL-1995 (Rel. 44, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 52 AA; 5187 MW; 829FBEB4792EA30F CRC64; SEPAPSPTTP EPTSEPAPSP TTPEPTSEPA PSPTTPEPTS EPAPSPTTPE PT // ID Q14489 PRELIMINARY; PRT; 58 AA. AC Q14489; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE RIBOSOMAL PROTEIN S10 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RA Dmitrenko V.V., Garifulin O.M., Shostak K.A., Smikodub A.I., RA Kavsan V.M.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; Z70761; CAA94807.1; -. KW Ribosomal protein. FT NON_TER 1 1 FT NON_TER 58 58 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for ribosomal protein S10 ** [1] ** 1-174 ** Dmitrenko V.V., Garifulin O.M., Shostak K.A., Smikodub A.I., ** Kavsan V.M.; ** "Characterization of different mRNA types expressed in human ** brain"; ** Unpublished. ** [2] ** 1-174 ** Dmitrenko V.V.; ** ; ** Submitted (12-APR-1996) to the EMBL/GenBank/DDBJ databases. ** Dmitrenko V. V., Institute of Molecular Biology and Genetics, ** Biosynthesis of Nucleic Acids, Zabolotnogo 150, Kiev, Ukraine, ** 252627 ** source 1..174 ** /organism="Homo sapiens" ** /clone="ICRFp507K114" ** /dev_stage="fetus" ** /tissue_type="brain" ** /clone_lib="S. Meier-Ewert's cDNA library no. 507" ** CDS <1..>174 ** /codon_start=1 ** /product="ribosomal protein S10" ** /db_xref="PID:e236293" ** CDS_1_OUT_OF_1 ** 15-APR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 58 AA; 6281 MW; CB8CCC9198F69FDB CRC64; KGLEGERPAR LTRGEADRDT YRRSAVPPGA DKKAEAGLGQ QPEFQFRGGF GRGRGQPP // ID Q14497 PRELIMINARY; PRT; 25 AA. AC Q14497; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE CCAAT BINDING FACTOR SUBUNIT C (FRAGMENT). GN HCBF-C. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RA Dmitrenko V.V., Garifulin O.M., Shostak K.A., Smikodub A.I., RA Kavsan V.M.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; Z70024; CAA93846.1; -. FT NON_TER 25 25 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for CCAAT binding factor subunit gamma ** [1] ** Dmitrenko V.V., Garifulin O.M., Shostak K.A., Smikodub A.I., ** Kavsan V.M.; ** "Characterization of different mRNA types expressed in human ** brain"; ** Unpublished. ** [2] ** 1-270 ** Dmitrenko V.V.; ** ; ** Submitted (07-MAR-1996) to the EMBL/GenBank/DDBJ databases. ** Dmitrenko V. V., Institute of Molecular Biology and Genetics, ** Biosynthesis of Nucleic Acids, Zabolotnogo 150, Kiev, Ukraine, ** 252627 ** source 1..270 ** /organism="Homo sapiens" ** /clone="ICRFp507N0593" ** /dev_stage="fetus" ** /tissue_type="brain" ** /clone_lib="S. Meier-Ewert's cDNA library no.507" ** CDS 196..>270 ** /product="CCAAT binding factor subunit C" ** /function="transcription factor" ** /gene="hCBF-C" ** /note="homologous to rat CCAAT binding factor subunit ** C ** (rCBF-C)" ** /db_xref="PID:e226027" ** CDS_1_OUT_OF_1 ** 08-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 25 AA; 2649 MW; 12DE150C48C31875 CRC64; MSTEGGFGGT SSSDAQQSLQ SFWPR // ID Q14551 PRELIMINARY; PRT; 39 AA. AC Q14551; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE ALBUMIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RA Dmitrenko V.V., Kavsan V.M.; RL Submitted (JAN-1990) to the EMBL/GenBank/DDBJ databases. DR EMBL; X51365; CAA35749.1; -. FT NON_TER 1 1 FT NON_TER 39 39 ** ** ################# SOURCE SECTION ################## ** Human mRNA for albumin (clone pHA19) ** [1] ** 1-124 ** Dmitrenko V.V., Kavasan V.M.; ** ; ** Submitted (04-JAN-1990) to the EMBL/GenBank/DDBJ databases. ** Dmitrenko V.V., Kavasan V.M., Institute of Molecular Biology and ** Genetics, Acad. Sci. Ukr. SSR, 252627 Kiev, Zabolotnogo Str. 150, ** USSR. ** [2] ** 1-124 ** Dmitrenko V.V., Kavsan V.M.; ** ; ** Unpublished. ** For clones pHA1,pHA12 and pHA8,25 see and . ** Data kindly reviewed (18-SEP-1990) by Dmitrenko V.V. ** source 1..117 ** /organism="Homo sapiens" ** /dev_stage="embryo" ** /tissue_type="liver" ** /cell_type="hepatocyte" ** CDS <1..>117 ** /codon_start=1 ** /product="albumin" ** /db_xref="PID:g930070" ** CDS_1_OUT_OF_1 ** 05-AUG-1995 (Rel. 44, Last updated, Version 4) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 39 AA; 4619 MW; ED477E0AD309370B CRC64; QLIHLFFFFV GVKPTPCLKN INFFNHFASF LCASINKKW // ID Q14579 PRELIMINARY; PRT; 30 AA. AC Q14579; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HUMER (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Oberbaeumer I.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; X85129; CAA59443.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for humer ** [1] ** Oberbaeumer I.; ** ; ** Submitted (06-MAR-1995) to the EMBL/GenBank/DDBJ databases. ** I. Oberbaeumer, Max-Planck-Institut fuer Biochemie, Am Klopferspitz ** 18a, D-82152 Martinsried, FRG ** [2] ** 1-643 ** Oberbaeumer I.; ** "A new member of the highly conserved multigene family of ** thiol-specific antioxidant proteins (TSA) of mouse with ** wide-spread occurrence in adherent cell lines: defining ** orthologous mRNAs by their 3' untranslated regions."; ** Unpublished. ** Related sequence: T10952; T10244 ** source 1..643 ** /organism="Homo sapiens" ** /cell_line="HT 1080 (fibrosarcoma, ATCC CCL 1212)" ** /clone_lib="RT-PCR" ** /clone="14" ** CDS <1..93 ** /partial ** /codon_start=1 ** /product="humer" ** /note="equivalent of mouse mer5 gene" ** /db_xref="PID:g854126" ** CDS_1_OUT_OF_1 ** 31-MAY-1995 (Rel. 43, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 30 AA; 3334 MW; 5713AF472692E46E CRC64; EVCPANWTPD SPTIKPSPAA SKEYFQKVNQ // ID Q14759 PRELIMINARY; PRT; 11 AA. AC Q14759; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE LYMPHOCYTE CYTOSOLIC PROTEIN 2 (FRAGMENT). GN LCP2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Sunden S.L.F., Carr L.L., Clements J.L., Motto D.G., Koretzky G.A.; RL Genomics 0:0-0(0). DR EMBL; U44065; AAA93308.1; -. FT NON_TER 1 1 FT NON_TER 11 11 ** ** ################# SOURCE SECTION ################## ** Human lymphocyte cytosolic protein 2 (LCP2) gene, partial cds, ** partial intron. ** [1] ** 1-500 ** Sunden S.L.F., Carr L.L., Clements J.L., Motto D.G., Koretzky G.A.; ** "Polymorphism in and localization of the gene encoding the 76 kDa ** SH2 domain-containing Leukocyte Protein (SLP-76) to chromosome ** 5q33.1-qter"; ** Unpublished. ** [2] ** 1-500 ** Clements J.L., Sunden S.L.F., Motto D.G., Koretzky G.A.; ** ; ** Submitted (29-DEC-1995) to the EMBL/GenBank/DDBJ databases. ** J.L. Clements, Pediatrics, University of Iowa, 440G EMRB, Iowa ** City, IA 52242, USA ** NCBI gi: 1203823 ** source 1..500 ** /organism="Homo sapiens" ** /chromosome="5" ** /map="5q33.1-qter" ** CDS <1..>34 ** /gene="LCP2" ** /note="SLP-76; 76 kDa SH2 domain-containing leukocyte ** protein; NCBI gi: 1203827" ** /codon_start=2 ** /product="lymphocyte cytosolic protein 2" ** /db_xref="PID:g1203827" ** CDS_1_OUT_OF_1 ** 08-APR-1996 (Rel. 47, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 11 AA; 1242 MW; D695104224072DDD CRC64; EAEAALRKIN Q // ID Q14760 PRELIMINARY; PRT; 25 AA. AC Q14760; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE LYMPHOCYTE CYTOSOLIC PROTEIN 2 (FRAGMENT). GN LCP2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Sunden S.L.F., Carr L.L., Clements J.L., Motto D.G., Koretzky G.A.; RL Genomics 0:0-0(0). DR EMBL; U44067; AAA93309.1; -. DR EMBL; U44066; AAA93309.1; JOINED. FT NON_TER 1 1 FT NON_TER 25 25 ** ** ################# SOURCE SECTION ################## ** Human lymphocyte cytosolic protein 2 (LCP2) gene, partial cds, ** partial intron. ** [1] ** 1-361 ** Sunden S.L.F., Carr L.L., Clements J.L., Motto D.G., Koretzky G.A.; ** "Polymorphism in and localization of the gene encoding the 76 kDa ** SH2 domain-containing Leukocyte Protein (SLP-76) to chromosome ** 5q33.1-qter"; ** Unpublished. ** [2] ** 1-361 ** Clements J.L., Sunden S.L.F., Motto D.G., Koretzky G.A.; ** ; ** Submitted (29-DEC-1995) to the EMBL/GenBank/DDBJ databases. ** J.L. Clements, Pediatrics, University of Iowa, 440G EMRB, Iowa ** City, IA 52242, USA ** NCBI gi: 1203825 ** source 1..361 ** /organism="Homo sapiens" ** /chromosome="5" ** /map="5q33.1-qter" ** CDS join(U44066:<1..36,322..>361) ** /gene="LCP2" ** /note="SLP-76; 76 kDa SH2 domain-containing leukocyte ** protein; NCBI gi: 1203828" ** /codon_start=1 ** /product="lymphocyte cytosolic protein 2" ** /db_xref="PID:g1203828" ** CDS_1_OUT_OF_1 ** 08-APR-1996 (Rel. 47, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 25 AA; 2868 MW; 8B7E8429F398865E CRC64; FYXXGTGLRG KEDXLSVXXI XDXFX // ID Q14864 PRELIMINARY; PRT; 109 AA. AC Q14864; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE MPS1 PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTAL; RA Spilsbury K., O'Mara M.A., Wu W., Rowe P.B., Symonds G., Takayama Y.; RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; L20314; AAA36324.1; -. FT NON_TER 1 1 FT NON_TER 109 109 ** ** ################# SOURCE SECTION ################## ** Human MPS1 gene, partial cds. ** [1] ** 1-328 ** Spilsbury K., O'Mara M.A., Wu W., Rowe P.B., Symonds G., ** Takayama Y.; ** "MPS1,a novel macrophage expressed gene isolated by differential ** cDNA analysis"; ** Unpublished. ** source 1..328 ** /organism="Homo sapiens" ** /sequenced_mol="DNA" ** /tissue_type="placental" ** CDS <1..>328 ** /note="partial protein" ** /product="MPS1 protein" ** /codon_start=1 ** /db_xref="PID:g553591" ** CDS_1_OUT_OF_1 ** 05-DEC-1993 (Rel. 38, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 109 AA; 12462 MW; A5205A8C4E70E893 CRC64; PVLEVLPGGG WDNLRNVDMG RVMELTYSNC RTTEDGQYII PDEIFTIPQK QSNLEMNSEI LESWANYQSS TSYSINTELS LFSKVNGKFS TDFQRMKTLQ VKDQAITTR // ID Q14865 PRELIMINARY; PRT; 246 AA. AC Q14865; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE MODULATOR RECOGNITION FACTOR 2 (FRAGMENT). GN MRF-2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=FORESKIN; RA Merrills B.W., Huang T.H., Oka T., LeBon T.R., Gertson P.N., RA Itakura K.; RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases. DR EMBL; M73837; AAA59870.1; -. DR INTERPRO; IPR001606; -. DR PFAM; PF01388; ARID; 1. FT NON_TER 1 1 FT NON_TER 246 246 ** ** ################# SOURCE SECTION ################## ** Human modulator recognition factor 2 (MRF-2) mRNA, complete cds. ** [1] ** 1-740 ** Merrills B.W., Huang T.H., Oka T., LeBon T.R., Gertson P.N., ** Itakura K.; ** "A new family of DNA binding factors contain a member responsive ** to retinoic acid"; ** Unpublished. ** NCBI gi: 188685 ** source 1..740 ** /organism="Homo sapiens" ** /cell_type="fibroblast (not transformed)" ** /haplotype="NA" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="foreskin" ** /tissue_lib="lambda gt11" ** CDS <1..>740 ** /gene="MRF-2" ** /note="NCBI gi: 553592" ** /codon_start=1 ** /product="modulator recognition factor 2" ** /db_xref="PID:g553592" ** CDS_1_OUT_OF_1 ** 18-JAN-1995 (Rel. 42, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01388; ARID; 14; 125; T; 19-JUN-2000; SQ SEQUENCE 246 AA; 27862 MW; 2AD44181EAFD476C CRC64; KVSNEEKPKV AIGEECRADE QAFLVALYKY MKERKTPIER IPYLGFKQIN LWTMFQAAQK LGGYETITAR RQWKHIYDEL GGNPGSTSAA TCTRRHYERL ILPYERFIKG EEDKPLPPIK PRKQENSSQE NENKTKVSGT KRIKHEIPKS KKEKENAPKP QDAAEVSSEQ EKEQETLISQ KSIPEPLPAA DMKKKIEGYQ EFSAKPLASR VDPEKDNETD QGSNSEKVAE EAGEKGPTPP LPSAPL // ID Q14880 PRELIMINARY; PRT; 187 AA. AC Q14880; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE MUCIN (FRAGMENT). GN MUC5B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=TRACHEOBRONCHIAL MUCOSA; RA Aubert J.; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; X74954; CAA52909.1; -. FT NON_TER 1 1 FT NON_TER 187 187 ** ** ################# SOURCE SECTION ################## ** H.sapiens MUC5B mRNA (clone JER28) for mucin (partial) ** [1] ** 1-561 ** Aubert J.; ** ; ** Submitted (07-SEP-1993) to the EMBL/GenBank/DDBJ databases. ** J. Aubert, Unite Inserm 16, Place de Verdun, 59045 Lille cedex, ** FRANCE ** source 1..561 ** /organism="Homo sapiens" ** /tissue_type="tracheobronchial mucosa" ** /chromosome="11" ** /map="11p15" ** /clone="JER28" ** CDS <1..>561 ** /gene="MUC5B" ** /product="mucin" ** /partial ** /codon_start=1 ** /db_xref="PID:g407070" ** CDS_1_OUT_OF_1 ** 08-OCT-1993 (Rel. 37, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 187 AA; 18993 MW; 8F89B7AA6C2F890E CRC64; SSTPGTTWIL TEPSTTATVT GPTGSTATAS STQATAGTPH VSTTATTPTV TSSKATPFSS PGTATALPAL RSTATTPTAT SFTAIPLSWA PTGPLSQTTT PRPPCPQPHP PPLQRLSTPP PVLTTTPPPT GHRLCGHPLL HPSNSSHYQS ADYHNHGFTA TPSSSPGTAR TLPVWISTTT TPTTRGS // ID Q14881 PRELIMINARY; PRT; 622 AA. AC Q14881; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE MUCIN (FRAGMENT). GN MUC5B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=TRACHEOBRONCHIAL MUCOSA; RA Desseyn J.L., Guyonnet-Duperat V., Porchet N., Aubert J.P., Laine A.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; X74955; CAA52910.1; -. FT NON_TER 1 1 FT NON_TER 622 622 ** ** ################# SOURCE SECTION ################## ** H.sapiens MUC5B mRNA (clone JER57) for mucin (partial) ** [1] ** Aubert J.; ** ; ** Submitted (07-SEP-1993) to the EMBL/GenBank/DDBJ databases. ** J. Aubert, Unite Inserm 16, Place de Verdun, 59045 Lille cedex, ** FRANCE ** [2] ** 1-1866 ** Desseyn J.L., Guyonnet-Duperat V., Porchet N., Aubert J.P., ** Laine A.; ** "Human mucin gene MUC5B: the 10.7 kb large central exon encodes ** various alternate subdomains resulting in a super repeat"; ** Unpublished. ** [3] ** 1-1866 ** Laine A.; ** ; ** Submitted (12-JUN-1996) to the EMBL/GenBank/DDBJ databases. ** A. Laine, Inserm U377, Place de Verdun, 59045 Lille cedex, FRANCE ** source 1..1866 ** /organism="Homo sapiens" ** /tissue_type="tracheobronchial mucosa" ** /chromosome="11" ** /map="11p15" ** /clone="JER57" ** /germline ** CDS <1..>1866 ** /gene="MUC5B" ** /product="mucin" ** /partial ** /codon_start=1 ** /db_xref="PID:e248524" ** CDS_1_OUT_OF_1 ** 12-JUN-1996 (Rel. 48, Last updated, Version 11) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 622 AA; 61787 MW; 4FC85A52F50D57E5 CRC64; LGLECRAQAQ PGVPLGELGQ VVECSLDFGL VCRNREQVGK FKMCFNYEIR VFCCNYGHCP STPATSSTAM PSSTPGTTWI LTELTTTATT TASTGSTATP SSTPGTAPPP KVLTSPATTP TATSSKATSS SSPRTATTLP VLTTTATKST ATSVTPIPSS TLGTTGTLPE QTTTPVATMS TIHPSSTPET THTSTVLTTK ATTTRATSST STPSSTPGTT WILTELTTAA TTTAGTGPTA TPSSTPGTTW ILTELTTTAT TTASTGSTAT LSSTPGTTWI LTEPSTTATV TVPTGSTATA SSTQATAGTP HVSTTATTPT VTSSKATPSS SPGTATALPA LRSTATTPTA TSFTAIPSSS LGTTWTRLSQ TTTPTATMST ATPSSTPETV HTSTVLTATA TTTGATGSVA TPSSTPGTAH TTKVPTTTTT GFTATPSSSP GTALTPPVWI STTTTPTTTT PTTSGSTVTP SSIPGTTHTA RVLTTTTTTV ATGSMATPSS STQTSGTPPS LTTTATTITA TGSTTNPSST PGTTPIPPVL TSTATTPAAT SSKATSSSSP RTATTLPVLT STATKSTATS FTPIPSSTLW TTWTVPAQTT TPMSTMSTIH TSSTPETTHT ST // ID Q14882 PRELIMINARY; PRT; 330 AA. AC Q14882; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE MUCIN (FRAGMENT). GN MUC5B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=TRACHEOBRONCHIAL MUCOSA; RA Aubert J.; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; X74956; CAA52911.1; -. FT NON_TER 1 1 FT NON_TER 330 330 ** ** ################# SOURCE SECTION ################## ** H.sapiens MUC5B mRNA (clone JUL10) for mucin (partial) ** [1] ** 1-991 ** Aubert J.; ** ; ** Submitted (07-SEP-1993) to the EMBL/GenBank/DDBJ databases. ** J. Aubert, Unite Inserm 16, Place de Verdun, 59045 Lille cedex, ** FRANCE ** source 1..991 ** /organism="Homo sapiens" ** /tissue_type="tracheobronchial mucosa" ** /chromosome="11" ** /map="11p15" ** /clone="JUL10" ** CDS <1..>991 ** /gene="MUC5B" ** /product="mucin" ** /partial ** /codon_start=1 ** /db_xref="PID:g407053" ** CDS_1_OUT_OF_1 ** 08-OCT-1993 (Rel. 37, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 330 AA; 35556 MW; 97892E19FFC4FA50 CRC64; PTKATTTRAT SSMSTPSSTP GMTWILTELT TAATTTAATA PHCDPVLHPR DHLDPHRAQH YSTVTVPTGS QPTASSTRGT AGTLKVLTSD HHTHSHQLQS HSLLQSRDCN RPSSTEKHSH HTHSYQRYSH PLFLPGTAWT RLSQTTTPTA TMSTATPSST PETVHTSTVL TTTATTTRAT ALWPPPPPPQ EQLTLPKCRL PQPRLHSYPL LQPRDGTHAS SVDQHNHHTH NQRLHGDPLL HPGTTHTATV LTTTTTTVPL VLWQHPPLAH RPVVLPPSLT TTATTITATG STTNPSSTPG TTPIPPVLTT TANHTCSHQQ HSDSLLCPRE // ID Q14913 PRELIMINARY; PRT; 40 AA. AC Q14913; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE NA+/CA2+ EXCHANGER (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=AIRWAY SMOOTH MUSCLE; RA Pitt A., Knox A.J.; RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; X91815; CAA62923.1; -. FT NON_TER 1 1 FT NON_TER 40 40 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for Na+/Ca2+ exchanger isoform ** [1] ** Pitt A., Knox A.J.; ** "Molecular characterization of thr Na+/Ca2+ exchanger isoform ** expressed in human airway smooth muscle."; ** Unpublished. ** [2] ** 1-122 ** Pitt A.; ** ; ** Submitted (07-SEP-1995) to the EMBL/GenBank/DDBJ databases. ** A. Pitt, Nottingham University, Respiratory Medicine, City ** Hospital, Hucknall Road, Nottingham, NG5 1PB, UK ** source 1..122 ** /organism="Homo sapiens" ** /dev_stage="adult" ** /tissue_type="airway smooth muscle" ** CDS join(<1..104,105..>122) ** /partial ** /codon_start=2 ** /product="Na+/Ca2+ exchanger" ** /note="alternatively spliced isoform variable region" ** /db_xref="PID:g1008973" ** CDS_1_OUT_OF_1 ** 04-OCT-1995 (Rel. 45, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 40 AA; 4787 MW; C9126B9105B01AC2 CRC64; KIITIRIFDR EEYEKECSLS LVLEEPKWIR RGMKGGFTIT // ID Q14928 PRELIMINARY; PRT; 41 AA. AC Q14928; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE KRUEPPEL-TYPE ZINC FINGER PROTEIN (FRAGMENT). GN ZNF169. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Dean M., Chidambaram A., Gerrard B.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U28322; AAA70187.1; -. DR INTERPRO; IPR001909; -. DR PFAM; PF01352; KRAB; 1. FT NON_TER 1 1 FT NON_TER 41 41 ** ** ################# SOURCE SECTION ################## ** Human Krueppel-type zinc finger protein (ZNF169) gene, partial cds. ** [1] ** 1-444 ** Dean M., Chidambaram A., Gerrard B.; ** ; ** Submitted (02-JUN-1995) to the EMBL/GenBank/DDBJ databases. ** Michael Dean, LVC, NCI-FCRDC, P.O. Box B, Frederick, MD 21702, USA ** NCBI gi: 903595 ** source 1..444 ** /organism="Homo sapiens" ** /map="9q22-31" ** /chromosome="9" ** CDS <59..>184 ** /gene="ZNF169" ** /note="NCBI gi: 903598" ** /codon_start=3 ** /product="Krueppel-type zinc finger protein" ** /db_xref="PID:g903598" ** CDS_1_OUT_OF_1 ** 26-JUL-1995 (Rel. 44, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01352; KRAB; 4; 41; T; 19-JUN-2000; SQ SEQUENCE 41 AA; 4816 MW; 653EF5ADE02B70AF CRC64; IDGFRDVAVA FTQKEWKLLS SAQRTLYREV MLENYSHLVS L // ID Q15175 PRELIMINARY; PRT; 535 AA. AC Q15175; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE PARANEOPLASTIC ANTIGEN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Fathallah-Shaykh H.M., Finizio J., Ho A., Rosenblum M., Posner J.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; L02867; AAA91850.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Homo sapiens 62 kDa paraneoplastic antigen mRNA, 3' end. ** [1] ** 1-2750 ** Fathallah-Shaykh H.M., Finizio J., Ho A., Rosenblum M., Posner J.; ** "Cloning and characterization of a second leucine zipper protein ** recognized by the sera of the patients with antibody associated ** paraneoplastic cerebellar degeneration"; ** Unpublished. ** NCBI gi: 1220352 ** source 1..2750 ** /organism="Homo sapiens" ** /cell_line="HeLa" ** /tissue_lib="1-ZapII" ** CDS <1..1608 ** /note="62 kDa; NCBI gi: 1220353" ** /codon_start=1 ** /product="paraneoplastic antigen" ** /db_xref="PID:g1220353" ** CDS_1_OUT_OF_1 ** 12-MAR-1996 (Rel. 47, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 535 AA; 58014 MW; 6C80A459E888A1DA CRC64; YRIPGGGTWQ SARPRVGSRR AVDGEGARRG LCSPSSRRWR PGPPQPHCPG PRAPALSCAA AAPARRPRGH AESRRDGGLG SAEEEESWYD QQDLEQDLHL AAELGKTLLE RNKELEGSLQ QMYSTNEEQV QEIEYLTKQL DTLRHVNEQH AKVYEQLDLT ARDLELTNHR LVLESKAAQQ KIHGLTETIE RLQAQVEELQ AQVEQLRGLE QLRVLREKRE RRRTIHTFPC LKELCTSPRC KDAFRLHSSS LELPAAPGAG ERAAADPGGG AALPGEPGAA AQGAGGARVH RGAAGVLGAG APAVRDGGLS PACAGAGGRA AGAAADEAGQ DLPTGSGTTT WPRPCSHPSR RPLRPTIPSP AAGTTWAPRT GSPHRQPLQA TWCARAAATL RSTPSWPKTQ PAGTRATSHC TPTALRKRGM SILREVDEQY HALLEKYEEL LSKCRQHGAG VRDAGVQTSR PISRDSSWRD LRGGEEGQGE VKAGEKSLSQ HVEAVDKRLE QSQPEYKALF KEIFSRIQKT KADINATKVK THSSK // ID Q15371 PRELIMINARY; PRT; 150 AA. AC Q15371; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE RIBOSOMAL PROTEIN L18A HOMOLOGUE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Zenz K.I.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; X80821; CAA56787.1; -. KW Ribosomal protein. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for ribosomal protein L18a homologue ** [1] ** Zenz K.I.; ** ; ** Unpublished. ** [2] ** 1-660 ** Zenz K.I.; ** ; ** Submitted (02-AUG-1994) to the EMBL/GenBank/DDBJ databases. ** K.I. Zenz, Institute of Immunology, Christian-Albrechts University, ** Kiel, Michaelisstr. 5, 24105 Kiel, FRG ** source 1..660 ** /organism="Homo sapiens" ** /cell_type="lymphocyte" ** /cell_line="human periferal lymphocytes" ** CDS <200..652 ** /partial ** /codon_start=1 ** /product="ribosomal protein L18a homologue" ** /db_xref="PID:g527580" ** CDS_1_OUT_OF_1 ** 05-AUG-1994 (Rel. 40, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 150 AA; 18050 MW; 4E5E933C97FA075F CRC64; TEDLFLNMEH ESLTLEKKSK LEKNIKDDKS TKEKHVSKER NFKEERDKIK KESENLLLWG MSAIEESIGL HLVEKEIDIE KQEKHIKESK EKPEKRSQIK EKDIEKMERK TFDKGQAYIR ITQTKWPYKK GEKEQKYCCL LKKPDGQREK // ID Q15489 PRELIMINARY; PRT; 55 AA. AC Q15489; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE MYELIN ASSOCIATED GLYCOPROTEIN (FRAGMENT). GN S-MAG. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RX MEDLINE=98154940; PubMed=9495552; RA Miescher G., Luetzelschwab R., Erne B., Ferracin F., Huber S., RA Stack A.J.; RT "Reciprocal expression of myelin-associated glycoprotein splice RT variants in the adult human peripheral and central nervous systems."; RL Brain Res. Mol. Brain Res. 52:308-315(1997). DR EMBL; X98405; CAA67055.1; -. KW Myelin. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for myelin associated glycoprotein, S-MAG ** [1] ** Miescher G., Luetzelschwab R., Huber S., Ferracin F., Erne B., ** Stack A.J.; ** "Differential expression of human MAG isoforms in brain and ** nerve"; ** Unpublished. ** [2] ** 1-446 ** Miescher G.C.; ** ; ** Submitted (15-MAY-1996) to the EMBL/GenBank/DDBJ databases. ** G.C. Miescher, University Hospitals Basel, Neurobiology Lab. ** Department of Research, Hebelstrasse 20, Kantonsspital Basel, ** Basel, 4031, Switzerland ** source 1..446 ** /organism="Homo sapiens" ** /chromosome="19" ** /map="q13.1" ** /dev_stage="adult" ** /lab_host="E.coli" ** /isolate="pMAG-PCRII#11" ** /tissue_type="brain" ** CDS <1..169 ** /codon_start=2 ** /gene="S-MAG" ** /product="myelin associated glycoprotein" ** /db_xref="PID:e248458" ** misc_feature 137..181 ** /note="alternative splice from exon 12" ** CDS_1_OUT_OF_1 ** 11-JUN-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 55 AA; 6106 MW; 34D851778133F87F CRC64; AIVCYITQTR RKKNVTESPS FSAGDNPPVL FSSDFRISGA PEKYESKEVS TLESH // ID Q15559 PRELIMINARY; PRT; 102 AA. AC Q15559; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE (CLONE TEC14) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Piek E., Mosselman S.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; L32558; AAA36727.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone tec14) mRNA, partial cds. ** [1] ** 1-320 ** Piek E., Mosselman S.; ** ; ** Unpublished. ** NCBI gi: 483354 ** source 1..320 ** /organism="Homo sapiens" ** /cell_line="Tera-2 (EC)" ** /sequenced_mol="cDNA to mRNA" ** /tissue_lib="lambda GEM2" ** CDS <1..311 ** /note="(embryonal carcinoma) cells. The sequence may ** contain mismatches (one strand sequenced only once). ** 97% ** identical in 320 bp overlap with human 54 kDA prot; ** ORF. ** sequence is expressed in human Tera-2 clone 13; NCBI ** gi: ** 483355." ** /codon_start=3 ** /db_xref="PID:g483355" ** CDS_1_OUT_OF_1 ** 19-MAY-1994 (Rel. 39, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 102 AA; 11659 MW; B447711590819F74 CRC64; IQANVHKGHR QRTYGSVIPH ILPLHVLKKT FSLRDFHFSV SLKKNLVLTC LDLFLGVRTP RNDPFVSMML LFTRFLDRPS TILGTGLLYT EGLTVALRLR LS // ID Q15570 PRELIMINARY; PRT; 130 AA. AC Q15570; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE BTF2P44 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., RA Anzevino R., Velona I., Brahe C., Scheffer H., Van Ommen G.J.B., RA Buys C.H.C.M.; RL Eur. J. Hum. Genet. 0:0-0(0). DR EMBL; U21911; AAA64502.1; -. FT NON_TER 130 130 ** ** ################# SOURCE SECTION ################## ** Human basic transcription factor BTF2p44 mRNA, 5' end, partial cds. ** [1] ** der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., ** Anzevino R., VELONA I., Brahe C., Scheffer H., van Ommen G.J.B., ** Buys C.H.C.M.; ** "A provisional transcript map of the spinal muscular atrophy (SMA) ** critical region"; ** Unpublished. ** [2] ** 1-548 ** der Steege G.; ** ; ** Submitted (28-FEB-1995) to the EMBL/GenBank/DDBJ databases. ** Gerrit Van der Steege, University of Groningen, Department of ** Medical Genetics, Antonius Deusinglaan 4, Groningen, 9713 AW, The ** Netherlands ** NCBI gi: 736401 ** source 1..548 ** /clone="5G3 5'-end" ** /clone_lib="library of A. Bernards" ** /organism="Homo sapiens" ** /chromosome="5" ** /map="5q13.1" ** /cell_type="pre-B-cells" ** CDS 157..>548 ** /note="basic transcription factor 2, 44 kDa subunit; ** NCBI ** gi: 736404" ** /codon_start=1 ** /product="BTF2p44" ** /db_xref="PID:g736404" ** CDS_1_OUT_OF_1 ** 23-MAY-1995 (Rel. 43, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 130 AA; 15293 MW; C681910BD2069D13 CRC64; MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH GQVRLGMMRH LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP ISQIGIIVTK SKRAEKLTEL SGNPRKXISS // ID Q15597 PRELIMINARY; PRT; 699 AA. AC Q15597; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE TRANSLATION INITIATIONFACTOR EIF-4GAMMA (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=OVARY; RA Klaudiny J.J., von der Kammer H.H., Scheit K.K.; RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; Z34918; CAA84397.1; -. DR PFAM; PF02020; IF5_eIF4_eIF2; 1. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for translation initiation factor eIF-4gamma ** (partial) ** [1] ** 1-2124 ** Klaudiny J.J., von der Kammer H.H., Scheit K.K.; ** "Characterization of secretory proteins of human ovarian follicle ** cells by cDNA cloning"; ** Unpublished. ** [2] ** 1-2124 ** von der Kammer H.; ** ; ** Submitted (30-JUN-1994) to the EMBL/GenBank/DDBJ databases. ** Heinz von der Kammer, Abteilung fuer Molekulare Biologie, ** Max-Planck-Institut fuer Biophysikalische Chemie, Am Fassberg 11, ** Goettingen, D-37077, Germany ** source 1..2124 ** /organism="Homo sapiens" ** /dev_stage="adult" ** /tissue_type="ovary" ** CDS <1..2100 ** /note="putative" ** /codon_start=1 ** /note="homologue" ** /product="translation initiationfactor eIF-4gamma" ** /db_xref="PID:g510307" ** CDS_1_OUT_OF_1 ** 04-JUL-1994 (Rel. 40, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF02020; IF5_eIF4_eIF2; 618; 699; T; 19-JUN-2000; SQ SEQUENCE 699 AA; 79421 MW; DC65F87073258175 CRC64; RRSIGNIKFI GELFKLKMLT EAIMHDCVVK LLKNHDEESL ECLCRLLTTI GKDLDFEKAK PRMDQYFNQM EKIVKERKTS SRIRFMLQDV IDLRLCNWVS RRADQGPKTI EQIHKEAKIE EQEEQRKVQQ LMTKEKRRPG VQRVDEGGWN TVQGAKNSRV LDPSKFLKIT KPTIDEKIQL VPKAQLGSWG KGSSGGAKAS ETDALRSSAS SLNRFSALQP PAPSGSTPST PVEFDSRRTL TSRGSMGREK NDKPLPSATA RPNTFMRGGS SKDLLDNQSQ EEQRREMLET VKQLTGGVDV ERNSTEAERN KTRESAKPEI SAMSAHDKAA LSEEELERKS KSIIDEFLHI NDFKEAMQCV EELNAQGLLH VFVRVGVEST LERSQITRDH MGQLLYQLVQ SEKLSKQDFF KGFSETLELA DDMAIDIPHI WLYLAELVTP MLKEGGISMR ELTIEFSKPL LPVGRAGVLL SEILHLLCKQ MSHKKVGALW READLSWKDF LPEGEDVHNF LLEQKLDFIE SDSPCSSEAL SKKELSAEEL YKRLEKLIIE DKANDEQIFD WVEANLDEIQ MSSPTFLRAL MTAVCKAAII ADSSTFRVDT AVIKQRVPIL LKYLDSDTEK ELQALYALQA SIVKLDQPAN LLRMFFDCLY DEEVISEDAF YKWESSKDPA EQNGKGVALK SVTAFFTWLR EAEEESEDN // ID Q15636 PRELIMINARY; PRT; 450 AA. AC Q15636; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE TRANSCRIPTION FACTOR (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Lania L.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. DR EMBL; L32162; AAA36767.1; -. DR INTERPRO; IPR001909; -. DR PFAM; PF01352; KRAB; 1. DR PFAM; PF02023; SCAN; 1. FT NON_TER 450 450 ** ** ################# SOURCE SECTION ################## ** Homo sapiens transcription factor mRNA, 5' end. ** [1] ** 1-1520 ** Lania L.; ** "Positional cloning of cDNAs from the human chromosome 3p21-22 ** region identifies a clustered organization of ZNF genes"; ** Unpublished. ** NCBI gi: 487835 ** source 1..1520 ** /organism="Homo sapiens" ** /sequenced_mol="cDNA to mRNA" ** CDS 171..>1520 ** /map="3p21-22" ** /note="NCBI gi: 487836" ** /product="transcription factor" ** /codon_start=1 ** /db_xref="PID:g487836" ** CDS_1_OUT_OF_1 ** 18-MAY-1994 (Rel. 39, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF01352; KRAB; 232; 293; T; 19-JUN-2000; **PM PFAM; PF02023; SCAN; 48; 153; T; 19-JUN-2000; SQ SEQUENCE 450 AA; 50359 MW; A2CC962BAD05C5C2 CRC64; MPPGRWHAAI SSGPVFEGAR ALQTVKKEEE DESYTPVQAR RPQTLNRPGQ ELFRQLFRQL RYHESSGPLE TLSRLRELCR WWLRPDVLSK AQILELLVLE QFLSILPGEL RVWVQLHNPE SGEELWPCWR SCRGTLMGHP GGTRALPEPR CALDGYRSLR SAQIWSLASP LRSSSALGDH LEPPYEIEAR DFLAGQSDTP AAQMPALFPR EGCPGDQVTP TRSLTAQLQE TMTFKDVEVT FSQDEWGWLD SAQRNLYRDV MLENYRNMAS LVGPFTKPAL ISWLEAREPW GLNMQAAQPK GNPVAAPTGD DLQSKTNKFI LNQEPLEEAE TLAVSSGCPA TSVSEGIDRS ILRESFQQNQ SRDKMRDLRE GQMEPPKSEL IGWGGGETSR WVRGGASPPP ALSPLFRITW SGHKDLKDLK VRGLRGLEAP RVNVWETEAN QAASTPGPPA // ID Q15662 PRELIMINARY; PRT; 368 AA. AC Q15662; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE TRANSFORMATION-RELATED PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=EPITHELIUM; RA Shen H., Steinberg M.L.; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. DR EMBL; L24521; AAA36776.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human transformation-related protein mRNA, 3' end. ** [1] ** 1-1240 ** Shen H., Steinberg M.L.; ** ; ** Unpublished. ** source 1..1240 ** /organism="Homo sapiens" ** /cell_type="SV40-transformed keratinocyte" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="epithelium" ** CDS <1..1109 ** /product="transformation-related protein" ** /codon_start=3 ** /db_xref="PID:g403460" ** repeat_region 1..283 ** /rpt_family="Alu" ** /note="Alu-like repeat" ** AA 1 -> 95 ** CDS_1_OUT_OF_1 ** 28-SEP-1993 (Rel. 37, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 368 AA; 42029 MW; A8B79E59EBBBA2B0 CRC64; DRLSLLSPRL ECNGMILAHC KLRLPGFKRF SCLSLPSSWD YRHVPPRQVH FVFSVETGFH RAGQAGLELL TSSVPPTSAF PKCWDYRRDD QAWPTLSSFR GLNKFAFLPK FFAHPISQFQ RVECNVGCPI LLAMKYLAYS SLPGADTMLY FYFYEQEASL AVCNICRQKF HWVLYQISHL YRGVIVDNFL LHPDGRFTWT IFFLSWVKQN SLVDFFFGTE SRSVALLPRL ECSGAMSTLH TVLRPAYSHI YHPDVKEKTH FLGNVFNKRK LQKKILKTPN PLCALHSAPS PSLPPFLRCT GRLPFYLGLD DFLFVAGALM FLPVSFLNPH TLTWPPQCCT RSDCNPLRGQ REISALSHSL PTGLSMPL // ID Q15706 PRELIMINARY; PRT; 112 AA. AC Q15706; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE 13 kDa DIFFERENTIATION-ASSOCIATED PROTEIN (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LUNG ADENOCARCINOMA; RA Wu M., Li B., Wang Z., Cai Y.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U34343; AAB03380.1; -. FT NON_TER 112 112 ** ** ################# SOURCE SECTION ################## ** Human 13kD differentiation-associated protein mRNA, partial cds. ** [1] ** 1-681 ** Wu M., Li B., Wang Z., Cai Y.; ** "Molecular cloning of differentiation associated gene from human ** lung adenocarcinoma cell line treated with all-trans retinoic ** acid"; ** Unpublished. ** [2] ** 1-681 ** Wu M.; ** ; ** Submitted (20-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** Min Wu, Department of Cell Biology, Cancer Institute, Chinese ** Academy of Medical Sciences, Panjiayuan, Chaoyang District, ** Beijing, 100021, China ** source 1..681 ** /organism="Homo sapiens" ** /clone="RA42" ** /sex="female" ** /cell_line="GLC-82" ** /tissue_type="lung adenocarcinoma" ** CDS 345..>681 ** /codon_start=1 ** /product="13kD differentiation-associated protein" ** /db_xref="PID:g995939" ** CDS_1_OUT_OF_1 ** 08-JUL-1996 (Rel. 48, Last updated, Version 3) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 112 AA; 13217 MW; 7751BF462C419080 CRC64; MGKNTFWDVE GSMVPPEWHR WLHSMTDDPP TTKPLTARKF IWTNHNFNVT GPQNNMYLIL PLERRFRSGS HLQHLTSKDN EEQLKHAKYG AFHVITLLLF TIHYNSQLKL CD // ID Q15734 PRELIMINARY; PRT; 232 AA. AC Q15734; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE PHOSPHATIDYLINOSITOL (4,5) BISPHOSPHATE 5-PHOSPHATASE HOMOLOG DE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Nussbaum R.L.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U45974; AAB03215.1; -. DR INTERPRO; IPR000300; -. DR PFAM; PF00783; IPPc; 1. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human phosphatidylinositol (4,5) bisphosphate 5-phosphatase homolog ** mRNA, partial cds. ** [1] ** 1-1616 ** Nussbaum R.L.; ** ; ** Submitted (11-JAN-1996) to the EMBL/GenBank/DDBJ databases. ** Robert L. Nussbaum, NCHGR, NIH, 49 Convent Drive, Bethesda, MD ** 20892, USA ** source 1..1616 ** /organism="Homo sapiens" ** /note="derived using EST HSC39F111, GenBank Accession ** Number F12413, and 5'RACE procedure" ** CDS <1..699 ** /note="phosphatidylinositol (4,5) bisphosphate ** 5-phosphatase homolog" ** /codon_start=1 ** /db_xref="PID:g1399103" ** CDS_1_OUT_OF_1 ** 08-JUL-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00783; IPPc; 2; 138; T; 19-JUN-2000; SQ SEQUENCE 232 AA; 26172 MW; 6C7B868147F97E75 CRC64; RQAWHEGFDE VFWFGDFNFR LSGGRTVVDA LLCQGLVVDV PALLQHDQLI REMRKGSIFK GFQEPDIHFL PSYKFDIGKD TYDSTSKQRT PSYTDRVLYR SRHKGDICPV SYSSCPGIKT SDHRPVYGLF RVKVRPGRDN IPLAAGKFDR ELYLLGIKRR ISKEIQRQQA LQSQNSSTIC SVFAERGLTA ATWGDCIDQN PLGRTKSLPP FGDPRDCGDR ASVPASQEGS QP // ID Q15735 PRELIMINARY; PRT; 397 AA. AC Q15735; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE PHOSPHATIDYLINOSITOL (4,5)BISPHOSPHATE 5-PHOSPHATASE HOMOLOG DE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BRAIN; RA Nussbaum R.L.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U45975; AAB03216.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human phosphatidylinositol (4,5)bisphosphate 5-phosphatase homolog ** mRNA, partial cds. ** [1] ** 1-1496 ** Nussbaum R.L.; ** ; ** Submitted (11-JAN-1996) to the EMBL/GenBank/DDBJ databases. ** Robert L. Nussbaum, NCHGR, NIH, 49 Convent Drive, Bethesda, MD ** 20892, USA ** source 1..1496 ** /organism="Homo sapiens" ** /note="derived using ESTs, GenBank Accession Number ** R13943 ** and R15390" ** /tissue_type="brain" ** /dev_stage="neonatal infant" ** CDS <1..1194 ** /note="phosphatidylinositol (4,5)bisphosphate ** 5-phosphatase ** homolog" ** /codon_start=1 ** /db_xref="PID:g1399105" ** CDS_1_OUT_OF_1 ** 08-JUL-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 397 AA; 43893 MW; 71418E311E24FBFA CRC64; ARGLHFVKFA IDSDQLHQLW EKDQLNMAKN TWPILKGFQE GPLNFAPTFK FDVGTNKYDT SAKKRKPAWT DRILWKVKAP GGGPSPSGRK SHRLQVTQHS YRSHMEYTVS DHKPVAAQFL LQFAFRDDMP LVRLEVADEW VRPEQAVVRY RMETVFARSS WDWIGLYRVG FRHCKDYVAY VWAKHEDVDG NTYQVTFSEE SLPKGHGDFI LGYYSHNHSI LIGITEPFQI SLPSSELASS STDSSGTSSE GEDDSTLELL APKSRSPSPG KSKRHRSRSP GLARFPGLAL RPSSRERRGA SRSPSPQSRR LSRVAPDRSS NGSSRGSSEE GPSGLPGPWA FPPAVPRSLG LLPALRLETV DPGGGGSWGP DREALAPNSL SPSPQGHRGL EEGGLGP // ID Q15752 PRELIMINARY; PRT; 73 AA. AC Q15752; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE RETINOBLASTOMA BINDING PROTEIN 3 (FRAGMENT). GN RBBP3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Vogt T., Welsh J., Stolz W., Kullmann F., Zamudio J., McClelland M.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U50848; AAB86738.1; -. FT NON_TER 1 1 FT NON_TER 73 73 ** ** ################# SOURCE SECTION ################## ** Human retinoblastoma binding protein 3 mRNA, partial cds. ** [1] ** 1-220 ** Vogt T., Welsh J., Stolz W., Kullmann F., McClelland M.; ** ; ** Submitted (06-MAR-1996) to the EMBL/GenBank/DDBJ databases. ** Thomas Vogt, Molecular Science, Sidney Kimmel Cancer Center, 11099 ** North Torrey Pines Road, San Diego, CA 92037, USA ** source 1..220 ** /organism="Homo sapiens" ** /dev_stage="newborn" ** /cell_type="melanocytes" ** CDS <1..>220 ** /gene="RBBP3" ** /note="mRNA is differentially regulated in TPA treated ** cells, i.e., upregulated; sequence has potential to ** form a ** zinc finger motif; new member of the RBBP familiy" ** /codon_start=3 ** /product="retinoblastoma binding protein 3" ** /db_xref="PID:g1480479" ** CDS_1_OUT_OF_1 ** 10-AUG-1996 (Rel. 48, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 73 AA; 8378 MW; DC60BF32D7943E3A CRC64; GDSYHTFXXI PPLHDVPKGD WRCPKCLAQE CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM VPL // ID Q15810 PRELIMINARY; PRT; 77 AA. AC Q15810; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE CLONE 137308 ORF1 (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Sampson M., McClendon D., Barlow C., Wiley K.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RA Hamilton R.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U60873; AAB05597.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human clone 137308 mRNA, partial cds. ** [1] ** 1-601 ** Sampson M., McClendon D., Barlow C., Wiley K.; ** "Human cDNA clone 137308"; ** Unpublished. ** [2] ** 1-601 ** Hamilton R.; ** ; ** Submitted (14-JUN-1996) to the EMBL/GenBank/DDBJ databases. ** Biological Sciences, Mississippi College, 200 South Capitol Street, ** Clinton, MS 39058, USA ** source 1..601 ** /organism="Homo sapiens" ** /clone="137308" ** CDS <1..235 ** /note="orf1 protein." ** /codon_start=2 ** /db_xref="PID:g1478282" ** CDS_1_OUT_OF_1 ** 03-AUG-1996 (Rel. 48, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 77 AA; 8689 MW; 0B3EBD4DF30BA6C2 CRC64; ARVQEGRPWR REPASIDACR LNFQRLRRRK FSNVLFPGLA QEALYSGGYH LKFADELMGG NLKKSTADAS GSRGHQL // ID Q15888 PRELIMINARY; PRT; 8 AA. AC Q15888; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP15H8A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32069; AAA73878.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP15H8A) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557141 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP15H8A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="chromosome X" ** /note="ORF; NCBI gi: 558107" ** /codon_start=2 ** /db_xref="PID:g558107" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 1068 MW; 0315A37EAB5B0763 CRC64; KPEYCWSR // ID Q15889 PRELIMINARY; PRT; 8 AA. AC Q15889; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP15H8B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32070; AAA73879.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP15H8B) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557142 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP15H8B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="chromosome X" ** /note="ORF; NCBI gi: 558108" ** /codon_start=1 ** /db_xref="PID:g558108" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 865 MW; 0474472325A761E7 CRC64; LHPSKLNG // ID Q15890 PRELIMINARY; PRT; 8 AA. AC Q15890; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP19G12A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32083; AAA73880.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP19G12A) mRNA, partial cds. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557146 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP19G12A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xp11.1-q11" ** /note="ORF; NCBI gi: 558109" ** /codon_start=1 ** /db_xref="PID:g558109" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 975 MW; 605EA6C5BEA5A2D3 CRC64; WVSCSQCY // ID Q15891 PRELIMINARY; PRT; 9 AA. AC Q15891; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP2E8B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32131; AAA73881.1; -. FT NON_TER 1 1 FT NON_TER 9 9 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP2E8B) mRNA, partial cds. ** [1] ** 1-26 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557154 ** source 1..26 ** /organism="Homo sapiens" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>26 ** /map="chromosome 17" ** /note="ORF; NCBI gi: 557735" ** /codon_start=1 ** /db_xref="PID:g557735" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 7) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 9 AA; 1030 MW; E56635A1A33686D1 CRC64; EHQMKTSLG // ID Q15892 PRELIMINARY; PRT; 9 AA. AC Q15892; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP3B4A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32071; AAA73882.1; -. FT NON_TER 1 1 FT NON_TER 9 9 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP3B4A) mRNA, partial EST. ** [1] ** 1-26 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557159 ** source 1..26 ** /organism="Homo sapiens" ** /clone="XP3B4A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>26 ** /map="Xq24" ** /note="ORF; NCBI gi: 558110" ** /codon_start=1 ** /db_xref="PID:g558110" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 9 AA; 971 MW; 49B22732CDC40B17 CRC64; ALERAVLLS // ID Q15893 PRELIMINARY; PRT; 8 AA. AC Q15893; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP587A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32073; AAA73883.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP587A) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557169 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP587A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq22" ** /note="ORF; NCBI gi: 558111" ** /codon_start=1 ** /db_xref="PID:g558111" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 874 MW; DAA1B6D7376456C5 CRC64; SQNPLQTS // ID Q15894 PRELIMINARY; PRT; 8 AA. AC Q15894; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP587B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32074; AAA73884.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP587B) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557170 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP587B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq22" ** /note="ORF; NCBI gi: 558112" ** /codon_start=1 ** /db_xref="PID:g558112" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 952 MW; EBC735B1E1F1B6D6 CRC64; MQTHHSLV // ID Q15895 PRELIMINARY; PRT; 8 AA. AC Q15895; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP6A10A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32075; AAA73885.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP6A10A) mRNA, partial EST. ** [1] ** 1-25 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557173 ** source 1..25 ** /organism="Homo sapiens" ** /clone="XP6A10A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>25 ** /map="Xq21.3-q22" ** /note="ORF; NCBI gi: 558113" ** /codon_start=1 ** /db_xref="PID:g558113" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 921 MW; C6C735B33686C1AA CRC64; DTQMKSLV // ID Q15896 PRELIMINARY; PRT; 9 AA. AC Q15896; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP6A10B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32076; AAA73886.1; -. FT NON_TER 1 1 FT NON_TER 9 9 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP6A10B) mRNA, partial EST. ** [1] ** 1-28 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557174 ** source 1..28 ** /organism="Homo sapiens" ** /clone="XP6A10B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>28 ** /map="Xq21.3-q22" ** /note="ORF; NCBI gi: 558114" ** /codon_start=1 ** /db_xref="PID:g558114" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 9 AA; 1047 MW; 11D15731B2C9C054 CRC64; ENIFVTLIV // ID Q15897 PRELIMINARY; PRT; 7 AA. AC Q15897; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP6A11A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32077; AAA73887.1; -. FT NON_TER 1 1 FT NON_TER 7 7 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP6A11A) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557175 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP6A11A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq22" ** /note="ORF; NCBI gi: 558115" ** /codon_start=3 ** /db_xref="PID:g558115" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 7 AA; 814 MW; 672B1DD3372046B0 CRC64; QILKAEL // ID Q15898 PRELIMINARY; PRT; 8 AA. AC Q15898; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP6A11B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32078; AAA73888.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP6A11B) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557176 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP6A11B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq22" ** /note="ORF; NCBI gi: 558116" ** /codon_start=1 ** /db_xref="PID:g558116" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 938 MW; 34A415B0477B45BB CRC64; ESYPISRS // ID Q15900 PRELIMINARY; PRT; 8 AA. AC Q15900; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP7B11A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32079; AAA73890.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP7B11A) mRNA, partial EST. ** [1] ** 1-25 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557179 ** source 1..25 ** /organism="Homo sapiens" ** /clone="XP7B11A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>25 ** /map="Xq27.3-q28,2,3,16" ** /note="ORF; NCBI gi: 558117" ** /codon_start=2 ** /db_xref="PID:g558117" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 931 MW; B5DDC403369AAEB1 CRC64; HCDMKRAA // ID Q15901 PRELIMINARY; PRT; 8 AA. AC Q15901; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP7B11B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32080; AAA73891.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP7B11B) mRNA, partial EST. ** [1] ** 1-25 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557180 ** source 1..25 ** /organism="Homo sapiens" ** /clone="XP7B11B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>25 ** /map="Xq27.3-q28, 2, 3, 16" ** /note="ORF; NCBI gi: 558118" ** /codon_start=1 ** /db_xref="PID:g558118" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 860 MW; 37D72878676729CB CRC64; EFLPGGLQ // ID Q15902 PRELIMINARY; PRT; 8 AA. AC Q15902; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP7E7A) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32081; AAA73892.1; -. FT NON_TER 1 1 FT NON_TER 8 8 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP7E7A) mRNA, partial EST. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557183 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP7E7A" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq24" ** /note="ORF; NCBI gi: 558119" ** /codon_start=2 ** /db_xref="PID:g558119" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 8 AA; 931 MW; 83D699CAB1B1B2C9 CRC64; FVTTDFMA // ID Q15903 PRELIMINARY; PRT; 7 AA. AC Q15903; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE (CLONE XP7E7B) (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., RA Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., Zhao Z.Y., RA Caskey C.T.H.; RL Hum. Mol. Genet. 0:0-0(0). DR EMBL; L32082; AAA73893.1; -. FT NON_TER 1 1 FT NON_TER 7 7 ** ** ################# SOURCE SECTION ################## ** Homo sapiens (clone XP7E7B) mRNA, partial cds. ** [1] ** 1-24 ** Lee C.C., Yazdani A., Wehnert M., Bailey J., Couch L., Xiong M., ** Coolbaugh M.I., Chinault C.A., Baldini A., Lindsay E.A., ** Zhao Z.Y., Caskey C.T.H.; ** "Isolation of chromosome-specific genes by reciprocal probing of ** arrayed cDNAs and cosmid libraries"; ** Unpublished. ** NCBI gi: 557184 ** source 1..24 ** /organism="Homo sapiens" ** /clone="XP7E7B" ** /haplotype="diploid" ** /sequenced_mol="cDNA to mRNA" ** /tissue_type="placenta" ** CDS <1..>24 ** /map="Xq24" ** /note="ORF; NCBI gi: 558120" ** /codon_start=3 ** /db_xref="PID:g558120" ** CDS_1_OUT_OF_1 ** 10-AUG-1995 (Rel. 44, Last updated, Version 6) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 7 AA; 849 MW; 6B040339CDD33DB0 CRC64; AKAFKRE // ID Q16467 PRELIMINARY; PRT; 43 AA. AC Q16467; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-NOV-1996 (TrEMBLrel. 01, Last annotation update) DE PROTON ATPASE HOMOLOGUE (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Bhat K.S.; RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases. DR EMBL; L05089; AAC15853.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human proton ATPase homologue mRNA, 3' end. ** [1] ** 1-373 ** Bhat K.S.; ** "Expressed sequence tags from a human cell line"; ** Unpublished. ** source 1..373 ** /organism="Homo sapiens" ** CDS 1..132 ** /note="Expressed Sequence Tag; amino acid sequence ** shows ** homology with carboxy end of yeast proton ATPase ** proteolipid chain (PIR:A34633)" ** /note="putative" ** /codon_start=1 ** /citation=[1] ** /partial ** /db_xref="PID:g190378" ** CDS_1_OUT_OF_1 ** 08-DEC-1992 (Rel. 34, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 43 AA; 4393 MW; 6E7292577E46BDB3 CRC64; VGSGAALADA QNPSLFVKIL IVEIFGSALA SLGSSSQFFR PPE // ID Q16779 PRELIMINARY; PRT; 51 AA. AC Q16779; DT 01-NOV-1996 (TrEMBLrel. 01, Created) DT 01-NOV-1996 (TrEMBLrel. 01, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HEXOKINASE III (EC 2.7.1.1) (GLUCOKINASE) (HEXOKINASE TYPE IV) DE (FRAGMENT). GN HK3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Colosimo A., Calabrese G., Gennarelli M., Ruzzo A., Sangiuolo F., RA Magnani M., Palka G., Novelli G., DallaPiccola B.; RL Cytogenet. Cell Genet. 0:0-0(0). CC -!- CATALYTIC ACTIVITY: ATP + D-HEXOSE = ADP + D-HEXOSE 6-PHOSPHATE. DR EMBL; L37749; AAB03512.1; -. KW Transferase. FT NON_TER 1 1 FT NON_TER 51 51 ** ** ################# SOURCE SECTION ################## ** Human hexokinase III (HK3) gene, partial cds. ** [1] ** 1-245 ** Colosimo A., Calabrese G., Gennarelli M., Ruzzo A., Sangiuolo F., ** Magnani M., Palka G., Novelli G., Dallapiccola B.; ** "Assignment of the hexokinase type 3 (HK3) gene to human ** chromosome band 5q35.3 by somatic cell hybrids and in situ ** hybridization"; ** Unpublished. ** [2] ** 1-245 ** Colosimo A.; ** ; ** Submitted (11-NOV-1994) to the EMBL/GenBank/DDBJ databases. ** Sanita' Pubblica e Biologia Cellulare, Cattedra di Genetica Umana ** Universita, Via di Tor Vergata, 135, Rome 00133, Italy ** source 1..245 ** /organism="Homo sapiens" ** /clone="pHKIII" ** /map="5q35.3" ** /chromosome="5" ** CDS join(<1..103,197..>245) ** /gene="HK3" ** /EC_number="2.7.1.1" ** /codon_start=1 ** /product="hexokinase III" ** /db_xref="PID:g1402644" ** CDS_1_OUT_OF_1 ** 09-JUL-1996 (Rel. 48, Last updated, Version 4) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 51 AA; 5505 MW; 52380713EE23C165 CRC64; TWSGGPLGTM ALWPCSAPAL MQVWTRRPST PASRGLKRWS AACTWVKSSA T // ID Q92484 PRELIMINARY; PRT; 177 AA. AC Q92484; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-FEB-1997 (TrEMBLrel. 02, Last annotation update) DE ACID SPHINGOMYELINASE-LIKE PHOSPHODIESTERASE (FRAGMENT). GN ASML3A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Hofmann K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; Y08136; CAA69330.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for ASM-like phosphodiesterase 3a ** [1] ** Hofmann K.; ** "Acid Sphingomyelinase is a member of a multi-gene family and ** shares motifs with a large family of metallo-phosphoesterases"; ** Unpublished. ** [2] ** 1-863 ** Hofmann K.; ** ; ** Submitted (17-SEP-1996) to the EMBL/GenBank/DDBJ databases. ** K. Hofmann, Isrec (Swiss Inst. F. Exp. Canc. Res.), Bioinformatics ** Group, Chemin Des Boveresses 155, Ch/1066 Epalinges S/Lausanne, ** SWITZERLAND ** source 1..863 ** /organism="Homo sapiens" ** CDS <1..536 ** /codon_start=3 ** /gene="ASML3a" ** /product="acid sphingomyelinase-like ** phosphodiesterase" ** /note="putative" ** /db_xref="PID:e266650" ** CDS_1_OUT_OF_1 ** 19-SEP-1996 (Rel. 49, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 177 AA; 20634 MW; CA38DDAE817B87EC CRC64; DIFQKYSDVI AGQFYGHTHR DSIMVLSDKK GSPVNSLFVA PAVTPVKSVL EKQTNNPGIR LFQYDPRDYK LLDMLQYYLN LTEANLKGES IWKLEYILTQ TYDIEDLQPE SLYGLAKQFT ILDSKQFIKY YNYFFVSYDS SVTCDKTCKA FQICAIMNLD NISYADCLKQ LYIKHKY // ID Q92485 PRELIMINARY; PRT; 465 AA. AC Q92485; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-JUN-2000 (TrEMBLrel. 14, Last annotation update) DE ACID SPHINGOMYELINASE-LIKE PHOSPHODIESTERASE. GN ASML3B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Hofmann K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; Y08134; CAA69328.1; -. DR INTERPRO; IPR000934; -. ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for ASM-like phosphodiesterase 3b ** [1] ** Hofmann K.; ** "Acid Sphingomyelinase is a member of a multi-gene family and ** shares motifs with a large family of metallo-phosphoesterases"; ** Unpublished. ** [2] ** 1-1610 ** Hofmann K.; ** ; ** Submitted (17-SEP-1996) to the EMBL/GenBank/DDBJ databases. ** K. Hofmann, Isrec (Swiss Inst. F. Exp. Canc. Res.), Bioinformatics ** Group, Chemin Des Boveresses 155, Ch/1066 Epalinges S/Lausanne, ** SWITZERLAND ** source 1..1610 ** /organism="Homo sapiens" ** CDS 122..1519 ** /gene="ASML3b" ** /product="acid sphingomyelinase-like ** phosphodiesterase" ** /note="putative" ** /db_xref="PID:e266651" ** CDS_1_OUT_OF_1 ** 19-SEP-1996 (Rel. 49, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PROSITE; PS50185; PHOSPHO_ESTER; 21; 284; T; 19-JUN-2000; SQ SEQUENCE 465 AA; 51910 MW; AE9FBF92A2C1ED32 CRC64; MRLLAWLIFL ANWGGARAEP GKFWHIADLH LDPDYKVSKD PFQVCPSAGS QPVPDAGPWG DYLCDSPWAL INSSIYAMKE IEPEPDFILW TGDDTPHVPD EKLGEAAVLE IVERLTKLIR EVFPDTKVYA ALGNHDFHPK NQFPAGSNNI YNQIAELWKP WLSNESIALF KKGAFYCEKL PGPSGAGRIV VLNTNLYYTS NALTADMADP GQQFQWLEDV LTDASKAGDM VYIVGHVPPG FFEKTQNKAW FREGFNEKYL KVVRKHHRVI AGQFFGHHHT DSFRMLYDDA GVPISAMFIT PGVTPWKTTL PGVVNGANNP AIRVFEYDRA TLSLXDMVTY FMNLSQANAQ GTPRWELEYQ LTEAYGVPDA SAHSIDTVLD RIAGDQSTLQ RYYVYNSVSY SAGVCDEACS MQHVCAMRQV DIDAYTTCLY ASGTTPVPQL PXLLMALLGL CTTRAVTCQA HHSSW // ID Q92661 PRELIMINARY; PRT; 55 AA. AC Q92661; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE UV-B REPRESSED SEQUENCE, HUR 7 (FRAGMENT). GN HUR 7. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Abts H.F., Breuhahn K., Michel G., Esser P., Ruzicka T.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; X98307; CAA66951.1; -. DR HSSP; P05619; 1HLE. DR INTERPRO; IPR000215; -. DR PFAM; PF00079; serpin; 1. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** H.sapiens mRNA for UV-B repressed sequence, HUR 7 ** [1] ** Abts H.F., Breuhahn K., Michel G., Esser P., Ruzicka T.; ** "Analysis of UV-B modulated gene expression in human keratinocytes ** by mRNA differential display PCR (DD-PCR)"; ** Unpublished. ** [2] ** 1-405 ** Abts H.F.; ** ; ** Submitted (22-MAY-1996) to the EMBL/GenBank/DDBJ databases. ** H.F. Abts, Heinrich-Heine-Universitaet Duesseldorf, Dermatologie, ** Cytokinlabor, Geb.11.80, Moorenstrasse 5, 40225 Duesseldorf, FRG ** source 1..405 ** /organism="Homo sapiens" ** /cell_line="HaCaT" ** /cell_type="keratinocyte" ** CDS <1..170 ** /codon_start=3 ** /gene="HUR 7" ** /db_xref="PID:e260052" ** CDS_1_OUT_OF_1 ** 01-SEP-1996 (Rel. 49, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; **PM PFAM; PF00079; serpin; 2; 34; T; 19-JUN-2000; SQ SEQUENCE 55 AA; 6224 MW; 107A694FEA43F7E6 CRC64; LEDLQAKILG IPYKNNDLSM FVLLPNDIDG LEKVNAYTSL FFLSFPKAFC LRASE // ID Q92771 PRELIMINARY; PRT; 734 AA. AC Q92771; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-AUG-1998 (TrEMBLrel. 07, Last annotation update) DE HELICASE (FRAGMENT). GN CHLR2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RA Amann J.M., Kidd V.J., Lahti J.M.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. DR EMBL; U33834; AAB06963.1; -. KW Helicase. FT NON_TER 1 1 FT NON_TER 734 734 ** ** ################# SOURCE SECTION ################## ** Human CHL1-related helicase (CHLR2) mRNA, partial cds. ** [1] ** 1-2202 ** Amann J.M., Kidd V.J., Lahti J.M.; ** "Isolation and characterization of a human gene related to the ** yeast chromosome transmission fidelity gene, CHL1"; ** Unpublished. ** [2] ** 1-2202 ** Lahti J.M.; ** ; ** Submitted (11-AUG-1995) to the EMBL/GenBank/DDBJ databases. ** Jill M. Lahti, St. Jude Children's Research Hospital, Tumor Cell ** Biology, 332 N. Lauderdale St., Memphis, TN 38105, USA, 38105 ** source 1..2202 ** /organism="Homo sapiens" ** /clone="human CHL-Related 2" ** /clone_lib="HeLa cDNA, K562 cDNA, human fetal liver ** cDNA" ** CDS <1..>2202 ** /gene="CHLR2" ** /codon_start=1 ** /product="helicase" ** /db_xref="PID:g1517818" ** CDS_1_OUT_OF_1 ** 01-SEP-1996 (Rel. 49, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 734 AA; 82439 MW; FBAC66E4801D5F73 CRC64; HRVQLKYAAK RLRQEEEERE NLLRLSREML ETGPEAEWLE QLESGEEELV LAEYESDEEK KVASGVDEDE DDLEEEHITK IYYCSRTHSQ LAQFVHEVKK SPFGKDVRLV SLGSQQNLCV NEDVRSLGSV QLINDRCVDM QRSRHEKKKG AEEEKPKRRR QEKQAACPFY NHEQMGLLRD EALAEVKDME QLLALGKEAR ACPYYRSRLA IPAAQLVVLS YQMLLHAATR QAAGIRLQDQ VVIIDEAHNL IDTITGMHSV EVSGSQLCQA HSQLLQYMER YGKRLKAKNL MYLKQILYLL EKFVAVLGGN IKQNPNTQSL SQTGMELKTI NDFLFQSQID NINLFKVQRY CEKSMISRKL FGFTERYGAV FSSREQPKLA GFQQFLQSLQ PRTTEALAAP ADESQASVPQ PASPLMHIEG FLAALTTANQ DGRVILSRQG SLSQSTLKFL LLNPAVHFAQ VVKECRAVVI AGGTMQPVSD FRQQLLACAG VEAERVVEFS CGHVIPPDNI LPLVICIGVS NQPLEFTFQK RDLPQMMDEV GRILCNLCSV VSGGVVCFFP SYEYLRQVHA HWEKGGLLGH LAARKKIFQE PKSAHQVEQV LLAYSRCIQA CGQERGPVTG ALLLSVVGGK MSEGINFSDN LGRCVVMVGM PFPNIRSAEL QEKMAYLDQT LPRAPGQAPP GKALVENLCM KAVNQSIGRA IRHQKDFASI VLLDQRYARP PVLAKLPAWI RARV // ID Q92792 PRELIMINARY; PRT; 177 AA. AC Q92792; DT 01-FEB-1997 (TrEMBLrel. 02, Created) DT 01-FEB-1997 (TrEMBLrel. 02, Last sequence update) DT 01-FEB-1997 (TrEMBLrel. 02, Last annotation update) DE D13S824E LOCUS (FRAGMENT). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=BONE MARROW; RA Still I.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. DR EMBL; U47635; AAB18856.1; -. FT NON_TER 1 1 ** ** ################# SOURCE SECTION ################## ** Human D13S824E locus mRNA, complete cds. ** [1] ** 1-2486 ** Still I.; ** ; ** Submitted (29-JAN-1996) to the EMBL/GenBank/DDBJ databases. ** Ivan Still, Neurosciences, Cleveland Clinic Foundation, 9500 Euclid ** Avenue, Cleveland, Ohio 44195, USA ** Auffray, C. et al (1995). IMAGE: Integration molecular analysis of ** the human genome and its expression. C.R. Acad. Sci. Paris 318: ** 263-272. ** source 1..2486 ** /organism="Homo sapiens" ** /chromosome="13" ** /tissue_type="bone marrow" ** /cell_type="HeLa" ** /clone_lib="Clontech catolog HL5005a; Stratagene ** catalog ** 936201" ** CDS <1..534 ** /note="DSEG number: D13S824E; orf" ** /codon_start=1 ** /db_xref="PID:g1669391" ** CDS_1_OUT_OF_1 ** 15-NOV-1996 (Rel. 49, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_HUMAN **OX 9606; SQ SEQUENCE 177 AA; 20647 MW; 9005F0FE031F92B5 CRC64; KRRAQVEGED LFPVAISFGR PKEYFPPLYS SESHRFTVLE PNTVSFNFKF WRNMYHQFDR TLHPRQSVFN IIMNMNEQNK QLEKDIKDLE SKIKQRKNKQ TDGILTKELL HSVHPESPNL KTSLCFKEQT LLPVNDALRT IEGSSPADNR YSEYAEEFSK SEPAVVSLEY GVARMTC // ID O54521 PRELIMINARY; PRT; 144 AA. AC O54521; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAY-2000 (TrEMBLrel. 13, Last annotation update) DE SLYA. GN SLYA. OS Salmonella enterica serovar Typhi (made up common name to get long OS OS line){EI3}. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Salmonella. OX NCBI_TaxID=90370, 119912; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=TY2, RF-1; RA Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., RA Nonaka T., Matsui H., Kawahara K., Danbara H.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. DR EMBL; AB010777; BAA24582.1; -. DR EMBL; AB010776; BAA24581.1; -. DR InterPro; IPR000835; B_TESTDOMAIN. DR InterPro; IPR001835; A_TESTDOMAIN. DR Pfam; PF01047; MarR; 1. DR PRINTS; PR00598; HTHMARR. DR PROSITE; PS01117; HTH_MARR_FAMILY; 1. DR SMART; SM1234; Smarty. ** ** ################# SOURCE SECTION ################## ** Salmonella choleraesuis serovar Typhi gene for SlyA, complete cds. ** [1] ** 1-636 ** Okada N.; ** ; ** Submitted (27-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Nobuhiko Okada, Kitasato University, School of Pharmaceutical ** Sciences, ** Department of Microbiology; 5-9-1 Shirokane, Minato, Tokyo 108-8641, ** Japan (E-mail:okadan@platinum.pharm.kitasato-u.ac.j p, ** Tel:03-3444-6161, ** Fax:03-3444-4831) ** [2] ** Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., Nonaka ** T., ** Matsui H., Kawahara K., Danbara H.; ** "Identification of TTG initiation codon in slyA of Salmonella, a gene ** required for survival within macrophages"; ** Unpublished. ** [1] ** 1-636 ** Okada N.; ** ; ** Submitted (27-JAN-1998) to the EMBL/GenBank/DDBJ databases. ** Nobuhiko Okada, Kitasato University, School of Pharmaceutical ** Sciences, ** Department of Microbiology; 5-9-1 Shirokane, Minato, Tokyo 108-8641, ** Japan (E-mail:okadan@platinum.pharm.kitasato-u.ac.j p, ** Tel:03-3444-6161, ** Fax:03-3444-4831) ** [2] ** Kawakami T., Kaneko A., Sekiya K., Okada N., Imajho-Ohmi S., Nonaka ** T., ** Matsui H., Kawahara K., Danbara H.; ** "Identification of TTG initiation codon in slyA of Salmonella, a gene ** required for survival within macrophages"; ** Unpublished. ** source 1..636 ** /organism="Salmonella choleraesuis serovar Typhi" ** /sequenced_mol="DNA" ** /strain="Ty2" ** CDS 154..588 ** /codon_start=1 ** /db_xref="PID:d1025502" ** /transl_table=11 ** /gene="slyA" ** /product="SlyA" ** CDS_IN_EMBL_ENTRY 1 ** ORGANISM DOESN'T EXIST IN SP ** 11-FEB-1998 (Rel. 54, Last updated, Version 2) ** source 1..636 ** /organism="Salmonella choleraesuis choleraesuis" ** /sequenced_mol="DNA" ** /strain="RF-1" ** CDS 154..588 ** /codon_start=1 ** /db_xref="PID:d1025501" ** /transl_table=11 ** /gene="slyA" ** /product="SlyA" ** CDS_IN_EMBL_ENTRY 1 ** ORGANISM DOESN'T EXIST IN SP ** 11-FEB-1998 (Rel. 54, Last updated, Version 2) ** ################# INTERNAL SECTION ################## **PM PFAM; PF01047; MarR; 29; 133; T; 19-JUN-2000; **PM PRINTS; PR00598; HTHMARR; 47; 63; T; 19-JUN-2000; **PM PRINTS; PR00598; HTHMARR; 64; 79; T; 19-JUN-2000; **PM PRINTS; PR00598; HTHMARR; 83; 99; T; 19-JUN-2000; **PM PRINTS; PR00598; HTHMARR; 113; 133; T; 19-JUN-2000; **PM PROSITE; PS01117; HTH_MARR_FAMILY; 62; 96; T; 19-JUN-2000; SQ SEQUENCE 144 AA; 16448 MW; 4647F7704F2D78DE CRC64; MESPLGSDLA RLVRIWRALI DHRLKPLELT QTHWVTLHNI HQLPPDQSQI QLAKAIGIEQ PSLVRTLDQL EDKGLISRQT CASDRRAKRI KLTEKAEPLI AEMEEVIHKT RGEILAGISS EEIELLIKLV AKLEHNIMEL HSHD // ID TRA9_MYCTU STANDARD; PRT; 278 AA. AC P19774; DT 01-FEB-1991 (Rel. 17, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE PUTATIVE TRANSPOSASE FOR INSERTION SEQUENCE ELEMENT IS986/IS6110 DE (ORFB). GN (RV0796 OR MTV042.06) AND (RV2106 OR MTCY261.02) AND GN (RV2279 OR MTCY339.31C) AND (RV2355 OR MTCY98.24) AND GN (RV2814C OR MTCY16B7.29) AND (RV3185 OR MTV014.29) AND GN (RV3187 OR MTV014.31) AND (RV3326 OR MTV016.26). OS Mycobacterium tuberculosis. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1773; KW Transposable element; Transposition; DNA-binding; DNA recombination. SQ SEQUENCE 278 AA; 31369 MW; E4D33328228D7676 CRC64; MPIAPSTYYD HINREPSRRE LRDGELKEHI SRVHAANYGV YGARKVWLTL NREGIEVARC TVERLMTKLG LSGTTRGKAR RTTIADPATA RPADLVQRRF GPPAPNRLWV ADLTYVSTWA GFAYVAFVTD AYARRILGWR VASTMATSMV LDAIEQAIWT RQQEGVLDLK DVIHHTDRGS QYTSIRFSER LAEAGIQPSV GAVGSSYDNA LAETINGLYK TELIKPGKPW RSIEDVELAT ARWVDWFNHR RLYQYCGDVP PVELEAAYYA QRQRPAAG // ID Q9ZQ91 PRELIMINARY; PRT; 312 AA. AC Q9ZQ91; DT 01-MAY-1999 (TrEMBLrel. 10, Created) DT 01-MAY-1999 (TrEMBLrel. 10, Last sequence update) DT 01-JUN-2001 (TrEMBLrel. 17, Last annotation update) DE PUTATIVE HYDROLASE (CONTAINS AN ESTERASE/LIPASE/THIOESTERASE ACTIVE DE SITE SERINE DOMAIN (PROSITE: PS50187). GN T4M8.1. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; eudicotyledons; core eudicots; Rosidae; eurosids II; OC Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Lin X., Kaul S., Shea T.P., Fujii C.Y., Shen M., VanAken S.E., RA Barnstead M.E., Mason T.M., Bowman C.L., Ronning C.M., Benito M., RA Carrera A.J., Creasy T.H., Buell C.R., Town C.D., Nierman W.C., RA Fraser C.M., Venter J.C.; RT "Arabidopsis thaliana chromosome II BAC T4M8 genomic sequence."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. DR EMBL; AC006284; AAD17422.1; -. DR InterPro; IPR000379; Est_lip_thioest_actsite. KW Hydrolase. ** ** ################# SOURCE SECTION ################## ** Arabidopsis thaliana chromosome II BAC T4M8 genomic sequence, ** complete sequence. ** [1] ** 1-89137 ** Lin X., Kaul S., Shea T.P., Fujii C.Y., Shen M., VanAken S.E., ** Barnstead M.E., Mason T.M., Bowman C.L., Ronning C.M., Benito M., ** Carrera A.J., Creasy T.H., Buell C.R., Town C.D., Nierman W.C., ** Fraser C.M., Venter J.C.; ** "Arabidopsis thaliana chromosome II BAC T4M8 genomic sequence"; ** Unpublished. ** [2] ** 1-89137 ** Lin X., Kaul S.; ** ; ** Submitted (05-JAN-1999) to the EMBL/GenBank/DDBJ databases. ** The Institute for Genomic Research, 9712 Medical Center Dr, Rockville, ** MD 20850, USA, xlin@tigr.org ** [3] ** 1-89137 ** Lin X.; ** ; ** Submitted (04-MAR-1999) to the EMBL/GenBank/DDBJ databases. ** The Institute for Genomic Research, 9712 Medical Center Dr., Rockville, ** MD 20850, USA ** On Mar 4, 1999 this sequence version replaced gi:4156124. ** Address all correspondence to: ** Xiaoying Lin ** The Institute for Genomic Research ** 9712 Medical Center Dr. ** Rockville, MD 20850, USA ** e-mail: xlin@tigr.org ** BAC clone T4M8 is from Arabidopsis chromosome II and is contained ** in the YAC clone CIC11A04. ** The orientation of the sequence is from SP6 to T7 end of the BAC ** clone. ** Genes were identified by a combination of three methods: Gene ** prediction programs including GRAIL (available by anonymous ftp ** from arthur.epm.ornl.gov), Genefinder (Phil Green, University of ** Washington), Genscan (Chris Burge, ** http://gnomic.stanford.edu/~chris/GENSCANW.html), and NetPlantGene ** (http://www.cbs.dtu.dk/netpgene/cbsnetpgene.html), searches of the ** complete sequence against a peptide database and the Arabidopsis ** EST database at TIGR (http://www.tigr.org/tdb/at/at.html). ** Annotated genes are named to indicate the level of evidence for ** their annotation. Genes with similarity to other proteins are named ** after the database hits. Genes without significant peptide ** similarity but with EST similarity are named as 'unknown' proteins. ** Genes without protein or EST similarity, that are predicted by more ** than two gene prediction programs over most of their length are ** annotated as 'hypothetical' proteins. Genes encoding tRNAs are ** predicted by tRNAscan-SE (Sean Eddy, ** http://genome.wustl.edu/eddy/tRNAscan-SE/). Simple repeats are ** identified by repeatmasker (Arian Smit, ** http://ftp.genome.washington.edu/RM/RepeatMasker.html). Regions of ** genomic sequence that are not annotated as genes but have predicted ** exons by GRAIL are annotated as misc features. ** source 1..89137 ** /organism="Arabidopsis thaliana" ** /chromosome="II" ** /db_xref="taxon:3702" ** /cultivar="Columbia" ** /map="CIC11A04" ** /clone="T4M8" ** CDS complement(1731..2669) ** /codon_start=1 ** /db_xref="PID:g4335745" ** /gene="T4M8.1" ** /product="putative hydrolase (contains an ** esterase/lipase/thioesterase active site serine domain ** (prosite: PS50187)" ** /protein_id="AAD17422.1" ** CDS_IN_EMBL_ENTRY 30 ** 12-MAR-1999 (Rel. 59, Last updated, Version 4) ** ################# INTERNAL SECTION ################## **ID XXXX_ARATH **PM PROSITE; PS50187; ESTERASE; 69; 174; T; 28-JAN-2000; SQ SEQUENCE 312 AA; 34750 MW; 1D9B933F2BE9DD78 CRC64; MDSVIAFDRS PMFRVYKSGR IERLLGETTV PPSLTPQNGV VSKDIIHSPE KNLSLRIYLP EKVTVKKLPI LIYFHGGGFI IETAFSPPYH TFLTSAVAAA NCLAISVNYR RAPEFPVPIP YEDSWDSLKW VLTHITGTGP ETWINKHGDF GKVFLAGDSA GGNISHHLTM RAKKEKLCDS LISGIILIHP YFWSKTPIDE FEVRDVGKTK GVEGSWRVAS PNSKQGVDDP WLNVVGSDPS GLGCGRVLVM VAGDDLFVRQ GWCYAEKLKK SGWEGEVEVM ETKNEGHVFH LKNPNSDNAR QVVKKLEEFI NK // ID Q9JSZ7 PRELIMINARY; PRT; 355 AA. AC Q9JSZ7; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE UDP-N-acetylglucosamine--N-acetylmuramyl-(pentape pyrophosphoryl- DE undecaprenol N-acetylglucosamine transferase (EC 2.4.1.){EI1}. GN MURG OR NMA2062{EP4}. OS Neisseria meningitidis (serogroup A){EP3}. OC Bacteria; Proteobacteria; beta subdivision; Neisseriaceae; Neisseria. OX NCBI_TaxID=65699; RN [1]{EP3} RP SEQUENCE FROM N.A. RC STRAIN=Z2491 / SEROGROUP A / SEROTYPE 4A; RX MEDLINE=20222556; PubMed=10761919; RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C., RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., RA Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., RA Jagels K., Leather S., Moule S., Mungall K., Quail M.A., RA Rajandream M.A., Rutherford K.M., Simmonds M., Skelton J., RA Whitehead S., Spratt B.G., Barrell B.G.; RT "Complete DNA sequence of a serogroup A strain of Neisseria RT menigitidis Z2491."; RL Nature 404:502-506(2000). DR EMBL; AL162758; CAB85280.1; -.{EI1} KW Transferase{EP2}; Glycosyltransferase{EP2}; Complete proteome{EP5}. ** ** ################# SOURCE SECTION ################## ** Neisseria meningitidis serogroup A strain Z2491 complete genome; segment ** 7/7 ** [1] ** 1-195767 ** Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C., Klee S.R., ** Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M., Davis P., ** Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K., Leather S., ** Moule S., Mungall K., Quail M.A., Rajandream M.A., Rutherford K.M., ** Simmonds M., Skelton J., Whitehead S., Spratt B.G., Barrell B.G.; ** "Complete DNA sequence of a serogroup A strain of Neisseria menigitidis ** Z2491"; ** Nature 404:502-506(2000). ** [2] ** 1-195767 ** Parkhill J.; ** ; ** Submitted (30-MAR-2000) to the EMBL/GenBank/DDBJ databases. ** Submitted on behalf of the Neisseria sequencing team, Sanger Centre, ** Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA E-mail: ** parkhill@sanger.ac.uk ** Notes: ** ** Details of N. meningitidis sequencing at the Sanger Centre ** are available on the World Wide Web. ** (URL, http://www.sanger.ac.uk/Projects/N_meningitidis/) ** ** source 1..195767 ** /db_xref="taxon:487" ** /note="serogroup: A" ** /organism="Neisseria meningitidis" ** /strain="Z2491" ** CDS complement(21643..22710) ** /note="NMA2062, murG, ** UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) ** pyrophosphoryl-undecaprenol N-acetylglucosamine ** transferase, len: 355aa; similar to many eg. SW:P17443 ** (MURG_ECOLI) murG, ** UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) ** pyrophosphoryl-undecaprenol N-acetylglucosamine transferase ** from Escherichia coli (354 aa) fasta scores; E(): 0, 46.2% ** identity in 346 aa overlap." ** /transl_table=11 ** /gene="murG" ** /product="UDP-N-acetylglucosamine--N-acetylmuramyl-(pentape ** pyrophosphoryl-undecaprenol N-acetylglucosamine ** transferase" ** /EC_number="2.4.1.-" ** /protein_id="CAB85280.1" ** misc_feature complement(22163..22172) ** /label=DUS ** /note="Core DNA uptake sequence: gccgtctgaa" ** AA 181 -> 183 ** CDS_IN_EMBL_ENTRY 179 ** 30-MAR-2000 (Rel. 63, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **CP 65699; Chromosome; 2011349; -1065; ATG; ; AL157959.1. **EV EI1; EMBL; -; CAB85280.1; 21-AUG-2000. **EV EP2; TREMBL; -; CAB85280.1; 21-AUG-2000. **EV EP3; RefFix; -; -; 20-SEP-2000. **EV EP4; GenFix; -; v1.2; 20-SEP-2000. **EV EP5; ProtChange; -; addKW; 01-MAY-2001. **ID XXXX_NEIME SQ SEQUENCE 355 AA; 38056 MW; DD93836BB897C401 CRC64; MGGKTFMLMA GGTGGHIFPA LAVADSLRAR GHHVIWLGSK DSMEERIVPQ YDILLETLAI KGVRGNGIKR KLMLPFTLYQ TVREAQQIIR KHRVECVIGF GGFVTFPGGL AAKLLGVPIV IHEQNAVAGL SNRHLSRWAK RVLYAFPKAF SHEGGLVGNP VRADISNLPV PAERFQGREG RLKILVVGGS LGADVLNKTV PQALALLPDN ARPQMYHQSG RGKLGSLQAD YDALGVQAEC VEFITDMVSA YRDADLVICR AGALTIAELT AAGLGALLVP YPHAVDDHQT ANARFMVQAE AGLLLPQTQL TAEKLAEILG GLNREKCLKW AENARTLALP HSADDVAEAA IACAA // ID ALYS_MYCPH STANDARD; PRT; 17 AA. AC P81528; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Autolysin (EC 3.5.1.28) (N-acetylmuramoyl-L-alanine amidase) DE (Peptidoglycan hydrolase) (Fragment). GN LYTA. OS Mycobacterium phlei. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1771; RN [1] RP SEQUENCE. RC STRAIN=425; RX MEDLINE=99140149; PubMed=10206696; RA Li Z.S., Beveridge T.J., Betts J., Clarke A.J.; RT "Partial characterization of a major autolysin from Mycobacterium RT phlei."; RL Microbiology 145:169-176(1999). CC -!- CATALYTIC ACTIVITY: HYDROLYZES THE LINK BETWEEN N-ACETYLMURAMOYL CC RESIDUES AND L-AMINO ACID RESIDUES IN CERTAIN BACTERIAL CELL-WALL CC GLYCOPEPTIDES. CC -!- MISCELLANEOUS: THE OPTIMUM PH OF THIS ENZYME IS 7.5. KW Hydrolase; Cell wall. FT VARIANT 1 1 V -> I OR L. FT VARIANT 2 2 A -> G. FT VARIANT 14 14 I -> L. FT NON_TER 1 1 FT NON_TER 17 17 ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 17 AA; 1817 MW; 1FACA3240F5C4EC5 CRC64; VAVKATTTEE ETEIPAK // ID GAG_HV1MN STANDARD; PRT; 506 AA. AC P05888; DT 01-NOV-1988 (Rel. 09, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE GAG POLYPROTEIN [Contains: CORE PROTEINS P17, P24, P2, P7, P1, P6]. GN GAG. OS Human immunodeficiency virus type 1 (MN isolate) (HIV-1). OC Viruses; Retroid viruses; Retroviridae; Lentivirus. OX NCBI_TaxID=11696; RN [1] RP SEQUENCE, AND POST-TRANSLATIONAL MODIFICATIONS. RX MEDLINE=92194415; PubMed=1548743; RA Henderson L.E., Bowers M.A., Sowder R.C. II, Serabyn S.A., RA Johnson D.G., Bess J.W. Jr., Arthur L.O., Bryant D.K., Fenselau C.; RT "Gag proteins of the highly replicative MN strain of human RT immunodeficiency virus type 1: posttranslational modifications, RT proteolytic processings, and complete amino acid sequences."; RL J. Virol. 66:1856-1865(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88219542; PubMed=3369091; RA Gurgo C., Guo H.-G., Franchini G., Aldovini A., Collalti E., RA Farrell K., Wong-Staal F., Gallo R.C., Reitz M.S. Jr.; RT "Envelope sequences of two new United States HIV-1 isolates."; RL Virology 164:531-536(1988). RN [3] RP STRUCTURE BY NMR OF 380-434. RX MEDLINE=93278285; PubMed=1304355; RA Summers M.F., Henderson L.E., Chance M.R., Bess J.W. Jr., South T.L., RA Blake P.R., Sagi I., Perez-Alvarado G., Sowder R.C. III, Hare D.R., RA Arthur L.O.; RT "Nucleocapsid zinc fingers detected in retroviruses: EXAFS studies of RT intact viruses and the solution-state structure of the nucleocapsid RT protein from HIV-1."; RL Protein Sci. 1:563-574(1992). CC -!- FUNCTION: PERFORMS HIGHLY COMPLEX ORCHESTRATED TASKS DURING THE CC ASSEMBLY, BUDDING, MATURATION, AND INFECTION STAGES OF THE VIRAL CC REPLICATION CYCLE. DURING VIRAL ASSEMBLY, THE PROTEINS FORM CC MEMBRANE ASSOCIATIONS AND SELF-ASSOCIATIONS THAT ULTIMATELY RESULT CC IN BUDDING OF AN IMMATURE VIRION FROM THE INFECTED CELL. GAG CC PRECURSORS ALSO FUNCTION DURING VIRAL ASSEMBLY TO SELECTIVELY BIND CC AND PACKAGE TWO PLUS STRANDS OF GENOMIC RNA. CC -!- PTM: THE P24 PROTEIN IS PHOSPHORYLATED. CC -!- MISCELLANEOUS: THE MN ISOLATE WAS TAKEN FROM A PEDIATRIC AIDS CC PATIENT IN 1984. CC -------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License. CC -------------------------------------------------------------------------- DR EMBL; M17449; AAA44853.1; -. DR PIR; A38068; A38068. DR PDB; 1AAF; 31-JAN-94. DR HIV; M17449; GAG$MN. DR InterPro; IPR000721; Gag_p24. DR InterPro; IPR000071; Retroviral_gag_p17. DR InterPro; IPR001878; Znf_CCHC. DR Pfam; PF00540; gag_p17; 1. DR Pfam; PF00607; gag_p24; 1. DR Pfam; PF00098; zf-CCHC; 2. DR PRINTS; PR00234; HIV1MATRIX. DR PRINTS; PR00939; C2HCZNFINGER. DR SMART; SM00343; ZnF_C2HC; 2. KW AIDS; Core protein; Polyprotein; Myristate; Phosphorylation; KW Zinc-finger; 3D-structure. FT INIT_MET 0 0 FT CHAIN 1 134 CORE PROTEIN P17 (MATRIX ANTIGEN). FT CHAIN 135 365 CORE PROTEIN P24 (CORE ANTIGEN). FT CHAIN 366 379 CORE PROTEIN P2. FT CHAIN 380 434 CORE PROTEIN P7 (NUCLEOCAPSID PROTEIN). FT CHAIN 435 450 CORE PROTEIN P1. FT CHAIN 451 506 CORE PROTEIN P6. FT ZN_FING 394 407 C2HC-TYPE. FT LIPID 1 1 MYRISTATE. FT VARIANT 34 34 V -> I. FT VARIANT 45 45 I -> V. FT VARIANT 74 74 R -> L OR S OR N. FT VARIANT 92 92 K -> E. FT CONFLICT 17 17 K -> N (IN REF. 2). FT CONFLICT 141 141 Q -> E (IN REF. 2). FT CONFLICT 220 220 A -> V (IN REF. 2). FT CONFLICT 226 226 A -> T (IN REF. 2). FT CONFLICT 318 319 WM -> RT (IN REF. 2). FT CONFLICT 447 448 PG -> R (IN REF. 2). SQ SEQUENCE 506 AA; 56630 MW; AC6F3CEB691C4726 CRC64; GARASVLSGG ELDRWEKIRL RPGGKKKYKL KHVVWASREL ERFAINPGLL ETSEGCRQIL GQLQPSLQTG SEERKSLYNT VATLYCVHQK IKIKDTKEAL EKIEEEQNKS KKKAQQAAAD TGNRGNSSQV SQNYPIVQNI QGQMVHQAIS PRTLNAWVKV VEEKAFSPEV IPMFSALSEG ATPQDLNTML NTVGGHQAAM QMLKETINEE AAEWDRLHPA HAGPIAPGQM REPRGSDIAG TTSTLQEQIG WMTNNPPIPV GEIYKRWIIL GLNKIVRMYS PSSILDIRQG PKEPFRDYVD RFYKTLRAEQ ASQEVKNWMT ETLLVQNANP DCKTILKALG PAATLEEMMT ACQGVGGPGH KARVLAEAMS QVTNSATIMM QRGNFRNQRK IIKCFNCGKE GHIAKNCRAP RKRGCWKCGK EGHQMKDCTE RQANFLGKIW PSCKGRPGNF PQSRTEPTAP PEESFRFGEE TTTPYQKQEK KQETIDKDLY PLASLKSLFG NDPLSQ // ID LDLR_HUMAN STANDARD; PRT; 860 AA. AC P01130; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE Low-density lipoprotein receptor precursor (LDL receptor). GN LDLR. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; FT VARIANT 667 667 C -> Y (IN FRENCH CANADIAN-2; 5% OF FT FRENCH CANADIANS). FT /FTId=VAR_005407. FT VARIANT 685 685 P -> L (IN GUJERAT/ZAMBIA/BELGIAN/DUTCH/ FT SWEDEN/JAPAN). ** ** ################# INTERNAL SECTION ################## **CL 19p13.3; SQ SEQUENCE 860 AA; 95376 MW; A4C28E9B8BADAD5E CRC64; MGPWGWKLRW TVALLLAAAG TAVGDRCERN EFQCQDGKCI SYKWVCDGSA ECQDGSDESQ ETCLSVTCKS GDFSCGGRVN RCIPQFWRCD GQVDCDNGSD EQGCPPKTCS QDEFRCHDGK CISRQFVCDS DRDCLDGSDE ASCPVLTCGP ASFQCNSSTC IPQLWACDND PDCEDGSDEW PQRCRGLYVF QGDSSPCSAF EFHCLSGECI HSSWRCDGGP DCKDKSDEEN CAVATCRPDE FQCSDGNCIH GSRQCDREYD CKDMSDEVGC VNVTLCEGPN KFKCHSGECI TLDKVCNMAR DCRDWSDEPI KECGTNECLD NNGGCSHVCN DLKIGYECLC PDGFQLVAQR RCEDIDECQD PDTCSQLCVN LEGGYKCQCE EGFQLDPHTK ACKAVGSIAY LFFTNRHEVR KMTLDRSEYT SLIPNLRNVV ALDTEVASNR IYWSDLSQRM ICSTQLDRAH GVSSYDTVIS RDIQAPDGLA VDWIHSNIYW TDSVLGTVSV ADTKGVKRKT LFRENGSKPR AIVVDPVHGF MYWTDWGTPA KIKKGGLNGV DIYSLVTENI QWPNGITLDL LSGRLYWVDS KLHSISSIDV NGGNRKTILE DEKRLAHPFS LAVFEDKVFW TDIINEAIFS ANRLTGSDVN LLAENLLSPE DMVLFHNLTQ PRGVNWCERT TLSNGGCQYL CLPAPQINPH SPKFTCACPD GMLLARDMRS CLTEAEAAVA TQETSTVRLK VSSTAVRTQH TTTRPVPDTS RLPGATPGLT TVEIVTMSHQ ALGDVAGRGN EKKPSSVRAL SIVLPIVLLV FLCLGVFLLW KNWRLKNINS INFDNPVYQK TTEDEVHICH NQDGYSYPSR QMVSLEDDVA // ID H13_RABIT STANDARD; PRT; 213 AA. AC P02251; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Histone H1.3. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE. RA Hsiang M., Largman C.R., Cole R.D.; ** /NO TITLE. RL Unpublished results, cited by: RL Cole R.D.; RL (In) Ts'o P.O.P. (eds.); RL The molecular biology of the mammalian genetic apparatus, pp.1:93-104, RL Elsevier, Amsterdam (1977). RN [2] RP SEQUENCE OF 1-72. RX MEDLINE=72068710; PubMed=5167020; RA Rall S.C., Cole R.D.; RT "Amino acid sequence and sequence variability of the amino-terminal RT regions of lysine-rich histones."; RL J. Biol. Chem. 246:7175-7190(1971). RN [3] RP SEQUENCE OF 73-107. RX MEDLINE=74143498; PubMed=4822503; RA Jones G.M.T., Rall S.C., Cole R.D.; RT "Extension of the amino acid sequence of a lysine-rich histone."; RL J. Biol. Chem. 249:2548-2553(1974). CC -!- FUNCTION: HISTONES H1 ARE NECESSARY FOR THE CONDENSATION OF CC NUCLEOSOME CHAINS INTO HIGHER ORDER STRUCTURES. CC -!- SUBCELLULAR LOCATION: NUCLEAR. CC -!- SIMILARITY: BELONGS TO THE HISTONE H1/H5 FAMILY. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=1; CC Comment=This is just a test; CC Name=VI; CC IsoId=P02251-1; Sequence=Displayed; DR PIR; A02578; HSRB13. DR HSSP; P08287; 1GHC. DR InterPro; IPR001386; Linker_histone. DR Pfam; PF00538; linker_histone; 1. DR SMART; SM00526; H15; 1. KW Chromosomal protein; Nuclear protein; DNA-binding; Multigene family; KW Acetylation. FT DOMAIN 37 110 GLOBULAR. FT MOD_RES 1 1 ACETYLATION. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 213 AA; 21423 MW; 21DE34BBD10D894E CRC64; SEAPAETAAP APAEKSPAKK KKAAKKPGAG AAKRKAAGPP VSELITKAVA ASKERNGLSL AALKKALAAG GYDVEKNNSR IKLGLKSLVS KGTLVETKGT GASGSFKLDK KAASGEAKPK PKKAGAAKPK KPAGATPKKP KKAAGAKKAV KKTPKKAPKP KAAAKPKVAK PKSPAKVAKS PKKAKAVKPK AAKPKAPKPK AAKAKKTAAK KKK // ID ANGT_HUMAN STANDARD; PRT; 485 AA. AC P01019; Q16358; Q16359; Q96F91; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Angiotensinogen precursor [Contains: Angiotensin I (Ang I); DE Angiotensin II (Ang II); Angiotensin III (Ang III) (Des-Asp[1]- DE angiotensin II)]. GN AGT OR SERPINA8. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89170129; PubMed=2924688; RA Gaillard I., Clauser E., Corvol P.; RT "Structure of human angiotensinogen gene."; RL DNA 8:87-99(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=85000455; PubMed=6089875; RA Kageyama R., Ohkubo H., Nakanishi S.; RT "Primary structure of human preangiotensinogen deduced from the cloned RT cDNA sequence."; RL Biochemistry 23:3603-3609(1984). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=90237063; PubMed=1692023; RA Fukamizu A., Takahashi S., Seo M.S., Tada M., Tanimoto K., Uehara S., RA Murakami K.; RT "Structure and expression of the human angiotensinogen gene. RT Identification of a unique and highly active promoter."; RL J. Biol. Chem. 265:7576-7582(1990). RN [4] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RA Strausberg R.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 1-338 FROM N.A. RX MEDLINE=87244745; PubMed=2885106; RA Kunapuli S.P., Kumar A.; RT "Molecular cloning of human angiotensinogen cDNA and evidence for the RT presence of its mRNA in rat heart."; RL Circ. Res. 60:786-790(1987). RN [6] RP SEQUENCE OF 34-45, AND SUBUNITS. RC TISSUE=Serum; RX MEDLINE=95293954; PubMed=7539791; RA Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., RA Stigbrand T., Gleich G.J., Sottrup-Jensen L.; RT "Identification of angiotensinogen and complement C3dg as novel RT proteins binding the proform of eosinophil major basic protein in RT human pregnancy serum and plasma."; RL J. Biol. Chem. 270:13645-13651(1995). RN [7] RP SEQUENCE OF 34-43. RX MEDLINE=69014170; PubMed=4300938; RA Arakawa K., Minohara A., Yamada J., Nakamura M.; RT "Enzymatic degradation and electrophoresis of human angiotensin I."; RL Biochim. Biophys. Acta 168:106-112(1968). RN [8] RP CARBOHYDRATE-LINKAGE SITES. RX MEDLINE=86056581; PubMed=3934016; RA Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P.; RT "Processing of rat and human angiotensinogen precursors by microsomal RT membranes."; RL Mol. Cell. Endocrinol. 43:31-40(1985). RN [9] RP FUNCTION OF ANGIOTENSIN III. RX MEDLINE=75166949; PubMed=1132082; RA Goodfriend T.L., Peach M.J.; RT "Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and RT speculation for its role as an important agonist in the renin - RT angiotensin system."; RL Circ. Res. 36:38-48(1975). RN [10] RP STRUCTURE BY NMR OF ANGIOTENSIN II. RX MEDLINE=98151281; PubMed=9492317; RA Carpenter K.A., Wilkes B.C., Schiller P.W.; RT "The octapeptide angiotensin II adopts a well-defined structure in a RT phospholipid environment."; RL Eur. J. Biochem. 251:448-453(1998). RN [11] RP VARIANTS MET-207; THR-268 AND CYS-281. RX MEDLINE=93008239; PubMed=1394429; RA Jeunemaitre X., Soubrier F., Kotelevtsev Y.V., Lifton R.P., RA Williams C.S., Charru A., Hunt S.C., Hopkins P.N., Williams R.R., RA Lalouel J.-M., Corvol P.; RT "Molecular basis of human hypertension: role of angiotensinogen."; RL Cell 71:169-180(1992). RN [12] RP VARIANT THR-268. RX MEDLINE=93291876; PubMed=8513325; RA Ward K., Hata A., Jeunemaitre X., Helin C., Nelson L., Namikawa C., RA Farrington P.F., Ogasawara M., Suzumori K., Tomoda S., Berrebi S., RA Sasaki M., Corvol P., Lifton R.P., Lalouel J.-M.; RT "A molecular variant of angiotensinogen associated with RT preeclampsia."; RL Nat. Genet. 4:59-61(1993). RN [13] RP VARIANTS ILE-242; ARG-244 AND CYS-281. RX MEDLINE=95331754; PubMed=7607642; RA Hixson J.E., Powers P.K.; RT "Detection and characterization of new mutations in the human RT angiotensinogen gene (AGT)."; RL Hum. Genet. 96:110-112(1995). RN [14] RP CHARACTERIZATION OF VARIANT CYS-281. RX MEDLINE=96199253; PubMed=8621667; RA Gimenez-Roqueplo A.P., Leconte I., Cohen P., Simon D., Guyene T.T., RA Celerier J., Pau B., Corvol P., Clauser E., Jeunemaitre X.; RT "The natural mutation Y248C of human angiotensinogen leads to abnormal RT glycosylation and altered immunological recognition of the protein."; RL J. Biol. Chem. 271:9838-9844(1996). CC -!- FUNCTION: IN RESPONSE TO LOWERED BLOOD PRESSURE, THE ENZYME RENIN CC CLEAVES ANGIOTENSIN I, FROM ANGIOTENSINOGEN. ACE (ANGIOTENSIN CC CONVERTING ENZYME) THEN REMOVES A DIPEPTIDE TO YIELD THE CC PHYSIOLOGICALLY ACTIVE PEPTIDE ANGIOTENSIN II, THE MOST POTENT CC PRESSOR SUBSTANCE KNOWN, WHICH HELPS REGULATE VOLUME AND MINERAL CC BALANCE OF BODY FLUIDS. CC -!- FUNCTION: Angiotensin III stimulates aldosterone release. CC -!- SUBUNIT: During pregnancy, exists as a disulfide-linked 2:2 CC heterotetramer with the proform of PRG2 and as a complex (probably CC a 2:2:2 heterohexamer) with pro-PRG2 and C3dg. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Synthesized by the liver and secreted in the CC plasma. CC -!- DISEASE: AGT SEEMS TO BE ASSOCIATED WITH A PREDISPOSITION TO CC ESSENTIAL HYPERTENSION AS WELL AS PREGNANCY-INDUCED HYPERTENSION CC (PIH) (PREECLAMPSIA). CC -!- SIMILARITY: BELONGS TO THE SERPIN FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-10 IS THE INITIATOR. DR EMBL; K02215; AAA51731.1; -. DR EMBL; M24689; AAA51679.1; -. DR EMBL; M24686; AAA51679.1; JOINED. DR EMBL; M24687; AAA51679.1; JOINED. DR EMBL; M24688; AAA51679.1; JOINED. DR EMBL; X15324; CAA33385.1; -. DR EMBL; X15325; CAA33385.1; JOINED. DR EMBL; X15326; CAA33385.1; JOINED. DR EMBL; X15327; CAA33385.1; JOINED. DR EMBL; M69110; AAA52282.1; -. DR EMBL; BC011519; AAH11519.1; -. DR EMBL; S78529; AAD14287.1; -. DR EMBL; S78530; AAD14288.1; -. DR PIR; A01249; ANHU. DR PIR; A31362; A31362. DR PIR; A35203; A35203. DR SWISS-2DPAGE; P01019; HUMAN. DR HGNC; HGNC:333; AGT. DR MIM; 106150; -. DR GO; GO:0005625; C:soluble fraction; TAS. DR GO; GO:0004867; F:serine protease inhibitor activity; TAS. DR GO; GO:0007166; P:cell surface receptor linked signal transdu...; TAS. DR GO; GO:0007267; P:cell-cell signaling; TAS. DR GO; GO:0007565; P:pregnancy; TAS. DR GO; GO:0008217; P:regulation of blood pressure; TAS. DR InterPro; IPR000227; Angiotensngn. DR InterPro; IPR000215; Serpin. DR Pfam; PF00079; serpin; 1. DR PRINTS; PR00654; ANGIOTENSNGN. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. KW Vasoconstrictor; Glycoprotein; Plasma; Serpin; Signal; KW Disease mutation; Polymorphism. FT SIGNAL 1 33 FT CHAIN 34 485 ANGIOTENSINOGEN. FT PEPTIDE 34 43 ANGIOTENSIN I. FT PEPTIDE 34 41 ANGIOTENSIN II. FT PEPTIDE 35 41 ANGIOTENSIN III. FT CARBOHYD 47 47 N-LINKED (GLCNAC...). FT CARBOHYD 170 170 N-LINKED (GLCNAC...). FT CARBOHYD 304 304 N-LINKED (GLCNAC...). FT CARBOHYD 328 328 N-LINKED (GLCNAC...). FT VARIANT 207 207 T -> M (IN dbSNP:4762). FT /FTId=VAR_007093. FT VARIANT 242 242 T -> I (IN HYPERTENSION). FT /FTId=VAR_007094. FT VARIANT 244 244 L -> R (IN HYPERTENSION). FT /FTId=VAR_007095. FT VARIANT 268 268 M -> T (IN HYPERTENSION; dbSNP:699). FT /FTId=VAR_007096. FT VARIANT 281 281 Y -> C (IN HYPERTENSION; ALTERS THE FT STRUCTURE, GLYCOSYLATION AND SECRETION OF FT ANGIOTENSINOGEN). FT /FTId=VAR_007097. FT VARIANT 392 392 L -> M (IN dbSNP:1805090). FT /FTId=VAR_014573. FT CONFLICT 333 333 Q -> E (IN REF. 1). FT CONFLICT 335 335 P -> S (IN REF. 4). ** ** ################# INTERNAL SECTION ################## **CL 1q42-q43; SQ SEQUENCE 485 AA; 53154 MW; 5026C2DFB2DD236E CRC64; MRKRAPQSEM APAGVSLRAT ILCLLAWAGL AAGDRVYIHP FHLVIHNEST CEQLAKANAG KPKDPTFIPA PIQAKTSPVD EKALQDQLVL VAAKLDTEDK LRAAMVGMLA NFLGFRIYGM HSELWGVVHG ATVLSPTAVF GTLASLYLGA LDHTADRLQA ILGVPWKDKN CTSRLDAHKV LSALQAVQGL LVAQGRADSQ AQLLLSTVVG VFTAPGLHLK QPFVQGLALY TPVVLPRSLD FTELDVAAEK IDRFMQAVTG WKTGCSLMGA SVDSTLAFNT YVHFQGKMKG FSLLAEPQEF WVDNSTSVSV PMLSGMGTFQ HWSDIQDNFS VTQVPFTESA CLLLIQPHYA SDLDKVEGLT FQQNSLNWMK KLSPRTIHLT MPQLVLQGSY DLQDLLAQAE LPAILHTELN LQKLSNDRIR VGEVLNSIFF ELEADEREPT ESTQQLNKPE VLEVTLNRPF LFAVYDQSAT ALHFLGRVAN PLSTA // ID NRTC_SYNY3 STANDARD; PRT; 670 AA. AC P73450; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Nitrate transport ATP-binding protein nrtC. GN NRTC OR SLL1452. OS Synechocystis sp. (strain PCC 6803). OC Bacteria; Cyanobacteria; Chroococcales; Synechocystis. OX NCBI_TaxID=1148; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97061201; PubMed=8905231; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., RA Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the RT entire genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: PROBABLY PART OF A HIGH-AFFINITY BINDING-PROTEIN- CC DEPENDENT TRANSPORT SYSTEM FOR NITRATE. PROBABLY RESPONSIBLE FOR CC ENERGY COUPLING TO THE TRANSPORT SYSTEM. CC -!- SUBCELLULAR LOCATION: Membrane-associated (Potential). CC -!- SIMILARITY: BELONGS TO THE ABC TRANSPORTER FAMILY. CC -!- SIMILARITY: SOME, IN THE C-TERMINAL DOMAIN TO NRTA. DR EMBL; D90906; BAA17490.1; -. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transporter. DR InterPro; IPR005890; NtrCD. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR01184; ntrCD; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. KW Transport; ATP-binding; Membrane; Nitrate assimilation; KW Complete proteome. FT DOMAIN 1 254 ABC TRANSPORTER. FT DOMAIN 240 250 INTERNAL. FT DOMAIN 255 278 LINKER. FT DOMAIN 279 670 NTRA-LIKE. FT NP_BIND 42 49 ATP (POTENTIAL). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 670 AA; 75101 MW; 03B47E6C7918AD14 CRC64; MMPFIEIDHV DRIFPLPDGG RYIALKNIEL KISQGEFISL IGHSGCGKST LLNMISGLDK PTFGGVIMEG KEITEPGPER MVVFQNYSLL PWLTVRQNIA LAVNRVLRDL PKPEQEKIID DNIALVGLQR AAHKRPGELS GGMKQRVAIA RALSTRPKVL LLDEPFGALD ALTRGNLQER LMEIVQESGV TCIMVTHDVD EALLLSDRVV MLTTGPEAHI GQILEVPIPR PRHRLEVVNH PSYYALRGEM VYFLNQQKRA KKVGAVSQFA EAMGGNGLEK INLDLGFIPL TDCAPLVVAK EKGFFQKHGL EQVNLVKEPS WQAIADGIRE RRLDGAQMVA GMPLALTLGM GGKTPLPMVT AMVMSRNGNA ITLSKKFAEA GVKTLEDLRL KLAETPDQVS TLGMVHPASM QNLLLRYWLA SGSIDPDQDI NLMRLPPPQM VSNLEAGNID GFCVGEPWNS YAVKQNLGYV IATDLDIWNG HPEKVLGMRE EWVNKYPATH LALVKALLEA CEYCDDRRHR QEILDYLALP QYVGTSTEYI SPGFLTEYDQ GNDAEAEMLL DFNQFYVKQS NYPSRSEGLW ILTQLARWGY IDFPKNWVEI IERVRRPDLF GEACRHLGWP DLEGDHHNVS LFDGMVFTPN DPLGYIKRFT IHRDIQVTEI LIDQIDQVNQ // ID FAS2_PENPA STANDARD; PRT; 1857 AA. AC P15368; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: Acyl DE carrier; 3-oxoacyl-[acyl-carrier protein] reductase (EC 1.1.1.100) DE (Beta-ketoacyl reductase); 3-oxoacyl-[acyl-carrier protein] synthase DE (EC 2.3.1.41) (Beta-ketoacyl synthase)]. GN FAS2. OS Penicillium patulum (Penicillium griseofulvum). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; Penicillium. OX NCBI_TaxID=5078; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89030697; PubMed=3053172; RA Wiesner P., Beck J., Beck K.-F., Ripka S., Mueller G., Luecke S., RA Schweizer E.; RT "Isolation and sequence analysis of the fatty acid synthetase FAS2 RT gene from Penicillium patulum."; RL Eur. J. Biochem. 177:69-79(1988). CC -!- FUNCTION: FATTY ACID SYNTHETASE CATALYZES THE FORMATION OF LONG- CC CHAIN FATTY ACIDS FROM ACETYL-COA, MALONYL-COA AND NADPH. THE CC ALPHA SUBUNIT CONTAINS DOMAINS FOR: ACYL CARRIER PROTEIN, 3- CC OXOACYL-[ACYL-CARRIER PROTEIN] REDUCTASE, AND 3-OXOACYL-[ACYL- CC CARRIER-PROTEIN] SYNTHASE. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + N malonyl-CoA + 2N NADPH = a CC long-chain acyl-CoA + N CoA + N CO(2) + 2N NADP(+). CC -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier protein] + malonyl-[acyl- CC carrier protein] = 3-oxoacyl-[acyl-carrier protein] + CO(2) + CC [acyl-carrier protein]. CC -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier protein] + CC NADP(+) = 3-oxoacyl-[acyl-carrier protein] + NADPH. CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional CC subunits (alpha and beta). CC -!- SIMILARITY: TO THE FATTY ACID SYNTHETASE, SUBUNIT ALPHA FROM OTHER CC FUNGI. DR EMBL; M37461; AAA33695.1; -. DR PIR; S01787; S01787. DR InterPro; IPR000794; Ketoacyl-synt. DR InterPro; IPR004568; Pantethn_trn. DR InterPro; IPR006162; Ppantne_attach. DR Pfam; PF01648; ACPS; 1. DR Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; ketoacyl-synt_C; 1. DR ProDom; PD004282; ACPS; 1. DR TIGRFAMs; TIGR00556; pantethn_trn; 1. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1. KW Fatty acid biosynthesis; Multifunctional enzyme; Oxidoreductase; KW Transferase; NADP; Phosphopantetheine. FT DOMAIN 1 ? ACYL CARRIER (ACP). FT DOMAIN 648 845 BETA-KETOACYL REDUCTASE. FT DOMAIN ? 1857 BETA-KETOACYL SYNTHASE. FT ACT_SITE 1275 1275 BETA-KETOACYL SYNTHASE (BY SIMILARITY). FT BINDING 174 174 PHOSPHOPANTETHEINE (BY SIMILARITY). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 1857 AA; 204466 MW; 34BAFD547D93FEE6 CRC64; MRPEVEQELA HTLLVELLAY QFASPVRWIE TQDVILAEQR TERIVEIGPA DTLGGMARRT LASKYEAYDA ATSVQRQILC YNKDAKEIYY DVDPVEEEPE ATEPAPSATP AAPAAAPAAG APPPPPSAGP AASVEDIPVT AVDILRTLVA QKLKKSLADV PLSKAIKDLV GGKSTLQNEI LGDLGKEFGS TPEKPEDVPL DELGASMQAT FNGQLGKQSS SLIARMVSSK MPGGFNITSV RKYLETRWGL GSGRQDGVLL LALTMEPAAR LGSEVDAKAY LDDVTNKYAA SAGVNLSAPV AGGDSGGAGG GMVMDPAAID ALTKDQRALF KQQLEIIARY LKMDLRGGEK AHVISQETQK ALQAQLDLWQ AEHGDFYASG IEPSFDQLKA RVYDSSWNWA RQDALSMYYD IIFGRLQVVD REIVSQCIRI MNRSNPLLLD FMQYHIDNCP TERGETYQLA KELGQQLIEN CREVLEVAPV YKDVAVPTGP QTTIDARGNI SYKETPRTSA RKLEHYVKHM AEGGPISEYS NRTKVQNDLK SVYKLIRKQH RLSKSSQLQF DALYKDVVHA LGMNESQIIP QENGHSKKGG RSAAKRNTPT RPGKVETIPF LHLKKKTEHG WDYNKKLTGI YLNVTESAAK DGLSFQGKNV LMTGAGAGSI GAEVLQGLIS GGAQVIVTTS RFSREVTEYY QAMYARYGAR GSQLVVVPFN QGSKQDVEAL VEYIYDTKKG LGWDLDFVVP FAAIPENGRE IDSIDSKSEL AHRIMLTNLL RLLGSVKTQK QAHGFETRPA QVILPLSPNH GTFGNDGLYS ESKLALETLF NRWYSENWGH YLTICGAVIG WTRGTGLMSG NNMVAEGVEK LGVRTFSQQE MAFNLLGLMS PAIVNLCQLD PVFADLNGGL QFIPDLKGLM TKLRTDIMET SDVRQAVMKE TAIEHNIVNG EDSGVLYKKV IAEPRANIKF EFPNLPDWEK EVKPLNENLK GMVNLDKVVV VTGFSEVGPW GNSRTRWEME SKGKFSLEGC VEMAWIMGLI KHHNGPLKGQ AYSGWVDAKT GEPVDDKDVK PKYEKHILEH TGIRLIEPEL FKGYDPKKKQ LLQEIVIQED LEPFEASKET AEEFKREHGD KVEIFEIPES GEYTVRLCKG ATMLIPKALQ FDRLVAGQVP TGWDASRYGI PDDIISQVDP VTLFVLVCTA EAMLSAGVTD PYEFYKYVHL SEVGNCIGSG IGGTHRLRGM YKDRFLDKPL QKDILQESFI NTMSAWVNML LLSSTGPIKT PVGCCATAVE SVDIGYETIV EGKARVCFVG GFDDFQEEGS YEFANMKATS NAEDEFAHGR TPQEMSRPTT TTRAGFMESQ GCGMQLIMTA QLALDMGVPI HGIIALTTTA TDKIGRSVRS VPAPGQGVLT TARENPGKFP SPLLDIKYRR RQLDLRKKQI NEWQEAELLY LQEEAEAMKA QSDETFNEAE YMQERAQHIE REAIRQEKDA QYSLGNNFWK QDSRIAPLRG AMATWGLTVD DIDVASFHGT STVANDKNES DVICQQMKHL GRSKGNAVMG IFQKYLTGHP KGAAGAWMFN GCLQVLDSGL VPGNRNADNV DKVMEKFDYI VYPSRSIQTD GVKAFSVTSF GFGQKGAQVI GIHPKYLYAT LDQAQYEAYK TKVEARQKKA YRYFHNGLIN NSIFVAKSKA PYEDEQQSKV FLNPDYRVSV DKKTSELKFS TTAPEAKQSE STRQTLESLA KANATENSKI GVDVEHIDSV NIENETFVER NFTQSEQDYC RKAASPQSSF AGRWSAKEAV FKSLGVSSKG AGAALKDIEI GVDANGAPVV NLHGAAAAAA KQAGVKQVSV SISHSDSQAV AVAVSQF // ID UKA1_HUMAN STANDARD; PRT; 19 AA. AC P31940; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Unknown protein from 2D-page of epidermal keratinocytes (Spot 1118) DE (Fragments). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE. RC TISSUE=Keratinocytes; RX MEDLINE=93162043; PubMed=1286667; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 7.24, ITS MW IS: 23.5 kDa. DR Aarhus/Ghent-2DPAGE; 1118; IEF. FT UNSURE 6 6 FT UNSURE 17 17 FT NON_CONS 6 7 FT NON_CONS 12 13 FT NON_TER 1 1 FT NON_TER 19 19 ** ** ################# INTERNAL SECTION ################## **CL ?; SQ SEQUENCE 19 AA; 2087 MW; EF7515F79D50DE12 CRC64; HIGLVRLTPT EVQEPIITA // ID A4_MOUSE STANDARD; PRT; 770 AA. AC P12023; DT 01-OCT-1989 (Rel. 12, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Alzheimer's disease amyloid A4 protein homolog precursor DE (Amyloidogenic glycoprotein) (AG). GN APP. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE OF 1-289 AND 365-770 FROM N.A. RC STRAIN=BALB/c; TISSUE=Brain; RX MEDLINE=92096458; PubMed=1756177; RA de Strooper B., van Leuven F., van den Berghe H.; RT "The amyloid beta protein precursor or proteinase nexin II from mouse RT is closer related to its human homolog than previously reported."; RL Biochim. Biophys. Acta 1129:141-143(1991). RN [2] RP SEQUENCE OF 1-289 AND 365-770 FROM N.A. RC TISSUE=Brain; RX MEDLINE=88106489; PubMed=3322280; RA Yamada T., Sasaki H., Furuya H., Miyata T., Goto I., Sakaki Y.; RT "Complementary DNA for the mouse homolog of the human amyloid beta RT protein precursor."; RL Biochem. Biophys. Res. Commun. 149:665-671(1987). RN [3] RP REVISIONS. RA Yamada T.; RL Submitted (MAR-1988) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE OF 289-364 FROM N.A. RC STRAIN=CD-1; TISSUE=Placenta; RX MEDLINE=89345111; PubMed=2569710; RA Fukuchi K., Martin G.M., Deeb S.S.; RT "Sequence of the protease inhibitor domain of the A4 amyloid protein RT precursor of Mus domesticus."; RL Nucleic Acids Res. 17:5396-5396(1989). RN [5] RP SEQUENCE OF 1-19 FROM N.A. RX MEDLINE=92209998; PubMed=1555768; RA Izumi R., Yamada T., Yoshikai S.I., Sasaki H., Hattori M., Sakai Y.; RT "Positive and negative regulatory elements for the expression of the RT Alzheimer's disease amyloid precursor-encoding gene in mouse."; RL Gene 112:189-195(1992). RN [6] RP SEQUENCE OF 281-380 FROM N.A., AND ALTERNATIVE SPLICING. RC TISSUE=Brain, and Kidney; RX MEDLINE=89149813; PubMed=2493250; RA Yamada T., Sasaki H., Dohura K., Goto I., Sakaki Y.; RT "Structure and expression of the alternatively-spliced forms of mRNA RT for the mouse homolog of Alzheimer's disease amyloid beta protein RT precursor."; RL Biochem. Biophys. Res. Commun. 158:906-912(1989). RN [7] RP PHOSPHORYLATION. RX MEDLINE=22028091; PubMed=11912189; RA Taru H., Iijima K.-I., Hase M., Kirino Y., Yagi Y., Suzuki T.; RT "Interaction of Alzheimer's beta-amyloid precursor family proteins RT with scaffold proteins of the JNK signaling cascade."; RL J. Biol. Chem. 277:20070-20078(2002). CC -!- SUBCELLULAR LOCATION: Type I membrane protein. Mature, CC phosphorylated APP is largely located on the plasma membrane of CC cell bodies and the growth cones of neurites of mature neurons (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=APP(770); CC IsoId=P12023-1; Sequence=Displayed; CC Name=APP(395); CC IsoId=P12023-4; Sequence=Not described; CC Name=APP(563); CC IsoId=P12023-5; Sequence=Not described; CC Name=APP(695); CC IsoId=P12023-2; Sequence=VSP_000012, VSP_000013; CC Name=APP(751); CC IsoId=P12023-3; Sequence=VSP_000014; CC -!- TISSUE SPECIFICITY: Isoform APP(770) is expressed in kidney. CC Isoform APP(751) is widely expressed. Isoform APP(695) is CC expressed in brain, kidney and liver. CC -!- DOMAIN: The clathrin-binding site is essential for its association CC with X11-alpha, -beta, and -gamma. The sequence specific CC recognition extends to peptide residues that are C-terminal to the CC NPXY motif. This interaction appears to be independent of CC phosphorylation. Binds to Jip1 which may result in the CC phosphorylation of App by members of the JNK-signaling cascade. CC Cytoplasmic domain binds Apbb1, phosphorylation within this domain CC results in a conformational change which prevents protein binding CC (By similarity). CC -!- SIMILARITY: BELONGS TO THE APP FAMILY. CC -!- SIMILARITY: Contains 1 BPTI/Kunitz inhibitor domain. DR EMBL; X59379; -; NOT_ANNOTATED_CDS. DR EMBL; M18373; AAA37139.1; -. DR EMBL; X15210; CAA33280.1; -. DR EMBL; D10603; BAA01456.1; -. DR EMBL; M24397; AAA39929.1; -. DR PIR; A27485; A27485. DR PIR; S04855; S04855. DR PIR; S19727; S19727. DR HSSP; P05067; 1AAP. DR MGI; MGI:88059; App. DR InterPro; IPR001868; A4_APP. DR InterPro; IPR001255; Beta-APP. DR InterPro; IPR002223; Kunitz_BPTI. DR Pfam; PF02177; A4_EXTRA; 1. DR Pfam; PF03494; Beta-APP; 1. DR Pfam; PF00014; Kunitz_BPTI; 1. DR PRINTS; PR00203; AMYLOIDA4. DR PRINTS; PR00759; BASICPTASE. DR ProDom; PD000222; Kunitz_BPTI; 1. DR SMART; SM00006; A4_EXTRA; 1. DR SMART; SM00131; KU; 1. DR PROSITE; PS00319; A4_EXTRA; 1. DR PROSITE; PS00320; A4_INTRA; 1. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. KW Glycoprotein; Amyloid; Neurone; Transmembrane; Signal; KW Alternative splicing; Serine protease inhibitor; Phosphorylation. FT SIGNAL 1 17 BY SIMILARITY. FT CHAIN 18 770 ALZHEIMER'S DISEASE AMYLOID A4 PROTEIN FT HOMOLOG. FT TOPO_DOM 18 699 EXTRACELLULAR (POTENTIAL). FT TRANSMEM 700 723 POTENTIAL. FT TOPO_DOM 724 770 CYTOPLASMIC (POTENTIAL). FT DOMAIN 287 345 BPTI/KUNITZ INHIBITOR. FT DOMAIN 673 715 EQUIVALENT OF BETA-AMYLOID PROTEIN. FT SITE 759 762 CLATHRIN-BINDING (BY SIMILARITY). FT MOD_RES 743 743 PHOSPHORYLATION. FT CARBOHYD 542 542 N-LINKED (GLCNAC...) (POTENTIAL). FT CARBOHYD 571 571 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 291 341 BY SIMILARITY. FT DISULFID 300 324 BY SIMILARITY. FT DISULFID 316 337 BY SIMILARITY. FT VAR_SEQ 289 289 E -> V (in isoform APP(695)). FT /FTId=VSP_000012. FT VAR_SEQ 290 364 Missing (in isoform APP(695)). FT /FTId=VSP_000013. FT VAR_SEQ 346 380 Missing (in isoform APP(751)). FT /FTId=VSP_000014. ** ** ################# INTERNAL SECTION ################## **IS P12023-6 **ZB SAO, 16-SEP-2002; SQ SEQUENCE 770 AA; 86752 MW; 26C50DE0890CAF7A CRC64; MLPSLALLLL AAWTVRALEV PTDGNAGLLA EPQIAMFCGK LNMHMNVQNG KWESDPSGTK TCIGTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHTH IVIPYRCLVG EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR GVEFVCCPLA EESDSVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVADVEEE EADDDEDVED GDEVEEEAEE PYEEATERTT STATTTTTTT ESVEEVVREV CSEQAETGPC RAMISRWYFD VTEGKCVPFF YGGCGGNRNN FDTEEYCMAV CGSVSTQSLL KTTSEPLPQD PDKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL QAVPPRPHHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET KTTVELLPVN GEFSLDDLQP WHPFGVDSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN IKTEEISEVK MDAEFGHDSG FEVRHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN // ID WASL_RAT STANDARD; PRT; 501 AA. AC O08816; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Neural Wiskott-Aldrich syndrome protein (N-WASP). GN WASL. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97464048; PubMed=9322739; RA Fukuoka M., Miki H., Takenawa T.; RT "Identification of N-WASP homologs in human and rat brain."; RL Gene 196:43-48(1997). CC -!- FUNCTION: REGULATES ACTIN POLYMERIZATION BY STIMULATING THE ACTIN- CC NUCLEATING ACTIVITY OF THE ACTIN-RELATED PROTEIN 2/3 (ARP2/3) CC COMPLEX (BY SIMILARITY). CC -!- SUBUNIT: BINDS ACTIN AND ARP2/3 COMPLEX; INTERACTS WITH CDC42 CC BINDS TO SH3 DOMAINS OF ASH/GRB2 (BY SIMILARITY). CC -!- SIMILARITY: Contains 1 CRIB domain. CC -!- SIMILARITY: Contains 1 WH1 domain. CC -!- SIMILARITY: Contains 2 WH2 domains. DR EMBL; D88461; BAA21534.1; -. DR InterPro; IPR000697; EVH1. DR InterPro; IPR000095; PAKbox/Rhobndng. DR InterPro; IPR001960; WH1. DR InterPro; IPR003124; WH2. DR Pfam; PF00786; PBD; 1. DR Pfam; PF00568; WH1; 1. DR Pfam; PF02205; WH2; 2. ** PRINTS; PR01217; PRICHEXTENSN; FALSE_POS_1. DR SMART; SM00285; PBD; 1. DR SMART; SM00461; WH1; 1. DR SMART; SM00246; WH2; 2. DR PROSITE; PS50108; CRIB; 1. KW Actin-binding; Repeat. FT DOMAIN 31 135 WH1. FT DOMAIN 200 213 CRIB. FT DOMAIN 401 418 WH2 1. FT DOMAIN 429 446 WH2 2. FT COMPBIAS 274 385 PRO-RICH. FT COMPBIAS 482 501 ASP-RICH. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 501 AA; 54325 MW; 480E21F26F7FC77E CRC64; MSSGQQPPRR VTNVGSLLLT PQENESLFSF LGKKCVTMSS AVVQLYAADR NCMWSKKCSG VACLVKDNPQ RSYFLRIFDI KDGKLLWEQE LYNNFVYNSP RGYFHTFAGD TCQVALNFAN EEEAKKFRKA VTDLLGRRQR KSEKRRDAPN GPNLPMATVD IKNPEITTNR FYSSQVNNIS HTKEKKKGKA KKKRLTKADI GTPSNFQHIG HVGWDPNTGF DLNNLDPELK NLFDMCGISE AQLKDRETSK VIYDFIEKTG GVEAVKNELR RQAPPPPPPS RGGPPPPPPP PHSSGPPPPP ARGRGAPPPP PSRAPTAAPP PPPPSRPGVV VPPPPPNRMY PPPPPALPSS APSGPPPPPP LSMAGSTAPP PPPPPPPPPG PPPPPGLPSD GDHQVPASSG NKAALLDQIR EGAQLKKVEQ NSRPVSCSGR DALLDQIRQG IQLKSVSDGQ ESTPPTPAPT SGIVGALMEV MQKRSKAIHS SDEDEDDDDE EDFQDDDEWE D // ID Q9B1S6 PRELIMINARY; PRT; 260 AA. AC Q9B1S6; DT 01-JUN-2001 (TrEMBLrel. 17, Created) DT 01-JUN-2001 (TrEMBLrel. 17, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Cytochrome c oxidase subunit III (EC 1.9.3.1) (Cytochrome co oxidase DE subunit III) (Cytochrome c oxidase polypeptide III) (Cytochrome DE oxidase subunit III){EP249}. GN COX3{EI2}. OS Homo sapiens (Human). OG Mitochondrion{EI3}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606{EP248}; RN [1]{EI3} RP SEQUENCE FROM N.A. RX MEDLINE=21012010; PubMed=11130070; RA Ingman M., Kaessmann H., Paabo S., Gyllensten U.; RT "Mitochondrial genome variation and the origin of modern humans."; RL Nature 408:708-713(2000). RN [2]{EI3} RP SEQUENCE FROM N.A. RX MEDLINE=21176314; PubMed=11279504; RA Ingman M., Kaessmann H., Paabo S., Gyllensten U.; RT "correction: Mitochondrial genome variation and the origin of modern RT humans."; RL Nature 410:611-611(2001). RN [3]{EI3} RP SEQUENCE FROM N.A. RA Ingman M., Kaessmann H., Paabo S., Gyllensten U.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [4]{EI2} RP SEQUENCE FROM N.A. RX PubMed=11553319; RA Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; RT "Major genomic mitochondrial lineages delineate early human RT expansions."; RL BMC Genet. 2:13-13(2001). RN [5]{EI2} RP SEQUENCE FROM N.A. RA Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [6]{EI79} RP SEQUENCE FROM N.A. RX MEDLINE=22062553; PubMed=12022039; RA Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., RA Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., RA Barbosa M., Paco-Larson M.L., Petzl-Erler M.L., Valente V., RA Santos S.E., Zago M.A.; RT "Mitochondrial genome diversity of Native Americans supports a single RT early entry of founder populations into America."; RL Am. J. Hum. Genet. 71:187-192(2002). RN [7]{EI118} RP SEQUENCE FROM N.A. RX MEDLINE=22406325; PubMed=12509511; RA Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., RA Hosseini S., Brandon M., Easley K., Chen E., Brown M.D., RA Sukernik R.I., Olckers A., Wallace D.C.; RT "Natural selection shaped regional mtDNA variation in humans."; RL Proc. Natl. Acad. Sci. U.S.A. 100:171-176(2003). RN [8]{EI157} RP SEQUENCE FROM N.A. RC STRAIN=GD7812, LN7550, LN7589, SD10313, XJ8426, EWK28, QD8141, GD7834, RC Miao271, DW48, WH6954, WH6967, Mg246, LN7595, GD7817, WH6958, GD7829, RC SD10352, XJ8420, SD10334, WH6979, SD10324, XJ8416, LN7711, QD8166, RC GD7837n, QD8168, GD7811, GD7830, WH6980, XJ8451, GD7809, YN289, RC GD7813, SD10362, GD7825, XJ8435, GD7824, LN7710, QD8167, YN163, RC WH6973, and QD8147; RA Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; RT "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from RT Complete Sequences."; RL Am. J. Hum. Genet. 0:0-0(2003). RN [9]{EI200} RP SEQUENCE FROM N.A. RC STRAIN=Aus14, Aus15, Aus16, Aus17, Aus20, Aus21, Aus22, Aus23, B2, B4, RC B6, E4, E9, F5, Y6, Y7, C1112, C1190, CAM, T1331, K11b, M306, 961, RC 100, CP8, GP4, WE16, WE18, WE23, WE4, WE7, 36, NG12, NG29, SH10, SH17, RC SH19, SH23, SH29, SH33, S1216, S1220, 496, 513, DCH002, Sb13, and RC Sb29; RX MEDLINE=22723755; PubMed=12840039; RA Ingman M., Gyllensten U.; RT "Mitochondrial genome variation and evolutionary history of Australian RT and new guinean aborigines."; RL Genome Res. 13:1600-1606(2003). CC -!- FUNCTION: Subunits I, II and III form the functional core of the CC enzyme complex (By similarity){EA1}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) = 4 ferricytochrome CC c + 2 H(2)O{EA1}. CC -!- SIMILARITY: BELONGS TO THE CYTOCHROME C OXIDASE SUBUNIT 3 CC FAMILY{EA1}. DR EMBL; AF347015; AAK17889.2; -.{EI3} DR EMBL; AF346963; AAK17213.1; -.{EI4} DR EMBL; AF346964; AAK17226.2; -.{EI5} DR EMBL; AF346966; AAK17252.1; -.{EI6} DR EMBL; AF346967; AAK17265.2; -.{EI7} DR EMBL; AF346968; AAK17278.2; -.{EI8} DR EMBL; AF346969; AAK17291.2; -.{EI9} DR EMBL; AF346970; AAK17304.2; -.{EI10} DR EMBL; AF346971; AAK17317.2; -.{EI11} DR EMBL; AF346972; AAK17330.2; -.{EI12} DR EMBL; AF346973; AAK17343.2; -.{EI13} DR EMBL; AF346974; AAK17356.2; -.{EI14} DR EMBL; AF346975; AAK17369.2; -.{EI15} DR EMBL; AF346976; AAK17382.1; -.{EI16} DR EMBL; AF346977; AAK17395.1; -.{EI17} DR EMBL; AF346978; AAK17408.1; -.{EI18} DR EMBL; AF346979; AAK17421.1; -.{EI19} DR EMBL; AF346980; AAK17434.2; -.{EI20} DR EMBL; AF346981; AAK17447.2; -.{EI21} DR EMBL; AF346982; AAK17460.1; -.{EI22} DR EMBL; AF346983; AAK17473.1; -.{EI23} DR EMBL; AF346984; AAK17486.2; -.{EI24} DR EMBL; AF346985; AAK17499.2; -.{EI25} DR EMBL; AF346986; AAK17512.2; -.{EI26} DR EMBL; AF346987; AAK17525.2; -.{EI27} DR EMBL; AF346990; AAK17564.1; -.{EI28} DR EMBL; AF346991; AAK17577.2; -.{EI29} DR EMBL; AF346992; AAK17590.2; -.{EI30} DR EMBL; AF346993; AAK17603.2; -.{EI31} DR EMBL; AF346994; AAK17616.2; -.{EI32} DR EMBL; AF346995; AAK17629.2; -.{EI33} DR EMBL; AF346996; AAK17642.2; -.{EI34} DR EMBL; AF346997; AAK17655.2; -.{EI35} DR EMBL; AF346998; AAK17668.2; -.{EI36} DR EMBL; AF346999; AAK17681.2; -.{EI37} DR EMBL; AF347000; AAK17694.1; -.{EI38} DR EMBL; AF347001; AAK17707.2; -.{EI39} DR EMBL; AF347002; AAK17720.2; -.{EI40} DR EMBL; AF347003; AAK17733.2; -.{EI41} DR EMBL; AF347004; AAK17746.2; -.{EI42} DR EMBL; AF347005; AAK17759.2; -.{EI43} DR EMBL; AF347006; AAK17772.2; -.{EI44} DR EMBL; AF347007; AAK17785.2; -.{EI45} DR EMBL; AF347008; AAK17798.2; -.{EI46} DR EMBL; AF347009; AAK17811.2; -.{EI47} DR EMBL; AF347011; AAK17837.2; -.{EI48} DR EMBL; AF347014; AAK17876.2; -.{EI49} DR EMBL; AF382013; AAL54806.1; -.{EI2} DR EMBL; AF381981; AAL54393.1; -.{EI50} DR EMBL; AF381982; AAL54403.1; -.{EI51} DR EMBL; AF381983; AAL54416.1; -.{EI52} DR EMBL; AF381984; AAL54429.1; -.{EI53} DR EMBL; AF381985; AAL54442.1; -.{EI54} DR EMBL; AF381986; AAL54455.1; -.{EI55} DR EMBL; AF381987; AAL54468.1; -.{EI56} DR EMBL; AF381988; AAL54481.1; -.{EI57} DR EMBL; AF381990; AAL54507.1; -.{EI58} DR EMBL; AF381991; AAL54520.1; -.{EI59} DR EMBL; AF381993; AAL54546.1; -.{EI60} DR EMBL; AF381994; AAL54559.1; -.{EI61} DR EMBL; AF381995; AAL54572.1; -.{EI62} DR EMBL; AF381996; AAL54585.1; -.{EI63} DR EMBL; AF381998; AAL54611.1; -.{EI64} DR EMBL; AF381999; AAL54624.1; -.{EI65} DR EMBL; AF382000; AAL54637.1; -.{EI66} DR EMBL; AF382001; AAL54650.1; -.{EI67} DR EMBL; AF382002; AAL54663.1; -.{EI68} DR EMBL; AF382003; AAL54676.1; -.{EI69} DR EMBL; AF382004; AAL54689.1; -.{EI70} DR EMBL; AF382005; AAL54702.1; -.{EI71} DR EMBL; AF382006; AAL54715.1; -.{EI72} DR EMBL; AF382007; AAL54728.1; -.{EI73} DR EMBL; AF382008; AAL54741.1; -.{EI74} DR EMBL; AF382009; AAL54754.1; -.{EI75} DR EMBL; AF382010; AAL54767.1; -.{EI76} DR EMBL; AF382011; AAL54780.1; -.{EI77} DR EMBL; AF382012; AAL54793.1; -.{EI78} DR EMBL; AF465941; AAN14542.1; -.{EI79} DR EMBL; AF465942; AAN14553.1; -.{EI80} DR EMBL; AF465943; AAN14564.1; -.{EI81} DR EMBL; AF465944; AAN14575.1; -.{EI82} DR EMBL; AF465945; AAN14586.1; -.{EI83} DR EMBL; AF465946; AAN14597.1; -.{EI84} DR EMBL; AF465947; AAN14608.1; -.{EI85} DR EMBL; AF465948; AAN14619.1; -.{EI86} DR EMBL; AF465949; AAN14630.1; -.{EI87} DR EMBL; AF465950; AAN14641.1; -.{EI88} DR EMBL; AF465951; AAN14652.1; -.{EI89} DR EMBL; AF465952; AAN14663.1; -.{EI90} DR EMBL; AF465953; AAN14674.1; -.{EI91} DR EMBL; AF465954; AAN14685.1; -.{EI92} DR EMBL; AF465955; AAN14696.1; -.{EI93} DR EMBL; AF465956; AAN14707.1; -.{EI94} DR EMBL; AF465958; AAN14729.1; -.{EI95} DR EMBL; AF465959; AAN14740.1; -.{EI96} DR EMBL; AF465960; AAN14751.1; -.{EI97} DR EMBL; AF465961; AAN14762.1; -.{EI98} DR EMBL; AF465962; AAN14773.1; -.{EI99} DR EMBL; AF465963; AAN14784.1; -.{EI100} DR EMBL; AF465964; AAN14795.1; -.{EI101} DR EMBL; AF465965; AAN14806.1; -.{EI102} DR EMBL; AF465966; AAN14817.1; -.{EI103} DR EMBL; AF465967; AAN14828.1; -.{EI104} DR EMBL; AF465968; AAN14839.1; -.{EI105} DR EMBL; AF465969; AAN14850.1; -.{EI106} DR EMBL; AF465970; AAN14861.1; -.{EI107} DR EMBL; AF465971; AAN14872.1; -.{EI108} DR EMBL; AF465972; AAN14883.1; -.{EI109} DR EMBL; AF465973; AAN14894.1; -.{EI110} DR EMBL; AF465974; AAN14905.1; -.{EI111} DR EMBL; AF465975; AAN14916.1; -.{EI112} DR EMBL; AF465976; AAN14927.1; -.{EI113} DR EMBL; AF465977; AAN14938.1; -.{EI114} DR EMBL; AF465978; AAN14949.1; -.{EI115} DR EMBL; AF465979; AAN14960.1; -.{EI116} DR EMBL; AF465980; AAN14971.1; -.{EI117} DR EMBL; AY195745; AAO88286.1; -.{EI118} DR EMBL; AY195747; AAO88312.1; -.{EI119} DR EMBL; AY195750; AAO88351.1; -.{EI120} DR EMBL; AY195751; AAO88364.1; -.{EI121} DR EMBL; AY195752; AAO88377.1; -.{EI122} DR EMBL; AY195754; AAO88403.1; -.{EI123} DR EMBL; AY195755; AAO88416.1; -.{EI124} DR EMBL; AY195757; AAO88442.1; -.{EI125} DR EMBL; AY195758; AAO88455.1; -.{EI126} DR EMBL; AY195759; AAO88468.1; -.{EI127} DR EMBL; AY195760; AAO88481.1; -.{EI128} DR EMBL; AY195761; AAO88494.1; -.{EI129} DR EMBL; AY195762; AAO88507.1; -.{EI130} DR EMBL; AY195763; AAO88520.1; -.{EI131} DR EMBL; AY195764; AAO88533.1; -.{EI132} DR EMBL; AY195765; AAO88546.1; -.{EI133} DR EMBL; AY195766; AAO88559.1; -.{EI134} DR EMBL; AY195767; AAO88572.1; -.{EI135} DR EMBL; AY195768; AAO88585.1; -.{EI136} DR EMBL; AY195771; AAO88624.1; -.{EI137} DR EMBL; AY195772; AAO88637.1; -.{EI138} DR EMBL; AY195773; AAO88650.1; -.{EI139} DR EMBL; AY195774; AAO88663.1; -.{EI140} DR EMBL; AY195775; AAO88676.1; -.{EI141} DR EMBL; AY195776; AAO88689.1; -.{EI142} DR EMBL; AY195777; AAO88702.1; -.{EI143} DR EMBL; AY195778; AAO88715.1; -.{EI144} DR EMBL; AY195779; AAO88728.1; -.{EI145} DR EMBL; AY195780; AAO88741.1; -.{EI146} DR EMBL; AY195781; AAO88754.1; -.{EI147} DR EMBL; AY195782; AAO88767.1; -.{EI148} DR EMBL; AY195783; AAO88780.1; -.{EI149} DR EMBL; AY195784; AAO88793.1; -.{EI150} DR EMBL; AY195786; AAO88819.1; -.{EI151} DR EMBL; AY195787; AAO88832.1; -.{EI152} DR EMBL; AY195788; AAO88845.1; -.{EI153} DR EMBL; AY195790; AAO88871.1; -.{EI154} DR EMBL; AY195791; AAO88884.1; -.{EI155} DR EMBL; AY195792; AAO88897.1; -.{EI156} DR EMBL; AY255133; AAO66624.1; -.{EI157} DR EMBL; AY255134; AAO66637.1; -.{EI158} DR EMBL; AY255135; AAO66650.1; -.{EI159} DR EMBL; AY255136; AAO66663.1; -.{EI160} DR EMBL; AY255138; AAO66689.1; -.{EI161} DR EMBL; AY255139; AAO66702.1; -.{EI162} DR EMBL; AY255140; AAO66715.1; -.{EI163} DR EMBL; AY255141; AAO66728.1; -.{EI164} DR EMBL; AY255142; AAO66741.1; -.{EI165} DR EMBL; AY255143; AAO66754.1; -.{EI166} DR EMBL; AY255144; AAO66767.1; -.{EI167} DR EMBL; AY255145; AAO66780.1; -.{EI168} DR EMBL; AY255146; AAO66793.1; -.{EI169} DR EMBL; AY255147; AAO66806.1; -.{EI170} DR EMBL; AY255148; AAO66819.1; -.{EI171} DR EMBL; AY255150; AAO66845.1; -.{EI172} DR EMBL; AY255151; AAO66858.1; -.{EI173} DR EMBL; AY255152; AAO66871.1; -.{EI174} DR EMBL; AY255153; AAO66884.1; -.{EI175} DR EMBL; AY255154; AAO66897.1; -.{EI176} DR EMBL; AY255155; AAO66910.1; -.{EI177} DR EMBL; AY255156; AAO66923.1; -.{EI178} DR EMBL; AY255157; AAO66936.1; -.{EI179} DR EMBL; AY255158; AAO66949.1; -.{EI180} DR EMBL; AY255160; AAO66975.1; -.{EI181} DR EMBL; AY255162; AAO67001.1; -.{EI182} DR EMBL; AY255163; AAO67014.1; -.{EI183} DR EMBL; AY255164; AAO67027.1; -.{EI184} DR EMBL; AY255165; AAO67040.1; -.{EI185} DR EMBL; AY255166; AAO67053.1; -.{EI186} DR EMBL; AY255167; AAO67066.1; -.{EI187} DR EMBL; AY255168; AAO67079.1; -.{EI188} DR EMBL; AY255169; AAO67091.1; -.{EI189} DR EMBL; AY255170; AAO67104.1; -.{EI190} DR EMBL; AY255171; AAO67117.1; -.{EI191} DR EMBL; AY255172; AAO67130.1; -.{EI192} DR EMBL; AY255174; AAO67156.1; -.{EI193} DR EMBL; AY255175; AAO67169.1; -.{EI194} DR EMBL; AY255176; AAO67182.1; -.{EI195} DR EMBL; AY255177; AAO67195.1; -.{EI196} DR EMBL; AY255178; AAO67208.1; -.{EI197} DR EMBL; AY255179; AAO67221.1; -.{EI198} DR EMBL; AY255180; AAO67234.1; -.{EI199} DR EMBL; AY289052; AAP47899.1; -.{EI200} DR EMBL; AY289053; AAP47912.1; -.{EI201} DR EMBL; AY289054; AAP47925.1; -.{EI202} DR EMBL; AY289055; AAP47938.1; -.{EI203} DR EMBL; AY289056; AAP47951.1; -.{EI204} DR EMBL; AY289057; AAP47964.1; -.{EI205} DR EMBL; AY289058; AAP47977.1; -.{EI206} DR EMBL; AY289059; AAP47990.1; -.{EI207} DR EMBL; AY289060; AAP48003.1; -.{EI208} DR EMBL; AY289061; AAP48016.1; -.{EI209} DR EMBL; AY289062; AAP48029.1; -.{EI210} DR EMBL; AY289063; AAP48042.1; -.{EI211} DR EMBL; AY289064; AAP48055.1; -.{EI212} DR EMBL; AY289065; AAP48068.1; -.{EI213} DR EMBL; AY289066; AAP48081.1; -.{EI214} DR EMBL; AY289067; AAP48094.1; -.{EI215} DR EMBL; AY289068; AAP48107.1; -.{EI216} DR EMBL; AY289069; AAP48120.1; -.{EI217} DR EMBL; AY289070; AAP48133.1; -.{EI218} DR EMBL; AY289071; AAP48146.1; -.{EI219} DR EMBL; AY289072; AAP48159.1; -.{EI220} DR EMBL; AY289074; AAP48185.1; -.{EI221} DR EMBL; AY289075; AAP48198.1; -.{EI222} DR EMBL; AY289076; AAP48211.1; -.{EI223} DR EMBL; AY289077; AAP48224.1; -.{EI224} DR EMBL; AY289078; AAP48237.1; -.{EI225} DR EMBL; AY289079; AAP48250.1; -.{EI226} DR EMBL; AY289080; AAP48263.1; -.{EI227} DR EMBL; AY289081; AAP48276.1; -.{EI228} DR EMBL; AY289082; AAP48289.1; -.{EI229} DR EMBL; AY289083; AAP48302.1; -.{EI230} DR EMBL; AY289084; AAP48315.1; -.{EI231} DR EMBL; AY289085; AAP48328.1; -.{EI232} DR EMBL; AY289086; AAP48341.1; -.{EI233} DR EMBL; AY289087; AAP48354.1; -.{EI234} DR EMBL; AY289088; AAP48367.1; -.{EI235} DR EMBL; AY289089; AAP48380.1; -.{EI236} DR EMBL; AY289090; AAP48393.1; -.{EI237} DR EMBL; AY289091; AAP48406.1; -.{EI238} DR EMBL; AY289092; AAP48419.1; -.{EI239} DR EMBL; AY289093; AAP48431.1; -.{EI240} DR EMBL; AY289094; AAP48444.1; -.{EI241} DR EMBL; AY289095; AAP48457.1; -.{EI242} DR EMBL; AY289096; AAP48470.1; -.{EI243} DR EMBL; AY289099; AAP48509.1; -.{EI244} DR EMBL; AY289100; AAP48522.1; -.{EI245} DR EMBL; AY289101; AAP48535.1; -.{EI246} DR EMBL; AY289102; AAP48548.1; -.{EI247} DR GO; GO:0016021; C:integral to membrane; IEA. DR GO; GO:0005739; C:mitochondrion; IEA. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA. DR GO; GO:0016491; F:oxidoreductase activity; IEA. DR GO; GO:0006118; P:electron transport; IEA. DR InterPro; IPR000298; CytC_oxdse_III. DR Pfam; PF00510; COX3; 1. DR ProDom; PD000382; CytC_oxdse_III; 1. DR TIGRFAMs; TIGR01732; tiny_TM_bacill; 1. DR PROSITE; PS50253; COX3; 1. KW Oxidoreductase{EA1}; Transmembrane{EA1}; Mitochondrion{EA1,EP248}. ** ** ################# SOURCE SECTION ################## ** Homo sapiens mitochondrion, complete genome. ** [1] ** 1-16571 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16571 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16571 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16574 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16574 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16574 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16571 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16571 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16566 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16566 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16566 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16571 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16571 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16558 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16558 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16558 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16568 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16568 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16568 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16566 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16566 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16566 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16561 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16561 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16562 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16562 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16562 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16561 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16561 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16572 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16572 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16570 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16570 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16572 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16572 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16572 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16572 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16568 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16568 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16568 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16560 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16560 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16569 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16569 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16562 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16562 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16562 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 21012010. ** PUBMED; 11130070. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "Mitochondrial genome variation and the origin of modern humans"; ** Nature 408(6813):708-713(2000). ** [2] ** 1-16567 ** MEDLINE; 21176314. ** PUBMED; 11279504. ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** "correction: Mitochondrial genome variation and the origin of modern ** humans"; ** Nature 410(6828):611-611(2001). ** [3] ** 1-16567 ** Ingman M., Kaessmann H., Paabo S., Gyllensten U.; ** ; ** Submitted (09-FEB-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16568 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16568 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16570 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16570 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16570 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16570 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16571 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16571 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16567 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16567 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16568 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16568 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16570 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16570 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16572 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16572 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16570 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16570 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16560 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16560 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16564 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16564 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16568 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16568 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16568 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16568 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-16569 ** PUBMED; 11553319. ** Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C., Cabrera V.M.; ** "Major genomic mitochondrial lineages delineate early human expansions"; ** BMC Genet. 2(1):13-13(2001). ** [2] ** 1-16569 ** Cabrera V.M., Maca-Meyer N., Gonzalez A.M., Larruga J.M., Flores C.; ** ; ** Submitted (18-MAY-2001) to the EMBL/GenBank/DDBJ databases. ** Genetics, University of La Laguna, Biology, La Laguna, Tenerife 38271, ** Spain ** [1] ** 1-8828 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8828 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8827 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8827 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8828 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8828 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8820 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8820 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8820 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8820 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-8829 ** MEDLINE; 22062553. ** PUBMED; 12022039. ** Silva W.A. Jr., Bonatto S.L., Holanda A.J., Ribeiro-Dos-Santos A.K., ** Paixao B.M., Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larson M.L., Petzl-Erler M.L., Valente V., Santos S.E., Zago M.A.; ** "Mitochondrial genome diversity of Native Americans supports a single early ** entry of founder populations into America"; ** Am. J. Hum. Genet. 71(1):187-192(2002). ** [2] ** 1-8829 ** Silva W.A. Jr., Bonatto S.L., Ribeiro-Dos-Santos A.K., Paixao M., ** Goldman G.H., Abe-Sandes K., Rodriguez-Delfin L., Barbosa M., ** Paco-Larcon M.L., Petzl-Erles M.L., Valente V., Santos S.E., Zago M.A.; ** ; ** Submitted (06-JAN-2002) to the EMBL/GenBank/DDBJ databases. ** Molecular Biology, Center for Cell-Based Therapy, Rua Tenente Catao Roxo, ** 2501, Ribeirao Preto, Sao Paulo 14051-140, Brazil ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16566 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16566 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16565 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16565 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16572 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16572 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16567 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16567 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16557 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16557 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16567 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16567 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16568 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16568 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16565 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16565 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16566 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16566 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16566 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16566 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16570 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16570 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16567 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16567 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16569 ** MEDLINE; 22406325. ** PUBMED; 12509511. ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** "Natural selection shaped regional mtDNA variation in humans"; ** Proc. Natl. Acad. Sci. U.S.A. 100(1):171-176(2003). ** [2] ** 1-16569 ** Mishmar D., Ruiz-Pesini E., Golik P., Macaulay V., Clark A.G., Hosseini S., ** Brandon M., Easley K., Chen E., Brown M.D., Sukernik R.I., Olckers A., ** Wallace D.C.; ** ; ** Submitted (11-DEC-2002) to the EMBL/GenBank/DDBJ databases. ** MAMMAG, University of California, Irvine, 2nd Floor Hewitt Hall, Irvine, ** California 92697-3940, USA ** [1] ** 1-16556 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16556 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16492 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16492 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16562 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16562 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16486 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16486 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16571 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16571 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16561 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16561 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16558 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16558 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16574 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16574 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16579 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16579 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16576 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16576 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16575 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16575 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16566 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16566 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16558 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16558 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16566 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16566 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16569 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16562 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16562 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16567 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16570 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16576 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16576 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16559 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16559 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** "Phylogeny of East Asian Mitochondrial DNA Lineages Inferred from Complete ** Sequences"; ** Am. J. Hum. Genet. 0:0-0(2003). ** [2] ** 1-16568 ** Kong Q.-P., Yao Y.-G., Sun C., Bandelt H.-J., Zhu C.-L., Zhang Y.-P.; ** ; ** Submitted (12-MAR-2003) to the EMBL/GenBank/DDBJ databases. ** Chinese Academy of Sciences, Laboratory of Molecular Evolution and Genome ** Diversity, Kunming Institute of Zoology, Kunming, Yunnan 650223, China ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16571 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16575 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16575 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16573 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16573 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16559 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16559 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16560 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16567 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16567 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16568 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16568 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16571 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16560 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16568 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16568 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16570 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16570 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16571 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16571 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16574 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16574 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16572 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16572 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16569 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16569 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16561 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16561 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16560 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** [1] ** 1-16560 ** MEDLINE; 22723755. ** PUBMED; 12840039. ** Ingman M., Gyllensten U.; ** "Mitochondrial genome variation and evolutionary history of Australian and ** new guinean aborigines"; ** Genome Res. 13(7):1600-1606(2003). ** [2] ** 1-16560 ** Ingman M., Gyllensten U.; ** ; ** Submitted (02-MAY-2003) to the EMBL/GenBank/DDBJ databases. ** Genetics and Pathology, Uppsala University, Rudbeck Laboratory, Dag ** Hammarsjolds vag 20, Uppsala 751 85, Sweden ** source 1..16571 ** /db_xref="taxon:9606" ** /note="from African (Yoruba) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17889.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /country="Australia" ** /db_xref="taxon:9606" ** /note="from Aborigine" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17213.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16574 ** /country="Australia" ** /db_xref="taxon:9606" ** /note="from Aborigine" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9212..9992 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17226.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from Asian Indian" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17252.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Bamileke)" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17265.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 4) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Biaka)" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17278.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Biaka)" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17291.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from Buriat individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17304.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from Chukchi individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17317.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17330.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17343.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16571 ** /db_xref="taxon:9606" ** /note="from Crimean Tatar individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17356.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from Dutch individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17369.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from African (Effik) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17382.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from African (Effik) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17395.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from English individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17408.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from Evenki individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17421.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from African (Ewondo) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17434.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from French individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17447.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from Georgian individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17460.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from German individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17473.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from South American Indian (Guarani) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17486.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Hausa) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17499.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Ibo) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17512.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16566 ** /db_xref="taxon:9606" ** /note="from African (Ibo) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17525.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from Japanese individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17564.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from Khirgiz individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17577.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16571 ** /db_xref="taxon:9606" ** /note="from African (Kikuyu) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17590.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16558 ** /db_xref="taxon:9606" ** /note="from Korean individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9196..9976 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17603.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from African (Lisongo) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17616.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16568 ** /db_xref="taxon:9606" ** /note="from African (Mandenka) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17629.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16566 ** /db_xref="taxon:9606" ** /note="from African (Mbenzele) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17642.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Mbenzele) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17655.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16561 ** /db_xref="taxon:9606" ** /note="from African (Mbuti) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9199..9979 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17668.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16562 ** /db_xref="taxon:9606" ** /note="from African (Mbuti) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9200..9980 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17681.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from African (Mkamba) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17694.1" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 2) ** source 1..16561 ** /db_xref="taxon:9606" ** /note="from North American Indian (Piman) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9199..9979 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17707.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16572 ** /db_xref="taxon:9606" ** /note="from PNG (Coast) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17720.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16570 ** /db_xref="taxon:9606" ** /note="from PNG (Coast) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17733.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16572 ** /db_xref="taxon:9606" ** /note="from PNG (Highland) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17746.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16572 ** /db_xref="taxon:9606" ** /note="from PNG (Highland) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17759.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16568 ** /db_xref="taxon:9606" ** /note="from Saami individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17772.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16560 ** /db_xref="taxon:9606" ** /note="from Samoan individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17785.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16569 ** /db_xref="taxon:9606" ** /note="from African (San) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17798.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (San) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17811.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16562 ** /db_xref="taxon:9606" ** /note="from Uzbek individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9200..9980 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17837.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /db_xref="taxon:9606" ** /note="from African (Yoruba) individual" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAK17876.2" ** CDS_IN_EMBL_ENTRY 13 ** 12-APR-2001 (Rel. 67, Last updated, Version 3) ** source 1..16567 ** /country="India" ** /db_xref="taxon:9606" ** /haplotype="M*2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="2619" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54806.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16568 ** /country="Mauritania" ** /db_xref="taxon:9606" ** /haplotype="L2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="441" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome co oxidase subunit III" ** /protein_id="AAL54393.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Spain: Canary Islands, Tenerife" ** /db_xref="taxon:9606" ** /haplotype="U31" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="117" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54403.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="U32" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="249" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54416.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16570 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="M11" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="250" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54429.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16570 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="T5" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="252" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54442.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="X" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="255" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54455.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="J1b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="268" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54468.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="L1a" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="271" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54481.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Morocco: Berber" ** /db_xref="taxon:9606" ** /haplotype="V" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="364" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54507.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Mauritania" ** /db_xref="taxon:9606" ** /haplotype="L3b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="430" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54520.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Mauritania" ** /db_xref="taxon:9606" ** /haplotype="H1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="446" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54546.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Mauritania" ** /db_xref="taxon:9606" ** /haplotype="L1b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="451" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54559.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="U21" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="766" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54572.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16571 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="M12" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="771" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54585.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="L3d" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="800" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54611.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16567 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="N1b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="832" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54624.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Jordan" ** /db_xref="taxon:9606" ** /haplotype="U2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="842" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54637.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16568 ** /country="Spain: Maragato" ** /db_xref="taxon:9606" ** /haplotype="J2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M26" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54650.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16570 ** /country="Spain: Maragato" ** /db_xref="taxon:9606" ** /haplotype="H2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M27" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54663.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Spain: Maragato" ** /db_xref="taxon:9606" ** /haplotype="W" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M47" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54676.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Spain: Leon" ** /db_xref="taxon:9606" ** /haplotype="U22" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M68" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54689.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16572 ** /country="Spain: Leon" ** /db_xref="taxon:9606" ** /haplotype="K" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M72" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54702.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16570 ** /country="Spain: Leon" ** /db_xref="taxon:9606" ** /haplotype="T1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M78" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54715.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16560 ** /country="Spain: Leon" ** /db_xref="taxon:9606" ** /haplotype="I" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M90" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54728.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Morocco" ** /db_xref="taxon:9606" ** /haplotype="U6" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="279" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54741.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16564 ** /country="Spain: Canary Islands, Tenerife" ** /db_xref="taxon:9606" ** /haplotype="C" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="4" ** CDS 9202..9982 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54754.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16568 ** /country="Spain: Canary Islands, Hierro" ** /db_xref="taxon:9606" ** /haplotype="A" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="248" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54767.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16568 ** /country="Spain: Andalusia" ** /db_xref="taxon:9606" ** /haplotype="U7" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="1646" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54780.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..16569 ** /country="Philippines" ** /db_xref="taxon:9606" ** /haplotype="M*1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="2601" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAL54793.1" ** CDS_IN_EMBL_ENTRY 13 ** 02-JAN-2002 (Rel. 70, Last updated, Version 1) ** source 1..8828 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="African" ** /clone="NGR0524" ** CDS 2059..2839 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14542.1" ** CDS_IN_EMBL_ENTRY 10 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8827 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="African" ** /clone="NGR0522" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14553.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="African" ** /clone="NGR0475" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14564.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="African" ** /clone="NGR0510" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14575.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="ARL0058" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14586.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Japanese" ** /clone="JAP1043" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14597.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Japanese" ** /clone="JAP1045" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14608.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8828 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Japanese" ** /clone="JAP1044" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14619.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="GRC0149" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14630.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KCR0029" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14641.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KRC0033" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14652.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="GRC0131" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14663.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="GRC0169" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14674.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KTN0018" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14685.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KTN0209" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14696.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KTN0130" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14707.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8820 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KPO0001" ** CDS 2051..2831 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14729.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8820 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KPO0039" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14740.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="KPO0023" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14751.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="PTJ0068" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14762.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="PTJ0003" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14773.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="PTJ0001" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14784.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Peru" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1876" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14795.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Peru" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1881" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14806.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Peru" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1875" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14817.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Peru" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1878" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14828.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="QUE1880" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14839.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="TYR0004" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14850.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="TYR0016" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14861.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Caucasian" ** /clone="WTE1145" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14872.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Caucasian" ** /clone="WTE1182" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14883.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Caucasian" ** /clone="WTE1150" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14894.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="WPI0167" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14905.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0623" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14916.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0665" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14927.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0669" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14938.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0591" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14949.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0650" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14960.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..8829 ** /country="Brazil" ** /db_xref="taxon:9606" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Amerindian" ** /clone="YAN0637" ** CDS 2060..2840 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_table=2 ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAN14971.1" ** CDS_IN_EMBL_ENTRY 11 ** 20-SEP-2002 (Rel. 73, Last updated, Version 1) ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E12T" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="T haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88286.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="E4H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88312.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E17V" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="V haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88351.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16566 ** /db_xref="taxon:9606" ** /haplotype="E2H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9984,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88364.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E7H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88377.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E9J" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="J haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88403.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="As11G" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="G haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88416.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E6H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88442.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E5H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88455.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16565 ** /db_xref="taxon:9606" ** /haplotype="Na4C" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Native American" ** /isolation_source="C haplogroup Native American" ** CDS 9203..9983 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9983,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88468.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="As1A" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="A haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88481.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="As12Z" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Z Haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88494.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="As7G" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="G Halogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88507.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /haplotype="As4C" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Asian" ** /isolation_source="C Haplogroup Asian" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88520.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E19U" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="U haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88533.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="E13K" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="K haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88546.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16567 ** /db_xref="taxon:9606" ** /haplotype="A11L2b" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L2b haplogroup" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88559.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E11T" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="T haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88572.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E15W" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="W haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88585.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="As2A" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Asian" ** /isolation_source="A haplogroup Asian" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88624.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="As5C" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Asian" ** /isolation_source="C haplogroup Asian" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88637.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="E18X" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="European" ** /isolation_source="X haplogroup European" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88650.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="E10J" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="J haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88663.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="E1H" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="H haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88676.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="A9L2a" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L2a haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88689.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16557 ** /db_xref="taxon:9606" ** /haplotype="A10L1A2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L1A2 haplogroup" ** CDS 9195..9975 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9975,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88702.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="E8J" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="J haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88715.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E14W" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="W haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88728.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16567 ** /db_xref="taxon:9606" ** /haplotype="A2L1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L1a haplogroup" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88741.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="E16V" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="V haplogroup" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88754.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /haplotype="A7NL" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L3 haplogroup" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88767.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16565 ** /db_xref="taxon:9606" ** /haplotype="A4L1B2" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L1B2 haplogroup" ** CDS 9203..9983 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9983,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88780.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16566 ** /db_xref="taxon:9606" ** /haplotype="A8NL" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L3 haplogroup" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88793.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16566 ** /db_xref="taxon:9606" ** /haplotype="Na5A" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Native American" ** /isolation_source="A haplogroup Native American" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9984,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88819.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="Na3X" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Native American" ** /isolation_source="X haplogroup Native American" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88832.1" ** 11-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="A5L2A1" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="L2A1 haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88845.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /haplotype="As8D" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Asian" ** /isolation_source="D haplogroup Asian" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88871.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16567 ** /db_xref="taxon:9606" ** /haplotype="As10F" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="F haplogroup" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88884.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /haplotype="As9Y" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Y haplogroup" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome oxidase subunit III" ** /protein_id="AAO88897.1" ** 10-APR-2003 Last updated, EMBL entry ** source 1..16556 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7812" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9195..9975 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9975,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66624.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16492 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7550" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9130..9910 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9910,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66637.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16562 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7589" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9200..9980 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9980,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66650.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16486 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10313" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9124..9904 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9904,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66663.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16571 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8426" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9989,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66689.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="EWK28" ** /isolation_source="Ewenki from Inner Mongolia" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66702.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8141" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9199..9979 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9979,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66715.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7834" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66728.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Miao271" ** /isolation_source="Miao from Fenghuang, Hunan" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66741.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="DW48" ** /isolation_source="Daur from Inner Mongolia" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66754.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6954" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66767.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16558 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6967" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9196..9976 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9976,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66780.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Mg246" ** /isolation_source="Mongolian from Inner Mongolia" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66793.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16574 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7595" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9212..9992 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9992,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66806.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7817" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66819.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16579 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6958" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9217..9997 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9997,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66845.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7829" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66858.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10352" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66871.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8420" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66884.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16576 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10334" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9214..9994 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9994,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66897.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6979" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66910.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10324" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66923.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8416" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66936.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7711" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66949.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8166" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO66975.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7837n" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67001.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16575 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8168" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9213..9993 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9993,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67014.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16566 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7811" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9984,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67027.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16558 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7830" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9196..9976 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9976,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67040.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16566 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6980" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9204..9984 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9984,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67053.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8451" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67066.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7809" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67079.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="YN289" ** /isolation_source="Han from Kunming, Yunnan" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67091.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16562 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7813" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9200..9980 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9980,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67104.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SD10362" ** /isolation_source="Han from Tai'an, Shandong" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67117.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7825" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67130.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="XJ8435" ** /isolation_source="Han from Yili, Xinjiang" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67156.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GD7824" ** /isolation_source="Han from Zhanjiang, Guangdong" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67169.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="LN7710" ** /isolation_source="Han from Fengcheng, Liaoning" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67182.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8167" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67195.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16576 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="YN163" ** /isolation_source="Han from Kunming, Yunnan" ** CDS 9214..9994 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9994,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67208.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16559 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WH6973" ** /isolation_source="Han from Wuhan, Hubei" ** CDS 9197..9977 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9977,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67221.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /country="China" ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="QD8147" ** /isolation_source="Han from Qingdao, Shandong" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAO67234.1" ** 18-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus14" ** /isolation_source="Australian Aborigine" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47899.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16571 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus15" ** /isolation_source="Australian Aborigine" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9989,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47912.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus16" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47925.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus17" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47938.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus20" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47951.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus21" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47964.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus22" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47977.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16575 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Aus23" ** /isolation_source="Australian Aborigine" ** CDS 9212..9992 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9992,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP47990.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="B2" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48003.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="B4" ** /isolation_source="Australian Aborigine" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48016.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="B6" ** /isolation_source="Australian Aborigine" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48029.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="E4" ** /isolation_source="Australian Aborigine" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48042.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="E9" ** /isolation_source="Australian Aborigine" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48055.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="F5" ** /isolation_source="Australian Aborigine" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48068.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16573 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Y6" ** /isolation_source="Australian Aborigine" ** CDS 9211..9991 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9991,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48081.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Y7" ** /isolation_source="Australian Aborigine" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48094.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16559 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="C1112" ** /isolation_source="Cook Islander" ** CDS 9197..9977 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9977,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48107.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16560 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="C1190" ** /isolation_source="Cook Islander" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48120.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="CAM" ** /isolation_source="Filipino" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48133.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16567 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="T1331" ** /isolation_source="Southern Indian (Kannada)" ** CDS 9205..9985 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9985,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48146.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="K11b" ** /isolation_source="Southern Indian (Koraga)" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48159.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="M306" ** /isolation_source="Southern Indian (Mullukurunan)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48185.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16571 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="961" ** /isolation_source="Nasioi" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9989,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48198.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16560 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="100" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9197..9977 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9977,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48211.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="CP8" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48224.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="GP4" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48237.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE16" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48250.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE18" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48263.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16568 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE23" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9206..9986 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9986,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48276.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE4" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48289.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="WE7" ** /isolation_source="Papua New Guinean (Coastal)" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48302.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="36" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48315.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="NG12" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48328.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="NG29" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48341.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH10" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48354.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16570 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH17" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9208..9988 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9988,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48367.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH19" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48380.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH23" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48393.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16571 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH29" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9209..9989 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9989,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48406.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="SH33" ** /isolation_source="Papua New Guinean (Highland)" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48419.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="S1216" ** /isolation_source="Samoan" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48431.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="S1220" ** /isolation_source="Samoan" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48444.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16574 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="496" ** /isolation_source="Taiwanese Indian" ** CDS 9212..9992 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9992,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48457.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16572 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="513" ** /isolation_source="Taiwanese Indian" ** CDS 9210..9990 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9990,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48470.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16569 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="DCH002" ** /isolation_source="Thai" ** CDS 9207..9987 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9987,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48509.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16561 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Sb13" ** /isolation_source="Thai" ** CDS 9199..9979 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9979,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48522.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16560 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolate="Sb29" ** /isolation_source="Thai" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48535.1" ** 08-JUL-2003 Last updated, EMBL entry ** source 1..16560 ** /db_xref="taxon:9606" ** /mol_type="genomic DNA" ** /organelle="mitochondrion" ** /organism="Homo sapiens" ** /isolation_source="Tongan" ** CDS 9198..9978 ** /codon_start=1 ** /note="TAA stop codon is completed by the addition of 3' A ** residues to the mRNA" ** /transl_except=(pos:9978,aa:TERM) ** /transl_table=2 ** /gene="COX3" ** /product="cytochrome c oxidase subunit III" ** /protein_id="AAP48548.1" ** 08-JUL-2003 Last updated, EMBL entry ** ################# INTERNAL SECTION ################## **EV EA1; Rulebase; -; RU003375V0.42; 18-NOV-2002. **EV EI2; EMBL; -; AAL54806.1; 07-FEB-2002. **EV EI3; EMBL; -; AAK17889.2; 26-APR-2001. **EV EI4; EMBL; -; AAK17213.1; 26-APR-2001. **EV EI5; EMBL; -; AAK17226.2; 26-APR-2001. **EV EI6; EMBL; -; AAK17252.1; 26-APR-2001. **EV EI7; EMBL; -; AAK17265.2; 26-APR-2001. **EV EI8; EMBL; -; AAK17278.2; 26-APR-2001. **EV EI9; EMBL; -; AAK17291.2; 26-APR-2001. **EV EI10; EMBL; -; AAK17304.2; 26-APR-2001. **EV EI11; EMBL; -; AAK17317.2; 26-APR-2001. **EV EI12; EMBL; -; AAK17330.2; 26-APR-2001. **EV EI13; EMBL; -; AAK17343.2; 26-APR-2001. **EV EI14; EMBL; -; AAK17356.2; 26-APR-2001. **EV EI15; EMBL; -; AAK17369.2; 26-APR-2001. **EV EI16; EMBL; -; AAK17382.1; 26-APR-2001. **EV EI17; EMBL; -; AAK17395.1; 26-APR-2001. **EV EI18; EMBL; -; AAK17408.1; 26-APR-2001. **EV EI19; EMBL; -; AAK17421.1; 26-APR-2001. **EV EI20; EMBL; -; AAK17434.2; 26-APR-2001. **EV EI21; EMBL; -; AAK17447.2; 26-APR-2001. **EV EI22; EMBL; -; AAK17460.1; 26-APR-2001. **EV EI23; EMBL; -; AAK17473.1; 26-APR-2001. **EV EI24; EMBL; -; AAK17486.2; 26-APR-2001. **EV EI25; EMBL; -; AAK17499.2; 26-APR-2001. **EV EI26; EMBL; -; AAK17512.2; 26-APR-2001. **EV EI27; EMBL; -; AAK17525.2; 26-APR-2001. **EV EI28; EMBL; -; AAK17564.1; 26-APR-2001. **EV EI29; EMBL; -; AAK17577.2; 26-APR-2001. **EV EI30; EMBL; -; AAK17590.2; 26-APR-2001. **EV EI31; EMBL; -; AAK17603.2; 26-APR-2001. **EV EI32; EMBL; -; AAK17616.2; 26-APR-2001. **EV EI33; EMBL; -; AAK17629.2; 26-APR-2001. **EV EI34; EMBL; -; AAK17642.2; 26-APR-2001. **EV EI35; EMBL; -; AAK17655.2; 26-APR-2001. **EV EI36; EMBL; -; AAK17668.2; 26-APR-2001. **EV EI37; EMBL; -; AAK17681.2; 26-APR-2001. **EV EI38; EMBL; -; AAK17694.1; 26-APR-2001. **EV EI39; EMBL; -; AAK17707.2; 26-APR-2001. **EV EI40; EMBL; -; AAK17720.2; 26-APR-2001. **EV EI41; EMBL; -; AAK17733.2; 26-APR-2001. **EV EI42; EMBL; -; AAK17746.2; 26-APR-2001. **EV EI43; EMBL; -; AAK17759.2; 26-APR-2001. **EV EI44; EMBL; -; AAK17772.2; 26-APR-2001. **EV EI45; EMBL; -; AAK17785.2; 26-APR-2001. **EV EI46; EMBL; -; AAK17798.2; 26-APR-2001. **EV EI47; EMBL; -; AAK17811.2; 26-APR-2001. **EV EI48; EMBL; -; AAK17837.2; 26-APR-2001. **EV EI49; EMBL; -; AAK17876.2; 26-APR-2001. **EV EI50; EMBL; -; AAL54393.1; 07-FEB-2002. **EV EI51; EMBL; -; AAL54403.1; 07-FEB-2002. **EV EI52; EMBL; -; AAL54416.1; 07-FEB-2002. **EV EI53; EMBL; -; AAL54429.1; 07-FEB-2002. **EV EI54; EMBL; -; AAL54442.1; 07-FEB-2002. **EV EI55; EMBL; -; AAL54455.1; 07-FEB-2002. **EV EI56; EMBL; -; AAL54468.1; 07-FEB-2002. **EV EI57; EMBL; -; AAL54481.1; 07-FEB-2002. **EV EI58; EMBL; -; AAL54507.1; 07-FEB-2002. **EV EI59; EMBL; -; AAL54520.1; 07-FEB-2002. **EV EI60; EMBL; -; AAL54546.1; 07-FEB-2002. **EV EI61; EMBL; -; AAL54559.1; 07-FEB-2002. **EV EI62; EMBL; -; AAL54572.1; 07-FEB-2002. **EV EI63; EMBL; -; AAL54585.1; 07-FEB-2002. **EV EI64; EMBL; -; AAL54611.1; 07-FEB-2002. **EV EI65; EMBL; -; AAL54624.1; 07-FEB-2002. **EV EI66; EMBL; -; AAL54637.1; 07-FEB-2002. **EV EI67; EMBL; -; AAL54650.1; 07-FEB-2002. **EV EI68; EMBL; -; AAL54663.1; 07-FEB-2002. **EV EI69; EMBL; -; AAL54676.1; 07-FEB-2002. **EV EI70; EMBL; -; AAL54689.1; 07-FEB-2002. **EV EI71; EMBL; -; AAL54702.1; 07-FEB-2002. **EV EI72; EMBL; -; AAL54715.1; 07-FEB-2002. **EV EI73; EMBL; -; AAL54728.1; 07-FEB-2002. **EV EI74; EMBL; -; AAL54741.1; 07-FEB-2002. **EV EI75; EMBL; -; AAL54754.1; 07-FEB-2002. **EV EI76; EMBL; -; AAL54767.1; 07-FEB-2002. **EV EI77; EMBL; -; AAL54780.1; 07-FEB-2002. **EV EI78; EMBL; -; AAL54793.1; 07-FEB-2002. **EV EI79; EMBL; -; AAN14542.1; 12-DEC-2002. **EV EI80; EMBL; -; AAN14553.1; 12-DEC-2002. **EV EI81; EMBL; -; AAN14564.1; 12-DEC-2002. **EV EI82; EMBL; -; AAN14575.1; 12-DEC-2002. **EV EI83; EMBL; -; AAN14586.1; 12-DEC-2002. **EV EI84; EMBL; -; AAN14597.1; 12-DEC-2002. **EV EI85; EMBL; -; AAN14608.1; 12-DEC-2002. **EV EI86; EMBL; -; AAN14619.1; 12-DEC-2002. **EV EI87; EMBL; -; AAN14630.1; 12-DEC-2002. **EV EI88; EMBL; -; AAN14641.1; 12-DEC-2002. **EV EI89; EMBL; -; AAN14652.1; 12-DEC-2002. **EV EI90; EMBL; -; AAN14663.1; 12-DEC-2002. **EV EI91; EMBL; -; AAN14674.1; 12-DEC-2002. **EV EI92; EMBL; -; AAN14685.1; 12-DEC-2002. **EV EI93; EMBL; -; AAN14696.1; 12-DEC-2002. **EV EI94; EMBL; -; AAN14707.1; 12-DEC-2002. **EV EI95; EMBL; -; AAN14729.1; 12-DEC-2002. **EV EI96; EMBL; -; AAN14740.1; 12-DEC-2002. **EV EI97; EMBL; -; AAN14751.1; 12-DEC-2002. **EV EI98; EMBL; -; AAN14762.1; 12-DEC-2002. **EV EI99; EMBL; -; AAN14773.1; 12-DEC-2002. **EV EI100; EMBL; -; AAN14784.1; 12-DEC-2002. **EV EI101; EMBL; -; AAN14795.1; 12-DEC-2002. **EV EI102; EMBL; -; AAN14806.1; 12-DEC-2002. **EV EI103; EMBL; -; AAN14817.1; 12-DEC-2002. **EV EI104; EMBL; -; AAN14828.1; 12-DEC-2002. **EV EI105; EMBL; -; AAN14839.1; 12-DEC-2002. **EV EI106; EMBL; -; AAN14850.1; 12-DEC-2002. **EV EI107; EMBL; -; AAN14861.1; 12-DEC-2002. **EV EI108; EMBL; -; AAN14872.1; 12-DEC-2002. **EV EI109; EMBL; -; AAN14883.1; 12-DEC-2002. **EV EI110; EMBL; -; AAN14894.1; 12-DEC-2002. **EV EI111; EMBL; -; AAN14905.1; 12-DEC-2002. **EV EI112; EMBL; -; AAN14916.1; 12-DEC-2002. **EV EI113; EMBL; -; AAN14927.1; 12-DEC-2002. **EV EI114; EMBL; -; AAN14938.1; 12-DEC-2002. **EV EI115; EMBL; -; AAN14949.1; 12-DEC-2002. **EV EI116; EMBL; -; AAN14960.1; 12-DEC-2002. **EV EI117; EMBL; -; AAN14971.1; 12-DEC-2002. **EV EI118; EMBL; -; AAO88286.1; 14-APR-2003. **EV EI119; EMBL; -; AAO88312.1; 14-APR-2003. **EV EI120; EMBL; -; AAO88351.1; 14-APR-2003. **EV EI121; EMBL; -; AAO88364.1; 14-APR-2003. **EV EI122; EMBL; -; AAO88377.1; 14-APR-2003. **EV EI123; EMBL; -; AAO88403.1; 14-APR-2003. **EV EI124; EMBL; -; AAO88416.1; 14-APR-2003. **EV EI125; EMBL; -; AAO88442.1; 14-APR-2003. **EV EI126; EMBL; -; AAO88455.1; 14-APR-2003. **EV EI127; EMBL; -; AAO88468.1; 14-APR-2003. **EV EI128; EMBL; -; AAO88481.1; 14-APR-2003. **EV EI129; EMBL; -; AAO88494.1; 14-APR-2003. **EV EI130; EMBL; -; AAO88507.1; 14-APR-2003. **EV EI131; EMBL; -; AAO88520.1; 14-APR-2003. **EV EI132; EMBL; -; AAO88533.1; 14-APR-2003. **EV EI133; EMBL; -; AAO88546.1; 14-APR-2003. **EV EI134; EMBL; -; AAO88559.1; 14-APR-2003. **EV EI135; EMBL; -; AAO88572.1; 14-APR-2003. **EV EI136; EMBL; -; AAO88585.1; 14-APR-2003. **EV EI137; EMBL; -; AAO88624.1; 14-APR-2003. **EV EI138; EMBL; -; AAO88637.1; 14-APR-2003. **EV EI139; EMBL; -; AAO88650.1; 14-APR-2003. **EV EI140; EMBL; -; AAO88663.1; 14-APR-2003. **EV EI141; EMBL; -; AAO88676.1; 14-APR-2003. **EV EI142; EMBL; -; AAO88689.1; 14-APR-2003. **EV EI143; EMBL; -; AAO88702.1; 14-APR-2003. **EV EI144; EMBL; -; AAO88715.1; 14-APR-2003. **EV EI145; EMBL; -; AAO88728.1; 14-APR-2003. **EV EI146; EMBL; -; AAO88741.1; 14-APR-2003. **EV EI147; EMBL; -; AAO88754.1; 14-APR-2003. **EV EI148; EMBL; -; AAO88767.1; 14-APR-2003. **EV EI149; EMBL; -; AAO88780.1; 14-APR-2003. **EV EI150; EMBL; -; AAO88793.1; 14-APR-2003. **EV EI151; EMBL; -; AAO88819.1; 14-APR-2003. **EV EI152; EMBL; -; AAO88832.1; 14-APR-2003. **EV EI153; EMBL; -; AAO88845.1; 14-APR-2003. **EV EI154; EMBL; -; AAO88871.1; 14-APR-2003. **EV EI155; EMBL; -; AAO88884.1; 14-APR-2003. **EV EI156; EMBL; -; AAO88897.1; 14-APR-2003. **EV EI157; EMBL; -; AAO66624.1; 23-JUL-2003. **EV EI158; EMBL; -; AAO66637.1; 23-JUL-2003. **EV EI159; EMBL; -; AAO66650.1; 23-JUL-2003. **EV EI160; EMBL; -; AAO66663.1; 23-JUL-2003. **EV EI161; EMBL; -; AAO66689.1; 23-JUL-2003. **EV EI162; EMBL; -; AAO66702.1; 23-JUL-2003. **EV EI163; EMBL; -; AAO66715.1; 23-JUL-2003. **EV EI164; EMBL; -; AAO66728.1; 23-JUL-2003. **EV EI165; EMBL; -; AAO66741.1; 23-JUL-2003. **EV EI166; EMBL; -; AAO66754.1; 23-JUL-2003. **EV EI167; EMBL; -; AAO66767.1; 23-JUL-2003. **EV EI168; EMBL; -; AAO66780.1; 23-JUL-2003. **EV EI169; EMBL; -; AAO66793.1; 23-JUL-2003. **EV EI170; EMBL; -; AAO66806.1; 23-JUL-2003. **EV EI171; EMBL; -; AAO66819.1; 23-JUL-2003. **EV EI172; EMBL; -; AAO66845.1; 23-JUL-2003. **EV EI173; EMBL; -; AAO66858.1; 23-JUL-2003. **EV EI174; EMBL; -; AAO66871.1; 23-JUL-2003. **EV EI175; EMBL; -; AAO66884.1; 23-JUL-2003. **EV EI176; EMBL; -; AAO66897.1; 23-JUL-2003. **EV EI177; EMBL; -; AAO66910.1; 23-JUL-2003. **EV EI178; EMBL; -; AAO66923.1; 23-JUL-2003. **EV EI179; EMBL; -; AAO66936.1; 23-JUL-2003. **EV EI180; EMBL; -; AAO66949.1; 23-JUL-2003. **EV EI181; EMBL; -; AAO66975.1; 23-JUL-2003. **EV EI182; EMBL; -; AAO67001.1; 23-JUL-2003. **EV EI183; EMBL; -; AAO67014.1; 23-JUL-2003. **EV EI184; EMBL; -; AAO67027.1; 23-JUL-2003. **EV EI185; EMBL; -; AAO67040.1; 23-JUL-2003. **EV EI186; EMBL; -; AAO67053.1; 23-JUL-2003. **EV EI187; EMBL; -; AAO67066.1; 23-JUL-2003. **EV EI188; EMBL; -; AAO67079.1; 23-JUL-2003. **EV EI189; EMBL; -; AAO67091.1; 23-JUL-2003. **EV EI190; EMBL; -; AAO67104.1; 23-JUL-2003. **EV EI191; EMBL; -; AAO67117.1; 23-JUL-2003. **EV EI192; EMBL; -; AAO67130.1; 23-JUL-2003. **EV EI193; EMBL; -; AAO67156.1; 23-JUL-2003. **EV EI194; EMBL; -; AAO67169.1; 23-JUL-2003. **EV EI195; EMBL; -; AAO67182.1; 23-JUL-2003. **EV EI196; EMBL; -; AAO67195.1; 23-JUL-2003. **EV EI197; EMBL; -; AAO67208.1; 23-JUL-2003. **EV EI198; EMBL; -; AAO67221.1; 23-JUL-2003. **EV EI199; EMBL; -; AAO67234.1; 23-JUL-2003. **EV EI200; EMBL; -; AAP47899.1; 14-JUL-2003. **EV EI201; EMBL; -; AAP47912.1; 14-JUL-2003. **EV EI202; EMBL; -; AAP47925.1; 14-JUL-2003. **EV EI203; EMBL; -; AAP47938.1; 14-JUL-2003. **EV EI204; EMBL; -; AAP47951.1; 14-JUL-2003. **EV EI205; EMBL; -; AAP47964.1; 14-JUL-2003. **EV EI206; EMBL; -; AAP47977.1; 14-JUL-2003. **EV EI207; EMBL; -; AAP47990.1; 14-JUL-2003. **EV EI208; EMBL; -; AAP48003.1; 14-JUL-2003. **EV EI209; EMBL; -; AAP48016.1; 14-JUL-2003. **EV EI210; EMBL; -; AAP48029.1; 14-JUL-2003. **EV EI211; EMBL; -; AAP48042.1; 14-JUL-2003. **EV EI212; EMBL; -; AAP48055.1; 14-JUL-2003. **EV EI213; EMBL; -; AAP48068.1; 14-JUL-2003. **EV EI214; EMBL; -; AAP48081.1; 14-JUL-2003. **EV EI215; EMBL; -; AAP48094.1; 14-JUL-2003. **EV EI216; EMBL; -; AAP48107.1; 14-JUL-2003. **EV EI217; EMBL; -; AAP48120.1; 14-JUL-2003. **EV EI218; EMBL; -; AAP48133.1; 14-JUL-2003. **EV EI219; EMBL; -; AAP48146.1; 14-JUL-2003. **EV EI220; EMBL; -; AAP48159.1; 14-JUL-2003. **EV EI221; EMBL; -; AAP48185.1; 14-JUL-2003. **EV EI222; EMBL; -; AAP48198.1; 14-JUL-2003. **EV EI223; EMBL; -; AAP48211.1; 14-JUL-2003. **EV EI224; EMBL; -; AAP48224.1; 14-JUL-2003. **EV EI225; EMBL; -; AAP48237.1; 14-JUL-2003. **EV EI226; EMBL; -; AAP48250.1; 14-JUL-2003. **EV EI227; EMBL; -; AAP48263.1; 14-JUL-2003. **EV EI228; EMBL; -; AAP48276.1; 14-JUL-2003. **EV EI229; EMBL; -; AAP48289.1; 14-JUL-2003. **EV EI230; EMBL; -; AAP48302.1; 14-JUL-2003. **EV EI231; EMBL; -; AAP48315.1; 14-JUL-2003. **EV EI232; EMBL; -; AAP48328.1; 14-JUL-2003. **EV EI233; EMBL; -; AAP48341.1; 14-JUL-2003. **EV EI234; EMBL; -; AAP48354.1; 14-JUL-2003. **EV EI235; EMBL; -; AAP48367.1; 14-JUL-2003. **EV EI236; EMBL; -; AAP48380.1; 14-JUL-2003. **EV EI237; EMBL; -; AAP48393.1; 14-JUL-2003. **EV EI238; EMBL; -; AAP48406.1; 14-JUL-2003. **EV EI239; EMBL; -; AAP48419.1; 14-JUL-2003. **EV EI240; EMBL; -; AAP48431.1; 14-JUL-2003. **EV EI241; EMBL; -; AAP48444.1; 14-JUL-2003. **EV EI242; EMBL; -; AAP48457.1; 14-JUL-2003. **EV EI243; EMBL; -; AAP48470.1; 14-JUL-2003. **EV EI244; EMBL; -; AAP48509.1; 14-JUL-2003. **EV EI245; EMBL; -; AAP48522.1; 14-JUL-2003. **EV EI246; EMBL; -; AAP48535.1; 14-JUL-2003. **EV EI247; EMBL; -; AAP48548.1; 14-JUL-2003. **EV EP248; TrEMBL; -; AAK17889.2; 26-APR-2001. **EV EP249; Merge; -; -; 18-JUN-2003. **ID XXXX_HUMAN **PM ProDom; PD000382; CytC_oxdse_III; 6; 260; T; 14-APR-2003; **PM Pfam; PF00510; COX3; 6; 260; T; 06-NOV-2003; **PM PROSITE; PS50253; COX3; 4; 260; T; 07-NOV-2003; **PM TIGRFAMs; TIGR01732; tiny_TM_bacill; 190; 215; T; 23-OCT-2003; SQ SEQUENCE 260 AA; 29864 MW; 1385EF748B7C1488 CRC64; MTHQSHAYHM VKPSPWPLTG ALSALLMTSG LAMWFHFHSM TLLMLGLLTN TLTMYQWWRD VTRESTYQGH HTPPVQKGLR YGMILFITSE VFFFAGFFWA FYHSSLAPTP QLGGHWPPTG ITPLNPLEVP LLNTSVLLAS GVSITWAHHS LMENNRNQMI QALLITILLG LYFTLLQASE YFESPFTISD GIYGSTFFVA TGFHGLHVII GSTFLTICFI RQLMFHFTSK HHFGFEAAAW YWHFVDVVWL FLYVSIYWWG // ID 3BHS_BOVIN STANDARD; PRT; 372 AA. AC P14893; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE 3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase (3Beta-HSD) DE [Includes: 3-beta-hydroxy-delta(5)-steroid dehydrogenase DE (EC 1.1.1.145) (3-beta-hydroxy-5-ene steroid dehydrogenase) DE (Progesterone reductase); Steroid delta-isomerase (EC 5.3.3.1) (Delta- DE 5-3-ketosteroid isomerase)]. GN HSD3B. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Ovary; RX MEDLINE=90092517; PubMed=2599102; RA Zhao H.-F., Simard J., Labrie C., Breton N., Rheaume E., Luu-The V., RA Labrie F.; RT "Molecular cloning, cDNA structure and predicted amino acid sequence RT of bovine 3 beta-hydroxy-5-ene steroid dehydrogenase/delta 5-delta 4 RT isomerase."; RL FEBS Lett. 259:153-157(1989). RN [2] RP PARTIAL SEQUENCE, AND CD STUDIES. RC TISSUE=Adrenal gland; RX MEDLINE=91329389; PubMed=1868086; RA Rutherfurd K.J., Chen S., Shively J.E.; RT "Isolation and amino acid sequence analysis of bovine adrenal 3 beta- RT hydroxysteroid dehydrogenase/steroid isomerase."; RL Biochemistry 30:8108-8116(1991). CC -!- FUNCTION: 3beta-HSD is a bifunctional enzyme, that catalyzes the CC oxidative conversion of delta(5)-ene-3-beta-hydroxy steroid, and CC the oxidative conversion of ketosteroids. The 3beta-HSD enzymatic CC system plays a crucial role in the biosynthesis of all classes of CC hormonal steroids. CC -!- CATALYTIC ACTIVITY: 3-beta-hydroxy-delta(5)-steroid + NAD(+) = 3- CC oxo-delta(5)-steroid + NADH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-delta(5)-steroid = a 3-oxo-delta(4)- CC steroid. CC -!- PATHWAY: Steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum and mitochondrial CC membrane-bound protein. CC -!- SIMILARITY: Belongs to the 3beta-HSD family. DR EMBL; X17614; CAA35615.1; -. DR PIR; S07102; DEBOHS. DR InterPro; IPR002225; 3Beta_HSD. DR Pfam; PF01073; 3Beta_HSD; 1. KW Steroidogenesis; Oxidoreductase; NAD; Isomerase; Mitochondrion; KW Multifunctional enzyme; Transmembrane; Endoplasmic reticulum; KW Direct protein sequencing. FT INIT_MET 0 0 FT TRANSMEM 74 91 0 (Potential). FT TRANSMEM 287 305 Potential. FT NP_BIND 5 36 NAD (Potential). FT CONFLICT 141 219 AKLRKELVETSEVRKAVSIETALEHKVVNGNSADAAYAQVE FT IQPRANIQLDFPELKPYKQVKQIAPAELEGLLDLERVI -> FT CLNCVKSWLKLLKLERQFPSKLLWSIRLSMAIALMLHMLKS FT KFNQELTFNWTSQNRNHTNRLNKLLPLSLRVCWIWKELF FT (in Ref. 1). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 372 AA; 42088 MW; 5B8481DEEA5807BC CRC64; AGWSCLVTGG GGFLGQRIIC LLVEEKDLQE IRVLDKVFRP EVREEFSKLQ SKIKLTLLEG DILDEQCLKG ACQGTSVVIH TASVIDVRNA VPRETIMNVN VKGTQLLLEA CVQASVPVFI HTSTIEVAGP NSYREIIQDG REEEHHESAW SSPYPYSKKL AEKAVLGANG WALKNGGTLY TCALRPMYIY GEGSPFLSAY MHGALNNNGI LTNHCKFSRV NPVYVGNVAW AHILALRALR DPKKVPNIQG QFYYISDDTP HQSYDDLNYT LSKEWGFCLD SRMSLPISLQ YWLAFLLEIV SFLLSPIYKY NPCFNRHLVT LSNSVFTFSY KKAQRDLGYE PLYTWEEAKQ KTKEWIGSLV KQHKETLKTK IH // ID CBP1_HORVU STANDARD; PRT; 499 AA. AC P07519; P07520; DT 01-APR-1988 (Rel. 07, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Serine carboxypeptidase I precursor (EC 3.4.16.5) (Carboxypeptidase C) DE (CP-MI). GN Name=CBP1; Synonyms=CXP;1; OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; Pooideae; OC Triticeae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Aleurone; RA Rocher A., Lok F., Cameron-Mills V., von Wettstein D.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 88-499 FROM N.A. RX MEDLINE=88298749; PubMed=3403516; RA Doan N.P., Fincher G.B.; RT "The A- and B-chains of carboxypeptidase I from germinated barley RT originate from a single precursor polypeptide."; RL J. Biol. Chem. 263:11106-11110(1988). RN [3] RP SEQUENCE OF 31-296 AND 352-499. ** MEDLINE=None; PubMed=None; RA Soerensen S.B., Breddam K., Svendsen I.; RT "Primary structure of carboxypeptidase I from malted barley."; RL Carlsberg Res. Commun. 51:475-485(1986). CC -!- FUNCTION: May be involved in the degradation of small peptides (2- CC 5 residues) or in the degradation of storage proteins in the CC embryo. CC -!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with a CC broad specificity. CC -!- SUBUNIT: Carboxypeptidase I is a dimer, where each monomer is CC composed of two chains linked by disulfide bonds. CC -!- SUBCELLULAR LOCATION: Secreted into the endosperm. CC -!- DEVELOPMENTAL STAGE: After one day of germination, mainly found in CC the scutellum of the developing grain; barely detectable after CC four days, and absent from the mature grain. A lower level of CC expression is seen in the aleurone both during development and CC germination. CC -!- PTM: Three disulfide bonds are present. CC -!- PTM: The linker peptide is endoproteolytically excised during CC enzyme maturation. CC -!- SIMILARITY: Belongs to peptidase family S10. DR EMBL; Y09603; CAA70816.1; -. DR EMBL; J03897; AAA32940.1; -. DR PIR; T05367; CPBHS. DR HSSP; P08819; 1WHT. DR MEROPS; S10.004; -. DR InterPro; IPR001563; Peptidase_S10. DR InterPro; IPR000379; Ser_estrs. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR ProDom; PD001189; Serine_carbpept; 2. DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. KW Hydrolase; Carboxypeptidase; Glycoprotein; Zymogen; Signal; KW Direct protein sequencing. FT SIGNAL 1 30 Potential. FT CHAIN 31 296 Serine carboxypeptidase I chain A. FT PROPEP 297 351 Linker peptide. FT CHAIN 352 499 Serine carboxypeptidase I chain B. FT ACT_SITE 188 188 By similarity. FT ACT_SITE 423 423 By similarity. FT ACT_SITE 476 476 By similarity. FT SITE 497 499 Microbody targeting signal (Potential). FT CARBOHYD 148 148 N-linked (GlcNAc...). FT CARBOHYD 262 262 N-linked (GlcNAc...). FT CARBOHYD 407 407 N-linked (GlcNAc...). FT CONFLICT 102 102 H -> P (in Ref. 3). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 499 AA; 54096 MW; 9C6674B14D9DB9BF CRC64; MARCRRRSGC TAGAALLLLL ALALSGGGGA APQGAEVTGL PGFDGALPSK HYAGYVTVDE GHGRNLFYYV VESERDPGKD PVVLWLNGGP GCSSFDGFVY EHGPFNFESG GSVKSLPKLH LNPYAWSKVS TMIYLDSPAG VGLSYSKNVS DYETGDLKTA TDSHTFLLKW FQLYPEFLSN PFYIAGESYA GVYVPTLSHE VVKGIQGGAK PTINFKGYMV GNGVCDTIFD GNALVPFAHG MGLISDEIYQ QASTSCHGNY WNATDGKCDT AISKIESLIS GLNIYDILEP CYHSRSIKEV NLQNSKLPQS FKDLGTTNKP FPVRTRMLGR AWPLRAPVKA GRVPSWQEVA SGVPCMSDEV ATAWLDNAAV RSAIHAQSVS AIGPWLLCTD KLYFVHDAGS MIAYHKNLTS QGYRAIIFSG DHDMCVPFTG SEAWTKSLGY GVVDSWRPWI TNGQVSGYTE GYEHGLTFAT IKGAGHTVPE YKPQEAFAFY SRWLAGSKL // ID YCXD_CYAPA STANDARD; PRT; 244 AA. AC P48334; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 29-MAR-2004 (Rel. 43, Last annotation update) DE Probable ABC transporter ATP-binding protein in ycf23-apcF intergenic DE region (ORF244). OS Cyanophora paradoxa. OG Cyanelle. OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora. OX NCBI_TaxID=2762; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=UTEX LB 555 / Pringsheim; ** MEDLINE=None; PubMed=None; RA Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J., RA Bryant D.A.; RT "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa."; RL Plant Mol. Biol. Rep. 13:327-332(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=UTEX LB 555 / Pringsheim; RA Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M., RA Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., RA Steiner J.M., Jakowitsch J., Bohnert H.J., Bryant D.A.; RT "The complete sequence of the cyanelle genome of Cyanophora paradoxa: RT the genetic complexity of a primitive plastid."; RL (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., RL Schwemmler W. (eds.); RL Eukaryotism and Symbiosis, pp.40-48, Springer-Verlag, Heidelberg RL (1997). CC -!- SUBCELLULAR LOCATION: Cyanelle. CC -!- SIMILARITY: Belongs to the ABC transporter family. DR EMBL; U30821; AAA81304.1; -. DR PIR; T06961; T06961. DR HSSP; P58301; 1F2T. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR003439; ABC_transporter. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. KW Hypothetical protein; ATP-binding; Transport; Cyanelle. FT NP_BIND 41 48 ATP (Potential). ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 244 AA; 27747 MW; 4C5B357FF9C55D3B CRC64; MFYTLPKQLE INNLTVSYPH GTVLQNIFLT IESGKLIGII GPNGAGKSTL LKTIIEQIKP ISGEIFYQGA PLKNQRARIG YVPQRAQVDW DFPINVWDVV MMARLKKIGW FSSYSKKSYE CVKAALEKVD MLKYKDRNIR ELSGGQQQRV FLARLLAQEA DLLLLDEPFT GVDFQTQKII FSLLKEQIAS NKIVIVIHHD LGESIINFDE LILLNKKIIS HDLTTKILNS KKLSTLFGEH IYAN // ID CYC_ARUMA STANDARD; PRT; 111 AA. AC P00065; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Cytochrome c. OS Arum maculatum (Cuckoo-pint). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Araceae; Arum. OX NCBI_TaxID=4458; RN [1] RP SEQUENCE. RA Boulter D.; ** /NO TITLE. RL Unpublished results, cited by: RL Dickerson R.E., Timkovich R.; RL (In) Boyer P.D. (eds.); RL The enzymes (3rd ed.), pp.11:397-547, Academic Press, New York (1975). CC -!- FUNCTION: Electron carrier protein. The oxidized form of the CC cytochrome c heme group can accept an electron from the heme group CC of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c CC then transfers this electron to the cytochrome oxidase complex, CC the final protein carrier in the mitochondrial electron-transport CC chain. CC -!- SUBCELLULAR LOCATION: Mitochondrial matrix. CC -!- PTM: Binds 1 heme group per subunit. CC -!- SIMILARITY: Belongs to the cytochrome c family. DR PIR; A00057; CCRM. DR HSSP; P00055; 1CCR. DR InterPro; IPR000345; CytC_heme_BS. DR InterPro; IPR009056; Cytochrome_c. DR InterPro; IPR003088; Cyt_CI. DR InterPro; IPR002327; Cyt_CIAB. DR Pfam; PF00034; Cytochrom_C; 1. DR PRINTS; PR00604; CYTCHRMECIAB. DR ProDom; PD000375; Cyt_CIAB; 1. DR PROSITE; PS00190; CYTOCHROME_C; 1. KW Mitochondrion; Electron transport; Respiratory chain; Heme; KW Acetylation; Direct protein sequencing. FT METAL 26 26 Iron (heme axial ligand). FT METAL 88 88 Iron (heme axial ligand). FT BINDING 22 22 Heme (covalent). FT BINDING 25 25 Heme (covalent). FT MOD_RES 1 1 N-acetylalanine. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 111 AA; 12020 MW; 6F7C201451D52E47 CRC64; ASFAEAPPGN PKAGEKIFKT KCAQCHTVEK GAGHKQGPNL NGLFGRQSGT TAGYSYSAAN KNMAVIWEES TLYDYLLNPX KYIPGTKMVF PGLXKPQERA DLIAYLKEST A // ID TAP2_HUMAN STANDARD; PRT; 686 AA. AC Q03519; Q9UQ83; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Antigen peptide transporter 2 (APT2) (Peptide transporter TAP2) DE (Peptide transporter PSF2) (Peptide supply factor 2) (PSF-2) (Peptide DE transporter involved in antigen processing 2). GN Name=TAP2; Synonyms=ABCB3, PSF2, RING11, Y1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (TAP2*0101). RX MEDLINE=93085727; PubMed=1453454; RA Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., RA Trowsdale J.; RT "DNA sequence analysis of 66 kb of the human MHC class II region RT encoding a cluster of genes for antigen processing."; RL J. Mol. Biol. 228:433-441(1992). RN [2] RP SEQUENCE FROM N.A. (TAP2*0101/TAP2*0201). RX MEDLINE=92159069; PubMed=1741401; RA Powis S.H., Mockridge I., Kelly A., Kerr L.-A., Glynne R.J., RA Gileadi U., Beck S., Trowsdale J.; RT "Polymorphism in a second ABC transporter gene located within the RT class II region of the human major histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 89:1463-1467(1992). RN [3] RP SEQUENCE FROM N.A. (TAP2*0201). RX MEDLINE=92052217; PubMed=1946428; RA Bahram S., Arnold D., Bresnahan M., Strominger J.L., Spies T.; RT "Two putative subunits of a peptide pump encoded in the human major RT histocompatibility complex class II region."; RL Proc. Natl. Acad. Sci. U.S.A. 88:10094-10098(1991). RN [4] RP SEQUENCE FROM N.A. (TAP2*0102). RX MEDLINE=93154779; PubMed=8428770; RA Powis S.H., Tonks S., Mockridge I., Kelly A.P., Bodmer J.G., RA Trowsdale J.; RT "Alleles and haplotypes of the MHC-encoded ABC transporters TAP1 and RT TAP2."; RL Immunogenetics 37:373-380(1993). RN [5] RP SEQUENCE FROM N.A. (TAP2*0101). RX MEDLINE=96144827; PubMed=8568858; RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., RA Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., RA Radley E., Thorpe K.L., Trowsdale J.; RT "Evolutionary dynamics of non-coding sequences within the class II RT region of the human MHC."; RL J. Mol. Biol. 255:1-13(1996). RN [6] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [7] RP SEQUENCE OF 65-686 FROM N.A. (TAP2*0103). RC TISSUE=Blood; RX MEDLINE=95313033; PubMed=7792761; RA Cano P., Baxter-Lowe L.A.; RT "Novel human TAP2*103 allele shows further polymorphism in the ATP- RT binding domain."; RL Tissue Antigens 45:139-142(1995). RN [8] RP SEQUENCE OF 204-686 FROM N.A., AND VARIANTS THR-374 AND ILE-467. RA Tang J., Allen S., Karita E., Musonda R., Kaslow R.A.; RT "New TAP2 polymorphisms in Africans."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP SEQUENCE OF 517-645 FROM N.A. (TAP2*0101/TAP2*0102). RA Singal D.P., Ye M., D'Souza M.; RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases. RN [10] RP SEQUENCE OF 517-645 FROM N.A. (TAP2*0101/TAP2*0102). RX MEDLINE=94215245; PubMed=8162639; RA Singal D.P., Ye M., Qiu X., D'Souza M.; RT "Polymorphisms in the TAP2 gene and their association with rheumatoid RT arthritis."; RL Clin. Exp. Rheumatol. 12:29-33(1994). RN [11] RP PEPTIDE-BINDING SITE. RX PubMed=8955196; RA Nijenhuis M., Hammerling G.J.; RT "Multiple regions of the transporter associated with antigen RT processing (TAP) contribute to its peptide binding site."; RL J. Immunol. 157:5467-5477(1996). RN [12] RP INHIBITION BY ICP47. RX PubMed=8670825; RA Ahn K., Meyer T.H., Uebel S., Sempe P., Djaballah H., Yang Y., RA Peterson P.A., Frueh K., Tampe R.; RT "Molecular mechanism and species specificity of TAP inhibition by RT herpes simplex virus ICP47."; RL EMBO J. 15:3247-3255(1996). RN [13] RP INHIBITION BY US6 GLYCOPROTEIN. RX PubMed=9175839; RA Ahn K., Gruhler A., Galocha B., Jones T.R., Wiertz E.J.H.J., RA Ploegh H.L., Peterson P.A., Yang Y., Frueh K.; RT "The ER-luminal domain of the HCMV glycoprotein US6 inhibits peptide RT translocation by TAP."; RL Immunity 6:613-621(1997). RN [14] RP INHIBITION BY US6 GLYCOPROTEIN. RX PubMed=11157746; RA Hewitt E.W., Gupta S.S., Lehner P.J.; RT "The human cytomegalovirus gene product US6 inhibits ATP binding by RT TAP."; RL EMBO J. 20:387-396(2001). RN [15] RP INHIBITION BY E3-19K GLYCOPROTEIN. RX PubMed=10227971; RA Bennett E.M., Bennink J.R., Yewdell J.W., Brodsky F.M.; RT "Cutting edge: adenovirus E19 has two mechanisms for affecting class I RT MHC expression."; RL J. Immunol. 162:5049-5052(1999). RN [16] RP VARIANTS ILE-379 AND ALA-665. RX MEDLINE=92237283; PubMed=1570316; RA Colonna M., Bresnahan M., Bahram S., Strominger J.L., Spies T.; RT "Allelic variants of the human putative peptide transporter involved RT in antigen processing."; RL Proc. Natl. Acad. Sci. U.S.A. 89:3932-3936(1992). RN [17] RP VARIANT TAP2*BKY2 VAL-577. RX MEDLINE=97464203; PubMed=9324024; RA Kumagai S., Kanagawa S., Morinobu A., Takada M., Nakamura K., RA Sugai S., Maruya E., Saji H.; RT "Association of a new allele of the TAP2 gene, TAP2*Bky2 (Val577), RT with susceptibility to Sjogren's syndrome."; RL Arthritis Rheum. 40:1685-1692(1997). RN [18] RP VARIANTS THR-374; ILE-379; ILE-467; SER-513 THR-565; CYS-651; ALA-665 RP AND GLN-GLU-GLY-GLN-ASP-LEU-TYR-SER-ARG-LEU-VAL-GLN-GLN-ARG-LEU-MET- RP ASP-686 INS, AND DEFINITION OF ALLELES. RX MEDLINE=21190086; PubMed=11294565; DOI=10.1038/sj/gene/6363731; RA Tang J., Freedman D.O., Allen S., Karita E., Musonda R., Braga C., RA Jamieson B.D., Louie L., Kaslow R.A.; RT "Genotyping TAP2 variants in North American Caucasians, Brazilians, RT and Africans."; RL Genes Immun. 2:32-40(2001). CC -!- FUNCTION: Involved in the transport of antigens from the cytoplasm CC to the endoplasmic reticulum for association with MHC class I CC molecules. Also acts as a molecular scaffold for the final stage CC of MHC class I folding, namely the binding of peptide. Nascent MHC CC class I molecules associate with TAP via tapasin. Inhibited by the CC covalent attachment of herpes simplex virus ICP47 protein, which CC blocks the peptide-binding site of TAP. Inhibited by human CC cytomegalovirus US6 glycoprotein, which binds to the lumenal side CC of the TAP complex and inhibits peptide translocation by CC specifically blocking ATP-binding to TAP1 and prevents the CC conformational rearrangement of TAP induced by peptide binding. CC Inhibited by human adenovirus E3-19K glycoprotein, which binds the CC TAP complex and acts as a tapasin inhibitor, preventing MHC class CC I/TAP association. CC -!- SUBUNIT: Heterodimer of TAP1 and TAP2. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. Endoplasmic CC reticulum. The transmembrane segments seem to form a pore in the CC membrane. CC -!- INDUCTION: By interferon gamma. CC -!- DOMAIN: The peptide-binding site is shared between the cytoplasmic CC loops of TAP1 and TAP2. CC -!- POLYMORPHISM: 4 common alleles are officially recognized: CC TAP2*0101 (TAP2A or PSF2A or RING11A), TAP2*0102 (TAP2E), CC TAP2*0103 (TAP2F), and TAP2*0201 (TAP2B or PSF2B or RING11B). CC Other relatively common alleles have been identified: TAP2*01D, CC TAP2*01E, TAP2*01F, TAP2*01G, TAP2*01H, TAP2*02B, TAP2*02C CC (TAP2*0202), TAP2*02D, TAP2*02E, TAP2*02F, TAP2*03A and TAP2*04A. CC The sequence shown is that of TAP2*0101. CC -!- POLYMORPHISM: The allele TAP2*Bky2 is commonly found only in the CC Japanese population. It may be associated with susceptibility to CC Sjoegren's syndrome, an autoimmune disorder characterized by CC abnormal dryness of the conjunctiva, cornea and mouth due to CC exocrine glands dysfunction. CC -!- SIMILARITY: Belongs to the ABC transporter family. MDR subfamily. DR EMBL; X66401; CAA47027.1; -. DR EMBL; M84748; -; NOT_ANNOTATED_CDS. DR EMBL; M74447; AAA59841.1; -. DR EMBL; Z22935; CAA80522.1; -. DR EMBL; Z22936; CAA80523.1; -. DR EMBL; X87344; CAA60788.1; -. DR EMBL; U07844; AAA79901.1; -. DR EMBL; BC002751; AAH02751.1; -. DR EMBL; AF100418; AAD23381.1; -. DR EMBL; AF100415; AAD23381.1; JOINED. DR EMBL; AF100416; AAD23381.1; JOINED. DR EMBL; AF100417; AAD23381.1; JOINED. DR EMBL; L09191; AAA58648.1; -. DR EMBL; L10287; AAA58649.1; -. DR PIR; B41538; B41538. DR HSSP; Q03518; 1JJ7. DR HGNC; HGNC:44; TAP2. DR MIM; 170261; -. DR GO; GO:0005829; C:cytosol; NAS. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IMP. DR GO; GO:0016021; C:integral to membrane; NAS. DR GO; GO:0042825; C:TAP complex; NAS. DR GO; GO:0005524; F:ATP binding; NAS. DR GO; GO:0004409; F:homoaconitate hydratase activity; NAS. DR GO; GO:0042288; F:MHC class I protein binding; NAS. DR GO; GO:0042605; F:peptide antigen binding; NAS. DR GO; GO:0015433; F:peptide antigen transporter activity; NAS. DR GO; GO:0042301; F:phosphate binding; NAS. DR GO; GO:0046982; F:protein heterodimerization activity; IPI. DR GO; GO:0046980; F:tapasin binding; IPI. DR GO; GO:0048004; P:antigen presentation, endogenous peptide an...; NAS. DR GO; GO:0019885; P:antigen processing, endogenous antigen via ...; NAS. DR GO; GO:0046967; P:cytosol to ER transport; NAS. DR GO; GO:0006886; P:intracellular protein transport; IMP. DR GO; GO:0015833; P:peptide transport; NAS. DR GO; GO:0006461; P:protein complex assembly; NAS. DR InterPro; IPR003593; AAA_ATPase. DR InterPro; IPR001140; ABC_TM_transpt. DR InterPro; IPR003439; ABC_transporter. DR InterPro; IPR005293; Ag_transporter2. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR ProDom; PD000006; ABC_transporter; 1. DR SMART; SM00382; AAA; 1. DR TIGRFAMs; TIGR00958; 3a01208; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. KW Immune response; Transport; Peptide transport; Endoplasmic reticulum; KW ATP-binding; Transmembrane; Polymorphism. FT TOPO_DOM 1 6 Lumenal (Potential). FT TRANSMEM 7 27 1 (Potential). FT TOPO_DOM 28 56 Cytoplasmic (Potential). FT TRANSMEM 57 77 2 (Potential). FT TOPO_DOM 78 98 Lumenal (Potential). FT TRANSMEM 99 119 3 (Potential). FT TOPO_DOM 120 148 Cytoplasmic (Potential). FT TRANSMEM 149 169 4 (Potential). FT TOPO_DOM 170 187 Lumenal (Potential). FT TRANSMEM 188 208 5 (Potential). FT TOPO_DOM 209 266 Cytoplasmic (Potential). FT TRANSMEM 267 287 6 (Potential). FT TOPO_DOM 288 293 Lumenal (Potential). FT TRANSMEM 294 314 7 (Potential). FT TOPO_DOM 315 374 Cytoplasmic (Potential). FT TRANSMEM 375 395 8 (Potential). FT TOPO_DOM 396 408 Lumenal (Potential). FT TRANSMEM 409 429 9 (Potential). FT TOPO_DOM 430 686 Cytoplasmic (Potential). FT NP_BIND 503 510 ATP (Potential). FT REGION 301 389 Involved in peptide-binding site. FT REGION 414 433 Involved in peptide-binding site. FT REGION 468 686 ABC transporter. FT VARIANT 374 374 A -> T (in allele TAP2*01F, allele FT TAP2*01G, allele TAP2*01H, allele FT TAP2*02B and allele TAP2*02D). FT /FTId=VAR_014997. FT VARIANT 379 379 V -> I (in allele TAP2*01D, allele FT TAP2*01E, allele TAP2*01G, allele FT TAP2*02C and allele TAP2*02F; FT dbSNP:1800454). FT /FTId=VAR_000094. FT VARIANT 467 467 V -> I (in allele TAP2*01F and allele FT TAP2*02D). FT /FTId=VAR_014998. FT VARIANT 513 513 A -> S (rare polymorphism). FT /FTId=VAR_014999. FT VARIANT 565 565 A -> T (in allele TAP2*0102, allele FT TAP2*01D, allele TAP2*02E and allele FT TAP2*02F). FT /FTId=VAR_000095. FT VARIANT 577 577 M -> V (in allele TAP2*BKY2). FT /FTId=VAR_015000. FT VARIANT 651 651 R -> C (in allele TAP2*0103 and allele FT TAP2*01G). FT /FTId=VAR_000096. FT VARIANT 665 665 T -> A (in allele TAP2*0201, allele FT TAP2*02B, allele TAP2*02C, allele FT TAP2*02D, allele TAP2*02E, allele FT TAP2*02F, allele TAP2*04A and allele FT TAP2*Bky2; dbSNP:241447). FT /FTId=VAR_000097. FT VARIANT 686 686 L -> LQEGQDLYSRLVQQRLMD (in allele FT TAP2*0201, allele TAP2*02B, allele FT TAP2*02C, allele TAP2*02D, allele FT TAP2*02E, allele TAP2*02F, allele FT TAP2*03A and allele TAP2*Bky2). FT /FTId=VAR_000098. ** ** ################# INTERNAL SECTION ################## **CL 6p21.3; **ZB CHH, 8-JAN-2004; SQ SEQUENCE 686 AA; 75664 MW; E7E4A7F6A2A3B48B CRC64; MRLPDLRPWT SLLLVDAALL WLLQGPLGTL LPQGLPGLWL EGTLRLGGLW GLLKLRGLLG FVGTLLLPLC LATPLTVSLR ALVAGASRAP PARVASAPWS WLLVGYGAAG LSWSLWAVLS PPGAQEKEQD QVNNKVLMWR LLKLSRPDLP LLVAAFFFLV LAVLGETLIP HYSGRVIDIL GGDFDPHAFA SAIFFMCLFS FGSSLSAGCR GGCFTYTMSR INLRIREQLF SSLLRQDLGF FQETKTGELN SRLSSDTTLM SNWLPLNANV LLRSLVKVVG LYGFMLSISP RLTLLSLLHM PFTIAAEKVY NTRHQEVLRE IQDAVARAGQ VVREAVGGLQ TVRSFGAEEH EVCRYKEALE QCRQLYWRRD LERALYLLVR RVLHLGVQML MLSCGLQQMQ DGELTQGSLL SFMIYQESVG SYVQTLVYIY GDMLSNVGAA EKVFSYMDRQ PNLPSPGTLA PTTLQGVVKF QDVSFAYPNR PDRPVLKGLT FTLRPGEVTA LVGPNGSGKS TVAALLQNLY QPTGGQVLLD EKPISQYEHC YLHSQVVSVG QEPVLFSGSV RNNIAYGLQS CEDDKVMAAA QAAHADDFIQ EMEHGIYTDV GEKGSQLAAG QKQRLAIARA LVRDPRVLIL DEATSALDVQ CEQALQDWNS RGDRTVLVIA HRLQTVQRAH QILVLQEGKL QKLAQL // ID CIN5_HUMAN STANDARD; PRT; 2016 AA. AC Q14524; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-JUN-2004 (Rel. 44, Last annotation update) DE Sodium channel protein type V alpha subunit (Voltage-gated sodium DE channel alpha subunit Nav1.5) (Sodium channel protein, cardiac muscle DE alpha-subunit) (HH1). GN Name=SCN5A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Heart; RX MEDLINE=92115699; PubMed=1309946; RA Gellens M.E., George A.L. Jr., Chen L.Q., Chahine M., Horn R., RA Barchi R.L., Kallen R.G.; RT "Primary structure and functional expression of the human cardiac RT tetrodotoxin-insensitive voltage-dependent sodium channel."; RL Proc. Natl. Acad. Sci. U.S.A. 89:554-558(1992). RN [2] RP VARIANTS LQT3. RX MEDLINE=95196273; PubMed=7889574; RA Wang Q., Shen J., Splawski I., Atkinson D., Li Z., Robinson J.L., RA Moss A.J., Towbin J.A., Keating M.T.; RT "SCN5A mutations associated with an inherited cardiac arrhythmia, long RT QT syndrome."; RL Cell 80:805-811(1995). RN [3] RP VARIANTS LQT3. RX MEDLINE=96081224; PubMed=8541846; RA Wang Q., Shen J., Li Z., Timothy K.W., Vincent G.M., Priori S.G., RA Schwartz P.J., Keating M.T.; RT "Cardiac sodium channel mutations in patients with long QT syndrome, RT an inherited cardiac arrhythmia."; RL Hum. Mol. Genet. 4:1603-1607(1995). RN [4] RP VARIANT LQT3 1505-LYS--GLN-1507 DEL. RX MEDLINE=95379949; PubMed=7651517; RA Bennett P.B., Yazawa K., Makita N., George A.L. Jr.; RT "Molecular mechanism for an inherited cardiac arrhythmia."; RL Nature 376:683-685(1995). RN [5] RP VARIANT LQT3 GLY-1790. RX MEDLINE=98349542; PubMed=9686753; RA An R.H., Wang X.L., Kerem B., Benhorin J., Medina A., Goldmit M., RA Kass R.S.; RT "Novel LQT-3 mutation affects Na+ channel activity through RT interactions between alpha- and beta1-subunits."; RL Circ. Res. 83:141-146(1998). RN [6] RP VARIANT LQT3 GLN-1623. RX MEDLINE=98165676; PubMed=9506831; RA Makita N., Shirai N., Nagashima M., Matsuoka R., Yamada Y., Tohse N., RA Kitabatake A.; RT "A de novo missense mutation of human cardiac Na(+) channel exhibiting RT novel molecular mechanisms of long QT syndrome."; RL FEBS Lett. 423:5-9(1998). RN [7] RP VARIANT LQT3 GLY-1839. ** MEDLINE=None; PubMed=None; RA Benhorin J., Goldmit M., Maccluer J.W., Blangero J., Goffen R., RA Leibovitch A., Rahat A., Wang Q., Medina A., Towbin J.A., Kerem B.; RT "Identification of a new SCN5A mutation, D1840G, associated with the RT long QT syndrome."; RL Hum. Mutat. 12:72-72(1998). RN [8] RP VARIANT LQT3 GLN-1623. ** MEDLINE=None; PubMed=None; RA Yamagishi H., Furutani M., Kamisago M., Morikawa Y., Kojima Y., RA Hino Y., Furutani Y., Kimura M., Imamura S.-I., Takao A., Momma K., RA Matsuoka R.; RT "A De Novo missense mutation (R1623Q) of the SCN5A gene in a Japanese RT girl with sporadic long QT syndrome."; RL Hum. Mutat. 12:481-481(1998). RN [9] RP VARIANTS BRUGADA SYNDROME TRP-1232 AND MET-1620. RX PubMed=9521325; DOI=10.1038/32675; RA Chen Q., Kirsch G.E., Zhang D., Brugada R., Brugada J., Brugada P., RA Potenza D., Moya A., Borggrefe M., Breithardt G., Ortiz-Lopez R., RA Wang Z., Antzelevitch C., O'Brien R.E., Schulze-Bahr E., Keating M.T., RA Towbin J.A., Wang Q.; RT "Genetic basis and molecular mechanism for idiopathic ventricular RT fibrillation."; RL Nature 392:293-296(1998). RN [10] RP VARIANTS LQT3 MET-1304 AND MET-1645, AND VARIANT ASN-1500. RX MEDLINE=99439526; PubMed=10508990; RA Wattanasirichaigoon D., Vesely M.R., Duggal P., Levine J.C., RA Blume E.D., Wolff G.S., Edwards S.B., Beggs A.H.; RT "Sodium channel abnormalities are infrequent in patients with long QT RT syndrome: identification of two novel SCN5A mutations."; RL Am. J. Med. Genet. 86:470-476(1999). RN [11] RP CHARATERIZATION OF VARIANTS BRUGADA SYNDROME TRP-1512 AND THR-1924. RX PubMed=10690282; RA Rook M.B., Bezzina Alshinawi C., Groenewegen W.A., van Gelder I.C., RA van Ginneken A.C.G., Jongsma H.J., Mannens M.M.A.M., Wilde A.A.M.; RT "Human SCN5A gene mutations alter cardiac sodium channel kinetics and RT are associated with the Brugada syndrome."; RL Cardiovasc. Res. 44:507-517(1999). RN [12] RP VARIANT LQT3 LYS-1784. RX MEDLINE=99307063; PubMed=10377081; RA Wei J., Wang D.W., Alings M., Fish F., Wathen M., Roden D.M., RA George A.L. Jr.; RT "Congenital long-QT syndrome caused by a novel mutation in a conserved RT acidic domain of the cardiac Na+ channel."; RL Circulation 99:3165-3171(1999). RN [13] RP CHARACTERIZATION OF VARIANT BRUGADA SYNDROME MET-1620. RX PubMed=10532948; RA Dumaine R., Towbin J.A., Brugada P., Vatta M., Nesterenko D.V., RA Nesterenko V.V., Brugada J., Brugada R., Antzelevitch C.; RT "Ionic mechanisms responsible for the electrocardiographic phenotype RT of the Brugada syndrome are temperature dependent."; RL Circ. Res. 85:803-809(1999). RN [14] RP CHARACTERIZATION OF VARIANT LQT3/BRUGADA SYNDROME ASP-1795 INS. RX PubMed=10590249; RA Bezzina C.R., Veldkamp M.W., van Den Berg M.P., Postma A.V., RA Rook M.B., Viersma J.-W., van Langen I.M., Tan-Sindhunata G., RA Bink-Boelkens M.T.E., van Der Hout A.H., Mannens M.M.A.M., RA Wilde A.A.M.; RT "A single Na(+) channel mutation causing both long-QT and Brugada RT syndromes."; RL Circ. Res. 85:1206-1213(1999). RN [15] RP DISEASE. RX PubMed=10471492; DOI=10.1038/12618; RA Schott J.-J., Alshinawi C., Kyndt F., Probst V., Hoorntje T.M., RA Hulsbeek M., Wilde A.A.M., Escande D., Mannens M.M.A.M., Le Marec H.; RT "Cardiac conduction defects associate with mutations in SCN5A."; RL Nat. Genet. 23:20-21(1999). RN [16] RP CHARACTERIZATION OF VARIANT BRUGADA SYNDROME MET-1620. RX PubMed=10618304; RA Makita N., Shirai N., Wang D.W., Sasaki K., George A.L. Jr., Kanno M., RA Kitabatake A.; RT "Cardiac Na(+) channel dysfunction in Brugada syndrome is aggravated RT by beta(1)-subunit."; RL Circulation 101:54-60(2000). RN [17] RP VARIANTS LQT3 ASN-1114; VAL-1501; LEU-1623; HIS-1644 AND ASN-1787. RX MEDLINE=20432616; PubMed=10973849; RA Splawski I., Shen J., Timothy K.W., Lehmann M.H., Priori S., RA Robinson J.L., Moss A.J., Schwartz P.J., Towbin J.A., Vincent G.M., RA Keating M.T.; RT "Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, RT KCNE1, and KCNE2."; RL Circulation 102:1178-1185(2000). RN [18] RP VARIANT IVF LEU-1710. RX PubMed=10940383; RA Akai J., Makita N., Sakurada H., Shirai N., Ueda K., Kitabatake A., RA Nakazawa K., Kimura A., Hiraoka M.; RT "A novel SCN5A mutation associated with idiopathic ventricular RT fibrillation without typical ECG findings of Brugada syndrome."; RL FEBS Lett. 479:29-34(2000). RN [19] RP VARIANT LQT3 ASN-941. RX PubMed=10911008; RA Schwartz P.J., Priori S.G., Dumaine R., Napolitano C., RA Antzelevitch C., Stramba-Badiale M., Richard T.A., Berti M.R., RA Bloise R.; RT "A molecular link between the sudden infant death syndrome and the RT long-QT syndrome."; RL N. Engl. J. Med. 343:262-267(2000). RN [20] RP CHARACTERIZATION OF VARIANTS LQT3 CYS-1795 AND BRUGADA SYNDROME RP HIS-1795. RX PubMed=11410597; DOI=10.1074/jbc.M104471200; RA Rivolta I., Abriel H., Tateyama M., Liu H., Memmi M., Vardas P., RA Napolitano C., Priori S.G., Kass R.S.; RT "Inherited Brugada and long QT-3 syndrome mutations of a single RT residue of the cardiac sodium channel confer distinct channel and RT clinical phenotypes."; RL J. Biol. Chem. 276:30623-30630(2001). RN [21] RP VARIANT SSS1/BRUGADA SYNDROME ARG-1408. RX PubMed=11748104; RA Kyndt F., Probst V., Potet F., Demolombe S., Chevallier J.-C., RA Baro I., Moisan J.-P., Boisseau P., Schott J.-J., Escande D., RA Le Marec H.; RT "Novel SCN5A mutation leading either to isolated cardiac conduction RT defect or Brugada syndrome in a large French family."; RL Circulation 104:3081-3086(2001). RN [22] RP CHARACTERIZATION OF VARIANTS LQT3 SER-997 AND HIS-1826. RX PubMed=11710892; RA Ackerman M.J., Siu B.L., Sturner W.Q., Tester D.J., Valdivia C.R., RA Makielski J.C., Towbin J.A.; RT "Postmortem molecular analysis of SCN5A defects in sudden infant death RT syndrome."; RL JAMA 286:2264-2269(2001). RN [23] RP CHARACTERIZATION OF VARIANT CARDIAC CONDUCTION DEFECT CYS-514. RX PubMed=11234013; DOI=10.1038/35059090; RA Tan H.L., Bink-Boelkens M.T.E., Bezzina C.R., Viswanathan P.C., RA Beaufort-Krol G.C.M., van Tintelen P.J., van den Berg M.P., RA Wilde A.A.M., Balser J.R.; RT "A sodium-channel mutation causes isolated cardiac conduction RT disease."; RL Nature 409:1043-1047(2001). RN [24] RP CHARATCTERIZATION OF VARIANTS PROGRESSIVE FAMILIAL HEART BLOCK TYPE I RP SER-298 AND ASN-1595. RX PubMed=11804990; RA Wang D.W., Viswanathan P.C., Balser J.R., George A.L. Jr., RA Benson D.W.; RT "Clinical, genetic and biophysical characterisation of SCN5A mutations RT associated with atrioventricular block."; RL Circulation 105:341-346(2002). RN [25] RP VIRTUAL MODELING OF VARIANT LQT3/BRUGADA SYNDROME ASP-1795 INS. RX PubMed=11889015; RA Clancy C.E., Rudy Y.; RT "Na(+) channel mutation that causes both Brugada and long-QT syndrome RT phenotypes: a simulation study of mechanism."; RL Circulation 105:1208-1213(2002). RN [26] RP CHARACTERIZATION OF VARIANTS BRUGADA SYNDROME HIS-367; VAL-735 AND RP GLN-1193. RX PubMed=11823453; RA Vatta M., Dumaine R., Varghese G., Richard T.A., Shimizu W., RA Aihara N., Nademanee K., Brugada R., Brugada J., Veerakul G., Li H., RA Bowles N.E., Brugada P., Antzelevitch C., Towbin J.A.; RT "Genetic and biophysical basis of sudden unexplained nocturnal death RT syndrome (SUNDS), a disease allelic to Brugada syndrome."; RL Hum. Mol. Genet. 11:337-345(2002). RN [27] RP VARIANT ACQUIRED ARRHYTHMIA TYR-1103. RX PubMed=12471205; RA Chen S., Chung M.K., Martin D., Rozich R., Tchou P.J., Wang Q.; RT "SNP S1103Y in the cardiac sodium channel gene SCN5A is associated RT with cardiac arrhythmias and sudden death in a white family."; RL J. Med. Genet. 39:913-915(2002). RN [28] RP VARIANT ACQUIRED ARRHYTHMIA TYR-1103. RX PubMed=12193783; DOI=10.1126/science.1073569; RA Splawski I., Timothy K.W., Tateyama M., Clancy C.E., Malhotra A., RA Beggs A.H., Cappuccio F.P., Sagnella G.A., Kass R.S., Keating M.T.; RT "Variant of SCN5A sodium channel implicated in risk of cardiac RT arrhythmia."; RL Science 297:1333-1336(2002). RN [29] RP VARIANT LQT3 PHE-619. RX MEDLINE=22560398; PubMed=12673799; DOI=10.1002/humu.9136; RA Wehrens X.H., Rossenbacker T., Jongbloed R.J., Gewillig M., RA Heidbuchel H., Doevendans P.A., Vos M.A., Wellens H.J., Kass R.S.; RT "A novel mutation L619F in the cardiac Na+ channel SCN5A associated RT with long-QT syndrome (LQT3): a role for the I-II linker in RT inactivation gating."; RL Hum. Mutat. 21:552-552(2003). RN [30] RP VARIANTS SSS1 ILE-220; LEU-1298 AND ARG-1408. RX PubMed=14523039; DOI=10.1172/JCI200318062; RA Benson D.W., Wang D.W., Dyment M., Knilans T.K., Fish F.A., RA Strieper M.J., Rhodes T.H., George A.L. Jr.; RT "Congenital sick sinus syndrome caused by recessive mutations in the RT cardiac sodium channel gene (SCN5A)."; RL J. Clin. Invest. 112:1019-1028(2003). CC -!- FUNCTION: This protein mediates the voltage-dependent sodium ion CC permeability of excitable membranes. Assuming opened or closed CC conformations in response to the voltage difference across the CC membrane, the protein forms a sodium-selective channel through CC which Na+ ions may pass in accordance with their electrochemical CC gradient. It is a tetrodotoxin-resistant Na+ channel isoform. This CC channel is responsible for the initial upstroke of the action CC potential in the electrocardiogram. CC -!- SUBUNIT: Interacts with the PDZ domain of the syntrophin SNTA1, CC SNTB1 and SNTB2 (By similarity). CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in human atrial and ventricular CC cardiac muscle but not in adult skeletal muscle, brain, CC myometrium, liver, or spleen. CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5 CC hydrophobic segments (S1,S2,S3,S5,S6) and one positively charged CC segment (S4). Segments S4 are probably the voltage-sensors and are CC characterized by a series of positively charged amino acids at CC every third position. CC -!- DISEASE: Defects in SCN5A are a cause of progressive familial CC heart block type I (PFHBI) [MIM:113900]; also known as Lenegre-Lev CC disease or progressive cardiac conduction defect (PCCD). PFHBI is CC characterized by progressive alteration of cardiac conduction CC through the His-Purkinje system with right or left bundle branch CC block and widening of QRS complexes, leading to complete atrio- CC ventricular block and causing syncope and sudden death. PFHBI CC inheritance is autosomal dominant. CC -!- DISEASE: Defects in SCN5A are the cause of long QT syndrome type 3 CC (LQT3) [MIM:603830]. LQT3 is an autosomal dominant cardiac disease CC characterized by prolonged QT interval on electrocardiogram, CC recurrent syncope and sudden cardiac death. CC -!- DISEASE: Defects in SCN5A are the cause of Brugada syndrome CC [MIM:601144]. Brugada syndrome is an autosomal dominant inherited CC arrhythmia that causes the ventricles to beat so fast that they CC can prevent the blood from circulating efficiently in the body. CC When this situation occurs (called ventricular fibrillation), the CC individual will faint and may die in a few minutes if the heart is CC not reset. Brugada syndrome is an idiopathic ventricular CC fibrillation (IVF) syndrome characterized by right bundle branch CC block and ST elevation on an electrocardiogram (ECG). While CC Brugada syndrome is a disease that usually affects people in their CC 30's, it has actually been described at all ages. CC -!- DISEASE: Defects in SCN5A are the cause of autosomal recessive CC sick sinus syndrome 1 (SSS1) [MIM:608567]. The term 'sick sinus CC syndrome' encompasses a variety of conditions caused by sinus node CC dysfunction. The most common clinical manifestations are syncope, CC presyncope, dizziness, and fatigue. Electrocardiogram typically CC shows sinus bradycardia, sinus arrest, and/or sinoatrial block. CC Episodes of atrial tachycardias coexisting with sinus bradycardia CC ('tachycardia-bradycardia syndrome') are also common in this CC disorder. SSS occurs most often in the elderly associated with CC underlying heart disease or previous cardiac surgery, but can also CC occur in the fetus, infant, or child without heart disease or CC other contributing factors, in which case it is considered to be a CC congenital disorder. CC -!- DISEASE: Defects in SCN5A are a cause of idiopathic ventricular CC fibrillation (IVF) [MIM:603829]; also called paroxysmal familial CC ventricular fibrillation. IVF is a self originated, of unknown CC causation, ventricular fibrillation that causes the ventricles to CC beat so fast that they can prevent the blood from circulating CC efficiently in the body. This disorder is not truly idiopathic in CC many cases but can be caused by specific mutations such as those CC in the SCN5A gene. IVF is said to cause more than 300,000 sudden CC deaths each year in the United States alone. In approximately 5 to CC 12% of cases, there are no demonstrable cardiac or noncardiac CC causes to account for the episode, which is therefore classified CC as idiopathic ventricular fibrillation. CC -!- DISEASE: Defects in SCN5A are a cause of sudden infant death CC syndrome (SIDS) [MIM:272120]. SIDS remains elusive in its causes CC and devastating in its consequences. Despite the impressive CC decline in the incidence of SIDS since the recommendation to avoid CC the prone sleep position, SIDS remains a leading cause of death in CC the first year of life. CC -!- MISCELLANEOUS: Na+ channels in mammalian cardiac membrane have CC functional properties quite distinct from Na+ channels in nerve CC and skeletal muscle. CC -!- SIMILARITY: Belongs to the sodium channel family. CC -!- SIMILARITY: Contains 1 IQ domain. CC -!- WEB RESOURCE: Name=LQTSdb; Note=SCN5A mutations page; CC URL="http://www.ssi.dk/en/forskning/lqtsdb/scn5a.htm"; CC -!- WEB RESOURCE: Name=CaBP; Note=Calpain; CC URL="http://structbio.vanderbilt.edu/cabp_database/general/prot_pages/calpain.html"; DR EMBL; M77235; AAA58644.1; -. DR PIR; A38195; A38195. DR HSSP; P04775; 1BYY. DR HGNC; HGNC:10593; SCN5A. DR MIM; 600163; -. DR MIM; 113900; -. DR MIM; 603830; -. DR MIM; 601144; -. DR MIM; 608567; -. DR MIM; 603829; -. DR MIM; 272120; -. DR GO; GO:0005248; F:voltage-gated sodium channel activity; TAS. DR GO; GO:0006936; P:muscle contraction; TAS. DR GO; GO:0008016; P:regulation of heart rate; TAS. DR GO; GO:0006814; P:sodium ion transport; TAS. DR InterPro; IPR001682; Ca/Na_pore. DR InterPro; IPR002111; Cat_channel_TrpL. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR000048; IQ_region. DR InterPro; IPR005820; M+channel_nlg. DR InterPro; IPR001696; Na_channel. DR InterPro; IPR008053; Na_channel5. DR InterPro; IPR010526; Na_trans_assoc. DR Pfam; PF00520; Ion_trans; 4. DR Pfam; PF00612; IQ; 1. DR Pfam; PF06512; Na_trans_assoc; 1. DR PRINTS; PR00170; NACHANNEL. DR PRINTS; PR01666; NACHANNEL5. DR PROSITE; PS50096; IQ; FALSE_NEG. KW Ionic channel; Transmembrane; Ion transport; Voltage-gated channel; KW Glycoprotein; Repeat; Multigene family; Phosphorylation; Polymorphism; KW Disease mutation; Long QT syndrome; Sodium channel. FT TRANSMEM 127 150 S1 of repeat I (Potential). FT TRANSMEM 159 178 S2 of repeat I (Potential). FT TRANSMEM 192 210 S3 of repeat I (Potential). FT TRANSMEM 217 236 S4 of repeat I (Potential). FT TRANSMEM 253 276 S5 of repeat I (Potential). FT TRANSMEM 390 415 S6 of repeat I (Potential). FT TRANSMEM 712 736 S1 of repeat II (Potential). FT TRANSMEM 748 771 S2 of repeat II (Potential). FT TRANSMEM 780 799 S3 of repeat II (Potential). FT TRANSMEM 806 825 S4 of repeat II (Potential). FT TRANSMEM 842 862 S5 of repeat II (Potential). FT TRANSMEM 914 939 S6 of repeat II (Potential). FT TRANSMEM 1201 1224 S1 of repeat III (Potential). FT TRANSMEM 1238 1263 S2 of repeat III (Potential). FT TRANSMEM 1270 1291 S3 of repeat III (Potential). FT TRANSMEM 1296 1317 S4 of repeat III (Potential). FT TRANSMEM 1337 1359 S5 of repeat III (Potential). FT TRANSMEM 1444 1470 S6 of repeat III (Potential). FT TRANSMEM 1524 1547 S1 of repeat IV (Potential). FT TRANSMEM 1559 1582 S2 of repeat IV (Potential). FT TRANSMEM 1589 1612 S3 of repeat IV (Potential). FT TRANSMEM 1623 1644 S4 of repeat IV (Potential). FT TRANSMEM 1660 1682 S5 of repeat IV (Potential). FT TRANSMEM 1748 1772 S6 of repeat IV (Potential). FT CARBOHYD 214 214 N-linked (GlcNAc...) (Potential). FT CARBOHYD 283 283 N-linked (GlcNAc...) (Potential). FT CARBOHYD 288 288 N-linked (GlcNAc...) (Potential). FT CARBOHYD 291 291 N-linked (GlcNAc...) (Potential). FT CARBOHYD 318 318 N-linked (GlcNAc...) (Potential). FT CARBOHYD 328 328 N-linked (GlcNAc...) (Potential). FT CARBOHYD 548 548 N-linked (GlcNAc...) (Potential). FT CARBOHYD 592 592 N-linked (GlcNAc...) (Potential). FT CARBOHYD 740 740 N-linked (GlcNAc...) (Potential). FT CARBOHYD 803 803 N-linked (GlcNAc...) (Potential). FT CARBOHYD 841 841 N-linked (GlcNAc...) (Potential). FT CARBOHYD 864 864 N-linked (GlcNAc...) (Potential). FT CARBOHYD 946 946 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1365 1365 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1374 1374 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1380 1380 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1388 1388 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1736 1736 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1774 1774 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1955 1955 N-linked (GlcNAc...) (Potential). FT VARIANT 220 220 T -> I (in SSS1). FT /FTId=VAR_017670. FT VARIANT 298 298 G -> S (in progressive familial heart FT block type I; significant defect in the FT kinetics of fast-channel inactivation FT distinct from mutations reported in FT LQT3). FT /FTId=VAR_017671. FT VARIANT 367 367 R -> H (in Brugada syndrome; express no FT current). FT /FTId=VAR_017672. FT VARIANT 425 425 R -> H (in AT-III deficiency; type-II; FT Glasgow/Sheffield/Chicago/Avranches/ FT Kumamoto-2; increases affinity for FT heparin). FT /FTId=VAR_007074. FT VARIANT 514 514 G -> C (in cardiac conduction defect). FT /FTId=VAR_017673. FT VARIANT 558 558 H -> R (in dbSNP:1805124). FT /FTId=VAR_008955. FT VARIANT 619 619 L -> F (in LQT3). FT /FTId=VAR_015682. FT VARIANT 735 735 A -> V (in Brugada syndrome; expresses FT currents with steady state activation FT voltage shifted to more positive FT potentials and exhibit reduced sodium FT channel current at the end of phase I of FT the action potential). FT /FTId=VAR_017674. FT VARIANT 941 941 S -> N (in LQT3; also in SIDS). FT /FTId=VAR_017675. FT VARIANT 997 997 A -> S (in LQT3; sodium current FT characterized by slower decay and a 2- to FT 3-fold increase in late sodium current). FT /FTId=VAR_017676. FT VARIANT 1090 1090 P -> L (in dbSNP:1805125). FT /FTId=VAR_014464. FT VARIANT 1103 1103 S -> Y (in acquired arrhythmia; FT susceptibility to). FT /FTId=VAR_017677. FT VARIANT 1114 1114 D -> N (in LQT3). FT /FTId=VAR_009935. FT VARIANT 1193 1193 R -> Q (in Brugada syndrome; accelerates FT the inactivation of the sodium channel FT current and exhibit reduced sodium FT channel current at the end of phase I of FT the action potential). FT /FTId=VAR_017678. FT VARIANT 1232 1232 R -> W (in Brugada syndrome; could be a FT rare polymorphism). FT /FTId=VAR_017679. FT VARIANT 1298 1298 P -> L (in SSS1). FT /FTId=VAR_017680. FT VARIANT 1304 1304 T -> M (in LQT3). FT /FTId=VAR_008956. FT VARIANT 1325 1325 N -> S (in LQT3). FT /FTId=VAR_001577. FT VARIANT 1408 1408 G -> R (in SSS1 and Brugada syndrome; FT also in cardiac conduction defect). FT /FTId=VAR_017681. FT VARIANT 1500 1500 K -> N. FT /FTId=VAR_008957. FT VARIANT 1501 1501 L -> V (in LQT3). FT /FTId=VAR_009936. FT VARIANT 1505 1507 Missing (in LQT3). FT /FTId=VAR_001576. FT VARIANT 1512 1512 R -> W (in Brugada syndrome; FT significantly affects cardiac sodium FT channel characteristics; associated with FT an increase in inward sodium current FT during the action potential upstroke). FT /FTId=VAR_017682. FT VARIANT 1595 1595 D -> N (in progressive familial heart FT block type I; significant defect in the FT kinetics of fast-channel inactivation FT distinct from mutations reported in FT LQT3). FT /FTId=VAR_017683. FT VARIANT 1620 1620 T -> M (in Brugada syndrome; FT arrhythmogenicity revealed only at FT temperatures approaching the physiologic FT range). FT /FTId=VAR_017684. FT VARIANT 1623 1623 R -> L (in LQT3). FT /FTId=VAR_009937. FT VARIANT 1623 1623 R -> Q (in LQT3). FT /FTId=VAR_001578. FT VARIANT 1644 1644 R -> H (in LQT3). FT /FTId=VAR_001579. FT VARIANT 1645 1645 T -> M (in LQT3). FT /FTId=VAR_008958. FT VARIANT 1710 1710 S -> L (in IVF). FT /FTId=VAR_017685. FT VARIANT 1784 1784 E -> K (in LQT3). FT /FTId=VAR_008959. FT VARIANT 1787 1787 S -> N (in LQT3). FT /FTId=VAR_009938. FT VARIANT 1790 1790 D -> G (in LQT3). FT /FTId=VAR_001580. FT VARIANT 1795 1795 Y -> C (in LQT3; slows the onset of FT activation, but does not cause a marked FT negative shift in the voltage dependence FT of inactivation or affect the kinetics of FT the recovery from inactivation; increases FT the expression of sustained Na(+) channel FT activity and promotes entrance into an FT intermediate or slowly developing FT inactivated state). FT /FTId=VAR_019123. FT VARIANT 1795 1795 Y -> H (in Brugada syndrome; accelerates FT the onset of activation and causes a FT marked negative shift in the voltage FT dependence of inactivation; does not FT affect the kinetics of the recovery from FT inactivation; increases the expression of FT sustained Na(+) channel activity and FT promotes entrance into an intermediate or FT slowly developing inactivated state). FT /FTId=VAR_019124. FT VARIANT 1795 1795 Y -> YD (in LQT3 and Brugada syndrome; FT 7.3-mV negative shift of the steady-state FT inactivation curve and 8.1-mV positive FT shift of the steady-state activation FT curve; may reduced sodium current during FT the upstroke of the action potential). FT /FTId=VAR_017686. FT VARIANT 1826 1826 R -> H (in LQT3; sodium current FT characterized by slower decay and a 2- to FT 3-fold increase in late sodium current). FT /FTId=VAR_017687. FT VARIANT 1839 1839 D -> G (in LQT3). FT /FTId=VAR_001581. FT VARIANT 1924 1924 A -> T (in Brugada syndrome; FT significantly affect cardiac sodium FT channel characteristics; associated with FT an increase in inward sodium current FT during the action potential upstroke). FT /FTId=VAR_017688. ** ** ################# INTERNAL SECTION ################## **CL 3p21; **ZB SYP, 23-JUL-2002; SQ SEQUENCE 2016 AA; 227162 MW; ED97598D215E349E CRC64; MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSTTLQ ESREGLPEEE APRPQLDLQA SKKLPDLYGN PPQELIGEPL EDLDPFYSTQ KTFIVLNKGK TIFRFSATNA LYVLSPFHPV RRAAVKILVH SLFNMLIMCT ILTNCVFMAQ HDPPPWTKYV EYTFTAIYTF ESLVKILARA FCLHAFTFLR DPWNWLDFSV IIMAYTTEFV DLGNVSALRT FRVLRALKTI SVISGLKTIV GALIQSVKKL ADVMVLTVFC LSVFALIGLQ LFMGNLRHKC VRNFTALNGT NGSVEADGLV WESLDLYLSD PENYLLKNGT SDVLLCGNSS DAGTCPEGYR CLKAGENPDH GYTSFDSFAW AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG SFYLVNLILA VVAMAYEEQN QATIAETEEK EKRFQEAMEM LKKEHEALTI RGVDTVSRSS LEMSPLAPVN SHERRSKRRK RMSSGTEECG EDRLPKSDSE DGPRAMNHLS LTRGLSRTSM KPRSSRGSIF TFRRRDLGSE ADFADDENST ARESESHHTS LLVPWPLRRT SAQGQPSPGT SAPGHALHGK KNSTVDCNGV VSLLGAGDPE ATSPGSHLLR PVMLEHPPDT TTPSEEPGGP QMLTSQAPCV DGFEEPGARQ RALSAVSVLT SALEELEESR HKCPPCWNRL AQRYLIWECC PLWMSIKQGV KLVVMDPFTD LTITMCIVLN TLFMALEHYN MTSEFEEMLQ VGNLVFTGIF TAEMTFKIIA LDPYYYFQQG WNIFDSIIVI LSLMELGLSR MSNLSVLRSF RLLRVFKLAK SWPTLNTLIK IIGNSVGALG NLTLVLAIIV FIFAVVGMQL FGKNYSELRD SDSGLLPRWH MMDFFHAFLI IFRILCGEWI ETMWDCMEVS GQSLCLLVFL LVMVIGNLVV LNLFLALLLS SFSADNLTAP DEDREMNNLQ LALARIQRGL RFVKRTTWDF CCGLLRHRPQ KPAALAAQGQ LPSCIATPYS PPPPETEKVP PTRKETQFEE GEQPGQGTPG DPEPVCVPIA VAESDTDDQE EDEENSLGTE EESSKQQESQ PVSGWPRGPP DSRTWSQVSA TASSEAEASA SQADWRQQWK AEPQAPGCGE TPEDSCSEGS TADMTNTAEL LEQIPDLGQD VKDPEDCFTE GCVRRCPCCA VDTTQAPGKV WWRLRKTCYH IVEHSWFETF IIFMILLSSG ALAFEDIYLE ERKTIKVLLE YADKMFTYVF VLEMLLKWVA YGFKKYFTNA WCWLDFLIVD VSLVSLVANT LGFAEMGPIK SLRTLRALRP LRALSRFEGM RVVVNALVGA IPSIMNVLLV CLIFWLIFSI MGVNLFAGKF GRCINQTEGD LPLNYTIVNN KSQCESLNLT GELYWTKVKV NFDNVGAGYL ALLQVATFKG WMDIMYAAVD SRGYEEQPQW EYNLYMYIYF VIFIIFGSFF TLNLFIGVII DNFNQQKKKL GGQDIFMTEE QKKYYNAMKK LGSKKPQKPI PRPLNKYQGF IFDIVTKQAF DVTIMFLICL NMVTMMVETD DQSPEKINIL AKINLLFVAI FTGECIVKLA ALRHYYFTNS WNIFDFVVVI LSIVGTVLSD IIQKYFFSPT LFRVIRLARI GRILRLIRGA KGIRTLLFAL MMSLPALFNI GLLLFLVMFI YSIFGMANFA YVKWEAGIDD MFNFQTFANS MLCLFQITTS AGWDGLLSPI LNTGPPYCDP TLPNSNGSRG DCGSPAVGIL FFTTYIIISF LIVVNMYIAI ILENFSVATE ESTEPLSEDD FDMFYEIWEK FDPEATQFIE YSVLSDFADA LSEPLRIAKP NQISLINMDL PMVSGDRIHC MDILFAFTKR VLGESGEMDA LKIQMEEKFM AANPSKISYE PITTTLRRKH EEVSAMVIQR AFRRHLLQRS LKHASFLFRQ QAGSGLSEED APEREGLIAY VMSENFSRPL GPPSSSSISS TSFPPSYDSV TRATSDNLQV RGSDYSHSED LADFPPSPDR DRESIV // ID Q9DIX3 PRELIMINARY; PRT; 56 AA. AC Q9DIX3; DT 01-MAR-2001 (TrEMBLrel. 16, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE VP1 capsid protein and P2A protease (Fragment){EI4}. GN Name=VP1 and P2A{EI4}; OS Hepatitis A virus. OC Viruses; ssRNA positive-strand viruses, no DNA stage; Picornaviridae; OC Hepatovirus. OX NCBI_TaxID=12092{EI4}; RN [1]{EI4} RP SEQUENCE FROM N.A. RX MEDLINE=21259955; PubMed=11360240; RA Diaz B.I., Sariol C.A., Normann A., Rodriguez L.A., Flehmig B.; RT "Genetic relatedness of Cuban HAV wild-type isolates."; RL J. Med. Virol. 64:96-103(2001). DR EMBL; AJ245534; CAC17887.1; -.{EI4} DR PIR; PQ0427; PQ0427. DR PIR; PQ0428; PQ0428. DR GO; GO:0008233; F:peptidase activity; IEA. DR InterPro; IPR000886; ER_target_S. DR PROSITE; PS00014; ER_TARGET; UNKNOWN_1. KW Protease{EP2}. FT NON_TER 1 1 {EI4} FT NON_TER 56 56 {EI4} ** ** ################# INTERNAL SECTION ################## **EV EI4; EMBL; -; CAC17887.1; 11-MAY-2004. **EV EP2; TrEMBL; -; CAC17887.1; 11-MAY-2004. **PM PROSITE; PS00014; ER_TARGET; 53; 56; ?; 27-APR-2004; SQ SEQUENCE 56 AA; 6628 MW; 465CF4B35C1EF4BC CRC64; ESMMSRIAAG DLESSVDDPR SDEDRRFESH IECRKPYKEL RLEVGKQRLK YAQEEL // ID Q27383 PRELIMINARY; PRT; 378 AA. AC Q27383; DT 01-JUN-1998 (TrEMBLrel. 06, Created) DT 01-JUN-1998 (TrEMBLrel. 06, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Hypothetical 40.7 kDa protein R09F10.2 in chromosome X precursor. GN Name=R09F10.2; GN and GN Name=abu-9{EI1}; ORFNames=R09F10.2{EI1}, R09F10.7{EI2}; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Couch J.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP REVISIONS TO C-TERMINUS. ** MEDLINE=None; PubMed=None; RA Ambler R.P.; ** /NO TITLE. RL Unpublished results, cited by: RL McGinnis J., Sinclair-day J.D., Sykes A.G., Powls R., Moore J., RL Wright P.D.; RL Inorg. Chem. 27:2306-2312(1988). RN [3] RP SEQUENCE. RC TISSUE=Plasma; RA Moorad D.R., Luo C., Garcia G.E., Doctor B.P.; RT "Amino acid sequence of horse serum butyrycholinesterase."; RL (In) Doctor B.P., Taylor P., Quinn D.M., Rotundo R.L., Gentry M.K. RL (eds.); RL Structure and function of cholinesterases and related proteins, RL pp.145-146, Plenum Press, New York and London (1998). CC -!- WEB RESOURCE: Name=Androgen receptor gene mutations database; CC URL="http://www.mcgill.ca/androgendb/"; CC -!- SIMILARITY: BELONGS TO FAMILY UPF. DR EMBL; U64859; AAC69090.1; -. DR PIR; B89588; B89588. DR WormBase; R09F10.2; CE07436. DR WormBase; R09F10.7; CE07436. DR InterPro; IPR009475; DUF1096. DR InterPro; IPR003341; DUF139. DR Pfam; PF02363; C_tripleX; 9. DR Pfam; PF06493; DUF1096; 1. KW Hypothetical protein; Signal. FT SIGNAL 1 18 POTENTIAL. FT CHAIN 19 378 HYPOTHETICAL PROTEIN R09F10.2. ** ** ################# SOURCE SECTION ################## ** Caenorhabditis elegans cosmid R09F10. ** [1] ** 1-31934 ** MEDLINE; 94150718. ** Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield ** J., ** Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., ** Dear S., Du Z., Durbin R., Favello A., Fulton L., Gardner A., Green ** P., ** Hawkins T., Hillier L., Jier M., Johnston L., Jones M., Kershaw J., ** Kirsten J., Laister N., Latreille P., Lightning J., Lloyd C., ** McMurray A., Mortimore B., O'Callaghan M., Parsons J., Percy C., ** Rifken L., Roopra A., Saunders D., Shownkeen R., Smaldon N., Smith A., ** Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., ** Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., ** Wilkinson-Sproat J., Wohldman P.; ** "2.2 Mb of contiguous nucleotide sequence from chromosome III of C. ** elegans"; ** Nature 368:32-38(1994). ** [2] ** 1-31934 ** Couch J.; ** "The sequence of C. elegans cosmid R09F10"; ** Unpublished. ** [3] ** 1-31934 ** Waterston R.; ** ; ** Submitted (22-JUL-1996) to the EMBL/GenBank/DDBJ databases. ** Genome Sequencing Center Department of Genetics, Washington ** University, ** St. Louis, MO 63110, USA, and Sanger Centre, Hinxton Hall Cambridge ** CB10 ** IRQ, England e-mail: rw@nematode.wustl.edu and jes@sanger.ac.uk ** Submitted by: Genome Sequencing Center Department of Genetics, ** Washington University, St. Louis, MO 63110, USA, and Sanger Centre, ** Hinxton Hall Cambridge CB10 IRQ, England e-mail: ** rw@nematode.wustl.edu and jes@sanger.ac.uk NEIGHBORING COSMID ** INFORMATION: The 5' cosmid is F13B9, 600 bp overlap;3' cosmid is ** F55E10, 200 bp overlap. Actual start of this cosmid is at base ** position 595 of CELR09F10; actual end is at 7938 of CELF55E10 ** NOTES: Coding sequences below are predicted from computer analysis, ** using the program Genefinder(P. Green and L. Hillier, ms in ** preparation). ** source 1..31934 ** /organism="Caenorhabditis elegans" ** /chromosome="X" ** /strain="Bristol N2" ** /clone="R09F10" ** CDS join(complement(26227..26277),complement(26009. ** .26179), ** complement(25045..25959)) ** /codon_start=1 ** /db_xref="PID:g1465855" ** /evidence=NOT_EXPERIMENTAL ** /note="glutamine-rich protein" ** /gene="R09f10.7" ** CDS_IN_EMBL_ENTRY 8 ** 01-OCT-1996 (Rel. 49, Last updated, Version 5) ** Caenorhabditis elegans cosmid R09F10. ** [1] ** 1-31934 ** MEDLINE; 94150718. ** Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield ** J., ** Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M., ** Dear S., Du Z., Durbin R., Favello A., Fulton L., Gardner A., Green ** P., ** Hawkins T., Hillier L., Jier M., Johnston L., Jones M., Kershaw J., ** Kirsten J., Laister N., Latreille P., Lightning J., Lloyd C., ** McMurray A., Mortimore B., O'Callaghan M., Parsons J., Percy C., ** Rifken L., Roopra A., Saunders D., Shownkeen R., Smaldon N., Smith A., ** Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K., ** Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L., ** Wilkinson-Sproat J., Wohldman P.; ** "2.2 Mb of contiguous nucleotide sequence from chromosome III of C. ** elegans"; ** Nature 368:32-38(1994). ** [2] ** 1-31934 ** Couch J.; ** "The sequence of C. elegans cosmid R09F10"; ** Unpublished. ** [3] ** 1-31934 ** Waterston R.; ** ; ** Submitted (22-JUL-1996) to the EMBL/GenBank/DDBJ databases. ** Genome Sequencing Center Department of Genetics, Washington ** University, ** St. Louis, MO 63110, USA, and Sanger Centre, Hinxton Hall Cambridge ** CB10 ** IRQ, England e-mail: rw@nematode.wustl.edu and jes@sanger.ac.uk ** Submitted by: Genome Sequencing Center Department of Genetics, ** Washington University, St. Louis, MO 63110, USA, and Sanger Centre, ** Hinxton Hall Cambridge CB10 IRQ, England e-mail: ** rw@nematode.wustl.edu and jes@sanger.ac.uk NEIGHBORING COSMID ** INFORMATION: The 5' cosmid is F13B9, 600 bp overlap;3' cosmid is ** F55E10, 200 bp overlap. Actual start of this cosmid is at base ** position 595 of CELR09F10; actual end is at 7938 of CELF55E10 ** NOTES: Coding sequences below are predicted from computer analysis, ** using the program Genefinder(P. Green and L. Hillier, ms in ** preparation). ** source 1..31934 ** /organism="Caenorhabditis elegans" ** /chromosome="X" ** /strain="Bristol N2" ** /clone="R09F10" ** CDS join(27488..27538,27586..27756,27806..28720) ** /codon_start=1 ** /db_xref="PID:g1465856" ** /evidence=NOT_EXPERIMENTAL ** /note="glutamine-rich protein" ** /gene="R09f10.2" ** CDS_IN_EMBL_ENTRY 8 ** 01-OCT-1996 (Rel. 49, Last updated, Version 5) ** FAMILY UPF CONSISTS OF Q17400, Q17401, Q19919, Q19594 AND Q27383. ** FOR THIS ENTRY AMOS, THERE ARE TWO CDS IN THE SAME COSMID WHICH ** ENCODE IDENTICAL PROTEINS AND SO I HAVE MERGED. I HAVE USED THE ** FIRST CDS FOR NOMENCLATURE. ** ################# INTERNAL SECTION ################## **EV EI1; WormBase_ADD; -; R09F10.2; 23-MAY-2004. **EV EI2; WormBase_ADD; -; R09F10.7; 23-MAY-2004. **ID XXXX_CAEEL **PM Pfam; PF02363; C_tripleX; 131; 147; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 153; 169; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 191; 207; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 213; 229; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 259; 275; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 305; 321; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 327; 343; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 78; 94; T; 06-MAY-2004; **PM Pfam; PF02363; C_tripleX; 99; 115; T; 06-MAY-2004; **PM Pfam; PF06493; DUF1096; 3; 65; T; 06-MAY-2004; **ZZ CREATED AND FINISHED BY CLAIRE. SQ SEQUENCE 378 AA; 40683 MW; E58B416BFE3A7610 CRC64; MRFITLAVFF ACALVASSSV LREKRHCGCA QPQQSQCSCQ QVQQTQSCSC QSAPVQQQAP SCSCAQPQQT QTVQVQSTQC APACQQSCRQ QCQSAPAVSQ CQPMCQQQCQ SQCTPMYNPP ATTTTTPAPV VQCQPMCQQQ CQSTCVQQQQ PVSQCQPQCQ QQCNVACDAT TTTTSAPQVI HIQLEIQQAQ VQCQPACQQQ CQSSCVQQQQ PAKQCASSCN TQCTNACQQT AQATQQVIYG QNSNTQMYDP YNNQQQQQAN CAPACQPACD NSCIQQTAAP IYNPTTTSAP QVVQIVLQAS VAQSSQCAPQ CEQSCQQQCV QQQQPVAQCQ SACQSSCSSS CQAAQPATVA CQQAPQSNQC SCQSNYSPCG QGQCCRRK // ID TAU_HUMAN STANDARD; PRT; 757 AA. AC P10636; P18518; Q14799; Q15549; Q15550; Q15551; Q9UDJ3; Q9UMH0; AC Q9UQ96; DT 01-JUL-1989 (Rel. 11, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE Microtubule-associated protein tau (Neurofibrillary tangle protein) DE (Paired helical filament-tau) (PHF-tau). GN Name=MAPT; Synonyms=MTBT1, TAU; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS PNS-TAU; TAU-A AND TAU-F). RA Andreadis A.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. (ISOFORM TAU-A). RC TISSUE=Brain; RX MEDLINE=88234557; PubMed=3131773; RA Goedert M., Wischik C., Crowther R., Walker J., Klug A.; RT "Cloning and sequencing of the cDNA encoding a core protein of the RT paired helical filament of Alzheimer disease: identification as the RT microtubule-associated protein tau."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4051-4055(1988). RN [3] RP SEQUENCE FROM N.A. (ISOFORMS TAU-B; TAU-C; TAU-E AND TAU-F). RC TISSUE=Brain; RX MEDLINE=90380393; PubMed=2484340; RA Goedert M., Spillantini M.G., Jakes R., Rutherford D., Crowther R.A.; RT "Multiple isoforms of human microtubule-associated protein tau: RT sequences and localization in neurofibrillary tangles of Alzheimer's RT disease."; RL Neuron 3:519-526(1989). RN [4] RP SEQUENCE FROM N.A. (ISOFORM TAU-D). RC TISSUE=Brain; RX MEDLINE=89251564; PubMed=2498079; RA Goedert M., Spillantini M.G., Potier M.C., Ulrich J., Crowther R.A.; RT "Cloning and sequencing of the cDNA encoding an isoform of RT microtubule-associated protein tau containing four tandem repeats: RT differential expression of tau protein mRNAs in human brain."; RL EMBO J. 8:393-399(1989). RN [5] RP SEQUENCE FROM N.A. (ISOFORMS TAU-A AND FETAL-TAU). RC TISSUE=Fetal brain; RX MEDLINE=90180482; PubMed=2516729; RA Lee G., Neve R.L., Kosik K.S.; RT "The microtubule binding domain of tau protein."; RL Neuron 2:1615-1624(1989). RN [6] RP SEQUENCE FROM N.A. (ISOFORM TAU-F), AND ALTERNATIVE SPLICING. RX MEDLINE=93041757; PubMed=1420178; RA Andreadis A., Brown W.M., Kosik K.S.; RT "Structure and novel exons of the human tau gene."; RL Biochemistry 31:10626-10633(1992). RN [7] RP SEQUENCE FROM N.A. (ISOFORM TAU-A). RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [8] RP SEQUENCE OF 591-621 FROM N.A. RC TISSUE=Brain; RX MEDLINE=89193714; PubMed=2495000; RA Mori H., Hamada Y., Kawaguchi M., Honda T., Kondo J., Ihara Y.; RT "A distinct form of tau is selectively incorporated into Alzheimer's RT paired helical filaments."; RL Biochem. Biophys. Res. Commun. 159:1221-1226(1989). RN [9] RP SEQUENCE OF 1-72; 102-380; 467-496; 507-570; 576-582; 591-606; RP 615-633; 638-656; 660-663; 670-699 AND 702-757. RC TISSUE=Brain; RX MEDLINE=92381012; PubMed=1512244; RA Hasegawa M., Morishima-Kawashima M., Takio K., Suzuki M., Titani K., RA Ihara Y.; RT "Protein sequence and mass spectrometric analyses of tau in the RT Alzheimer's disease brain."; RL J. Biol. Chem. 267:17047-17054(1992). RN [10] RP SEQUENCE OF 576-583; 607-610; 615-627; 638-647 AND 670-685, RP PHOSPHORYLATION, AND MUTAGENESIS. RX MEDLINE=95221434; PubMed=7706316; RA Drewes G., Trinczek B., Illenberger S., Biernat J., Schmitt-Ulms G., RA Meyer H.E., Mandelkow E.-M., Mandelkow E.; RT "Microtubule-associated protein/microtubule affinity-regulating kinase RT (p110mark). A novel protein kinase that regulates tau-microtubule RT interactions and dynamic instability by phosphorylation at the RT Alzheimer-specific site serine 262."; RL J. Biol. Chem. 270:7679-7688(1995). RN [11] RP REVIEW. RX MEDLINE=91320377; PubMed=1713721; DOI=10.1016/0166-2236(91)90105-4; RA Goedert M., Crowther R.A., Garner C.C.; RT "Molecular characterization of microtubule-associated proteins tau and RT MAP2."; RL Trends Neurosci. 14:193-199(1991). RN [12] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX MEDLINE=20283597; PubMed=10747907; DOI=10.1074/jbc.M000389200; RA Maas T., Eidenmueller J., Brandt R.; RT "Interaction of tau with the neural membrane cortex is regulated by RT phosphorylation at sites that are modified in paired helical RT filaments."; RL J. Biol. Chem. 275:15733-15740(2000). RN [13] RP PHOSPHORYLATION, AND MUTAGENESIS. RX MEDLINE=98413833; PubMed=9735171; RA Sengupta A., Kabat J., Novak M., Wu Q., Grundke-Iqbal I., Iqbal K.; RT "Phosphorylation of tau at both Thr 231 and Ser 262 is required for RT maximal inhibition of its binding to microtubules."; RL Arch. Biochem. Biophys. 357:299-309(1998). RN [14] RP PHOSPHORYLATION, AND MUTAGENESIS. RX MEDLINE=98278959; PubMed=9614189; RA Illenberger S., Zheng-Fischhofer Q., Preuss U., Stamer K., Baumann K., RA Trinczek B., Biernat J., Godemann R., Mandelkow E.-M., Mandelkow E.; RT "The endogenous and cell cycle-dependent phosphorylation of tau RT protein in living cells: implications for Alzheimer's disease."; RL Mol. Biol. Cell 9:1495-1512(1998). RN [15] RP GLYCATION. RX MEDLINE=97465580; PubMed=9326300; RA Nacharaju P., Ko L., Yen S.H.; RT "Characterization of in vitro glycation sites of tau."; RL J. Neurochem. 69:1709-1719(1997). RN [16] RP REVIEW ON VARIANTS. RX MEDLINE=20437008; PubMed=10899436; DOI=10.1016/S0925-4439(00)00037-5; RA Goedert M., Spillantini M.G.; RT "Tau mutations in frontotemporal dementia FTDP-17 and their relevance RT for Alzheimer's disease."; RL Biochim. Biophys. Acta 1502:110-121(2000). RN [17] RP VARIANT FTDP17 MET-653, AND VARIANTS ASN-284; ALA-288; TYR-440 AND RP PRO-446. RX MEDLINE=98291804; PubMed=9629852; RA Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., RA Anderson L., Andreadis A., Wiederholt W.C., Raskind M., RA Schellenberg G.D.; RT "Tau is a candidate gene for chromosome 17 frontotemporal dementia."; RL Ann. Neurol. 43:815-825(1998). RN [18] RP ERRATUM. ** MEDLINE=None; PubMed=None; RA Poorkaj P., Bird T.D., Wijsman E., Nemens E., Garruto R.M., RA Anderson L., Andreadis A., Wiederholt W.C., Raskind M., RA Schellenberg G.D.; ** /NO TITLE. RL Ann. Neurol. 44:428-428(1998). RN [19] RP VARIANT FTDP17 LEU-617. RX MEDLINE=98409513; PubMed=9736786; RA Dumanchin C., Camuzat A., Campion D., Verpillat P., Hannequin D., RA Dubois B., Saugier-Veber P., Martin C., Penet C., Charbonnier F., RA Agid Y., Frebourg T., Brice A.; RT "Segregation of a missense mutation in the microtubule-associated RT protein tau gene with familial frontotemporal dementia and RT parkinsonism."; RL Hum. Mol. Genet. 7:1825-1829(1998). RN [20] RP VARIANTS FTDP17 VAL-588; LEU-617 AND TRP-722. RX MEDLINE=98303385; PubMed=9641683; DOI=10.1038/31508; RA Hutton M., Lendon C.L., Rizzu P., Baker M., Froelich S., Houlden H., RA Pickering-Brown S., Chakraverty S., Isaacs A., Grover A., Hackett J., RA Adamson J., Lincoln S., Dickson D., Davies P., Petersen R.C., RA Stevens M., de Graaff E., Wauters E., van Baren J., Hillebrand M., RA Joosse M., Kwon J.M., Nowotny P., Che L.K., Norton J., Morris J.C., RA Reed L.A., Trojanowski J., Basun H., Lannfelt L., Neystat M., Fahn S., RA Dark F., Tannenberg T., Dodd P.R., Hayward N., Kwok J.B.J., RA Schofield P.R., Andreadis A., Snowden J., Craufurd D., Neary D., RA Owen F., Oostra B.A., Hardy J., Goate A., van Swieten J., Mann D., RA Lynch T., Heutink P.; RT "Association of missense and 5'-splice-site mutations in tau with the RT inherited dementia FTDP-17."; RL Nature 393:702-705(1998). RN [21] RP VARIANT PPND LYS-595, AND VARIANT FTDP17 LEU-617. RX MEDLINE=99007274; PubMed=9789048; RA Clark L.N., Poorkaj P., Wszolek Z., Geschwind D.H., Nasreddine Z.S., RA Miller B., Li D., Payami H., Awert F., Markopoulou K., Andreadis A., RA D'Souza I., Lee V.M.-Y., Reed L., Trojanowski J.Q., Zhukareva V., RA Bird T., Schellenberg G., Wilhelmsen K.C.; RT "Pathogenic implications of mutations in the tau gene in pallido- RT ponto-nigral degeneration and related neurodegenerative disorders RT linked to chromosome 17."; RL Proc. Natl. Acad. Sci. U.S.A. 95:13103-13107(1998). RN [22] RP VARIANTS FTDP17 VAL-588; LYS-596 DEL; LEU-617 AND TRP-722. RX MEDLINE=99138654; PubMed=9973279; RA Rizzu P., Van Swieten J.C., Joosse M., Hasegawa M., Stevens M., RA Tibben A., Niermeijer M.F., Hillebrand M., Ravid R., Oostra B.A., RA Goedert M., van Duijn C.M., Heutink P.; RT "High prevalence of mutations in the microtubule-associated protein RT tau in a population study of frontotemporal dementia in the RT Netherlands."; RL Am. J. Hum. Genet. 64:414-421(1999). RN [23] RP VARIANTS FTDP17 LEU-617; MET-653 AND TRP-722. RX MEDLINE=99229757; PubMed=10214944; RA Nacharaju P., Lewis J., Easson C., Yen S., Hackett J., Hutton M., RA Yen S.H.; RT "Accelerated filament formation from tau protein with specific FTDP-17 RT missense mutations."; RL FEBS Lett. 447:195-199(1999). RN [24] RP VARIANT FTDP17/CBD SER-617. RX MEDLINE=99301293; PubMed=10374757; RA Bugiani O., Murrell J.R., Giaccone G., Hasegawa M., Ghigo G., RA Tabaton M., Morbin M., Primavera A., Carella F., Solaro C., RA Grisoli M., Savoiardo M., Spillantini M.G., Tagliavini F., Goedert M., RA Ghetti B.; RT "Frontotemporal dementia and corticobasal degeneration in a family RT with a P301S mutation in tau."; RL J. Neuropathol. Exp. Neurol. 58:667-677(1999). RN [25] RP VARIANT DEMENTIA ARG-705. RX MEDLINE=20068246; PubMed=10604746; RA Murrell J.R., Spillantini M.G., Zolo P., Guazzelli M., Smith M.J., RA Hasegawa M., Redi F., Crowther R.A., Pietrini P., Ghetti B., RA Goedert M.; RT "Tau gene mutation G389R causes a tauopathy with abundant pick body- RT like inclusions and axonal deposits."; RL J. Neuropathol. Exp. Neurol. 58:1207-1226(1999). RN [26] RP VARIANTS PSP ASN-284 AND ALA-288. RX MEDLINE=20001812; PubMed=10534245; RA Higgins J.J., Adler R.L., Loveless J.M.; RT "Mutational analysis of the tau gene in progressive supranuclear RT palsy."; RL Neurology 53:1421-1424(1999). RN [27] RP VARIANT FTDP17 ASN-621. RX MEDLINE=99223277; PubMed=10208578; RA Iijima M., Tabira T., Poorkaj P., Schellenberg G.D., Trojanowski J.Q., RA Lee V.M.-Y., Schmidt M.L., Takahashi K., Nabika T., Matsumoto T., RA Yamashita Y., Yoshioka S., Ishino H.; RT "A distinct familial presenile dementia with a novel missense mutation RT in the tau gene."; RL NeuroReport 10:497-501(1999). RN [28] RP VARIANT DEMENTIA THR-573. RX MEDLINE=20539309; PubMed=11089577; RA Rizzini C., Goedert M., Hodges J.R., Smith M.J., Jakes R., Hills R., RA Xuereb J.H., Crowther R.A., Spillantini M.G.; RT "Tau gene mutation K257T causes a tauopathy similar to Pick's RT disease."; RL J. Neuropathol. Exp. Neurol. 59:990-1001(2000). CC -!- FUNCTION: Promotes microtubule assembly and stability, and might CC be involved in the establishment and maintenance of neuronal CC polarity. The C-terminus binds axonal microtubules while the N- CC terminus binds neural plasma membrane components, suggesting that CC tau functions as a linker protein between both. Axonal polarity is CC predetermined by tau localization (in the neuronal cell) in the CC domain of the cell body defined by the centrosome. The short CC isoforms allow plasticity of the cytoskeleton whereas the longer CC isoforms may preferentially play a role in its stabilization. CC -!- SUBCELLULAR LOCATION: Mostly found in the axons of neurons, in the CC cytosol and in association with plasma membrane components. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Comment=Additional isoforms seem to exist. Isoforms differ from CC each other by the presence or absence of up to 5 of the 15 CC exons. One of these optional exons contains the additional CC tau/MAP repeat; CC Name=PNS-tau; CC IsoId=P10636-1; Sequence=Displayed; CC Name=Fetal-tau; CC IsoId=P10636-2; Sequence=VSP_003175, VSP_003176, VSP_003177, CC VSP_003178, VSP_003179, VSP_003180, CC VSP_003181; CC Name=Tau-A; CC IsoId=P10636-3; Sequence=VSP_003176, VSP_003177, VSP_003179, CC VSP_003180, VSP_003181; CC Name=Tau-B; CC IsoId=P10636-4; Sequence=VSP_003177, VSP_003179, VSP_003180, CC VSP_003181; CC Name=Tau-C; Synonyms=Tau-3; CC IsoId=P10636-5; Sequence=VSP_003179, VSP_003180, VSP_003181; CC Name=Tau-D; CC IsoId=P10636-6; Sequence=VSP_003176, VSP_003177, VSP_003179, CC VSP_003180; CC Name=Tau-E; CC IsoId=P10636-7; Sequence=VSP_003177, VSP_003179, VSP_003180; CC Name=Tau-F; Synonyms=Tau-4; CC IsoId=P10636-8; Sequence=VSP_003179, VSP_003180; CC -!- TISSUE SPECIFICITY: Expressed in neurons. PNS-tau is expressed in CC the peripheral nervous system while the others are expressed in CC the central nervous system. CC -!- DEVELOPMENTAL STAGE: Four-repeat (type II) tau is expressed in an CC adult-specific manner and is not found in fetal brain, whereas CC three-repeat (type I) tau is found in both adult and fetal brain. CC -!- DOMAIN: The tau/MAP repeat binds to tubulin. Type I isoforms CC contain 3 repeats while type II isoforms contain 4 repeats. CC -!- PTM: Phosphorylation at serine and threonine residues in S-P or T- CC P motifs by proline-directed protein kinases (PDPK: CDC2, CDK5, CC GSK-3, MAPK) (only 2-3 sites per protein in interphase, seven-fold CC increase in mitosis, and in PHF-tau), and at serine residues in K- CC X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK) CC in Alzheimer's diseased brains. Phosphorylation decreases with CC age. Phosphorylation within tau's repeat domain or in flanking CC regions seems to reduce tau's interaction with, respectively, CC microtubules or plasma membrane components. CC -!- PTM: Glycation of PHF-tau, but not normal brain tau. Glycation is CC a non-enzymatic posttranslational modification that involves a CC covalent linkage between a sugar and an amino group of a protein CC molecule forming ketoamine. Subsequent oxidation, fragmentation CC and/or crosslinking of ketoamine leads to the production of CC advanced glycation endproducts (AGES). Glycation may play a role CC in stabilizing PHF aggregation leading to tangle formation in AD. CC -!- PTM: Phosphorylation on Ser-609, Ser-621, Ser-640 and Ser-672 in CC several isoforms during mitosis. CC -!- DISEASE: In Alzheimer disease, the neuronal cytoskeleton in the CC brain is progressively disrupted and replaced by tangles of paired CC helical filaments (PHF) and straight filaments, mainly composed of CC hyperphosphorylated forms of TAU (PHF-TAU or AD P-TAU). CC -!- DISEASE: Defects in MAPT are a cause of frontotemporal dementia CC and parkinsonism linked to chromosome 17 (FTDP17) [MIM:600274]; CC also historically termed Pick's disease. This form of CC frontotemporal dementia is characterized by presenile dementia CC with behavioral changes, deterioration of cognitive capacities and CC loss of memory. In some cases, parkinsonian symptoms are CC prominent. Neuropathological changes include frontotemporal CC atrophy often associated with atrophy of the basal ganglia, CC substantia nigra, amygdala. In most cases, protein tau deposits CC are found in glial cells and/or neurons. CC -!- DISEASE: Defects in MAPT are a cause of pallido-ponto-nigral CC degeneration (PPND) [MIM:168610]. The clinical features include CC ocular motility abnormalities, dystonia and urinary incontinence, CC beside progressive parkinsonism and dementia. CC -!- DISEASE: Defects in MAPT are a cause of corticobasal degeneration CC (CBD). It is marked by extrapyramidal signs and apraxia and can be CC associated with memory loss. Neuropathologic features may overlap CC Alzheimer's disease, progressive supranuclear palsy, and CC Parkinson's disease. CC -!- DISEASE: Defects in MAPT may predispose to progressive CC supranuclear palsy (PSP) [MIM:601104]; also known as steele- CC richardson-olszewski syndrome. It is characterized by akinetic- CC rigid syndrome, supranuclear gaze palsy, pyramidal tract CC dysfunction, pseudobulbar signs and cognitive capacities CC deterioration. Neurofibrillary tangles and gliosis but no amyloid CC plaques are found in diseased brains. CC -!- DISEASE: Defects in MAPT may be a cause of hereditary dysphasic CC disinhibition dementia (HDDD) [MIM:607485], a frontotemporal CC dementia characterized by progressive cognitive deficits with CC memory loss and personality changes, severe dysphasic disturbances CC leading to mutism, and hyperphagia. CC -!- SIMILARITY: Contains 4 Tau/MAP repeats. CC -!- WEB RESOURCE: Name=HotMolecBase; Note=Tau entry; CC URL="http://bioinformatics.weizmann.ac.il/hotmolecbase/entries/tau.htm"; CC -!- WEB RESOURCE: Name=Alzheimer Research Forum; Note=Tau mutations; CC URL="http://www.alzforum.org/res/com/mut/tau/default.asp"; CC -!- 100% SWISS-PROT IDENTITY: Q8X251. CC -!- INTERACTION: CC Q9H074:dkfzp586c051; NbExp=3; IntAct=EBI-81531, EBI-81519; CC Q04637:EIF4G1; NbExp=1; IntAct=EBI-81531, EBI-73711; CC -!- INTERACTION: CC Q8NI08:-; NbExp=1; IntAct=EBI-80809, EBI-80799; CC Q9Y618:ncor2; NbExp=1; IntAct=EBI-80809, EBI-80830; CC -!- INTERACTION: CC Self; NbExp=1; IntAct=EBI-123485, EBI-123485; CC Q9W158:cg4612; NbExp=1; IntAct=EBI-123485, EBI-89895; CC Q9VYI0:fne; NbExp=1; IntAct=EBI-123485, EBI-126770; CC -!- INTERACTION: CC Q8C1S0:2410018m14rik (xeno); NbExp=1; IntAct=EBI-394562, EBI-398761; CC Q15528:surf5; NbExp=1; IntAct=EBI-394562, EBI-394687; CC Q9CQI9:thrap6 (xeno); NbExp=1; IntAct=EBI-394562, EBI-309220; CC -!- INTERACTION: CC P13607:atp-alpha; NbExp=1; IntAct=EBI-126914, EBI-213208; CC P11450:fcp3c; NbExp=1; IntAct=EBI-126914, EBI-159556; DR EMBL; AF047863; AAC04277.1; -. DR EMBL; AF027491; AAC04277.1; JOINED. DR EMBL; AF047856; AAC04277.1; JOINED. DR EMBL; AF047857; AAC04277.1; JOINED. DR EMBL; AF027492; AAC04277.1; JOINED. DR EMBL; AF047858; AAC04277.1; JOINED. DR EMBL; AF027493; AAC04277.1; JOINED. DR EMBL; AF047859; AAC04277.1; JOINED. DR EMBL; AF047860; AAC04277.1; JOINED. DR EMBL; AF047862; AAC04277.1; JOINED. DR EMBL; AF027494; AAC04277.1; JOINED. DR EMBL; AF027495; AAC04277.1; JOINED. DR EMBL; AF027496; AAC04277.1; JOINED. DR EMBL; J03778; AAA60615.1; -. DR EMBL; X14474; CAA32636.1; -. DR EMBL; AF027491; AAC04279.1; -. DR EMBL; AF047856; AAC04279.1; JOINED. DR EMBL; AF047857; AAC04279.1; JOINED. DR EMBL; AF027492; AAC04279.1; JOINED. DR EMBL; AF027493; AAC04279.1; JOINED. DR EMBL; AF047860; AAC04279.1; JOINED. DR EMBL; AF047862; AAC04279.1; JOINED. DR EMBL; AF027494; AAC04279.1; JOINED. DR EMBL; AF027495; AAC04279.1; JOINED. DR EMBL; AF027496; AAC04279.1; JOINED. DR EMBL; AF047863; AAC04279.1; JOINED. DR EMBL; AF027491; AAC04278.1; -. DR EMBL; AF027492; AAC04278.1; JOINED. DR EMBL; AF027493; AAC04278.1; JOINED. DR EMBL; AF047860; AAC04278.1; JOINED. DR EMBL; AF047862; AAC04278.1; JOINED. DR EMBL; AF027495; AAC04278.1; JOINED. DR EMBL; AF027496; AAC04278.1; JOINED. DR EMBL; AF047863; AAC04278.1; JOINED. DR EMBL; BC000558; AAH00558.1; -. DR EMBL; M25298; AAA57264.1; -. DR PIR; I52232; I52232. DR PIR; JS0370; QRHUT1. DR PDB; 1I8H; NMR; A=541-553. DR HGNC; HGNC:6893; MAPT. DR MIM; 157140; -. DR MIM; 168610; -. DR MIM; 600274; -. DR MIM; 172700; -. DR MIM; 601104; -. DR MIM; 607485; -. DR GO; GO:0030424; C:axon; NAS. DR GO; GO:0005829; C:cytosol; TAS. DR GO; GO:0005875; C:microtubule associated complex; TAS. DR GO; GO:0005886; C:plasma membrane; TAS. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS. DR GO; GO:0007026; P:microtubule stabilization; NAS. DR InterPro; IPR002955; Tau_protein. DR InterPro; IPR001084; Tubulin_Tau. DR Pfam; PF00418; Tubulin-binding; 4. DR PRINTS; PR01261; TAUPROTEIN. ** PRINTS; PR01217; PRICHEXTENSN; FALSE_POS_1. DR PROSITE; PS00229; TAU_MAP; 4. KW 3D-structure; Acetylation; Alternative splicing; Alzheimer's disease; KW Cytoskeleton; Direct protein sequencing; Disease mutation; KW Glycoprotein; Microtubule; Phosphorylation; Polymorphism; Repeat. FT INIT_MET 0 0 FT REPEAT 560 590 Tau/MAP motif 1. FT REPEAT 591 621 Tau/MAP motif 2. FT REPEAT 622 652 Tau/MAP motif 3. FT REPEAT 653 684 Tau/MAP motif 4. FT MOD_RES 1 1 N-acetylalanine. FT MOD_RES 45 45 Phosphoserine (by PDPK) (partial). FT MOD_RES 49 49 Phosphothreonine (by PDPK) (partial). FT MOD_RES 469 469 Phosphothreonine (by PDPK) (partial). FT MOD_RES 483 483 Deamidated asparagine (in form Tau and FT form PHF-Tau) (partial). FT MOD_RES 491 491 Phosphothreonine (by PDPK) (partial). FT MOD_RES 497 497 Phosphothreonine (by PDPK) (partial). FT MOD_RES 514 514 Phosphoserine (by PDPK) (partial). FT MOD_RES 515 515 Phosphoserine (by PDPK) (partial). FT MOD_RES 518 518 Phosphoserine (by PDPK) (partial). FT MOD_RES 521 521 Phosphothreonine (by PDPK) (partial). FT MOD_RES 528 528 Phosphothreonine (by PDPK) (partial). FT MOD_RES 530 530 Phosphoserine (by PKA) (partial). FT MOD_RES 533 533 Phosphothreonine (by PDPK) (partial). FT MOD_RES 547 547 Phosphothreonine (by PDPK) (partial). FT MOD_RES 551 551 Phosphoserine (by PDPK) (partial). FT MOD_RES 578 578 Phosphoserine (by MARK1). FT MOD_RES 595 595 Deamidated asparagine (in form Tau and FT form PHF-Tau) (partial). FT MOD_RES 609 609 Phosphoserine (by MARK1) (in PHF-tau). FT MOD_RES 621 621 Phosphoserine (by MARK1) (in PHF-tau). FT MOD_RES 640 640 Phosphoserine (by MARK1) (in PHF-tau). FT MOD_RES 672 672 Phosphoserine (by MARK1) (in PHF-tau). FT MOD_RES 712 712 Phosphoserine (by PDPK) (partial). FT MOD_RES 720 720 Phosphoserine (by PDPK) (partial). FT MOD_RES 725 725 Phosphoserine (Potential). FT MOD_RES 729 729 Phosphoserine (Potential). FT MOD_RES 732 732 Phosphoserine (by CaMK2). FT MOD_RES 738 738 Phosphoserine (by PDPK) (partial). FT CARBOHYD 86 86 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 382 382 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 466 466 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 479 479 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 490 490 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 541 541 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 550 550 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 575 575 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 596 596 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 597 597 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 663 663 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 669 669 N-linked (Glc) (glycation); in PHF-tau. FT CARBOHYD 685 685 N-linked (Glc) (glycation); in PHF-tau. FT DISULFID 607 638 By similarity. FT VAR_SEQ 1 43 AEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAG FT LK -> LRALQQRKR (in isoform Fetal-tau). FT /FTId=VSP_003175. FT VAR_SEQ 44 72 Missing (in isoform Tau-A, isoform Tau-D FT and isoform Fetal-tau). FT /FTId=VSP_003176. FT VAR_SEQ 73 101 Missing (in isoform Tau-A, isoform Tau-B, FT isoform Tau-D, isoform Tau-E and isoform FT Fetal-tau). FT /FTId=VSP_003177. FT VAR_SEQ 102 103 Missing (in isoform Fetal-tau). FT /FTId=VSP_003178. FT VAR_SEQ 124 374 Missing (in isoform Tau-A, isoform Tau-B, FT isoform Tau-C, isoform Tau-D, isoform FT Tau-E, isoform Tau-F and isoform Fetal- FT tau). FT /FTId=VSP_003179. FT VAR_SEQ 394 459 Missing (in isoform Tau-A, isoform Tau-B, FT isoform Tau-C, isoform Tau-D, isoform FT Tau-E, isoform Tau-F and isoform Fetal- FT tau). FT /FTId=VSP_003180. FT VAR_SEQ 591 621 Missing (in isoform Tau-A, isoform Tau-B, FT isoform Tau-C and isoform Fetal-tau). FT /FTId=VSP_003181. FT VARIANT 284 284 D -> N (risk factor for progressive FT supranuclear palsy). FT /FTId=VAR_010340. FT VARIANT 288 288 V -> A (risk factor for progressive FT supranuclear palsy). FT /FTId=VAR_010341. FT VARIANT 440 440 H -> Y. FT /FTId=VAR_010342. FT VARIANT 446 446 S -> P. FT /FTId=VAR_010343. FT VARIANT 573 573 K -> T (in a dementia resembling Pick's FT disease). FT /FTId=VAR_010344. FT VARIANT 588 588 G -> V (in FTDP17). FT /FTId=VAR_010345. FT VARIANT 595 595 N -> K (in PPND). FT /FTId=VAR_010346. FT VARIANT 596 596 Missing (in FTDP17). FT /FTId=VAR_010347. FT VARIANT 617 617 P -> L (in FTDP17; most common mutation; FT reduction in the ability to promote FT microtubule assembly; accelerated FT aggregation of Tau into filaments). FT /FTId=VAR_010348. FT VARIANT 617 617 P -> S (in FTDP17 and in CBD; reduction FT in the ability to promote microtubule FT assembly). FT /FTId=VAR_010349. FT VARIANT 621 621 S -> N (in FTDP17; minimal parkinsonism; FT very early age of onset). FT /FTId=VAR_010350. FT VARIANT 653 653 V -> M (in FTDP17; ultrastructural and FT biochemical characteristics FT indistinguishable from Alzheimer's FT disease; accelerated aggregation of Tau FT into filaments). FT /FTId=VAR_010351. FT VARIANT 705 705 G -> R (in FTDP17; in a dementia FT resembling Pick's disease). FT /FTId=VAR_010352. FT VARIANT 722 722 R -> W (in FTDP17; accelerated FT aggregation of Tau into filaments). FT /FTId=VAR_010353. FT MUTAGEN 514 514 S->E: No association with plasma FT membrane. FT MUTAGEN 515 515 S->E: No association with plasma FT membrane. FT MUTAGEN 518 518 S->E: No association with plasma FT membrane. FT MUTAGEN 530 530 S->A: No decrease in microtubule-binding FT and nucleation activity after in vitro FT phosphorylation of mutant protein. FT MUTAGEN 547 547 T->A: 50% Decrease in microtubule-binding FT after in vitro phosphorylation of mutant FT protein. FT MUTAGEN 547 547 T->E: No association with plasma FT membrane. FT MUTAGEN 551 551 S->A: 70% decrease in microtubule-binding FT after in vitro phosphorylation of mutant FT protein. FT MUTAGEN 551 551 S->E: No association with plasma FT membrane. FT MUTAGEN 573 573 K->T: Reduced ability to promote FT microtubule assembly. FT MUTAGEN 578 578 S->A: 8% decrease in microtubule-binding FT after in vitro phosphorylation of mutant FT protein. FT MUTAGEN 712 712 S->E: No association with plasma FT membrane. FT MUTAGEN 720 720 S->E: No association with plasma FT membrane. FT MUTAGEN 725 725 S->E: No association with plasma FT membrane. FT MUTAGEN 729 729 S->E: No association with plasma FT membrane. FT MUTAGEN 738 738 S->E: No association with plasma FT membrane. ** ** ################# INTERNAL SECTION ################## **CL 17q21.1; **IS P10636-9 **ZC EMBL; BC000558; AAH00558.1; -. 11-05-2003 SQ SEQUENCE 757 AA; 78746 MW; 1426CEB011C1CC73 CRC64; AEPRQEFEVM EDHAGTYGLG DRKDQGGYTM HQDQEGDTDA GLKESPLQTP TEDGSEEPGS ETSDAKSTPT AEDVTAPLVD EGAPGKQAAA QPHTEIPEGT TAEEAGIGDT PSLEDEAAGH VTQEPESGKV VQEGFLREPG PPGLSHQLMS GMPGAPLLPE GPREATRQPS GTGPEDTEGG RHAPELLKHQ LLGDLHQEGP PLKGAGGKER PGSKEEVDED RDVDESSPQD SPPSKASPAQ DGRPPQTAAR EATSIPGFPA EGAIPLPVDF LSKVSTEIPA SEPDGPSVGR AKGQDAPLEF TFHVEITPNV QKEQAHSEEH LGRAAFPGAP GEGPEARGPS LGEDTKEADL PEPSEKQPAA APRGKPVSRV PQLKARMVSK SKDGTGSDDK KAKTSTRSSA KTLKNRPCLS PKLPTPGSSD PLIQPSSPAV CPEPPSSPKH VSSVTSRTGS SGAKEMKLKG ADGKTKIATP RGAAPPGQKG QANATRIPAK TPPAPKTPPS SGEPPKSGDR SGYSSPGSPG TPGSRSRTPS LPTPPTREPK KVAVVRTPPK SPSSAKSRLQ TAPVPMPDLK NVKSKIGSTE NLKHQPGGGK VQIINKKLDL SNVQSKCGSK DNIKHVPGGG SVQIVYKPVD LSKVTSKCGS LGNIHHKPGG GQVEVKSEKL DFKDRVQSKI GSLDNITHVP GGGNKKIETH KLTFRENAKA KTDHGAEIVY KSPVVSGDTS PRHLSNVSST GSIDMVDSPQ LATLADEVSA SLAKQGL // ID ZEA1_MAIZE STANDARD; PRT; 234 AA. AC P02859; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 01-MAY-2005 (Rel. 47, Last annotation update) DE Zein-alpha precursor (19 kDa) (Clone A30). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC PACCAD clade; Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=82081837; PubMed=6895552; RA Geraghty D., Peifer M.A., Rubenstein I., Messing J.; RT "The primary structure of a plant storage protein: zein."; RL Nucleic Acids Res. 9:5163-5174(1981). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=84207882; PubMed=6233138; RA Hu N.T., Peifer M.A., Heidecker G., Messing J., Rubenstein I.; RT "Primary structure of a genomic zein sequence of maize."; RL EMBO J. 1:1337-1342(1982). CC -!- FUNCTION: Zeins are major seed storage proteins. CC -!- MISCELLANEOUS: The alpha zeins of 19 kDa and 22 kDa account for CC 70% of the total zein fraction. They are encoded by a large CC multigene family. CC -!- MISCELLANEOUS: Structurally, 19 kDa and 19 kDa zeins are composed CC of nine adjacent, topologically antiparallel helices clustered CC within a distorted cylinder. CC -!- SIMILARITY: Belongs to the zein family. DR EMBL; V01481; CAA24728.1; -; mRNA. DR EMBL; V01481; CAA24728.1; -; mRNA.{EP1} DR PIR; A90967; ZIZM3. DR MaizeGDB; 58096; -. DR InterPro; IPR002530; Zein. DR Pfam; PF01559; Zein; 1. KW Multigene family; Repeat; Seed storage protein; Signal; KW Storage protein. FT SIGNAL 1 21 FT CHAIN 22 234 Zein-alpha. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 234 AA; 25404 MW; 502A99D438CA5DAA CRC64; MAAKIFCLLM LLGLSASAAT ATIFPQCSQA PIASLLPPYL SPAVSSVCEN PILQPYRIQQ AIAAGILPLS PLFLQQSSAL LQQLPLVHLL AQNIRAQQLQ QLVLANLAAY SQQQQFLPFN QLAALNSASY LQQQQLPFSQ LPAAYPQQFL PFNQLAALNS PAYLQQQQLL PFSQLAGVSP ATFLTQPQLL PFYQHAAPNA GTLLQLQQLL PFNQLALTNL AAFYQQPIIG GALF // ID ENTK_HUMAN Reviewed; 1019 AA. AC P98073; Q2NKL7; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 22-JUL-2008, entry version 94. DE RecName: Full=Enteropeptidase; DE EC=3.4.21.9; DE AltName: Full=Enterokinase; DE AltName: Full=Serine protease 7; DE Contains: DE RecName: Full=Enteropeptidase non-catalytic heavy chain; DE Contains: DE RecName: Full=Enteropeptidase catalytic light chain; DE Flags: Precursor; GN Name=PRSS7; Synonyms=ENTK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Duodenum; RX MEDLINE=95234679; PubMed=7718557; DOI=10.1021/bi00014a008; RA Kitamoto Y., Veile R.A., Donis-Keller H., Sadler J.E.; RT "cDNA sequence and chromosomal localization of human enterokinase, the RT proteolytic activator of trypsinogen."; RL Biochemistry 34:4562-4568(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN ENTEROKINASE RP DEFICIENCY. RX MEDLINE=21606074; PubMed=11719902; DOI=10.1086/338456; RA Holzinger A., Maier E.M., Buck C., Mayerhofer P.U., Kappler M., RA Haworth J.C., Moroz S.P., Hadorn H.-B., Sadler J.E., Roscher A.A.; RT "Mutations in the proenteropeptidase gene are the molecular cause of RT congenital enteropeptidase deficiency."; RL Am. J. Hum. Genet. 70:20-25(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-134 RP AND PRO-732. RX MEDLINE=20289799; PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., RA Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 749-1019. RC TISSUE=Duodenum; RX MEDLINE=94329561; PubMed=8052624; RA Kitamoto Y., Yuan X., Wu Q., McCourt D.W., Sadler J.E.; RT "Enterokinase, the initiator of intestinal digestion, is a mosaic RT protease composed of a distinctive assortment of domains."; RL Proc. Natl. Acad. Sci. U.S.A. 91:7588-7592(1994). CC -!- FUNCTION: Responsible for initiating activation of pancreatic CC proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase CC A). It catalyzes the conversion of trypsinogen to trypsin which in CC turn activates other proenzymes including chymotrypsinogen, CC procarboxypeptidases, and proelastases. CC -!- CATALYTIC ACTIVITY: Activation of trypsinogen by selective CC cleavage of 6-Lys-|-Ile-7 bond. CC -!- SUBUNIT: Heterodimer of a catalytic (light) chain and a CC multidomain (heavy) chain linked by a disulfide bond. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane CC protein (Probable). CC -!- TISSUE SPECIFICITY: Intestinal brush border. CC -!- PTM: The chains are derived from a single precursor that is CC cleaved by a trypsin-like protease. CC -!- DISEASE: Defects in PRSS7 are a cause of enterokinase deficiency CC [MIM:226200]; a life-threatening intestinal malabsorption disorder CC characterized by diarrhea and failure to thrive. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC -!- SIMILARITY: Contains 2 CUB domains. CC -!- SIMILARITY: Contains 2 LDL-receptor class A domains. CC -!- SIMILARITY: Contains 1 MAM domain. CC -!- SIMILARITY: Contains 1 peptidase S1 domain. CC -!- SIMILARITY: Contains 1 SEA domain. CC -!- SIMILARITY: Contains 1 SRCR domain. DR EMBL; U09860; AAC50138.1; -; mRNA. DR EMBL; Y19124; CAB65555.1; -; Genomic_DNA. DR EMBL; Y19125; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19126; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19127; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19128; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19129; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19130; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19131; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19132; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19133; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19134; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19135; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19136; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19137; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19138; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19139; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19140; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19141; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19142; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; Y19143; CAB65555.1; JOINED; Genomic_DNA. DR EMBL; AL163218; CAB90392.1; -; Genomic_DNA. DR EMBL; AL163217; CAB90389.1; -; Genomic_DNA. DR EMBL; BC111749; AAI11750.1; -; mRNA. DR PIR; A56318; A56318. DR RefSeq; NP_002763.1; -. DR UniGene; Hs.149473; -. DR HSSP; P98072; 1EKB. DR SMR; P98073; 785-1019. DR MEROPS; S01.156; -. DR Ensembl; ENSG00000154646; Homo sapiens. DR GeneID; 5651; -. DR KEGG; hsa:5651; -. DR H-InvDB; HIX0040924; -. DR HGNC; HGNC:9490; PRSS7. DR HPA; HPA015611; -. DR MIM; 226200; phenotype. DR MIM; 606635; gene. DR PharmGKB; PA33839; -. DR HOGENOM; P98073; -. DR HOVERGEN; P98073; -. DR LinkHub; P98073; -. DR ArrayExpress; P98073; -. DR CleanEx; HS_PRSS7; -. DR GermOnline; ENSG00000154646; Homo sapiens. DR GO; GO:0005903; C:brush border; TAS:ProtInc. DR InterPro; IPR000859; CUB. DR InterPro; IPR002172; LDL_rcpt_classA_cys-rich. DR InterPro; IPR000998; MAM. DR InterPro; IPR011163; Pept_S1A_enterop. DR InterPro; IPR001254; Peptidase_S1_S6. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR000082; SEA. DR InterPro; IPR001190; Srcr_rcpt. DR InterPro; IPR017448; Srcr_rcpt-rel. DR Gene3D; G3DSA:2.60.120.290; CUB; 2. DR Gene3D; G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 1. DR Pfam; PF00431; CUB; 2. DR Pfam; PF00057; Ldl_recept_a; 2. DR Pfam; PF00629; MAM; 1. DR Pfam; PF01390; SEA; 1. DR Pfam; PF00530; SRCR; 1. DR Pfam; PF00089; Trypsin; 1. DR PIRSF; PIRSF001138; Enteropeptidase; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR PRINTS; PR00261; LDLRECEPTOR. DR PRINTS; PR00020; MAMDOMAIN. DR SMART; SM00042; CUB; 2. DR SMART; SM00192; LDLa; 2. DR SMART; SM00137; MAM; 1. DR SMART; SM00200; SEA; 1. DR SMART; SM00020; Tryp_SPc; 1. DR PROSITE; PS01180; CUB; 2. DR PROSITE; PS01209; LDLRA_1; 2. DR PROSITE; PS50068; LDLRA_2; 2. DR PROSITE; PS00740; MAM_1; 1. DR PROSITE; PS50060; MAM_2; 1. DR PROSITE; PS50024; SEA; 1. DR PROSITE; PS00420; SRCR_1; FALSE_NEG. DR PROSITE; PS50287; SRCR_2; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 2: Evidence at transcript level; KW Glycoprotein; Hydrolase; Lipoprotein; Membrane; Myristate; KW Polymorphism; Protease; Repeat; Serine protease; Signal-anchor; KW Transmembrane; Zymogen. FT CHAIN 1 784 Enteropeptidase non-catalytic heavy FT chain. FT /FTId=PRO_0000027719. FT CHAIN 785 1019 Enteropeptidase catalytic light chain. FT /FTId=PRO_0000027720. FT TOPO_DOM 1 18 Cytoplasmic (Potential). FT TRANSMEM 19 47 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 48 1019 Extracellular (Potential). FT DOMAIN 52 169 SEA. FT DOMAIN 182 223 LDL-receptor class A 1. FT DOMAIN 225 334 CUB 1. FT DOMAIN 342 504 MAM. FT DOMAIN 524 634 CUB 2. FT DOMAIN 641 679 LDL-receptor class A 2. FT DOMAIN 678 771 SRCR. FT DOMAIN 785 1019 Peptidase S1. FT ACT_SITE 825 825 Charge relay system (By similarity). FT ACT_SITE 876 876 Charge relay system (By similarity). FT ACT_SITE 971 971 Charge relay system (By similarity). FT LIPID 2 2 N-myristoyl glycine (Potential). FT CARBOHYD 116 116 N-linked (GlcNAc...) (Potential). FT CARBOHYD 147 147 N-linked (GlcNAc...) (Potential). FT CARBOHYD 179 179 N-linked (GlcNAc...) (Potential). FT CARBOHYD 328 328 N-linked (GlcNAc...) (Potential). FT CARBOHYD 335 335 N-linked (GlcNAc...) (Potential). FT CARBOHYD 388 388 N-linked (GlcNAc...) (Potential). FT CARBOHYD 440 440 N-linked (GlcNAc...) (Potential). FT CARBOHYD 470 470 N-linked (GlcNAc...) (Potential). FT CARBOHYD 503 503 N-linked (GlcNAc...) (Potential). FT CARBOHYD 534 534 N-linked (GlcNAc...) (Potential). FT CARBOHYD 630 630 N-linked (GlcNAc...) (Potential). FT CARBOHYD 682 682 N-linked (GlcNAc...) (Potential). FT CARBOHYD 706 706 N-linked (GlcNAc...) (Potential). FT CARBOHYD 725 725 N-linked (GlcNAc...) (Potential). FT CARBOHYD 848 848 N-linked (GlcNAc...) (Potential). FT CARBOHYD 887 887 N-linked (GlcNAc...) (Potential). FT CARBOHYD 909 909 N-linked (GlcNAc...) (Potential). FT CARBOHYD 949 949 N-linked (GlcNAc...) (Potential). FT DISULFID 184 197 By similarity. FT DISULFID 191 210 By similarity. FT DISULFID 204 221 By similarity. FT DISULFID 225 253 By similarity. FT DISULFID 524 552 By similarity. FT DISULFID 643 655 By similarity. FT DISULFID 650 668 By similarity. FT DISULFID 662 677 By similarity. FT DISULFID 757 767 By similarity. FT DISULFID 772 896 Interchain (between heavy and light FT chains) (By similarity). FT DISULFID 810 826 By similarity. FT DISULFID 910 977 By similarity. FT DISULFID 941 956 By similarity. FT DISULFID 967 995 By similarity. FT VARIANT 65 65 T -> I (in dbSNP:rs35987974). FT /FTId=VAR_031686. FT VARIANT 77 77 K -> R (in dbSNP:rs2824804). FT /FTId=VAR_021940. FT VARIANT 134 134 Q -> E (in dbSNP:rs2824790). FT /FTId=VAR_031687. FT VARIANT 545 545 S -> C (in dbSNP:rs8134187). FT /FTId=VAR_031688. FT VARIANT 641 641 E -> K (in dbSNP:rs2273204). FT /FTId=VAR_020175. FT VARIANT 660 660 N -> H (in dbSNP:rs11088674). FT /FTId=VAR_024292. FT VARIANT 732 732 S -> P (in dbSNP:rs2824721). FT /FTId=VAR_031689. FT VARIANT 828 828 Y -> C (in dbSNP:rs8130110). FT /FTId=VAR_031690. FT CONFLICT 754 771 SQQCLQDSLIRLQCNHKS -> RRNAKNEIDALSPIILIA FT (in Ref. 3; CAB90389). ** ** ################# INTERNAL SECTION ################## **CL 21q21.1; **YY VAR_031687: AA shown in Swiss-Prot is the most frequent; 19-MAR-2007. **YY VAR_031688: AA shown in Swiss-Prot is the most frequent; 19-MAR-2007. **ZB NAG, 23-Mar-2007; SQ SEQUENCE 1019 AA; 112924 MW; B6AAA245F6D4A563 CRC64; MGSKRGISSR HHSLSSYEIM FAALFAILVV LCAGLIAVSC LTIKESQRGA ALGQSHEARA TFKITSGVTY NPNLQDKLSV DFKVLAFDLQ QMIDEIFLSS NLKNEYKNSR VLQFENGSII VVFDLFFAQW VSDQNVKEEL IQGLEANKSS QLVTFHIDLN SVDILDKLTT TSHLATPGNV SIECLPGSSP CTDALTCIKA DLFCDGEVNC PDGSDEDNKM CATVCDGRFL LTGSSGSFQA THYPKPSETS VVCQWIIRVN QGLSIKLSFD DFNTYYTDIL DIYEGVGSSK ILRASIWETN PGTIRIFSNQ VTATFLIESD ESDYVGFNAT YTAFNSSELN NYEKINCNFE DGFCFWVQDL NDDNEWERIQ GSTFSPFTGP NFDHTFGNAS GFYISTPTGP GGRQERVGLL SLPLDPTLEP ACLSFWYHMY GENVHKLSIN ISNDQNMEKT VFQKEGNYGD NWNYGQVTLN ETVKFKVAFN AFKNKILSDI ALDDISLTYG ICNGSLYPEP TLVPTPPPEL PTDCGGPFEL WEPNTTFSST NFPNSYPNLA FCVWILNAQK GKNIQLHFQE FDLENINDVV EIRDGEEADS LLLAVYTGPG PVKDVFSTTN RMTVLLITND VLARGGFKAN FTTGYHLGIP EPCKADHFQC KNGECVPLVN LCDGHLHCED GSDEADCVRF FNGTTNNNGL VRFRIQSIWH TACAENWTTQ ISNDVCQLLG LGSGNSSKPI FSTDGGPFVK LNTAPDGHLI LTPSQQCLQD SLIRLQCNHK SCGKKLAAQD ITPKIVGGSN AKEGAWPWVV GLYYGGRLLC GASLVSSDWL VSAAHCVYGR NLEPSKWTAI LGLHMKSNLT SPQTVPRLID EIVINPHYNR RRKDNDIAMM HLEFKVNYTD YIQPICLPEE NQVFPPGRNC SIAGWGTVVY QGTTANILQE ADVPLLSNER CQQQMPEYNI TENMICAGYE EGGIDSCQGD SGGPLMCQEN NRWFLAGVTS FGYKCALPNR PGVYARVSRF TEWIQSFLH // ID Q27861_9HYMN Unreviewed; 41 AA. AC Q27861; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 22-JUL-2008, entry version 32. DE SubName: Full=Histone H3{EI1}; DE EC=3.4.21.9; DE AltName: Full=Enterokinase{EI5}; DE Flags: Fragment{EI8}; Precursor{EI7}; GN Name=histone H3II{EI1}; OS Tetrahymena hegewischi. OC Eukaryota; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae; OC Tetrahymena. OX NCBI_TaxID=5923{EI1}; RN [1]{EI1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=KP7{EI1}; RX MEDLINE=92203991; PubMed=1552842; RA Sadler L.A., Brunk C.F.; RT "Phylogenetic relationships and unusual diversity in histone H4 RT proteins within the Tetrahymena pyriformis complex."; RL Mol. Biol. Evol. 9:70-84(1992). CC -!- SIMILARITY: Belongs to the histone H3 family{EA4}. DR EMBL; M73210; AAA75643.1; -; Genomic_DNA.{EI1} DR GO; GO:0000786; C:nucleosome; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR000164; Histone_H3. DR Gene3D; G3DSA:1.10.20.10; Histone-fold; 1. DR PANTHER; PTHR11426; Histone_H3; 1. DR PRINTS; PR00622; HISTONEH3. DR PROSITE; PS00322; HISTONE_H3_1; UNKNOWN_1. PE 3: Inferred from homology; FT NON_TER 41 41 {EI1} ** ** ################# INTERNAL SECTION ################## **EV EA4; Rulebase; TREMBL; RU004194V0.230S0031185; 11-MAR-2008. **EV EI1; EMBL; -; AAA75643.1; 23-APR-2004. **PM Gene3D; G3DSA:1.10.20.10; Histone-fold; 2; 40; T; 16-NOV-2006; **PM PANTHER; PTHR11426; Histone_H3; 1; 40; T; 27-APR-2007; **PM PRINTS; PR00622; HISTONEH3; 17; 31; T; 30-SEP-2005; **PM PRINTS; PR00622; HISTONEH3; 34; 41; T; 30-SEP-2005; **PM PRINTS; PR00622; HISTONEH3; 3; 17; T; 30-SEP-2005; **PM PROSITE; PS00322; HISTONE_H3_1; 15; 21; ?; 07-OCT-2007; SQ SEQUENCE 41 AA; 4316 MW; E343DF37507B58D9 CRC64; MARTKQTARK STGAKAPRKQ LASKAARKSA PATGGIKKPH E // ID CAPSD_PCV2 Reviewed; 233 AA. AC O56129; Q8BB11; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 05-APR-2011, entry version 41. DE RecName: Full=Capsid protein; GN Name=Cap; ORFNames=ORF2; OS Porcine circovirus 2 (PCV2). OC Viruses; ssDNA viruses; Circoviridae; Circovirus. OX NCBI_TaxID=85708; OH NCBI_TaxID=9823; Sus scrofa (Pig). DR EMBL; AF027217; AAC59463.1; -; Genomic_DNA. DR EMBL; AY094619; AAM21849.1; -; Genomic_DNA. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW. DR GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW. DR InterPro; IPR003383; Circovirus_ORF2_capsid. DR Pfam; PF02443; Circo_capsid; 1. PE 1: Evidence at protein level; KW Capsid protein; Clathrin- and KW caveolin-independent endocytosis of virus by host; Complete proteome; KW DNA-binding; Host nucleus; Host-virus interaction; KW Initiation of viral infection; T=1 icosahedral capsid protein; KW Viral attachment to host cell; Viral penetration into host cytoplasm; KW Viral penetration into host nucleus; Virion; KW Virus endocytosis by host. FT CHAIN 1 233 Capsid protein. FT /FTId=PRO_0000133085. ** ** ################# INTERNAL SECTION ################## **ZA PHL, 07-SEP-2005; **ZB CHH, 25-MAY-2009; CHH, 25-JAN-2011; CHH, 14-MAR-2011; SQ SEQUENCE 233 AA; 27897 MW; 3C664C4B4E83AB58 CRC64; MTYPRRRYRR RRHRPRSHLG QILRRRPWLV HPRHRYRWRR KNGIFNTRLS RTFGYTVKAT TVRTPSWAVD MMRFNIDDFV PPGGGTNKIS IPFEYYRIRK VKVEFWPCSP ITQGDRGVGS TAVILDDNFV TKATALTYDP YVNYSSRHTI PQPFSYHSRY FTPKPVLDST IDYFQPNNKR TQLWLRLQTS RNVDHVGLGT AFENSIYDQD YNIRVTMYVQ FREFNLKDPP LKP // ID PCLO_RAT Reviewed; 1380 AA. AC Q9JKS6; Q9JLT1; DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 14-MAY-2014, entry version 108. DE RecName: Full=Protein piccolo {ECO:0000269|PubMed:11285225}; DE AltName: Full=Aczonin; DE AltName: Full=Multidomain presynaptic cytomatrix protein; GN Name=vcp {ECO:0000313|EMBL:AAH50488.1, GN ECO:0000313|ZFIN:ZDB-GENE-030131-5408}; Synonyms=cdc48; GN ORFNames=si:ch211-113n10.2; OG Plasmid pCP301 {ECO:0000313|EMBL:AAH50488.1, OG ECO:0000269|PubMed:11285225}, Plasmid pWR100, Plasmid pINV_F6_M1382, OG and Plasmid pSF5; Chloroplast. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] {ECO:0000269|PubMed:11285225} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH RABAC1. RX PubMed=10707984; DOI=10.1016/S0896-6273(00)80883-1; RA Fenster S.D., Chung W.J., Zhai R., Cases-Langhoff C., Voss B., RA Garner A.M., Kaempf U., Kindler S., Gundelfinger E.D., Garner C.C.; RT "Piccolo, a presynaptic zinc finger protein structurally related to RT bassoon."; RL Neuron 25:203-214(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Fenster S.D., Cases-Langhoff C., Gundelfinger E.D., Garner C.C.; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: May act as a scaffolding protein involved in the CC organization of synaptic active zones and in synaptic vesicle CC trafficking (By similarity). {ECO:0000250|UniProtKB:Q9QYX7}. CC -!- SUBUNIT: Interacts with RABAC1/PRA1, RIMS2 and profilin (By CC similarity). {ECO:0000269|PubMed:10707984}. CC -!- INTERACTION: CC Q920M9:Siah1; NbExp=2; IntAct=EBI-2271602, EBI-957514; CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- SUBCELLULAR LOCATION: Cell junction, synapse. Note=Concentrated at CC presynaptic side of synaptic junctions. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane CC {ECO:0000269|PubMed:12766230, ECO:0000269|Ref.11}; Peripheral CC membrane protein {ECO:0000269|PubMed:12766230, CC ECO:0000269|PubMed:18431481}. Plastid, chloroplast stroma. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9JKS6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9JKS6-2; Sequence=VSP_003930, VSP_003931; CC Name=3; CC IsoId=Q9JKS6-3; Sequence=VSP_018194; CC -!- RNA EDITING: Modified_positions=1, 4, 18, 33 CC {ECO:0000269|PubMed:10707984, ECO:0000269|PubMed:11285225}, 34, CC 72, 80, 86, 95, 121, 123, 154, 155, 156, 163, 169, 193, 196, 233, CC 295, 346; Note=The initiator methionine is created by RNA editing. CC The nonsense codons at positions 72, 121, 169, 193 and 346 are CC modified to sense codons. {ECO:0000269|PubMed:10707984}. CC -!- RNA EDITING: Modified_positions=Not_applicable; Note=a. CC -!- DOMAIN: C2 domain 1 is involved in binding calcium and CC phospholipids. Calcium binds with low affinity but with high CC specificity and induces a large conformational change. CC {ECO:0000269|PubMed:11285225}. CC -!- DISEASE: Spastic paraplegia 4, autosomal dominant (SPG4) CC [MIM:182601]: A form of spastic paraplegia, a neurodegenerative CC disorder characterized by a slow, gradual, progressive weakness CC and spasticity of the lower limbs. Rate of progression and the CC severity of symptoms are quite variable. Initial symptoms may CC include difficulty with balance, weakness and stiffness in the CC legs, muscle spasms, and dragging the toes when walking. In some CC forms of the disorder, bladder symptoms (such as incontinence) may CC appear, or the weakness and stiffness may spread to other parts of CC the body. {ECO:0000269|PubMed:10610178, CC ECO:0000269|PubMed:10699187, ECO:0000269|PubMed:11015453, CC ECO:0000269|PubMed:11039577, ECO:0000269|PubMed:11087788, CC ECO:0000269|PubMed:11309678, ECO:0000269|PubMed:11843700, CC ECO:0000269|PubMed:11985387, ECO:0000269|PubMed:12124993, CC ECO:0000269|PubMed:12161613, ECO:0000269|PubMed:12163196, CC ECO:0000269|PubMed:12202986, ECO:0000269|PubMed:12460147, CC ECO:0000269|PubMed:12552568, ECO:0000269|PubMed:12939659, CC ECO:0000269|PubMed:14732620, ECO:0000269|PubMed:15159500, CC ECO:0000269|PubMed:15210521, ECO:0000269|PubMed:15248095, CC ECO:0000269|PubMed:15326248, ECO:0000269|PubMed:15482961, CC ECO:0000269|PubMed:16682546, ECO:0000269|PubMed:16684598, CC ECO:0000269|PubMed:17594340, ECO:0000269|PubMed:20214791, CC ECO:0000269|PubMed:20550563, ECO:0000269|PubMed:20562464, CC ECO:0000269|PubMed:20718791, ECO:0000269|PubMed:20932283}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.45 mM for ATP {ECO:0000269|PubMed:15716377, CC ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:22637577}; CC Vmax=1.2 nmol/min/ug enzyme {ECO:0000269|PubMed:15716377, CC ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:22637577}; CC Note=Kinetic parameters shown are for full length enzyme. N- CC terminally truncated spastin (residues 228-616), which has been CC shown to exhibit full severing activity, shows a basal ATP CC turnover rate of 0.78 sec(-1) in the absence of microtubules, a CC KM of 0.16 mM for ATP, and the ATP turnover rate is extrapolated CC to 3.83 sec(-1) in the presence of microtubules. ATPase activity CC shows non-Michaelis-Menten kinetics in the presence of CC microtubules, but is close to non-cooperative behavior in their CC absence (PubMed:22637577). {ECO:0000269|PubMed:15716377, CC ECO:0000269|PubMed:17389232, ECO:0000269|PubMed:22637577}; CC -!- SIMILARITY: Contains 2 C2 domains. {ECO:0000269|PubMed:11285225}. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=This alternative splicing is restricted to C4 species of CC Flaveria. {ECO:0000269|PubMed:7550380, CC ECO:0000269|PubMed:8771790, ECO:0000269|Ref.3}; CC Name=1; Synonyms=Long, Long variant 1; CC IsoId=Q9UBP0-1; Sequence=Displayed; CC Note=No experimental confirmation available. {ECO:0000305}; CC Name=2; Synonyms=Long variant 2; CC IsoId=Q9UBP0-2; Sequence=VSP_000024; CC -!- SEQUENCE CAUTION: CC Sequence=AAH52843.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=AAI06097.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAC33868.1; Type=Frameshift; Positions=1759; CC -!- RNA EDITING: Modified_positions=207 {ECO:0000269|PubMed:17018572, CC ECO:0000269|Ref.6}; Note=Partially edited. Target of Adar. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR Pfam; PF00168; C2; 2. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF05715; zf-piccolo; 2. DR SMART; SM00239; C2; 2. DR SMART; SM00228; PDZ; 1. DR SUPFAM; SSF49562; SSF49562; 2. DR SUPFAM; SSF50156; SSF50156; 1. DR SUPFAM; SSF57903; SSF57903; 2. DR PROSITE; PS50004; C2; 2. DR PROSITE; PS50106; PDZ; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; KW Calcium/phospholipid-binding; Cell junction; Complete proteome; KW Glycoprotein; Metal-binding; Phosphoprotein; Reference proteome; KW Repeat; Synapse; Zinc; Zinc-finger. FT CHAIN 1 5085 Protein piccolo. FT /FTId=PRO_0000058252. FT TRANSIT 1 29 MITOCHONDRION{EC2}. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:22814378}. FT DOMAIN 4442 4536 PDZ.{ECO:0000269|PubMed:11285225}. FT DOMAIN 4653 4752 C2 1. {ECO:0000269|PubMed:11285225}. FT DOMAIN 4968 5059 C2 2. {ECO:0000269|PubMed:11285225}. FT ZN_FING 523 547 C4-type (Potential). FT {ECO:0000269|PubMed:10707984}. FT ZN_FING 1010 1033 C4-type (Potential). FT {ECO:0000269|PubMed:10707984}. FT REGION 372 491 12 X 10 AA tandem approximate repeats of FT P-A-K-P-Q-P-Q-Q-P-X. FT COMPBIAS 2351 2362 Poly-Pro. {ECO:0000269|PubMed:11285225}. FT MOD_RES 3 3 Phosphoserine. FT MOD_RES 1778 1778 Phosphoserine (By similarity). FT MOD_RES 3374 3374 Phosphoserine (By similarity). FT MOD_RES 3392 3392 Phosphothreonine (By similarity). FT CARBOHYD 2702 2702 O-linked (GlcNAc) (By similarity). FT CARBOHYD 2976 2976 O-linked (GlcNAc) (By similarity). FT VAR_SEQ 4687 4695 Missing (in isoform 3). FT /FTId=VSP_018194. FT VAR_SEQ 4876 4880 TKPTN -> SKRRK (in isoform 2). FT {ECO:0000269|PubMed:11285225}. FT /FTId=VSP_003930. FT VAR_SEQ 4881 5085 Missing (in isoform 2). FT {ECO:0000269|PubMed:11285225}. FT /FTId=VSP_003931. FT VARIANT 3 3 A -> L{EC2}. FT /FTId=VAR_000001. FT VARIANT 3 3 A -> LFSJFSHLJSDHFLSJLFHSJLLSJKDHFLSKJFHJ FT . FT VARIANT 23 23 Missing. {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:8906617, FT ECO:0000269|PubMed:9009220, FT ECO:0000269|PubMed:9921897}. FT VARIANT 386 386 N -> S (in SPG4). FT MUTAGEN 4668 4668 D->A: Complete loss of calcium-binding FT and calcium-dependent phospholipid FT binding activity. FT {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4674 4674 D->A: Complete loss of calcium-binding FT and calcium-dependent phospholipid FT binding activity. FT {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4688 4689 VM->SS: 10-fold increase in affinity for FT calcium. {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4688 4688 V->S: Small increase in affinity for FT calcium. {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4689 4689 M->S: Increased affinity for calcium. FT {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4690 4691 VV->SS: 10-fold increase in affinity for FT calcium. {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4692 4693 QN->AA: Moderate increase in affinity for FT calcium. {ECO:0000269|PubMed:11285225}. FT MUTAGEN 4694 4694 A->S: No effect on calcium-binding FT activity. {ECO:0000269|PubMed:11285225}. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 1380 AA; 144367 MW; 13497D39F4CE32B8 CRC64; MGNEASLEGE GLPEGLAAAA GAGGSGSALH PGIPAGMEAD LSQLSEEERR QIAAVMSRAQ GLPKGSVPPA AAESPSMHRK QELDSSQAPQ QPGKPPDPGR PTQPGLSKSR TTDTFRSEQK LPGRSPSTIS LKESKSRTDF KEEYKSSMMP GFFSDVNPLS AVSSVVNKFN PFDLISDSEA SQEETTKKQK VVQKEQGKSE GMAKPPLQQP SPKPIPKQQG QVKEVIQQDS SPKSVSSQQA EKVKPQAPGT GKPSQQSPAQ TPAQQASPGK PVAQQPGSAK ATVQQPGPAK SPAQPAGTGK SPAQPPAKTP GQQAGLEKTS SSQQPGPKSL AQTPGHGKFP LGPVKSPAQQ PGTAKHPAQQ PGPQTAAKVP GPTKTPAQQS GPGKTPAQQP GPTKPSPQQP IPAKPQPQQP VATKTQPQQS APAKPQPQQP APAKPQPQQP TPAKPQPQPP TPAKPQPQPP TATKPQPQPP TATKPHHQQP GLAKPSAQQP TKSISQTVTG RPLQPPPTSA AQTPAQGLSK TICPLCNTTE LLLHIPEKAN FNTCTECQST VCSLCGFNPN PHLTEIKEWL CLNCQMQRAL GGDLAAAIPS SPQPTPKAAT APTATASKSP VPSQQASPKK EPPSKQDSPK ALESKKPPEP KKPPEPKKPP EPKKPPPLVK QPTLHGPTPA TAPQLPVAEA LPEPAPPKEP SGPLPEQAKA PVGDVEPKQP KMTETRADIQ SSSTTKPDIL SSQVQSQAQV KTASPLKTDS AKPSQSFPPT GEKTTPLDSK AMPRPASDSK IISQPGPGSE SKDPKHIDPI QKKDEPKKAQ PKGSPKPETK PVPKGSPTPS GTRPTAGQAA PPSQQPPKPQ EQSRRFSLNL GGITDAPKSQ PTTPQETVTG KLFGFGASIF SQASNLISTA GQQGPHPQTG PAAPSKQAPT PSQSPAAQGP AKSTGQLPPA PAKATAVKKE AKAAAAENLE SKPEQAPTAK KTEKDKKPPP AKVGKPPPSE PEKAVPAHKP DKTTKPKPAC PLCRTELNLG SQEPPNFNTC TECKNQVCNL CGFNPTPHLT EIQEWLCLNC QTQRAISGQL GDMGKMPPAP SGPKASPMPA PAEPSSQKTP TGTQVKGKKK EAEGKTEAEK PVPEKETASI EKTPPMVTTD QKLEESEGKK SKVSALPEKK PSEEEKAISA DKKERKPPAE EKPPLEEKKP IPVDKKLPPE AKPLSSEGEE KHEILKAHVQ IPEEEPTGKV AAKAGEEEQQ PDSRPEALPG ATPLTLPKAG EKERAVAQPQ AEGSSKDGQG ERSKEKTEKE EDKSDTSSSQ QPKSPQGLSD TGYSSDGISG SLGEIPSLIP SDEKDLLKGL KKDSFSQESS PSSPSDLAKL ESTVLSILEA QASTLVGEKA // ID RIBA1_ARATH Reviewed; 543 AA. AC P47924; Q9SBA8; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 10-JAN-2003, sequence version 2. DT 24-JUN-2015, entry version 119. DE RecName: Full=Bifunctional riboflavin biosynthesis protein RIBA 1, chloroplastic; DE Short=AtRIBA1; DE Includes: DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase; DE Short=DHBP synthase; DE EC=4.1.99.12; DE Flags: Precursor; GN Name=RIBA1; Synonyms=RIBBA; OrderedLocusNames=At5g64300; GN ORFNames=MSJ1.14; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae; OC Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10783978; DOI=10.1016/S0031-9422(00)00013-3; RA Herz S.W., Eberhardt S., Bacher A.; RT "Biosynthesis of riboflavin in plants. The ribA gene of Arabidopsis RT thaliana specifies a bifunctional GTP cyclohydrolase II/3,4-dihydroxy- RT 2-butanone 4-phosphate synthase."; RL Phytochemistry 53:723-731(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=9501997; DOI=10.1093/dnares/4.6.401; RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. RT Sequence features of the regions of 1,191,918 bp covered by seventeen RT physically assigned P1 clones."; RL DNA Res. 4:401-414(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 279-543. RX PubMed=7642114; DOI=10.1016/0378-1119(95)00246-3; RA Kobayashi M., Sugiyama M., Yamamoto K.; RT "Isolation of cDNAs encoding GTP cyclohydrolase II from Arabidopsis RT thaliana."; RL Gene 160:303-304(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=10835424; DOI=10.1074/jbc.M003127200; RA Turk E., Kim O., Le Coutre J., Whitelegge J.P., Eskandari S., RA Lam J.T., Kreman M., Zampighi G., Faull K.F., Wright E.M.; RT "Molecular characterization of Vibrio parahaemolyticus vSGLT: a model RT for sodium-coupled sugar cotransporters."; RL J. Biol. Chem. 275:25711-25716(2000). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19376835; DOI=10.1104/pp.109.138677; RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., RA Grossmann J., Gruissem W., Baginsky S.; RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel RT chloroplast kinase substrates and phosphorylation networks."; RL Plant Physiol. 150:889-903(2009). RN [7] RP VARIANT GLN-229 (ISOFORM 2). RX PubMed=18514161; DOI=10.1016/j.ajhg.2008.04.020; RA Tanaka M., Olsen R.W., Medina M.T., Schwartz E., Alonso M.E., RA Duron R.M., Castro-Ortega R., Martinez-Juarez I.E., RA Pascual-Castroviejo I., Machado-Salas J., Silva R., Bailey J.N., RA Bai D., Ochoa A., Jara-Prado A., Pineda G., Macdonald R.L., RA Delgado-Escueta A.V.; RT "Hyperglycosylation and reduced GABA currents of mutated GABRB3 RT polypeptide in remitting childhood absence epilepsy."; RL Am. J. Hum. Genet. 82:1249-1261(2008). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, AND RP SUBCELLULAR LOCATION. RX PubMed=23203051; DOI=10.3390/ijms131114086; RA Hiltunen H.M., Illarionov B., Hedtke B., Fischer M., Grimm B.; RT "Arabidopsis RIBA Proteins: two out of three isoforms have lost their RT bifunctional activity in riboflavin biosynthesis."; RL Int. J. Mol. Sci. 13:14086-14105(2012). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22081402; DOI=10.1007/s11103-011-9846-1; RA Hedtke B., Alawady A., Albacete A., Kobayashi K., Melzer M., RA Roitsch T., Masuda T., Grimm B.; RT "Deficiency in riboflavin biosynthesis affects tetrapyrrole RT biosynthesis in etiolated Arabidopsis tissue."; RL Plant Mol. Biol. 78:77-93(2012). RN [10] RP DISRUPTION PHENOTYPE. RX PubMed=19797057; DOI=10.1074/jbc.M109.030247; RA Nagy R., Grob H., Weder B., Green P., Klein M., Frelet-Barrand A., RA Schjoerring J.K., Brearley C., Martinoia E.; RT "The Arabidopsis ATP-binding cassette protein AtMRP5/AtABCC5 is a high RT affinity inositol hexakisphosphate transporter involved in guard cell RT signaling and phytate storage."; RL J. Biol. Chem. 284:33614-33622(2009). RN [11] RP ALLERGEN. RX PubMed=21848516; DOI=10.1111/j.1398-9995.2011.02683.x; RA An S., Ma D., Wei J.F., Yang X., Yang H.W., Yang H., Xu X., He S., RA Lai R.; RT "A novel allergen Tab y 1 with inhibitory activity of platelet RT aggregation from salivary glands of horseflies."; RL Allergy 66:1420-1427(2011). RN [12] RP ALLERGEN. RX PubMed=12100054; DOI=10.1046/j.1365-2222.2002.01411.x; RA Codina R., Ardusso L., Lockey R.F., Crisci C.D., Jaen C., RA Bertoya N.H.; RT "Identification of the soybean hull allergens involved in RT sensitization to soybean dust in a rural population from Argentina and RT N-terminal sequence of a major 50 KD allergen."; RL Clin. Exp. Allergy 32:1059-1063(2002). RN [13] RP SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DOMAIN. RX PubMed=24389466; DOI=10.1038/nsmb.2740; RA Boel G., Smith P.C., Ning W., Englander M.T., Chen B., Hashem Y., RA Testa A.J., Fischer J.J., Wieden H.J., Frank J., Gonzalez R.L. Jr., RA Hunt J.F.; RT "The ABC-F protein EttA gates ribosome entry into the translation RT elongation cycle."; RL Nat. Struct. Mol. Biol. 21:143-151(2014). RN [14] RP SUBUNIT, AND DOMAIN. RX PubMed=24389465; DOI=10.1038/nsmb.2741; RA Chen B., Boel G., Hashem Y., Ning W., Fei J., Wang C., RA Gonzalez R.L. Jr., Hunt J.F., Frank J.; RT "EttA regulates translation by binding the ribosomal E site and RT restricting ribosome-tRNA dynamics."; RL Nat. Struct. Mol. Biol. 21:152-159(2014). RN [15] RP INDUCTION. RX PubMed=21094157; DOI=10.1016/j.febslet.2010.11.025; RA Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.; RT "14-3-3 proteins fine-tune plant nutrient metabolism."; RL FEBS Lett. 585:143-147(2011). RN [16] RP COFACTOR, AND BIOTECHNOLOGY. RX PubMed=23269834; DOI=10.1073/pnas.1214159110; RA Kim S., Yamaoka Y., Ono H., Kim H., Shim D., Maeshima M., RA Martinoia E., Cahoon E.B., Nishida I., Lee Y.; RT "AtABCA9 transporter supplies fatty acids for lipid synthesis to the RT endoplasmic reticulum."; RL Proc. Natl. Acad. Sci. U.S.A. 110:773-778(2013). RN [17] RP BIOTECHNOLOGY. RX PubMed=16244144; DOI=10.1104/pp.105.068684; RA Van Hoewyk D., Garifullina G.F., Ackley A.R., Abdel-Ghany S.E., RA Marcus M.A., Fakra S., Ishiyama K., Inoue E., Pilon M., Takahashi H., RA Pilon-Smits E.A.; RT "Overexpression of AtCpNifS enhances selenium tolerance and RT accumulation in Arabidopsis."; RL Plant Physiol. 139:1518-1528(2005). RN [18] RP DEVELOPMENTAL STAGE. RX PubMed=9675899; DOI=10.1046/j.1365-313X.1998.00151.x; RA Hirner B., Fischer W.-N., Rentsch D., Kwart M., Frommer W.B.; RT "Developmental control of H+/amino acid permease gene expression RT during seed development of Arabidopsis."; RL Plant J. 14:535-544(1998). RN [19] RP DEVELOPMENTAL STAGE. RX PubMed=12376641; DOI=10.1104/pp.008110; RA Fatland B.L., Ke J., Anderson M.D., Mentzen W.I., Cui L.W., RA Allred C.C., Johnston J.L., Nikolau B.J., Wurtele E.S.; RT "Molecular characterization of a heteromeric ATP-citrate lyase that RT generates cytosolic acetyl-coenzyme A in Arabidopsis."; RL Plant Physiol. 130:740-756(2002). RN [20] RP DISEASE. RX PubMed=17315199; DOI=10.1002/hipo.20268; RA Almgren M., Persson A.S., Fenghua C., Witgen B.M., Schalling M., RA Nyengaard J.R., Lavebratt C.; RT "Lack of potassium channel induces proliferation and survival causing RT increased neurogenesis and two-fold hippocampus enlargement."; RL Hippocampus 17:292-304(2007). RN [21] RP DISEASE. RX PubMed=8995755; DOI=10.1007/s003359900259; RA Donahue L.R., Cook S.A., Johnson K.R., Bronson R.T., Davisson M.T.; RT "Megencephaly: a new mouse mutation on chromosome 6 that causes RT hypertrophy of the brain."; RL Mamm. Genome 7:871-876(1996). RN [22] RP DISEASE. RX PubMed=21966978; DOI=10.1111/j.1460-9568.2011.07834.x; RA Fisahn A., Lavebratt C., Canlon B.; RT "Acoustic startle hypersensitivity in Mceph mice and its effect on RT hippocampal excitability."; RL Eur. J. Neurosci. 34:1121-1130(2011). RN [23] RP ENZYME REGULATION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=6750031; RA Ogrydziak D.M., Scharf S.J.; RT "Alkaline extracellular protease produced by Saccharomycopsis RT lipolytica CX161-1B."; RL J. Gen. Microbiol. 128:1225-1234(1982). RN [24] RP ENZYME REGULATION, CATALYTIC ACTIVITY, AND PROTEOLYTIC PROCESSING. RX PubMed=2649495; RA Matoba S., Ogrydziak D.M.; RT "A novel location for dipeptidyl aminopeptidase processing sites in RT the alkaline extracellular protease of Yarrowia lipolytica."; RL J. Biol. Chem. 264:6037-6043(1989). RN [25] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=17432872; DOI=10.1021/jf0633894; RA Poza M., Sestelo A.B., Ageitos J.M., Vallejo J.A., Veiga-Crespo P., RA Villa T.G.; RT "Cloning and expression of the XPR2 gene from Yarrowia lipolytica in RT Pichia pastoris."; RL J. Agric. Food Chem. 55:3944-3948(2007). RN [26] RP PROTEOLYTIC PROCESSING. RX PubMed=9353927; RA Matoba S., Morano K.A., Klionsky D.J., Kim K., Ogrydziak D.M.; RT "Dipeptidyl aminopeptidase processing and biosynthesis of alkaline RT extracellular protease from Yarrowia lipolytica."; RL Microbiology 143:3263-3272(1997). RN [27] RP PHARMACEUTICAL. RX PubMed=21949405; DOI=10.1073/pnas.1108495108; RA Crawford M.A., Lowe D.E., Fisher D.J., Stibitz S., Plaut R.D., RA Beaber J.W., Zemansky J., Mehrad B., Glomski I.J., Strieter R.M., RA Hughes M.A.; RT "Identification of the bacterial protein FtsX as a unique target of RT chemokine-mediated antimicrobial activity against Bacillus RT anthracis."; RL Proc. Natl. Acad. Sci. U.S.A. 108:17159-17164(2011). RN [28] RP PHARMACEUTICAL. RX PubMed=16632613; DOI=10.1073/pnas.0509392103; RA Rutten L., Geurtsen J., Lambert W., Smolenaers J.J., Bonvin A.M., RA de Haan A., van der Ley P., Egmond M.R., Gros P., Tommassen J.; RT "Crystal structure and catalytic mechanism of the LPS 3-O-deacylase RT PagL from Pseudomonas aeruginosa."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7071-7076(2006). RN [29] RP INVOLVEMENT IN ASTHMA RESPONSE TO GLUCOCORTICOID TREATMENT, AND TISSUE RP SPECIFICITY. RX PubMed=21991891; DOI=10.1056/NEJMoa0911353; RA Tantisira K.G., Lasky-Su J., Harada M., Murphy A., Litonjua A.A., RA Himes B.E., Lange C., Lazarus R., Sylvia J., Klanderman B., Duan Q.L., RA Qiu W., Hirota T., Martinez F.D., Mauger D., Sorkness C., Szefler S., RA Lazarus S.C., Lemanske R.F. Jr., Peters S.P., Lima J.J., Nakamura Y., RA Tamari M., Weiss S.T.; RT "Genomewide association between GLCCI1 and response to glucocorticoid RT therapy in asthma."; RL N. Engl. J. Med. 365:1173-1183(2011). RN [30] RP INVOLVEMENT IN CHRONIC OBSTRUCTIVE PULMONARY DISEASE RESPONSE TO RP GLUCOCORTICOID TREATMENT. RX PubMed=22187997; DOI=10.1056/NEJMc1112547#SA2; RA Van den Berge M., Hiemstra P.S., Postma D.S.; RT "Genetics of glucocorticoids in asthma."; RL N. Engl. J. Med. 365:2434-2435(2011). RN [31] RP RNA EDITING, AND SUBCELLULAR LOCATION. RC TISSUE=Ehrlich ascites tumor cell; RX PubMed=9372446; RA Petzelt C., Joswig G., Mincheva A., Lichter P., Stammer H., Werner D.; RT "The centrosomal protein centrosomin A and the nuclear protein RT centrosomin B derive from one gene by post-transcriptional processes RT involving RNA editing."; RL J. Cell Sci. 110:2573-2578(1997). RN [32] {ECO:0000305} RP RNA EDITING. RX PubMed=17018572; DOI=10.1261/rna.254306; RA Stapleton M., Carlson J.W., Celniker S.E.; RT "RNA editing in Drosophila melanogaster: new targets and functional RT consequences."; RL RNA 12:1922-1932(2006). RN [33] RP TOXIC DOSE. RC TISSUE=Venom; RX PubMed=3075905; RA Masci P.P., Whitaker A.N., de Jersey J.; RT "Purification and characterization of a prothrombin activator from the RT venom of the Australian brown snake, Pseudonaja textilis textilis."; RL Biochem. Int. 17:825-835(1988). RN [34] RP TOXIC DOSE. RC TISSUE=Venom gland; RX PubMed=15351847; DOI=10.1267/THRO04090509; RA Rao V.S., Swarup S., Kini R.M.; RT "The catalytic subunit of pseutarin C, a group C prothrombin activator RT from the venom of Pseudonaja textilis, is structurally similar to RT mammalian blood coagulation factor Xa."; RL Thromb. Haemost. 92:509-521(2004). RN [35] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12111146; DOI=10.1007/s00253-002-1012-x; RA Kiiskinen L.-L., Viikari L., Kruus K.; RT "Purification and characterisation of a novel laccase from the RT ascomycete Melanocarpus albomyces."; RL Appl. Microbiol. Biotechnol. 59:198-204(2002). RN [36] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12118243; DOI=10.1038/nsb823; RA Hakulinen N., Kiiskinen L.-L., Kruus K., Saloheimo M., Paananen A., RA Koivula A., Rouvinen J.; RT "Crystal structure of a laccase from Melanocarpus albomyces with an RT intact trinuclear copper site."; RL Nat. Struct. Biol. 9:601-605(2002). RN [37] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=21592966; DOI=10.1074/jbc.M110.212183; RA Kilmartin J.R., Maher M.J., Krusong K., Noble C.J., Hanson G.R., RA Bernhardt P.V., Riley M.J., Kappler U.; RT "Insights into structure and function of the active site of SoxAX RT cytochromes."; RL J. Biol. Chem. 286:24872-24881(2011). RN [38] {ECO:0000305} RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18552405; DOI=10.1074/jbc.M800315200; RA Kappler U., Bernhardt P.V., Kilmartin J., Riley M.J., Teschner J., RA McKenzie K.J., Hanson G.R.; RT "SoxAX cytochromes, a new type of heme copper protein involved in RT bacterial energy generation from sulfur compounds."; RL J. Biol. Chem. 283:22206-22214(2008). RN [39] RP MASS SPECTROMETRY OF FORMYLATED FORM. RX PubMed=10757971; DOI=10.1021/bi000150m; RA le Coutre J., Whitelegge J.P., Gross A., Turk E., Wright E.M., RA Kaback H.R., Faull K.F.; RT "Proteomics on full-length membrane proteins using mass RT spectrometry."; RL Biochemistry 39:4237-4242(2000). CC -!- FUNCTION: Involved in the retrieval of endoplasmic reticulum CC membrane proteins from the early Golgi compartment. Required for CC correct localization of SEC12, SEC71 and SEC63 in the endoplasmic CC reticulum (By similarity). {ECO:0000250}. RIBA2 and RIBA3 CC together are not able to complement the loss of function of RIBA1. CC {ECO:0000269|PubMed:22081402}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. {ECO:0000269|PubMed:17432872, CC ECO:0000269|PubMed:23203051}. CC -!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity CC for peptide bonds, and a preference for a large uncharged residue CC in P1. {ECO:0000269|PubMed:6750031}. Hydrolyzes peptide amides. CC {ECO:0000269|PubMed:2649495}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:23203051, CC ECO:0000269|PubMed:23269834}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:23269834}. CC The purified enzyme contains a mixture of Fe(2+) and Zn(2+) bound CC in the active site, and a single equivalent of metal is required CC for full catalytic activity. {ECO:0000269|PubMed:23203051}; CC -!- ENZYME REGULATION: The protease activity is completely inhibited CC by the serine inhibitor PMSF but is not affected by thiol group CC inhibitors and in the presence of dithiothreitol. In the presence CC of high concentrations of o-phenanthroline the protease activity CC is only partially inhibited. {ECO:0000269|PubMed:6750031}. The CC pro-region plays an inhibitory role and may provide a mechanism CC for preventing premature activation in the secretory pathway. CC {ECO:0000269|PubMed:2649495}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Absorption: CC Abs(max)=~280 nm {ECO:0000269|PubMed:12111146, CC ECO:0000269|PubMed:12118243}; CC Note=Exhibits a shoulder at 360 nm, a smaller absorption peak at CC 450 nm, and a second, larger peak at 590 nm. CC {ECO:0000269|PubMed:12118243}. Absorption peak at 450 nm CC disappears at high pH. {ECO:0000269|PubMed:12111146}; CC Kinetic parameters: CC KM=0.49 mM for glutathione (at pH 6.0) CC {ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; CC KM=0.19 mM for glutathione (at pH 7.0) CC {ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; CC Vmax=0.124 uM/min/mg enzyme (copper-free) at pH 6.2 CC {ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; CC Vmax=1.54 uM/min/mg enzyme (copper-loaded) at pH 6.2 CC {ECO:0000269|PubMed:18552405, ECO:0000269|PubMed:21592966}; CC Note=kcat is 8.72 s(-1) and 5.7 s(-1) for glutathione at pH 6.0 CC and pH 7.0, respectively. {ECO:0000269|PubMed:18552405}. Vmax CC decreases a lot at pH 7.0. {ECO:0000269|PubMed:21592966}; CC pH dependence: CC Optimum pH is 9.0-10.0. {ECO:0000269|PubMed:6750031}. Inactive CC when pH is greater than 8.0. {ECO:0000269|PubMed:17432872}; CC Redox potential: CC E(0) is -479 mV for heme at pH 8.0. CC {ECO:0000269|PubMed:21592966}. E(0) is -430 mV for heme at pH 6 CC with copper-loaded SoxAX, -455 mV for heme at pH 7 with copper- CC loaded SoxAX, -486 mV for heme at pH 8 with copper-loaded SoxAX, CC -424 mV for heme at pH 6 with copper-free SoxAX, -479 mV for CC heme at pH 7 with copper-free SoxAX, -507 mV for heme at pH 8 CC with copper-free SoxAX and -196 mV for copper center. CC {ECO:0000269|PubMed:18552405}. The Fe (III/II) potentials are CC +133 mV at pH 6.0, +104 mV at pH 7.0, +49 at pH 7.9 and +10 mV CC at pH 8.7. {ECO:0000269|PubMed:18552405, CC ECO:0000269|PubMed:21592966}; CC Temperature dependence: CC Optimum temperature is 40 degrees Celsius. CC {ECO:0000269|PubMed:6750031}. Inactive when temperature drops CC below 20 degrees Celsius. {ECO:0000269|PubMed:17432872}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2- CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step CC 1/1. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino- CC 6-(D-ribitylamino)uracil from GTP: step 1/4. CC -!- SUBUNIT: Interacts with AXL1, AXL2, IQG1 and SEC3. CC {ECO:0000269|PubMed:24389465}. Probably contacts ribosomal CC proteins L1, L5, L33 and S7, the 16S and 23S rRNA and the P site CC containing tRNA(fMet). {ECO:0000269|PubMed:24389466}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP- CC Rule:MF_03000}. Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000269|PubMed:23203051}. Nucleus CC {ECO:0000269|PubMed:9372446}. Note=Centrosomin-A is found in the CC centrosome. {ECO:0000269|PubMed:23203051}. Centrosomin-B is found CC in the nucleus. {ECO:0000269|PubMed:9372446}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms may be produced by alternative CC initiation, both from non-canonical start codons upstream of the CC initiator methionine displayed and from other canonical start CC codons downstream of that displayed. CC {ECO:0000303|PubMed:10835424}. The precise sites of translation CC initiation have not been unambiguously identified. CC {ECO:0000269|PubMed:10835424}; CC Name=1; CC IsoId=P47924-1; Sequence=Displayed; CC Name=2; CC IsoId=P47924-2; Sequence=VSP_002721; CC Note=Most abundantly expressed isoform, at mRNA level. CC {ECO:0000269|PubMed:10835424}. Contains a phosphothreonine at CC position 214. {ECO:0000269|PubMed:10835424}. Ref.5 (AAF80602) CC sequence is in conflict in position: 223:K->E. {ECO:0000305}. CC Variant in position: 229:P->Q (in dbSNP:rs1141138). CC {ECO:0000269|PubMed:18514161}. Ref.5 (AAF80602) sequence differs CC from that shown due to several frameshifts. {ECO:0000305}; CC -!- TISSUE SPECIFICITY: Expressed in leaves, shoots, roots, flowers CC and siliques. {ECO:0000269|PubMed:23203051}. Predominantly CC expressed in lung, spleen, thymus and testis and, at lower levels, CC in brain, bone marrow, peripheral leukocytes, skin and trachea. CC {ECO:0000269|PubMed:21991891}. CC -!- DEVELOPMENTAL STAGE: Expressed in endosperm during early stages of CC seed development. Strongly induced at heart stage of CC embryogenesis. {ECO:0000269|PubMed:9675899}. Expressed in flower CC buds at stage 6 of development in tapetal cells and at stage 10 in CC the epidermal cells of growing petals and ovaries. In young CC siliques, expressed transiently in the inner integument of the CC ovules just prior to testal deposition. CC {ECO:0000269|PubMed:12376641}. CC -!- INDUCTION: Constitutively expressed, increases in stationary phase CC (at protein level). {ECO:0000269|PubMed:24389466}. Induced by CC nitrogen (N) and phosphate (P) deprivation in leaves, but CC repressed by potassium (K) and N deprivation in roots. CC {ECO:0000269|PubMed:21094157}. CC -!- DOMAIN: The arm domain (residues 95-139) is inserted in the first CC ABC transporter domain. Its deletion abrogates the growth arrest CC and translation inhibition effect of the double Q-188/Q-470 CC mutation. When deleted impairs fitness in long-term (up to 6 days) CC growth in stationary phase. {ECO:0000269|PubMed:24389466}. CC Probably contacts ribosomal protein L1. CC {ECO:0000269|PubMed:24389465}. CC -!- PTM: The 10 consecutive -X-Ala- or -X-Pro- dipeptides located over CC 100 amino acids upstream of the N-terminal of mature XPR2 are CC subject to dipeptidyl aminopeptidase (DPAPase)-processing. CC {ECO:0000269|PubMed:9353927}. DPAPase activity is not necessary CC for XPR6 cleavage and for secretion of mature active XPR2. CC {ECO:0000269|PubMed:2649495}. CC -!- RNA EDITING: Modified_positions=Not_applicable; Note=Some CC positions are modified by RNA editing via nucleotide deletion, up CC to position 787. The unedited version gives rise to centrosomin-B CC (shown here). The fully edited version gives rise to centrosomin- CC A, in which the C-terminal sequence is replaced up to position 787 CC by Ser-Ile-Val-Ala-STOP. A combination of alternative splicing and CC RNA editing resulting in this template G deletion could also CC explain the generation of centrosomin-A mRNA. CC {ECO:0000269|PubMed:9372446}. Target of Adar. CC {ECO:0000269|PubMed:17018572}; CC -!- MASS SPECTROMETRY: Mass=60680; Method=Electrospray; Range=1-543; CC Note=Formylated form.; Evidence={ECO:0000269|PubMed:10757971}; CC -!- POLYMORPHISM: Polymorphisms dbSNP:rs37972 and dbSNP:rs37973, CC located in GLCCI1 promoter region, are associated with a decreased CC response to glucorticoid treatment [MIM:614400] in asthma CC patients. {ECO:0000269|PubMed:21991891}. Same observations have CC been found in chronic obstructive pulmonary disease patients. CC {ECO:0000269|PubMed:22187997}. The mean increase in forced CC expiratory volume in 1 second in glucorticoid treated subjects who CC are homozygous for the mutant (G) rs37973 allele is only about CC one-third of that seen in similarly treated subjects who are CC homozygous for the wild-type allele (A). CC {ECO:0000269|PubMed:21991891}. These polymorphisms affect GLCCI1 CC transcription level. {ECO:0000269|PubMed:21991891, CC ECO:0000269|PubMed:22187997}. CC -!- DISEASE: Note=A spontaneous mutation leading to a frameshift and CC truncation of Kcna2 causes megencephaly with a 25% increase of CC brain weight relative to wild-type. Especially the hippocampus CC shows increased proliferation of neurons and astrocytes, leading CC to increased brain volume. {ECO:0000269|PubMed:17315199}. Mutant CC mice appear normal at birth. After 3-4 weeks, they display low CC body weight, a subtle shakiness in their gait, a preference for a CC strange sitting position that is maintained for periods ranging CC from 30 seconds to several minutes, excessive lacrimation and CC acoustic startle hypersensitivity. {ECO:0000269|PubMed:21966978, CC ECO:0000269|PubMed:8995755}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype when heterozygous. CC Bleached phenotype and no viable seeds produced when homozygous. CC {ECO:0000269|PubMed:22081402}. Low phytic acid levels in seed CC tissue. {ECO:0000269|PubMed:19797057}. CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE. CC {ECO:0000269|PubMed:21848516}. Sensitization is common in subjects CC who are repeatedly exposed to G.max dust. Common symptoms are CC bronchial asthma and allergic rhinitis. CC {ECO:0000269|PubMed:12100054}. CC -!- TOXIC DOSE: Intravenous injection (23 ug/kg bodyweight) of the CC group C prothrombin activator causes death in rats through CC disseminated intravascular coagulopathy. CC {ECO:0000269|PubMed:3075905}. To the contrary, pseutarin-C is not CC lethal even at 10 mg/kg in mice when injected intraperitoneally. CC {ECO:0000269|PubMed:15351847}. CC -!- BIOTECHNOLOGY: Overexpression of ABCA9 increases seed oil content. CC {ECO:0000269|PubMed:23269834}. NFS2-overexpressing transgenic CC plants have enhanced ability to tolerate and accumulate Se and may CC be used in phytoremediation. {ECO:0000269|PubMed:16244144}. CC -!- PHARMACEUTICAL: Potential therapeutic target of chemokine-mediated CC antimicrobial activity against B.anthracis to treat infection. CC {ECO:0000269|PubMed:21949405}. Might be useful for the development CC of new vaccines or adjuvants because of its LPS-modifying CC properties. May be used for the design of inhibitors with possible CC therapeutic value. {ECO:0000303|PubMed:16632613}. CC -!- SIMILARITY: In the N-terminal section; belongs to the DHBP CC synthase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the GTP CC cyclohydrolase II family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HNH domain. {ECO:0000305}. CC -!- SIMILARITY: To phage T4 mobB and mobD. {ECO:0000305}. CC -!- CAUTION: The active site cysteine and glutamate residues are not CC conserved in this protein. Its activity is therefore unsure. CC {ECO:0000305}. Dermonecrotic toxins were previously known as CC sphingomyelin phosphodiesterase D based on their ability to CC hydrolyze sphingomyelin into choline and acylsphingosine CC phosphate. Based on additional biochemical analysis, the enzymes CC have been renamed phospholipase D to represent a more accurate and CC broader denomination. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA08113.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; DR EMBL; AJ000053; CAA03884.1; -; Genomic_DNA. DR EMBL; AB008268; BAB09861.1; -; Genomic_DNA. DR EMBL; CP002688; AED97867.1; -; Genomic_DNA. DR EMBL; D45165; BAA08113.1; ALT_INIT; mRNA. DR EMBL; AF255301; AAF80602.1; -; mRNA. DR PIR; JC4209; JC4209. DR RefSeq; NP_201235.4; NM_125826.4. DR UniGene; At.49217; -. DR ProteinModelPortal; P47924; -. DR SMR; P47924; 125-502. DR MINT; MINT-8063173; -. DR STRING; 3702.AT5G64300.1; -. DR PaxDb; P47924; -. DR PRIDE; P47924; -. DR EnsemblPlants; AT5G64300.1; AT5G64300.1; AT5G64300. DR GeneID; 836551; -. DR KEGG; ath:AT5G64300; -. DR GeneFarm; 2299; 254. DR TAIR; AT5G64300; -. DR eggNOG; COG0108; -. DR HOGENOM; HOG000115440; -. DR InParanoid; P47924; -. DR KO; K14652; -. DR OMA; LMVDRNT; -. DR PhylomeDB; P47924; -. DR BioCyc; ARA:AT5G64300-MONOMER; -. DR BioCyc; MetaCyc:AT5G64300-MONOMER; -. DR BRENDA; 4.1.99.12; 399. DR UniPathway; UPA00275; UER00399. DR UniPathway; UPA00275; UER00400. DR PRO; PR:P47924; -. DR Proteomes; UP000006548; Chromosome 5. DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB. DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR. DR GO; GO:0016020; C:membrane; IDA:TAIR. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IMP:UniProtKB. DR Gene3D; 3.90.870.10; -; 1. DR HAMAP; MF_00179; RibA; 1. DR HAMAP; MF_00180; RibB; 1. DR HAMAP; MF_01283; RibBA; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR000422; DHBP_synthase_RibB. DR InterPro; IPR000926; GTP_CycHdrlaseII_RibA. DR InterPro; IPR016299; Riboflavin_synth_RibBA. DR Pfam; PF00926; DHBP_synthase; 1. DR Pfam; PF00925; GTP_cyclohydro2; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00505; ribA; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 1: Evidence at protein level; KW Allergen; Alternative splicing; Chloroplast; Complete proteome; KW Cytoplasm; Cytoskeleton; GTP-binding; Hydrolase; Lyase; Magnesium; KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Nucleus; Pharmaceutical; Plastid; Reference proteome; KW Riboflavin biosynthesis; Transit peptide; Zinc. FT TRANSIT 1 56 Chloroplast. {ECO:0000255|HAMAP- FT Rule:MF_03000}. FT CHAIN 57 543 Bifunctional riboflavin biosynthesis FT protein RIBA 1, chloroplastic. FT /FTId=PRO_0000030436. FT NP_BIND 379 383 GTP. {ECO:0000250}. FT NP_BIND 423 425 GTP. {ECO:0000250}. FT REGION 57 328 DHBP synthase. FT REGION 152 153 D-ribulose 5-phosphate binding. FT {ECO:0000250}. FT REGION 267 271 D-ribulose 5-phosphate binding. FT {ECO:0000250}. FT REGION 329 543 GTP cyclohydrolase II. FT COMPBIAS 7 10 Poly-Ser. FT COMPBIAS 144 147 Poly-Val. FT ACT_SITE 457 457 Proton acceptor; for GTP cyclohydrolase FT activity. {ECO:0000255}. FT ACT_SITE 459 459 Nucleophile; for GTP cyclohydrolase FT activity. {ECO:0000250}. FT METAL 153 153 Magnesium or manganese 1. {ECO:0000250}. FT METAL 153 153 Magnesium or manganese 2. {ECO:0000250}. FT METAL 270 270 Magnesium or manganese 2. {ECO:0000250}. FT METAL 384 384 Zinc; catalytic. {ECO:0000250}. FT METAL 395 395 Zinc; catalytic. {ECO:0000250}. FT METAL 397 397 Zinc; catalytic. {ECO:0000250}. FT BINDING 157 157 D-ribulose 5-phosphate. {ECO:0000250}. FT BINDING 291 291 D-ribulose 5-phosphate. {ECO:0000250}. FT BINDING 400 400 GTP. {ECO:0000250}. FT BINDING 445 445 GTP. {ECO:0000250}. FT BINDING 480 480 GTP. {ECO:0000250}. FT BINDING 485 485 GTP. {ECO:0000250}. FT SITE 253 253 Essential for DHBP synthase activity. FT {ECO:0000250}. FT SITE 291 291 Essential for DHBP synthase activity. FT {ECO:0000250}. FT VAR_SEQ 203 203 E -> ETYMAVSFIGGTDGWFAGVSKMVDAAPGHFEMILDQ FT SNPQYMNLPGIAVLIGGLWVANLYYWGFNQYIIQRTLAAK FT (in isoform 2). FT /FTId=VSP_002721. ** ** ################# INTERNAL SECTION ################## **DR TAIR-CDS; AT5G64300.1; TAIR10; P47924-1. **EV ECO:0000250; -; XXX; 01-JAN-1900. **EV ECO:0000255; -; XXX; 01-JAN-1900. **EV ECO:0000255; HAMAP-Rule:MF_03000; SEG; 30-JUN-2015. **EV ECO:0000269; PubMed:10757971; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:10835424; SEG; 30-JUN-2015. **EV ECO:0000269; PubMed:12100054; EMB; 09-APR-2013. **EV ECO:0000269; PubMed:12111146; JUJ; 19-APR-2006. **EV ECO:0000269; PubMed:12118243; JUJ; 19-APR-2006. **EV ECO:0000269; PubMed:12376641; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:15351847; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:16244144; MIS; 14-JAN-2015. **EV ECO:0000269; PubMed:17018572; ELS; 27-MAR-2008. **EV ECO:0000269; PubMed:17315199; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:17432872; SEG; 29-JUN-2015. **EV ECO:0000269; PubMed:18514161; SEG; 30-JUN-2015. **EV ECO:0000269; PubMed:18552405; KAL; 17-JUN-2013. **EV ECO:0000269; PubMed:19797057; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:21094157; MAF; 23-APR-2015. **EV ECO:0000269; PubMed:21592966; KAL; 13-JUN-2013. **EV ECO:0000269; PubMed:21848516; MNS; 14-OCT-2011. **EV ECO:0000269; PubMed:21949405; KAL; 09-JAN-2013. **EV ECO:0000269; PubMed:21966978; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:21991891; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:22081402; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:22187997; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:23203051; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:23269834; MIT; 19-JUN-2010. **EV ECO:0000269; PubMed:24389465; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:24389466; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:2649495; MAF; 23-APR-2015. **EV ECO:0000269; PubMed:3075905; SEG; 30-JUN-2015. **EV ECO:0000269; PubMed:6750031; MAF; 23-APR-2015. **EV ECO:0000269; PubMed:8995755; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:9353927; SEG; 29-JUN-2015. **EV ECO:0000269; PubMed:9372446; XXX; 01-JAN-1900. **EV ECO:0000269; PubMed:9675899; XXX; 01-JAN-1900. **EV ECO:0000303; PubMed:10835424; SEG; 30-JUN-2015. **EV ECO:0000303; PubMed:16632613; KAL; 30-APR-2013. **EV ECO:0000305; -; SEG; 30-JUN-2015. **IS P47924-3 **ZB MIT, 21-JUL-2004; ELC, 15-NOV-2007; MIS, 02-MAY-2013; SQ SEQUENCE 543 AA; 59056 MW; 31D89A500E42BF81 CRC64; MSSINLSSSS PSTISLSRSR LSQSSTTLLH GLHRVTLPSN HPLSTFSIKT NTGKVKAAVI SREDDLLSFT NGNTPLSNGS LIDDRTEEPL EADSVSLGTL AADSAPAPAN GFVAEDDDFE LDLPTPGFSS IPEAIEDIRQ GKLVVVVDDE DRENEGDLVM AAQLATPEAM AFIVRHGTGI VCVSMKEDDL ERLHLPLMVN QKENEEKLST AFTVTVDAKH GTTTGVSARD RATTILSLAS RDSKPEDFNR PGHIFPLKYR EGGVLKRAGH TEASVDLTVL AGLDPVGVLC EIVDDDGSMA RLPKLREFAA ENNLKVVSIA DLIRYRRKRD KLVERASAAR IPTMWGPFTA YCYRSILDGI EHIAMVKGEI GDGQDILVRV HSECLTGDIF GSARCDCGNQ LALSMQQIEA TGRGVLVYLR GHEGRGIGLG HKLRAYNLQD AGRDTVEANE ELGLPVDSRE YGIGAQIIRD LGVRTMKLMT NNPAKYVGLK GYGLAIVGRV PLLSLITKEN KRYLETKRTK MGHMYGLKFK GDVVEKIESE SES // Swissknife_1.75/t/DEs.txl.expected0000644005110600510130000001162710357506347017341 0ustar ecastroSwissProtURIDINE 5'-MONOPHOSPHATE SYNTHASE (UMP SYNTHASE) (RUDIMENTARY-LIKE-PROTEIN) [Includes: OROTATE PHOSPHORIBOSYLTRANSFERASE (EC 2.4.2.10) (OPRTASE); OROTIDINE 5'-PHOSPHATE DECARBOXYLASE (EC 4.1.1.23) (OMPDECASE)] (Fragments) list : "URIDINE 5'-MONOPHOSPHATE SYNTHASE", "UMP SYNTHASE", "RUDIMENTARY-LIKE-PROTEIN" hasFragment : Fragments childType : > list : "OROTATE PHOSPHORIBOSYLTRANSFERASE", "EC 2.4.2.10", "OPRTASE" hasFragment : childType : Includes list : "OROTIDINE 5'-PHOSPHATE DECARBOXYLASE", "EC 4.1.1.23", "OMPDECASE" hasFragment : childType : Includes // ID PYR5_DROME STANDARD; PRT; 493 AA. AC Q01637; Q24221; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 30-MAY-2000, entry version 1. DE URIDINE 5'-MONOPHOSPHATE SYNTHASE (UMP SYNTHASE) (RUDIMENTARY-LIKE- DE PROTEIN) [INCLUDES: OROTATE PHOSPHORIBOSYLTRANSFERASE (EC 2.4.2.10) DE (OPRTASE); OROTIDINE 5'-PHOSPHATE DECARBOXYLASE (EC 4.1.1.23) DE (OMPDECASE)] (Fragments). GN R-L. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Eisenberg M.T., Kirkpatrick R., Rawls J.; RL Submitted (XXX-1992) to the EMBL/GenBank/DDBJ databases. SQ SEQUENCE 493 AA; 53327 MW; 56479CDAB1F6A308 CRC64; MVAQNSDKMR ALALKLFEIN AFKFGDFKMK VGINSPVYFD LRVIVSLGLP QQTVSDLLVE HIKDKQLSAK HVCGVPYTAL PRATIVSVQQ GTPMLVRRKE AKAYGTKKLV EGIFNAGDTC LIVEDVVTSG SSILDTVRDL QGEGIVVTDA VVVVDREQGG VANIAKHGVR MHSLFTLSFL LNTLHEAGRI EKSTVEAVAK YIAAVQINSD GTFVGGDKVT FPAANDLQRT KLTYESRANL AKSAVAKRLF NLIASKQTNL CLAADLTHAD EILDVADKCG PYICLLKTHV DIVEDFSDKF IADLQALAQR HNFLLMEDRK FADIGNTVSL QYGKGIYKIS SWADLVTAHT LPGRSILQGL KAGLGEGGAG KERGVFLLAE MSASGNLIDA KYKENSNKIA TEGADVDFVA GVVCQSSDAF AFPGLLQLTP GVKIDEGVDQ LGQQYQSPEH VVKERGADIG VVGRGILKAS SPKQAAQTYR DRLWAAYQDR VAK // ID PYR5_DROME STANDARD; PRT; 493 AA. AC Q01637; Q24221; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 30-MAY-2000, entry version 1. DE Some strange protein (Fragment) (Version 2). GN R-L. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RA Eisenberg M.T., Kirkpatrick R., Rawls J.; RL Submitted (XXX-1992) to the EMBL/GenBank/DDBJ databases. SQ SEQUENCE 493 AA; 53327 MW; 56479CDAB1F6A308 CRC64; MVAQNSDKMR ALALKLFEIN AFKFGDFKMK VGINSPVYFD LRVIVSLGLP QQTVSDLLVE HIKDKQLSAK HVCGVPYTAL PRATIVSVQQ GTPMLVRRKE AKAYGTKKLV EGIFNAGDTC LIVEDVVTSG SSILDTVRDL QGEGIVVTDA VVVVDREQGG VANIAKHGVR MHSLFTLSFL LNTLHEAGRI EKSTVEAVAK YIAAVQINSD GTFVGGDKVT FPAANDLQRT KLTYESRANL AKSAVAKRLF NLIASKQTNL CLAADLTHAD EILDVADKCG PYICLLKTHV DIVEDFSDKF IADLQALAQR HNFLLMEDRK FADIGNTVSL QYGKGIYKIS SWADLVTAHT LPGRSILQGL KAGLGEGGAG KERGVFLLAE MSASGNLIDA KYKENSNKIA TEGADVDFVA GVVCQSSDAF AFPGLLQLTP GVKIDEGVDQ LGQQYQSPEH VVKERGADIG VVGRGILKAS SPKQAAQTYR DRLWAAYQDR VAK // (2'-5')OLIGOADENYLATE SYNTHETASE 1A (EC 2.7.7.-) ((2-5')OLIGO(A) SYNTHETASE 1A) (2-5A SYNTHETASE 1A) list : "(2'-5')OLIGOADENYLATE SYNTHETASE 1A", "EC 2.7.7.-", "(2-5')OLIGO(A) SYNTHETASE 1A", "2-5A SYNTHETASE 1A" hasFragment : childType : > // Arginine biosynthesis bifunctional protein argJ [Includes: Glutamate- and N-acetyltransferase (EC 2.3.1.35) (Ornithine acetyltransferase) (Ornithine transacetylase) (OATASE); Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGS)] [Contains: Arginine biosynthesis bifunctional protein alpha chain; Arginine biosynthesis bifunctional protein beta chain] list : "Arginine biosynthesis bifunctional protein argJ" hasFragment : childType : > list : "Glutamate- and N-acetyltransferase", "EC 2.3.1.35", "Ornithine acetyltransferase", "Ornithine transacetylase", "OATASE" hasFragment : childType : Includes list : "Amino-acid acetyltransferase", "EC 2.3.1.1", "N-acetylglutamate synthase", "AGS" hasFragment : childType : Includes list : "Arginine biosynthesis bifunctional protein alpha chain" hasFragment : childType : Contains list : "Arginine biosynthesis bifunctional protein beta chain" hasFragment : childType : Contains // Angiotensinogen precursor [Contains: Angiotensin I (Ang I); Angiotensin II (Ang II); Angiotensin III (Ang III) (Des-Asp[1]-angiotensin II)] list : "Angiotensinogen precursor" hasFragment : childType : > list : "Angiotensin I", "Ang I" hasFragment : childType : Contains list : "Angiotensin II", "Ang II" hasFragment : childType : Contains list : "Angiotensin III", "Ang III", "Des-Asp[1]-angiotensin II" hasFragment : childType : Contains // Swissknife_1.75/t/util.txl0000644005110600510130000002142607432502662016035 0ustar ecastroSwissProtID DCTQ_RHOSH PRELIMINARY; PRT; 227 AA. AC Q9LBD9; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE Putative small C4-dicarboxylate integral membrane transport protein. GN DCTQ. OS Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1063; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=4P1; ** nothing has been published RA Omrani M.D.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR C4-DICARBOXYLATE TRANSPORT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (BY SIMILARITY). **this miscellaneous CC line should be deleted CC -!- MISCELLANEOUS: SHOWS POOR SPECIFICITY. DR EMBL; AF005842; AAF72734.1; -. KW Transmembrane; Transport. FT DOMAIN 1 10 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 11 29 BY SIMILARITY. FT DOMAIN 30 68 PERIPLASMIC (BY SIMILARITY). FT TRANSMEM 69 91 BY SIMILARITY. FT DOMAIN 92 112 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 113 133 BY SIMILARITY. FT DOMAIN 134 152 PERIPLASMIC (BY SIMILARITY). FT TRANSMEM 153 173 BY SIMILARITY. FT DOMAIN 174 227 CYTOPLASMIC (BY SIMILARITY). ** ** ################# SOURCE SECTION ################## ** Rhodobacter sphaeroides C4-dicarboxylate binding-protein precursor (dctP), ** small integral membrane transport protein (dctQ) and large integral ** membrane transport protein (dctM) genes, complete cds. ** source 1..3718 ** /db_xref="taxon:1063" ** /organism="Rhodobacter sphaeroides" ** /strain="4P1" ** CDS 1214..1897 ** /codon_start=1 ** /note="DctQ; contains four putative transmembrane helices" ** /transl_table=11 ** /gene="dctQ" ** /product="small integral membrane transport protein" ** /protein_id="AAF72734.1" ** CDS_IN_EMBL_ENTRY 3 ** 02-JUN-2000 (Rel. 63, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_RHOSH **ZZ CREATED AND FINISHED BY MICHELE. **ZZ CURATED. SQ SEQUENCE 227 AA; 24991 MW; 2208AD920C1230DA CRC64; MMRLLDRLEE TLIASLIAAA TGLIFVSVVQ RYSLGLLADG VAFFRGHDMP ELSAMMRSAY LGLREFNLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINKLDERK RGFFILLGLG AGALFTGIIA TLGGNFVWHM AQTSAISPDL ELPMWLVYLA IPLGSALMCF RFLQVAVIFA RTGELAHHDH GHVEGVDTED EGIDVLGSTF LKSPLTPRDL VEKPKDE // ID DCTQ_WOLSU PRELIMINARY; PRT; 170 AA. AC Q9ZEJ3; DT 01-MAY-1999 (TrEMBLrel. 10, Created) DT 01-MAY-1999 (TrEMBLrel. 10, Last sequence update) DT 01-MAY-1999 (TrEMBLrel. 10, Last annotation update) DE Small C4-dicarboxylate integral membrane transport protein. ** unsure gene name, ** will be deleted GN DCTQ. OS Wolinella succinogenes. OC Bacteria; Proteobacteria; epsilon subdivision; Helicobacter group; OC Wolinella. OX NCBI_TaxID=844; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DSMZ 1740; RX MEDLINE=20461222; PubMed=11004174; RA Ullmann R., Gross R., Simon J., Unden G., Kroeger A.; RT "Transport of C(4)-dicarboxylates in Wolinella succinogenes."; RL J. Bacteriol. 182:5757-5764(2000). CC -!- FUNCTION: INVOLVED IN THE ELECTROGENIC UNIPORT OF C4- CC DICARBOXYLATES. ** or should this be in similarity?, do things in similarity have to have ** a dr line? CC -!- PATHWAY: BELONGS TO THE TRIPARTITE ATP-INDEPENDENT PERIPLASMIC CC (TRAP) TRANSPORTER FAMILY DR EMBL; AJ132740; CAA10757.1; -. ** ** ################# SOURCE SECTION ################## ** Wolinella succinogenes dctP, dctQ and dctM genes, and partial orfN ** source 1..3309 ** /organism="Wolinella succinogenes" ** /db_xref="taxon:844" ** CDS 1086..1598 ** /db_xref="PID:e1375211" ** /transl_table=11 ** /gene="dctQ" ** /product="small integral C4-dicarboxylate membrane ** transport protein, putative" ** /protein_id="CAA10757.1" ** CDS_IN_EMBL_ENTRY 4 ** 04-FEB-1999 (Rel. 58, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_WOLSU **ZZ CREATED AND FINISHED BY MICHELE. SQ SEQUENCE 170 AA; 18753 MW; 4CCF9F77E2F85C20 CRC64; MSKFFEILDL GIAAMNKSIA VIGISTGVIL AFINVVLRYF FDSGLTWAGE TINYLFIWSA LFGAAYGFKK GIHIAVTILV ERFPPLLAKA SLMIASLISL IFLLFIAYFG LHYVLLVKDM GFMSVDLGIP QWIPMVVIPV AFFAASYRVG EKIYEISKQP ADTVVKSAGR // ID DCTQ_RHOCA PRELIMINARY; PRT; 227 AA. AC O07837; DT 01-JUL-1997 (TrEMBLrel. 04, Created) DT 01-JUL-1997 (TrEMBLrel. 04, Last sequence update) DT 01-NOV-1998 (TrEMBLrel. 08, Last annotation update) DE Small C4-dicarboxylate integral membrane transport protein. GN DCTQ. OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1061; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=B11; RX MEDLINE=92236423; PubMed=1809844; RA Shaw J.G., Hamblin M.J., Kelly D.J.; RT "Purification, characterization and nucleotide sequence of the RT periplasmic C4-dicarboxylate-binding protein (DctP) from Rhodobacter RT capsulatus."; RL Mol. Microbiol. 5:3055-3062(1991). RN [2] RP SEQUENCE FROM N.A. ** I see SB10003 / St Louis as the strain from table 1, not B10. RC STRAIN=B11; RX MEDLINE=97431499; PubMed=9287004; RA Forward J.A., Behrendt M.C., Wyborn N.R., Cross R., Kelly D.J.; RT "TRAP transporters: a new family of periplasmic solute transport RT systems encoded by the dctPQM genes of Rhodobacter capsulatus and by RT homologs in diverse gram-negative bacteria."; RL J. Bacteriol. 179:5482-5493(1997). RN [3] RP DISCUSSION OF SEQUENCE. RX MEDLINE=20090467; PubMed=10627041; RA Rabus R., Jack D.L., Kelly D.J., Saier M.H. Jr; RT "TRAP transporters: an ancient family of extracytoplasmic RT solute-receptor-dependent secondary active transporters."; RL Microbiology 145:3431-3445(1999). RN [4] RP TOPOLOGY. RC STRAIN=B10; RX PubMed=11150659; RA Wyborn N.R., Alderson J., Andrews S.C., Kelly D.J.; RT "Topological analysis of DctQ, the small integral membrane protein of RT the C4-dicarboxylate TRAP transporter of Rhodobacter capsulatus."; RL FEMS Microbiol. Lett. 194:13-17(2001). CC -!- FUNCTION: REQUIRED FOR C4-DICARBOXYLATE TRANSPORT (table 2,ref2). ** we could also say that transport is thought to use the membrane ** potential, in that case we might put it into function. Note that in ** ref 4 the use of an electrochemical gradient for energy is now sure ** and is cited in the intro. CC -!- ENZYME REGULATION: TRANSPORT IS SENSITIVE TO MEMBRANE POTENTIAL CC UNCOUPLERS AND VANADATE INSENSITIVE (ref2 figs 6&7). ** inner membrane upon expression in ecoli, but can we extrapolate to Rhoca? CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (ref2 fig4). DR EMBL; X63974; CAA45386.1; -. DR PROSITE; PS12345; TEST_DOMAIN; 1. ** PROSITE; PS12346; FALSE_DOMAIN; FALSE_POS. KW Transmembrane; Transport. FT DOMAIN 1 10 CYTOPLASMIC. FT TRANSMEM 11 29 FT DOMAIN 30 68 PERIPLASMIC. FT TRANSMEM 69 91 FT DOMAIN 92 112 CYTOPLASMIC. FT TRANSMEM 113 133 FT DOMAIN 134 152 PERIPLASMIC. FT TRANSMEM 153 173 FT DOMAIN 174 227 CYTOPLASMIC. ** transmembrane regions are unsure ** ** ################# SOURCE SECTION ################## ** R capsulatus dctP gene for C4-dicarboxylase binding protein ** source 1..4500 ** /organism="Rhodobacter capsulatus" ** /strain="B10" ** /clone_lib="Cosmid, pLAFR1" ** /clone="pDCT200, pDCT205" ** /chromosome="1" ** CDS 1084..1767 ** /gene="dctQ" ** /product="small integral membrane transport protein" ** /db_xref="PID:e324693" ** CDS_2_OUT_OF_5 ** 26-JUN-1997 (Rel. 52, Last updated, Version 20) ** ################# INTERNAL SECTION ################## **ID XXXX_RHOCA SQ SEQUENCE 227 AA; 24763 MW; 0DE9D59DE5450F99 CRC64; MLRILDRAEE VLIAALIATA TVLIFVSVTH RFTLGFVADF VGFFRGHGMT GAAAAAKSLY TTLRGINLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINRLDAPK RRFFILLGLG AGALFTGIIA TLGANFVLHM YHASSTSPDL ELPMWLVYLA IPMGSSLMCF RFLQVAFGFA RTGELPHHDH GHVDGVDTEN EGIDAEGDVL LHSPLTPRDL VEKPKDN // Swissknife_1.75/t/FTId.t0000644005110600510130000000140410265736434015300 0ustar ecastroSwissProt# Checks if FTIds are handled correctly. use Carp; use SWISS::Entry; # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}FTId.txl"; my $testout = "${where}FTId.txl.out"; my $expectedout = "${where}FTId.txl"; open (IN, $testin); open (OUT, ">$testout"); local $/ = "//\n"; while (){ $entry = SWISS::Entry->fromText($_, 1, 1); print OUT $entry->toText(); } close IN; close OUT; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; Swissknife_1.75/t/identity.t0000644005110600510130000000303110225167417016334 0ustar ecastroSwissProt# Swissknife Test Harness Script for fullparse # # Purpose: # After a full parse, the output file should be identical # to the input. # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 1; } BEGIN { if ($] >= 5.008 and $] < 5.008002) { warn " WARNING: You are running perl version 5.8.0 or 5.8.1. There is a bug in these perl versions that may causes a crash when Swissknife is run on certain entries. If you get a 'Segmentation fault' or a funny output such as ('int' \$__val) in the following test (identity), you should use either an older or a more recent version of perl, or use Swissknife at your own risk. "; } } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}identity.txl"; my $testout = "${where}identity.txl.out"; my $expectedout = "${where}identity.txl.expected"; open (IN, $testin); open (OUT, ">$testout"); use SWISS::Entry; # Read an entire record at a time $/ = "\/\/\n"; while (){ # Read the entry $entry = SWISS::Entry->fromText($_, 1); $entry->reformat; $entry -> CCs -> filter(&SWISS::CCs::ccTopic('ALTERNATIVE PRODUCTS')); $entry->DRs->sort; $entry->FTs->sort($entry->SQs->length); print OUT $entry->toText; } close IN; close OUT; print "checking expected output...\n"; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; Swissknife_1.75/t/util.t0000644005110600510130000000132110225167420015452 0ustar ecastroSwissProt# Swissknife Test Harness Script # # Purpose: # Check utility methods. use Carp; # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}util.txl"; open (IN, $testin); use SWISS::Entry; # Check reply from isCurated(): # Read an entire record at a time $/ = "\/\/\n"; # Read the entries while (){ $entry = SWISS::Entry->fromText($_); push @results, $entry->isCurated(); } test 2, (join "",@results) eq "100"; Swissknife_1.75/t/annot.txl.expected0000644005110600510130000014562712437070154020006 0ustar ecastroSwissProtID DCTQ_RHOSH Unreviewed; 227 AA. AC Q9LBD9; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE Putative small C4-dicarboxylate integral membrane transport protein. OS Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1063; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=4P1; RA Omrani M.D.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: REQUIRED FOR C4-DICARBOXYLATE TRANSPORT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (BY SIMILARITY). CC -!- SEQUENCE CAUTION: CC Sequence=CAI21743; Type=Erroneous gene model prediction; CC Sequence=CAI21743; Type=Miscellaneous discrepancy; Positions=1528; CC Sequence=CAI22254; Type=Erroneous gene model prediction; Positions=1528, 1529; CC Sequence=CAI22254; Type=Miscellaneous discrepancy; Positions=Several; Note=Translated as Gln; DR EMBL; AF005842; AAF72734.1; -. PE 1; Evidence at protein level; KW Transmembrane; Transport. FT TOPO_DOM 1 10 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 11 29 BY SIMILARITY. FT TOPO_DOM 30 68 PERIPLASMIC (BY SIMILARITY). FT TRANSMEM 69 91 BY SIMILARITY. FT TOPO_DOM 92 112 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 113 133 BY SIMILARITY. FT TOPO_DOM 134 152 PERIPLASMIC (BY SIMILARITY). FT TRANSMEM 153 173 BY SIMILARITY. FT TOPO_DOM 174 227 CYTOPLASMIC (BY SIMILARITY). ** ** ################# SOURCE SECTION ################## ** Rhodobacter sphaeroides C4-dicarboxylate binding-protein precursor (dctP), ** small integral membrane transport protein (dctQ) and large integral ** membrane transport protein (dctM) genes, complete cds. ** source 1..3718 ** /db_xref="taxon:1063" ** /organism="Rhodobacter sphaeroides" ** /strain="4P1" ** CDS 1214..1897 ** /codon_start=1 ** /note="DctQ; contains four putative transmembrane helices" ** /transl_table=11 ** /gene="dctQ" ** /product="small integral membrane transport protein" ** /protein_id="AAF72734.1" ** CDS_IN_EMBL_ENTRY 3 ** 02-JUN-2000 (Rel. 63, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_RHOSH SQ SEQUENCE 227 AA; 24991 MW; 2208AD920C1230DA CRC64; MMRLLDRLEE TLIASLIAAA TGLIFVSVVQ RYSLGLLADG VAFFRGHDMP ELSAMMRSAY LGLREFNLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINKLDERK RGFFILLGLG AGALFTGIIA TLGGNFVWHM AQTSAISPDL ELPMWLVYLA IPLGSALMCF RFLQVAVIFA RTGELAHHDH GHVEGVDTED EGIDVLGSTF LKSPLTPRDL VEKPKDE // ID DCTQ_RHOSH Unreviewed; 227 AA. AC Q9LBD9; DT 01-OCT-2000 (TrEMBLrel. 15, Created) DT 01-OCT-2000 (TrEMBLrel. 15, Last sequence update) DT 01-OCT-2000 (TrEMBLrel. 15, Last annotation update) DE Putative small C4-dicarboxylate integral membrane transport protein. OS Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1063; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=4P1; ** nothing has been published RA Omrani M.D.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. **this miscellaneous CC line should be deleted CC -!- FUNCTION: REQUIRED FOR C4-DICARBOXYLATE TRANSPORT (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (BY SIMILARITY). CC -!- SEQUENCE CAUTION: CC Sequence=CAI21743; Type=Erroneous gene model prediction; CC Sequence=CAI21743; Type=Miscellaneous discrepancy; Positions=1528; CC Sequence=CAI22254; Type=Erroneous gene model prediction; Positions=1528, 1529; CC Sequence=CAI22254; Type=Miscellaneous discrepancy; Positions=Several; Note=Translated as Gln; DR EMBL; AF005842; AAF72734.1; -. PE 1; Evidence at protein level; KW Transmembrane; Transport. FT TOPO_DOM 1 10 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 11 29 BY SIMILARITY. FT TOPO_DOM 30 68 PERIPLASMIC (BY SIMILARITY). FT TRANSMEM 69 91 BY SIMILARITY. FT TOPO_DOM 92 112 CYTOPLASMIC (BY SIMILARITY). FT TRANSMEM 113 133 BY SIMILARITY. FT TOPO_DOM 134 152 PERIPLASMIC (BY SIMILARITY). FT TRANSMEM 153 173 BY SIMILARITY. **argh FT TOPO_DOM 174 227 CYTOPLASMIC (BY SIMILARITY). ** ** ################# SOURCE SECTION ################## ** Rhodobacter sphaeroides C4-dicarboxylate binding-protein precursor (dctP), ** small integral membrane transport protein (dctQ) and large integral ** membrane transport protein (dctM) genes, complete cds. ** source 1..3718 ** /db_xref="taxon:1063" ** /organism="Rhodobacter sphaeroides" ** /strain="4P1" ** CDS 1214..1897 ** /codon_start=1 ** /note="DctQ; contains four putative transmembrane helices" ** /transl_table=11 ** /gene="dctQ" ** /product="small integral membrane transport protein" ** /protein_id="AAF72734.1" ** CDS_IN_EMBL_ENTRY 3 ** 02-JUN-2000 (Rel. 63, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_RHOSH SQ SEQUENCE 227 AA; 24991 MW; 2208AD920C1230DA CRC64; MMRLLDRLEE TLIASLIAAA TGLIFVSVVQ RYSLGLLADG VAFFRGHDMP ELSAMMRSAY LGLREFNLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINKLDERK RGFFILLGLG AGALFTGIIA TLGGNFVWHM AQTSAISPDL ELPMWLVYLA IPLGSALMCF RFLQVAVIFA RTGELAHHDH GHVEGVDTED EGIDVLGSTF LKSPLTPRDL VEKPKDE // ID DCTQ_WOLSU PRELIMINARY; PRT; 170 AA. AC Q9ZEJ3; DT 01-MAY-1999 (TrEMBLrel. 10, Created) DT 01-MAY-1999 (TrEMBLrel. 10, Last sequence update) DT 01-MAY-1999 (TrEMBLrel. 10, Last annotation update) DE Small C4-dicarboxylate integral membrane transport protein. OS Wolinella succinogenes. OC Bacteria; Proteobacteria; epsilon subdivision; Helicobacter group; OC Wolinella. OX NCBI_TaxID=844; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DSMZ 1740; RX MEDLINE=20461222; PubMed=11004174; RA Ullmann R., Gross R., Simon J., Unden G., Kroeger A.; RT "Transport of C(4)-dicarboxylates in Wolinella succinogenes."; RL J. Bacteriol. 182:5757-5764(2000). CC -!- FUNCTION: INVOLVED IN THE ELECTROGENIC UNIPORT OF C4- CC DICARBOXYLATES. CC -!- PATHWAY: BELONGS TO THE TRIPARTITE ATP-INDEPENDENT PERIPLASMIC CC (TRAP) TRANSPORTER FAMILY. DR EMBL; AJ132740; CAA10757.1; -. ** ** ################# SOURCE SECTION ################## ** Wolinella succinogenes dctP, dctQ and dctM genes, and partial orfN ** source 1..3309 ** /organism="Wolinella succinogenes" ** /db_xref="taxon:844" ** CDS 1086..1598 ** /db_xref="PID:e1375211" ** /transl_table=11 ** /gene="dctQ" ** /product="small integral C4-dicarboxylate membrane ** transport protein, putative" ** /protein_id="CAA10757.1" ** CDS_IN_EMBL_ENTRY 4 ** 04-FEB-1999 (Rel. 58, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_WOLSU SQ SEQUENCE 170 AA; 18754 MW; 4CCF9F77E2F85C20 CRC64; MSKFFEILDL GIAAMNKSIA VIGISTGVIL AFINVVLRYF FDSGLTWAGE TINYLFIWSA LFGAAYGFKK GIHIAVTILV ERFPPLLAKA SLMIASLISL IFLLFIAYFG LHYVLLVKDM GFMSVDLGIP QWIPMVVIPV AFFAASYRVG EKIYEISKQP ADTVVKSAGR // ID DCTQ_WOLSU PRELIMINARY; PRT; 170 AA. AC Q9ZEJ3; DT 01-MAY-1999 (TrEMBLrel. 10, Created) DT 01-MAY-1999 (TrEMBLrel. 10, Last sequence update) DT 01-MAY-1999 (TrEMBLrel. 10, Last annotation update) DE Small C4-dicarboxylate integral membrane transport protein. OS Wolinella succinogenes. OC Bacteria; Proteobacteria; epsilon subdivision; Helicobacter group; OC Wolinella. OX NCBI_TaxID=844; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DSMZ 1740; RX MEDLINE=20461222; PubMed=11004174; RA Ullmann R., Gross R., Simon J., Unden G., Kroeger A.; RT "Transport of C(4)-dicarboxylates in Wolinella succinogenes."; RL J. Bacteriol. 182:5757-5764(2000). CC -!- FUNCTION: INVOLVED IN THE ELECTROGENIC UNIPORT OF C4- CC DICARBOXYLATES. ** or should this be in similarity?, do things in similarity have to have ++ a dr line? CC -!- PATHWAY: BELONGS TO THE TRIPARTITE ATP-INDEPENDENT PERIPLASMIC CC (TRAP) TRANSPORTER FAMILY. DR EMBL; AJ132740; CAA10757.1; -. ** ** ################# SOURCE SECTION ################## ** Wolinella succinogenes dctP, dctQ and dctM genes, and partial orfN ** source 1..3309 ** /organism="Wolinella succinogenes" ** /db_xref="taxon:844" ** CDS 1086..1598 ** /db_xref="PID:e1375211" ** /transl_table=11 ** /gene="dctQ" ** /product="small integral C4-dicarboxylate membrane ** transport protein, putative" ** /protein_id="CAA10757.1" ** CDS_IN_EMBL_ENTRY 4 ** 04-FEB-1999 (Rel. 58, Last updated, Version 1) ** ################# INTERNAL SECTION ################## **ID XXXX_WOLSU **ZZ unsure gene name, **ZZ will be deleted SQ SEQUENCE 170 AA; 18754 MW; 4CCF9F77E2F85C20 CRC64; MSKFFEILDL GIAAMNKSIA VIGISTGVIL AFINVVLRYF FDSGLTWAGE TINYLFIWSA LFGAAYGFKK GIHIAVTILV ERFPPLLAKA SLMIASLISL IFLLFIAYFG LHYVLLVKDM GFMSVDLGIP QWIPMVVIPV AFFAASYRVG EKIYEISKQP ADTVVKSAGR // ID DCTQ_RHOCA PRELIMINARY; PRT; 227 AA. AC O07837; DT 01-JUL-1997 (TrEMBLrel. 04, Created) DT 01-JUL-1997 (TrEMBLrel. 04, Last sequence update) DT 01-NOV-1998 (TrEMBLrel. 08, Last annotation update) DE Small C4-dicarboxylate integral membrane transport protein. OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1061; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=B11; RX MEDLINE=92236423; PubMed=1809844; RA Shaw J.G., Hamblin M.J., Kelly D.J.; RT "Purification, characterization and nucleotide sequence of the RT periplasmic C4-dicarboxylate-binding protein (DctP) from Rhodobacter RT capsulatus."; RL Mol. Microbiol. 5:3055-3062(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=B11; RX MEDLINE=97431499; PubMed=9287004; RA Forward J.A., Behrendt M.C., Wyborn N.R., Cross R., Kelly D.J.; RT "TRAP transporters: a new family of periplasmic solute transport RT systems encoded by the dctPQM genes of Rhodobacter capsulatus and by RT homologs in diverse gram-negative bacteria."; RL J. Bacteriol. 179:5482-5493(1997). RN [3] RP DISCUSSION OF SEQUENCE. RX MEDLINE=20090467; PubMed=10627041; RA Rabus R., Jack D.L., Kelly D.J., Saier M.H. Jr; RT "TRAP transporters: an ancient family of extracytoplasmic solute- RT receptor-dependent secondary active transporters."; RL Microbiology 145:3431-3445(1999). RN [4] RP TOPOLOGY. RC STRAIN=B10; RX PubMed=11150659; RA Wyborn N.R., Alderson J., Andrews S.C., Kelly D.J.; RT "Topological analysis of DctQ, the small integral membrane protein of RT the C4-dicarboxylate TRAP transporter of Rhodobacter capsulatus."; RL FEMS Microbiol. Lett. 194:13-17(2001). CC -!- FUNCTION: REQUIRED FOR C4-DICARBOXYLATE TRANSPORT (table 2,ref2). CC -!- ENZYME REGULATION: TRANSPORT IS SENSITIVE TO MEMBRANE POTENTIAL CC UNCOUPLERS AND VANADATE INSENSITIVE (ref2 figs 6&7). CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (ref2 fig4). DR EMBL; AE009099; AAL42381.1; -. DR EMBL; X63974; CAA45386.1; -. DR Pfam; PF00627; UBA; 1. DR PROSITE; PS12345; TEST_DOMAIN; 1. ** PROSITE; PS12346; FALSE_DOMAIN; FALSE_POS. KW Transmembrane; Transport. FT TOPO_DOM 1 10 CYTOPLASMIC. FT TRANSMEM 11 29 FT TOPO_DOM 30 68 PERIPLASMIC. FT TRANSMEM 69 91 FT TOPO_DOM 92 112 CYTOPLASMIC. FT TRANSMEM 113 133 FT TOPO_DOM 134 152 PERIPLASMIC. FT TRANSMEM 153 173 FT TOPO_DOM 174 227 CYTOPLASMIC. ** ** ################# SOURCE SECTION ################## ** transmembrane regions are unsure ** R capsulatus dctP gene for C4-dicarboxylase binding protein ** source 1..4500 ** /organism="Rhodobacter capsulatus" ** /strain="B10" ** /clone_lib="Cosmid, pLAFR1" ** /clone="pDCT200, pDCT205" ** /chromosome="1" ** CDS 1084..1767 ** /gene="dctQ" ** /product="small integral membrane transport protein" ** /db_xref="PID:e324693" ** CDS_2_OUT_OF_5 ** 26-JUN-1997 (Rel. 52, Last updated, Version 20) ** ################# INTERNAL SECTION ################## **ID XXXX_RHOCA SQ SEQUENCE 227 AA; 24763 MW; 0DE9D59DE5450F99 CRC64; MLRILDRAEE VLIAALIATA TVLIFVSVTH RFTLGFVADF VGFFRGHGMT GAAAAAKSLY TTLRGINLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINRLDAPK RRFFILLGLG AGALFTGIIA TLGANFVLHM YHASSTSPDL ELPMWLVYLA IPMGSSLMCF RFLQVAFGFA RTGELPHHDH GHVDGVDTEN EGIDAEGDVL LHSPLTPRDL VEKPKDN // ID DCTQ_RHOCA PRELIMINARY; PRT; 227 AA. AC O07837; DT 01-JUL-1997 (TrEMBLrel. 04, Created) DT 01-JUL-1997 (TrEMBLrel. 04, Last sequence update) DT 01-NOV-1998 (TrEMBLrel. 08, Last annotation update) DE Small C4-dicarboxylate integral membrane transport protein. OS Rhodobacter capsulatus (Rhodopseudomonas capsulata). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1061; RN [1] RP SEQUENCE FROM N.A. ** I see SB10003 / St Louis as the strain from table 1, not B10. This may ** be due to an error. RC STRAIN=B11; RX MEDLINE=92236423; PubMed=1809844; RA Shaw J.G., Hamblin M.J., Kelly D.J.; RT "Purification, characterization and nucleotide sequence of the RT periplasmic C4-dicarboxylate-binding protein (DctP) from Rhodobacter RT capsulatus."; RL Mol. Microbiol. 5:3055-3062(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=B11; RX MEDLINE=97431499; PubMed=9287004; RA Forward J.A., Behrendt M.C., Wyborn N.R., Cross R., Kelly D.J.; RT "TRAP transporters: a new family of periplasmic solute transport RT systems encoded by the dctPQM genes of Rhodobacter capsulatus and by RT homologs in diverse gram-negative bacteria."; RL J. Bacteriol. 179:5482-5493(1997). RN [3] RP DISCUSSION OF SEQUENCE. RX MEDLINE=20090467; PubMed=10627041; RA Rabus R., Jack D.L., Kelly D.J., Saier M.H. Jr; RT "TRAP transporters: an ancient family of extracytoplasmic solute- RT receptor-dependent secondary active transporters."; RL Microbiology 145:3431-3445(1999). RN [4] RP TOPOLOGY. RC STRAIN=B10; RX PubMed=11150659; RA Wyborn N.R., Alderson J., Andrews S.C., Kelly D.J.; RT "Topological analysis of DctQ, the small integral membrane protein of RT the C4-dicarboxylate TRAP transporter of Rhodobacter capsulatus."; RL FEMS Microbiol. Lett. 194:13-17(2001). CC -!- FUNCTION: REQUIRED FOR C4-DICARBOXYLATE TRANSPORT (table 2,ref2). ** we could also say that transport is thought to use the membrane ** potential, in that case we might put it into function. Note that in ** ref 4 the use of an electrochemical gradient for energy is now sure ** and is cited in the intro. CC -!- ENZYME REGULATION: TRANSPORT IS SENSITIVE TO MEMBRANE POTENTIAL CC UNCOUPLERS AND VANADATE INSENSITIVE (ref2 figs 6&7). ** inner membrane upon expression in ecoli, but can we extrapolate to ** Rhoca? CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN (ref2 fig4). DR EMBL; AE009099; AAL42381.1; -. DR EMBL; X63974; CAA45386.1; -. DR Pfam; PF00627; UBA; 1. DR PROSITE; PS12345; TEST_DOMAIN; 1. ** PROSITE; PS12346; FALSE_DOMAIN; FALSE_POS. KW Transmembrane; Transport. FT TOPO_DOM 1 10 CYTOPLASMIC. FT TRANSMEM 11 29 FT TOPO_DOM 30 68 PERIPLASMIC. FT TRANSMEM 69 91 FT TOPO_DOM 92 112 CYTOPLASMIC. FT TRANSMEM 113 133 FT TOPO_DOM 134 152 PERIPLASMIC. FT TRANSMEM 153 173 FT TOPO_DOM 174 227 CYTOPLASMIC. ** ** ################# SOURCE SECTION ################## ** transmembrane regions are unsure ** R capsulatus dctP gene for C4-dicarboxylase binding protein ** source 1..4500 ** /organism="Rhodobacter capsulatus" ** /strain="B10" ** /clone_lib="Cosmid, pLAFR1" ** /clone="pDCT200, pDCT205" ** /chromosome="1" ** CDS 1084..1767 ** /gene="dctQ" ** /product="small integral membrane transport protein" ** /db_xref="PID:e324693" ** CDS_2_OUT_OF_5 ** 26-JUN-1997 (Rel. 52, Last updated, Version 20) ** ################# INTERNAL SECTION ################## **ID XXXX_RHOCA SQ SEQUENCE 227 AA; 24763 MW; 0DE9D59DE5450F99 CRC64; MLRILDRAEE VLIAALIATA TVLIFVSVTH RFTLGFVADF VGFFRGHGMT GAAAAAKSLY TTLRGINLVW AQELCIILFV WMAKFGAAYG VRTGIHVGID VLINRLDAPK RRFFILLGLG AGALFTGIIA TLGANFVLHM YHASSTSPDL ELPMWLVYLA IPMGSSLMCF RFLQVAFGFA RTGELPHHDH GHVDGVDTEN EGIDAEGDVL LHSPLTPRDL VEKPKDN // ID BL1A_HUMAN PRELIMINARY; PRT; 835 AA. **BCLA_human = O95999 AC Q9H165; Q86W14; Q8WU92; Q96JL6; Q9H163; Q9H164; Q9H3G9; Q9NWA7; DT 01-MAR-2001 (TrEMBLrel. 16, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-MAR-2003 (TrEMBLrel. 23, Last annotation update) DE B-cell CLL/lymphoma 11A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 4 AND 5). RC TISSUE=Fetal brain; RX PubMed=11161790; RA Saiki Y., Yamazaki Y., Yoshida M., Katoh O., Nakamura T.; RT "Human EVI9, a homologue of the mouse myeloid leukemia gene, is RT expressed in the hematopoietic progenitors and down-regulated during RT myeloid differentiation of HL60 cells."; RL Genomics 70:387-391(2000). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 3). RX PubMed=11719382; RA Satterwhite E., Sonoki T., Willis T.G., Harder L., Nowak R., RA Arriola E.L., Liu H., Price H.P., Gesk S., Steinemann D., RA Schlegelberger B., Oscier D.G., Siebert R., Tucker P.W., Dyer M.J.; RT "The BCL11 gene family: involvement of BCL11A in lymphoid RT malignancies."; RL Blood 98:3413-3420(2001). RN [3] RP SEQUENCE FROM N.A. (ISOFORM 6). RA Suriyapperuma S.P., Sarfarazi M.; RT "Identification of a new isoform for B-cell CLL/lymphoma 11A (BCL11A) RT gene."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11853319; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXII. RT The complete sequences of 50 new cDNA clones which code for large RT proteins."; RL DNA Res. 8:319-327(2001). RN [5] RP SEQUENCE FROM N.A. (ISOFORM 7). RC TISSUE=Embryo; RX PubMed=14702039; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J.-I., Saito K., Kawai Y., Isono Y., Nakamura Y., RA Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., RA Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., RA Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., RA Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., RA Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., RA Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., RA Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., RA Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., RA Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., RA Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Lymph; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: An essential factor in lymphopoiesis and is required for CC B-cell formation in fetal liver. May play important roles in CC leukemogenesis and hematopoiesis. Might act as a dominant proto- CC oncogene. Potentiates ARP1-mediated transcriptional repression in CC a trichostatin-insensitive manner (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=XL; CC IsoId=Q9H165-1; Sequence=Displayed; CC Name=2; Synonyms=L; CC IsoId=Q9H165-2; Sequence=?; CC Name=3; Synonyms=S; CC IsoId=Q9H165-3; Sequence=?; CC Note=May be due to an exon skipping; CC Name=4; CC IsoId=Q9H165-4; Sequence=?; CC Name=5; CC IsoId=Q9H165-5; Sequence=?; CC Name=6; CC IsoId=Q9H165-6; Sequence=?; CC Name=7; CC IsoId=Q9H165-7; Sequence=?; CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, spleen CC thymus, bone marrow and testis. Expressed in CD34-positive myeloid CC precursor cells, B cells, monocytes, and megakaryoctes. Expression CC is tightly regulated during B-cell development. CC -!- DISEASE: May be involved in lymphoid malignancies through either CC chromosomal translocation t(2;14)(p13;q32.3), or amplification. DR EMBL; AF080216; AAG49025.1; -. DR EMBL; AJ404611; CAC17723.1; -. DR EMBL; AJ404612; CAC17724.1; -. DR EMBL; AJ404613; CAC17725.1; -. DR EMBL; AY228763; AAO88272.1; -. DR EMBL; AB058712; BAB47438.1; ALT_INIT. DR EMBL; AK001035; BAA91476.1; -. DR EMBL; BC021098; AAH21098.1; ALT_INIT. DR HGNC; HGNC:13221; BCL11A. DR MIM; 606557; -. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 6. DR SMART; SM00355; ZnF_C2H2; 6. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. DR HSSP; P15822; 1BBO. KW Alternative splicing; B-cell activation; Chromosomal translocation; KW Metal-binding; Transcription regulation; Zinc; Zinc-finger. FT ZN_FING 170 193 C2H2-type 1. FT ZN_FING 377 399 C2H2-type 2. FT ZN_FING 405 429 C2H2-type 3. FT ZN_FING 742 764 C2H2-type 4. FT ZN_FING 770 792 C2H2-type 5. FT ZN_FING 800 823 C2H2-type 6. FT COMPBIAS 260 373 Pro-rich. FT COMPBIAS 481 509 Glu-rich. FT VAR_SEQ 1 648 Missing (in isoform 7). FT VAR_SEQ 1 1 M -> MSKGTDEDIFSGVSFFLTRLSRCEPSRRPPAPQPT FT (in isoform 4 and isoform 5). FT VAR_SEQ 129 163 DKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGIC -> G FT (in isoform 6). FT VAR_SEQ 211 239 VGIPSGLGAECPSQPPLHGIHIADNNPFN -> CSSHTPIR FT RSTQRAQDVWQFSDGSRALKF (in isoform 5). FT VAR_SEQ 212 243 GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI -> LHTPP FT FGVVPRELKMCGSFRMEAREPLSSEKI (in isoform FT 3). FT VAR_SEQ 240 835 Missing (in isoform 5). FT VAR_SEQ 244 835 Missing (in isoform 3). FT VAR_SEQ 522 532 Missing (in isoform 4). FT VAR_SEQ 745 773 EYCGKVFKNCSNLTVHRRSHTGERPYKCE -> SSHTPIRR FT STQRAQDVWQFSDGSSRALKF (in isoform 2). FT VAR_SEQ 745 773 EYCGKVFKNCSNLTVHRRSHTGERPYKCE -> SSHTPIRR FT STQRAQDVWQFSDGSSRALKF (in isoform 4). FT VAR_SEQ 774 835 Missing (in isoform 2). FT CONFLICT 119 119 G -> R (in Ref. 2). FT CONFLICT 316 316 S -> F (in Ref. 1). FT CONFLICT 386 386 F -> L (in Ref. 1). FT CONFLICT 648 648 A -> T (in Ref. 2; CAC17723/CAC17724). FT CONFLICT 653 653 E -> D (in Ref. 1). FT CONFLICT 730 730 P -> T (in Ref. 2; CAC17723/CAC17724). ** ** ################# INTERNAL SECTION ################## **CL 2p16.1; **NI BCLLA **IS Q9H165-8. SQ SEQUENCE 835 AA; 91197 MW; D36A7D0BE6976DCF CRC64; MSRRKQGKPQ HLSKREFSPE PLEAILTDDE PDHGPLGAPE GDHDLLTCGQ CQMNFPLGDI LIFIEHKRKQ CNGSLCLEKA VDKPPSPSPI EMKKASNPVE VGIQVTPEDD DCLSTSSRGI CPKQEHIADK LLHWRGLSSP RSAHGALIPT PGMSAEYAPQ GICKDEPSSY TCTTCKQPFT SAWFLLQHAQ NTHGLRIYLE SEHGSPLTPR VGIPSGLGAE CPSQPPLHGI HIADNNPFNL LRIPGSVSRE ASGLAEGRFP PTPPLFSPPP RHHLDPHRIE RLGAEEMALA THHPSAFDRV LRLNPMAMEP PAMDFSRRLR ELAGNTSSPP LSPGRPSPMQ RLLQPFQPGS KPPFLATPPL PPLQSAPPPS QPPVKSKSCE FCGKTFKFQS NLVVHRRSHT GEKPYKCNLC DHACTQASKL KRHMKTHMHK SSPMTVKSDD GLSTASSPEP GTSDLVGSAS SALKSVVAKF KSENDPNLIP ENGDEEEEED DEEEEEEEEE EEEELTESER VDYGFGLSLE AARHHENSSR GAVVGVGDES RALPDVMQGM VLSSMQHFSE AFHQVLGEKH KRGHLAEAEG HRDTCDEDSV AGESDRIDDG TVNGRGCSPG ESASGGLSKK LLLGSPSSLS PFSKRIKLEK EFDLPPAAMP NTENVYSQWL AGYAASRQLK DPFLSFGDSR QSPFASSSEH SSENGSLRFS TPPGELDGGI SGRSGTGSGG STPHISGPGP GRPSSKEGRR SDTCEYCGKV FKNCSNLTVH RRSHTGERPY KCELCNYACA QSSKLTRHMK THGQVGKDVY KCEICKMPFS VYSTLEKHMK KWHSDRVLNN DIKTE // ID BL1A_HUMAN PRELIMINARY; PRT; 835 AA. **BCLA_human = O95999 AC Q9H165; Q86W14; Q8WU92; Q96JL6; Q9H163; Q9H164; Q9H3G9; Q9NWA7; DT 01-MAR-2001 (TrEMBLrel. 16, Created) DT 01-MAR-2001 (TrEMBLrel. 16, Last sequence update) DT 01-MAR-2003 (TrEMBLrel. 23, Last annotation update) DE B-cell CLL/lymphoma 11A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; ** Q9H3G9; RN [1] RP SEQUENCE FROM N.A. (ISOFORMS 4 AND 5). RC TISSUE=Fetal brain; RX PubMed=11161790; RA Saiki Y., Yamazaki Y., Yoshida M., Katoh O., Nakamura T.; RT "Human EVI9, a homologue of the mouse myeloid leukemia gene, is RT expressed in the hematopoietic progenitors and down-regulated during RT myeloid differentiation of HL60 cells."; RL Genomics 70:387-391(2000). ** Q9H165 Q9H163; Q9H164; RN [2] RP SEQUENCE FROM N.A. (ISOFORMS 1; 2 AND 3). RX PubMed=11719382; RA Satterwhite E., Sonoki T., Willis T.G., Harder L., Nowak R., RA Arriola E.L., Liu H., Price H.P., Gesk S., Steinemann D., RA Schlegelberger B., Oscier D.G., Siebert R., Tucker P.W., Dyer M.J.; RT "The BCL11 gene family: involvement of BCL11A in lymphoid RT malignancies."; RL Blood 98:3413-3420(2001). **Q86W14; RN [3] RP SEQUENCE FROM N.A. (ISOFORM 6). RA Suriyapperuma S.P., Sarfarazi M.; RT "Identification of a new isoform for B-cell CLL/lymphoma 11A (BCL11A) RT gene."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. ** Q96JL6 RN [4] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Brain; RX PubMed=11853319; RA Nagase T., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XXII. RT The complete sequences of 50 new cDNA clones which code for large RT proteins."; RL DNA Res. 8:319-327(2001). ** Q9NWA7; RN [5] RP SEQUENCE FROM N.A. (ISOFORM 7). RC TISSUE=Embryo; RX PubMed=14702039; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J.-I., Saito K., Kawai Y., Isono Y., Nakamura Y., RA Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., RA Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., RA Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., RA Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., RA Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., RA Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., RA Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., RA Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., RA Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., RA Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). ** Q96JL6 RN [6] RP SEQUENCE FROM N.A. (ISOFORM 2). RC TISSUE=Lymph; RX MEDLINE=22388257; PubMed=12477932; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). ** PG 387 REF1 CC -!- FUNCTION: An essential factor in lymphopoiesis and is required for CC B-cell formation in fetal liver. May play important roles in CC leukemogenesis and hematopoiesis. Might act as a dominant proto- CC oncogene. Potentiates ARP1-mediated transcriptional repression in CC a trichostatin-insensitive manner (By similarity). **CC -!- SUBCELLULAR LOCATION: Nuclear. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=XL; CC IsoId=Q9H165-1; Sequence=Displayed; CC Name=2; Synonyms=L; CC IsoId=Q9H165-2; Sequence=?; CC Name=3; Synonyms=S; CC IsoId=Q9H165-3; Sequence=?; CC Note=May be due to an exon skipping; CC Name=4; CC IsoId=Q9H165-4; Sequence=?; CC Name=5; CC IsoId=Q9H165-5; Sequence=?; CC Name=6; CC IsoId=Q9H165-6; Sequence=?; CC Name=7; CC IsoId=Q9H165-7; Sequence=?; **PG 389 REF1 2 pg3415 CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, spleen CC thymus, bone marrow and testis. Expressed in CD34-positive myeloid CC precursor cells, B cells, monocytes, and megakaryoctes. Expression CC is tightly regulated during B-cell development. CC -!- DISEASE: May be involved in lymphoid malignancies through either CC chromosomal translocation t(2;14)(p13;q32.3), or amplification. **add standard line about chromosomal translocation, add Ft line for **breakpoints if known **add cc similarity ** Q9H3G9; DR EMBL; AF080216; AAG49025.1; -. ** Q9H165; Q9H163;Q9H164; DR EMBL; AJ404611; CAC17723.1; -. DR EMBL; AJ404612; CAC17724.1; -. DR EMBL; AJ404613; CAC17725.1; -. **Q86W14; DR EMBL; AY228763; AAO88272.1; -. **Q96JL6; Q8WU92; DR EMBL; AB058712; BAB47438.1; ALT_INIT. ** Q9NWA7; DR EMBL; AK001035; BAA91476.1; -. **Q96JL6; Q8WU92; DR EMBL; BC021098; AAH21098.1; ALT_INIT. DR HGNC; HGNC:13221; BCL11A. DR MIM; 606557; -. DR InterPro; IPR007087; Znf_C2H2. DR Pfam; PF00096; zf-C2H2; 6. DR SMART; SM00355; ZnF_C2H2; 6. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6. DR HSSP; P15822; 1BBO. KW Alternative splicing; B-cell activation; Chromosomal translocation; KW Metal-binding; Transcription regulation; Zinc; Zinc-finger. FT ZN_FING 170 193 C2H2-type 1. FT ZN_FING 377 399 C2H2-type 2. FT ZN_FING 405 429 C2H2-type 3. FT ZN_FING 742 764 C2H2-type 4. FT ZN_FING 770 792 C2H2-type 5. FT ZN_FING 800 823 C2H2-type 6. FT COMPBIAS 260 373 Pro-rich. FT COMPBIAS 481 509 Glu-rich. FT VAR_SEQ 1 648 Missing (in isoform 7). FT VAR_SEQ 1 1 M -> MSKGTDEDIFSGVSFFLTRLSRCEPSRRPPAPQPT FT (in isoform 4 and isoform 5). FT VAR_SEQ 129 163 DKLLHWRGLSSPRSAHGALIPTPGMSAEYAPQGIC -> G FT (in isoform 6). FT VAR_SEQ 211 239 VGIPSGLGAECPSQPPLHGIHIADNNPFN -> CSSHTPIR FT RSTQRAQDVWQFSDGSRALKF (in isoform 5). FT VAR_SEQ 212 243 GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI -> LHTPP FT FGVVPRELKMCGSFRMEAREPLSSEKI (in isoform FT 3). FT VAR_SEQ 240 835 Missing (in isoform 5). FT VAR_SEQ 244 835 Missing (in isoform 3). FT VAR_SEQ 522 532 Missing (in isoform 4). FT VAR_SEQ 745 773 EYCGKVFKNCSNLTVHRRSHTGERPYKCE -> SSHTPIRR FT STQRAQDVWQFSDGSSRALKF (in isoform 2). FT VAR_SEQ 745 773 EYCGKVFKNCSNLTVHRRSHTGERPYKCE -> SSHTPIRR FT STQRAQDVWQFSDGSSRALKF (in isoform 4). FT VAR_SEQ 774 835 Missing (in isoform 2). FT CONFLICT 119 119 G -> R (in Ref. 2). FT CONFLICT 316 316 S -> F (in Ref. 1). FT CONFLICT 386 386 F -> L (in Ref. 1). FT CONFLICT 648 648 A -> T (in Ref. 2; CAC17723/CAC17724). FT CONFLICT 653 653 E -> D (in Ref. 1). FT CONFLICT 730 730 P -> T (in Ref. 2; CAC17723/CAC17724). ** ** ################# INTERNAL SECTION ################## **CL 2p16.1; **NI BCLLA **IS Q9H165-8. SQ SEQUENCE 835 AA; 91197 MW; D36A7D0BE6976DCF CRC64; MSRRKQGKPQ HLSKREFSPE PLEAILTDDE PDHGPLGAPE GDHDLLTCGQ CQMNFPLGDI LIFIEHKRKQ CNGSLCLEKA VDKPPSPSPI EMKKASNPVE VGIQVTPEDD DCLSTSSRGI CPKQEHIADK LLHWRGLSSP RSAHGALIPT PGMSAEYAPQ GICKDEPSSY TCTTCKQPFT SAWFLLQHAQ NTHGLRIYLE SEHGSPLTPR VGIPSGLGAE CPSQPPLHGI HIADNNPFNL LRIPGSVSRE ASGLAEGRFP PTPPLFSPPP RHHLDPHRIE RLGAEEMALA THHPSAFDRV LRLNPMAMEP PAMDFSRRLR ELAGNTSSPP LSPGRPSPMQ RLLQPFQPGS KPPFLATPPL PPLQSAPPPS QPPVKSKSCE FCGKTFKFQS NLVVHRRSHT GEKPYKCNLC DHACTQASKL KRHMKTHMHK SSPMTVKSDD GLSTASSPEP GTSDLVGSAS SALKSVVAKF KSENDPNLIP ENGDEEEEED DEEEEEEEEE EEEELTESER VDYGFGLSLE AARHHENSSR GAVVGVGDES RALPDVMQGM VLSSMQHFSE AFHQVLGEKH KRGHLAEAEG HRDTCDEDSV AGESDRIDDG TVNGRGCSPG ESASGGLSKK LLLGSPSSLS PFSKRIKLEK EFDLPPAAMP NTENVYSQWL AGYAASRQLK DPFLSFGDSR QSPFASSSEH SSENGSLRFS TPPGELDGGI SGRSGTGSGG STPHISGPGP GRPSSKEGRR SDTCEYCGKV FKNCSNLTVH RRSHTGERPY KCELCNYACA QSSKLTRHMK THGQVGKDVY KCEICKMPFS VYSTLEKHMK KWHSDRVLNN DIKTE // ID NUSG_SULAC STANDARD; PRT; 152 AA. AC P27341; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative transcription antitermination protein nusG. OS Sulfolobus acidocaldarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=2285; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92048486; PubMed=1658539; RA Ramirez C., Matheson A.T.; RT "A gene in the archaebacterium Sulfolobus solfataricus that codes for RT a protein equivalent to the alpha subunits of the signal recognition RT particle receptor in eukaryotes."; RL Mol. Microbiol. 5:1687-1693(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 33909 / NCIB 11770 / DSM 639; RX MEDLINE=95226466; PubMed=7711082; RA Moll R., Schmidtke S., Schaefer G.; RT "Nucleotide sequence of a gene cluster encoding ribosomal proteins in RT the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius."; RL Biochim. Biophys. Acta 1261:315-318(1995). RN [3] RP SIMILARITY. RX MEDLINE=95206934; PubMed=7899076; RA Ouzounis C., Kyrpides N., Sander C.; RT "Novel protein families in archaean genomes."; RL Nucleic Acids Res. 23:565-570(1995). CC -!- SIMILARITY: TO BACTERIAL PROTEINS NUSG AND ALSO TO THE L24P FAMILY CC OF RIBOSOMAL PROTEINS. CC -!- CAUTION: Was originally (Ref.1) thought to originate from CC S.solfataricus strain P1, but the culture was contaminated with CC S.acidocaldarius. DR EMBL; X58538; CAA41431.1; -. DR EMBL; X77509; CAA54645.1; -. DR PIR; S53705; S53705. DR InterPro; IPR003257; Bac_NusG. DR InterPro; IPR005824; KOW. DR InterPro; IPR006646; KOW_sub. DR InterPro; IPR006645; NgN. DR InterPro; IPR008991; Transl_SH3_like. DR Pfam; PF00467; KOW; 1. DR ProDom; PD005267; Bac_NusG; 1. DR SMART; SM00739; KOW; 1. DR SMART; SM00738; NGN; 1. ** PROSITE; PS01108; RIBOSOMAL_L24; FALSE_POS_1. ** PROSITE; PS00430; TONB_DEPENDENT_REC_1; FALSE_POS_1. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 152 AA; 16877 MW; 316F31BBCC22620D CRC64; MEDFKYRNYY VLRVTGGQEI NVALILEERI KTNNINEIFS VVVPPNIKGY VILEATGPHV VKLISSGIRH VKGVAHGLIQ KEDVTKFVSK SVALPAVKEG DLVEVISGPF RGMQAQVVRV ESTKNEVVLN ILESSYPVQV TVPLEQVKPV KR // ID NUSG_SULAC STANDARD; PRT; 152 AA. AC P27341; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative transcription antitermination protein nusG. OS Sulfolobus acidocaldarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=2285; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92048486; PubMed=1658539; RA Ramirez C., Matheson A.T.; RT "A gene in the archaebacterium Sulfolobus solfataricus that codes for RT a protein equivalent to the alpha subunits of the signal recognition RT particle receptor in eukaryotes."; RL Mol. Microbiol. 5:1687-1693(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 33909 / NCIB 11770 / DSM 639; RX MEDLINE=95226466; PubMed=7711082; RA Moll R., Schmidtke S., Schaefer G.; RT "Nucleotide sequence of a gene cluster encoding ribosomal proteins in RT the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius."; RL Biochim. Biophys. Acta 1261:315-318(1995). RN [3] RP SIMILARITY. RX MEDLINE=95206934; PubMed=7899076; RA Ouzounis C., Kyrpides N., Sander C.; RT "Novel protein families in archaean genomes."; RL Nucleic Acids Res. 23:565-570(1995). CC -!- SIMILARITY: TO BACTERIAL PROTEINS NUSG AND ALSO TO THE L24P FAMILY CC OF RIBOSOMAL PROTEINS. CC -!- CAUTION: Was originally (Ref.1) thought to originate from CC S.solfataricus strain P1, but the culture was contaminated with CC S.acidocaldarius. DR EMBL; X58538; CAA41431.1; -. DR EMBL; X77509; CAA54645.1; -. DR PIR; S53705; S53705. DR InterPro; IPR003257; Bac_NusG. DR InterPro; IPR005824; KOW. DR InterPro; IPR006646; KOW_sub. DR InterPro; IPR006645; NgN. DR InterPro; IPR008991; Transl_SH3_like. DR Pfam; PF00467; KOW; 1. DR ProDom; PD005267; Bac_NusG; 1. DR SMART; SM00739; KOW; 1. DR SMART; SM00738; NGN; 1. ** PROSITE; PS01108; RIBOSOMAL_L24; FALSE_POS_1. ** PROSITE; PS00430; TONB_DEPENDENT_REC_1; FALSE_POS_1. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 152 AA; 16877 MW; 316F31BBCC22620D CRC64; MEDFKYRNYY VLRVTGGQEI NVALILEERI KTNNINEIFS VVVPPNIKGY VILEATGPHV VKLISSGIRH VKGVAHGLIQ KEDVTKFVSK SVALPAVKEG DLVEVISGPF RGMQAQVVRV ESTKNEVVLN ILESSYPVQV TVPLEQVKPV KR // ID NUSG_SULAC STANDARD; PRT; 152 AA. AC P27341; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative transcription antitermination protein nusG. OS Sulfolobus acidocaldarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=2285; CC -!- FUNCTION: Nonselective ADPR-gated cation channel mediating sodium CC and calcium ion influx in response to oxidative stress. CC Extracellular calcium passes through the channel and acts from the CC intracellular side as a positive regulator in channel activation CC by hydrogen superoxide. Also activated by nicotinamide adenine CC dinucleotide (NAD(+)), reactive nitrogen species and arachidonic CC acid. Confers susceptibility to cell death following oxidative CC stress. Isoform 2 does not seem to be regulated by ADPR. Has an CC ADP-ribose pyrophosphatase activity. CC -!- CATALYTIC ACTIVITY: ADP-ribose + H(2)O = AMP + D-ribose 5- CC phosphate. CC -!- COFACTOR: CC Note=Binds NAD(+).; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=100 uM for ADP-ribose; CC Vmax=0.1 umol/min/mg enzyme; CC -!- SUBUNIT: Isoform 1 can interact with isoform 3. This interaction CC decreases calcium influx through isoform 1 and suppresses CC susceptibility to oxidative stress-induced cell death. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=1; Synonyms=TRPM2-L; CC IsoId=O94759-1; Sequence=Displayed; CC Name=2; CC IsoId=O94759-2; Sequence=VSP_006574, VSP_006575; CC Name=3; Synonyms=TRPM2-S; CC IsoId=O94759-3; Sequence=?; CC -!- TISSUE SPECIFICITY: Highly expressed in brain and peripheral blood CC cells, such as neutrophils. Also detected in bone marrow, spleen, CC heart, liver and lung. Isoform 2 is found in neutrophil CC granulocytes. CC -!- SIMILARITY: Belongs to the transient receptor family. LTrpC CC subfamily. CC -!- CAUTION: Ref.5 sequence differs from that shown due to frameshifts CC in positions 1227 and 1237. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 152 AA; 16877 MW; 316F31BBCC22620D CRC64; MEDFKYRNYY VLRVTGGQEI NVALILEERI KTNNINEIFS VVVPPNIKGY VILEATGPHV VKLISSGIRH VKGVAHGLIQ KEDVTKFVSK SVALPAVKEG DLVEVISGPF RGMQAQVVRV ESTKNEVVLN ILESSYPVQV TVPLEQVKPV KR // ID NUSG_SULAC STANDARD; PRT; 152 AA. AC P27341; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative transcription antitermination protein nusG. OS Sulfolobus acidocaldarius. OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=2285; **no evidence found CC -!- FUNCTION: Nonselective ADPR-gated cation channel mediating sodium CC and calcium ion influx in response to oxidative stress. CC Extracellular calcium passes through the channel and acts from the CC intracellular side as a positive regulator in channel activation CC by hydrogen superoxide. Also activated by nicotinamide adenine CC dinucleotide (NAD(+)), reactive nitrogen species and arachidonic CC acid. Confers susceptibility to cell death following oxidative CC stress. Isoform 2 does not seem to be regulated by ADPR. Has an CC ADP-ribose pyrophosphatase activity. CC -!- CATALYTIC ACTIVITY: ADP-ribose + H(2)O = AMP + D-ribose 5- CC phosphate. CC -!- COFACTOR: CC Note=Binds NAD(+).; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=100 uM for ADP-ribose; CC Vmax=0.1 umol/min/mg enzyme; CC -!- SUBUNIT: Isoform 1 can interact with isoform 3. This interaction CC decreases calcium influx through isoform 1 and suppresses CC susceptibility to oxidative stress-induced cell death. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=1; Synonyms=TRPM2-L; CC IsoId=O94759-1; Sequence=Displayed; CC Name=2; CC IsoId=O94759-2; Sequence=VSP_006574, VSP_006575; CC Name=3; Synonyms=TRPM2-S; CC IsoId=O94759-3; Sequence=?; CC -!- TISSUE SPECIFICITY: Highly expressed in brain and peripheral blood CC cells, such as neutrophils. Also detected in bone marrow, spleen, CC heart, liver and lung. Isoform 2 is found in neutrophil CC granulocytes. CC -!- SIMILARITY: Belongs to the transient receptor family. LTrpC CC subfamily. CC -!- CAUTION: Ref.5 sequence differs from that shown due to frameshifts CC in positions 1227 and 1237. ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 152 AA; 16877 MW; 316F31BBCC22620D CRC64; MEDFKYRNYY VLRVTGGQEI NVALILEERI KTNNINEIFS VVVPPNIKGY VILEATGPHV VKLISSGIRH VKGVAHGLIQ KEDVTKFVSK SVALPAVKEG DLVEVISGPF RGMQAQVVRV ESTKNEVVLN ILESSYPVQV TVPLEQVKPV KR // ID PAX3_HUMAN STANDARD; PRT; 479 AA. AC P23760; Q16448; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Paired box protein Pax-3 (HUP2). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 479 AA; 52968 MW; 8AFCA674E3ACB4FE CRC64; MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNPDS SSAYCLPSTR HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE PTTTVSASCS QRLDHMKSLD SLPTSQSYCP PTYSTTGYSM DPVTGYQYGQ YGQSKPWTF // ID PAX3_HUMAN STANDARD; PRT; 479 AA. AC P23760; Q16448; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Paired box protein Pax-3 (HUP2). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; ** ** ################# INTERNAL SECTION ################## SQ SEQUENCE 479 AA; 52968 MW; 8AFCA674E3ACB4FE CRC64; MTTLAGAVPR MMRPGPGQNY PRSGFPLEVS TPLGQGRVNQ LGGVFINGRP LPNHIRHKIV EMAHHGIRPC VISRQLRVSH GCVSKILCRY QETGSIRPGA IGGSKPKQVT TPDVEKKIEE YKRENPGMFS WEIRDKLLKD AVCDRNTVPS VSSISRILRS KFGKGEEEEA DLERKEAEES EKKAKHSIDG ILSERASAPQ SDEGSDIDSE PDLPLKRKQR RSRTTFTAEQ LEELERAFER THYPDIYTRE ELAQRAKLTE ARVQVWFSNR RARWRKQAGA NQLMAFNHLI PGGFPPTAMP TLPTYQLSET SYQPTSIPQA VSDPSSTVHR PQPLPPSTVH QSTIPSNPDS SSAYCLPSTR HGFSSYTDSF VPPSGPSNPM NPTIGNGLSP QVMGLLTNHG GVPHQPQTDY ALSPLTGGLE PTTTVSASCS QRLDHMKSLD SLPTSQSYCP PTYSTTGYSM DPVTGYQYGQ YGQSKPWTF // Swissknife_1.75/t/fasta.txl.expected0000644005110600510130000000232211551045100017732 0ustar ecastroSwissProt>tr|Q9LBD9|DCTQ_RHOSH Putative small C4-dicarboxylate integral membrane transport protein OS=Rhodobacter sphaeroides GN=DCTQ MMRLLDRLEETLIASLIAAATGLIFVSVVQRYSLGLLADGVAFFRGHDMPELSAMMRSAY LGLREFNLVWAQELCIILFVWMAKFGAAYGVRTGIHVGIDVLINKLDERKRGFFILLGLG AGALFTGIIATLGGNFVWHMAQTSAISPDLELPMWLVYLAIPLGSALMCFRFLQVAVIFA RTGELAHHDHGHVEGVDTEDEGIDVLGSTFLKSPLTPRDLVEKPKDE >tr|Q9LBD9|DCTQ_RHOSH Putative small C4-dicarboxylate integral membrane transport protein with a very very very very very very very very very very very very very very very very very very very very very very very very very very very very very very very very very very very very long name (Fragment) OS=Rhodobacter sphaeroides MMRLLDRLEETLIASLIAAATGLIFVSVVQRYSLGLLADGVAFFRGHDMPELSAMMRSAY LGLREFNLVWAQELCIILFVWMAKFGAAYGVRTGIHVGIDVLINKLDERKRGFFILLGLG AGALFTGIIATLGGNFVWHMAQTSAISPDLELPMWLVYLAIPLGSALMCFRFLQVAVIFA RTGELAHHDHGHVEGVDTEDEGIDVLGSTFLKSPLTPRDLVEKPKDE >sp|Q2JI31|3MGH_SYNJB Putative 3-methyladenine DNA glycosylase OS=Synechococcus sp. (strain JA-2-3B'a(2-13)) GN=CYB_2817 SV=1 MEWLSQPAPLVAPALLGMVLVRQFADGLQVRAQIVETEAYTAGDPACHAYRRKTQRNQVM FGPPGHLYIYRIYGLYHCLNIVTEPEGIPAAVLIRAAQLDRLPDWIPANKQNQPARAAAG PGLLCQALRIDGSHNGWRLERAEAGQEGIWLEGSPSWQTQLSIVQTTRIGITQGAEIPWR WYIGGHPAVSRY Swissknife_1.75/examples/0000755005110600510130000000000013155516754015703 5ustar ecastroSwissProtSwissknife_1.75/examples/SWISS100.dat0000755005110600510130001206344312366166552017546 0ustar ecastroSwissProtID 1433B_HUMAN Reviewed; 246 AA. AC P31946; A8K9K2; E1P616; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-JUL-2014, entry version 166. DE RecName: Full=14-3-3 protein beta/alpha; DE AltName: Full=Protein 1054; DE AltName: Full=Protein kinase C inhibitor protein 1; DE Short=KCIP-1; DE Contains: DE RecName: Full=14-3-3 protein beta/alpha, N-terminally processed; GN Name=YWHAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Keratinocyte; RX PubMed=8515476; DOI=10.1006/jmbi.1993.1346; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RC TISSUE=Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 1-11; 14-57; 63-70; 106-117; 130-169 AND 215-246, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma; RA Bienvenut W.V., Zebisch A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [7] RP PROTEIN SEQUENCE OF 3-20. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP INTERACTION WITH AANAT. RX PubMed=11427721; DOI=10.1073/pnas.141118798; RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.; RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14- RT 3-3-binding switch in melatonin synthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001). RN [9] RP INTERACTION WITH CRTC2. RX PubMed=15454081; DOI=10.1016/j.cell.2004.09.015; RA Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., RA Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., RA Okamoto M., Montminy M.; RT "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive RT coincidence detector."; RL Cell 119:61-74(2004). RN [10] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). RN [11] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [12] RP INTERACTION WITH YAP1. RX PubMed=17974916; DOI=10.1101/gad.1602907; RA Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J., RA Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G., RA Lai Z.C., Guan K.L.; RT "Inactivation of YAP oncoprotein by the Hippo pathway is involved in RT cell contact inhibition and tissue growth control."; RL Genes Dev. 21:2747-2761(2007). RN [13] RP INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17717073; DOI=10.1210/me.2007-0323; RA Liu Y., Ross J.F., Bodine P.V.N., Billiard J.; RT "Homodimerization of Ror2 tyrosine kinase receptor induces 14-3- RT 3(beta) phosphorylation and promotes osteoblast differentiation and RT bone formation."; RL Mol. Endocrinol. 21:3050-3061(2007). RN [14] RP INTERACTION WITH GAB2. RX PubMed=19172738; DOI=10.1038/emboj.2008.159; RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., RA Guilhaus M., James D.E., Daly R.J.; RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by RT the Gab2 docking protein."; RL EMBO J. 27:2305-2316(2008). RN [15] RP FUNCTION, AND INTERACTION WITH SRPK2. RX PubMed=19592491; DOI=10.1074/jbc.M109.026237; RA Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.; RT "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell RT cycle and cell death in neurons."; RL J. Biol. Chem. 284:24512-24525(2009). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-117, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [20] RP INTERACTION WITH MYO1C. RX PubMed=24636949; DOI=10.1016/j.jmb.2014.03.004; RA Stefan Munnich M.H., Manstein D.J.; RT "Crystal structure of human myosin 1c - the motor in GLUT4 exocytosis: RT implications for Ca(2+)-regulation and 14-3-3 binding."; RL J. Mol. Biol. 426:2070-2081(2014). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, IDENTIFICATION BY MASS RP SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT. RX PubMed=17085597; DOI=10.1073/pnas.0605779103; RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.; RT "Structural basis for protein-protein interactions in the 14-3-3 RT protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006). RN [22] RP VARIANT ILE-99. RX PubMed=21248752; DOI=10.1038/nature09639; RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., RA Futreal P.A.; RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex RT gene PBRM1 in renal carcinoma."; RL Nature 469:539-542(2011). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathways. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. Negative CC regulator of osteogenesis. Blocks the nuclear translocation of the CC phosphorylated form (by AKT1) of SRPK2 and antagonizes its CC stimulatory effect on cyclin D1 expression resulting in blockage CC of neuronal apoptosis elicited by SRPK2. CC -!- SUBUNIT: Homodimer. Interacts with SAMSN1 and PRKCE (By CC similarity). Interacts with SSH1 and TORC2/CRTC2. Interacts with CC ABL1; the interaction results in cytoplasmic location of ABL1 and CC inhibition of cABL-mediated apoptosis. Interacts with ROR2 CC (dimer); the interaction results in phosphorylation of YWHAB on CC tyrosine residues. Interacts with GAB2 and YAP1 (phosphorylated CC form). Interacts with the phosphorylated (by AKT1) form of SRPK2. CC Interacts with PKA-phosphorylated AANAT. Interacts with MYO1C. CC -!- INTERACTION: CC Q76353:- (xeno); NbExp=3; IntAct=EBI-359815, EBI-6248077; CC Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359815, EBI-1567267; CC P15056:BRAF; NbExp=3; IntAct=EBI-359815, EBI-365980; CC P22681:CBL; NbExp=3; IntAct=EBI-359815, EBI-518228; CC O00257:CBX4; NbExp=2; IntAct=EBI-359815, EBI-722425; CC P30304:CDC25A; NbExp=8; IntAct=EBI-359815, EBI-747671; CC P30305:CDC25B; NbExp=4; IntAct=EBI-359815, EBI-1051746; CC O94921:CDK14; NbExp=5; IntAct=EBI-359815, EBI-1043945; CC P67828:CSNK1A1 (xeno); NbExp=3; IntAct=EBI-359815, EBI-7540603; CC Q9NYF0:DACT1; NbExp=4; IntAct=EBI-359815, EBI-3951744; CC Q13627-2:DYRK1A; NbExp=3; IntAct=EBI-359815, EBI-1053621; CC Q9UQC2:GAB2; NbExp=4; IntAct=EBI-359815, EBI-975200; CC P55040:GEM; NbExp=3; IntAct=EBI-359815, EBI-744104; CC P55041:Gem (xeno); NbExp=3; IntAct=EBI-359815, EBI-7082069; CC P56524:HDAC4; NbExp=3; IntAct=EBI-359815, EBI-308629; CC Q11184:let-756 (xeno); NbExp=2; IntAct=EBI-359815, EBI-3843983; CC Q5S007:LRRK2; NbExp=3; IntAct=EBI-359815, EBI-5323863; CC Q99759:MAP3K3; NbExp=2; IntAct=EBI-359815, EBI-307281; CC Q99683:MAP3K5; NbExp=3; IntAct=EBI-359815, EBI-476263; CC Q7KZI7:MARK2; NbExp=3; IntAct=EBI-359815, EBI-516560; CC P27448:MARK3; NbExp=4; IntAct=EBI-359815, EBI-707595; CC P04049:RAF1; NbExp=17; IntAct=EBI-359815, EBI-365996; CC Q96TC7:RMDN3; NbExp=5; IntAct=EBI-359815, EBI-1056589; CC P61587:RND3; NbExp=2; IntAct=EBI-359815, EBI-1111534; CC P61588:Rnd3 (xeno); NbExp=5; IntAct=EBI-359815, EBI-6930266; CC P78362:SRPK2; NbExp=2; IntAct=EBI-359815, EBI-593303; CC Q8WYL5:SSH1; NbExp=3; IntAct=EBI-359815, EBI-1222387; CC Q91YE8:Synpo2 (xeno); NbExp=3; IntAct=EBI-359815, EBI-7623057; CC P49815:TSC2; NbExp=4; IntAct=EBI-359815, EBI-396587; CC P46937:YAP1; NbExp=5; IntAct=EBI-359815, EBI-1044059; CC P62258:YWHAE; NbExp=3; IntAct=EBI-359815, EBI-356498; CC P22893:Zfp36 (xeno); NbExp=5; IntAct=EBI-359815, EBI-647803; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Identified by CC mass spectrometry in melanosome fractions from stage I to stage CC IV. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; CC IsoId=P31946-1; Sequence=Displayed; CC Name=Short; CC IsoId=P31946-2; Sequence=VSP_018632; CC Note=Contains a N-acetylmethionine at position 1 (By CC similarity); CC -!- PTM: The alpha, brain-specific form differs from the beta form in CC being phosphorylated (By similarity). Phosphorylated on Ser-60 by CC protein kinase C delta type catalytic subunit in a sphingosine- CC dependent fashion (By similarity). CC -!- PTM: Isoform Short contains a N-acetylmethionine at position 1 (By CC similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X57346; CAA40621.1; -; mRNA. DR EMBL; AK292717; BAF85406.1; -; mRNA. DR EMBL; AL008725; CAA15497.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75893.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75894.1; -; Genomic_DNA. DR EMBL; CH471077; EAW75896.1; -; Genomic_DNA. DR EMBL; BC001359; AAH01359.1; -; mRNA. DR CCDS; CCDS13339.1; -. [P31946-1] DR PIR; S34755; S34755. DR RefSeq; NP_003395.1; NM_003404.4. [P31946-1] DR RefSeq; NP_647539.1; NM_139323.3. [P31946-1] DR UniGene; Hs.643544; -. DR PDB; 2BQ0; X-ray; 2.50 A; A/B=2-239. DR PDB; 2C23; X-ray; 2.65 A; A=2-239. DR PDB; 4DNK; X-ray; 2.20 A; A/B=1-246. DR PDBsum; 2BQ0; -. DR PDBsum; 2C23; -. DR PDBsum; 4DNK; -. DR ProteinModelPortal; P31946; -. DR SMR; P31946; 1-234. DR BioGrid; 113361; 302. DR DIP; DIP-743N; -. DR IntAct; P31946; 240. DR MINT; MINT-99570; -. DR STRING; 9606.ENSP00000300161; -. DR PhosphoSite; P31946; -. DR DMDM; 1345590; -. DR OGP; P31946; -. DR REPRODUCTION-2DPAGE; IPI00216318; -. DR MaxQB; P31946; -. DR PaxDb; P31946; -. DR PRIDE; P31946; -. DR DNASU; 7529; -. DR Ensembl; ENST00000353703; ENSP00000300161; ENSG00000166913. [P31946-1] DR Ensembl; ENST00000372839; ENSP00000361930; ENSG00000166913. [P31946-1] DR GeneID; 7529; -. DR KEGG; hsa:7529; -. DR UCSC; uc002xmt.3; human. [P31946-1] DR CTD; 7529; -. DR GeneCards; GC20P043515; -. DR HGNC; HGNC:12849; YWHAB. DR HPA; CAB003759; -. DR HPA; HPA007925; -. DR HPA; HPA011212; -. DR MIM; 601289; gene. DR neXtProt; NX_P31946; -. DR PharmGKB; PA37438; -. DR eggNOG; COG5040; -. DR HOGENOM; HOG000240379; -. DR HOVERGEN; HBG050423; -. DR InParanoid; P31946; -. DR KO; K16197; -. DR OMA; MGREYRE; -. DR OrthoDB; EOG7HHWT3; -. DR PhylomeDB; P31946; -. DR TreeFam; TF102003; -. DR Reactome; REACT_111045; Developmental Biology. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_21257; Metabolism of RNA. DR Reactome; REACT_578; Apoptosis. DR Reactome; REACT_6900; Immune System. DR Reactome; REACT_71; Gene Expression. DR SignaLink; P31946; -. DR ChiTaRS; YWHAB; human. DR EvolutionaryTrace; P31946; -. DR GeneWiki; YWHAB; -. DR GenomeRNAi; 7529; -. DR NextBio; 29453; -. DR PRO; PR:P31946; -. DR ArrayExpress; P31946; -. DR Bgee; P31946; -. DR CleanEx; HS_YWHAB; -. DR Genevestigator; P31946; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL. DR GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL. DR GO; GO:0050815; F:phosphoserine binding; IPI:BHF-UCL. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl. DR GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0051220; P:cytoplasmic sequestering of protein; IDA:BHF-UCL. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0035329; P:hippo signaling; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome. DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:BHF-UCL. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:BHF-UCL. DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome. DR GO; GO:0016070; P:RNA metabolic process; TAS:Reactome. DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. DR Gene3D; 1.20.190.20; -; 1. DR InterPro; IPR000308; 14-3-3. DR InterPro; IPR023409; 14-3-3_CS. DR InterPro; IPR023410; 14-3-3_domain. DR PANTHER; PTHR18860; PTHR18860; 1. DR Pfam; PF00244; 14-3-3; 1. DR PIRSF; PIRSF000868; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR SUPFAM; SSF48445; SSF48445; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative initiation; Complete proteome; KW Cytoplasm; Direct protein sequencing; Nitration; Phosphoprotein; KW Polymorphism; Reference proteome. FT CHAIN 1 246 14-3-3 protein beta/alpha. FT /FTId=PRO_0000367900. FT INIT_MET 1 1 Removed; alternate. FT CHAIN 2 246 14-3-3 protein beta/alpha, N-terminally FT processed. FT /FTId=PRO_0000000003. FT SITE 58 58 Interaction with phosphoserine on FT interacting protein (By similarity). FT SITE 129 129 Interaction with phosphoserine on FT interacting protein (By similarity). FT MOD_RES 1 1 N-acetylmethionine; in 14-3-3 protein FT beta/alpha; alternate. FT MOD_RES 2 2 N-acetylthreonine; in 14-3-3 protein FT beta/alpha, N-terminally processed. FT MOD_RES 60 60 Phosphoserine (By similarity). FT MOD_RES 70 70 N6-acetyllysine. FT MOD_RES 84 84 Nitrated tyrosine (By similarity). FT MOD_RES 106 106 Nitrated tyrosine (By similarity). FT MOD_RES 117 117 N6-acetyllysine. FT MOD_RES 186 186 Phosphoserine (By similarity). FT VAR_SEQ 1 2 Missing (in isoform Short). FT /FTId=VSP_018632. FT VARIANT 99 99 V -> I (found in a renal cell carcinoma FT sample; somatic mutation). FT /FTId=VAR_064762. FT HELIX 5 17 FT HELIX 21 33 FT HELIX 40 69 FT HELIX 75 105 FT HELIX 107 110 FT HELIX 114 133 FT HELIX 139 161 FT HELIX 167 182 FT HELIX 187 202 FT HELIX 203 207 FT TURN 210 212 FT HELIX 213 232 SQ SEQUENCE 246 AA; 28082 MW; 6BE1A9BF97468017 CRC64; MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD AGEGEN // ID 1433E_HUMAN Reviewed; 255 AA. AC P62258; B3KY71; D3DTH5; P29360; P42655; Q4VJB6; Q53XZ5; Q63631; AC Q7M4R4; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 09-JUL-2014, entry version 124. DE RecName: Full=14-3-3 protein epsilon; DE Short=14-3-3E; GN Name=YWHAE; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=7644510; DOI=10.1073/pnas.92.17.7892; RA Conklin D.S., Galaktionov K., Beach D.; RT "14-3-3 proteins associate with cdc25 phosphatases."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=8858348; DOI=10.1101/gr.6.8.735; RA Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.; RT "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on RT chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome RT region."; RL Genome Res. 6:735-741(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8684458; DOI=10.1038/382308a0; RA Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T.; RT "Function of 14-3-3 proteins."; RL Nature 382:308-308(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SV), AND ALTERNATIVE SPLICING. RC TISSUE=Brain; RX PubMed=20417184; DOI=10.1016/j.bbrc.2010.04.104; RA Han D., Ye G., Liu T., Chen C., Yang X., Wan B., Pan Y., Yu L.; RT "Functional identification of a novel 14-3-3 epsilon splicing variant RT suggests dimerization is not necessary for 14-3-3 epsilon to inhibit RT UV-induced apoptosis."; RL Biochem. Biophys. Res. Commun. 396:401-406(2010). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Heart; RA Luk S.C.W., Lee C.Y., Waye M.M.Y.; RT "Sequence determination of human epsilon 14-3-3 protein."; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Tanigami A., Chong S.S., Ledbetter D.H.; RT "14-3-3 epsilon genomic sequence."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND SV). RC TISSUE=Caudate nucleus, Heart, and Subthalamic nucleus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP PROTEIN SEQUENCE OF 1-19. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [12] RP PROTEIN SEQUENCE OF 1-19; 30-50 AND 131-170, ACETYLATION AT MET-1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (MAY-2005) to UniProtKB. RN [13] RP PROTEIN SEQUENCE OF 103-108; 120-123; 131-141 AND 143-153. RC TISSUE=Histiocytic lymphoma; RX PubMed=2026444; RA Demeter J., Medzihradszky D., Kha H., Goetzl E.J., Turck C.W.; RT "Isolation and partial characterization of the structures of RT fibroblast activating factor-related proteins from U937 cells."; RL Immunology 72:350-354(1991). RN [14] RP PROTEIN SEQUENCE OF 131-141 AND 154-190, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [15] RP INTERACTION WITH HCV CORE PROTEIN. RX PubMed=10644344; DOI=10.1128/JVI.74.4.1736-1741.2000; RA Aoki H., Hayashi J., Moriyama M., Arakawa Y., Hino O.; RT "Hepatitis C virus core protein interacts with 14-3-3 protein and RT activates the kinase Raf-1."; RL J. Virol. 74:1736-1741(2000). RN [16] RP INTERACTION WITH AANAT. RX PubMed=11427721; DOI=10.1073/pnas.141118798; RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.; RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14- RT 3-3-binding switch in melatonin synthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001). RN [17] RP INTERACTION WITH CDKN1B, AND SUBCELLULAR LOCATION. RX PubMed=12042314; DOI=10.1074/jbc.M203668200; RA Fujita N., Sato S., Katayama K., Tsuruo T.; RT "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 RT and cytoplasmic localization."; RL J. Biol. Chem. 277:28706-28713(2002). RN [18] RP INTERACTION WITH GRB10. RX PubMed=15722337; DOI=10.1074/jbc.M501477200; RA Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.; RT "Phosphorylation of grb10 regulates its interaction with 14-3-3."; RL J. Biol. Chem. 280:16987-16993(2005). RN [19] RP INTERACTION WITH ABL1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15696159; DOI=10.1038/ncb1228; RA Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.; RT "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of RT c-Abl in the apoptotic response to DNA damage."; RL Nat. Cell Biol. 7:278-285(2005). RN [20] RP INTERACTION WITH YWHAZ. RX PubMed=16376338; DOI=10.1016/j.febslet.2005.12.024; RA Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.; RT "Protein kinase A phosphorylates and regulates dimerization of 14-3-3 RT epsilon."; RL FEBS Lett. 580:305-310(2006). RN [21] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [22] RP INTERACTION WITH GAB2. RX PubMed=19172738; DOI=10.1038/emboj.2008.159; RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., RA Guilhaus M., James D.E., Daly R.J.; RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by RT the Gab2 docking protein."; RL EMBO J. 27:2305-2316(2008). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by RT enrichment and fractionation of phosphopeptides with strong anion RT exchange chromatography."; RL Proteomics 8:1346-1361(2008). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [25] RP INTERACTION WITH SRPK2. RX PubMed=19592491; DOI=10.1074/jbc.M109.026237; RA Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.; RT "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell RT cycle and cell death in neurons."; RL J. Biol. Chem. 284:24512-24525(2009). RN [26] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50; LYS-69; LYS-118 AND RP LYS-123, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [30] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-233, IDENTIFICATION BY RP MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT. RX PubMed=17085597; DOI=10.1073/pnas.0605779103; RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.; RT "Structural basis for protein-protein interactions in the 14-3-3 RT protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathways. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Heterodimerizes with YWHAZ. Interacts with CC NDEL1, ARHGEF28 and TIAM2 (By similarity). Interacts with HCV core CC protein. Interacts with ABL1 (phosphorylated form); the CC interaction retains it in the cytoplasm. Weakly interacts with CC CDKN1B. Interacts with GAB2. Interacts with phosphorylated GRB10. CC Interacts with PKA-phosphorylated AANAT. Interacts with the CC phosphorylated (by AKT1) form of SRPK2. CC -!- INTERACTION: CC O92972:- (xeno); NbExp=5; IntAct=EBI-356498, EBI-9213553; CC O14727:APAF1; NbExp=2; IntAct=EBI-356498, EBI-446492; CC O00257-3:CBX4; NbExp=2; IntAct=EBI-356498, EBI-4392727; CC O94921:CDK14; NbExp=3; IntAct=EBI-356498, EBI-1043945; CC Q9UKT5:FBXO4; NbExp=5; IntAct=EBI-356498, EBI-960409; CC P56524:HDAC4; NbExp=4; IntAct=EBI-356498, EBI-308629; CC Q14678-2:KANK1; NbExp=3; IntAct=EBI-356498, EBI-6173812; CC Q5S007:LRRK2; NbExp=4; IntAct=EBI-356498, EBI-5323863; CC Q99759:MAP3K3; NbExp=3; IntAct=EBI-356498, EBI-307281; CC O15151:MDM4; NbExp=3; IntAct=EBI-356498, EBI-398437; CC P58340:MLF1; NbExp=3; IntAct=EBI-356498, EBI-721328; CC O35244:Prdx6 (xeno); NbExp=2; IntAct=EBI-356498, EBI-915490; CC P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-356498, EBI-6930266; CC Q99469:STAC; NbExp=2; IntAct=EBI-356498, EBI-2652799; CC Q9GZV5:WWTR1; NbExp=3; IntAct=EBI-356498, EBI-747743; CC P31946:YWHAB; NbExp=3; IntAct=EBI-356498, EBI-359815; CC P61981:YWHAG; NbExp=4; IntAct=EBI-356498, EBI-359832; CC P63104:YWHAZ; NbExp=5; IntAct=EBI-356498, EBI-347088; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome. CC Note=Identified by mass spectrometry in melanosome fractions from CC stage I to stage IV. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P62258-1; Sequence=Displayed; CC Name=SV; CC IsoId=P62258-2; Sequence=VSP_040621; CC Note=Unable to dimerize with YWHAZ; CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U20972; AAC50175.1; -; mRNA. DR EMBL; U54778; AAC50710.1; -; mRNA. DR EMBL; U43399; AAC50625.1; -; mRNA. DR EMBL; U43430; AAD00026.1; -; mRNA. DR EMBL; U28936; AAA75301.1; -; mRNA. DR EMBL; AB017103; BAA32538.1; -; Genomic_DNA. DR EMBL; AY883089; AAX68683.1; -; mRNA. DR EMBL; AK128785; BAG54733.1; -; mRNA. DR EMBL; AK295260; BAG58249.1; -; mRNA. DR EMBL; AK316185; BAH14556.1; -; mRNA. DR EMBL; BT007161; AAP35825.1; -; mRNA. DR EMBL; CH471108; EAW90628.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90629.1; -; Genomic_DNA. DR EMBL; BC000179; AAH00179.1; -; mRNA. DR EMBL; BC001440; AAH01440.1; -; mRNA. DR CCDS; CCDS11001.1; -. [P62258-1] DR PIR; A61235; A61235. DR PIR; I38947; I38947. DR RefSeq; NP_006752.1; NM_006761.4. [P62258-1] DR UniGene; Hs.513851; -. DR PDB; 2BR9; X-ray; 1.75 A; A=1-233. DR PDB; 3UAL; X-ray; 1.80 A; A=1-232. DR PDB; 3UBW; X-ray; 1.90 A; A=1-234. DR PDBsum; 2BR9; -. DR PDBsum; 3UAL; -. DR PDBsum; 3UBW; -. DR ProteinModelPortal; P62258; -. DR SMR; P62258; 3-232. DR BioGrid; 113363; 316. DR DIP; DIP-36676N; -. DR IntAct; P62258; 147. DR MINT; MINT-4998623; -. DR STRING; 9606.ENSP00000264335; -. DR PhosphoSite; P62258; -. DR DMDM; 51702210; -. DR OGP; P42655; -. DR UCD-2DPAGE; P62258; -. DR MaxQB; P62258; -. DR PaxDb; P62258; -. DR PeptideAtlas; P62258; -. DR PRIDE; P62258; -. DR DNASU; 7531; -. DR Ensembl; ENST00000264335; ENSP00000264335; ENSG00000108953. [P62258-1] DR Ensembl; ENST00000571732; ENSP00000461762; ENSG00000108953. [P62258-2] DR GeneID; 7531; -. DR KEGG; hsa:7531; -. DR UCSC; uc002fsj.3; human. [P62258-1] DR CTD; 7531; -. DR GeneCards; GC17M001148; -. DR H-InvDB; HIX0013751; -. DR H-InvDB; HIX0030006; -. DR HGNC; HGNC:12851; YWHAE. DR HPA; CAB016200; -. DR HPA; CAB021109; -. DR HPA; CAB047350; -. DR HPA; HPA008445; -. DR MIM; 605066; gene. DR neXtProt; NX_P62258; -. DR Orphanet; 217385; 17p13.3 microduplication syndrome. DR Orphanet; 261257; Distal 17p13.3 microdeletion syndrome. DR Orphanet; 531; Miller-Dieker syndrome. DR PharmGKB; PA37440; -. DR eggNOG; COG5040; -. DR HOVERGEN; HBG050423; -. DR InParanoid; P62258; -. DR KO; K06630; -. DR OMA; MQESDKP; -. DR OrthoDB; EOG7HHWT3; -. DR PhylomeDB; P62258; -. DR TreeFam; TF102003; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_120956; Cellular responses to stress. DR Reactome; REACT_578; Apoptosis. DR SignaLink; P62258; -. DR ChiTaRS; YWHAE; human. DR EvolutionaryTrace; P62258; -. DR GeneWiki; YWHAE; -. DR GenomeRNAi; 7531; -. DR NextBio; 29461; -. DR PMAP-CutDB; P62258; -. DR PRO; PR:P62258; -. DR ArrayExpress; P62258; -. DR Bgee; P62258; -. DR CleanEx; HS_YWHAE; -. DR Genevestigator; P62258; -. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB. DR GO; GO:0005871; C:kinesin complex; IEA:Ensembl. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL. DR GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL. DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProt. DR GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL. DR GO; GO:0050815; F:phosphoserine binding; IPI:BHF-UCL. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0035329; P:hippo signaling; TAS:Reactome. DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IC:BHF-UCL. DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome. DR GO; GO:1902309; P:negative regulation of peptidyl-serine dephosphorylation; IDA:BHF-UCL. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IC:BHF-UCL. DR GO; GO:0003064; P:regulation of heart rate by hormone; NAS:BHF-UCL. DR GO; GO:0060306; P:regulation of membrane repolarization; IDA:BHF-UCL. DR GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL. DR GO; GO:0021762; P:substantia nigra development; IEP:UniProt. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 1.20.190.20; -; 1. DR InterPro; IPR000308; 14-3-3. DR InterPro; IPR023409; 14-3-3_CS. DR InterPro; IPR023410; 14-3-3_domain. DR PANTHER; PTHR18860; PTHR18860; 1. DR Pfam; PF00244; 14-3-3; 1. DR PIRSF; PIRSF000868; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR SUPFAM; SSF48445; SSF48445; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Cytoplasm; Direct protein sequencing; Host-virus interaction; KW Phosphoprotein; Reference proteome. FT CHAIN 1 255 14-3-3 protein epsilon. FT /FTId=PRO_0000058618. FT SITE 57 57 Interaction with phosphoserine on FT interacting protein. FT SITE 130 130 Interaction with phosphoserine on FT interacting protein. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 50 50 N6-acetyllysine. FT MOD_RES 69 69 N6-acetyllysine. FT MOD_RES 118 118 N6-acetyllysine. FT MOD_RES 123 123 N6-acetyllysine. FT MOD_RES 210 210 Phosphoserine. FT VAR_SEQ 1 22 Missing (in isoform SV). FT /FTId=VSP_040621. FT CONFLICT 106 107 KH -> NY (in Ref. 13; AA sequence). FT CONFLICT 143 143 E -> F (in Ref. 13; AA sequence). FT CONFLICT 148 148 S -> T (in Ref. 13; AA sequence). FT HELIX 4 17 FT HELIX 20 31 FT HELIX 39 73 FT HELIX 76 106 FT HELIX 108 111 FT HELIX 115 135 FT HELIX 138 162 FT HELIX 168 183 FT HELIX 188 204 FT HELIX 205 208 FT TURN 211 213 FT HELIX 214 231 SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64; MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ // ID 1433F_HUMAN Reviewed; 246 AA. AC Q04917; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 09-JUL-2014, entry version 161. DE RecName: Full=14-3-3 protein eta; DE AltName: Full=Protein AS1; GN Name=YWHAH; Synonyms=YWHA1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=8218406; DOI=10.1016/0167-4781(93)90053-G; RA Swanson K.D., Dhar M.S., Joshi J.G.; RT "The human and bovine 14-3-3 eta protein mRNAs are highly conserved in RT both their translated and untranslated regions."; RL Biochim. Biophys. Acta 1216:145-148(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Brain; RX PubMed=1578511; DOI=10.1002/jnr.490310403; RA Ichimura-Ohshima Y., Morii K., Ichimura T., Araki K., Takahashi Y., RA Isobe T., Minoshima S., Fukuyama R., Shimizu N., Kuwano R.; RT "cDNA cloning and chromosome assignment of the gene for human brain RT 14-3-3 protein eta chain."; RL J. Neurosci. Res. 31:600-605(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Leffers H., Tommerup N., Celis J.E.; RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8561965; DOI=10.1007/BF02740697; RA Muratake T., Hayashi S., Ichimura Y., Morii K., Kuwano R., RA Ichikawa T., Kumanishi T., Isobe T., Watanabe M., Kondo H.; RT "The effect on methamphetamine on the mRNA level for 14.3.3 eta chain RT in the human cultured cells."; RL Mol. Neurobiol. 11:223-230(1995). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8812417; DOI=10.1006/geno.1996.0426; RA Muratake T., Hayashi S., Ichikawa T., Kumanishi T., Ichimura Y., RA Kuwano R., Isobe T., Wang Y., Minoshima S., Shimizu N., Takahashi Y.; RT "Structural organization and chromosomal assignment of the human 14-3- RT 3 eta chain gene (YWHAH)."; RL Genomics 36:63-69(1996). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-225. RC TISSUE=Keratinocyte; RX PubMed=8515476; DOI=10.1006/jmbi.1993.1346; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [10] RP PROTEIN SEQUENCE OF 2-10. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [11] RP PROTEIN SEQUENCE OF 2-10; 29-50; 62-69; 126-132; 144-155; 163-172 AND RP 218-227, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLY-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V.; RL Submitted (AUG-2005) to UniProtKB. RN [12] RP INTERACTION WITH AR; ESR1; ESR2; MC2R; NRIP1; NR3C1; PPARBP AND THRA. RX PubMed=11266503; DOI=10.1210/me.15.4.501; RA Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., RA Gustafsson J.-A.; RT "Regulation of glucocorticoid receptor activity by 14-3-3-dependent RT intracellular relocalization of the corepressor RIP140."; RL Mol. Endocrinol. 15:501-511(2001). RN [13] RP FUNCTION, AND INTERACTION WITH PDPK1. RX PubMed=12177059; DOI=10.1074/jbc.M205141200; RA Sato S., Fujita N., Tsuruo T.; RT "Regulation of kinase activity of 3-phosphoinositide-dependent protein RT kinase-1 by binding to 14-3-3."; RL J. Biol. Chem. 277:39360-39367(2002). RN [14] RP INTERACTION WITH CDKN1B. RX PubMed=14504289; DOI=10.1074/jbc.M306614200; RA Fujita N., Sato S., Tsuruo T.; RT "Phosphorylation of p27Kip1 at threonine 198 by p90 ribosomal protein RT S6 kinases promotes its binding to 14-3-3 and cytoplasmic RT localization."; RL J. Biol. Chem. 278:49254-49260(2003). RN [15] RP INTERACTION WITH ABL1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15696159; DOI=10.1038/ncb1228; RA Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.; RT "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of RT c-Abl in the apoptotic response to DNA damage."; RL Nat. Cell Biol. 7:278-285(2005). RN [16] RP INTERACTION WITH GAB2. RX PubMed=19172738; DOI=10.1038/emboj.2008.159; RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., RA Guilhaus M., James D.E., Daly R.J.; RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by RT the Gab2 docking protein."; RL EMBO J. 27:2305-2316(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), IDENTIFICATION BY MASS RP SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT. RX PubMed=17085597; DOI=10.1073/pnas.0605779103; RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.; RT "Structural basis for protein-protein interactions in the 14-3-3 RT protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathways. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC Negatively regulates the kinase activity of PDPK1. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with many nuclear CC hormone receptors and cofactors including AR, ESR1, ESR2, MC2R, CC NR3C1, NRIP1, PPARBP and THRA. Interacts with ABL1 (phosphorylated CC form); the interaction retains it in the cytoplasm. Interacts with CC ARHGEF28 and CDK16 (By similarity). Weakly interacts with CDKN1B. CC Interacts with GAB2. Interacts with KCNK18 in a phosphorylation- CC dependent manner. Interacts with SAMSN1 (By similarity). Interacts CC with the 'Ser-241' phosphorylated form of PDPK1. CC -!- INTERACTION: CC Q96B36:AKT1S1; NbExp=3; IntAct=EBI-306940, EBI-720593; CC Q8N5S9:CAMKK1; NbExp=5; IntAct=EBI-306940, EBI-6424030; CC P30305:CDC25B; NbExp=3; IntAct=EBI-306940, EBI-1051746; CC O94921:CDK14; NbExp=3; IntAct=EBI-306940, EBI-1043945; CC P67828:CSNK1A1 (xeno); NbExp=8; IntAct=EBI-306940, EBI-7540603; CC O60565:GREM1; NbExp=5; IntAct=EBI-306940, EBI-944395; CC P56524:HDAC4; NbExp=3; IntAct=EBI-306940, EBI-308629; CC Q14678-2:KANK1; NbExp=3; IntAct=EBI-306940, EBI-6173812; CC Q5S007:LRRK2; NbExp=3; IntAct=EBI-306940, EBI-5323863; CC Q7KZI7:MARK2; NbExp=8; IntAct=EBI-306940, EBI-516560; CC P27448:MARK3; NbExp=4; IntAct=EBI-306940, EBI-707595; CC Q96L34:MARK4; NbExp=6; IntAct=EBI-306940, EBI-302319; CC Q8TEW0:PARD3; NbExp=6; IntAct=EBI-306940, EBI-81968; CC Q9NPB6:PARD6A; NbExp=2; IntAct=EBI-306940, EBI-81876; CC Q9BYG5:PARD6B; NbExp=2; IntAct=EBI-306940, EBI-295391; CC Q9BYG4:PARD6G; NbExp=2; IntAct=EBI-306940, EBI-295417; CC P41743:PRKCI; NbExp=3; IntAct=EBI-306940, EBI-286199; CC P04049:RAF1; NbExp=3; IntAct=EBI-306940, EBI-365996; CC P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-306940, EBI-6930266; CC -!- TISSUE SPECIFICITY: Expressed mainly in the brain and present in CC other tissues albeit at lower levels. CC -!- PTM: Phosphorylated on Ser-59 by protein kinase C delta type CC catalytic subunit in a sphingosine-dependent fashion (By CC similarity). CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L20422; AAA35483.1; -; mRNA. DR EMBL; X80536; CAA56676.1; -; Genomic_DNA. DR EMBL; X78138; CAA55017.1; -; mRNA. DR EMBL; X57345; CAA40620.1; -; mRNA. DR EMBL; D78577; BAA11418.1; -; Genomic_DNA. DR EMBL; S80794; AAB36036.1; -; mRNA. DR EMBL; CR456612; CAG30498.1; -; mRNA. DR EMBL; Z82248; CAB05112.1; -; Genomic_DNA. DR EMBL; BC003047; AAH03047.1; -; mRNA. DR CCDS; CCDS13901.1; -. DR PIR; S34756; S34756. DR PIR; S38509; S38509. DR PIR; S38532; S38532. DR RefSeq; NP_003396.1; NM_003405.3. DR UniGene; Hs.226755; -. DR PDB; 2C63; X-ray; 2.15 A; A/B/C/D=2-246. DR PDB; 2C74; X-ray; 2.70 A; A/B=2-246. DR PDBsum; 2C63; -. DR PDBsum; 2C74; -. DR ProteinModelPortal; Q04917; -. DR SMR; Q04917; 3-235. DR BioGrid; 113365; 121. DR DIP; DIP-27566N; -. DR IntAct; Q04917; 144. DR MINT; MINT-124456; -. DR STRING; 9606.ENSP00000248975; -. DR PhosphoSite; Q04917; -. DR DMDM; 1345593; -. DR MaxQB; Q04917; -. DR PaxDb; Q04917; -. DR PeptideAtlas; Q04917; -. DR PRIDE; Q04917; -. DR DNASU; 7533; -. DR Ensembl; ENST00000248975; ENSP00000248975; ENSG00000128245. DR GeneID; 7533; -. DR KEGG; hsa:7533; -. DR UCSC; uc003alz.3; human. DR CTD; 7533; -. DR GeneCards; GC22P032340; -. DR HGNC; HGNC:12853; YWHAH. DR HPA; CAB025918; -. DR MIM; 113508; gene. DR neXtProt; NX_Q04917; -. DR PharmGKB; PA37442; -. DR eggNOG; COG5040; -. DR HOGENOM; HOG000240379; -. DR HOVERGEN; HBG050423; -. DR InParanoid; Q04917; -. DR KO; K16198; -. DR OMA; ESSEAAY; -. DR OrthoDB; EOG7HHWT3; -. DR PhylomeDB; Q04917; -. DR TreeFam; TF102003; -. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_578; Apoptosis. DR SignaLink; Q04917; -. DR ChiTaRS; YWHAH; human. DR EvolutionaryTrace; Q04917; -. DR GeneWiki; YWHAH; -. DR GenomeRNAi; 7533; -. DR NextBio; 29471; -. DR PRO; PR:Q04917; -. DR ArrayExpress; Q04917; -. DR Bgee; Q04917; -. DR CleanEx; HS_YWHAH; -. DR Genevestigator; Q04917; -. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB. DR GO; GO:0014704; C:intercalated disc; IC:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. DR GO; GO:0035259; F:glucocorticoid receptor binding; IPI:UniProtKB. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB. DR GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL. DR GO; GO:0017080; F:sodium channel regulator activity; IDA:BHF-UCL. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0006713; P:glucocorticoid catabolic process; IDA:UniProtKB. DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0086010; P:membrane depolarization during action potential; IDA:BHF-UCL. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISS:UniProtKB. DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IDA:BHF-UCL. DR GO; GO:0002028; P:regulation of sodium ion transport; IDA:BHF-UCL. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB. DR GO; GO:0021762; P:substantia nigra development; IEP:UniProt. DR Gene3D; 1.20.190.20; -; 1. DR InterPro; IPR000308; 14-3-3. DR InterPro; IPR023409; 14-3-3_CS. DR InterPro; IPR023410; 14-3-3_domain. DR PANTHER; PTHR18860; PTHR18860; 1. DR Pfam; PF00244; 14-3-3; 1. DR PIRSF; PIRSF000868; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR SUPFAM; SSF48445; SSF48445; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; KW Direct protein sequencing; Phosphoprotein; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 246 14-3-3 protein eta. FT /FTId=PRO_0000058623. FT SITE 57 57 Interaction with phosphoserine on FT interacting protein. FT SITE 132 132 Interaction with phosphoserine on FT interacting protein. FT MOD_RES 2 2 N-acetylglycine. FT MOD_RES 25 25 Phosphoserine. FT MOD_RES 59 59 Phosphoserine (By similarity). FT CONFLICT 144 144 N -> T (in Ref. 9; CAA40620). FT CONFLICT 157 157 A -> G (in Ref. 1; AAA35483). FT CONFLICT 237 237 Q -> L (in Ref. 1; AAA35483). FT HELIX 4 16 FT HELIX 20 31 FT HELIX 39 73 FT HELIX 76 106 FT TURN 107 111 FT HELIX 117 137 FT HELIX 140 164 FT HELIX 170 185 FT HELIX 190 206 FT HELIX 207 210 FT TURN 213 215 FT HELIX 216 234 SQ SEQUENCE 246 AA; 28219 MW; D70FBC100C45D6E5 CRC64; MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LSLLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEQMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN // ID 1433G_HUMAN Reviewed; 247 AA. AC P61981; O70457; P35214; Q6FH52; Q9UDP2; Q9UN99; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-JUL-2014, entry version 122. DE RecName: Full=14-3-3 protein gamma; DE AltName: Full=Protein kinase C inhibitor protein 1; DE Short=KCIP-1; DE Contains: DE RecName: Full=14-3-3 protein gamma, N-terminally processed; GN Name=YWHAG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND INTERACTION WITH RP RAF1. RC TISSUE=Vascular smooth muscle; RX PubMed=10433554; DOI=10.1089/104454999315105; RA Autieri M.V., Carbone C.J.; RT "14-3-3gamma interacts with and is phosphorylated by multiple protein RT kinase C isoforms in PDGF-stimulated human vascular smooth muscle RT cells."; RL DNA Cell Biol. 18:555-564(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=10486217; DOI=10.1006/geno.1999.5887; RA Horie M., Suzuki M., Takahashi E., Tanigami A.; RT "Cloning, expression, and chromosomal mapping of the human 14-3-3gamma RT gene (YWHAG) to 7q11.23."; RL Genomics 60:241-243(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Endometrial tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 1-10; 13-56; 62-69; 133-172 AND 199-227, CLEAVAGE RP OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND VAL-2, RP PHOSPHORYLATION AT THR-145, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Colon carcinoma, and Hepatoma; RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Zebisch A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [7] RP PROTEIN SEQUENCE OF 2-12. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP PROTEIN SEQUENCE OF 2-10; 13-19; 29-42; 62-69; 133-143 AND 218-227, RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Platelet; RA Bienvenut W.V., Claeys D.; RL Submitted (NOV-2005) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 92-110; 199-217 AND 228-247, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP INTERACTION WITH AANAT. RX PubMed=11427721; DOI=10.1073/pnas.141118798; RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.; RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14- RT 3-3-binding switch in melatonin synthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001). RN [11] RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT VAL-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14534293; DOI=10.1074/jbc.M309039200; RA Towbin H., Bair K.W., DeCaprio J.A., Eck M.J., Kim S., Kinder F.R., RA Morollo A., Mueller D.R., Schindler P., Song H.K., van Oostrum J., RA Versace R.W., Voshol H., Wood J., Zabludoff S., Phillips P.E.; RT "Proteomics-based target identification: bengamides as a new class of RT methionine aminopeptidase inhibitors."; RL J. Biol. Chem. 278:52964-52971(2003). RN [12] RP INTERACTION WITH CRTC2. RX PubMed=15454081; DOI=10.1016/j.cell.2004.09.015; RA Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G., RA Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H., RA Okamoto M., Montminy M.; RT "The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive RT coincidence detector."; RL Cell 119:61-74(2004). RN [13] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). RN [14] RP INTERACTION WITH ABL1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15696159; DOI=10.1038/ncb1228; RA Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.; RT "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of RT c-Abl in the apoptotic response to DNA damage."; RL Nat. Cell Biol. 7:278-285(2005). RN [15] RP FUNCTION IN TP53 ACTIVATION, AND INTERACTION WITH MDM4. RX PubMed=16511572; DOI=10.1038/sj.emboj.7601010; RA Jin Y., Dai M.S., Lu S.Z., Xu Y., Luo Z., Zhao Y., Lu H.; RT "14-3-3gamma binds to MDMX that is phosphorylated by UV-activated RT Chk1, resulting in p53 activation."; RL EMBO J. 25:1207-1218(2006). RN [16] RP INTERACTION WITH GAB2. RX PubMed=19172738; DOI=10.1038/emboj.2008.159; RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., RA Guilhaus M., James D.E., Daly R.J.; RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by RT the Gab2 docking protein."; RL EMBO J. 27:2305-2316(2008). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS), IDENTIFICATION BY MASS RP SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT. RX PubMed=17085597; DOI=10.1073/pnas.0605779103; RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.; RT "Structural basis for protein-protein interactions in the 14-3-3 RT protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathways. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Homodimer. Interacts with SAMSN1 (By similarity). CC Interacts with RAF1, SSH1 and CRTC2/TORC2. Interacts with ABL1 CC (phosphorylated form); the interaction retains it in the CC cytoplasm. Interacts with GAB2. Interacts with MDM4 CC (phosphorylated); negatively regulates MDM4 activity toward TP53. CC Interacts with PKA-phosphorylated AANAT. CC -!- INTERACTION: CC O14757:CHEK1; NbExp=7; IntAct=EBI-359832, EBI-974488; CC P67828:CSNK1A1 (xeno); NbExp=3; IntAct=EBI-359832, EBI-7540603; CC P56524:HDAC4; NbExp=3; IntAct=EBI-359832, EBI-308629; CC Q14678-2:KANK1; NbExp=3; IntAct=EBI-359832, EBI-6173812; CC Q5S007:LRRK2; NbExp=3; IntAct=EBI-359832, EBI-5323863; CC Q7KZI7:MARK2; NbExp=2; IntAct=EBI-359832, EBI-516560; CC P27448:MARK3; NbExp=2; IntAct=EBI-359832, EBI-707595; CC O15151:MDM4; NbExp=7; IntAct=EBI-359832, EBI-398437; CC P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-359832, EBI-6930266; CC P04637:TP53; NbExp=5; IntAct=EBI-359832, EBI-366083; CC P62258:YWHAE; NbExp=4; IntAct=EBI-359832, EBI-356498; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in brain, skeletal muscle, CC and heart. CC -!- PTM: Phosphorylated by various PKC isozymes. CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF142498; AAD48408.1; -; mRNA. DR EMBL; AB024334; BAA85184.1; -; mRNA. DR EMBL; CR541904; CAG46702.1; -; mRNA. DR EMBL; CR541925; CAG46723.1; -; mRNA. DR EMBL; AC006388; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020963; AAH20963.1; -; mRNA. DR CCDS; CCDS5584.1; -. DR RefSeq; NP_036611.2; NM_012479.3. DR UniGene; Hs.744840; -. DR PDB; 2B05; X-ray; 2.55 A; A/B/C/D/E/F=2-247. DR PDB; 3UZD; X-ray; 1.86 A; A=1-247. DR PDB; 4E2E; X-ray; 2.25 A; A=1-247. DR PDB; 4J6S; X-ray; 3.08 A; A/B/C/D=1-247. DR PDB; 4O46; X-ray; 2.90 A; A/B/C/D/E/F=1-247. DR PDBsum; 2B05; -. DR PDBsum; 3UZD; -. DR PDBsum; 4E2E; -. DR PDBsum; 4J6S; -. DR PDBsum; 4O46; -. DR ProteinModelPortal; P61981; -. DR SMR; P61981; 1-235. DR BioGrid; 113364; 255. DR IntAct; P61981; 101. DR MINT; MINT-248956; -. DR STRING; 9606.ENSP00000306330; -. DR BindingDB; P61981; -. DR ChEMBL; CHEMBL1293296; -. DR PhosphoSite; P61981; -. DR DMDM; 48428721; -. DR REPRODUCTION-2DPAGE; IPI00220642; -. DR MaxQB; P61981; -. DR PaxDb; P61981; -. DR PeptideAtlas; P61981; -. DR PRIDE; P61981; -. DR DNASU; 7532; -. DR Ensembl; ENST00000307630; ENSP00000306330; ENSG00000170027. DR GeneID; 7532; -. DR KEGG; hsa:7532; -. DR UCSC; uc011kgj.1; human. DR CTD; 7532; -. DR GeneCards; GC07M075956; -. DR HGNC; HGNC:12852; YWHAG. DR HPA; CAB013274; -. DR HPA; CAB018389; -. DR HPA; HPA026918; -. DR MIM; 605356; gene. DR neXtProt; NX_P61981; -. DR PharmGKB; PA37441; -. DR eggNOG; COG5040; -. DR HOGENOM; HOG000240379; -. DR HOVERGEN; HBG050423; -. DR InParanoid; P61981; -. DR KO; K16198; -. DR OMA; CSETQHE; -. DR OrthoDB; EOG7HHWT3; -. DR PhylomeDB; P61981; -. DR TreeFam; TF102003; -. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_578; Apoptosis. DR SignaLink; P61981; -. DR ChiTaRS; YWHAG; human. DR EvolutionaryTrace; P61981; -. DR GeneWiki; YWHAG; -. DR GenomeRNAi; 7532; -. DR NextBio; 29467; -. DR PRO; PR:P61981; -. DR ArrayExpress; P61981; -. DR Bgee; P61981; -. DR CleanEx; HS_YWHAG; -. DR Genevestigator; P61981; -. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB. DR GO; GO:0008426; F:protein kinase C inhibitor activity; NAS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome. DR GO; GO:0006469; P:negative regulation of protein kinase activity; NAS:UniProtKB. DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; NAS:GOC. DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:UniProtKB. DR GO; GO:0009966; P:regulation of signal transduction; NAS:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB. DR Gene3D; 1.20.190.20; -; 1. DR InterPro; IPR000308; 14-3-3. DR InterPro; IPR023409; 14-3-3_CS. DR InterPro; IPR023410; 14-3-3_domain. DR PANTHER; PTHR18860; PTHR18860; 1. DR Pfam; PF00244; 14-3-3; 1. DR PIRSF; PIRSF000868; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR SUPFAM; SSF48445; SSF48445; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Phosphoprotein; Reference proteome. FT CHAIN 1 247 14-3-3 protein gamma. FT /FTId=PRO_0000367907. FT INIT_MET 1 1 Removed; alternate. FT CHAIN 2 247 14-3-3 protein gamma, N-terminally FT processed. FT /FTId=PRO_0000058606. FT SITE 57 57 Interaction with phosphoserine on FT interacting protein. FT SITE 132 132 Interaction with phosphoserine on FT interacting protein. FT MOD_RES 1 1 N-acetylmethionine; in 14-3-3 protein FT gamma; alternate; partial. FT MOD_RES 2 2 N-acetylvaline; in 14-3-3 protein gamma, FT N-terminally processed; partial. FT MOD_RES 2 2 N-acetylvaline; partial. FT MOD_RES 145 145 Phosphothreonine. FT CONFLICT 4 4 R -> P (in Ref. 1; AAD48408). FT CONFLICT 19 19 R -> G (in Ref. 1; AAD48408). FT CONFLICT 78 78 Missing (in Ref. 1; AAD48408). FT CONFLICT 89 89 I -> V (in Ref. 1; AAD48408). FT CONFLICT 104 104 L -> V (in Ref. 1; AAD48408). FT CONFLICT 109 109 I -> Y (in Ref. 1; AAD48408). FT CONFLICT 119 122 SKVF -> RKDL (in Ref. 1; AAD48408). FT CONFLICT 144 145 AT -> GD (in Ref. 1; AAD48408). FT CONFLICT 157 158 AH -> R (in Ref. 1; AAD48408). FT CONFLICT 200 202 AFD -> EFE (in Ref. 1; AAD48408). FT CONFLICT 214 214 D -> E (in Ref. 1; AAD48408). FT CONFLICT 240 240 D -> DH (in Ref. 1; AAD48408). FT HELIX 4 16 FT HELIX 20 31 FT HELIX 39 70 FT HELIX 79 106 FT HELIX 108 111 FT HELIX 117 137 FT HELIX 140 164 FT HELIX 170 185 FT HELIX 190 206 FT HELIX 207 210 FT TURN 213 215 FT HELIX 216 233 SQ SEQUENCE 247 AA; 28303 MW; B0D16C6DE1F4455D CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN // ID 1433S_HUMAN Reviewed; 248 AA. AC P31947; Q6FH30; Q6FH51; Q96DH0; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 09-JUL-2014, entry version 153. DE RecName: Full=14-3-3 protein sigma; DE AltName: Full=Epithelial cell marker protein 1; DE AltName: Full=Stratifin; GN Name=SFN; Synonyms=HME1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Epithelium; RX PubMed=1390337; RA Prasad G.L., Valverius E.M., McDuffie E., Cooper H.L.; RT "Complementary DNA cloning of a novel epithelial cell marker protein, RT HME1, that may be down-regulated in neoplastic mammary cells."; RL Cell Growth Differ. 3:507-513(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 19-25; RP 42-49; 118-122; 130-139; 149-159; 161-181; 196-199; 225-229 AND RP 231-239. RC TISSUE=Keratinocyte; RX PubMed=8515476; DOI=10.1006/jmbi.1993.1346; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RX PubMed=9659898; DOI=10.1016/S1097-2765(00)80002-7; RA Hermeking H., Lengauer C., Polyak K., He T.-C., Zhang L., RA Thiagalingam S., Kinzler K.W., Vogelstein B.; RT "14-3-3 sigma is a p53-regulated inhibitor of G2/M progression."; RL Mol. Cell 1:3-11(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cervix, Lung, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 42-49 AND 118-122. RC TISSUE=Keratinocyte; RX PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [8] RP IDENTIFICATION IN A COMPLEX WITH XPO7; ARHGAP1; EIF4A1; VPS26A; VPS29 RP AND VPS35. RX PubMed=15282546; DOI=10.1038/sj.emboj.7600338; RA Mingot J.-M., Bohnsack M.T., Jaekle U., Goerlich D.; RT "Exportin 7 defines a novel general nuclear export pathway."; RL EMBO J. 23:3227-3236(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP FUNCTION IN MDM2 UBIQUITINATION, AND UBIQUITINATION BY RFFL. RX PubMed=18382127; RA Yang W., Dicker D.T., Chen J., El-Deiry W.S.; RT "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing RT MDM2."; RL Cell Cycle 7:670-682(2008). RN [11] RP INTERACTION WITH GAB2. RX PubMed=19172738; DOI=10.1038/emboj.2008.159; RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., RA Guilhaus M., James D.E., Daly R.J.; RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by RT the Gab2 docking protein."; RL EMBO J. 27:2305-2316(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP INTERACTION WITH SRPK2. RX PubMed=19592491; DOI=10.1074/jbc.M109.026237; RA Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.; RT "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell RT cycle and cell death in neurons."; RL J. Biol. Chem. 284:24512-24525(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-248, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP INTERACTION WITH COPS6 AND RFWD2. RX PubMed=21625211; DOI=10.1038/onc.2011.192; RA Choi H.H., Gully C., Su C.H., Velazquez-Torres G., Chou P.C., RA Tseng C., Zhao R., Phan L., Shaiken T., Chen J., Yeung S.C., Lee M.H.; RT "COP9 signalosome subunit 6 stabilizes COP1, which functions as an E3 RT ubiquitin ligase for 14-3-3sigma."; RL Oncogene 30:4791-4801(2011). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PHOSPHOSERINE RP PEPTIDE. RX PubMed=15731107; DOI=10.1074/jbc.M500982200; RA Wilker E.W., Grant R.A., Artim S.C., Yaffe M.B.; RT "A structural basis for 14-3-3sigma functional specificity."; RL J. Biol. Chem. 280:18891-18898(2005). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-231 IN COMPLEX WITH PADI6 RP PHOSPHOPEPTIDES. RX PubMed=22634725; DOI=10.1016/j.jsb.2012.05.010; RA Rose R., Rose M., Ottmann C.; RT "Identification and structural characterization of two 14-3-3 binding RT sites in the human peptidylarginine deiminase type VI."; RL J. Struct. Biol. 180:65-72(2012). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathways. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. When CC bound to KRT17, regulates protein synthesis and epithelial cell CC growth by stimulating Akt/mTOR pathway. May also regulate MDM2 CC autoubiquitination and degradation and thereby activate p53/TP53. CC -!- FUNCTION: p53-regulated inhibitor of G2/M progression. CC -!- SUBUNIT: Homodimer. Interacts with KRT17 and SAMSN1 (By CC similarity). Found in a complex with XPO7, EIF4A1, ARHGAP1, CC VPS26A, VPS29, VPS35 and SFN. Interacts with GAB2. Interacts with CC SRPK2. Interacts with COPS6. Interacts with RFWD2; this CC interaction leads to proteasomal degradation. CC -!- INTERACTION: CC P00519:ABL1; NbExp=2; IntAct=EBI-476295, EBI-375543; CC Q96IF1:AJUBA; NbExp=2; IntAct=EBI-476295, EBI-949782; CC Q92934:BAD; NbExp=4; IntAct=EBI-476295, EBI-700771; CC Q7L5N1:COPS6; NbExp=7; IntAct=EBI-476295, EBI-486838; CC Q9UJM3:ERRFI1; NbExp=3; IntAct=EBI-476295, EBI-2941912; CC O60269:GPRIN2; NbExp=2; IntAct=EBI-476295, EBI-740397; CC P56524:HDAC4; NbExp=4; IntAct=EBI-476295, EBI-308629; CC Q9UQL6:HDAC5; NbExp=3; IntAct=EBI-476295, EBI-715576; CC Q8WUI4:HDAC7; NbExp=3; IntAct=EBI-476295, EBI-1048378; CC Q14103-4:HNRNPD; NbExp=7; IntAct=EBI-476295, EBI-432545; CC P27448:MARK3; NbExp=2; IntAct=EBI-476295, EBI-707595; CC O00444:PLK4; NbExp=2; IntAct=EBI-476295, EBI-746202; CC P04049:RAF1; NbExp=2; IntAct=EBI-476295, EBI-365996; CC Q8NFH8-2:REPS2; NbExp=2; IntAct=EBI-476295, EBI-8029141; CC Q8NHY2:RFWD2; NbExp=6; IntAct=EBI-476295, EBI-1176214; CC P04637:TP53; NbExp=4; IntAct=EBI-476295, EBI-366083; CC P63104:YWHAZ; NbExp=2; IntAct=EBI-476295, EBI-347088; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity). CC Secreted. Note=May be secreted by a non-classical secretory CC pathway. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P31947-1; Sequence=Displayed; CC Name=2; CC IsoId=P31947-2; Sequence=VSP_021768; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Present mainly in tissues enriched in CC stratified squamous keratinizing epithelium. CC -!- PTM: Ubiquitinated. Ubiquitination by RFFL induces proteasomal CC degradation and indirectly regulates p53/TP53 activation. CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M93010; AAA59546.1; -; mRNA. DR EMBL; X57348; CAA40623.1; -; mRNA. DR EMBL; AF029081; AAC52029.1; -; Genomic_DNA. DR EMBL; AF029082; AAC52030.1; -; mRNA. DR EMBL; CR541905; CAG46703.1; -; mRNA. DR EMBL; CR541926; CAG46724.1; -; mRNA. DR EMBL; AL034380; CAB92118.1; -; Genomic_DNA. DR EMBL; BC000329; AAH00329.1; -; mRNA. DR EMBL; BC000995; AAH00995.1; -; mRNA. DR EMBL; BC001550; AAH01550.1; -; mRNA. DR EMBL; BC002995; AAH02995.1; -; mRNA. DR EMBL; BC023552; AAH23552.1; -; mRNA. DR CCDS; CCDS288.1; -. [P31947-1] DR PIR; S34753; S34753. DR PIR; S38956; S38956. DR RefSeq; NP_006133.1; NM_006142.3. [P31947-1] DR UniGene; Hs.523718; -. DR PDB; 1YWT; X-ray; 2.40 A; A/B=1-248. DR PDB; 1YZ5; X-ray; 2.80 A; A/B=1-248. DR PDB; 3IQJ; X-ray; 1.15 A; A=1-231. DR PDB; 3IQU; X-ray; 1.05 A; A=1-231. DR PDB; 3IQV; X-ray; 1.20 A; A=1-231. DR PDB; 3LW1; X-ray; 1.28 A; A=1-248. DR PDB; 3MHR; X-ray; 1.15 A; A=1-231. DR PDB; 3O8I; X-ray; 2.00 A; A=1-231. DR PDB; 3P1N; X-ray; 1.40 A; A=1-231. DR PDB; 3P1O; X-ray; 1.90 A; A=1-231. DR PDB; 3P1P; X-ray; 1.95 A; A=1-231. DR PDB; 3P1Q; X-ray; 1.70 A; A=1-231. DR PDB; 3P1R; X-ray; 1.70 A; A=1-231. DR PDB; 3P1S; X-ray; 1.65 A; A=1-231. DR PDB; 3SMK; X-ray; 2.10 A; A=1-231. DR PDB; 3SML; X-ray; 1.90 A; A=1-231. DR PDB; 3SMM; X-ray; 2.00 A; A=1-231. DR PDB; 3SMN; X-ray; 2.00 A; A=1-231. DR PDB; 3SMO; X-ray; 1.80 A; A=1-231. DR PDB; 3SPR; X-ray; 1.99 A; A=1-231. DR PDB; 3T0L; X-ray; 1.60 A; A=1-231. DR PDB; 3T0M; X-ray; 1.62 A; A=1-231. DR PDB; 3U9X; X-ray; 1.80 A; A=1-231. DR PDB; 3UX0; X-ray; 1.75 A; A=1-231. DR PDB; 4DAT; X-ray; 1.40 A; A=1-231. DR PDB; 4DAU; X-ray; 2.00 A; A=1-231. DR PDB; 4DHM; X-ray; 1.70 A; A=1-231. DR PDB; 4DHN; X-ray; 1.80 A; A=1-231. DR PDB; 4DHO; X-ray; 1.70 A; A=1-231. DR PDB; 4DHP; X-ray; 1.75 A; A=1-231. DR PDB; 4DHQ; X-ray; 1.75 A; A=1-231. DR PDB; 4DHR; X-ray; 1.40 A; A=1-231. DR PDB; 4DHS; X-ray; 1.74 A; A=1-231. DR PDB; 4DHT; X-ray; 1.80 A; A=1-231. DR PDB; 4DHU; X-ray; 1.67 A; A=1-231. DR PDB; 4FL5; X-ray; 1.90 A; A/B=1-231. DR PDB; 4FR3; X-ray; 1.90 A; A=1-231. DR PDB; 4HQW; X-ray; 2.35 A; A=1-231. DR PDB; 4HRU; X-ray; 3.15 A; A=1-231. DR PDB; 4IEA; X-ray; 1.70 A; A=1-231. DR PDB; 4JC3; X-ray; 2.05 A; A=1-231. DR PDB; 4JDD; X-ray; 2.10 A; A=1-231. DR PDBsum; 1YWT; -. DR PDBsum; 1YZ5; -. DR PDBsum; 3IQJ; -. DR PDBsum; 3IQU; -. DR PDBsum; 3IQV; -. DR PDBsum; 3LW1; -. DR PDBsum; 3MHR; -. DR PDBsum; 3O8I; -. DR PDBsum; 3P1N; -. DR PDBsum; 3P1O; -. DR PDBsum; 3P1P; -. DR PDBsum; 3P1Q; -. DR PDBsum; 3P1R; -. DR PDBsum; 3P1S; -. DR PDBsum; 3SMK; -. DR PDBsum; 3SML; -. DR PDBsum; 3SMM; -. DR PDBsum; 3SMN; -. DR PDBsum; 3SMO; -. DR PDBsum; 3SPR; -. DR PDBsum; 3T0L; -. DR PDBsum; 3T0M; -. DR PDBsum; 3U9X; -. DR PDBsum; 3UX0; -. DR PDBsum; 4DAT; -. DR PDBsum; 4DAU; -. DR PDBsum; 4DHM; -. DR PDBsum; 4DHN; -. DR PDBsum; 4DHO; -. DR PDBsum; 4DHP; -. DR PDBsum; 4DHQ; -. DR PDBsum; 4DHR; -. DR PDBsum; 4DHS; -. DR PDBsum; 4DHT; -. DR PDBsum; 4DHU; -. DR PDBsum; 4FL5; -. DR PDBsum; 4FR3; -. DR PDBsum; 4HQW; -. DR PDBsum; 4HRU; -. DR PDBsum; 4IEA; -. DR PDBsum; 4JC3; -. DR PDBsum; 4JDD; -. DR ProteinModelPortal; P31947; -. DR SMR; P31947; 1-231. DR BioGrid; 109072; 138. DR DIP; DIP-29861N; -. DR IntAct; P31947; 149. DR MINT; MINT-108060; -. DR STRING; 9606.ENSP00000340989; -. DR BindingDB; P31947; -. DR ChEMBL; CHEMBL1909482; -. DR PhosphoSite; P31947; -. DR DMDM; 398953; -. DR OGP; P31947; -. DR SWISS-2DPAGE; P31947; -. DR MaxQB; P31947; -. DR PaxDb; P31947; -. DR PeptideAtlas; P31947; -. DR PRIDE; P31947; -. DR DNASU; 2810; -. DR Ensembl; ENST00000339276; ENSP00000340989; ENSG00000175793. [P31947-1] DR GeneID; 2810; -. DR KEGG; hsa:2810; -. DR UCSC; uc001bnc.1; human. [P31947-1] DR CTD; 2810; -. DR GeneCards; GC01P027189; -. DR HGNC; HGNC:10773; SFN. DR HPA; CAB006268; -. DR HPA; CAB040552; -. DR HPA; HPA011105; -. DR MIM; 601290; gene. DR neXtProt; NX_P31947; -. DR PharmGKB; PA177; -. DR eggNOG; COG5040; -. DR HOGENOM; HOG000240379; -. DR HOVERGEN; HBG050423; -. DR InParanoid; P31947; -. DR KO; K06644; -. DR OMA; EQKGNEE; -. DR OrthoDB; EOG7HHWT3; -. DR PhylomeDB; P31947; -. DR TreeFam; TF102003; -. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_578; Apoptosis. DR SignaLink; P31947; -. DR EvolutionaryTrace; P31947; -. DR GeneWiki; Stratifin; -. DR GenomeRNAi; 2810; -. DR NextBio; 11071; -. DR PRO; PR:P31947; -. DR Bgee; P31947; -. DR CleanEx; HS_SFN; -. DR Genevestigator; P31947; -. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008426; F:protein kinase C inhibitor activity; TAS:ProtInc. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:HGNC. DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl. DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:HGNC. DR GO; GO:0006469; P:negative regulation of protein kinase activity; TAS:ProtInc. DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; TAS:GOC. DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl. DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; ISS:UniProtKB. DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl. DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl. DR GO; GO:0010482; P:regulation of epidermal cell division; ISS:UniProtKB. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IDA:HGNC. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR Gene3D; 1.20.190.20; -; 1. DR InterPro; IPR000308; 14-3-3. DR InterPro; IPR023409; 14-3-3_CS. DR InterPro; IPR023410; 14-3-3_domain. DR PANTHER; PTHR18860; PTHR18860; 1. DR Pfam; PF00244; 14-3-3; 1. DR PIRSF; PIRSF000868; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR SUPFAM; SSF48445; SSF48445; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Secreted; Ubl conjugation. FT CHAIN 1 248 14-3-3 protein sigma. FT /FTId=PRO_0000058643. FT SITE 56 56 Interaction with phosphoserine on FT interacting protein. FT SITE 129 129 Interaction with phosphoserine on FT interacting protein. FT MOD_RES 5 5 Phosphoserine. FT MOD_RES 248 248 Phosphoserine. FT VAR_SEQ 85 116 Missing (in isoform 2). FT /FTId=VSP_021768. FT VARIANT 155 155 M -> I (in dbSNP:rs11542705). FT /FTId=VAR_048095. FT CONFLICT 77 77 K -> M (in Ref. 4; CAG46703). FT CONFLICT 120 120 Y -> H (in Ref. 2; AAA59546). FT CONFLICT 242 242 A -> V (in Ref. 2; AAA59546). FT HELIX 3 15 FT HELIX 19 31 FT HELIX 38 69 FT HELIX 80 104 FT HELIX 107 110 FT HELIX 114 134 FT STRAND 137 139 FT HELIX 140 161 FT HELIX 167 182 FT HELIX 187 204 FT HELIX 205 207 FT HELIX 210 230 SQ SEQUENCE 248 AA; 27774 MW; 7F4B44E3AA59ECE6 CRC64; MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS // ID 1433T_HUMAN Reviewed; 245 AA. AC P27348; D6W4Z5; Q567U5; Q5TZU8; Q9UP48; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 09-JUL-2014, entry version 158. DE RecName: Full=14-3-3 protein theta; DE AltName: Full=14-3-3 protein T-cell; DE AltName: Full=14-3-3 protein tau; DE AltName: Full=Protein HS1; GN Name=YWHAQ; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=T-cell; RX PubMed=2015305; DOI=10.1016/0167-4781(91)90136-A; RA Nielsen P.J.; RT "Primary structure of a human protein kinase regulator protein."; RL Biochim. Biophys. Acta 1088:425-428(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Keratinocyte; RX PubMed=8515476; DOI=10.1006/jmbi.1993.1346; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta, Skin, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 1-18. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP PROTEIN SEQUENCE OF 1-9; 28-49; 61-68; 104-115; 139-167 AND 213-222, RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma, and Hepatoma; RA Bienvenut W.V., Dhillon A.S., Kolch W.; RL Submitted (FEB-2008) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-245. RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP PHOSPHORYLATION AT SER-232, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=9360956; DOI=10.1074/jbc.272.46.28882; RA Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., RA Morrice N., Moelling K., Aitken A.; RT "14-3-3 is phosphorylated by casein kinase I on residue 233. RT Phosphorylation at this site in vivo regulates Raf/14-3-3 RT interaction."; RL J. Biol. Chem. 272:28882-28888(1997). RN [10] RP TISSUE SPECIFICITY. RX PubMed=11080204; DOI=10.1046/j.1471-4159.2000.0752511.x; RA Malaspina A., Kaushik N., de Belleroche J.; RT "A 14-3-3 mRNA is up-regulated in amyotrophic lateral sclerosis spinal RT cord."; RL J. Neurochem. 75:2511-2520(2000). RN [11] RP INTERACTION WITH CDKN1B. RX PubMed=12042314; DOI=10.1074/jbc.M203668200; RA Fujita N., Sato S., Katayama K., Tsuruo T.; RT "Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 RT and cytoplasmic localization."; RL J. Biol. Chem. 277:28706-28713(2002). RN [12] RP FUNCTION, AND INTERACTION WITH PDPK1. RX PubMed=12177059; DOI=10.1074/jbc.M205141200; RA Sato S., Fujita N., Tsuruo T.; RT "Regulation of kinase activity of 3-phosphoinositide-dependent protein RT kinase-1 by binding to 14-3-3."; RL J. Biol. Chem. 277:39360-39367(2002). RN [13] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [15] RP INTERACTION WITH GAB2. RX PubMed=19172738; DOI=10.1038/emboj.2008.159; RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., RA Guilhaus M., James D.E., Daly R.J.; RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by RT the Gab2 docking protein."; RL EMBO J. 27:2305-2316(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3; LYS-49; LYS-68 AND RP LYS-115, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=7603573; DOI=10.1038/376188a0; RA Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., Aitken A., RA Gamblin S.J.; RT "Structure of a 14-3-3 protein and implications for coordination of RT multiple signalling pathways."; RL Nature 376:188-191(1995). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234, IDENTIFICATION BY MASS RP SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT. RX PubMed=17085597; DOI=10.1073/pnas.0605779103; RA Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., RA Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.; RT "Structural basis for protein-protein interactions in the 14-3-3 RT protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathways. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC Negatively regulates the kinase activity of PDPK1. CC -!- SUBUNIT: Homodimer. Interacts with CDK16 (By similarity). CC Interacts with SSH1. Interacts with CDKN1B ('Thr-198' CC phosphorylated form); the interaction translocates CDKN1B to the CC cytoplasm. Interacts with GAB2. Interacts with the 'Ser-241' CC phosphorylated form of PDPK1. CC -!- INTERACTION: CC Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359854, EBI-1567267; CC P49407:ARRB1; NbExp=3; IntAct=EBI-359854, EBI-743313; CC P32121:ARRB2; NbExp=3; IntAct=EBI-359854, EBI-714559; CC P22681:CBL; NbExp=6; IntAct=EBI-359854, EBI-518228; CC O94921:CDK14; NbExp=3; IntAct=EBI-359854, EBI-1043945; CC P46527:CDKN1B; NbExp=4; IntAct=EBI-359854, EBI-519280; CC P67828:CSNK1A1 (xeno); NbExp=2; IntAct=EBI-359854, EBI-7540603; CC P00533:EGFR; NbExp=5; IntAct=EBI-359854, EBI-297353; CC P23945:FSHR; NbExp=4; IntAct=EBI-359854, EBI-848239; CC Q14678:KANK1; NbExp=2; IntAct=EBI-359854, EBI-2556221; CC Q14678-2:KANK1; NbExp=3; IntAct=EBI-359854, EBI-6173812; CC Q5S007:LRRK2; NbExp=7; IntAct=EBI-359854, EBI-5323863; CC P61588:Rnd3 (xeno); NbExp=2; IntAct=EBI-359854, EBI-6930266; CC Q8WYL5:SSH1; NbExp=2; IntAct=EBI-359854, EBI-1222387; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In neurons, axonally CC transported to the nerve terminals. CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain, heart and CC pancreas, and at lower levels in kidney and placenta. Up-regulated CC in the lumbar spinal cord from patients with sporadic amyotrophic CC lateral sclerosis (ALS) compared with controls, with highest CC levels of expression in individuals with predominant lower motor CC neuron involvement. CC -!- PTM: Ser-232 is probably phosphorylated by CK1. CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X56468; CAA39840.1; -; mRNA. DR EMBL; X57347; CAA40622.1; -; mRNA. DR EMBL; BT020014; AAV38817.1; -; mRNA. DR EMBL; CH471053; EAX00977.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00979.1; -; Genomic_DNA. DR EMBL; BC050601; AAH50601.1; -; mRNA. DR EMBL; BC056867; AAH56867.1; -; mRNA. DR EMBL; BC093019; AAH93019.1; -; mRNA. DR EMBL; AF070556; AAC28640.1; -; mRNA. DR CCDS; CCDS1666.1; -. DR PIR; S15076; S15076. DR RefSeq; NP_006817.1; NM_006826.3. DR UniGene; Hs.74405; -. DR PDB; 2BTP; X-ray; 2.80 A; A/B=1-234. DR PDBsum; 2BTP; -. DR ProteinModelPortal; P27348; -. DR SMR; P27348; 1-230. DR BioGrid; 116168; 380. DR DIP; DIP-27584N; -. DR IntAct; P27348; 80. DR MINT; MINT-121282; -. DR STRING; 9606.ENSP00000238081; -. DR PhosphoSite; P27348; -. DR DMDM; 112690; -. DR OGP; P27348; -. DR REPRODUCTION-2DPAGE; IPI00018146; -. DR MaxQB; P27348; -. DR PaxDb; P27348; -. DR PeptideAtlas; P27348; -. DR PRIDE; P27348; -. DR DNASU; 10971; -. DR Ensembl; ENST00000238081; ENSP00000238081; ENSG00000134308. DR Ensembl; ENST00000381844; ENSP00000371267; ENSG00000134308. DR GeneID; 10971; -. DR KEGG; hsa:10971; -. DR UCSC; uc002qzx.3; human. DR CTD; 10971; -. DR GeneCards; GC02M009724; -. DR H-InvDB; HIX0077146; -. DR HGNC; HGNC:12854; YWHAQ. DR HPA; CAB010286; -. DR HPA; HPA007925; -. DR MIM; 609009; gene. DR neXtProt; NX_P27348; -. DR PharmGKB; PA37443; -. DR eggNOG; COG5040; -. DR HOGENOM; HOG000240379; -. DR HOVERGEN; HBG050423; -. DR InParanoid; P27348; -. DR KO; K16197; -. DR OMA; CELRSIC; -. DR OrthoDB; EOG7HHWT3; -. DR PhylomeDB; P27348; -. DR TreeFam; TF102002; -. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_578; Apoptosis. DR SignaLink; P27348; -. DR ChiTaRS; YWHAQ; human. DR EvolutionaryTrace; P27348; -. DR GeneWiki; YWHAQ; -. DR GenomeRNAi; 10971; -. DR NextBio; 41686; -. DR PMAP-CutDB; P27348; -. DR PRO; PR:P27348; -. DR ArrayExpress; P27348; -. DR Bgee; P27348; -. DR CleanEx; HS_YWHAQ; -. DR Genevestigator; P27348; -. DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL. DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0006605; P:protein targeting; IEA:Ensembl. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl. DR GO; GO:0021762; P:substantia nigra development; IEP:UniProt. DR Gene3D; 1.20.190.20; -; 1. DR InterPro; IPR000308; 14-3-3. DR InterPro; IPR023409; 14-3-3_CS. DR InterPro; IPR023410; 14-3-3_domain. DR PANTHER; PTHR18860; PTHR18860; 1. DR Pfam; PF00244; 14-3-3; 1. DR PIRSF; PIRSF000868; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR SUPFAM; SSF48445; SSF48445; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Phosphoprotein; Reference proteome. FT CHAIN 1 245 14-3-3 protein theta. FT /FTId=PRO_0000058636. FT SITE 56 56 Interaction with phosphoserine on FT interacting protein. FT SITE 127 127 Interaction with phosphoserine on FT interacting protein. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 3 3 N6-acetyllysine. FT MOD_RES 49 49 N6-acetyllysine. FT MOD_RES 68 68 N6-acetyllysine. FT MOD_RES 115 115 N6-acetyllysine. FT MOD_RES 232 232 Phosphoserine. FT CONFLICT 136 136 D -> N (in Ref. 3; AAV38817). FT HELIX 3 15 FT HELIX 19 31 FT HELIX 38 68 FT HELIX 75 103 FT TURN 104 108 FT HELIX 112 132 FT HELIX 135 159 FT HELIX 165 180 FT HELIX 185 201 FT TURN 202 205 FT HELIX 208 227 SQ SEQUENCE 245 AA; 27764 MW; 175534325E9E37C4 CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 1433Z_HUMAN Reviewed; 245 AA. AC P63104; A8K1N0; B7Z465; P29213; P29312; Q32P43; Q5XJ08; Q6GPI2; AC Q6IN74; Q6NUR9; Q6P3U9; Q86V33; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 09-JUL-2014, entry version 129. DE RecName: Full=14-3-3 protein zeta/delta; DE AltName: Full=Protein kinase C inhibitor protein 1; DE Short=KCIP-1; GN Name=YWHAZ; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=1577711; RA Zupan L.A., Steffens D.L., Berry C.A., Landt M.L., Gross R.W.; RT "Cloning and expression of a human 14-3-3 protein mediating RT phospholipolysis. Identification of an arachidonoyl-enzyme RT intermediate during catalysis."; RL J. Biol. Chem. 267:8707-8710(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=9512661; DOI=10.1016/S0167-4781(97)00171-1; RA Seluja G.A., Pietromonaco S.F., Elias L.; RT "Two unique 5' untranslated regions in mRNAs encoding human 14-3-3 RT zeta: differential expression in hemopoietic cells."; RL Biochim. Biophys. Acta 1395:281-287(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Hippocampus, and Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Colon, Eye, Melanoma, PNS, Skin, Testis, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 1-18. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP PROTEIN SEQUENCE OF 1-9; 12-18; 28-49; 61-68; 86-91; 128-158 AND RP 213-222, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma, and Platelet; RA Bienvenut W.V., Potts A., Barblan J., Claeys D., Quadroni M.; RL Submitted (NOV-2005) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 92-103; 140-157; 194-212 AND 223-245, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP PHOSPHORYLATION AT THR-232, INTERACTION WITH RAF1, AND FUNCTION. RX PubMed=9360956; DOI=10.1074/jbc.272.46.28882; RA Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y., RA Morrice N., Moelling K., Aitken A.; RT "14-3-3 is phosphorylated by casein kinase I on residue 233. RT Phosphorylation at this site in vivo regulates Raf/14-3-3 RT interaction."; RL J. Biol. Chem. 272:28882-28888(1997). RN [10] RP INTERACTION WITH TLK2. RX PubMed=10455159; DOI=10.1074/jbc.274.35.24865; RA Zhang S., Xing H., Muslin A.J.; RT "Nuclear localization of protein kinase U-alpha is regulated by 14-3- RT 3."; RL J. Biol. Chem. 274:24865-24872(1999). RN [11] RP INTERACTION WITH AANAT. RX PubMed=11427721; DOI=10.1073/pnas.141118798; RA Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H., RA Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T., RA Beauverger P., Ferry G., Boutin J.A., Klein D.C.; RT "Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14- RT 3-3-binding switch in melatonin synthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001). RN [12] RP PHOSPHORYLATION AT SER-58, AND INTERACTION WITH AKT1. RX PubMed=11956222; DOI=10.1074/jbc.M203167200; RA Powell D.W., Rane M.J., Chen Q., Singh S., McLeish K.R.; RT "Identification of 14-3-3zeta as a protein kinase B/Akt substrate."; RL J. Biol. Chem. 277:21639-21642(2002). RN [13] RP PHOSPHORYLATION AT SER-58, AND DIMERIZATION. RX PubMed=12865427; DOI=10.1074/jbc.M304689200; RA Woodcock J.M., Murphy J., Stomski F.C., Berndt M.C., Lopez A.F.; RT "The dimeric versus monomeric status of 14-3-3zeta is controlled by RT phosphorylation of Ser58 at the dimer interface."; RL J. Biol. Chem. 278:36323-36327(2003). RN [14] RP INTERACTION WITH AANAT, AND FUNCTION. RX PubMed=14578935; DOI=10.1038/nsb1005; RA Zheng W., Zhang Z., Ganguly S., Weller J.L., Klein D.C., Cole P.A.; RT "Cellular stabilization of the melatonin rhythm enzyme induced by RT nonhydrolyzable phosphonate incorporation."; RL Nat. Struct. Biol. 10:1054-1057(2003). RN [15] RP PHOSPHORYLATION AT SER-184, INTERACTION WITH BAX, FUNCTION, AND RP MUTAGENESIS OF SER-184. RX PubMed=15071501; DOI=10.1038/sj.emboj.7600194; RA Tsuruta F., Sunayama J., Mori Y., Hattori S., Shimizu S., RA Tsujimoto Y., Yoshioka K., Masuyama N., Gotoh Y.; RT "JNK promotes Bax translocation to mitochondria through RT phosphorylation of 14-3-3 proteins."; RL EMBO J. 23:1889-1899(2004). RN [16] RP INTERACTION WITH SSH1. RX PubMed=15159416; DOI=10.1083/jcb.200401136; RA Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M., RA Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.; RT "A pathway of neuregulin-induced activation of cofilin-phosphatase RT Slingshot and cofilin in lamellipodia."; RL J. Cell Biol. 165:465-471(2004). RN [17] RP INTERACTION WITH MLLT7. RX PubMed=16114898; DOI=10.1021/bi050618r; RA Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J., RA Boura E., Obsil T.; RT "14-3-3 protein interacts with nuclear localization sequence of RT forkhead transcription factor FoxO4."; RL Biochemistry 44:11608-11617(2005). RN [18] RP INTERACTION WITH SSH1. RX PubMed=15660133; DOI=10.1038/sj.emboj.7600543; RA Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N., RA Sarcevic B., Sampath R., Bamburg J.R., Bernard O.; RT "Interplay between components of a novel LIM kinase-slingshot RT phosphatase complex regulates cofilin."; RL EMBO J. 24:473-486(2005). RN [19] RP PHOSPHORYLATION AT SER-58, AND MUTAGENESIS OF SER-58. RX PubMed=15883165; DOI=10.1074/jbc.M409081200; RA Ma Y., Pitson S., Hercus T., Murphy J., Lopez A., Woodcock J.; RT "Sphingosine activates protein kinase A type II by a novel cAMP- RT independent mechanism."; RL J. Biol. Chem. 280:26011-26017(2005). RN [20] RP INTERACTION WITH ABL1, IDENTIFICATION BY MASS SPECTROMETRY, RP PHOSPHORYLATION AT SER-184, AND MUTAGENESIS OF SER-184. RX PubMed=15696159; DOI=10.1038/ncb1228; RA Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.; RT "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of RT c-Abl in the apoptotic response to DNA damage."; RL Nat. Cell Biol. 7:278-285(2005). RN [21] RP INTERACTION WITH AANAT, AND FUNCTION. RX PubMed=15644438; DOI=10.1073/pnas.0406871102; RA Ganguly S., Weller J.L., Ho A., Chemineau P., Malpaux B., Klein D.C.; RT "Melatonin synthesis: 14-3-3-dependent activation and inhibition of RT arylalkylamine N-acetyltransferase mediated by phosphoserine-205."; RL Proc. Natl. Acad. Sci. U.S.A. 102:1222-1227(2005). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [23] RP PHOSPHORYLATION AT SER-58, DIMERIZATION, INTERACTION WITH TP53 AND RP YWHAE, FUNCTION, AND MUTAGENESIS OF SER-58. RX PubMed=16376338; DOI=10.1016/j.febslet.2005.12.024; RA Gu Y.-M., Jin Y.-H., Choi J.-K., Baek K.-H., Yeo C.-Y., Lee K.-Y.; RT "Protein kinase A phosphorylates and regulates dimerization of 14-3-3 RT epsilon."; RL FEBS Lett. 580:305-310(2006). RN [24] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [25] RP INTERACTION WITH NOXA1, AND MUTAGENESIS OF LYS-49. RX PubMed=17913709; DOI=10.1074/jbc.M704754200; RA Kim J.-S., Diebold B.A., Babior B.M., Knaus U.G., Bokoch G.M.; RT "Regulation of Nox1 activity via PKA-mediated phosphorylation of NoxA1 RT and 14-3-3 binding."; RL J. Biol. Chem. 282:34787-34800(2007). RN [26] RP INTERACTION WITH ARHGEF2. RX PubMed=14970201; DOI=10.1074/jbc.M400084200; RA Zenke F.T., Krendel M., DerMardirossian C., King C.C., Bohl B.P., RA Bokoch G.M.; RT "p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding to RT GEF-H1, a microtubule-localized Rho exchange factor."; RL J. Biol. Chem. 279:18392-18400(2004). RN [27] RP INTERACTION WITH GAB2. RX PubMed=19172738; DOI=10.1038/emboj.2008.159; RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., RA Guilhaus M., James D.E., Daly R.J.; RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by RT the Gab2 docking protein."; RL EMBO J. 27:2305-2316(2008). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [31] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-3 AND LYS-68, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND THR-232, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [36] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=10488331; DOI=10.1016/S1097-2765(00)80363-9; RA Rittinger K., Budman J., Xu J., Volinia S., Cantley L.C., RA Smerdon S.J., Gamblin S.J., Yaffe M.B.; RT "Structural analysis of 14-3-3 phosphopeptide complexes identifies a RT dual role for the nuclear export signal of 14-3-3 in ligand binding."; RL Mol. Cell 4:153-166(1999). RN [38] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH AANAT. RX PubMed=11336675; DOI=10.1016/S0092-8674(01)00316-6; RA Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F.; RT "Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase RT complex. a role for scaffolding in enzyme regulation."; RL Cell 105:257-267(2001). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HISTONE H3 RP PHOSPHOPEPTIDE. RX PubMed=16246723; DOI=10.1016/j.molcel.2005.08.032; RA Macdonald N., Welburn J.P.I., Noble M.E.M., Nguyen A., Yaffe M.B., RA Clynes D., Moggs J.G., Orphanides G., Thomson S., Edmunds J.W., RA Clayton A.L., Endicott J.A., Mahadevan L.C.; RT "Molecular basis for the recognition of phosphorylated and RT phosphoacetylated histone h3 by 14-3-3."; RL Mol. Cell 20:199-211(2005). RN [40] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-230 IN COMPLEX WITH RP PSEUDOMONAS AERUGINOSA EXOS. RX PubMed=17235285; DOI=10.1038/sj.emboj.7601530; RA Ottmann C., Yasmin L., Weyand M., Veesenmeyer J.L., Diaz M.H., RA Palmer R.H., Francis M.S., Hauser A.R., Wittinghofer A., Hallberg B.; RT "Phosphorylation-independent interaction between 14-3-3 and exoenzyme RT S: from structure to pathogenesis."; RL EMBO J. 26:902-913(2007). CC -!- FUNCTION: Adapter protein implicated in the regulation of a large CC spectrum of both general and specialized signaling pathways. Binds CC to a large number of partners, usually by recognition of a CC phosphoserine or phosphothreonine motif. Binding generally results CC in the modulation of the activity of the binding partner. CC -!- SUBUNIT: Interacts with CDK16 and BSPRY (By similarity). Interacts CC with WEE1 (C-terminal). Interacts with SAMSN1 (By similarity). CC Interacts with MLF1 (phosphorylated form); the interaction retains CC it in the cytoplasm (By similarity). Interacts with Thr- CC phosphorylated ITGB2 (By similarity). Interacts with BCL2L11 (By CC similarity). Homodimer. Heterodimerizes with YWHAE. Homo- and CC hetero-dimerization is inhibited by phosphorylation on Ser-58. CC Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. Interacts with CC Pseudomonas aeruginosa exoS (unphosphorylated form). Interacts CC with BAX; the interaction occurs in the cytoplasm. Under stress CC conditions, MAPK8-mediated phosphorylation releases BAX to CC mitochondria. Interacts with phosphorylated RAF1; the interaction CC is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts CC with TP53; the interaction enhances p53 transcriptional activity. CC The Ser-58 phosphorylated form inhibits this interaction and p53 CC transcriptional activity. Interacts with ABL1 (phosphorylated CC form); the interaction retains ABL1 in the cytoplasm. Interacts CC with PKA-phosphorylated AANAT; the interaction modulates AANAT CC enzymatic activity by increasing affinity for arylalkylamines and CC acetyl-CoA and protecting the enzyme from dephosphorylation and CC proteasomal degradation. It may also prevent thiol-dependent CC inactivation. Interacts with AKT1; the interaction phosphorylates CC YWHAZ and modulates dimerization. Interacts with GAB2 and TLK2. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-347088, EBI-347088; CC Q29495:AANAT (xeno); NbExp=3; IntAct=EBI-347088, EBI-446413; CC P00519:ABL1; NbExp=2; IntAct=EBI-347088, EBI-375543; CC P60709:ACTB; NbExp=3; IntAct=EBI-347088, EBI-353944; CC Q9P0K1:ADAM22; NbExp=3; IntAct=EBI-347088, EBI-1567236; CC Q9P0K1-3:ADAM22; NbExp=3; IntAct=EBI-347088, EBI-1567267; CC P10398:ARAF; NbExp=3; IntAct=EBI-347088, EBI-365961; CC Q92974:ARHGEF2; NbExp=2; IntAct=EBI-347088, EBI-302405; CC P25705:ATP5A1; NbExp=3; IntAct=EBI-347088, EBI-351437; CC P06576:ATP5B; NbExp=2; IntAct=EBI-347088, EBI-356231; CC Q92934:BAD; NbExp=5; IntAct=EBI-347088, EBI-700771; CC Q61337:Bad (xeno); NbExp=3; IntAct=EBI-347088, EBI-400328; CC P15056:BRAF; NbExp=3; IntAct=EBI-347088, EBI-365980; CC P62158:CALM3; NbExp=2; IntAct=EBI-347088, EBI-397435; CC O00257-3:CBX4; NbExp=2; IntAct=EBI-347088, EBI-4392727; CC P30304:CDC25A; NbExp=2; IntAct=EBI-347088, EBI-747671; CC P30305:CDC25B; NbExp=4; IntAct=EBI-347088, EBI-1051746; CC Q00537:CDK17; NbExp=2; IntAct=EBI-347088, EBI-624648; CC Q07002:CDK18; NbExp=2; IntAct=EBI-347088, EBI-746238; CC P23528:CFL1; NbExp=3; IntAct=EBI-347088, EBI-352733; CC P31327:CPS1; NbExp=2; IntAct=EBI-347088, EBI-536811; CC P67828:CSNK1A1 (xeno); NbExp=4; IntAct=EBI-347088, EBI-7540603; CC P68104:EEF1A1; NbExp=2; IntAct=EBI-347088, EBI-352162; CC P00533:EGFR; NbExp=4; IntAct=EBI-347088, EBI-297353; CC P06733:ENO1; NbExp=2; IntAct=EBI-347088, EBI-353877; CC Q16658:FSCN1; NbExp=3; IntAct=EBI-347088, EBI-351076; CC P30793:GCH1; NbExp=4; IntAct=EBI-347088, EBI-958183; CC P49841:GSK3B; NbExp=4; IntAct=EBI-347088, EBI-373586; CC P56524:HDAC4; NbExp=5; IntAct=EBI-347088, EBI-308629; CC Q9UQL6:HDAC5; NbExp=2; IntAct=EBI-347088, EBI-715576; CC Q8WUI4:HDAC7; NbExp=3; IntAct=EBI-347088, EBI-1048378; CC P0C0S8:HIST1H2AM; NbExp=2; IntAct=EBI-347088, EBI-1390628; CC P68431:HIST1H3D; NbExp=3; IntAct=EBI-347088, EBI-79722; CC P62805:HIST2H4B; NbExp=3; IntAct=EBI-347088, EBI-302023; CC P07910:HNRNPC; NbExp=2; IntAct=EBI-347088, EBI-357966; CC P04792:HSPB1; NbExp=2; IntAct=EBI-347088, EBI-352682; CC Q02241:KIF23; NbExp=5; IntAct=EBI-347088, EBI-306852; CC P02545:LMNA; NbExp=2; IntAct=EBI-347088, EBI-351935; CC Q5S007:LRRK2; NbExp=7; IntAct=EBI-347088, EBI-5323863; CC Q99683:MAP3K5; NbExp=3; IntAct=EBI-347088, EBI-476263; CC P10636:MAPT; NbExp=8; IntAct=EBI-347088, EBI-366182; CC P10636-3:MAPT; NbExp=9; IntAct=EBI-347088, EBI-7145070; CC P29172:MAPT (xeno); NbExp=2; IntAct=EBI-347088, EBI-7291149; CC Q7KZI7:MARK2; NbExp=6; IntAct=EBI-347088, EBI-516560; CC P27448:MARK3; NbExp=9; IntAct=EBI-347088, EBI-707595; CC P19338:NCL; NbExp=2; IntAct=EBI-347088, EBI-346967; CC P06748:NPM1; NbExp=2; IntAct=EBI-347088, EBI-78579; CC Q8TEW0:PARD3; NbExp=4; IntAct=EBI-347088, EBI-81968; CC Q02156:PRKCE; NbExp=5; IntAct=EBI-347088, EBI-706254; CC O14744:PRMT5; NbExp=2; IntAct=EBI-347088, EBI-351098; CC P04049:RAF1; NbExp=12; IntAct=EBI-347088, EBI-365996; CC Q8NFH8-2:REPS2; NbExp=2; IntAct=EBI-347088, EBI-8029141; CC P61587:RND3; NbExp=11; IntAct=EBI-347088, EBI-1111534; CC P61588:Rnd3 (xeno); NbExp=3; IntAct=EBI-347088, EBI-6930266; CC P23396:RPS3; NbExp=2; IntAct=EBI-347088, EBI-351193; CC P31947:SFN; NbExp=2; IntAct=EBI-347088, EBI-476295; CC P57059:SIK1; NbExp=4; IntAct=EBI-347088, EBI-1181640; CC Q9Y2K2:SIK3; NbExp=5; IntAct=EBI-347088, EBI-1181460; CC O94875:SORBS2; NbExp=2; IntAct=EBI-347088, EBI-311323; CC Q15831:STK11; NbExp=6; IntAct=EBI-347088, EBI-306838; CC O00506:STK25; NbExp=2; IntAct=EBI-347088, EBI-618295; CC P36897:TGFBR1; NbExp=4; IntAct=EBI-347088, EBI-1027557; CC P04637:TP53; NbExp=2; IntAct=EBI-347088, EBI-366083; CC P49815:TSC2; NbExp=7; IntAct=EBI-347088, EBI-396587; CC P55072:VCP; NbExp=2; IntAct=EBI-347088, EBI-355164; CC P08670:VIM; NbExp=2; IntAct=EBI-347088, EBI-353844; CC P30291:WEE1; NbExp=3; IntAct=EBI-347088, EBI-914695; CC P46937:YAP1; NbExp=3; IntAct=EBI-347088, EBI-1044059; CC P62258:YWHAE; NbExp=5; IntAct=EBI-347088, EBI-356498; CC Q9NYL2:ZAK; NbExp=4; IntAct=EBI-347088, EBI-602273; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage CC I to stage IV melanosomes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P63104-1; Sequence=Displayed; CC Name=2; CC IsoId=P63104-2; Sequence=VSP_047505; CC Note=No experimental confirmation available; CC -!- PTM: The delta, brain-specific form differs from the zeta form in CC being phosphorylated (By similarity). Phosphorylation on Ser-184 CC by MAPK8; promotes dissociation of BAX and translocation of BAX to CC mitochondria. Phosphorylation on Thr-232; inhibits binding of CC RAF1. Phosphorylated on Ser-58 by PKA and protein kinase C delta CC type catalytic subunit in a sphingosine-dependent fashion. CC Phosphorylation on Ser-58 by PKA; disrupts homodimerization and CC heterodimerization with YHAE and TP53. CC -!- SIMILARITY: Belongs to the 14-3-3 family. CC -!- CAUTION: Was originally (PubMed:1577711) thought to have CC phospholipase A2 activity. CC -!- SEQUENCE CAUTION: CC Sequence=AAH51814.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=AAH73141.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M86400; AAA36446.1; -; mRNA. DR EMBL; U28964; AAC52052.1; -; mRNA. DR EMBL; AK289945; BAF82634.1; -; mRNA. DR EMBL; AK296902; BAH12451.1; -; mRNA. DR EMBL; CH471060; EAW91823.1; -; Genomic_DNA. DR EMBL; BC003623; AAH03623.3; -; mRNA. DR EMBL; BC051814; AAH51814.1; ALT_INIT; mRNA. DR EMBL; BC063824; AAH63824.2; -; mRNA. DR EMBL; BC068456; AAH68456.2; -; mRNA. DR EMBL; BC072426; AAH72426.2; -; mRNA. DR EMBL; BC073141; AAH73141.1; ALT_INIT; mRNA. DR EMBL; BC083508; AAH83508.2; -; mRNA. DR EMBL; BC099904; AAH99904.1; -; mRNA. DR EMBL; BC101483; AAI01484.1; -; mRNA. DR EMBL; BC108281; AAI08282.1; -; mRNA. DR EMBL; BC111951; AAI11952.1; -; mRNA. DR CCDS; CCDS6290.1; -. [P63104-1] DR PIR; A38246; PSHUAM. DR RefSeq; NP_001129171.1; NM_001135699.1. [P63104-1] DR RefSeq; NP_001129172.1; NM_001135700.1. [P63104-1] DR RefSeq; NP_001129173.1; NM_001135701.1. [P63104-1] DR RefSeq; NP_001129174.1; NM_001135702.1. [P63104-1] DR RefSeq; NP_003397.1; NM_003406.3. [P63104-1] DR RefSeq; NP_663723.1; NM_145690.2. [P63104-1] DR RefSeq; XP_005251118.1; XM_005251061.1. [P63104-1] DR RefSeq; XP_005251119.1; XM_005251062.1. [P63104-1] DR RefSeq; XP_005251120.1; XM_005251063.1. [P63104-1] DR UniGene; Hs.492407; -. DR PDB; 1IB1; X-ray; 2.70 A; A/B/C/D=1-245. DR PDB; 1QJA; X-ray; 2.00 A; A/B=1-245. DR PDB; 1QJB; X-ray; 2.00 A; A/B=1-245. DR PDB; 2C1J; X-ray; 2.60 A; A/B=1-245. DR PDB; 2C1N; X-ray; 2.00 A; A/B=1-245. DR PDB; 2O02; X-ray; 1.50 A; A/B=1-230. DR PDB; 2WH0; X-ray; 2.25 A; A/B/C/D=1-245. DR PDB; 3CU8; X-ray; 2.40 A; A/B=1-245. DR PDB; 3NKX; X-ray; 2.40 A; A/B=1-245. DR PDB; 3RDH; X-ray; 2.39 A; A/B/C/D=1-245. DR PDB; 4BG6; X-ray; 2.30 A; A/B=1-245. DR PDB; 4FJ3; X-ray; 1.95 A; A/B=1-230. DR PDB; 4HKC; X-ray; 2.20 A; A=1-245. DR PDB; 4IHL; X-ray; 2.20 A; A/B=1-230. DR PDB; 4N7G; X-ray; 2.25 A; A=1-230. DR PDB; 4N7Y; X-ray; 2.16 A; A/B=1-230. DR PDB; 4N84; X-ray; 2.50 A; A/B=1-230. DR PDBsum; 1IB1; -. DR PDBsum; 1QJA; -. DR PDBsum; 1QJB; -. DR PDBsum; 2C1J; -. DR PDBsum; 2C1N; -. DR PDBsum; 2O02; -. DR PDBsum; 2WH0; -. DR PDBsum; 3CU8; -. DR PDBsum; 3NKX; -. DR PDBsum; 3RDH; -. DR PDBsum; 4BG6; -. DR PDBsum; 4FJ3; -. DR PDBsum; 4HKC; -. DR PDBsum; 4IHL; -. DR PDBsum; 4N7G; -. DR PDBsum; 4N7Y; -. DR PDBsum; 4N84; -. DR ProteinModelPortal; P63104; -. DR SMR; P63104; 1-230. DR BioGrid; 113366; 372. DR DIP; DIP-563N; -. DR IntAct; P63104; 513. DR MINT; MINT-89071; -. DR DrugBank; DB01381; Ginkgo biloba. DR PhosphoSite; P63104; -. DR DMDM; 52000887; -. DR DOSAC-COBS-2DPAGE; P63104; -. DR OGP; P63104; -. DR UCD-2DPAGE; P63104; -. DR MaxQB; P63104; -. DR PaxDb; P63104; -. DR PRIDE; P63104; -. DR DNASU; 7534; -. DR Ensembl; ENST00000353245; ENSP00000309503; ENSG00000164924. [P63104-1] DR Ensembl; ENST00000395951; ENSP00000379281; ENSG00000164924. [P63104-1] DR Ensembl; ENST00000395953; ENSP00000379283; ENSG00000164924. [P63104-1] DR Ensembl; ENST00000395956; ENSP00000379286; ENSG00000164924. [P63104-1] DR Ensembl; ENST00000395957; ENSP00000379287; ENSG00000164924. [P63104-1] DR Ensembl; ENST00000395958; ENSP00000379288; ENSG00000164924. [P63104-1] DR Ensembl; ENST00000419477; ENSP00000395114; ENSG00000164924. [P63104-1] DR Ensembl; ENST00000457309; ENSP00000398599; ENSG00000164924. [P63104-1] DR Ensembl; ENST00000522542; ENSP00000430072; ENSG00000164924. [P63104-2] DR GeneID; 7534; -. DR KEGG; hsa:7534; -. DR UCSC; uc003yjv.2; human. [P63104-1] DR CTD; 7534; -. DR GeneCards; GC08M101930; -. DR HGNC; HGNC:12855; YWHAZ. DR HPA; CAB005065; -. DR MIM; 601288; gene. DR neXtProt; NX_P63104; -. DR PharmGKB; PA37444; -. DR eggNOG; COG5040; -. DR HOVERGEN; HBG050423; -. DR InParanoid; P63104; -. DR KO; K16197; -. DR OrthoDB; EOG7HHWT3; -. DR PhylomeDB; P63104; -. DR TreeFam; TF102003; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_21257; Metabolism of RNA. DR Reactome; REACT_578; Apoptosis. DR Reactome; REACT_604; Hemostasis. DR Reactome; REACT_6900; Immune System. DR Reactome; REACT_71; Gene Expression. DR SignaLink; P63104; -. DR ChiTaRS; YWHAZ; human. DR EvolutionaryTrace; P63104; -. DR GeneWiki; YWHAZ; -. DR GenomeRNAi; 7534; -. DR NextBio; 29475; -. DR PRO; PR:P63104; -. DR ArrayExpress; P63104; -. DR Bgee; P63104; -. DR Genevestigator; P63104; -. DR GO; GO:0072562; C:blood microparticle; IDA:UniProt. DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProt. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB. DR GO; GO:0042629; C:mast cell granule; IEA:GOC. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProt. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0043234; C:protein complex; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB. DR GO; GO:0006915; P:apoptotic process; TAS:Reactome. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0002553; P:histamine secretion by mast cell; IEA:Ensembl. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome. DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0006626; P:protein targeting to mitochondrion; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0016070; P:RNA metabolic process; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR Gene3D; 1.20.190.20; -; 1. DR InterPro; IPR000308; 14-3-3. DR InterPro; IPR023409; 14-3-3_CS. DR InterPro; IPR023410; 14-3-3_domain. DR PANTHER; PTHR18860; PTHR18860; 1. DR Pfam; PF00244; 14-3-3; 1. DR PIRSF; PIRSF000868; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR SUPFAM; SSF48445; SSF48445; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Cytoplasm; Direct protein sequencing; Phosphoprotein; KW Reference proteome. FT CHAIN 1 245 14-3-3 protein zeta/delta. FT /FTId=PRO_0000058627. FT SITE 56 56 Interaction with phosphoserine on FT interacting protein (By similarity). FT SITE 127 127 Interaction with phosphoserine on FT interacting protein (By similarity). FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 3 3 N6-acetyllysine. FT MOD_RES 58 58 Phosphoserine; by PKA and PKB/AKT1. FT MOD_RES 68 68 N6-acetyllysine. FT MOD_RES 184 184 Phosphoserine; by MAPK8. FT MOD_RES 207 207 Phosphoserine. FT MOD_RES 232 232 Phosphothreonine; by CK1. FT VAR_SEQ 1 98 MDKNELVQKAKLAEQAERYDDMAACMKSVTEQGAELSNEER FT NLLSVAYKNVVGARRSSWRVVSSIEQKTEGAEKKQQMAREY FT REKIETELRDICNDVL -> MSQPCRKLWRHNYETSSCIEF FT LK (in isoform 2). FT /FTId=VSP_047505. FT MUTAGEN 49 49 K->E: Loss of interaction with NOXA1. FT MUTAGEN 58 58 S->A: Loss of sphingosine-activated PKA FT phosphorylation. Promotes FT homodimerization and heterodimerization FT with YWHAE. Enhanced transcriptional FT activity of P53. FT MUTAGEN 58 58 S->E: Loss of homodimerization. Reduced FT dimerization with YWHAE. Significantly FT reduced interaction with P53. No FT enhancement of P53 transcriptional FT activity. FT MUTAGEN 184 184 S->A: On DNA damage, loss of MAPK8- FT mediated phosphorylation. Loss of binding FT ABL1. Attenuates ABL1-mediated apoptosis. FT No loss of interaction with BAX under FT stress conditions. Inhibits translocation FT of BAX to mitochondria. FT CONFLICT 22 22 M -> V (in Ref. 5; AAH68456). FT CONFLICT 136 136 D -> G (in Ref. 3; BAH12451). FT HELIX 3 15 FT HELIX 19 31 FT HELIX 38 67 FT TURN 69 71 FT HELIX 76 103 FT HELIX 105 108 FT HELIX 112 131 FT HELIX 135 159 FT HELIX 165 180 FT HELIX 185 200 FT HELIX 201 205 FT TURN 208 210 FT HELIX 211 228 SQ SEQUENCE 245 AA; 27745 MW; D464DF2286BBFE60 CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 1A01_HUMAN Reviewed; 365 AA. AC P30443; O77964; O78171; Q9MYA3; Q9TP25; Q9TQP5; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 09-JUL-2014, entry version 131. DE RecName: Full=HLA class I histocompatibility antigen, A-1 alpha chain; DE AltName: Full=MHC class I antigen A*1; DE Flags: Precursor; GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*01:01). RX PubMed=3375250; DOI=10.1073/pnas.85.11.4005; RA Parham P., Lomen C.E., Lawlor D.A., Ways J.P., Holmes N., Coppin H.L., RA Salter R.D., Wan A.M., Ennis P.D.; RT "Nature of polymorphism in HLA-A, -B, and -C molecules."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4005-4009(1988). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*01:01). RX PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE A*01:01). RA Warren E.; RL Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01). RX PubMed=2251137; DOI=10.1093/nar/18.22.6701; RA Girdlestone J.; RT "Nucleotide sequence of an HLA-A1 gene."; RL Nucleic Acids Res. 18:6701-6701(1990). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*01:01). RX PubMed=9349617; DOI=10.1111/j.1399-0039.1997.tb02885.x; RA Laforet M., Froelich N., Parissiadis A., Pfeiffer B., Schell A., RA Faller B., Woehl-Jaegle M.L., Cazenave J.-P., Tongio M.M.; RT "A nucleotide insertion in exon 4 is responsible for the absence of RT expression of an HLA-A*01 allele."; RL Tissue Antigens 50:347-350(1997). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE A*01:01). RA Waller M.J., Robinson J., Marsh S.G.E.; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE A*01:01). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*01:02). RX PubMed=7761977; DOI=10.1111/j.1399-0039.1995.tb02437.x; RA Browning M.J., Madrigal J.A., Krausa P., Kowalski H., Allsopp C.E., RA Little A.-M., Turner S., Adams E.J., Arnett K.L., Bodmer W.F., RA Parham P.; RT "The HLA-A,B,C genotype of the class I negative cell line Daudi RT reveals novel HLA-A and -B alleles."; RL Tissue Antigens 45:177-187(1995). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*01:03). RX PubMed=9438203; DOI=10.1016/S0198-8859(97)00204-8; RA Sitha S., Scheltinga S.A., Johnston-Dow L.A., White C.B., RA der van Zwan A.W., Bakema J.E., Rozemuller E.H., van der Tweel J.G., RA Kronink M.N., Tilanus M.G.J.; RT "A generic sequencing based typing approach for the identification of RT HLA-A diversity."; RL Hum. Immunol. 57:120-128(1997). RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*01:03). RC TISSUE=Blood; RX PubMed=11182232; DOI=10.1016/S0198-8859(00)00238-X; RA Poland G.A., Sohni Y., Domanico M., Kroning C.M., DeGoey S.R., RA Jimale M., Jacobson R.M., Moore S.B.; RT "High frequency of HLA-A*0103 allele in a Somali population."; RL Hum. Immunol. 62:197-200(2001). RN [11] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*01:06). RX PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [12] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*01:07). RA Tamouza R., Fortier C., Mahfoudh N., Schaeffer V., Poirier J.C., RA Marzais F., Gautreau C., Charron D.; RT "A new HLA-A*01 allele."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [13] RP SULFATION. RX PubMed=3121736; RA Sant A.J., Zacheis M., Rumbarger T., Giacoletto K.S., Schwartz B.D.; RT "Human Ia alpha- and beta-chains are sulfated."; RL J. Immunol. 140:155-160(1988). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 25-298 IN COMPLEX WITH MAGE RP ANTIGENIC PEPTIDE AND ANTIBODY, AND DISULFIDE BONDS. RX PubMed=15537658; DOI=10.1074/jbc.M411323200; RA Hulsmeyer M., Chames P., Hillig R.C., Stanfield R.L., Held G., RA Coulie P.G., Alings C., Wille G., Saenger W., Uchanska-Ziegler B., RA Hoogenboom H.R., Ziegler A.; RT "A major histocompatibility complex-peptide-restricted antibody and t RT cell receptor molecules recognize their target by distinct binding RT modes: crystal structure of human leukocyte antigen (HLA)-A1-MAGE-A1 RT in complex with FAB-HYB3."; RL J. Biol. Chem. 280:2972-2980(2005). RN [16] RP VARIANT [LARGE SCALE ANALYSIS] THR-166, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Sulfated. CC -!- PTM: Polyubiquitinated in a post ER compartment through CC interaction with human herpesvirus 8 MIR1 protein. This targets CC the protein for rapid degradation via the ubiquitin system (By CC similarity). CC -!- POLYMORPHISM: The following alleles of A-1 are known: A*01:01, CC A*01:02, A*01:03, A*01:06 and A*01:07. The sequence shown is that CC of A*01:01. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M24043; AAA59652.1; -; Genomic_DNA. DR EMBL; X55710; CAA39243.1; -; Genomic_DNA. DR EMBL; Z93949; CAB07989.1; -; Genomic_DNA. DR EMBL; AJ278305; CAB93537.1; -; Genomic_DNA. DR EMBL; BC003069; AAH03069.1; -; mRNA. DR EMBL; U07161; AAA80569.1; -; mRNA. DR EMBL; Y12469; CAA73072.1; -; Genomic_DNA. DR EMBL; Y12470; CAA73073.1; -; Genomic_DNA. DR EMBL; AH008863; AAF19525.1; -; Genomic_DNA. DR EMBL; AH007762; AAD33894.1; -; Genomic_DNA. DR EMBL; AH009407; AAF73862.1; -; Genomic_DNA. DR CCDS; CCDS34373.1; -. DR PIR; I38518; I38518. DR PIR; I61856; I61856. DR RefSeq; NP_001229687.1; NM_001242758.1. DR UniGene; Hs.181244; -. DR UniGene; Hs.713441; -. DR PDB; 1W72; X-ray; 2.15 A; A/D=25-298. DR PDB; 3BO8; X-ray; 1.80 A; A=25-298. DR PDB; 4NQV; X-ray; 2.39 A; A/C/E/G/I/K=25-298. DR PDB; 4NQX; X-ray; 2.00 A; A/C/E/G/I/K=25-308. DR PDBsum; 1W72; -. DR PDBsum; 3BO8; -. DR PDBsum; 4NQV; -. DR PDBsum; 4NQX; -. DR ProteinModelPortal; P30443; -. DR SMR; P30443; 25-298. DR BioGrid; 109350; 33. DR IntAct; P30443; 1. DR MINT; MINT-4655826; -. DR DMDM; 231347; -. DR PaxDb; P30443; -. DR PRIDE; P30443; -. DR DNASU; 3105; -. DR Ensembl; ENST00000431930; ENSP00000406366; ENSG00000229215. DR Ensembl; ENST00000443552; ENSP00000404678; ENSG00000224320. DR Ensembl; ENST00000549869; ENSP00000447635; ENSG00000224320. DR Ensembl; ENST00000552193; ENSP00000447614; ENSG00000229215. DR GeneID; 3105; -. DR KEGG; hsa:3105; -. DR UCSC; uc011ejp.2; human. DR CTD; 3105; -. DR GeneCards; GC06P029949; -. DR GeneCards; GC06Pi29846; -. DR GeneCards; GC06Pj29898; -. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR neXtProt; NX_P30443; -. DR Orphanet; 179; Chorioretinopathy, Birdshot type. DR eggNOG; NOG42056; -. DR HOVERGEN; HBG016709; -. DR KO; K06751; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-A; human. DR EvolutionaryTrace; P30443; -. DR GenomeRNAi; 3105; -. DR NextBio; 12319; -. DR CleanEx; HS_HLA-A; -. DR Genevestigator; P30443; -. DR GO; GO:0009986; C:cell surface; ISS:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030881; F:beta-2-microglobulin binding; ISS:UniProt. DR GO; GO:0042605; F:peptide antigen binding; IBA:RefGenome. DR GO; GO:0005102; F:receptor binding; IBA:RefGenome. DR GO; GO:0046977; F:TAP binding; IDA:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB. DR GO; GO:0006955; P:immune response; IMP:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:UniProt. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Host-virus interaction; Immunity; Immunoglobulin domain; Membrane; KW MHC I; Polymorphism; Reference proteome; Signal; Sulfation; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-1 alpha chain. FT /FTId=PRO_0000018813. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT MOD_RES 83 83 Sulfotyrosine (Potential). FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 33 33 F -> S (in allele A*01:02; FT dbSNP:rs2075684). FT /FTId=VAR_004332. FT VARIANT 41 41 R -> S (in allele A*01:02). FT /FTId=VAR_004333. FT VARIANT 80 80 G -> R (in allele A*01:07). FT /FTId=VAR_016719. FT VARIANT 89 89 R -> G (in dbSNP:rs1059459). FT /FTId=VAR_056247. FT VARIANT 91 91 M -> V (in allele A*01:07). FT /FTId=VAR_016720. FT VARIANT 100 100 A -> E (in allele A*01:07). FT /FTId=VAR_016721. FT VARIANT 114 114 D -> A (in allele A*01:07). FT /FTId=VAR_016722. FT VARIANT 121 121 I -> M (in allele A*01:03). FT /FTId=VAR_016723. FT VARIANT 131 131 G -> W (in dbSNP:rs1136702). FT /FTId=VAR_056248. FT VARIANT 133 133 F -> L (in dbSNP:rs1059488). FT /FTId=VAR_056249. FT VARIANT 151 151 N -> K (in dbSNP:rs1059509). FT /FTId=VAR_056250. FT VARIANT 166 166 I -> T (in dbSNP:rs1059516). FT /FTId=VAR_056251. FT VARIANT 169 169 R -> H (in dbSNP:rs1059520). FT /FTId=VAR_056252. FT VARIANT 180 180 R -> L (in allele A*01:06). FT /FTId=VAR_016724. FT VARIANT 182 182 V -> A (in allele A*01:06). FT /FTId=VAR_016725. FT VARIANT 205 205 R -> H (in dbSNP:rs17185861). FT /FTId=VAR_056253. FT STRAND 27 36 FT STRAND 41 43 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT STRAND 70 73 FT HELIX 74 76 FT HELIX 81 109 FT STRAND 113 115 FT STRAND 118 127 FT STRAND 133 142 FT STRAND 145 150 FT STRAND 157 159 FT HELIX 162 173 FT HELIX 176 185 FT HELIX 187 198 FT HELIX 200 203 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT STRAND 246 248 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT HELIX 278 280 FT STRAND 281 286 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 365 AA; 40846 MW; 8667AFF3F06C4932 CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQKME PRAPWIEQEG PEYWDQETRN MKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAVHAAEQR RVYLEGRCVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A02_HUMAN Reviewed; 365 AA. AC P01892; O19619; P06338; P10313; P30444; P30445; P30446; P30514; AC Q29680; Q29837; Q29899; Q95352; Q95380; Q9TPX8; Q9TPX9; Q9TPY0; AC Q9TQH5; Q9TQI3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 09-JUL-2014, entry version 168. DE RecName: Full=HLA class I histocompatibility antigen, A-2 alpha chain; DE AltName: Full=MHC class I antigen A*2; DE Flags: Precursor; GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01). RX PubMed=2982951; RA Koller B.H., Orr H.T.; RT "Cloning and complete sequence of an HLA-A2 gene: analysis of two HLA- RT A alleles at the nucleotide level."; RL J. Immunol. 134:2727-2733(1985). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*02:01). RX PubMed=2914713; DOI=10.1007/BF00395855; RA Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., Boccoli G., RA Giannella G., Peschle C., Boncinelli E.; RT "Three new class I HLA alleles: structure of mRNAs and alternative RT mechanisms of processing."; RL Immunogenetics 29:80-91(1989). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE A*02:01). RX PubMed=2320591; DOI=10.1073/pnas.87.7.2833; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 91-365. RX PubMed=3863816; RA Davidson W.F., Kress M., Khoury G., Jay G.; RT "Comparison of HLA class I gene sequences. Derivation of locus- RT specific oligonucleotide probes specific for HLA-A, HLA-B, and HLA-C RT genes."; RL J. Biol. Chem. 260:13414-13423(1985). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELES A*02:01; A*02:11 AND A*02:12). RX PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 39-365 (ALLELE A*02:01). RX PubMed=3874058; RA Krangel M.S.; RT "Unusual RNA splicing generates a secreted form of HLA-A2 in a RT mutagenized B lymphoblastoid cell line."; RL EMBO J. 4:1205-1210(1985). RN [7] RP PROTEIN SEQUENCE OF 25-295 (ALLELE A*02:01). RX PubMed=92029; DOI=10.1073/pnas.76.9.4395; RA Orr H.T., Lopez de Castro J.A., Parham P., Ploegh H.L., RA Strominger J.L.; RT "Comparison of amino acid sequences of two human histocompatibility RT antigens, HLA-A2 and HLA-B7: location of putative alloantigenic RT sites."; RL Proc. Natl. Acad. Sci. U.S.A. 76:4395-4399(1979). RN [8] RP SEQUENCE REVISION (ALLELE A*02:01). RX PubMed=6179086; DOI=10.1073/pnas.79.12.3813; RA Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.; RT "Structure of crossreactive human histocompatibility antigens HLA-A28 RT and HLA-A2: possible implications for the generation of HLA RT polymorphism."; RL Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*02:01). RC TISSUE=Blood; RX PubMed=7836067; DOI=10.1016/0198-8859(94)90087-6; RA Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.; RT "HLA class I allele (HLA-A2) expression defect associated with a RT mutation in its enhancer B inverted CAT box in two families."; RL Hum. Immunol. 41:69-73(1994). RN [10] RP SEQUENCE REVISION. RA Balas A.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE (ALLELE A*02:01). RA Cox S.T.; RT "Confirmation of HLA-A*0201."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELES A*02:02 AND RP A*02:03). RX PubMed=3497874; DOI=10.1007/BF00365911; RA Mattson D.H., Handy D.E., Bradley D.A., Coligan J.E., Cowan E.P., RA Biddison W.E.; RT "DNA sequences of the genes that encode the CTL-defined HLA-A2 RT variants M7 and DK1."; RL Immunogenetics 26:190-192(1987). RN [13] RP NUCLEOTIDE SEQUENCE (ALLELES A*02:03 AND A*02:05). RX PubMed=3496393; RA Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.; RT "Multiple genetic mechanisms have contributed to the generation of the RT HLA-A2/A28 family of class I MHC molecules."; RL J. Immunol. 139:936-941(1987). RN [14] RP NUCLEOTIDE SEQUENCE (ALLELES A*02:03 AND A*02:05). RA Domena J.D.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:04). RX PubMed=1937577; DOI=10.1007/BF00211991; RA Castano A.R., Lopez de Castro J.A.; RT "Structure of the HLA-A*0204 antigen, found in South American Indians. RT Spatial clustering of HLA-A2 subtype polymorphism."; RL Immunogenetics 34:281-285(1991). RN [16] RP NUCLEOTIDE SEQUENCE OF 9-365 (ALLELE A*02:04). RX PubMed=1589035; DOI=10.1038/357329a0; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [17] RP NUCLEOTIDE SEQUENCE (ALLELE A*02:06). RX PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [18] RP PARTIAL PROTEIN SEQUENCE (ALLELE A*02:06). RX PubMed=3489037; RA Ezquerra A., Domenech N., van der Poel J., Strominger J.L., Vega M.A., RA Lopez de Castro J.A.; RT "Molecular analysis of an HLA-A2 functional variant CLA defined by RT cytolytic T lymphocytes."; RL J. Immunol. 137:1642-1649(1986). RN [19] RP PARTIAL PROTEIN SEQUENCE (ALLELE A*02:07). RX PubMed=2448239; DOI=10.1007/BF00346586; RA Domenech N., Ezquerra A., Castano R., Lopez de Castro J.A.; RT "Structural analysis of HLA-A2.4 functional variant KNE. Implications RT for the mapping of HLA-A2-specific T-cell epitopes."; RL Immunogenetics 27:196-202(1988). RN [20] RP PARTIAL PROTEIN SEQUENCE (ALLELE A*02:08). RX PubMed=2457548; DOI=10.1007/BF00375853; RA Domenech N., Castano R., Goulmy E., Lopez de Castro J.A.; RT "Molecular analysis of HLA-A2.4 functional variant KLO: close RT structural and evolutionary relatedness to the HLA-A2.2 subtype."; RL Immunogenetics 28:143-152(1988). RN [21] RP PARTIAL PROTEIN SEQUENCE (ALLELE A*02:09). RX PubMed=3258580; DOI=10.1007/BF00395130; RA Castano R., Ezquerra A., Domenech N., Lopez de Castro J.A.; RT "An HLA-A2 population variant with structural polymorphism in the RT alpha 3 region."; RL Immunogenetics 27:345-355(1988). RN [22] RP NUCLEOTIDE SEQUENCE (ALLELE A*02:10). RX PubMed=2783680; DOI=10.1007/BF00395859; RA Epstein H., Kennedy L., Holmes N.; RT "An Oriental HLA-A2 subtype is closely related to a subset of RT Caucasoid HLA-A2 alleles."; RL Immunogenetics 29:112-116(1989). RN [23] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-365 (ALLELE A*02:11). RX PubMed=1559719; DOI=10.1007/BF00189898; RA Castano A.R., Lopez de Castro J.A.; RT "Structure of the HLA-A*0211 (A2.5) subtype: further evidence for RT selection-driven diversification of HLA-A2 antigens."; RL Immunogenetics 35:344-346(1992). RN [24] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:13). RX PubMed=8168863; DOI=10.1007/BF00189243; RA Barber D.F., Fernandez J.M., Lopez de Castro J.A.; RT "Primary structure of a new HLA-A2 subtype: HLA-A*0213."; RL Immunogenetics 39:378-378(1994). RN [25] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:16). RX PubMed=7759139; DOI=10.1007/BF00164000; RA Barouch D., Krausa P., Bodmer J., Browning M.J., McMichael A.J.; RT "Identification of a novel HLA-A2 subtype, HLA-A*0216."; RL Immunogenetics 41:388-388(1995). RN [26] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:17). RC TISSUE=Blood; RX PubMed=7652742; DOI=10.1111/j.1399-0039.1995.tb02464.x; RA Selvakumar A., Granja C.B., Salazar M., Alosco S.M., Yunis E.J., RA Dupont B.; RT "A novel subtype of A2 (A*0217) isolated from the South American RT Indian B-cell line AMALA."; RL Tissue Antigens 45:343-347(1995). RN [27] RP NUCLEOTIDE SEQUENCE (ALLELE A*02:18). RC TISSUE=Blood; RA Kashiwase K., Tokunaga K., Ishikawa Y., Oohashi H., Hashimoto M., RA Akaza T., Tadokoro K., Juji T.; RT "A new A2 sequence HLA-A2K from Japanese."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [28] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*02:20). RC TISSUE=Blood; RX PubMed=9008310; DOI=10.1111/j.1399-0039.1996.tb02691.x; RA Fleischhauer K., Zino E., Mazzi B., Severini G.M., Benazzi E., RA Bordignon C.; RT "HLA-A*02 subtype distribution in Caucasians from northern Italy: RT identification of A*0220."; RL Tissue Antigens 48:673-679(1996). RN [29] RP NUCLEOTIDE SEQUENCE (ALLELE A*02:21). RC TISSUE=Blood; RA Szmania S., Baxter-Lowe L.A.; RT "Nucleotide sequence of a novel HLA-A2 gene."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [30] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*02:31). RX PubMed=10689125; DOI=10.1016/S0198-8859(99)00155-X; RA Ellis J.M., Henson V., Slack R., Ng J., Hartzman R.J., Hurley C.K.; RT "Frequencies of HLA-A2 alleles in five U.S. population groups. RT Predominance Of A*02011 and identification of HLA-A*0231."; RL Hum. Immunol. 61:334-340(2000). RN [31] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-298 (ALLELE A*02:34). RX PubMed=10746792; DOI=10.1034/j.1399-0039.2000.550212.x; RA Moses J.H., Greville W.D., Downes J., McClenahan W., Kennedy A., RA Dunckley H.; RT "A new HLA-A*02 allele, A*0234, detected by polymerase chain reaction RT using sequence-specific primers (PCR-SSP)."; RL Tissue Antigens 55:175-177(2000). RN [32] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*02:35; A*02:36 AND A*02:37). RX PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [35] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [36] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF A*02:01. RX PubMed=3309677; DOI=10.1038/329506a0; RA Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., Strominger J.L., RA Wiley D.C.; RT "Structure of the human class I histocompatibility antigen, HLA-A2."; RL Nature 329:506-512(1987). RN [37] RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I. RX PubMed=11390610; DOI=10.1128/JVI.75.13.6086-6094.2001; RA Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L., RA Mulloy J.C., Jacobson S., Franchini G.; RT "Free major histocompatibility complex class I heavy chain is RT preferentially targeted for degradation by human T-cell RT leukemia/lymphotropic virus type 1 p12(I) protein."; RL J. Virol. 75:6086-6094(2001). RN [38] RP INTERACTION WITH HUMAN HERPESVIRUS 8 MIR1 PROTEIN, AND UBIQUITINATION. RX PubMed=12006494; DOI=10.1093/emboj/21.10.2418; RA Hewitt E.W., Duncan L., Mufti D., Baker J., Stevenson P.G., RA Lehner P.J.; RT "Ubiquitylation of MHC class I by the K3 viral protein signals RT internalization and TSG101-dependent degradation."; RL EMBO J. 21:2418-2429(2002). RN [39] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 25-300 OF HLA-A/B2M RP HETERODIMER IN COMPLEX WITH TRAC AND TRBC1, AND DISULFIDE BONDS. RX PubMed=12796775; DOI=10.1038/ni942; RA Stewart-Jones G.B.E., McMichael A.J., Bell J.I., Stuart D.I., RA Jones E.Y.; RT "A structural basis for immunodominant human T cell receptor RT recognition."; RL Nat. Immunol. 4:657-663(2003). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF A*02:01. RX PubMed=2038058; DOI=10.1016/0022-2836(91)90567-P; RA Saper M.A., Bjorkman P.J., Wiley D.C.; RT "Refined structure of the human histocompatibility antigen HLA-A2 at RT 2.6-A resolution."; RL J. Mol. Biol. 219:277-319(1991). RN [41] RP VARIANT [LARGE SCALE ANALYSIS] GLU-176, VARIANT [LARGE SCALE ANALYSIS] RP TRP-180, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Dimer of alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein. CC Interacts with HTLV-1 accessory protein p12I. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment through CC interaction with human herpesvirus 8 MIR1 protein. This targets CC the protein for rapid degradation via the ubiquitin system. CC -!- POLYMORPHISM: The following alleles of A-2 are known: A*02:01, CC A*02:02, A*02:03, A*02:04, A*02:05, A*02:06 (A2.4A), A*02:07, CC A*02:08, A*02:09, A*02:10, A*02:11 (A2.5), A*02:12, A*02:13 CC (A*02SLU), A*02:16, A*02:17, A*02:18 (A2K), A*02:19, A*02:20, CC A*02:21, A*02:31, A*02:34 (A*AAT), A*02:35, A*02:36 and A*02:37. CC The sequence shown is that of A*02:01. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC -!- SEQUENCE CAUTION: CC Sequence=CAA41022.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown extensively; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K02883; AAA98727.1; -; Genomic_DNA. DR EMBL; M84379; AAA59606.1; -; mRNA. DR EMBL; X02457; CAA26297.1; -; mRNA. DR EMBL; M11887; AAA52656.1; -; mRNA. DR EMBL; M19670; AAA03683.2; -; Genomic_DNA. DR EMBL; AH003586; AAB02120.1; -; Genomic_DNA. DR EMBL; U03863; AAA03604.1; -; mRNA. DR EMBL; M86404; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X57954; CAA41022.1; ALT_SEQ; mRNA. DR EMBL; U02935; AAA76608.2; -; Genomic_DNA. DR EMBL; AJ555412; CAD87771.1; -; Genomic_DNA. DR EMBL; U03862; AAA03603.1; -; mRNA. DR EMBL; M24042; AAA59653.1; -; mRNA. DR EMBL; Z23071; CAA80612.1; -; mRNA. DR EMBL; M84377; AAA59603.1; -; mRNA. DR EMBL; X60764; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M84378; AAA59604.1; -; mRNA. DR EMBL; Z27120; CAA81644.1; -; mRNA. DR EMBL; Z46633; CAA86602.1; -; mRNA. DR EMBL; U18930; AAA87076.1; -; mRNA. DR EMBL; D83515; BAA11935.1; -; mRNA. DR EMBL; X96724; CAA65501.1; -; mRNA. DR EMBL; U56825; AAB17465.1; -; mRNA. DR EMBL; AH007560; AAD23437.1; -; Genomic_DNA. DR EMBL; AH007704; AAD30272.1; -; Genomic_DNA. DR EMBL; AH008013; AAD45690.1; -; Genomic_DNA. DR EMBL; AH008012; AAD45689.1; -; Genomic_DNA. DR EMBL; AH008007; AAD45324.1; -; Genomic_DNA. DR PIR; B24512; HLHU10. DR PIR; I37470; I37470. DR PIR; I37542; I37542. DR PIR; I38418; I38418. DR PIR; I38442; I38442. DR PIR; I38443; I38443. DR PIR; I55948; HLHUA2. DR PIR; I61857; I61857. DR PIR; I61902; I61902. DR PIR; I84448; I84448. DR RefSeq; XP_006725814.1; XM_006725751.1. DR UniGene; Hs.181244; -. DR UniGene; Hs.713441; -. DR PDB; 1AKJ; X-ray; 2.65 A; A=25-300. DR PDB; 1AO7; X-ray; 2.60 A; A=25-299. DR PDB; 1AQD; X-ray; 2.45 A; C/F/I/L=127-141. DR PDB; 1B0G; X-ray; 2.50 A; A/D=25-299. DR PDB; 1B0R; X-ray; 2.90 A; A=25-299. DR PDB; 1BD2; X-ray; 2.50 A; A=25-299. DR PDB; 1DUY; X-ray; 2.15 A; A/D=25-299. DR PDB; 1DUZ; X-ray; 1.80 A; A/D=25-299. DR PDB; 1EEY; X-ray; 2.25 A; A/D=25-299. DR PDB; 1EEZ; X-ray; 2.30 A; A/D=25-299. DR PDB; 1HHG; X-ray; 2.60 A; A/D=25-299. DR PDB; 1HHH; X-ray; 3.00 A; A=25-299. DR PDB; 1HHI; X-ray; 2.50 A; A/D=25-299. DR PDB; 1HHJ; X-ray; 2.50 A; A/D=25-299. DR PDB; 1HHK; X-ray; 2.50 A; A/D=25-299. DR PDB; 1HLA; X-ray; 3.50 A; A=25-294. DR PDB; 1I1F; X-ray; 2.80 A; A/D=25-299. DR PDB; 1I1Y; X-ray; 2.20 A; A/D=25-299. DR PDB; 1I4F; X-ray; 1.40 A; A=25-299. DR PDB; 1I7R; X-ray; 2.20 A; A/D=25-299. DR PDB; 1I7T; X-ray; 2.80 A; A/D=25-299. DR PDB; 1I7U; X-ray; 1.80 A; A/D=25-299. DR PDB; 1IM3; X-ray; 2.20 A; A/E/I/M=25-299. DR PDB; 1JF1; X-ray; 1.85 A; A=25-299. DR PDB; 1JHT; X-ray; 2.15 A; A=25-299. DR PDB; 1LP9; X-ray; 2.00 A; A/H=25-299. DR PDB; 1OGA; X-ray; 1.40 A; A=25-300. DR PDB; 1P7Q; X-ray; 3.40 A; A=25-300. DR PDB; 1QEW; X-ray; 2.20 A; A=25-299. DR PDB; 1QR1; X-ray; 2.40 A; A/D=25-299. DR PDB; 1QRN; X-ray; 2.80 A; A=25-298. DR PDB; 1QSE; X-ray; 2.80 A; A=25-298. DR PDB; 1QSF; X-ray; 2.80 A; A=25-298. DR PDB; 1S8D; X-ray; 2.20 A; A=25-299. DR PDB; 1S9W; X-ray; 2.20 A; A=25-298. DR PDB; 1S9X; X-ray; 2.50 A; A=25-298. DR PDB; 1S9Y; X-ray; 2.30 A; A=25-298. DR PDB; 1T1W; X-ray; 2.20 A; A=25-299. DR PDB; 1T1X; X-ray; 2.20 A; A=25-299. DR PDB; 1T1Y; X-ray; 2.00 A; A=25-299. DR PDB; 1T1Z; X-ray; 1.90 A; A=25-299. DR PDB; 1T20; X-ray; 2.20 A; A=25-299. DR PDB; 1T21; X-ray; 2.19 A; A=25-299. DR PDB; 1T22; X-ray; 2.20 A; A=25-299. DR PDB; 1TVB; X-ray; 1.80 A; A/D=25-299. DR PDB; 1TVH; X-ray; 1.80 A; A/D=25-299. DR PDB; 1UR7; Model; -; A=25-299. DR PDB; 2AV1; X-ray; 1.95 A; A/D=25-299. DR PDB; 2AV7; X-ray; 2.05 A; A/D=25-299. DR PDB; 2BNQ; X-ray; 1.70 A; A=25-300. DR PDB; 2BNR; X-ray; 1.90 A; A=25-300. DR PDB; 2C7U; X-ray; 2.38 A; A/D=25-300. DR PDB; 2CLR; X-ray; 2.00 A; A/D=25-299. DR PDB; 2F53; X-ray; 2.10 A; A=25-299. DR PDB; 2F54; X-ray; 2.70 A; A/F=25-298. DR PDB; 2GIT; X-ray; 1.70 A; A/D=25-299. DR PDB; 2GJ6; X-ray; 2.56 A; A=25-299. DR PDB; 2GT9; X-ray; 1.75 A; A/D=25-299. DR PDB; 2GTW; X-ray; 1.55 A; A/D=25-299. DR PDB; 2GTZ; X-ray; 1.70 A; A/D=25-299. DR PDB; 2GUO; X-ray; 1.90 A; A/D=25-299. DR PDB; 2J8U; X-ray; 2.88 A; A/H=25-299. DR PDB; 2JCC; X-ray; 2.50 A; A/H=25-299. DR PDB; 2P5E; X-ray; 1.89 A; A=25-300. DR PDB; 2P5W; X-ray; 2.20 A; A=25-300. DR PDB; 2PYE; X-ray; 2.30 A; A=25-300. DR PDB; 2UWE; X-ray; 2.40 A; A/H=25-299. DR PDB; 2V2W; X-ray; 1.60 A; A/D=25-300. DR PDB; 2V2X; X-ray; 1.60 A; A/D=25-300. DR PDB; 2VLJ; X-ray; 2.40 A; A=25-300. DR PDB; 2VLK; X-ray; 2.50 A; A=25-300. DR PDB; 2VLL; X-ray; 1.60 A; A/D=25-300. DR PDB; 2VLR; X-ray; 2.30 A; A/F=25-300. DR PDB; 2X4N; X-ray; 2.34 A; A/D=25-299. DR PDB; 2X4O; X-ray; 2.30 A; A/D=25-299. DR PDB; 2X4P; X-ray; 2.30 A; A/D=25-299. DR PDB; 2X4Q; X-ray; 1.90 A; A/D=25-299. DR PDB; 2X4R; X-ray; 2.30 A; A/D=25-299. DR PDB; 2X4S; X-ray; 2.55 A; A/D=25-299. DR PDB; 2X4T; X-ray; 2.30 A; A/D=25-299. DR PDB; 2X4U; X-ray; 2.10 A; A/D=25-299. DR PDB; 2X70; X-ray; 2.00 A; A/D=25-299. DR PDB; 3BGM; X-ray; 1.60 A; A=25-298. DR PDB; 3BH8; X-ray; 1.65 A; A=25-298. DR PDB; 3BH9; X-ray; 1.70 A; A=25-299. DR PDB; 3BHB; X-ray; 2.20 A; A=25-298. DR PDB; 3D25; X-ray; 1.30 A; A=25-298. DR PDB; 3D39; X-ray; 2.81 A; A=25-299. DR PDB; 3D3V; X-ray; 2.80 A; A=25-299. DR PDB; 3FQN; X-ray; 1.65 A; A=25-299. DR PDB; 3FQR; X-ray; 1.70 A; A=25-299. DR PDB; 3FQT; X-ray; 1.80 A; A=25-299. DR PDB; 3FQU; X-ray; 1.80 A; A=25-299. DR PDB; 3FQW; X-ray; 1.93 A; A=25-299. DR PDB; 3FQX; X-ray; 1.70 A; A=25-299. DR PDB; 3FT2; X-ray; 1.80 A; A=25-299. DR PDB; 3FT3; X-ray; 1.95 A; A=25-299. DR PDB; 3FT4; X-ray; 1.90 A; A=25-299. DR PDB; 3GIV; X-ray; 2.00 A; A/D=25-299. DR PDB; 3GJF; X-ray; 1.90 A; A/D=25-300. DR PDB; 3GSN; X-ray; 2.80 A; H=25-298. DR PDB; 3GSO; X-ray; 1.60 A; A=25-298. DR PDB; 3GSQ; X-ray; 2.12 A; A=25-298. DR PDB; 3GSR; X-ray; 1.95 A; A=25-298. DR PDB; 3GSU; X-ray; 1.80 A; A=25-299. DR PDB; 3GSV; X-ray; 1.90 A; A=25-299. DR PDB; 3GSW; X-ray; 1.81 A; A=25-298. DR PDB; 3GSX; X-ray; 2.10 A; A=25-298. DR PDB; 3H7B; X-ray; 1.88 A; A/D=25-299. DR PDB; 3H9H; X-ray; 2.00 A; A/D=25-299. DR PDB; 3H9S; X-ray; 2.70 A; A=25-299. DR PDB; 3HAE; X-ray; 2.90 A; A/D/J/P=25-300. DR PDB; 3HLA; X-ray; 2.60 A; A=25-294. DR PDB; 3HPJ; X-ray; 2.00 A; A/D=25-299. DR PDB; 3I6G; X-ray; 2.20 A; A/D=25-299. DR PDB; 3I6K; X-ray; 2.80 A; A/E=25-299. DR PDB; 3IXA; X-ray; 2.10 A; A/D=25-299. DR PDB; 3KLA; X-ray; 1.65 A; A/D=25-299. DR PDB; 3MGO; X-ray; 2.30 A; A/D/G/J=25-299. DR PDB; 3MGT; X-ray; 2.20 A; A/D/G/J=25-299. DR PDB; 3MR9; X-ray; 1.93 A; A=25-300. DR PDB; 3MRB; X-ray; 1.40 A; A=25-300. DR PDB; 3MRC; X-ray; 1.80 A; A=25-300. DR PDB; 3MRD; X-ray; 1.70 A; A=25-300. DR PDB; 3MRE; X-ray; 1.10 A; A=25-300. DR PDB; 3MRF; X-ray; 2.30 A; A=25-300. DR PDB; 3MRG; X-ray; 1.30 A; A=25-300. DR PDB; 3MRH; X-ray; 2.40 A; A=25-300. DR PDB; 3MRI; X-ray; 2.10 A; A=25-300. DR PDB; 3MRJ; X-ray; 1.87 A; A=25-300. DR PDB; 3MRK; X-ray; 1.40 A; A=25-300. DR PDB; 3MRL; X-ray; 2.41 A; A=25-300. DR PDB; 3MRM; X-ray; 1.90 A; A=25-300. DR PDB; 3MRN; X-ray; 2.30 A; A=25-300. DR PDB; 3MRO; X-ray; 2.35 A; A=25-300. DR PDB; 3MRP; X-ray; 2.10 A; A=25-300. DR PDB; 3MRQ; X-ray; 2.20 A; A=25-300. DR PDB; 3MRR; X-ray; 1.60 A; A=25-300. DR PDB; 3MYJ; X-ray; 1.89 A; A/D=25-299. DR PDB; 3O3A; X-ray; 1.80 A; A/D=25-299. DR PDB; 3O3B; X-ray; 1.90 A; A/D=25-299. DR PDB; 3O3D; X-ray; 1.70 A; A/D=25-299. DR PDB; 3O3E; X-ray; 1.85 A; A/D=25-299. DR PDB; 3O4L; X-ray; 2.54 A; A=25-300. DR PDB; 3PWJ; X-ray; 1.70 A; A/D=25-299. DR PDB; 3PWL; X-ray; 1.65 A; A/D=25-299. DR PDB; 3PWN; X-ray; 1.60 A; A/D=25-299. DR PDB; 3PWP; X-ray; 2.69 A; A=25-299. DR PDB; 3QDG; X-ray; 2.69 A; A=25-299. DR PDB; 3QDJ; X-ray; 2.30 A; A=25-299. DR PDB; 3QDM; X-ray; 2.80 A; A=25-299. DR PDB; 3QEQ; X-ray; 2.59 A; A=25-299. DR PDB; 3QFD; X-ray; 1.68 A; A/D=25-299. DR PDB; 3QFJ; X-ray; 2.29 A; A=25-299. DR PDB; 3REW; X-ray; 1.90 A; A/D=25-299. DR PDB; 3TO2; X-ray; 2.60 A; A=25-299. DR PDB; 3UTQ; X-ray; 1.67 A; A=25-300. DR PDB; 3UTS; X-ray; 2.71 A; A/F=25-300. DR PDB; 3UTT; X-ray; 2.60 A; A/F=25-299. DR PDB; 3V5D; X-ray; 2.00 A; A/D=25-299. DR PDB; 3V5H; X-ray; 1.63 A; A/D=25-299. DR PDB; 3V5K; X-ray; 2.31 A; A/D=25-299. DR PDB; 4E5X; X-ray; 1.95 A; A/D=25-299. DR PDB; 4EMZ; X-ray; 2.90 A; D/E=338-365. DR PDB; 4EN2; X-ray; 2.58 A; D/E=338-365. DR PDB; 4EUP; X-ray; 2.88 A; A/D=25-299. DR PDB; 4EUQ; X-ray; 2.69 A; A/D=25-299. DR PDB; 4FTV; X-ray; 2.74 A; A=25-299. DR PDB; 4GKN; X-ray; 2.75 A; A/D=25-300. DR PDB; 4GKS; X-ray; 2.35 A; A/D=25-300. DR PDB; 4I4W; X-ray; 1.77 A; A=25-300. DR PDB; 4JFD; X-ray; 2.46 A; A=25-300. DR PDB; 4JFE; X-ray; 2.70 A; A=25-300. DR PDB; 4JFF; X-ray; 2.43 A; A=25-300. DR PDB; 4JFO; X-ray; 2.11 A; A/D=25-299. DR PDB; 4JFP; X-ray; 1.91 A; A/D=25-300. DR PDB; 4JFQ; X-ray; 1.90 A; A/D=25-300. DR PDB; 4K7F; X-ray; 2.00 A; A/D=25-299. DR PDB; 4L29; X-ray; 3.09 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300. DR PDB; 4L3C; X-ray; 2.64 A; A/C/E/G/I/K/M/O/Q/S/U/W/Y/a=25-300. DR PDB; 4MNQ; X-ray; 2.74 A; A=25-300. DR PDBsum; 1AKJ; -. DR PDBsum; 1AO7; -. DR PDBsum; 1AQD; -. DR PDBsum; 1B0G; -. DR PDBsum; 1B0R; -. DR PDBsum; 1BD2; -. DR PDBsum; 1DUY; -. DR PDBsum; 1DUZ; -. DR PDBsum; 1EEY; -. DR PDBsum; 1EEZ; -. DR PDBsum; 1HHG; -. DR PDBsum; 1HHH; -. DR PDBsum; 1HHI; -. DR PDBsum; 1HHJ; -. DR PDBsum; 1HHK; -. DR PDBsum; 1HLA; -. DR PDBsum; 1I1F; -. DR PDBsum; 1I1Y; -. DR PDBsum; 1I4F; -. DR PDBsum; 1I7R; -. DR PDBsum; 1I7T; -. DR PDBsum; 1I7U; -. DR PDBsum; 1IM3; -. DR PDBsum; 1JF1; -. DR PDBsum; 1JHT; -. DR PDBsum; 1LP9; -. DR PDBsum; 1OGA; -. DR PDBsum; 1P7Q; -. DR PDBsum; 1QEW; -. DR PDBsum; 1QR1; -. DR PDBsum; 1QRN; -. DR PDBsum; 1QSE; -. DR PDBsum; 1QSF; -. DR PDBsum; 1S8D; -. DR PDBsum; 1S9W; -. DR PDBsum; 1S9X; -. DR PDBsum; 1S9Y; -. DR PDBsum; 1T1W; -. DR PDBsum; 1T1X; -. DR PDBsum; 1T1Y; -. DR PDBsum; 1T1Z; -. DR PDBsum; 1T20; -. DR PDBsum; 1T21; -. DR PDBsum; 1T22; -. DR PDBsum; 1TVB; -. DR PDBsum; 1TVH; -. DR PDBsum; 1UR7; -. DR PDBsum; 2AV1; -. DR PDBsum; 2AV7; -. DR PDBsum; 2BNQ; -. DR PDBsum; 2BNR; -. DR PDBsum; 2C7U; -. DR PDBsum; 2CLR; -. DR PDBsum; 2F53; -. DR PDBsum; 2F54; -. DR PDBsum; 2GIT; -. DR PDBsum; 2GJ6; -. DR PDBsum; 2GT9; -. DR PDBsum; 2GTW; -. DR PDBsum; 2GTZ; -. DR PDBsum; 2GUO; -. DR PDBsum; 2J8U; -. DR PDBsum; 2JCC; -. DR PDBsum; 2P5E; -. DR PDBsum; 2P5W; -. DR PDBsum; 2PYE; -. DR PDBsum; 2UWE; -. DR PDBsum; 2V2W; -. DR PDBsum; 2V2X; -. DR PDBsum; 2VLJ; -. DR PDBsum; 2VLK; -. DR PDBsum; 2VLL; -. DR PDBsum; 2VLR; -. DR PDBsum; 2X4N; -. DR PDBsum; 2X4O; -. DR PDBsum; 2X4P; -. DR PDBsum; 2X4Q; -. DR PDBsum; 2X4R; -. DR PDBsum; 2X4S; -. DR PDBsum; 2X4T; -. DR PDBsum; 2X4U; -. DR PDBsum; 2X70; -. DR PDBsum; 3BGM; -. DR PDBsum; 3BH8; -. DR PDBsum; 3BH9; -. DR PDBsum; 3BHB; -. DR PDBsum; 3D25; -. DR PDBsum; 3D39; -. DR PDBsum; 3D3V; -. DR PDBsum; 3FQN; -. DR PDBsum; 3FQR; -. DR PDBsum; 3FQT; -. DR PDBsum; 3FQU; -. DR PDBsum; 3FQW; -. DR PDBsum; 3FQX; -. DR PDBsum; 3FT2; -. DR PDBsum; 3FT3; -. DR PDBsum; 3FT4; -. DR PDBsum; 3GIV; -. DR PDBsum; 3GJF; -. DR PDBsum; 3GSN; -. DR PDBsum; 3GSO; -. DR PDBsum; 3GSQ; -. DR PDBsum; 3GSR; -. DR PDBsum; 3GSU; -. DR PDBsum; 3GSV; -. DR PDBsum; 3GSW; -. DR PDBsum; 3GSX; -. DR PDBsum; 3H7B; -. DR PDBsum; 3H9H; -. DR PDBsum; 3H9S; -. DR PDBsum; 3HAE; -. DR PDBsum; 3HLA; -. DR PDBsum; 3HPJ; -. DR PDBsum; 3I6G; -. DR PDBsum; 3I6K; -. DR PDBsum; 3IXA; -. DR PDBsum; 3KLA; -. DR PDBsum; 3MGO; -. DR PDBsum; 3MGT; -. DR PDBsum; 3MR9; -. DR PDBsum; 3MRB; -. DR PDBsum; 3MRC; -. DR PDBsum; 3MRD; -. DR PDBsum; 3MRE; -. DR PDBsum; 3MRF; -. DR PDBsum; 3MRG; -. DR PDBsum; 3MRH; -. DR PDBsum; 3MRI; -. DR PDBsum; 3MRJ; -. DR PDBsum; 3MRK; -. DR PDBsum; 3MRL; -. DR PDBsum; 3MRM; -. DR PDBsum; 3MRN; -. DR PDBsum; 3MRO; -. DR PDBsum; 3MRP; -. DR PDBsum; 3MRQ; -. DR PDBsum; 3MRR; -. DR PDBsum; 3MYJ; -. DR PDBsum; 3O3A; -. DR PDBsum; 3O3B; -. DR PDBsum; 3O3D; -. DR PDBsum; 3O3E; -. DR PDBsum; 3O4L; -. DR PDBsum; 3PWJ; -. DR PDBsum; 3PWL; -. DR PDBsum; 3PWN; -. DR PDBsum; 3PWP; -. DR PDBsum; 3QDG; -. DR PDBsum; 3QDJ; -. DR PDBsum; 3QDM; -. DR PDBsum; 3QEQ; -. DR PDBsum; 3QFD; -. DR PDBsum; 3QFJ; -. DR PDBsum; 3REW; -. DR PDBsum; 3TO2; -. DR PDBsum; 3UTQ; -. DR PDBsum; 3UTS; -. DR PDBsum; 3UTT; -. DR PDBsum; 3V5D; -. DR PDBsum; 3V5H; -. DR PDBsum; 3V5K; -. DR PDBsum; 4E5X; -. DR PDBsum; 4EMZ; -. DR PDBsum; 4EN2; -. DR PDBsum; 4EUP; -. DR PDBsum; 4EUQ; -. DR PDBsum; 4FTV; -. DR PDBsum; 4GKN; -. DR PDBsum; 4GKS; -. DR PDBsum; 4I4W; -. DR PDBsum; 4JFD; -. DR PDBsum; 4JFE; -. DR PDBsum; 4JFF; -. DR PDBsum; 4JFO; -. DR PDBsum; 4JFP; -. DR PDBsum; 4JFQ; -. DR PDBsum; 4K7F; -. DR PDBsum; 4L29; -. DR PDBsum; 4L3C; -. DR PDBsum; 4MNQ; -. DR ProteinModelPortal; P01892; -. DR SMR; P01892; 25-298. DR DIP; DIP-6085N; -. DR IntAct; P01892; 12. DR MINT; MINT-5000859; -. DR PhosphoSite; P01892; -. DR DMDM; 122138; -. DR MaxQB; P01892; -. DR PaxDb; P01892; -. DR PRIDE; P01892; -. DR Ensembl; ENST00000457879; ENSP00000403575; ENSG00000235657. DR Ensembl; ENST00000547271; ENSP00000447962; ENSG00000235657. DR GeneID; 3105; -. DR GeneCards; GC06P029949; -. DR GeneCards; GC06Pk29899; -. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR neXtProt; NX_P01892; -. DR eggNOG; NOG42056; -. DR HOVERGEN; HBG016709; -. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-A; human. DR EvolutionaryTrace; P01892; -. DR CleanEx; HS_HLA-A; -. DR Genevestigator; P01892; -. DR GO; GO:0009986; C:cell surface; IDA:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProt. DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProt. DR GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042612; C:MHC class I protein complex; IDA:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030881; F:beta-2-microglobulin binding; IDA:UniProt. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProt. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0005102; F:receptor binding; IPI:BHF-UCL. DR GO; GO:0046977; F:TAP binding; IDA:UniProt. DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IDA:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:UniProt. DR GO; GO:2000568; P:positive regulation of memory T cell activation; IDA:UniProt. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:UniProt. DR GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Host-virus interaction; Immunity; KW Membrane; MHC I; Phosphoprotein; Polymorphism; Reference proteome; KW Signal; Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-2 alpha chain. FT /FTId=PRO_0000018814. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT MOD_RES 356 356 Phosphoserine. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 33 33 F -> Y (in allele A*02:05, allele FT A*02:06, allele A*02:08, allele A*02:10 FT and allele A*02:21). FT /FTId=VAR_004334. FT VARIANT 54 54 D -> N (in allele A*02:21). FT /FTId=VAR_004335. FT VARIANT 65 65 A -> G (in allele A*02:31). FT /FTId=VAR_016726. FT VARIANT 67 67 Q -> R (in allele A*02:02, allele A*02:05 FT and allele A*02:08). FT /FTId=VAR_004336. FT VARIANT 90 90 K -> N (in allele A*02:08 and allele FT A*02:20). FT /FTId=VAR_004337. FT VARIANT 94 94 H -> Q (in allele A*02:34 and allele FT A*02:35). FT /FTId=VAR_016727. FT VARIANT 97 97 T -> I (in allele A*02:11). FT /FTId=VAR_004338. FT VARIANT 98 98 H -> D (in allele A*02:11 and allele FT A*02:35). FT /FTId=VAR_016728. FT VARIANT 119 119 V -> L (in allele A*02:02, allele FT A*02:05, allele A*02:08 and allele FT A*02:17). FT /FTId=VAR_004339. FT VARIANT 121 121 R -> M (in allele A*02:04 and allele FT A*02:17). FT /FTId=VAR_004340. FT VARIANT 123 123 Y -> C (in allele A*02:07 and allele FT A*02:18). FT /FTId=VAR_004341. FT VARIANT 123 123 Y -> F (in allele A*02:10 and allele FT A*02:17). FT /FTId=VAR_004342. FT VARIANT 131 131 W -> G (in allele A*02:10). FT /FTId=VAR_004343. FT VARIANT 162 162 M -> K (in allele A*02:18). FT /FTId=VAR_004344. FT VARIANT 173 173 A -> T (in allele A*02:03). FT /FTId=VAR_004345. FT VARIANT 176 176 V -> E (in allele A*02:03 and allele FT A*02:13). FT /FTId=VAR_004346. FT VARIANT 180 180 L -> Q (in allele A*02:12, allele A*02:13 FT and allele A*02:37). FT /FTId=VAR_004348. FT VARIANT 180 180 L -> W (in allele A*02:02, allele FT A*02:03, allele A*02:05 and allele FT A*02:08). FT /FTId=VAR_004347. FT VARIANT 187 187 T -> E (in allele A*02:16; requires 2 FT nucleotide substitutions). FT /FTId=VAR_004349. FT VARIANT 190 190 E -> D (in allele A*02:36 and allele FT A*02:37). FT /FTId=VAR_016729. FT VARIANT 191 191 W -> G (in allele A*02:36 and allele FT A*02:37). FT /FTId=VAR_016730. FT VARIANT 260 260 A -> E (in allele A*02:09). FT /FTId=VAR_004350. FT CONFLICT 115 115 G -> V (in Ref. 4; AAA52656). FT CONFLICT 140 140 Y -> V (in Ref. 4; AAA52656). FT CONFLICT 277 277 Q -> E (in Ref. 4; AAA52656). FT CONFLICT 318 318 F -> L (in Ref. 4; AAA52656). FT STRAND 27 36 FT STRAND 41 43 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT STRAND 70 73 FT HELIX 74 78 FT HELIX 81 108 FT STRAND 113 115 FT STRAND 118 127 FT STRAND 131 142 FT STRAND 145 150 FT STRAND 157 159 FT HELIX 162 173 FT HELIX 176 184 FT HELIX 187 198 FT HELIX 200 203 FT STRAND 210 235 FT STRAND 238 243 FT STRAND 246 248 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT STRAND 275 277 FT HELIX 278 280 FT STRAND 281 286 FT STRAND 290 292 FT STRAND 294 297 FT STRAND 348 350 SQ SEQUENCE 365 AA; 40922 MW; B54A97B24B337C08 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDGETRK VKAHSQTHRV DLGTLRGYYN QSEAGSHTVQ RMYGCDVGSD WRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A11_HUMAN Reviewed; 365 AA. AC P13746; O19605; O19606; Q29747; Q29835; Q5S3G1; Q9BCN0; Q9MYI5; AC Q9TQE9; Q9TQP6; Q9TQP7; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 09-JUL-2014, entry version 127. DE RecName: Full=HLA class I histocompatibility antigen, A-11 alpha chain; DE AltName: Full=MHC class I antigen A*11; DE Flags: Precursor; GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*11:01 AND A*11:02). RX PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES A*11:01 AND A*11:02). RX PubMed=8016845; DOI=10.1111/j.1399-0039.1994.tb02304.x; RA Lin L., Tokunaga K., Ishikawa Y., Bannai M., Kashiwase K., Kuwata S., RA Akaza T., Tadokoro K., Shibata Y., Juji T.; RT "Sequence analysis of serological HLA-A11 split antigens, A11.1 and RT A11.2."; RL Tissue Antigens 43:78-82(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*11:05). RX PubMed=10395112; DOI=10.1034/j.1399-0039.1999.530612.x; RA Morrell G., Whalley J., Stewart A., Day S., Lewis L., Makar Y., RA Ross J., Dunn P.P.; RT "Identification of an HLA-A11 serological variant and its RT characterization by sequencing based typing."; RL Tissue Antigens 53:591-594(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:03). RC TISSUE=Blood; RX PubMed=10703613; DOI=10.1034/j.1399-0039.2000.550113.x; RA Tijssen H.J., Sistermans E.A., van den Beucken M.J.G., Krausa P., RA Joosten I.; RT "Complete sequence analysis of the A*1103 allele."; RL Tissue Antigens 55:68-70(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:03). RC TISSUE=Blood; RX PubMed=10885562; DOI=10.1034/j.1399-0039.2000.550504.x; RA Tijssen H.J., Sistermans E.A., Joosten I.; RT "A unique second donor splice site in the intron 5 sequence of the RT HLA-A*11 alleles results in a class I transcript encoding a molecule RT with an elongated cytoplasmic domain."; RL Tissue Antigens 55:422-428(2000). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*11:05). RX PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:07). RX PubMed=11703829; DOI=10.1034/j.1399-0039.2001.580309.x; RA Pyo C.W., Choi H.B., Han H., Hong Y.S., Kim T.G.; RT "Identification of HLA-A*11 variant (A*1107) in the Korean RT population."; RL Tissue Antigens 58:190-192(2001). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:04) (ISOFORM 2). RX PubMed=17092262; DOI=10.1111/j.1399-0039.2006.00687.x; RA Sun Y., Liu S., Luo Y., Liang F., Xi Y.; RT "Identification and frequency of a novel HLA-A allele, A*110104."; RL Tissue Antigens 68:453-454(2006). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:04) (ISOFORM 2). RA Xu L.-H., Chi X.-Y., Jia Q.-T., Li F.-Y., Zha Q.-B., He X.-H.; RT "Cloning of high frequency HLA-B alleles from Chinese population."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*11:04). RA Bettinotti M.P.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-365 (ALLELE A*11:01). RX PubMed=2437024; DOI=10.1007/BF00404694; RA Cowan E.P., Jelachich M.L., Biddison W.E., Coligan J.E.; RT "DNA sequence of HLA-A11: remarkable homology with HLA-A3 allows RT identification of residues involved in epitopes recognized by RT antibodies and T cells."; RL Immunogenetics 25:241-250(1987). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*11:04). RA Chandanayingyong D., Sirikong M., Luangtrakool K., Srinak D., RA Rungroung E., Bejchandra S.; RT "A11 alleles (A*11O4)."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, VARIANT [LARGE RP SCALE ANALYSIS] SER-345, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 25-299 (ALLELE A*11:01) IN RP COMPLEX WITH SARS NUCLEOCAPSID PEPTIDE, AND DISULFIDE BONDS. RX PubMed=16041067; DOI=10.1107/S0907444905013090; RA Blicher T., Kastrup J.S., Buus S., Gajhede M.; RT "High-resolution structure of HLA-A*1101 in complex with SARS RT nucleocapsid peptide."; RL Acta Crystallogr. D 61:1031-1040(2005). RN [15] RP VARIANT [LARGE SCALE ANALYSIS] SER-345, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP VARIANT [LARGE SCALE ANALYSIS] THR-166, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P13746-1; Sequence=Displayed; CC Name=2; Synonyms=Long; CC IsoId=P13746-2; Sequence=VSP_008099; CC Note=Only produced by allele A*1103; CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-11 are known: A*11:01 (A- CC 11E), A*11:02 (A-11K), A*11:03, A*11:04, A*11:05 and A*11:07. The CC sequence shown is that of A*11:01. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X13111; CAA31503.1; -; mRNA. DR EMBL; X13112; CAA31504.1; -; mRNA. DR EMBL; D16841; BAA04117.1; -; mRNA. DR EMBL; D16842; BAA04118.1; -; mRNA. DR EMBL; AJ306733; CAC37336.1; -; Genomic_DNA. DR EMBL; X91399; CAA62745.1; -; mRNA. DR EMBL; Y17224; CAB38056.1; -; mRNA. DR EMBL; Y17224; CAB38057.1; -; mRNA. DR EMBL; AH007763; AAD33991.1; -; Genomic_DNA. DR EMBL; AF165065; AAF25781.1; -; mRNA. DR EMBL; DQ336694; ABC59611.1; -; mRNA. DR EMBL; AY786586; AAV53344.1; -; mRNA. DR EMBL; AY786587; AAV53345.1; -; mRNA. DR EMBL; U50574; AAB60406.1; -; mRNA. DR EMBL; AH003070; AAA65449.1; -; Genomic_DNA. DR EMBL; AH005647; AAB87052.1; -; Genomic_DNA. DR EMBL; AH005646; AAB87051.1; -; Genomic_DNA. DR PIR; I83063; I83063. DR PIR; S03536; A47636. DR UniGene; Hs.181244; -. DR UniGene; Hs.713441; -. DR PDB; 1Q94; X-ray; 2.40 A; A/D=25-299. DR PDB; 1QVO; X-ray; 2.22 A; A/D=25-299. DR PDB; 1X7Q; X-ray; 1.45 A; A=25-299. DR PDB; 2HN7; X-ray; 1.60 A; A=25-299. DR PDB; 4BEO; X-ray; 2.43 A; A/C=25-299. DR PDB; 4N8V; X-ray; 2.50 A; A/D=25-298. DR PDBsum; 1Q94; -. DR PDBsum; 1QVO; -. DR PDBsum; 1X7Q; -. DR PDBsum; 2HN7; -. DR PDBsum; 4BEO; -. DR PDBsum; 4N8V; -. DR ProteinModelPortal; P13746; -. DR SMR; P13746; 25-299. DR DMDM; 122157; -. DR MaxQB; P13746; -. DR PRIDE; P13746; -. DR Ensembl; ENST00000376809; ENSP00000366005; ENSG00000206503. DR Ensembl; ENST00000396634; ENSP00000379873; ENSG00000206503. DR GeneCards; GC06P029949; -. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR neXtProt; NX_P13746; -. DR HOVERGEN; HBG016709; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-A; human. DR EvolutionaryTrace; P13746; -. DR PRO; PR:P13746; -. DR ArrayExpress; P13746; -. DR Bgee; P13746; -. DR CleanEx; HS_HLA-A; -. DR Genevestigator; P13746; -. DR GO; GO:0009986; C:cell surface; IDA:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030881; F:beta-2-microglobulin binding; ISS:UniProt. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProt. DR GO; GO:0046977; F:TAP binding; IDA:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0042270; P:protection from natural killer cell mediated cytotoxicity; IDA:UniProt. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Disulfide bond; KW Glycoprotein; Host-virus interaction; Immunity; Membrane; MHC I; KW Phosphoprotein; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-11 alpha chain. FT /FTId=PRO_0000018816. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT MOD_RES 356 356 Phosphoserine. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 FT DISULFID 227 283 FT VAR_SEQ 337 337 S -> SGGEGVK (in isoform 2). FT /FTId=VSP_008099. FT VARIANT 43 43 E -> K (in allele A*11:02). FT /FTId=VAR_004353. FT VARIANT 89 89 R -> G (in dbSNP:rs1059459). FT /FTId=VAR_056254. FT VARIANT 94 94 Q -> H (in dbSNP:rs1059463). FT /FTId=VAR_056255. FT VARIANT 101 101 D -> N (in dbSNP:rs1136688). FT /FTId=VAR_056256. FT VARIANT 131 131 G -> W (in dbSNP:rs1136702). FT /FTId=VAR_056257. FT VARIANT 133 133 F -> L (in allele A*11:07; FT dbSNP:rs1059488). FT /FTId=VAR_016731. FT VARIANT 151 151 N -> K (in dbSNP:rs1059509). FT /FTId=VAR_056258. FT VARIANT 166 166 I -> T (in dbSNP:rs1059516). FT /FTId=VAR_056259. FT VARIANT 168 168 K -> E (in allele A*11:05). FT /FTId=VAR_016732. FT VARIANT 169 169 R -> H (in dbSNP:rs1059520). FT /FTId=VAR_056260. FT VARIANT 175 175 H -> R (in allele A*11:03). FT /FTId=VAR_016733. FT VARIANT 176 176 A -> E (in allele A*11:03). FT /FTId=VAR_016734. FT VARIANT 187 187 R -> T (in allele A*11:04). FT /FTId=VAR_016735. FT VARIANT 205 205 R -> H (in dbSNP:rs17185861). FT /FTId=VAR_056261. FT VARIANT 345 345 T -> S (in allele A*11:05). FT /FTId=VAR_016736. FT STRAND 27 36 FT STRAND 41 43 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT HELIX 74 76 FT HELIX 81 108 FT STRAND 113 115 FT STRAND 118 127 FT STRAND 133 142 FT STRAND 145 150 FT STRAND 157 159 FT HELIX 162 173 FT HELIX 176 185 FT HELIX 187 198 FT HELIX 200 203 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT STRAND 246 248 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT HELIX 278 280 FT STRAND 281 286 FT STRAND 288 292 FT STRAND 294 297 SQ SEQUENCE 365 AA; 40937 MW; FE449CE2D4BF6CC5 CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEDGSHTIQ IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHAAEQQ RAYLEGRCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A24_HUMAN Reviewed; 365 AA. AC P05534; P30448; P30449; Q29908; Q29909; Q29910; Q95355; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2003, sequence version 2. DT 09-JUL-2014, entry version 147. DE RecName: Full=HLA class I histocompatibility antigen, A-24 alpha chain; DE AltName: Full=Aw-24; DE AltName: Full=HLA class I histocompatibility antigen, A-9 alpha chain; DE AltName: Full=MHC class I antigen A*24; DE Flags: Precursor; GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*2401). RX PubMed=2987115; DOI=10.1007/BF00430931; RA N'Guyen C., Sodoyer R., Trucy J., Strachan T., Jordan B.R.; RT "The HLA-AW24 gene: sequence, surroundings and comparison with the RT HLA-A2 and HLA-A3 genes."; RL Immunogenetics 21:479-489(1985). RN [2] RP SEQUENCE REVISION. RA Jordan B.R.; RL Submitted (JUL-1988) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELES A*24:02 AND RP A*24:03). RX PubMed=1729171; DOI=10.1007/BF00216625; RA Little A.-M., Madrigal J.A., Parham P.; RT "Molecular definition of an elusive third HLA-A9 molecule: HLA-A9.3."; RL Immunogenetics 35:41-45(1992). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE A*24:02). RX PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*24:02). RX PubMed=9349616; DOI=10.1111/j.1399-0039.1997.tb02884.x; RA Laforet M., Froelich N., Parissiadis A., Bausinger H., Pfeiffer B., RA Tongio M.M.; RT "An intronic mutation responsible for a low level of expression of an RT HLA-A*24 allele."; RL Tissue Antigens 50:340-346(1997). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE A*24:08). RC TISSUE=Blood; RA Kashiwase K., Tokunaga K., Ishikawa Y., Qiu L., Furuya M., RA Sawanaka K., Akaza T., Tadokoro K., Juji T.; RT "Sequence analysis of a serological subtype, HLA-A9HH, observed in RT Japanese and the confirmatory sequence of A*2408."; RL MHC 3:9-14(1996). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-337 (ALLELE A*24:29). RA Dunn P.; RT "Confirmation of the sequence of HLA-A*2429 allele found in a RT potential bone marrow donor."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*24:10). RC TISSUE=Blood; RX PubMed=9008316; DOI=10.1111/j.1399-0039.1996.tb02697.x; RA Gao X., Matheson B.; RT "A novel HLA-A*24 (A*2410) identified in a Javanese population."; RL Tissue Antigens 48:711-713(1996). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES A*24:06; A*24:13 RP AND A*24:14). RC TISSUE=Blood; RX PubMed=9271829; DOI=10.1111/j.1399-0039.1997.tb02858.x; RA Gao X., Lester S., Matheson B., Boettcher B., McCluskey J.; RT "Three newly identified A*24 alleles: A*2406, A*2413 and A*2414."; RL Tissue Antigens 50:192-196(1997). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 25-298 (ALLELE A*24:02) IN RP COMPLEX WITH B2M AND CD8, AND DISULFIDE BONDS. RX PubMed=21645925; DOI=10.1016/j.molimm.2011.05.009; RA Shi Y., Qi J., Iwamoto A., Gao G.F.; RT "Plasticity of human CD8alphaalpha binding to peptide-HLA-A*2402."; RL Mol. Immunol. 48:2198-2202(2011). RN [14] RP VARIANT [LARGE SCALE ANALYSIS] TRP-180, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-24 are known: A*2401, CC A*24:02, A*24:03, A*24:06, A*24:08 (A9HH), A*24:10 (A*24JV), CC A*24:13 (A*24YM), A*24:14 (A*24SA) and A*24:29. Allele A*24:02 is CC represented in all major racial groups. Allele A*24:06 and allele CC A*24:13 are found in the Australian Aboriginal population. Allele CC A*24:14 is found in individuals of South American descent. The CC sequence shown is that of A*24:02. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M15497; AAA59611.1; -; Genomic_DNA. DR EMBL; M64740; AAA59600.1; -; mRNA. DR EMBL; M64741; AAA59601.1; -; Genomic_DNA. DR EMBL; Z72422; CAA96532.1; -; Genomic_DNA. DR EMBL; D83516; BAA11936.1; -; mRNA. DR EMBL; U37111; AAA83264.1; -; Genomic_DNA. DR EMBL; U37110; AAA83264.1; JOINED; Genomic_DNA. DR EMBL; U37113; AAA83265.1; -; Genomic_DNA. DR EMBL; U37112; AAA83265.1; JOINED; Genomic_DNA. DR EMBL; AH004915; AAB40048.1; -; Genomic_DNA. DR EMBL; AH005378; AAB60651.1; -; Genomic_DNA. DR PIR; I54416; I54416. DR UniGene; Hs.181244; -. DR UniGene; Hs.713441; -. DR PDB; 2BCK; X-ray; 2.80 A; A/D=25-300. DR PDB; 3I6L; X-ray; 2.40 A; D=25-298. DR PDB; 3NFN; X-ray; 2.39 A; A=25-298. DR PDB; 3QZW; X-ray; 2.80 A; A/D=25-298. DR PDB; 3VXM; X-ray; 2.50 A; A=25-298. DR PDB; 3VXN; X-ray; 1.95 A; A=25-298. DR PDB; 3VXO; X-ray; 2.61 A; A/D=25-298. DR PDB; 3VXP; X-ray; 2.50 A; A/D=25-298. DR PDB; 3VXR; X-ray; 2.40 A; A=25-298. DR PDB; 3VXS; X-ray; 1.80 A; A=25-298. DR PDB; 3VXU; X-ray; 2.70 A; A/F=25-298. DR PDB; 3W0W; X-ray; 2.60 A; A=25-298. DR PDB; 4F7M; X-ray; 2.40 A; A/D=25-298. DR PDB; 4F7P; X-ray; 1.90 A; A=25-298. DR PDB; 4F7T; X-ray; 1.70 A; A/D=25-298. DR PDBsum; 2BCK; -. DR PDBsum; 3I6L; -. DR PDBsum; 3NFN; -. DR PDBsum; 3QZW; -. DR PDBsum; 3VXM; -. DR PDBsum; 3VXN; -. DR PDBsum; 3VXO; -. DR PDBsum; 3VXP; -. DR PDBsum; 3VXR; -. DR PDBsum; 3VXS; -. DR PDBsum; 3VXU; -. DR PDBsum; 3W0W; -. DR PDBsum; 4F7M; -. DR PDBsum; 4F7P; -. DR PDBsum; 4F7T; -. DR ProteinModelPortal; P05534; -. DR SMR; P05534; 25-298. DR DMDM; 32363482; -. DR MaxQB; P05534; -. DR PaxDb; P05534; -. DR PRIDE; P05534; -. DR Ensembl; ENST00000431930; ENSP00000406366; ENSG00000229215. DR Ensembl; ENST00000443552; ENSP00000404678; ENSG00000224320. DR GeneCards; GC06P029949; -. DR GeneCards; GC06Pi29846; -. DR GeneCards; GC06Pj29898; -. DR H-InvDB; HIX0165910; -. DR H-InvDB; HIX0165954; -. DR H-InvDB; HIX0166079; -. DR H-InvDB; HIX0166152; -. DR H-InvDB; HIX0166432; -. DR H-InvDB; HIX0166685; -. DR H-InvDB; HIX0166954; -. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR neXtProt; NX_P05534; -. DR eggNOG; NOG42056; -. DR HOVERGEN; HBG016709; -. DR PhylomeDB; P05534; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-A; human. DR EvolutionaryTrace; P05534; -. DR PRO; PR:P05534; -. DR CleanEx; HS_HLA-A; -. DR Genevestigator; P05534; -. DR GO; GO:0009986; C:cell surface; ISS:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030881; F:beta-2-microglobulin binding; ISS:UniProt. DR GO; GO:0042605; F:peptide antigen binding; IEA:InterPro. DR GO; GO:0046977; F:TAP binding; IDA:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Host-virus interaction; Immunity; Membrane; MHC I; Phosphoprotein; KW Polymorphism; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-24 alpha chain. FT /FTId=PRO_0000018818. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT MOD_RES 356 356 Phosphoserine. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 5 5 A -> G (in allele A*2401). FT /FTId=VAR_004354. FT VARIANT 27 27 H -> Q (in allele A*24:08; FT dbSNP:rs41541319). FT /FTId=VAR_004355. FT VARIANT 86 86 E -> G (in allele A*24:08). FT /FTId=VAR_004356. FT VARIANT 89 89 G -> R (in allele A*24:08 and allele FT A*24:29). FT /FTId=VAR_004357. FT VARIANT 119 119 L -> V (in allele A*24:14). FT /FTId=VAR_015765. FT VARIANT 121 121 M -> R (in allele A*24:14). FT /FTId=VAR_015766. FT VARIANT 123 123 F -> Y (in allele A*24:14). FT /FTId=VAR_015767. FT VARIANT 131 131 G -> W (in allele A*24:14). FT /FTId=VAR_015768. FT VARIANT 180 180 Q -> L (in allele A*24:13). FT /FTId=VAR_015769. FT VARIANT 180 180 Q -> W (in allele A*24:06; requires 2 FT nucleotide substitutions). FT /FTId=VAR_004358. FT VARIANT 187 187 T -> R (in allele A*24:10). FT /FTId=VAR_015770. FT VARIANT 190 191 DG -> EW (in allele A*24:03 and allele FT A*24:10). FT /FTId=VAR_004359. FT VARIANT 205 205 R -> H (in dbSNP:rs17185861). FT /FTId=VAR_056263. FT VARIANT 206 206 T -> A (in allele A*2401). FT /FTId=VAR_004360. FT STRAND 27 36 FT TURN 39 41 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT STRAND 70 73 FT HELIX 74 78 FT HELIX 81 109 FT STRAND 113 115 FT STRAND 118 127 FT STRAND 133 142 FT STRAND 145 150 FT STRAND 157 159 FT HELIX 162 173 FT HELIX 176 185 FT HELIX 187 198 FT HELIX 200 203 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 246 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT STRAND 280 286 FT STRAND 290 292 FT STRAND 294 296 FT STRAND 298 300 SQ SEQUENCE 365 AA; 40689 MW; D33684D126F98EC3 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDEETGK VKAHSQTDRE NLRIALRYYN QSEAGSHTLQ MMFGCDVGSD GRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQITKRK WEAAHVAEQQ RAYLEGTCVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTVPIVG IIAGLVLLGA VITGAVVAAV MWRRNSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A30_HUMAN Reviewed; 365 AA. AC P16188; O19598; O62921; P30452; Q9UIP7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 2. DT 09-JUL-2014, entry version 120. DE RecName: Full=HLA class I histocompatibility antigen, A-30 alpha chain; DE AltName: Full=MHC class I antigen A*30; DE Flags: Precursor; GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*30:01). RX PubMed=2478623; RA Kato K., Trapani J.A., Allopenna J., Dupont B., Yang S.Y.; RT "Molecular analysis of the serologically defined HLA-Aw19 antigens. A RT genetically distinct family of HLA-A antigens comprising A29, A31, RT A32, and Aw33, but probably not A30."; RL J. Immunol. 143:3371-3378(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*30:01). RX PubMed=7871528; DOI=10.1111/j.1399-0039.1994.tb02393.x; RA Olerup O., Daniels T.J., Baxter-Lowe L.; RT "Correct sequence of the A*3001 allele obtained by PCR-SSP typing and RT automated nucleotide sequencing."; RL Tissue Antigens 44:265-267(1994). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE A*30:02). RX PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-279 (ALLELE A*30:03). RX PubMed=8458735; DOI=10.1016/0198-8859(93)90004-K; RA Choo S.Y., Starling G.C., Anasetti C., Hansen J.A.; RT "Selection of an unrelated donor for marrow transplantation RT facilitated by the molecular characterization of a novel HLA-A RT allele."; RL Hum. Immunol. 36:20-26(1993). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*30:04). RX PubMed=8522453; DOI=10.1016/0198-8859(95)00046-7; RA Krausa P., Carcassi C., Orru S., Bodmer J.G., Browning M.J., Contu L.; RT "Defining the allelic variants of HLA-A30 in the Sardinian population RT using amplification refractory mutation system -- polymerase chain RT reaction."; RL Hum. Immunol. 44:35-42(1995). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 26-206 (ALLELE A*30:04). RX PubMed=8838350; DOI=10.1111/j.1399-0039.1995.tb03133.x; RA Lienert K., Russ G., Bennett G., Gao X., McCluskey J.; RT "HLA-A*3004: a new A30 allele identified in an Australian Caucasoid RT population."; RL Tissue Antigens 46:394-397(1995). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-205 (ALLELE A*30:04). RX PubMed=8560452; DOI=10.1111/j.1399-0039.1995.tb02500.x; RA Blasczyk R., Wehling J., Paessler M., Hahn U., Huhn D., Salama A.; RT "A novel HLA-A30 allele (A*3004) identified by single-strand RT conformation polymorphism analysis and confirmed by solid-phase RT sequencing."; RL Tissue Antigens 46:322-326(1995). RN [8] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*30:06). RX PubMed=11098929; DOI=10.1034/j.1399-0039.2000.560401.x; RA Ellis J.M., Mack S.J., Leke R.F.G., Quakyi I., Johnson A.H., RA Hurley C.K.; RT "Diversity is demonstrated in class I HLA-A and HLA-B alleles in RT Cameroon, Africa: description of HLA-A*03012, *2612, *3006 and HLA- RT B*1403, *4016, *4703."; RL Tissue Antigens 56:291-302(2000). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*30:07). RX PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [10] RP NUCLEOTIDE SEQUENCE (ALLELE A*30:08). RX PubMed=11169261; DOI=10.1034/j.1399-0039.2001.057001070.x; RA Cox S.T., Mcwhinnie A.J., Koester R.P., Heine U., Holman R., RA Madrigal A.J., Little A.-M.; RT "Further diversity at HLA-A and -B loci identified in Afro-Caribbean RT potential bone marrow donors."; RL Tissue Antigens 57:70-72(2001). RN [11] RP VARIANT [LARGE SCALE ANALYSIS] GLY-80, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-30 are known: A*30:01 CC (A30.3), A*30:02, A*30:03, A*30:04 (A30W7), A*30:06, A*30:07 and CC A*30:08. The sequence shown is that of A*30:01. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M30576; AAA59612.1; -; Genomic_DNA. DR EMBL; U07234; AAA70162.1; -; mRNA. DR EMBL; X61702; CAA43871.1; -; mRNA. DR EMBL; M93657; AAA58650.1; -; Genomic_DNA. DR EMBL; Z34921; CAA84401.1; -; Genomic_DNA. DR EMBL; AH005195; AAB53658.1; -; Genomic_DNA. DR EMBL; U24261; AAB50434.1; -; mRNA. DR EMBL; X83770; CAA58723.1; -; Genomic_DNA. DR EMBL; X83771; CAA58724.1; -; Genomic_DNA. DR EMBL; AH006045; AAC14191.1; -; Genomic_DNA. DR EMBL; AH006148; AAC18600.1; -; Genomic_DNA. DR EMBL; AJ249308; CAB57306.1; -; Genomic_DNA. DR EMBL; AJ249309; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249310; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249311; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249312; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249313; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249314; CAB57306.1; JOINED; Genomic_DNA. DR EMBL; AJ249315; CAB57306.1; JOINED; Genomic_DNA. DR PIR; I38519; I38519. DR PIR; I54307; I54307. DR PIR; I56039; I56039. DR ProteinModelPortal; P16188; -. DR SMR; P16188; 25-298. DR DMDM; 1345596; -. DR MaxQB; P16188; -. DR PRIDE; P16188; -. DR Ensembl; ENST00000376809; ENSP00000366005; ENSG00000206503. DR Ensembl; ENST00000396634; ENSP00000379873; ENSG00000206503. DR GeneCards; GC06P029949; -. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR neXtProt; NX_P16188; -. DR HOVERGEN; HBG016709; -. DR TreeFam; TF336617; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-A; human. DR NextBio; 35537752; -. DR ArrayExpress; P16188; -. DR Bgee; P16188; -. DR CleanEx; HS_HLA-A; -. DR Genevestigator; P16188; -. DR GO; GO:0009986; C:cell surface; ISS:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030881; F:beta-2-microglobulin binding; ISS:UniProt. DR GO; GO:0042605; F:peptide antigen binding; IEA:InterPro. DR GO; GO:0046977; F:TAP binding; IDA:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; KW Host-virus interaction; Immunity; Membrane; MHC I; Phosphoprotein; KW Polymorphism; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-30 alpha chain. FT /FTId=PRO_0000018822. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT MOD_RES 356 356 Phosphoserine (By similarity). FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 21 21 H -> Q (in allele A*30:02, allele A*30:04 FT and allele A*30:08). FT /FTId=VAR_004366. FT VARIANT 33 33 S -> Y (in allele A*30:08). FT /FTId=VAR_010284. FT VARIANT 55 55 T -> A (in allele A*30:06). FT /FTId=VAR_016653. FT VARIANT 80 80 R -> G (in allele A*30:03). FT /FTId=VAR_004367. FT VARIANT 86 86 Q -> E (in allele A*30:07). FT /FTId=VAR_016738. FT VARIANT 89 90 RN -> GK (in allele A*30:07). FT /FTId=VAR_016739. FT VARIANT 89 89 R -> G (in dbSNP:rs1059459). FT /FTId=VAR_056271. FT VARIANT 94 94 Q -> H (in allele A*30:02, allele FT A*30:03, allele A*30:04, allele A*30:06 FT and allele A*30:07; dbSNP:rs1059463). FT /FTId=VAR_004368. FT VARIANT 100 101 VD -> EN (in allele A*30:02, allele FT A*30:03, allele A*30:04, allele A*30:06 FT and allele A*30:07). FT /FTId=VAR_004369. FT VARIANT 101 101 D -> N (in dbSNP:rs1136688). FT /FTId=VAR_056272. FT VARIANT 121 121 I -> M (in dbSNP:rs1136695). FT /FTId=VAR_056273. FT VARIANT 129 129 S -> P (in dbSNP:rs1136700). FT /FTId=VAR_056274. FT VARIANT 131 131 G -> W (in dbSNP:rs1136702). FT /FTId=VAR_056275. FT VARIANT 133 133 F -> L (in dbSNP:rs1059488). FT /FTId=VAR_056276. FT VARIANT 151 151 N -> K (in dbSNP:rs1059509). FT /FTId=VAR_056277. FT VARIANT 166 166 I -> T (in dbSNP:rs1059516). FT /FTId=VAR_056278. FT VARIANT 175 176 RW -> HV (in allele A*30:04 and allele FT A*30:06). FT /FTId=VAR_004370. FT VARIANT 176 176 W -> R (in allele A*30:02, allele A*30:03 FT and allele A*30:07). FT /FTId=VAR_004371. FT VARIANT 180 180 L -> W (in allele A*30:04 and allele FT A*30:06). FT /FTId=VAR_004372. FT VARIANT 205 205 R -> H (in dbSNP:rs17185861). FT /FTId=VAR_056279. FT CONFLICT 33 33 S -> F (in Ref. 1; AAA59612). SQ SEQUENCE 365 AA; 40905 MW; 521166D95FB1DC28 CRC64; MAVMAPRTLL LLLSGALALT HTWAGSHSMR YFSTSVSRPG SGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQER PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ IMYGCDVGSD GRFLRGYEQH AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARWAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A68_HUMAN Reviewed; 365 AA. AC P01891; O19673; O19695; O19794; O19795; O43907; O77938; O98010; AC P10315; P79505; Q9MYA5; Q9MYC4; Q9TQG7; Q9TQN5; Q9UIN2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 4. DT 09-JUL-2014, entry version 144. DE RecName: Full=HLA class I histocompatibility antigen, A-68 alpha chain; DE AltName: Full=Aw-68; DE AltName: Full=HLA class I histocompatibility antigen, A-28 alpha chain; DE AltName: Full=MHC class I antigen A*68; DE Flags: Precursor; GN Name=HLA-A; Synonyms=HLAA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE A*68:02). RX PubMed=3496393; RA Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.; RT "Multiple genetic mechanisms have contributed to the generation of the RT HLA-A2/A28 family of class I MHC molecules."; RL J. Immunol. 139:936-941(1987). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE A*68:02). RA Domena J.D.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE A*68:03). RX PubMed=8881043; DOI=10.1007/s002510050172; RA Ellexson M., Lau M., Terasaki P., Hildebrand W.H.; RT "Molecular characterization of HLA-A*6803."; RL Immunogenetics 45:78-79(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*68:08). RX PubMed=10395114; DOI=10.1034/j.1399-0039.1999.530614.x; RA Cox S.T., Arguello J.R., Marsh S.G.E., Boham E., Lau M., Kwan P.L., RA Madrigal J.A., Little A.-M.; RT "Sequence of HLA-A*6808."; RL Tissue Antigens 53:597-600(1999). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELE A*68:011). RC TISSUE=Blood; RA Cox S.T.; RT "Confirmation of HLA-A*68011."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A*68:17). RX PubMed=10885567; DOI=10.1034/j.1399-0039.2000.550509.x; RA Ramon D., Scott I., Cox S.T., Pesoa S., Vullo C., Little A.-M., RA Madrigal J.A.; RT "HLA-A*6817, identified in the Kolla Amerindians of north-west RT Argentina possesses a novel nucleotide substitution."; RL Tissue Antigens 55:453-454(2000). RN [7] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*68:06). RA Bei M., Hurley C.K.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE A*68:03). RC TISSUE=Blood; RX PubMed=9271640; DOI=10.1007/s002510050304; RA Vargas-Alarcon G., Martinez-Laso J., Gomez-Casado E., Perez-Blas M., RA Granados J., Alegre R., Alvarez M., Zuniga J., Arnaiz-Villena A.; RT "Description of HLA-A*6803 and A*68N in Mazatecan Indians from RT Mexico."; RL Immunogenetics 46:446-447(1997). RN [9] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*68:03). RC TISSUE=Blood; RA Blasczyk R.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE A*68:02). RA Edson S.M., Hurley C.K.; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*68:09 AND A*68:10). RX PubMed=10852390; DOI=10.1034/j.1399-0039.2000.550412.x; RA Ellis J., Steiner N.K., Kosman C., Henson V., Mitton W., Koester R., RA Ng J., Hartzman R.J., Hurley C.K.; RT "Seventeen more novel HLA-A locus alleles."; RL Tissue Antigens 55:369-373(2000). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-206 (ALLELE A*68:16). RX PubMed=10803837; DOI=10.1007/s002510050618; RA Gomez-Casado E., Martinez-Laso J., Gonzalez-Hevilla M., Longas J., RA Rubio I., Silvera-Redondo C., Garcia-Gomez A., Lowy E., RA Arnaiz-Villena A.; RT "A novel HLA-A*6816 allele possible generated by a point mutation in a RT Chilean from Punta Arenas (Magellan Strait)."; RL Immunogenetics 51:257-260(2000). RN [13] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES A*68:07 AND A*68:17). RX PubMed=11260503; DOI=10.1034/j.1399-0039.2001.057002095.x; RA Hickman H.D., Cavett J.W., Ellexson-Turner M.E., Sparkman J.N., RA Bennett T.T., Turner S., Sidebottom D.A., Trachtenberg E.A., RA Confer D.L., Hildebrand W.H.; RT "Non-conservative substitutions distinguish previously uncharacterized RT HLA-A molecules."; RL Tissue Antigens 57:95-102(2001). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-297 (ALLELE A*68:01). RX PubMed=3877632; RA Holmes N., Parham P.; RT "Exon shuffling in vivo can generate novel HLA class I molecules."; RL EMBO J. 4:2849-2854(1985). RN [15] RP PROTEIN SEQUENCE OF 25-294 (A*68:01). RX PubMed=6179086; DOI=10.1073/pnas.79.12.3813; RA Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.; RT "Structure of crossreactive human histocompatibility antigens HLA-A28 RT and HLA-A2: possible implications for the generation of HLA RT polymorphism."; RL Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (A*68:01). RX PubMed=1448153; DOI=10.1038/360364a0; RA Guo H.-C., Jardetzky T.S., Garrett T.P.J., Lane W.S., Strominger J.L., RA Wiley D.C.; RT "Different length peptides bind to HLA-Aw68 similarly at their ends RT but bulge out in the middle."; RL Nature 360:364-366(1992). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (A*68:01). RX PubMed=1448154; DOI=10.1038/360367a0; RA Silver M.L., Guo H.-C., Strominger J.L., Wiley D.C.; RT "Atomic structure of a human MHC molecule presenting an influenza RT virus peptide."; RL Nature 360:367-369(1992). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-199 (A*68:01). RX PubMed=7862664; DOI=10.1073/pnas.92.4.1218; RA Collins E.J., Garboczi D.N., Karpusas M.N., Wiley D.C.; RT "The three-dimensional structure of a class I major histocompatibility RT complex molecule missing the alpha 3 domain of the heavy chain."; RL Proc. Natl. Acad. Sci. U.S.A. 92:1218-1221(1995). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of A-68 are known: A*68:01 CC (Aw68.1), A*68:02, A*68:03. A*68:04, A*68:05, A*68:06, A*68:07, CC A*68:08, A*68:09, A*68:10, A*68:16 and A*68:17. The sequence shown CC is that of A*68:01. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U03861; AAA03602.1; -; mRNA. DR EMBL; X03070; CAB56605.1; -; Genomic_DNA. DR EMBL; X03071; CAB56606.1; -; Genomic_DNA. DR EMBL; U41057; AAB41292.1; -; mRNA. DR EMBL; AJ315642; CAC44382.1; -; Genomic_DNA. DR EMBL; AF144013; AAF74211.1; -; Genomic_DNA. DR EMBL; AJ245567; CAB59722.1; -; Genomic_DNA. DR EMBL; AH005127; AAB50567.1; -; Genomic_DNA. DR EMBL; U89946; AAB82079.1; -; Genomic_DNA. DR EMBL; U89947; AAB82080.1; -; Genomic_DNA. DR EMBL; AJ001274; CAA04647.1; -; mRNA. DR EMBL; AH006296; AAC25782.1; -; Genomic_DNA. DR EMBL; AH007538; AAD22270.1; -; Genomic_DNA. DR EMBL; AH007605; AAD27539.1; -; Genomic_DNA. DR EMBL; AJ223972; CAA11708.1; -; Genomic_DNA. DR EMBL; AH007201; AAD02208.1; -; Genomic_DNA. DR EMBL; AH009406; AAF73477.1; -; Genomic_DNA. DR PIR; A02187; HLHU28. DR PIR; A24671; HLHUAW. DR PIR; I38441; I38441. DR UniGene; Hs.181244; -. DR UniGene; Hs.713441; -. DR PDB; 1HSB; X-ray; 1.90 A; A=25-294. DR PDB; 1TMC; X-ray; 2.30 A; A=25-199. DR PDB; 2HLA; X-ray; 2.60 A; A=25-294. DR PDB; 4HWZ; X-ray; 2.40 A; A=25-298. DR PDB; 4HX1; X-ray; 1.80 A; A=25-296. DR PDB; 4I48; X-ray; 2.80 A; A=25-296. DR PDBsum; 1HSB; -. DR PDBsum; 1TMC; -. DR PDBsum; 2HLA; -. DR PDBsum; 4HWZ; -. DR PDBsum; 4HX1; -. DR PDBsum; 4I48; -. DR ProteinModelPortal; P01891; -. DR SMR; P01891; 25-294. DR MINT; MINT-274751; -. DR DMDM; 13124681; -. DR MaxQB; P01891; -. DR PRIDE; P01891; -. DR Ensembl; ENST00000457879; ENSP00000403575; ENSG00000235657. DR GeneCards; GC06P029949; -. DR GeneCards; GC06Pk29899; -. DR HGNC; HGNC:4931; HLA-A. DR MIM; 142800; gene. DR neXtProt; NX_P01891; -. DR HOVERGEN; HBG016709; -. DR PhylomeDB; P01891; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-A; human. DR EvolutionaryTrace; P01891; -. DR CleanEx; HS_HLA-A; -. DR Genevestigator; P01891; -. DR GO; GO:0009986; C:cell surface; ISS:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030881; F:beta-2-microglobulin binding; ISS:UniProt. DR GO; GO:0042605; F:peptide antigen binding; IEA:InterPro. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Host-virus interaction; Immunity; KW Membrane; MHC I; Phosphoprotein; Polymorphism; Reference proteome; KW Signal; Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 365 HLA class I histocompatibility antigen, FT A-68 alpha chain. FT /FTId=PRO_0000018830. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 365 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT MOD_RES 356 356 Phosphoserine. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 36 36 V -> M (in allele A*68:02). FT /FTId=VAR_004389. FT VARIANT 86 87 RN -> EE (in allele A*68:10). FT /FTId=VAR_010362. FT VARIANT 89 89 R -> G (in dbSNP:rs1059459). FT /FTId=VAR_056304. FT VARIANT 94 94 Q -> H (in allele A*68:03, allele A*68:04 FT and allele A*68:05; dbSNP:rs1059463). FT /FTId=VAR_010363. FT VARIANT 97 97 T -> I (in allele A*68:04). FT /FTId=VAR_010364. FT VARIANT 98 98 D -> H (in allele A*68:05). FT /FTId=VAR_010365. FT VARIANT 101 101 D -> N (in dbSNP:rs1136688). FT /FTId=VAR_056305. FT VARIANT 121 121 M -> R (in allele A*68:02). FT /FTId=VAR_004390. FT VARIANT 129 129 S -> P (in allele A*68:02; FT dbSNP:rs1136700). FT /FTId=VAR_004391. FT VARIANT 133 133 F -> L (in dbSNP:rs1059488). FT /FTId=VAR_056306. FT VARIANT 138 138 R -> E (in allele A*68:06; requires 2 FT nucleotide substitutions). FT /FTId=VAR_010366. FT VARIANT 138 138 R -> H (in allele A*68:02). FT /FTId=VAR_004392. FT VARIANT 140 140 D -> H (in allele A*68:06 and allele FT A*68:07). FT /FTId=VAR_010367. FT VARIANT 140 140 D -> V (in allele A*68:17). FT /FTId=VAR_010368. FT VARIANT 140 140 D -> Y (in allele A*68:02). FT /FTId=VAR_004393. FT VARIANT 175 175 H -> L (in allele A*68:16). FT /FTId=VAR_010369. FT VARIANT 180 180 W -> L (in allele A*68:08). FT /FTId=VAR_010370. FT VARIANT 180 180 W -> Q (in allele A*68:09; requires 2 FT nucleotide substitutions). FT /FTId=VAR_010371. FT CONFLICT 206 206 T -> A (in Ref. 12; AAF74211). FT CONFLICT 231 231 S -> G (in Ref. 15; AA sequence). FT STRAND 27 36 FT STRAND 41 43 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT HELIX 74 76 FT HELIX 81 108 FT STRAND 113 115 FT STRAND 118 127 FT STRAND 133 142 FT STRAND 145 150 FT STRAND 154 161 FT HELIX 162 173 FT HELIX 176 185 FT HELIX 187 198 FT HELIX 200 203 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT STRAND 246 248 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT HELIX 278 280 FT STRAND 281 286 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 365 AA; 40909 MW; 78539C59DB8B1DFC CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ MMYGCDVGSD GRFLRGYRQD AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQW RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWVA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1B07_HUMAN Reviewed; 362 AA. AC P01889; Q29638; Q29681; Q29854; Q29861; Q31613; Q5SRJ2; Q9GIX1; AC Q9TP95; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 3. DT 09-JUL-2014, entry version 151. DE RecName: Full=HLA class I histocompatibility antigen, B-7 alpha chain; DE AltName: Full=MHC class I antigen B*7; DE Flags: Precursor; GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:02). RX PubMed=2320591; DOI=10.1073/pnas.87.7.2833; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:02). RX PubMed=2700944; RA Parham P., Benjamin R.J., Chen B.P., Clayberger C., Ennis P.D., RA Krensky A.M., Lawlor D.A., Littman D.R., Norment A.M., Orr H.T., RA Salter R.D., Zemmour J.; RT "Diversity of class I HLA molecules: functional and evolutionary RT interactions with T cells."; RL Cold Spring Harb. Symp. Quant. Biol. 54:529-543(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:02). RX PubMed=2993161; DOI=10.1007/BF00563508; RA Sood A.K., Pan J., Biro P.A., Pereira D., Srivastava R., Reddy V.B., RA Duceman B.W., Weissman S.M.; RT "Structure and polymorphism of class I MHC antigen mRNA."; RL Immunogenetics 22:101-121(1985). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:02). RA Ellexson M.E., Zhang L., Hildebrand W.H.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:03). RX PubMed=8106270; DOI=10.1016/0198-8859(93)90533-7; RA Bergmans A., Tijssen H., Lardy J., Reekers P.; RT "Complete nucleotide sequence of HLA-B*0703, a B7-variant (BPOT)."; RL Hum. Immunol. 38:159-162(1993). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:04). RX PubMed=7652739; DOI=10.1111/j.1399-0039.1995.tb02461.x; RA Kubens B.S., Arnett K.L., Adams E.J., Parham P., Grosse-Wilde H.; RT "Definition of a new HLA-B7 subtype (B*0704) by isoelectric focusing, RT family studies and DNA sequence analysis."; RL Tissue Antigens 45:322-327(1995). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:05). RX PubMed=7878658; DOI=10.1111/j.1399-0039.1994.tb02402.x; RA Arnett K.L., Adams E.J., Domena J.D., Parham P.; RT "Structure of a novel subtype of B7 (B*0705) isolated from a Chinese RT individual."; RL Tissue Antigens 44:318-321(1994). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*07:03 AND B*07:05). RX PubMed=8537119; RA Smith K.D., Epperson D.F., Lutz C.T.; RT "Alloreactive cytotoxic T-lymphocyte-defined HLA-B7 subtypes differ in RT peptide antigen presentation."; RL Immunogenetics 43:27-37(1996). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*07:06). RX PubMed=8773323; DOI=10.1111/j.1399-0039.1996.tb02561.x; RA Sanz L., Vilches C., de Pablo R., Bunce M., Moreno M.E., Kreisler M.; RT "Haplotypic association of two new HLA class I alleles: Cw*15052 and RT B*0706: evolutionary relationships of HLA-Cw*15 alleles."; RL Tissue Antigens 47:329-332(1996). RN [10] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:18). RA Bettinotti M.P., Hadzikadic L., Dhillon G., Barracchini K., RA Marincola F.M.; RT "A new HLA-B allele."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:02). RA Marsh S.G.E.; RT "Intron sequences of HLA class I."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE (ALLELE B*07:02). RC TISSUE=Blood; RX PubMed=12622774; DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Subthalamic nucleus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*07:24). RC TISSUE=Peripheral blood; RX PubMed=11556973; DOI=10.1034/j.1399-0039.2001.057005471.x; RA Middleton D., Curran M.D., Anholts J.D., Reilly E.R., Schreuder G.M.; RT "Characterisation of a new HLA-B allele, HLA-B*0724."; RL Tissue Antigens 57:471-473(2001). RN [16] RP PROTEIN SEQUENCE OF 25-295 (B*07:02). RX PubMed=518865; DOI=10.1021/bi00592a030; RA Orr H.T., Lopez de Castro J.A., Lancet D., Strominger J.L.; RT "Complete amino acid sequence of a papain-solubilized human RT histocompatibility antigen, HLA-B7. 2. Sequence determination and RT search for homologies."; RL Biochemistry 18:5711-5720(1979). RN [17] RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I. RX PubMed=11390610; DOI=10.1128/JVI.75.13.6086-6094.2001; RA Johnson J.M., Nicot C., Fullen J., Ciminale V., Casareto L., RA Mulloy J.C., Jacobson S., Franchini G.; RT "Free major histocompatibility complex class I heavy chain is RT preferentially targeted for degradation by human T-cell RT leukemia/lymphotropic virus type 1 p12(I) protein."; RL J. Virol. 75:6086-6094(2001). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [19] RP VARIANT [LARGE SCALE ANALYSIS] THR-65, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). Interacts with HTLV-1 accessory protein p12I. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-7 are known: B*07:02 CC (B7.2), B*07:03 (BPOT), B*07:04, B*07:05, B*07:06 (B7_L79), CC B*07:18 and B*07:24. The sequence shown is B*07:02. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M32317; AAA36230.1; -; mRNA. DR EMBL; M16102; AAA59622.1; ALT_SEQ; mRNA. DR EMBL; U29057; AAA91229.1; -; mRNA. DR EMBL; X64454; CAA45785.1; -; mRNA. DR EMBL; U04245; AAA87398.1; -; mRNA. DR EMBL; L33922; AAA65639.1; -; mRNA. DR EMBL; U21052; AAA92563.1; -; mRNA. DR EMBL; U21053; AAA92564.1; -; mRNA. DR EMBL; X91749; CAA62864.1; -; mRNA. DR EMBL; AF189017; AAF01052.1; -; mRNA. DR EMBL; AJ309047; CAC35468.1; -; Genomic_DNA. DR EMBL; AJ292075; CAC33440.1; -; Genomic_DNA. DR EMBL; AL671883; CAI18148.1; -; Genomic_DNA. DR EMBL; AK313911; BAG36634.1; -; mRNA. DR EMBL; AJ401222; CAC10402.1; -; Genomic_DNA. DR CCDS; CCDS34394.1; -. DR PIR; B35997; HLHUB7. DR PIR; I54418; I54418. DR PIR; I59651; I59651. DR PIR; S60601; S60601. DR RefSeq; NP_005505.2; NM_005514.6. DR UniGene; Hs.654404; -. DR UniGene; Hs.77961; -. DR PDB; 3VCL; X-ray; 1.70 A; A=25-299. DR PDBsum; 3VCL; -. DR ProteinModelPortal; P01889; -. DR SMR; P01889; 25-299. DR BioGrid; 109351; 31. DR IntAct; P01889; 4. DR DMDM; 122162; -. DR MaxQB; P01889; -. DR PaxDb; P01889; -. DR PRIDE; P01889; -. DR Ensembl; ENST00000412585; ENSP00000399168; ENSG00000234745. DR GeneID; 3106; -. DR KEGG; hsa:3106; -. DR UCSC; uc003ntg.1; human. DR CTD; 3106; -. DR GeneCards; GC06M031321; -. DR HGNC; HGNC:4932; HLA-B. DR HPA; CAB015418; -. DR MIM; 142830; gene. DR neXtProt; NX_P01889; -. DR PharmGKB; PA35056; -. DR eggNOG; NOG42056; -. DR HOVERGEN; HBG016709; -. DR KO; K06751; -. DR OMA; FLANTRM; -. DR OrthoDB; EOG7JT6WQ; -. DR PhylomeDB; P01889; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-B; human. DR GeneWiki; HLA-B; -. DR GenomeRNAi; 3106; -. DR NextBio; 12323; -. DR PRO; PR:P01889; -. DR ArrayExpress; P01889; -. DR Bgee; P01889; -. DR CleanEx; HS_HLA-B; -. DR Genevestigator; P01889; -. DR GO; GO:0009986; C:cell surface; ISS:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProt. DR GO; GO:0005102; F:receptor binding; IPI:BHF-UCL. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:2001198; P:regulation of dendritic cell differentiation; IMP:BHF-UCL. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0032655; P:regulation of interleukin-12 production; IMP:BHF-UCL. DR GO; GO:0032675; P:regulation of interleukin-6 production; IMP:BHF-UCL. DR GO; GO:0002667; P:regulation of T cell anergy; IMP:BHF-UCL. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Host-virus interaction; Immunity; KW Membrane; MHC I; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-7 alpha chain. FT /FTId=PRO_0000018833. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Helical; (Potential). FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 4 4 M -> T (in dbSNP:rs1050458). FT /FTId=VAR_050332. FT VARIANT 9 9 V -> L (in dbSNP:rs1050462). FT /FTId=VAR_050333. FT VARIANT 17 17 L -> V (in dbSNP:rs1131165). FT /FTId=VAR_050334. FT VARIANT 35 35 S -> A (in dbSNP:rs1131170). FT /FTId=VAR_050335. FT VARIANT 36 36 V -> M (in dbSNP:rs1050486). FT /FTId=VAR_050336. FT VARIANT 48 48 S -> A (in dbSNP:rs713031). FT /FTId=VAR_061386. FT VARIANT 48 48 S -> P (in dbSNP:rs713031). FT /FTId=VAR_061387. FT VARIANT 48 48 S -> T (in dbSNP:rs713031). FT /FTId=VAR_061388. FT VARIANT 65 65 A -> T (in dbSNP:rs1050529). FT /FTId=VAR_050337. FT VARIANT 87 87 N -> D (in dbSNP:rs1050570). FT /FTId=VAR_050338. FT VARIANT 87 87 N -> K (in dbSNP:rs1065386). FT /FTId=VAR_059467. FT VARIANT 93 95 AQA -> TNT (in allele B*07:03). FT /FTId=VAR_016351. FT VARIANT 97 97 T -> A (in dbSNP:rs1050393). FT /FTId=VAR_050339. FT VARIANT 98 98 D -> Y (in dbSNP:rs1131215). FT /FTId=VAR_059468. FT VARIANT 101 101 S -> N (in dbSNP:rs1050388). FT /FTId=VAR_050340. FT VARIANT 118 119 TL -> II (in allele B*07:18). FT /FTId=VAR_016352. FT VARIANT 121 121 S -> R (in allele B*07:18). FT /FTId=VAR_016353. FT VARIANT 137 137 H -> Y (in dbSNP:rs1050379). FT /FTId=VAR_050341. FT VARIANT 138 138 D -> H (in dbSNP:rs709055). FT /FTId=VAR_061389. FT VARIANT 138 138 D -> N (in allele B*07:05 and allele FT B*07:06; dbSNP:rs709055). FT /FTId=VAR_016354. FT VARIANT 155 155 R -> S (in dbSNP:rs1050654). FT /FTId=VAR_050342. FT VARIANT 180 180 R -> D (in allele B*07:04; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016355. FT VARIANT 187 187 E -> A (in dbSNP:rs2308466). FT /FTId=VAR_059469. FT VARIANT 187 187 E -> G (in dbSNP:rs2308466). FT /FTId=VAR_059470. FT VARIANT 187 187 E -> K (in dbSNP:rs2523600). FT /FTId=VAR_059471. FT VARIANT 187 187 E -> L (in allele B*07:24; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016616. FT VARIANT 187 187 E -> Q (in dbSNP:rs2523600). FT /FTId=VAR_059472. FT VARIANT 187 187 E -> V (in dbSNP:rs2308466). FT /FTId=VAR_059473. FT VARIANT 195 195 Y -> H (in dbSNP:rs1050696). FT /FTId=VAR_050343. FT VARIANT 306 306 V -> I (in allele B*07:05; FT dbSNP:rs1131500). FT /FTId=VAR_016356. FT VARIANT 329 329 A -> T (in dbSNP:rs1051488). FT /FTId=VAR_050344. FT VARIANT 349 349 C -> S (in dbSNP:rs2308655). FT /FTId=VAR_061390. FT VARIANT 349 349 C -> Y (in dbSNP:rs2308655). FT /FTId=VAR_061391. FT CONFLICT 15 18 AALA -> GPW (in Ref. 3; AAA59622). FT CONFLICT 266 266 Q -> E (in Ref. 16; AA sequence). FT CONFLICT 268 268 W -> S (in Ref. 3; AAA59622). FT CONFLICT 297 297 R -> G (in Ref. 3; AAA59622). FT CONFLICT 314 315 GL -> RP (in Ref. 3; AAA59622). FT STRAND 27 36 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT HELIX 74 76 FT HELIX 81 108 FT STRAND 118 127 FT STRAND 133 142 FT STRAND 145 150 FT STRAND 157 161 FT HELIX 162 173 FT HELIX 176 185 FT HELIX 187 198 FT HELIX 200 203 FT STRAND 210 235 FT STRAND 238 243 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT HELIX 278 280 FT STRAND 281 286 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40460 MW; 5E5A7BDE031403D6 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHDQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGECVE WLRRYLENGK DKLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B15_HUMAN Reviewed; 362 AA. AC P30464; B0V0B8; P30465; P30513; Q29633; Q29636; Q29829; Q29953; AC Q29982; Q95343; Q95344; Q9BD06; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2003, sequence version 2. DT 09-JUL-2014, entry version 128. DE RecName: Full=HLA class I histocompatibility antigen, B-15 alpha chain; DE AltName: Full=MHC class I antigen B*15; DE Flags: Precursor; GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*15:02). RX PubMed=1801311; DOI=10.1111/j.1399-0039.1991.tb01895.x; RA Little A.-M., Parham P.; RT "The HLA-Bw75 subtype of B15: molecular characterization and RT comparison with crossreacting antigens."; RL Tissue Antigens 38:186-190(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*15:01; B*15:11 AND B*15:19). RX PubMed=7521976; DOI=10.1111/j.1399-0039.1994.tb02327.x; RA Hildebrand W.H., Domena J.D., Shen S.Y., Lau M., Terasaki P.I., RA Bunce M., Marsh S.G.E., Guttridge M.G., Bias W.B., Parham P.; RT "HLA-B15: a widespread and diverse family of HLA-B alleles."; RL Tissue Antigens 43:209-218(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*15:01; B*15:02 AND B*15:11). RC TISSUE=Blood; RX PubMed=8773315; DOI=10.1111/j.1399-0039.1996.tb02553.x; RA Lin L., Tokunaga K., Tanaka H., Nakajima F., Imanishi T., RA Kashiwase K., Bannai M., Mizuno S., Akaza T., Tadokoro K., Shibata Y., RA Juji T.; RT "Further molecular diversity in the HLA-B15 group."; RL Tissue Antigens 47:265-274(1996). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*15:03). RX PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELE B*15:04). RX PubMed=1589035; DOI=10.1038/357329a0; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE B*15:04). RC TISSUE=Blood; RA Ramos M., Barber D.F., Layrisse Z., de Castro J.A.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE (ALLELE B*15:01). RC TISSUE=Blood; RX PubMed=12622774; DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [8] RP NUCLEOTIDE SEQUENCE (ALLELE B*15:66). RX PubMed=12144628; DOI=10.1034/j.1399-0039.2002.590511.x; RA Cox S.T., Prokupek B., Baker F., Holman R., Leung V.T., Wong A.S., RA Madrigal J.A., Little A.-M.; RT "Identification of HLA-B*1566."; RL Tissue Antigens 59:424-425(2002). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-362 (ALLELE B*15:01). RX PubMed=2714852; DOI=10.1007/BF00352839; RA Pohla H., Kuon W., Tabaczewski P., Doerner C., Weiss E.H.; RT "Allelic variation in HLA-B and HLA-C sequences and the evolution of RT the HLA-B alleles."; RL Immunogenetics 29:297-307(1989). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-362 (ALLELE B*15:01). RX PubMed=8423049; DOI=10.1007/BF00216833; RA Choo S.Y., Fan L.A., Hansen J.A.; RT "Allelic variations clustered in the antigen binding sites of HLA-Bw62 RT molecules."; RL Immunogenetics 37:108-113(1993). RN [12] RP ASSOCIATION OF ALLELE B*15:02 WITH STEVENS-JOHNSON SYNDROME. RX PubMed=15057820; DOI=10.1038/428486a; RA Chung W.-H., Hung S.-I., Hong H.-S., Hsih M.-S., Yang L.-C., Ho H.-C., RA Wu J.-Y., Chen Y.-T.; RT "Medical genetics: a marker for Stevens-Johnson syndrome."; RL Nature 428:486-486(2004). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 25-300 (ALLELE B*15:01) IN RP COMPLEX WITH EBV NUCLEAR ANTIGEN AND UBE2 PEPTIDES, AND DISULFIDE RP BONDS. RX PubMed=17057332; DOI=10.1107/S0907444906027636; RA Roder G., Blicher T., Justesen S., Johannesen B., Kristensen O., RA Kastrup J., Buus S., Gajhede M.; RT "Crystal structures of two peptide-HLA-B*1501 complexes; structural RT characterization of the HLA-B62 supertype."; RL Acta Crystallogr. D 62:1300-1310(2006). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-15 are known: B*15:01 CC (Bw-62; B-62), B*15:02 (Bw-75, B-75), B*15:03 (Bw-72; B-72; B-70) CC B*15:04, B*15:11, B*15:19 and B*15:66. The sequence shown is that CC of B*15:01. CC -!- DISEASE: Stevens-Johnson syndrome (SJS) [MIM:608579]: A rare CC blistering mucocutaneous disease that share clinical and CC histopathologic features with toxic epidermal necrolysis. Both CC disorders are characterized by high fever, malaise, and a rapidly CC developing blistering exanthema of macules and target-like lesions CC accompanied by mucosal involvement. Stevens-Johnson syndrome is a CC milder disease characterized by destruction and detachment of the CC skin epithelium and mucous membranes involving less than 10% of CC the body surface area. Ocular symptoms include ulcerative CC conjunctivitis, keratitis, iritis, uveitis and sometimes CC blindness. It can be caused by a severe adverse reaction to CC particular types of medication, although Mycoplasma infections may CC induce some cases. Note=Disease susceptibility is associated with CC variations affecting the gene represented in this entry. Increased CC susceptibility to Stevens-Johnson syndrome is conferred by allele CC B*15:02. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M75138; AAA59630.1; -; mRNA. DR EMBL; U03859; AAA03601.1; -; mRNA. DR EMBL; U03027; AAA18902.1; -; mRNA. DR EMBL; L11604; AAA56836.1; -; mRNA. DR EMBL; D50292; BAA08823.1; -; mRNA. DR EMBL; D50293; BAA08824.1; -; mRNA. DR EMBL; D50294; BAA08825.1; -; mRNA. DR EMBL; X61709; CAA43878.1; -; mRNA. DR EMBL; M84382; AAA59632.1; -; mRNA. DR EMBL; U70528; AAB16918.1; -; mRNA. DR EMBL; AJ295140; CAC17462.1; -; Genomic_DNA. DR EMBL; AJ308399; CAC33441.1; -; Genomic_DNA. DR EMBL; CR759828; CAQ10738.1; -; Genomic_DNA. DR EMBL; M28203; AAA53258.1; -; mRNA. DR EMBL; M83193; AAA58628.1; -; mRNA. DR PIR; G01230; G01230. DR PIR; I38421; I38421. DR PIR; I62042; I62042. DR PIR; S16789; S16789. DR PIR; S24433; S24433. DR PIR; S77966; S77966. DR UniGene; Hs.654404; -. DR UniGene; Hs.77961; -. DR PDB; 1XR8; X-ray; 2.30 A; A=25-300. DR PDB; 1XR9; X-ray; 1.79 A; A=25-300. DR PDB; 3C9N; X-ray; 1.87 A; A=25-300. DR PDBsum; 1XR8; -. DR PDBsum; 1XR9; -. DR PDBsum; 3C9N; -. DR ProteinModelPortal; P30464; -. DR SMR; P30464; 25-300. DR IntAct; P30464; 1. DR DMDM; 34305703; -. DR MaxQB; P30464; -. DR PRIDE; P30464; -. DR Ensembl; ENST00000450871; ENSP00000388208; ENSG00000232126. DR UCSC; uc011hpo.2; human. DR GeneCards; GC06M031321; -. DR GeneCards; GC06Mm31398; -. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR MIM; 608579; phenotype. DR neXtProt; NX_P30464; -. DR Orphanet; 240841; Abacavir toxicity. DR Orphanet; 240845; Allopurinol toxicity. DR Orphanet; 825; Ankylosing spondylitis. DR Orphanet; 117; Behcet disease. DR Orphanet; 240871; Flucloxacilline toxicity. DR Orphanet; 240901; Fosphenytoin toxicity. DR Orphanet; 240899; Phenytoin toxicity. DR Orphanet; 275798; Pulmonary arterial hypertension associated with connective tissue disease. DR Orphanet; 36426; Stevens-Johnson syndrome. DR Orphanet; 241001; Susceptibility to hepatitis due to flucloxacilline treatment. DR Orphanet; 241005; Susceptibility to hypersensitivity syndrome due to abacavir treatment. DR Orphanet; 241035; Susceptibility to toxic epidermal necrolysis due to allopurinol treatment. DR Orphanet; 241037; Susceptibility to toxic epidermal necrolysis due to carbamazepine treatment. DR Orphanet; 241039; Susceptibility to toxic epidermal necrolysis due to phenytoin treatment. DR Orphanet; 241041; Susceptibility to toxic epidermal necrolysis due to phosphenytoin treatment. DR Orphanet; 3287; Takayasu arteritis. DR HOVERGEN; HBG016709; -. DR InParanoid; P30464; -. DR OMA; NTRISEN; -. DR PhylomeDB; P30464; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-B; human. DR EvolutionaryTrace; P30464; -. DR CleanEx; HS_HLA-B; -. DR Genevestigator; P30464; -. DR GO; GO:0009986; C:cell surface; ISS:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProt. DR GO; GO:0005102; F:receptor binding; IBA:RefGenome. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Host-virus interaction; Immunity; Membrane; MHC I; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-15 alpha chain. FT /FTId=PRO_0000018837. FT TOPO_DOM 25 309 Extracellular (Potential). FT TRANSMEM 310 333 Helical; (Potential). FT TOPO_DOM 334 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 309 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 48 48 A -> S (in allele B*15:03). FT /FTId=VAR_016365. FT VARIANT 69 70 MA -> EE (in allele B*15:03). FT /FTId=VAR_016366. FT VARIANT 87 87 E -> N (in allele B*15:02 and allele FT B*15:11; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016367. FT VARIANT 91 91 S -> C (in allele B*15:66). FT /FTId=VAR_016368. FT VARIANT 91 91 S -> Y (in allele B*15:11). FT /FTId=VAR_016369. FT VARIANT 118 119 TL -> II (in allele B*15:02). FT /FTId=VAR_016370. FT VARIANT 119 119 L -> W (in allele B*15:04). FT /FTId=VAR_016371. FT VARIANT 121 121 R -> T (in allele B*15:04). FT /FTId=VAR_016372. FT VARIANT 137 137 H -> Y (in allele B*15:02). FT /FTId=VAR_016373. FT VARIANT 180 180 W -> L (in allele B*15:02 and allele FT B*15:03). FT /FTId=VAR_016374. FT VARIANT 190 191 EW -> DG (in allele B*15:19). FT /FTId=VAR_016375. FT VARIANT 274 274 P -> L (in allele B*15:19). FT /FTId=VAR_016376. FT STRAND 27 36 FT STRAND 41 43 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT HELIX 74 76 FT HELIX 81 108 FT STRAND 118 127 FT STRAND 133 142 FT STRAND 145 150 FT STRAND 157 161 FT HELIX 162 173 FT HELIX 176 185 FT HELIX 187 198 FT HELIX 200 203 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT HELIX 249 251 FT STRAND 261 263 FT STRAND 265 274 FT HELIX 278 280 FT STRAND 281 286 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40388 MW; 86E938087372EBE0 CRC64; MRVTAPRTVL LLLSGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQW RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B27_HUMAN Reviewed; 362 AA. AC P03989; O19692; P10317; P10318; P19373; P30467; Q08136; Q29693; AC Q29846; Q29961; DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 2. DT 09-JUL-2014, entry version 151. DE RecName: Full=HLA class I histocompatibility antigen, B-27 alpha chain; DE AltName: Full=MHC class I antigen B*27; DE Flags: Precursor; GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*27:01). RX PubMed=3912316; RA Weiss E.H., Kuon W., Doerner C., Lang M., Riethmueller G.; RT "Organization, sequence and expression of the HLA-B27 gene: a RT molecular approach to analyze HLA and disease associations."; RL Immunobiology 170:367-380(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-361 (ALLELE B*27:01). RX PubMed=3485286; DOI=10.1073/pnas.83.5.1428; RA Szoets H., Riethmueller G., Weiss E., Meo T.; RT "Complete sequence of HLA-B27 cDNA identified through the RT characterization of structural markers unique to the HLA-A, -B, and -C RT allelic series."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1428-1432(1986). RN [3] RP PROTEIN SEQUENCE OF 25-295 (B*27:01). RX PubMed=2408663; DOI=10.1021/bi00328a025; RA Ezquerra A., Bragado R., Vega M.A., Strominger J.L., Woody J., RA Lopez de Castro J.A.; RT "Primary structure of papain-solubilized human histocompatibility RT antigen HLA-B27."; RL Biochemistry 24:1733-1741(1985). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES B*27:01 AND B*27:02). RX PubMed=3011411; RA Seemann G.H.A., Rein R.S., Brown C.S., Ploegh H.L.; RT "Gene conversion-like mechanisms may generate polymorphism in human RT class I genes."; RL EMBO J. 5:547-552(1986). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:02). RX PubMed=7482496; DOI=10.1111/j.1399-0039.1995.tb02475.x; RA Moses J.H., Marsh S.G.E., Arnett K.L., Adams E.J., Bodmer J.G., RA Parham P.; RT "On the nucleotide sequences of B*2702 and B*2705."; RL Tissue Antigens 46:50-53(1995). RN [6] RP PROTEIN SEQUENCE OF 86-107 AND 171-181 (B*27:02). RX PubMed=2414775; DOI=10.1073/pnas.82.21.7394; RA Vega M.A., Ezquerra A., Rojo S., Aparicio P., Bragado R., RA Lopez de Castro J.A.; RT "Structural analysis of an HLA-B27 functional variant: identification RT of residues that contribute to the specificity of recognition by RT cytolytic T lymphocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7394-7398(1985). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*27:03). RX PubMed=3286582; DOI=10.1016/0198-8859(88)90072-9; RA Choo S.Y., St John T., Orr H.T., Hansen J.A.; RT "Molecular analysis of the variant alloantigen HLA-B27d (HLA-B*2703) RT identifies a unique single amino acid substitution."; RL Hum. Immunol. 21:209-219(1988). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*27:04 AND B*27:06). RX PubMed=8550101; DOI=10.1007/BF00176678; RA Rudwaleit M., Bowness P., Wordsworth P.; RT "The nucleotide sequence of HLA-B*2704 reveals a new amino acid RT substitution in exon 4 which is also present in HLA-B*2706."; RL Immunogenetics 43:160-162(1996). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-298 (ALLELE B*27:05). RX PubMed=3489755; RA Coppin H.L., McDevitt H.O.; RT "Absence of polymorphism between HLA-B27 genomic exon sequences RT isolated from normal donors and ankylosing spondylitis patients."; RL J. Immunol. 137:2168-2172(1986). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:06). RX PubMed=8276469; DOI=10.1007/BF00241265; RA Vilches C., de Pablo R., Kreisler M.; RT "Nucleotide sequence of HLA-B*2706."; RL Immunogenetics 39:219-219(1994). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:07). RX PubMed=1711072; RA Choo Y.S., Fan L.A., Hansen J.A.; RT "A novel HLA-B27 allele maps B27 allospecificity to the region around RT position 70 in the alpha 1 domain."; RL J. Immunol. 147:174-180(1991). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:08). RX PubMed=7974468; DOI=10.1111/j.1399-0039.1994.tb02356.x; RA Hildebrand W.H., Domena J.D., Shen S.Y., Marsh S.G.E., Bunce M., RA Guttridge M.G., Darke C., Parham P.; RT "The HLA-B7Qui antigen is encoded by a new subtype of HLA-B27 RT (B*2708)."; RL Tissue Antigens 44:47-51(1994). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*27:09). RC TISSUE=Blood; RX PubMed=8089488; RA Del Porto P., D'Amato M., Fiorillo M.T., Tuosto L., Piccolella E., RA Sorrentino R.; RT "Identification of a novel HLA-B27 subtype by restriction analysis of RT a cytotoxic gamma/delta T cell clone."; RL J. Immunol. 153:3093-3100(1994). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-300. RX PubMed=1525820; DOI=10.1016/0092-8674(92)90252-8; RA Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.; RT "The three-dimensional structure of HLA-B27 at 2.1-A resolution RT suggests a general mechanism for tight peptide binding to MHC."; RL Cell 70:1035-1048(1992). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-300. RX PubMed=1922337; DOI=10.1038/353321a0; RA Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.; RT "The structure of HLA-B27 reveals nonamer self-peptides bound in an RT extended conformation."; RL Nature 353:321-325(1991). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-300. RX PubMed=12244049; DOI=10.1074/jbc.M206392200; RA Hulsmeyer M., Hillig R.C., Volz A., Ruhl M., Schroder W., Saenger W., RA Ziegler A., Uchanska-Ziegler B.; RT "HLA-B27 subtypes differentially associated with disease exhibit RT subtle structural alterations."; RL J. Biol. Chem. 277:47844-47853(2002). RN [18] RP 3D-STRUCTURE MODELING OF 115-206. RX PubMed=7846047; DOI=10.1073/pnas.92.3.753; RA Rognan D., Scapozza L., Folkers G., Daser A.; RT "Rational design of nonnatural peptides as high-affinity ligands for RT the HLA-B*2705 human leukocyte antigen."; RL Proc. Natl. Acad. Sci. U.S.A. 92:753-757(1995). RN [19] RP DISEASE, AND POSSIBLE PROTECTIVE ROLE OF ALLELE B*27:07. RX PubMed=15603872; DOI=10.1016/j.humimm.2004.08.177; RA Varnavidou-Nicolaidou A., Karpasitou K., Georgiou D., Stylianou G., RA Kokkofitou A., Michalis C., Constantina C., Gregoriadou C., RA Kyriakides G.; RT "HLA-B27 in the Greek Cypriot population: distribution of subtypes in RT patients with ankylosing spondylitis and other HLA-B27-related RT diseases. The possible protective role of B*2707."; RL Hum. Immunol. 65:1451-1454(2004). RN [20] RP VARIANT [LARGE SCALE ANALYSIS] THR-65, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-27 are known: CC B*27:01=B*27:05, B*27:02 (B27.2; B-27k; B27e), B*27:03 (B27d), CC B*27:04, B*27:06, B*27:07, B*27:08 (B7Qui) and B*27:09 (B27-ci). CC The sequence shown is that of B*27:01. CC -!- DISEASE: Spondyloarthropathy 1 (SPDA1) [MIM:106300]: A chronic CC rheumatic disease with multifactorial inheritance. It includes a CC spectrum of related disorders comprising ankylosing spondylitis, a CC subset of psoriatic arthritis, reactive arthritis (e.g. Reiter CC syndrome), arthritis associated with inflammatory bowel disease CC and undifferentiated spondyloarthropathy. These disorders may CC occur simultaneously or sequentially in the same patient, probably CC representing various phenotypic expressions of the same disease. CC Ankylosing spondylitis is the form of rheumatoid arthritis CC affecting the spine and is considered the prototype of CC seronegative spondyloarthropathies. It produces pain and stiffness CC as a result of inflammation of the sacroiliac, intervertebral, and CC costovertebral joints. Note=Disease susceptibility is associated CC with variations affecting the gene represented in this entry. A CC restricted number of HLA-B27 subtypes can be associated with CC ankylosing spondylitis and other B27-related diseases, and an CC elevated frequency of the B*2702 allele in ankylosing spondylitis CC patients is identified. The allele B*2707 seems to have a CC protective role some populations because it was found only in the CC healthy controls. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X03945; CAA27578.1; ALT_SEQ; Genomic_DNA. DR EMBL; X03664; CAA27301.1; -; Genomic_DNA. DR EMBL; X03667; CAA27301.1; JOINED; Genomic_DNA. DR EMBL; L38504; AAA69724.1; -; mRNA. DR EMBL; M54883; AAA59616.1; -; Genomic_DNA. DR EMBL; X03665; CAA27302.1; -; Genomic_DNA. DR EMBL; X03666; CAA27302.1; JOINED; Genomic_DNA. DR EMBL; M12967; AAA36221.1; -; Genomic_DNA. DR EMBL; U27608; AAC50444.1; -; mRNA. DR EMBL; U35734; AAC50447.1; -; mRNA. DR EMBL; M14013; AAA59643.1; -; Genomic_DNA. DR EMBL; X73578; CAA51980.1; -; mRNA. DR EMBL; M62852; AAA59647.1; -; mRNA. DR EMBL; L19923; AAA59658.1; -; mRNA. DR EMBL; Z33453; CAA83876.1; -; mRNA. DR PIR; I37515; I37515. DR PIR; I56116; I56116. DR PIR; S07441; HLHUB2. DR UniGene; Hs.654404; -. DR UniGene; Hs.77961; -. DR PDB; 1HSA; X-ray; 2.10 A; A/D=25-300. DR PDB; 1JGD; X-ray; 1.90 A; A=25-300. DR PDB; 1JGE; X-ray; 2.10 A; A=25-300. DR PDB; 1K5N; X-ray; 1.09 A; A=25-300. DR PDB; 1OF2; X-ray; 2.20 A; A=25-300. DR PDB; 1OGT; X-ray; 1.47 A; A=25-300. DR PDB; 1ROG; Model; -; A=25-206. DR PDB; 1ROH; Model; -; A=25-206. DR PDB; 1ROI; Model; -; A=25-206. DR PDB; 1ROJ; Model; -; A=25-206. DR PDB; 1ROK; Model; -; A=25-206. DR PDB; 1ROL; Model; -; A=25-206. DR PDB; 1UXS; X-ray; 1.55 A; A=25-300. DR PDB; 1UXW; X-ray; 1.71 A; A=25-300. DR PDB; 1W0V; X-ray; 2.27 A; A=25-300. DR PDB; 1W0W; X-ray; 2.10 A; A=25-300. DR PDB; 2A83; X-ray; 1.40 A; A=25-300. DR PDB; 2BSR; X-ray; 2.30 A; A=25-300. DR PDB; 2BSS; X-ray; 2.00 A; A=25-300. DR PDB; 2BST; X-ray; 2.10 A; A=25-300. DR PDB; 3B3I; X-ray; 1.86 A; A=25-300. DR PDB; 3B6S; X-ray; 1.80 A; A=25-300. DR PDB; 3BP4; X-ray; 1.85 A; A=25-300. DR PDB; 3BP7; X-ray; 1.80 A; A=25-300. DR PDB; 3CZF; X-ray; 1.20 A; A=25-300. DR PDB; 3D18; X-ray; 1.74 A; A=25-300. DR PDB; 3DTX; X-ray; 2.10 A; A=25-300. DR PDB; 3HCV; X-ray; 1.95 A; A=25-300. DR PDB; 3LV3; X-ray; 1.94 A; A=25-300. DR PDB; 4G8G; X-ray; 2.40 A; A=25-300. DR PDB; 4G8I; X-ray; 1.60 A; A=25-300. DR PDB; 4G9D; X-ray; 1.60 A; A=25-300. DR PDB; 4G9F; X-ray; 1.90 A; A=25-300. DR PDBsum; 1HSA; -. DR PDBsum; 1JGD; -. DR PDBsum; 1JGE; -. DR PDBsum; 1K5N; -. DR PDBsum; 1OF2; -. DR PDBsum; 1OGT; -. DR PDBsum; 1ROG; -. DR PDBsum; 1ROH; -. DR PDBsum; 1ROI; -. DR PDBsum; 1ROJ; -. DR PDBsum; 1ROK; -. DR PDBsum; 1ROL; -. DR PDBsum; 1UXS; -. DR PDBsum; 1UXW; -. DR PDBsum; 1W0V; -. DR PDBsum; 1W0W; -. DR PDBsum; 2A83; -. DR PDBsum; 2BSR; -. DR PDBsum; 2BSS; -. DR PDBsum; 2BST; -. DR PDBsum; 3B3I; -. DR PDBsum; 3B6S; -. DR PDBsum; 3BP4; -. DR PDBsum; 3BP7; -. DR PDBsum; 3CZF; -. DR PDBsum; 3D18; -. DR PDBsum; 3DTX; -. DR PDBsum; 3HCV; -. DR PDBsum; 3LV3; -. DR PDBsum; 4G8G; -. DR PDBsum; 4G8I; -. DR PDBsum; 4G9D; -. DR PDBsum; 4G9F; -. DR ProteinModelPortal; P03989; -. DR SMR; P03989; 25-300. DR DIP; DIP-6188N; -. DR IntAct; P03989; 1. DR MINT; MINT-247525; -. DR DMDM; 34305677; -. DR PaxDb; P03989; -. DR PRIDE; P03989; -. DR Ensembl; ENST00000435618; ENSP00000405178; ENSG00000224608. DR GeneCards; GC06M031321; -. DR GeneCards; GC06Ml31364; -. DR HGNC; HGNC:4932; HLA-B. DR MIM; 106300; phenotype. DR MIM; 142830; gene. DR neXtProt; NX_P03989; -. DR eggNOG; NOG42056; -. DR HOVERGEN; HBG016709; -. DR InParanoid; P03989; -. DR PhylomeDB; P03989; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-B; human. DR EvolutionaryTrace; P03989; -. DR CleanEx; HS_HLA-B; -. DR Genevestigator; P03989; -. DR GO; GO:0009986; C:cell surface; IDA:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; TAS:UniProtKB. DR GO; GO:0042612; C:MHC class I protein complex; IDA:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProt. DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IDA:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0006952; P:defense response; TAS:UniProtKB. DR GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB. DR GO; GO:0006955; P:immune response; IMP:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Host-virus interaction; Immunity; KW Membrane; MHC I; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-27 alpha chain. FT /FTId=PRO_0000018839. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 65 65 A -> T (in dbSNP:rs1050529). FT /FTId=VAR_056341. FT VARIANT 83 83 Y -> H (in allele B*27:03). FT /FTId=VAR_016379. FT VARIANT 101 101 D -> N (in allele B*27:02). FT /FTId=VAR_016380. FT VARIANT 101 101 D -> S (in allele B*27:04, allele B*27:06 FT and allele B*27:08; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016381. FT VARIANT 104 105 TL -> IA (in allele B*27:02). FT /FTId=VAR_016382. FT VARIANT 104 104 T -> N (in allele B*27:08). FT /FTId=VAR_016383. FT VARIANT 106 107 LR -> RG (in allele B*27:08). FT /FTId=VAR_016384. FT VARIANT 121 121 N -> S (in allele B*27:07). FT /FTId=VAR_016385. FT VARIANT 137 138 YH -> HN (in allele B*27:07). FT /FTId=VAR_016386. FT VARIANT 138 138 H -> D (in allele B*27:06). FT /FTId=VAR_016387. FT VARIANT 140 140 D -> H (in allele B*27:09). FT /FTId=VAR_016388. FT VARIANT 140 140 D -> Y (in allele B*27:06 and allele FT B*27:07). FT /FTId=VAR_016389. FT VARIANT 155 155 S -> R (in allele B*27:07). FT /FTId=VAR_016390. FT VARIANT 176 176 V -> E (in allele B*27:04 and allele FT B*27:06). FT /FTId=VAR_016391. FT VARIANT 235 235 A -> G (in allele B*27:04 and allele FT B*27:06). FT /FTId=VAR_016392. FT VARIANT 306 306 V -> I (in dbSNP:rs1131500). FT /FTId=VAR_056342. FT VARIANT 329 329 A -> T (in dbSNP:rs1051488). FT /FTId=VAR_056343. FT VARIANT 349 349 C -> S (in dbSNP:rs2308655). FT /FTId=VAR_061402. FT VARIANT 349 349 C -> Y (in dbSNP:rs2308655). FT /FTId=VAR_061403. FT CONFLICT 206 206 A -> V (in Ref. 2). FT CONFLICT 266 266 Q -> E (in Ref. 3; AA sequence). FT STRAND 27 36 FT STRAND 41 43 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT HELIX 74 76 FT HELIX 81 108 FT STRAND 113 115 FT STRAND 118 127 FT STRAND 133 142 FT STRAND 145 150 FT STRAND 157 161 FT HELIX 162 173 FT HELIX 176 185 FT HELIX 187 198 FT TURN 199 204 FT STRAND 210 219 FT STRAND 222 235 FT STRAND 238 243 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT HELIX 278 280 FT STRAND 281 286 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40428 MW; C8D2F154E3292031 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI CKAKAQTDRE DLRTLLRYYN QSEAGSHTLQ NMYGCDVGPD GRLLRGYHQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B35_HUMAN Reviewed; 362 AA. AC P30685; O62919; P30468; P30469; P30470; P30471; P30472; P30473; AC P30474; Q9GJM7; Q9TPV2; Q9TQH3; Q9TQH9; Q9TQN4; Q9TQN6; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 09-JUL-2014, entry version 136. DE RecName: Full=HLA class I histocompatibility antigen, B-35 alpha chain; DE AltName: Full=MHC class I antigen B*35; DE Flags: Precursor; GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*35:01). RX PubMed=2788131; DOI=10.1007/BF02421534; RA Ooba T., Hayashi H., Karaki S., Tanabe M., Kano K., Takiguchi M.; RT "The structure of HLA-B35 suggests that it is derived from HLA-Bw58 by RT two genetic mechanisms."; RL Immunogenetics 30:76-80(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*35:02). RX PubMed=1890016; DOI=10.1016/0198-8859(91)90020-A; RA Chertkoff L.P., Herrera M., Fainboim L., Satz M.L.; RT "Complete nucleotide sequence of a genomic clone encoding HLA-B35 RT isolated from a Caucasian individual of Hispanic origin. RT Identification of a new variant of HLA-B35."; RL Hum. Immunol. 31:153-158(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*35:03). RX PubMed=1541831; RA Zemmour J., Little A.-M., Schendel D.J., Parham P.; RT "The HLA-A,B 'negative' mutant cell line C1R expresses a novel HLA-B35 RT allele, which also has a point mutation in the translation initiation RT codon."; RL J. Immunol. 148:1941-1948(1992). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*35:03). RC TISSUE=Blood; RX PubMed=7759996; DOI=10.1084/jem.181.6.2037; RA Beck Y., Satz L., Takamiya Y., Nakayama S., Ling L., Ishikawa Y., RA Nagao T., Uchida H., Tokunaga K., Mueller C., Juji T., Takiguchi M.; RT "Polymorphism of human minor histocompatibility antigens: T cell RT recognition of human minor histocompatibility peptides presented by RT HLA-B35 subtype molecules."; RL J. Exp. Med. 181:2037-2048(1995). RN [5] RP NUCLEOTIDE SEQUENCE (ALLELES B*35:05 AND B*35:06). RX PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*35:07 AND B*35:08). RX PubMed=8316945; DOI=10.1111/j.1399-0039.1993.tb01993.x; RA Theiler G., Pando M., Delfino J.M., Takiguchi M., Satz M.L.; RT "Isolation and characterization of two new functional subtypes of HLA- RT B35."; RL Tissue Antigens 41:143-147(1993). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*35:08). RX PubMed=8138421; DOI=10.1016/0198-8859(93)90553-D; RA Steinle A., Reinhardt C., Noessner E., Uchanska-Ziegler B., RA Ziegler A., Schendel D.J.; RT "Microheterogeneity in HLA-B35 alleles influences peptide-dependent RT allorecognition by cytotoxic T cells but not binding of a peptide- RT restricted monoclonal antibody."; RL Hum. Immunol. 38:261-269(1993). RN [8] RP NUCLEOTIDE SEQUENCE OF 9-362 (ALLELE B*35:04). RX PubMed=1589035; DOI=10.1038/357329a0; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELES B*35:29 AND RP B*35:32). RX PubMed=10777103; DOI=10.1034/j.1399-0039.2000.550311.x; RA Kennedy C.T., Dodd R., Le T., Wallace R., Ng G., Greville W.D., RA Kennedy A., Taverniti A., Moses J.H., Clow N., Watson N., Dunckley H.; RT "Routine HLA-B genotyping with PCR-sequence-specific oligonucleotides RT (PCR-SSO) detects eight new alleles: B*0807, B*0809, B*1551, B*3529, RT B*3532, B*4025, B*5304 and B*5508."; RL Tissue Antigens 55:266-270(2000). RN [10] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELES B*35:25; B*35:28; B*35:29; RP B*35:30 AND B*35:36). RX PubMed=11556976; DOI=10.1034/j.1399-0039.2001.057005481.x; RA Steiner N.K., Kosman C., Jones P.F., Gans C.P., Rodriguez-Marino S.G., RA Rizzuto G., Baldassarre L.A., Edson S., Koester R., Sese D., RA Mitton W., Ng J., Hartzman R.J., Hurley C.K.; RT "Twenty-nine new HLA-B alleles associated with antigens in the 5C RT CREG."; RL Tissue Antigens 57:481-485(2001). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-300. RX PubMed=8624811; DOI=10.1016/S1074-7613(00)80429-X; RA Smith K.J., Reid S.W., Stuart D.I., McMichael A.J., Jones E.Y., RA Bell J.I.; RT "An altered position of the alpha 2 helix of MHC class I is revealed RT by the crystal structure of HLA-B*3501."; RL Immunity 4:203-214(1996). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=9878435; DOI=10.1006/jmbi.1998.2363; RA Menssen R., Orth P., Ziegler A., Saenger W.; RT "Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due RT to non-standard positioning of the C-terminus."; RL J. Mol. Biol. 285:645-653(1999). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] TYR-140, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-35 are known: B*35:01, CC B*35:02, B*35:03, B*35:04, B*35:05 (B35-G), B*35:06 (B35-K), CC B*35:07, B*35:08, B*35:25, B*35:28, B*35:29 (B*KG), B*35:30, CC B*35:32 (B*TMUL) and B*35:36. The sequence shown is that of CC B*35:01. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M28115; AAA59617.1; -; Genomic_DNA. DR EMBL; M28109; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28110; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28111; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28112; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28113; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M28114; AAA59617.1; JOINED; Genomic_DNA. DR EMBL; M63454; AAA59682.1; -; Genomic_DNA. DR EMBL; M81798; AAA59684.1; -; mRNA. DR EMBL; D50299; BAA08828.1; -; mRNA. DR EMBL; M84385; AAA59635.1; -; mRNA. DR EMBL; M84381; AAA59631.1; -; mRNA. DR EMBL; L04695; AAA59694.1; -; mRNA. DR EMBL; L04696; AAA52674.1; -; mRNA. DR EMBL; Z22651; CAA80366.1; -; mRNA. DR EMBL; M86403; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AH007565; AAD23460.1; -; Genomic_DNA. DR EMBL; AH007706; AAD30277.1; -; Genomic_DNA. DR EMBL; AH006372; AAC32570.1; -; Genomic_DNA. DR EMBL; AH007604; AAD27538.1; -; Genomic_DNA. DR EMBL; AH008126; AAD51745.1; -; Genomic_DNA. DR EMBL; AH007584; AAD26151.1; -; Genomic_DNA. DR EMBL; AH009759; AAG01819.1; -; Genomic_DNA. DR PIR; A45880; A45880. DR PIR; I54298; I54298. DR PIR; I56133; I56133. DR PIR; I61904; I61904. DR PIR; I61907; I61907. DR PIR; I81233; I81233. DR UniGene; Hs.654404; -. DR UniGene; Hs.77961; -. DR PDB; 1A1N; X-ray; 2.00 A; A=25-300. DR PDB; 1A9B; X-ray; 3.20 A; A/D=25-301. DR PDB; 1A9E; X-ray; 2.50 A; A=25-301. DR PDB; 1CG9; X-ray; 2.70 A; A=25-301. DR PDB; 1XH3; X-ray; 1.48 A; A=25-300. DR PDB; 1ZHK; X-ray; 1.60 A; A=25-300. DR PDB; 1ZHL; X-ray; 1.50 A; A=25-300. DR PDB; 1ZSD; X-ray; 1.70 A; A=25-300. DR PDB; 2AK4; X-ray; 2.50 A; A/F/K/Q=25-300. DR PDB; 2AXF; X-ray; 1.80 A; A=25-300. DR PDB; 2AXG; X-ray; 2.00 A; A=25-300. DR PDB; 2CIK; X-ray; 1.75 A; A=25-300. DR PDB; 2FYY; X-ray; 1.50 A; A=25-300. DR PDB; 2FZ3; X-ray; 1.90 A; A=25-300. DR PDB; 2H6P; X-ray; 1.90 A; A=25-300. DR PDB; 2NW3; X-ray; 1.70 A; A=25-300. DR PDB; 2NX5; X-ray; 2.70 A; A/F/K/Q=25-300. DR PDB; 3BW9; X-ray; 1.75 A; A=25-300. DR PDB; 3BWA; X-ray; 1.30 A; A=25-300. DR PDB; 3KWW; X-ray; 2.18 A; A=25-300. DR PDB; 3KXF; X-ray; 3.10 A; A/C/I/K=25-300. DR PDB; 3LKN; X-ray; 2.00 A; A=25-300. DR PDB; 3LKO; X-ray; 1.80 A; A=25-300. DR PDB; 3LKP; X-ray; 1.80 A; A=25-300. DR PDB; 3LKQ; X-ray; 1.80 A; A=25-300. DR PDB; 3LKR; X-ray; 2.00 A; A=25-300. DR PDB; 3LKS; X-ray; 1.90 A; A=25-300. DR PDB; 3MV7; X-ray; 2.00 A; A=25-300. DR PDB; 3MV8; X-ray; 2.10 A; A=25-300. DR PDB; 3MV9; X-ray; 2.70 A; A=25-300. DR PDB; 3VFS; X-ray; 1.85 A; A=25-300. DR PDB; 3VFT; X-ray; 1.95 A; A=25-300. DR PDB; 3VFU; X-ray; 1.65 A; A=25-300. DR PDB; 3VFV; X-ray; 1.55 A; A=25-300. DR PDB; 3VFW; X-ray; 2.30 A; A=25-300. DR PDB; 4PR5; X-ray; 1.80 A; A=25-300. DR PDB; 4PRN; X-ray; 1.65 A; A=25-300. DR PDBsum; 1A1N; -. DR PDBsum; 1A9B; -. DR PDBsum; 1A9E; -. DR PDBsum; 1CG9; -. DR PDBsum; 1XH3; -. DR PDBsum; 1ZHK; -. DR PDBsum; 1ZHL; -. DR PDBsum; 1ZSD; -. DR PDBsum; 2AK4; -. DR PDBsum; 2AXF; -. DR PDBsum; 2AXG; -. DR PDBsum; 2CIK; -. DR PDBsum; 2FYY; -. DR PDBsum; 2FZ3; -. DR PDBsum; 2H6P; -. DR PDBsum; 2NW3; -. DR PDBsum; 2NX5; -. DR PDBsum; 3BW9; -. DR PDBsum; 3BWA; -. DR PDBsum; 3KWW; -. DR PDBsum; 3KXF; -. DR PDBsum; 3LKN; -. DR PDBsum; 3LKO; -. DR PDBsum; 3LKP; -. DR PDBsum; 3LKQ; -. DR PDBsum; 3LKR; -. DR PDBsum; 3LKS; -. DR PDBsum; 3MV7; -. DR PDBsum; 3MV8; -. DR PDBsum; 3MV9; -. DR PDBsum; 3VFS; -. DR PDBsum; 3VFT; -. DR PDBsum; 3VFU; -. DR PDBsum; 3VFV; -. DR PDBsum; 3VFW; -. DR PDBsum; 4PR5; -. DR PDBsum; 4PRN; -. DR ProteinModelPortal; P30685; -. DR SMR; P30685; 25-300. DR IntAct; P30685; 1. DR MINT; MINT-1516663; -. DR DMDM; 231390; -. DR PRIDE; P30685; -. DR Ensembl; ENST00000359635; ENSP00000352656; ENSG00000206450. DR GeneCards; GC06M031321; -. DR GeneCards; GC06Mn31311; -. DR H-InvDB; HIX0167180; -. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR neXtProt; NX_P30685; -. DR HOVERGEN; HBG016709; -. DR InParanoid; P30685; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-B; human. DR EvolutionaryTrace; P30685; -. DR CleanEx; HS_HLA-B; -. DR Genevestigator; P30685; -. DR GO; GO:0009986; C:cell surface; ISS:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Host-virus interaction; Immunity; Membrane; MHC I; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-35 alpha chain. FT /FTId=PRO_0000018840. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 40 40 G -> V (in allele B*35:07). FT /FTId=VAR_016393. FT VARIANT 48 48 A -> S (in allele B*35:25). FT /FTId=VAR_016394. FT VARIANT 69 69 T -> E (in allele B*35:25; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016395. FT VARIANT 87 87 N -> E (in allele B*35:28; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016396. FT VARIANT 91 91 F -> S (in allele B*35:28). FT /FTId=VAR_016397. FT VARIANT 98 98 Y -> D (in allele B*35:29). FT /FTId=VAR_016398. FT VARIANT 107 107 G -> D (in allele B*35:36). FT /FTId=VAR_016399. FT VARIANT 118 119 II -> TL (in allele B*35:05 and allele FT B*35:32). FT /FTId=VAR_016400. FT VARIANT 121 121 R -> S (in allele B*35:05 and allele FT B*35:30). FT /FTId=VAR_016401. FT VARIANT 127 127 L -> V (in allele B*35:32). FT /FTId=VAR_016402. FT VARIANT 133 133 L -> F (in allele B*35:02). FT /FTId=VAR_016403. FT VARIANT 138 138 D -> N (in allele B*35:02, allele B*35:04 FT and allele B*35:06). FT /FTId=VAR_016404. FT VARIANT 140 140 S -> F (in allele B*35:06 and allele FT B*35:36). FT /FTId=VAR_016405. FT VARIANT 140 140 S -> Y (in allele B*35:02, allele B*35:03 FT and allele B*35:04). FT /FTId=VAR_016406. FT VARIANT 180 180 L -> R (in allele B*35:08). FT /FTId=VAR_016407. FT STRAND 27 36 FT STRAND 41 43 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT STRAND 69 71 FT HELIX 74 76 FT HELIX 81 108 FT STRAND 113 115 FT STRAND 118 127 FT STRAND 133 142 FT STRAND 145 150 FT STRAND 157 161 FT HELIX 162 173 FT HELIX 176 185 FT HELIX 187 198 FT HELIX 200 203 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT HELIX 278 280 FT STRAND 281 286 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40455 MW; 52906854FC43E7A6 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B39_HUMAN Reviewed; 362 AA. AC P30475; O02960; O78217; P30476; P79504; Q29665; Q29697; Q29749; AC Q29847; Q29852; Q29858; Q8HWF0; Q9TPQ7; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 09-JUL-2014, entry version 121. DE RecName: Full=HLA class I histocompatibility antigen, B-39 alpha chain; DE AltName: Full=MHC class I antigen B*39; DE Flags: Precursor; GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES B*39:01 AND B*39:02). RX PubMed=8420828; DOI=10.1007/BF00191887; RA Kato N., Karaki S., Kashiwase K., Mueller C., Akaza T., Juji T., RA Kano K., Takiguchi M.; RT "Molecular analysis of HLA-B39 subtypes."; RL Immunogenetics 37:212-216(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES B*39:02 AND B*39:05). RX PubMed=7725307; DOI=10.1111/j.1399-0039.1995.tb02410.x; RA Adams E.J., Martinez-Naves E., Arnett K.L., Little A.-M., Tyan D.B., RA Parham P.; RT "HLA-B16 antigens: sequence of the ST-16 antigen, further definition RT of two B38 subtypes and evidence for convergent evolution of B*3902."; RL Tissue Antigens 45:18-26(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*39:04). RC TISSUE=Peripheral blood; RX PubMed=7533753; DOI=10.1016/0198-8859(94)90042-6; RA Ogawa A., Tokunaga K., Nakajima F., Kikuchi A., Karaki S., RA Kashiwase K., Ge J., Hannestad K., Juji T., Takiguchi M.; RT "Identification of the gene encoding a novel HLA-B39 subtype. Two RT amino acid substitutions on the beta-sheet out of the peptide-binding RT floor form a novel serological epitope."; RL Hum. Immunol. 41:241-247(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*39:09). RC TISSUE=Blood; RX PubMed=8838352; DOI=10.1111/j.1399-0039.1995.tb03135.x; RA Ramos M., Postigo J.M., Vilches C., Layrisse Z., Lopez de Castro J.A.; RT "Primary structure of a novel HLA-B39 allele (B*3909) from the Warao RT Indians of Venezuela. Further evidence for local HLA-B diversification RT in South America."; RL Tissue Antigens 46:401-404(1995). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*39:06). RX PubMed=8795147; DOI=10.1111/j.1399-0039.1996.tb02582.x; RA Zhao W., Fernandez-Vina M.A., Lazaro A.M., Araujo H.A., Miller S., RA Stastny P.; RT "Full cDNA of a novel HLA-B39 subtype, B*39061."; RL Tissue Antigens 47:435-437(1996). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELE B*39:06). RA Zhang L., Ellexson M.E., Hildebrand W.H.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*39:10). RX PubMed=8988545; DOI=10.1111/j.1399-0039.1996.tb02676.x; RA Wells R.S., Parham P.; RT "A novel recombinant HLA-B*39 allele (B*3910) in a South African RT Zulu."; RL Tissue Antigens 48:595-597(1996). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*39:10). RX PubMed=9234488; DOI=10.1111/j.1399-0039.1997.tb02814.x; RA Vilches C., Bunce M., de Pablo R., Moreno M.E., Puente S., Sanz L., RA Kreisler M.; RT "The novel HLA-Cw*1802 allele is associated with B*5703 in the Bubi RT population from Equatorial Guinea."; RL Tissue Antigens 49:644-648(1997). RN [9] RP NUCLEOTIDE SEQUENCE (ALLELE B*39:01). RA Kashiwase K.; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*39:24). RC TISSUE=Peripheral blood; RX PubMed=12558815; DOI=10.1046/j.1365-2370.2003.00362.x; RA Estefania E., Gomez-Lozano N., de Pablo R., Moreno M.E., Vilches C.; RT "Complementary DNA sequence of the HLA-B*3924 allele."; RL Eur. J. Immunogenet. 30:11-12(2003). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-362 (ALLELE B*39:08). RX PubMed=8838356; DOI=10.1111/j.1399-0039.1995.tb03139.x; RA Adams E.J., Little A.-M., Arnett K.L., McAuley J.E., Williams R.C., RA Parham P.; RT "Three new HLA-B alleles found in Mexican-Americans."; RL Tissue Antigens 46:414-416(1995). RN [12] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*39:12). RX PubMed=10372543; DOI=10.1034/j.1399-0039.1999.530504.x; RA Marcos C.Y., Fernandez-Vina M.A., Lazaro A.M., Moraes M.E., RA Moraes J.R., Stastny P.; RT "Novel HLA-A and HLA-B alleles in South American Indians."; RL Tissue Antigens 53:476-485(1999). RN [13] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*39:12). RX PubMed=10600013; DOI=10.1016/S0198-8859(99)00092-0; RA Lazaro A.M., Moraes M.E., Marcos C.Y., Moraes J.R., RA Fernandez-Vina M.A., Stastny P.; RT "Evolution of HLA-class I compared to HLA-class II polymorphism in RT Terena, a South-American Indian tribe."; RL Hum. Immunol. 60:1138-1149(1999). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*39:23). RX PubMed=11260515; DOI=10.1034/j.1399-0039.2001.057002169.x; RA Akesaka T., Kashiwase K., Ishikawa Y., Tanaka H., Shimizu M., RA Kawai S., Akaza T., Takahashi T., Juji T.; RT "Allele frequency of HLA-B39 in the Japanese population and RT identification of a novel B39 allele, B*3923."; RL Tissue Antigens 57:169-172(2001). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-196 (ALLELE B*39:07). RX PubMed=7797264; DOI=10.1007/BF00164983; RA Garber T.L., Butler L.M., Trachtenberg E.A., Erlich H.A., Rickards O., RA De Stefano G., Watkins D.I.; RT "HLA-B alleles of the Cayapa of Ecuador: new B39 and B15 alleles."; RL Immunogenetics 42:19-27(1995). RN [16] RP VARIANT [LARGE SCALE ANALYSIS] THR-65, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-39 are known: B*39:01 CC (B39.1), B*39:02 (B9.2), B*39:03, B*39:04 (B39N), B*39:05 (ST-16), CC B*39:06 (B39G), B*39:07 (B39uw3), B*39:09, B*39:10, B*39:12 CC (B3901v), B*39:23 (B39022v1) and B*39:24. The sequence shown is CC that of B*39:01. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M94052; AAA52658.1; -; Genomic_DNA. DR EMBL; M94051; AAA52660.1; -; Genomic_DNA. DR EMBL; M94053; AAA52659.1; -; Genomic_DNA. DR EMBL; U04243; AAA87396.1; -; mRNA. DR EMBL; L36318; AAA73942.1; -; mRNA. DR EMBL; L22649; AAA69861.1; -; Genomic_DNA. DR EMBL; U29480; AAC50392.1; -; mRNA. DR EMBL; L42024; AAB59484.1; -; mRNA. DR EMBL; U29083; AAC32741.1; -; mRNA. DR EMBL; U56246; AAB01985.1; -; Genomic_DNA. DR EMBL; Y09058; CAA70261.1; -; mRNA. DR EMBL; AB091216; BAC11810.1; -; Genomic_DNA. DR EMBL; AB091218; BAC11811.1; -; Genomic_DNA. DR EMBL; AF428252; AAN63555.1; -; mRNA. DR EMBL; L42280; AAB51452.1; -; Genomic_DNA. DR EMBL; AH004887; AAB39108.1; -; Genomic_DNA. DR EMBL; AB032097; BAA84116.1; -; Genomic_DNA. DR EMBL; U15640; AAA74047.1; -; Genomic_DNA. DR PIR; I38876; I38876. DR PIR; I54314; I54314. DR PIR; I54505; I54505. DR PIR; I68850; I68850. DR PIR; I84488; I84488. DR UniGene; Hs.654404; -. DR UniGene; Hs.77961; -. DR ProteinModelPortal; P30475; -. DR SMR; P30475; 25-300. DR DMDM; 231398; -. DR PRIDE; P30475; -. DR Ensembl; ENST00000425848; ENSP00000400842; ENSG00000223532. DR GeneCards; GC06M031321; -. DR GeneCards; GC06Mj31312; -. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR neXtProt; NX_P30475; -. DR HOVERGEN; HBG016709; -. DR InParanoid; P30475; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-B; human. DR CleanEx; HS_HLA-B; -. DR Genevestigator; P30475; -. DR GO; GO:0009986; C:cell surface; ISS:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; KW Host-virus interaction; Immunity; Membrane; MHC I; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-39 alpha chain. FT /FTId=PRO_0000018843. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 4 4 M -> T (in dbSNP:rs1050458). FT /FTId=VAR_056355. FT VARIANT 9 9 V -> L (in dbSNP:rs1050462). FT /FTId=VAR_056356. FT VARIANT 17 17 L -> V (in dbSNP:rs1131165). FT /FTId=VAR_056357. FT VARIANT 33 33 Y -> D (in allele B*39:12). FT /FTId=VAR_016659. FT VARIANT 35 35 S -> A (in allele B*39:04 and allele FT B*39:12; dbSNP:rs1131170). FT /FTId=VAR_016421. FT VARIANT 36 36 V -> M (in allele B*39:04; FT dbSNP:rs1050486). FT /FTId=VAR_016660. FT VARIANT 48 48 S -> A (in dbSNP:rs713031). FT /FTId=VAR_061410. FT VARIANT 48 48 S -> P (in dbSNP:rs713031). FT /FTId=VAR_061411. FT VARIANT 48 48 S -> T (in dbSNP:rs713031). FT /FTId=VAR_061412. FT VARIANT 65 65 A -> T (in dbSNP:rs1050529). FT /FTId=VAR_056358. FT VARIANT 87 87 N -> D (in dbSNP:rs1050570). FT /FTId=VAR_056359. FT VARIANT 87 87 N -> E (in allele B*39:02, allele B*39:08 FT and allele B*39:23; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016422. FT VARIANT 87 87 N -> K (in dbSNP:rs1065386). FT /FTId=VAR_059479. FT VARIANT 91 91 C -> S (in allele B*39:02, allele B*39:08 FT and allele B*39:23). FT /FTId=VAR_016423. FT VARIANT 91 91 C -> Y (in allele B*39:10). FT /FTId=VAR_016424. FT VARIANT 97 97 T -> A (in dbSNP:rs1050393). FT /FTId=VAR_056360. FT VARIANT 98 98 D -> Y (in allele B*39:05, allele B*39:07 FT and allele B*39:08; dbSNP:rs1131215). FT /FTId=VAR_016425. FT VARIANT 119 119 L -> W (in allele B*39:06). FT /FTId=VAR_016426. FT VARIANT 121 121 R -> S (in allele B*39:03 and allele FT B*39:24). FT /FTId=VAR_016427. FT VARIANT 121 121 R -> T (in allele B*39:06). FT /FTId=VAR_016428. FT VARIANT 122 122 M -> T (in allele B*39:24). FT /FTId=VAR_016429. FT VARIANT 123 123 Y -> S (in allele B*39:09). FT /FTId=VAR_016430. FT VARIANT 138 138 N -> D (in allele B*39:07). FT /FTId=VAR_016431. FT VARIANT 140 140 F -> S (in allele B*39:07). FT /FTId=VAR_016432. FT VARIANT 168 168 Q -> R (in allele B*39:23). FT /FTId=VAR_016433. FT VARIANT 180 180 L -> R (in allele B*39:08). FT /FTId=VAR_016434. FT VARIANT 306 306 V -> I (in dbSNP:rs1131500). FT /FTId=VAR_056361. FT VARIANT 329 329 A -> T (in dbSNP:rs1051488). FT /FTId=VAR_056362. SQ SEQUENCE 362 AA; 40328 MW; 422698063DEAB039 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI CKTNTQTDRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RTYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B40_HUMAN Reviewed; 362 AA. AC Q04826; O19556; O19651; P01890; P30477; P30478; Q29762; Q29842; AC Q29855; Q30173; Q31603; Q9TPT6; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 09-JUL-2014, entry version 126. DE RecName: Full=HLA class I histocompatibility antigen, B-40 alpha chain; DE AltName: Full=Bw-60; DE AltName: Full=MHC class I antigen B*40; DE Flags: Precursor; GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ALLELE B*40:01). RX PubMed=2437025; DOI=10.1007/BF00404425; RA Ways J.W., Lawlor D.A., Wan A.M., Parham P.; RT "A transposable epitope of HLA-B7, B40 molecules."; RL Immunogenetics 25:323-328(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*40:01). RX PubMed=7517584; DOI=10.1111/j.1399-0039.1994.tb02294.x; RA Little A.-M., Domena J.D., Hildebrand W.H., Shen S.Y., Barber L.D., RA Marsh S.G.E., Bias W.B., Parham P.; RT "HLA-B67: a member of the HLA-B16 family that expresses the ME1 RT epitope."; RL Tissue Antigens 43:38-43(1994). RN [3] RP PROTEIN SEQUENCE OF 25-295 (B*40:01). RX PubMed=6193808; DOI=10.1021/bi00285a036; RA Lopez de Castro J.A., Bragado R., Strong D.M., Strominger J.L.; RT "Primary structure of papain-solubilized human histocompatibility RT antigen HLA-B40 (-Bw60). An outline of alloantigenic determinants."; RL Biochemistry 22:3961-3969(1983). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*40:02). RX PubMed=1362296; DOI=10.1111/j.1399-0039.1992.tb02053.x; RA Domena J.D., Johnston-Dow L., Parham P.; RT "The B*4002 allele encodes the B61 antigen: B40* is identical to RT B61."; RL Tissue Antigens 40:254-256(1992). RN [5] RP NUCLEOTIDE SEQUENCE OF 13-318 (ALLELE B*40:02). RC TISSUE=Blood; RX PubMed=1481202; DOI=10.1111/j.1399-0039.1992.tb02054.x; RA Lin L., Watanabe Y., Tokunaga K., Kuwata S., Kohsaka T., Akaza T.; RT "A common Japanese haplotype HLA-A26-Cw3-B61-DR9-DQ3 carries HLA- RT B*4002."; RL Tissue Antigens 40:257-260(1992). RN [6] RP NUCLEOTIDE SEQUENCE (ALLELES B*40:03 AND B*40:04). RX PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [7] RP NUCLEOTIDE SEQUENCE (ALLELE B*40:05). RX PubMed=1385528; RA Hildebrand W.H., Madrigal J.A., Belich M.P., Zemmour J., Ward F.E., RA Williams R.C., Parham P.; RT "Serologic cross-reactivities poorly reflect allelic relationships in RT the HLA-B12 and HLA-B21 groups. Dominant epitopes of the alpha 2 RT helix."; RL J. Immunol. 149:3563-3568(1992). RN [8] RP NUCLEOTIDE SEQUENCE (ALLELE B*40:06). RA Herrero M.J.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE (ALLELE B*40:06). RC TISSUE=Blood; RX PubMed=12622774; DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*40:08). RX PubMed=8525480; DOI=10.1111/j.1399-0039.1995.tb03120.x; RA Adams E.J., Little A.-M., Arnett K.L., Leushner J., Parham P.; RT "Identification of a novel HLA-B40 allele (B*4008) in a patient with RT leukemia."; RL Tissue Antigens 46:204-205(1995). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-206 (ALLELE B*40:09). RX PubMed=10372543; DOI=10.1034/j.1399-0039.1999.530504.x; RA Marcos C.Y., Fernandez-Vina M.A., Lazaro A.M., Moraes M.E., RA Moraes J.R., Stastny P.; RT "Novel HLA-A and HLA-B alleles in South American Indians."; RL Tissue Antigens 53:476-485(1999). RN [12] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*40:16). RX PubMed=11098929; DOI=10.1034/j.1399-0039.2000.560401.x; RA Ellis J.M., Mack S.J., Leke R.F.G., Quakyi I., Johnson A.H., RA Hurley C.K.; RT "Diversity is demonstrated in class I HLA-A and HLA-B alleles in RT Cameroon, Africa: description of HLA-A*03012, *2612, *3006 and HLA- RT B*1403, *4016, *4703."; RL Tissue Antigens 56:291-302(2000). RN [13] RP NUCLEOTIDE SEQUENCE OF 26-206 (ALLELE B*40:27). RA Pimtanothai N., Hurley C.K.; RT "Novel HLA-B allele."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [14] RP VARIANT [LARGE SCALE ANALYSIS] ASP-138, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-40 are known: B*40:01, CC B*40:02, B*40:03 (B40-G1), B*40:04 (B40-G2), B*40:05 (BN21), CC B*40:06, B*40:08, B*40:09, B*40:16 and B*40:27. The sequence shown CC is that of B*40:02. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U03698; AAA03719.1; -; mRNA. DR EMBL; L41628; AAA65040.1; -; Genomic_DNA. DR EMBL; L09736; AAA36224.1; -; mRNA. DR EMBL; D14343; BAA03277.1; -; mRNA. DR EMBL; M84383; AAA59633.1; -; mRNA. DR EMBL; M84384; AAA59634.1; -; mRNA. DR EMBL; M84694; AAA03661.1; -; mRNA. DR EMBL; X84725; CAA59215.1; -; mRNA. DR EMBL; AJ300180; CAC15501.1; -; Genomic_DNA. DR EMBL; AJ292253; CAC29021.1; -; Genomic_DNA. DR EMBL; L41353; AAC41923.1; -; Genomic_DNA. DR EMBL; L76934; AAA96270.1; -; mRNA. DR EMBL; AH005563; AAB70252.1; -; Genomic_DNA. DR EMBL; AH008232; AAD56943.1; -; Genomic_DNA. DR PIR; I38437; HLHU40. DR PIR; I56149; I56149. DR PIR; I59655; I59655. DR PIR; I61905; I61905. DR PIR; I61906; I61906. DR PIR; S52486; S52486. DR UniGene; Hs.654404; -. DR UniGene; Hs.77961; -. DR ProteinModelPortal; Q04826; -. DR SMR; Q04826; 25-298. DR DMDM; 416557; -. DR PRIDE; Q04826; -. DR Ensembl; ENST00000359635; ENSP00000352656; ENSG00000206450. DR GeneCards; GC06M031321; -. DR GeneCards; GC06Mn31311; -. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR neXtProt; NX_Q04826; -. DR HOVERGEN; HBG016709; -. DR InParanoid; Q04826; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-B; human. DR CleanEx; HS_HLA-B; -. DR Genevestigator; Q04826; -. DR GO; GO:0009986; C:cell surface; ISS:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Host-virus interaction; Immunity; Membrane; MHC I; KW Polymorphism; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-40 alpha chain. FT /FTId=PRO_0000018844. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 9 9 L -> V (in allele B*40:01). FT /FTId=VAR_016435. FT VARIANT 14 15 WG -> SA (in allele B*40:01). FT /FTId=VAR_016436. FT VARIANT 17 17 V -> L (in allele B*40:01). FT /FTId=VAR_016437. FT VARIANT 35 36 SV -> AM (in allele B*40:01 and allele FT B*40:16). FT /FTId=VAR_016438. FT VARIANT 87 87 E -> N (in allele B*40:08; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016439. FT VARIANT 91 91 S -> F (in allele B*40:08). FT /FTId=VAR_016440. FT VARIANT 101 101 S -> N (in dbSNP:rs1050388). FT /FTId=VAR_056363. FT VARIANT 118 119 TL -> II (in allele B*40:03). FT /FTId=VAR_016441. FT VARIANT 119 119 L -> W (in allele B*40:06). FT /FTId=VAR_016442. FT VARIANT 121 121 S -> R (in allele B*40:01 and allele FT B*40:03). FT /FTId=VAR_016443. FT VARIANT 121 121 S -> T (in allele B*40:06). FT /FTId=VAR_016444. FT VARIANT 127 127 V -> L (in allele B*40:03). FT /FTId=VAR_016445. FT VARIANT 137 137 H -> Y (in allele B*40:09; FT dbSNP:rs1050379). FT /FTId=VAR_016658. FT VARIANT 138 138 N -> D (in allele B*40:04 and allele FT B*40:09). FT /FTId=VAR_016446. FT VARIANT 140 140 Y -> N (in allele B*40:27). FT /FTId=VAR_016447. FT VARIANT 140 140 Y -> S (in allele B*40:04). FT /FTId=VAR_016448. FT VARIANT 155 155 R -> S (in dbSNP:rs1050654). FT /FTId=VAR_056364. FT VARIANT 167 167 T -> S (in allele B*40:01). FT /FTId=VAR_016449. FT VARIANT 171 171 W -> L (in allele B*40:01). FT /FTId=VAR_016450. FT VARIANT 176 176 V -> E (in allele B*40:05 and allele FT B*40:16). FT /FTId=VAR_016451. FT VARIANT 180 180 L -> R (in allele B*40:16). FT /FTId=VAR_016655. FT VARIANT 187 187 E -> L (in allele B*40:05; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016452. FT VARIANT 201 202 ET -> DK (in allele B*40:01 and allele FT B*40:16). FT /FTId=VAR_016453. FT VARIANT 204 204 Q -> E (in allele B*40:01 and allele FT B*40:16). FT /FTId=VAR_016454. FT VARIANT 306 306 V -> I (in dbSNP:rs1131500). FT /FTId=VAR_056365. FT VARIANT 329 329 A -> T (in dbSNP:rs1051488). FT /FTId=VAR_056366. FT VARIANT 349 349 C -> S (in dbSNP:rs2308655). FT /FTId=VAR_061413. FT VARIANT 349 349 C -> Y (in dbSNP:rs2308655). FT /FTId=VAR_061414. FT CONFLICT 167 167 Missing (in Ref. 3; AA sequence). SQ SEQUENCE 362 AA; 40505 MW; 7D66503ACD865152 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B51_HUMAN Reviewed; 362 AA. AC P18464; O19675; O78173; P30489; Q29851; Q29857; Q96IT9; Q9MY43; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 09-JUL-2014, entry version 132. DE RecName: Full=HLA class I histocompatibility antigen, B-51 alpha chain; DE AltName: Full=MHC class I antigen B*51; DE Flags: Precursor; GN Name=HLA-B; Synonyms=HLAB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*51:01). RX PubMed=2320591; DOI=10.1073/pnas.87.7.2833; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain reaction: RT frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*51:01). RX PubMed=2909619; RA Hayashi H., Ennis P.D., Ariga H., Salter R.D., Parham P., Kano K., RA Takiguchi M.; RT "HLA-B51 and HLA-Bw52 differ by only two amino acids which are in the RT helical region of the alpha 1 domain."; RL J. Immunol. 142:306-311(1989). RN [3] RP NUCLEOTIDE SEQUENCE (ALLELE B*51:01). RX PubMed=2714852; DOI=10.1007/BF00352839; RA Pohla H., Kuon W., Tabaczewski P., Doerner C., Weiss E.H.; RT "Allelic variation in HLA-B and HLA-C sequences and the evolution of RT the HLA-B alleles."; RL Immunogenetics 29:297-307(1989). RN [4] RP NUCLEOTIDE SEQUENCE (ALLELE B*51:04). RX PubMed=1317015; DOI=10.1038/357326a0; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*51:03). RC TISSUE=Peripheral blood; RX PubMed=8248893; DOI=10.1111/j.1399-0039.1993.tb02164.x; RA Kawaguchi G., Nakayama S., Nagao T., Takiguchi M.; RT "A single amino acid substitution at residue 167 forms a novel HLA-B51 RT subtype."; RL Tissue Antigens 42:39-41(1993). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*51:02). RX PubMed=8929712; DOI=10.1111/j.1399-0039.1996.tb02513.x; RA Prilliman K., Steiner N.K., Ellexson M., Stewart D., Lau M., RA Terasaki P., Hurley C.K., Hildebrand W.H.; RT "Novel alleles HLA-B*7802 and B*51022: evidence for convergency in the RT HLA-B5 family."; RL Tissue Antigens 47:49-57(1996). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE B*51:08). RX PubMed=9243753; DOI=10.1111/j.1399-0039.1997.tb02831.x; RA Vilches C., Bunce M., de Pablo R., Murray A.K., McIntyre C.A., RA Kreisler M.; RT "Complete coding regions of two novel HLA-B alleles detected by RT phototyping (PCR-SSP) in the British Caucasoid population: B*5108 and RT B*5002."; RL Tissue Antigens 50:38-41(1997). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE B*51:01). RX PubMed=11696219; DOI=10.1034/j.1399-0039.2001.580202.x; RA Sano K., Yabuki K., Imagawa Y., Shiina T., Mizuki N., Ohno S., RA Kulski J.K., Inoko H.; RT "The absence of disease-specific polymorphisms within the HLA-B51 gene RT that is the susceptible locus for Behcet's disease."; RL Tissue Antigens 58:77-82(2001). RN [9] RP NUCLEOTIDE SEQUENCE (ALLELE B*51:01). RX PubMed=12622774; DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ALLELE B*51:01). RX PubMed=7871529; DOI=10.1111/j.1399-0039.1994.tb02394.x; RA Steinle A., Schendel D.J.; RT "HLA class I alleles of LCL 721 and 174 x CEM.T2 (T2)."; RL Tissue Antigens 44:268-270(1994). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-362 (ALLELE B*51:01). RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE B*51:24). RC TISSUE=Peripheral blood; RX PubMed=11580855; DOI=10.1034/j.1399-0039.2001.580107.x; RA Anholts J.D.H., Kemps-Mols B., Verduijn W., Oudshoorn M., RA Schreuder G.M.T.; RT "Three newly identified HLA-B alleles: B*5124, B*5306, B*5307 and RT confirmation of B*0809 and B*5606."; RL Tissue Antigens 58:38-41(2001). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-300 (B*51:01). RX PubMed=10975842; DOI=10.4049/jimmunol.165.6.3260; RA Maenaka K., Maenaka T., Tomiyama H., Takiguchi M., Stuart D.I., RA Jones E.Y.; RT "Nonstandard peptide binding revealed by crystal structures of HLA- RT B*5101 complexed with HIV immunodominant epitopes."; RL J. Immunol. 165:3260-3267(2000). RN [15] RP INVOLVEMENT IN BEHCET DISEASE. RX PubMed=15063364; DOI=10.1016/j.coph.2003.10.009; RA Arayssi T., Hamdan A.; RT "New insights into the pathogenesis and therapy of Behcet's disease."; RL Curr. Opin. Pharmacol. 4:183-188(2004). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of B-51 are known: B*51:01, CC B*51:03, B*51:04, B*51:08 and B*51:24. The sequence shown is that CC of B*51:01. CC -!- MISCELLANEOUS: There is evidence that HLA-B51 is associated with CC susceptibility to Behcet disease. However, it is not certain CC whether HLA-B51 itself or a closely linked gene is responsible for CC susceptibility. The world distribution of HLA-B51 in healthy CC people corresponds to the global distribution of Behcet disease; CC in Southern hemisphere countries (Africa, South Pacific, etc.) and CC in some parts of Europe, the prevalence of HLA-B51 in healthy CC people is low or null, corresponding to a low prevalence of Behcet CC disease. The wide variation that exists in the relative risk of CC HLA-B51 would support other nongenetic risk factors. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M32319; AAA36232.1; -; mRNA. DR EMBL; M22792; AAA59620.1; ALT_SEQ; Genomic_DNA. DR EMBL; M22786; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22787; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22788; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22789; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22790; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; M22791; AAA59620.1; JOINED; Genomic_DNA. DR EMBL; L41087; AAA64513.1; -; Genomic_DNA. DR EMBL; L41086; AAA64513.1; JOINED; Genomic_DNA. DR EMBL; Z15143; CAA78849.1; -; mRNA. DR EMBL; M80670; AAA52661.1; -; Genomic_DNA. DR EMBL; L41925; AAC41979.1; -; mRNA. DR EMBL; Y08994; CAA70198.1; -; mRNA. DR EMBL; AB056860; BAB64902.1; -; Genomic_DNA. DR EMBL; AB056862; BAB64904.1; -; Genomic_DNA. DR EMBL; AB056863; BAB64905.1; -; Genomic_DNA. DR EMBL; AB056864; BAB64906.1; -; Genomic_DNA. DR EMBL; AB056865; BAB64907.1; -; Genomic_DNA. DR EMBL; AJ278903; CAC05371.1; -; Genomic_DNA. DR EMBL; BC007243; AAH07243.1; -; mRNA. DR EMBL; AJ276995; CAB86196.1; -; Genomic_DNA. DR EMBL; Z46808; CAA86838.1; -; mRNA. DR PIR; A30345; A30345. DR PIR; I37120; I37120. DR UniGene; Hs.654404; -. DR UniGene; Hs.77961; -. DR PDB; 1E27; X-ray; 2.20 A; A=25-300. DR PDB; 1E28; X-ray; 3.00 A; A=25-300. DR PDBsum; 1E27; -. DR PDBsum; 1E28; -. DR ProteinModelPortal; P18464; -. DR SMR; P18464; 25-300. DR DIP; DIP-6150N; -. DR MINT; MINT-144207; -. DR DMDM; 122172; -. DR PRIDE; P18464; -. DR Ensembl; ENST00000359635; ENSP00000352656; ENSG00000206450. DR GeneCards; GC06M031321; -. DR GeneCards; GC06Mn31311; -. DR H-InvDB; HIX0005715; -. DR HGNC; HGNC:4932; HLA-B. DR MIM; 142830; gene. DR neXtProt; NX_P18464; -. DR HOVERGEN; HBG016709; -. DR InParanoid; P18464; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-B; human. DR EvolutionaryTrace; P18464; -. DR CleanEx; HS_HLA-B; -. DR Genevestigator; P18464; -. DR GO; GO:0009986; C:cell surface; IDA:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042612; C:MHC class I protein complex; IDA:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProt. DR GO; GO:0002486; P:antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent; IDA:UniProt. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Host-virus interaction; Immunity; Membrane; MHC I; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 362 HLA class I histocompatibility antigen, FT B-51 alpha chain. FT /FTId=PRO_0000018854. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 332 Helical; (Potential). FT TOPO_DOM 333 362 Cytoplasmic (Potential). FT DOMAIN 209 295 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 118 121 TWQT -> IIQR (in allele B*51:04). FT /FTId=VAR_016478. FT VARIANT 155 155 S -> R (in allele B*51:24). FT /FTId=VAR_017442. FT VARIANT 176 176 E -> V (in allele B*51:08). FT /FTId=VAR_016479. FT VARIANT 180 180 L -> D (in allele B*51:08; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016480. FT VARIANT 191 191 W -> G (in allele B*51:03). FT /FTId=VAR_016481. FT VARIANT 195 195 H -> Y (in allele B*51:02). FT /FTId=VAR_016482. FT STRAND 27 36 FT STRAND 45 52 FT STRAND 55 61 FT STRAND 64 66 FT HELIX 74 78 FT HELIX 81 108 FT STRAND 118 127 FT STRAND 133 142 FT STRAND 145 150 FT STRAND 157 161 FT HELIX 162 173 FT HELIX 176 185 FT HELIX 187 198 FT HELIX 200 203 FT STRAND 210 217 FT STRAND 219 235 FT STRAND 238 243 FT HELIX 249 251 FT STRAND 252 254 FT STRAND 261 263 FT STRAND 265 274 FT HELIX 278 280 FT STRAND 281 286 FT STRAND 290 292 FT STRAND 294 296 SQ SEQUENCE 362 AA; 40566 MW; D104163B4CC71F92 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE NLRIALRYYN QSEAGSHTWQ TMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1C07_HUMAN Reviewed; 366 AA. AC P10321; O78061; O78083; Q29631; Q29652; Q29867; Q29990; Q95463; AC Q95603; Q9MY31; Q9TQP9; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 3. DT 09-JUL-2014, entry version 139. DE RecName: Full=HLA class I histocompatibility antigen, Cw-7 alpha chain; DE AltName: Full=MHC class I antigen Cw*7; DE Flags: Precursor; GN Name=HLA-C; Synonyms=HLAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*07:04). RX PubMed=7482492; DOI=10.1111/j.1399-0039.1995.tb02471.x; RA Vilches C., Bunce M., de Pablo R., Herrero M.J., Kreisler M.; RT "Anchored PCR cloning of the novel HLA-Cw*0704 allele detected by PCR- RT SSP."; RL Tissue Antigens 46:19-23(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES CW*07:02 AND CW*07:04). RC TISSUE=Blood; RX PubMed=8655361; DOI=10.1016/0198-8859(95)00150-6; RA Wang H., Tokunaga K., Ishikawa Y., Asahina A., Kuwata S., Akaza T., RA Tadokoro K., Shibata Y., Takiguchi M., Juji T.; RT "Identification and DNA typing of two Cw7 alleles (Cw*0702 and RT Cw*0704) in Japanese, with the corrected sequence of Cw*0702."; RL Hum. Immunol. 45:52-58(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*07:06). RX PubMed=9008313; DOI=10.1111/j.1399-0039.1996.tb02694.x; RA Vilches C., Bunce M., Sanz L., de Pablo R., Puente S., Kreisler M.; RT "Molecular cloning of two new HLA-C alleles: Cw*1801 and Cw*0706."; RL Tissue Antigens 48:698-702(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CW*07:02). RX PubMed=9435339; DOI=10.1007/s002510050350; RA Cooper S.L., Adams E.J., Wells R.S., Walker C.M., Parham P.; RT "A major histocompatibility complex class I allele shared by two RT species of chimpanzee."; RL Immunogenetics 47:212-217(1998). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*07:11). RX PubMed=10372547; DOI=10.1034/j.1399-0039.1999.530508.x; RA Baurain J.-F., Coulie P.G.; RT "Correction of HLA-Cw*0501 and identification of HLA-Cw*0711."; RL Tissue Antigens 53:510-512(1999). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES CW*07:02 AND CW*07:04). RC TISSUE=Blood; RX PubMed=12622774; DOI=10.1034/j.1399-0039.2003.610103.x; RA Cox S.T., McWhinnie A.J., Robinson J., Marsh S.G.E., Parham P., RA Madrigal J.A., Little A.-M.; RT "Cloning and sequencing full-length HLA-B and -C genes."; RL Tissue Antigens 61:20-48(2003). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE CW*07:04). RC TISSUE=Melanoma; RA Coulie P.G.; RT "Identification of a new HLA-Cw7 allele."; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-206 (ALLELE CW*07:01). RX PubMed=7871529; DOI=10.1111/j.1399-0039.1994.tb02394.x; RA Steinle A., Schendel D.J.; RT "HLA class I alleles of LCL 721 and 174 x CEM.T2 (T2)."; RL Tissue Antigens 44:268-270(1994). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-366 (ALLELE CW*07:03). RX PubMed=3863816; RA Davidson W.F., Kress M., Khoury G., Jay G.; RT "Comparison of HLA class I gene sequences. Derivation of locus- RT specific oligonucleotide probes specific for HLA-A, HLA-B, and HLA-C RT genes."; RL J. Biol. Chem. 260:13414-13423(1985). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-206 (ALLELE CW*07:09). RX PubMed=9686604; RA Turner S., Ellexson M.E., Hickman H.D., Sidebottom D.A., RA Fernandez-Vina M., Confer D.L., Hildebrand W.H.; RT "Sequence-based typing provides a new look at HLA-C diversity."; RL J. Immunol. 161:1406-1413(1998). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-338 (ALLELE CW*07:01). RX PubMed=10488744; DOI=10.1034/j.1399-0039.1999.540208.x; RA van der Vlies S.A., Voorter C.E., van den Berg-Loonen E.M.; RT "There is more to HLA -C than exons 2 and 3: sequencing exons 1, 4 and RT 5."; RL Tissue Antigens 54:169-177(1999). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 77-309 (ALLELE CW*07:01). RX PubMed=2714852; DOI=10.1007/BF00352839; RA Pohla H., Kuon W., Tabaczewski P., Doerner C., Weiss E.H.; RT "Allelic variation in HLA-B and HLA-C sequences and the evolution of RT the HLA-B alleles."; RL Immunogenetics 29:297-307(1989). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBUNIT: Heterodimer of an alpha chain and a beta chain (beta-2- CC microglobulin). Interacts with human herpesvirus 8 MIR1 protein CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- PTM: Polyubiquitinated in a post ER compartment by interaction CC with human herpesvirus 8 MIR1 protein. This targets the protein CC for rapid degradation via the ubiquitin system (By similarity). CC -!- POLYMORPHISM: The following alleles of Cw-7 are known: Cw*07:01, CC Cw*07:02, Cw*07:03, Cw*07:04, Cw*07:06, Cw*07:09 and Cw*07:11. The CC sequence shown is that of Cw*07:02. CC -!- SIMILARITY: Belongs to the MHC class I family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X83394; CAA58313.1; -; mRNA. DR EMBL; D38526; BAA07531.1; -; mRNA. DR EMBL; D49819; BAA08625.1; -; mRNA. DR EMBL; D49552; BAA08500.1; -; mRNA. DR EMBL; X97321; CAA65986.1; -; mRNA. DR EMBL; AJ001977; CAA05125.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ010749; CAA09341.1; -; mRNA. DR EMBL; AJ293016; CAC04321.1; -; Genomic_DNA. DR EMBL; AJ293017; CAC04322.1; -; Genomic_DNA. DR EMBL; AJ291815; CAC19191.1; -; Genomic_DNA. DR EMBL; U09853; AAA50217.1; -; mRNA. DR EMBL; AL671883; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z46810; CAA86840.1; -; mRNA. DR EMBL; M11886; AAA52665.1; -; mRNA. DR EMBL; AH006132; AAC17722.1; -; Genomic_DNA. DR EMBL; Y18533; CAB71800.1; -; Genomic_DNA. DR EMBL; Y18534; CAB71800.1; JOINED; Genomic_DNA. DR EMBL; Y18535; CAB71800.1; JOINED; Genomic_DNA. DR EMBL; Y18536; CAB71800.1; JOINED; Genomic_DNA. DR EMBL; M28207; AAA53259.1; -; mRNA. DR CCDS; CCDS34393.1; -. DR PIR; A24512; HLHUC4. DR PIR; I37078; I37078. DR PIR; I37529; I37529. DR PIR; I68750; I68750. DR RefSeq; NP_002108.4; NM_002117.5. DR UniGene; Hs.656020; -. DR UniGene; Hs.743218; -. DR UniGene; Hs.77961; -. DR PDB; 3BZF; X-ray; 2.50 A; P/Q=3-11. DR PDBsum; 3BZF; -. DR ProteinModelPortal; P10321; -. DR SMR; P10321; 26-298. DR BioGrid; 109352; 22. DR DMDM; 84028168; -. DR MaxQB; P10321; -. DR PRIDE; P10321; -. DR DNASU; 3107; -. DR Ensembl; ENST00000376228; ENSP00000365402; ENSG00000204525. DR GeneID; 3107; -. DR KEGG; hsa:3107; -. DR UCSC; uc003nsy.3; human. DR CTD; 3107; -. DR GeneCards; GC06M031236; -. DR HGNC; HGNC:4933; HLA-C. DR MIM; 142840; gene. DR neXtProt; NX_P10321; -. DR PharmGKB; PA35057; -. DR HOVERGEN; HBG016709; -. DR KO; K06751; -. DR OrthoDB; EOG7JT6WQ; -. DR PhylomeDB; P10321; -. DR TreeFam; TF336617; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-C; human. DR EvolutionaryTrace; P10321; -. DR GeneWiki; HLA-C; -. DR GenomeRNAi; 3107; -. DR NextBio; 12327; -. DR ArrayExpress; P10321; -. DR Bgee; P10321; -. DR CleanEx; HS_HLA-C; -. DR Genevestigator; P10321; -. DR GO; GO:0009986; C:cell surface; IDA:UniProt. DR GO; GO:0031901; C:early endosome membrane; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProt. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0042612; C:MHC class I protein complex; ISS:UniProt. DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProt. DR GO; GO:0005102; F:receptor binding; IBA:RefGenome. DR GO; GO:0042590; P:antigen processing and presentation of exogenous peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome. DR GO; GO:0002480; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independent; TAS:Reactome. DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:InterPro. DR GO; GO:0050776; P:regulation of immune response; TAS:Reactome. DR GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.30.500.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR027648; MHC_I_a. DR InterPro; IPR001039; MHC_I_a_a1/a2. DR InterPro; IPR010579; MHC_I_a_C. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR Pfam; PF06623; MHC_I_C; 1. DR PRINTS; PR01638; MHCCLASSI. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Host-virus interaction; Immunity; Membrane; MHC I; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 24 FT CHAIN 25 366 HLA class I histocompatibility antigen, FT Cw-7 alpha chain. FT /FTId=PRO_0000018874. FT TOPO_DOM 25 308 Extracellular (Potential). FT TRANSMEM 309 333 Helical; (Potential). FT TOPO_DOM 334 366 Cytoplasmic (Potential). FT DOMAIN 209 297 Ig-like C1-type. FT REGION 25 114 Alpha-1. FT REGION 115 206 Alpha-2. FT REGION 207 298 Alpha-3. FT REGION 299 308 Connecting peptide. FT CARBOHYD 110 110 N-linked (GlcNAc...) (By similarity). FT DISULFID 125 188 By similarity. FT DISULFID 227 283 By similarity. FT VARIANT 10 10 L -> I (in dbSNP:rs2308527). FT /FTId=VAR_059506. FT VARIANT 43 43 E -> K (in dbSNP:rs1050438). FT /FTId=VAR_050345. FT VARIANT 48 48 S -> A (in dbSNP:rs707911). FT /FTId=VAR_061450. FT VARIANT 48 48 S -> P (in dbSNP:rs707911). FT /FTId=VAR_061451. FT VARIANT 48 48 S -> T (in dbSNP:rs707911). FT /FTId=VAR_061452. FT VARIANT 73 73 A -> E (in dbSNP:rs1050409). FT /FTId=VAR_050346. FT VARIANT 76 76 V -> M (in dbSNP:rs1065382). FT /FTId=VAR_050347. FT VARIANT 90 90 K -> N (in allele Cw*07:01; FT dbSNP:rs28626310). FT /FTId=VAR_016590. FT VARIANT 97 97 A -> T (in dbSNP:rs41543814). FT /FTId=VAR_050348. FT VARIANT 101 101 S -> N (in allele Cw*07:09; FT dbSNP:rs2308557). FT /FTId=VAR_016591. FT VARIANT 104 104 N -> K (in allele Cw*07:09; FT dbSNP:rs17408553). FT /FTId=VAR_016592. FT VARIANT 119 119 L -> F (in allele Cw*07:04 and allele FT Cw*07:11; dbSNP:rs1071649). FT /FTId=VAR_016593. FT VARIANT 123 123 S -> C (in dbSNP:rs1131115). FT /FTId=VAR_059507. FT VARIANT 123 123 S -> F (in dbSNP:rs1131115). FT /FTId=VAR_059508. FT VARIANT 123 123 S -> Y (in allele Cw*07:01; FT dbSNP:rs1131115). FT /FTId=VAR_016594. FT VARIANT 137 137 Y -> H (in dbSNP:rs2308574). FT /FTId=VAR_050349. FT VARIANT 140 140 S -> F (in allele Cw*07:04 and allele FT Cw*07:11; dbSNP:rs713032). FT /FTId=VAR_016595. FT VARIANT 171 171 L -> W (in allele Cw*07:03; FT dbSNP:rs1050366). FT /FTId=VAR_016646. FT VARIANT 180 180 L -> D (in allele Cw*07:04 and allele FT Cw*07:11; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016596. FT VARIANT 182 182 A -> V (in dbSNP:rs1059539). FT /FTId=VAR_050350. FT VARIANT 187 187 T -> L (in allele Cw*07:03; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016647. FT VARIANT 201 201 E -> K (in allele Cw*07:04 and allele FT Cw0711; dbSNP:rs1131103). FT /FTId=VAR_016597. FT VARIANT 208 208 P -> H (in dbSNP:rs1131096). FT /FTId=VAR_061453. FT VARIANT 208 208 P -> R (in dbSNP:rs1131096). FT /FTId=VAR_061454. FT VARIANT 272 272 V -> M (in dbSNP:rs1050276). FT /FTId=VAR_050351. FT VARIANT 328 328 V -> I (in dbSNP:rs1050118). FT /FTId=VAR_050352. FT VARIANT 330 330 A -> V (in dbSNP:rs1050105). FT /FTId=VAR_050353. FT VARIANT 331 331 M -> K (in allele Cw*07:06; FT dbSNP:rs41542414). FT /FTId=VAR_016598. FT VARIANT 331 331 M -> V (in dbSNP:rs1130935). FT /FTId=VAR_050354. FT VARIANT 348 348 A -> V (in allele Cw*07:06; FT dbSNP:rs41559915). FT /FTId=VAR_016599. FT VARIANT 350 350 C -> S (in dbSNP:rs35708511). FT /FTId=VAR_061455. FT VARIANT 363 363 T -> A (in allele Cw*07:11; FT dbSNP:rs1130838). FT /FTId=VAR_016600. FT CONFLICT 15 16 GG -> AA (in Ref. 7; AAA50217). FT CONFLICT 41 41 R -> A (in Ref. 10; AAA52665). FT CONFLICT 309 309 M -> V (in Ref. 13; AAA53259). SQ SEQUENCE 366 AA; 40649 MW; 59C23D95FD1D0BC8 CRC64; MRVMAPRALL LLLSGGLALT ETWACSHSMR YFDTAVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV SLRNLRGYYN QSEDGSHTLQ RMSGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK LEAARAAEQL RAYLEGTCVE WLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL QEPLTLSWEP SSQPTIPIMG IVAGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA // ID 2A5D_HUMAN Reviewed; 602 AA. AC Q14738; A8K3I9; B5BUA6; O00494; O00696; Q15171; Q5TC39; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-JUL-2014, entry version 154. DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform; DE AltName: Full=PP2A B subunit isoform B'-delta; DE AltName: Full=PP2A B subunit isoform B56-delta; DE AltName: Full=PP2A B subunit isoform PR61-delta; DE AltName: Full=PP2A B subunit isoform R5-delta; GN Name=PPP2R5D; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA-1). RC TISSUE=Fetal brain; RX PubMed=8703017; DOI=10.1074/jbc.271.36.22081; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS DELTA-1 AND DELTA-3). RC TISSUE=Brain cortex; RX PubMed=9180267; DOI=10.1016/S0014-5793(97)00392-X; RA Tanabe O., Gomez G.A., Nishito Y., Usui H., Takeda M.; RT "Molecular heterogeneity of the cDNA encoding a 74-kDa regulatory RT subunit (B'' or delta) of human protein phosphatase 2A."; RL FEBS Lett. 408:52-56(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA-2), AND PROTEIN SEQUENCE OF RP 501-508; 550-559; 573-580 AND 584-601 (DELTA-1). RC TISSUE=Bone marrow, and Brain cortex; RX PubMed=8566219; DOI=10.1016/0014-5793(95)01500-0; RA Tanabe O., Nagase T., Murakami T., Nozaki H., Usui H., Nishito Y., RA Hayashi H., Kagamiyama H., Takeda M.; RT "Molecular cloning of a 74-kDa regulatory subunit (B'' or delta) of RT human protein phosphatase 2A."; RL FEBS Lett. 379:107-111(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA-2). RC TISSUE=Heart; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DELTA-1). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., RA Isogai T., Imai J., Watanabe S., Nomura N.; RT "Human protein factory for converting the transcriptome into an in RT vitro-expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS DELTA-1 AND DELTA-2). RC TISSUE=Colon, Eye, and Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP INTERACTION WITH SGOL1. RX PubMed=16541025; DOI=10.1038/nature04663; RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., RA Kawashima S.A., Watanabe Y.; RT "Shugoshin collaborates with protein phosphatase 2A to protect RT cohesin."; RL Nature 441:46-52(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP VARIANT SER-53. RX PubMed=23033978; DOI=10.1056/NEJMoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., RA Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., RA Brunner H.G., Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(2012). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. Interacts with SGOL1. CC -!- INTERACTION: CC O08785:Clock (xeno); NbExp=2; IntAct=EBI-396563, EBI-79859; CC Q13136:PPFIA1; NbExp=2; IntAct=EBI-396563, EBI-745426; CC P30153:PPP2R1A; NbExp=4; IntAct=EBI-396563, EBI-302388; CC P30154:PPP2R1B; NbExp=2; IntAct=EBI-396563, EBI-357094; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear in CC interphase, nuclear during mitosis. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Delta-1; CC IsoId=Q14738-1; Sequence=Displayed; CC Name=Delta-2; CC IsoId=Q14738-2; Sequence=VSP_005111; CC Name=Delta-3; CC IsoId=Q14738-3; Sequence=VSP_005110; CC -!- TISSUE SPECIFICITY: Isoform Delta-2 is widely expressed. Isoform CC Delta-1 is highly expressed in brain. CC -!- INDUCTION: By retinoic acid; in neuroblastoma cell lines. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L76702; AAB69751.1; -; mRNA. DR EMBL; AB000634; BAA20381.1; -; mRNA. DR EMBL; AB000635; BAA20382.1; -; mRNA. DR EMBL; D78360; BAA11372.1; -; mRNA. DR EMBL; AK290604; BAF83293.1; -; mRNA. DR EMBL; AB451342; BAG70156.1; -; mRNA. DR EMBL; AB451357; BAG70171.1; -; mRNA. DR EMBL; AL136304; CAI19791.1; -; Genomic_DNA. DR EMBL; CH471081; EAX04133.1; -; Genomic_DNA. DR EMBL; BC010692; AAH10692.1; -; mRNA. DR EMBL; BC001095; AAH01095.1; -; mRNA. DR EMBL; BC001175; AAH01175.1; -; mRNA. DR CCDS; CCDS43464.1; -. [Q14738-3] DR CCDS; CCDS4878.1; -. [Q14738-1] DR CCDS; CCDS55002.1; -. [Q14738-2] DR PIR; S68686; S68686. DR RefSeq; NP_001257405.1; NM_001270476.1. DR RefSeq; NP_006236.1; NM_006245.3. [Q14738-1] DR RefSeq; NP_851307.1; NM_180976.2. [Q14738-2] DR RefSeq; NP_851308.1; NM_180977.2. [Q14738-3] DR UniGene; Hs.533308; -. DR ProteinModelPortal; Q14738; -. DR SMR; Q14738; 110-512. DR BioGrid; 111520; 32. DR DIP; DIP-29961N; -. DR IntAct; Q14738; 26. DR MINT; MINT-5006095; -. DR STRING; 9606.ENSP00000417963; -. DR PhosphoSite; Q14738; -. DR DMDM; 7387495; -. DR MaxQB; Q14738; -. DR PaxDb; Q14738; -. DR PRIDE; Q14738; -. DR DNASU; 5528; -. DR Ensembl; ENST00000394110; ENSP00000377669; ENSG00000112640. [Q14738-2] DR Ensembl; ENST00000461010; ENSP00000420674; ENSG00000112640. [Q14738-3] DR Ensembl; ENST00000485511; ENSP00000417963; ENSG00000112640. [Q14738-1] DR GeneID; 5528; -. DR KEGG; hsa:5528; -. DR UCSC; uc003oth.4; human. [Q14738-1] DR UCSC; uc010jyd.4; human. [Q14738-3] DR UCSC; uc021yzq.2; human. [Q14738-2] DR CTD; 5528; -. DR GeneCards; GC06P042952; -. DR HGNC; HGNC:9312; PPP2R5D. DR HPA; HPA029045; -. DR HPA; HPA029046; -. DR MIM; 601646; gene. DR neXtProt; NX_Q14738; -. DR PharmGKB; PA33676; -. DR eggNOG; NOG264925; -. DR HOVERGEN; HBG000009; -. DR InParanoid; Q14738; -. DR KO; K11584; -. DR OMA; GSGRAEM; -. DR OrthoDB; EOG7C2R2S; -. DR PhylomeDB; Q14738; -. DR TreeFam; TF105556; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_21300; Mitotic M-M/G1 phases. DR Reactome; REACT_604; Hemostasis. DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines. DR Reactome; REACT_6900; Immune System. DR SignaLink; Q14738; -. DR GeneWiki; PPP2R5D; -. DR GenomeRNAi; 5528; -. DR NextBio; 21410; -. DR PRO; PR:Q14738; -. DR ArrayExpress; Q14738; -. DR Bgee; Q14738; -. DR CleanEx; HS_PPP2R5D; -. DR Genevestigator; Q14738; -. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:ProtInc. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:Reactome. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome. DR GO; GO:0016311; P:dephosphorylation; TAS:GOC. DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome. DR GO; GO:0006006; P:glucose metabolic process; TAS:Reactome. DR GO; GO:0006096; P:glycolytic process; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:0050790; P:regulation of catalytic activity; TAS:GOC. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome. DR GO; GO:0034166; P:toll-like receptor 10 signaling pathway; TAS:Reactome. DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; TAS:Reactome. DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; TAS:Reactome. DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; TAS:Reactome. DR GO; GO:0034146; P:toll-like receptor 5 signaling pathway; TAS:Reactome. DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; TAS:Reactome. DR GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; TAS:Reactome. DR GO; GO:0038124; P:toll-like receptor TLR6:TLR2 signaling pathway; TAS:Reactome. DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR002554; PP2A_B56. DR PANTHER; PTHR10257; PTHR10257; 1. DR Pfam; PF01603; B56; 1. DR PIRSF; PIRSF028043; PP2A_B56; 1. DR SUPFAM; SSF48371; SSF48371; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat. FT CHAIN 1 602 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit delta isoform. FT /FTId=PRO_0000071452. FT REPEAT 37 38 1. FT REPEAT 39 40 2. FT REPEAT 41 42 3. FT REPEAT 43 44 4. FT REPEAT 45 46 5. FT REPEAT 47 48 6; approximate. FT REPEAT 49 50 7; approximate. FT REPEAT 51 52 8. FT REGION 37 52 8 X 2 AA approximate tandem repeats of Q- FT P. FT MOTIF 523 530 SH3-binding; class I (Potential). FT MOTIF 548 565 Nuclear localization signal (Potential). FT MOD_RES 573 573 Phosphoserine. FT MOD_RES 598 598 Phosphoserine. FT VAR_SEQ 11 116 Missing (in isoform Delta-3). FT /FTId=VSP_005110. FT VAR_SEQ 85 116 Missing (in isoform Delta-2). FT /FTId=VSP_005111. FT VARIANT 53 53 P -> S (found in a patient with delayed FT psychomotor development, no speech and FT cataracts). FT /FTId=VAR_069414. SQ SEQUENCE 602 AA; 69992 MW; F15F71AF4E565387 CRC64; MPYKLKKEKE PPKVAKCTAK PSSSGKDGGG ENTEEAQPQP QPQPQPQAQS QPPSSNKRPS NSTPPPTQLS KIKYSGGPQI VKKERRQSSS RFNLSKNREL QKLPALKDSP TQEREELFIQ KLRQCCVLFD FVSDPLSDLK FKEVKRAGLN EMVEYITHSR DVVTEAIYPE AVTMFSVNLF RTLPPSSNPT GAEFDPEEDE PTLEAAWPHL QLVYEFFLRF LESPDFQPNI AKKYIDQKFV LALLDLFDSE DPRERDFLKT ILHRIYGKFL GLRAYIRRQI NHIFYRFIYE TEHHNGIAEL LEILGSIING FALPLKEEHK MFLIRVLLPL HKVKSLSVYH PQLAYCVVQF LEKESSLTEP VIVGLLKFWP KTHSPKEVMF LNELEEILDV IEPSEFSKVM EPLFRQLAKC VSSPHFQVAE RALYYWNNEY IMSLISDNAA RVLPIMFPAL YRNSKSHWNK TIHGLIYNAL KLFMEMNQKL FDDCTQQYKA EKQKGRFRMK EREEMWQKIE ELARLNPQYP MFRAPPPLPP VYSMETETPT AEDIQLLKRT VETEAVQMLK DIKKEKVLLR RKSELPQDVY TIKALEAHKR AEEFLTASQE AL // ID 2A5G_HUMAN Reviewed; 524 AA. AC Q13362; B4DYJ8; B5BUA5; F5GWP3; Q14391; Q15060; Q15174; Q6ZN33; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 09-JUL-2014, entry version 145. DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform; DE AltName: Full=PP2A B subunit isoform B'-gamma; DE AltName: Full=PP2A B subunit isoform B56-gamma; DE AltName: Full=PP2A B subunit isoform PR61-gamma; DE AltName: Full=PP2A B subunit isoform R5-gamma; DE AltName: Full=Renal carcinoma antigen NY-REN-29; GN Name=PPP2R5C; Synonyms=KIAA0044; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-3). RC TISSUE=Umbilical vein; RX PubMed=8617797; DOI=10.1074/jbc.271.9.5164; RA Tehrani M.A., Mumby M.C., Kamibayashi C.; RT "Identification of a novel protein phosphatase 2A regulatory subunit RT highly expressed in muscle."; RL J. Biol. Chem. 271:5164-5170(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA-1). RC TISSUE=Fetal retina; RX PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND PARTIAL RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Hippocampus, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA-3). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., RA Isogai T., Imai J., Watanabe S., Nomura N.; RT "Human protein factory for converting the transcriptome into an in RT vitro-expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., RA Quetier F., Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-524 (ISOFORM GAMMA-2). RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-524 (ISOFORM GAMMA-1). RX PubMed=7592815; DOI=10.1074/jbc.270.44.26123; RA McCright B., Virshup D.M.; RT "Identification of a new family of protein phosphatase 2A regulatory RT subunits."; RL J. Biol. Chem. 270:26123-26128(1995). RN [9] RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX PubMed=8703017; DOI=10.1074/jbc.271.36.22081; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). RN [10] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal- RT cell carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SGOL1, AND RP SUBCELLULAR LOCATION. RX PubMed=16580887; DOI=10.1016/j.devcel.2006.03.010; RA Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.; RT "PP2A is required for centromeric localization of Sgo1 and proper RT chromosome segregation."; RL Dev. Cell 10:575-585(2006). RN [12] RP FUNCTION, INTERACTION WITH IER3 AND ERK KINASES, AND PHOSPHORYLATION. RX PubMed=16456541; DOI=10.1038/sj.emboj.7600980; RA Letourneux C., Rocher G., Porteu F.; RT "B56-containing PP2A dephosphorylate ERK and their activity is RT controlled by the early gene IEX-1 and ERK."; RL EMBO J. 25:727-738(2006). RN [13] RP INTERACTION WITH SGOL1. RX PubMed=16541025; DOI=10.1038/nature04663; RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., RA Kawashima S.A., Watanabe Y.; RT "Shugoshin collaborates with protein phosphatase 2A to protect RT cohesin."; RL Nature 441:46-52(2006). RN [14] RP FUNCTION, INTERACTION WITH TP53, AND INDUCTION. RX PubMed=17245430; DOI=10.1038/sj.emboj.7601519; RA Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.; RT "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage- RT induced dephosphorylation of p53 at Thr55."; RL EMBO J. 26:402-411(2007). RN [15] RP INTERACTION WITH TP53. RX PubMed=17967874; DOI=10.1128/MCB.00983-07; RA Shouse G.P., Cai X., Liu X.; RT "Serine 15 phosphorylation of p53 directs its interaction with RT B56gamma and the tumor suppressor activity of B56gamma-specific RT protein phosphatase 2A."; RL Mol. Cell. Biol. 28:448-456(2008). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-442 IN COMPLEX WITH PPP2CA RP AND PPP2R1A. RX PubMed=17174897; DOI=10.1016/j.cell.2006.11.033; RA Xu Y., Xing Y., Chen Y., Chao Y., Lin Z., Fan E., Yu J.W., Strack S., RA Jeffrey P.D., Shi Y.; RT "Structure of the protein phosphatase 2A holoenzyme."; RL Cell 127:1239-1251(2006). RN [18] RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 30-436 IN COMPLEX WITH RP PPP2CA AND PPP2R1A. RX PubMed=17086192; DOI=10.1038/nature05351; RA Cho U.S., Xu W.; RT "Crystal structure of a protein phosphatase 2A heterotrimeric RT holoenzyme."; RL Nature 445:53-57(2007). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 34-436 IN COMPLEX WITH RP PPP2CA; PPP2R1A AND SGOL1. RX PubMed=19716788; DOI=10.1016/j.molcel.2009.06.031; RA Xu Z., Cetin B., Anger M., Cho U.S., Helmhart W., Nasmyth K., Xu W.; RT "Structure and function of the PP2A-shugoshin interaction."; RL Mol. Cell 35:426-441(2009). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 11-380. RX PubMed=18618707; DOI=10.1002/prot.22150; RA Magnusdottir A., Stenmark P., Flodin S., Nyman T., Kotenyova T., RA Graeslund S., Ogg D., Nordlund P.; RT "The structure of the PP2A regulatory subunit B56 gamma: the remaining RT piece of the PP2A jigsaw puzzle."; RL Proteins 74:212-221(2009). CC -!- FUNCTION: The B regulatory subunit might modulate substrate CC selectivity and catalytic activity, and also might direct the CC localization of the catalytic enzyme to a particular subcellular CC compartment. The PP2A-PPP2R5C holoenzyme may specifically CC dephosphorylate and activate TP53 and play a role in DNA damage- CC induced inhibition of cell proliferation. PP2A-PPP2R5C may also CC regulate the ERK signaling pathway through ERK dephosphorylation. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and CC PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), CC that associates with a variety of regulatory subunits. Proteins CC that associate with the core dimer include three families of CC regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 CC and R5/B'/B56 families), the 48 kDa variable regulatory subunit, CC viral proteins, and cell signaling molecules. Interacts with CC PPP2CA AND PPP2R1A; the interaction is direct. Interacts with CC SGOL1; the interaction is direct. Isoform 1 and isoform 2 interact CC with TP53 (phosphorylated at Ser-15 by ATM); increased upon DNA CC damage it drives PP2A-mediated dephosphorylation of TP53 at Thr- CC 55. Interacts with IER3 and/or ERK kinases; regulates ERK CC dephosphorylation. CC -!- INTERACTION: CC O96017:CHEK2; NbExp=4; IntAct=EBI-1266176, EBI-1180783; CC P46695:IER3; NbExp=2; IntAct=EBI-1266156, EBI-1748945; CC Q00987:MDM2; NbExp=5; IntAct=EBI-1266156, EBI-389668; CC P67775:PPP2CA; NbExp=7; IntAct=EBI-1266156, EBI-712311; CC P30153:PPP2R1A; NbExp=6; IntAct=EBI-1266156, EBI-302388; CC P30154:PPP2R1B; NbExp=2; IntAct=EBI-1266156, EBI-357094; CC P04637:TP53; NbExp=3; IntAct=EBI-1266156, EBI-366083; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=Gamma-3; CC IsoId=Q13362-1; Sequence=Displayed; CC Name=Gamma-1; CC IsoId=Q13362-2; Sequence=VSP_005112; CC Name=Gamma-2; CC IsoId=Q13362-3; Sequence=VSP_005113; CC Name=4; CC IsoId=Q13362-4; Sequence=VSP_043645, VSP_005113; CC Note=No experimental confirmation available; CC Name=5; CC IsoId=Q13362-5; Sequence=VSP_046768; CC Note=Ref.3 (BAG63760) sequence is in conflict in position: CC 3:N->K. No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highest levels in heart, skeletal muscle and CC brain. Lower levels in pancreas, kidney, lung and placenta. Very CC low levels in liver. CC -!- INDUCTION: Up-regulated upon DNA damage. CC -!- PTM: Isoform Gamma-3 is phosphorylated on serine residues. Isoform CC Gamma-1 phosphorylation by ERK2 is IER3-dependent and inhibits ERK CC dephosphorylation by PP2A-PPP2R5C. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56 CC family. CC -!- SEQUENCE CAUTION: CC Sequence=AAC50387.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAG63760.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U37352; AAC50387.1; ALT_INIT; mRNA. DR EMBL; Z69030; CAA93154.1; -; mRNA. DR EMBL; AK131391; BAD18542.1; -; mRNA. DR EMBL; AK302470; BAG63760.1; ALT_INIT; mRNA. DR EMBL; AB451341; BAG70155.1; -; mRNA. DR EMBL; AL118558; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137779; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471061; EAW81756.1; -; Genomic_DNA. DR EMBL; D26445; BAA05465.1; -; mRNA. DR EMBL; L42375; AAC37603.1; -; mRNA. DR CCDS; CCDS45163.1; -. [Q13362-2] DR CCDS; CCDS53911.1; -. [Q13362-4] DR CCDS; CCDS53912.1; -. [Q13362-5] DR CCDS; CCDS9964.1; -. [Q13362-1] DR CCDS; CCDS9965.1; -. [Q13362-3] DR RefSeq; NP_001155197.1; NM_001161725.1. [Q13362-5] DR RefSeq; NP_001155198.1; NM_001161726.1. [Q13362-4] DR RefSeq; NP_002710.2; NM_002719.3. [Q13362-1] DR RefSeq; NP_848701.1; NM_178586.2. [Q13362-3] DR RefSeq; NP_848702.1; NM_178587.2. [Q13362-2] DR RefSeq; XP_005267884.1; XM_005267827.1. DR UniGene; Hs.368264; -. DR PDB; 2IAE; X-ray; 3.50 A; B/E=30-436. DR PDB; 2JAK; X-ray; 2.60 A; A=11-380. DR PDB; 2NPP; X-ray; 3.30 A; B/E=1-442. DR PDB; 2NYL; X-ray; 3.80 A; B/E=38-425. DR PDB; 2NYM; X-ray; 3.60 A; B/E=38-425. DR PDB; 3FGA; X-ray; 2.70 A; B=34-436. DR PDBsum; 2IAE; -. DR PDBsum; 2JAK; -. DR PDBsum; 2NPP; -. DR PDBsum; 2NYL; -. DR PDBsum; 2NYM; -. DR PDBsum; 3FGA; -. DR ProteinModelPortal; Q13362; -. DR SMR; Q13362; 34-436. DR BioGrid; 111519; 26. DR DIP; DIP-39401N; -. DR IntAct; Q13362; 18. DR MINT; MINT-2835438; -. DR STRING; 9606.ENSP00000333905; -. DR PhosphoSite; Q13362; -. DR DMDM; 116241235; -. DR MaxQB; Q13362; -. DR PaxDb; Q13362; -. DR PRIDE; Q13362; -. DR DNASU; 5527; -. DR Ensembl; ENST00000328724; ENSP00000329009; ENSG00000078304. [Q13362-4] DR Ensembl; ENST00000334743; ENSP00000333905; ENSG00000078304. [Q13362-1] DR Ensembl; ENST00000350249; ENSP00000262239; ENSG00000078304. [Q13362-3] DR Ensembl; ENST00000422945; ENSP00000412324; ENSG00000078304. [Q13362-5] DR Ensembl; ENST00000445439; ENSP00000408389; ENSG00000078304. [Q13362-2] DR GeneID; 5527; -. DR KEGG; hsa:5527; -. DR UCSC; uc001ykk.3; human. [Q13362-4] DR UCSC; uc001ykn.3; human. [Q13362-2] DR UCSC; uc001yko.3; human. [Q13362-1] DR UCSC; uc001ykp.3; human. [Q13362-3] DR CTD; 5527; -. DR GeneCards; GC14P102228; -. DR HGNC; HGNC:9311; PPP2R5C. DR HPA; HPA027553; -. DR MIM; 601645; gene. DR neXtProt; NX_Q13362; -. DR PharmGKB; PA33674; -. DR eggNOG; NOG264925; -. DR HOGENOM; HOG000067326; -. DR HOVERGEN; HBG000009; -. DR KO; K11584; -. DR OMA; SERWEAD; -. DR PhylomeDB; Q13362; -. DR TreeFam; TF105556; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_21300; Mitotic M-M/G1 phases. DR Reactome; REACT_604; Hemostasis. DR Reactome; REACT_6900; Immune System. DR SignaLink; Q13362; -. DR ChiTaRS; PPP2R5C; human. DR EvolutionaryTrace; Q13362; -. DR GeneWiki; PPP2R5C; -. DR GenomeRNAi; 5527; -. DR NextBio; 21400; -. DR PMAP-CutDB; Q13362; -. DR PRO; PR:Q13362; -. DR ArrayExpress; Q13362; -. DR Bgee; Q13362; -. DR CleanEx; HS_PPP2R5C; -. DR Genevestigator; Q13362; -. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; IDA:UniProtKB. DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IDA:UniProtKB. DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:MGI. DR GO; GO:0050790; P:regulation of catalytic activity; IDA:GOC. DR GO; GO:0007165; P:signal transduction; NAS:UniProtKB. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR002554; PP2A_B56. DR PANTHER; PTHR10257; PTHR10257; 1. DR Pfam; PF01603; B56; 1. DR PIRSF; PIRSF028043; PP2A_B56; 1. DR SUPFAM; SSF48371; SSF48371; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Centromere; KW Chromosome; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome. FT CHAIN 1 524 Serine/threonine-protein phosphatase 2A FT 56 kDa regulatory subunit gamma isoform. FT /FTId=PRO_0000071457. FT MOTIF 416 422 Nuclear localization signal (Potential). FT MOD_RES 1 1 N-acetylmethionine. FT VAR_SEQ 1 31 MLTCNKAGSRMVVDAANSNGPFQPVVLLHIR -> MPNKNK FT KEKESPKAGKSGKSSKEGQDTVESEQISVRKNSLVAVPSTV FT SAKIKVPVSQPIVKKDKRQNSSRFSASNNRELQKLPSLK FT (in isoform 4). FT /FTId=VSP_043645. FT VAR_SEQ 1 30 MLTCNKAGSRMVVDAANSNGPFQPVVLLHI -> MPNKNKK FT EKESPKAGKSGKSSKEGQDTVESEGTSPEEPSSPKVPPPLL FT PELLVLIFGGLQG (in isoform 5). FT /FTId=VSP_046768. FT VAR_SEQ 443 524 YTVYSQASTMSIPVAMETDGPLFEDVQMLRKTVKDEAHQAQ FT KDPKKDRPLARRKSELPQDPHTKKALEAHCRADELASQDGR FT -> VLKKRIT (in isoform Gamma-1). FT /FTId=VSP_005112. FT VAR_SEQ 443 481 Missing (in isoform Gamma-2 and isoform FT 4). FT /FTId=VSP_005113. FT VARIANT 515 515 A -> P (in dbSNP:rs3742424). FT /FTId=VAR_051745. FT CONFLICT 494 494 R -> L (in Ref. 1; AAC50387). FT HELIX 40 48 FT STRAND 55 58 FT STRAND 59 62 FT HELIX 63 80 FT STRAND 83 85 FT HELIX 91 103 FT STRAND 115 118 FT HELIX 120 122 FT HELIX 131 146 FT HELIX 152 155 FT TURN 156 158 FT HELIX 161 170 FT HELIX 176 192 FT HELIX 194 196 FT HELIX 197 212 FT TURN 213 215 FT HELIX 221 233 FT HELIX 241 249 FT HELIX 252 255 FT HELIX 258 262 FT HELIX 264 277 FT HELIX 279 281 FT HELIX 282 291 FT HELIX 301 313 FT HELIX 317 335 FT HELIX 340 347 FT HELIX 348 351 FT HELIX 353 361 FT HELIX 363 366 FT TURN 367 369 FT TURN 372 377 FT HELIX 384 398 FT HELIX 409 430 SQ SEQUENCE 524 AA; 61061 MW; B9CBF54550D713F8 CRC64; MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK LKMKEREEAW VKIENLAKAN PQYTVYSQAS TMSIPVAMET DGPLFEDVQM LRKTVKDEAH QAQKDPKKDR PLARRKSELP QDPHTKKALE AHCRADELAS QDGR // ID 2AAA_HUMAN Reviewed; 589 AA. AC P30153; Q13773; Q6ICQ3; Q96DH3; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 4. DT 09-JUL-2014, entry version 150. DE RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform; DE AltName: Full=Medium tumor antigen-associated 61 kDa protein; DE AltName: Full=PP2A subunit A isoform PR65-alpha; DE AltName: Full=PP2A subunit A isoform R1-alpha; GN Name=PPP2R1A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 242-255. RC TISSUE=Placenta; RX PubMed=2554323; DOI=10.1073/pnas.86.22.8669; RA Walter G., Ferre F., Espiritu O., Carbone-Wiley A.; RT "Molecular cloning and sequence of cDNA encoding polyoma medium tumor RT antigen-associated 61-kDa protein."; RL Proc. Natl. Acad. Sci. U.S.A. 86:8669-8672(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2159327; DOI=10.1021/bi00465a002; RA Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., RA Merlevede W., Hofsteenge J., Stone S.R.; RT "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A RT have a similar 39 amino acid repeating structure."; RL Biochemistry 29:3166-3173(1990). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 34-46, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [6] RP PROTEIN SEQUENCE OF 204-214; 261-272 AND 521-527. RX PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [7] RP BINDING DOMAINS. RX PubMed=8254721; RA Ruediger R., Hentz M., Fait J., Mumby M., Walter G.; RT "Molecular model of the A subunit of protein phosphatase 2A: RT interaction with other subunits and tumor antigens."; RL J. Virol. 68:123-129(1994). RN [8] RP INTERACTION WITH IPO9. RX PubMed=12670497; DOI=10.1016/S0006-291X(03)00434-0; RA Lubert E.J., Sarge K.D.; RT "Interaction between protein phosphatase 2A and members of the RT importin beta superfamily."; RL Biochem. Biophys. Res. Commun. 303:908-913(2003). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, RP AND INTERACTION WITH SGOL1. RX PubMed=16580887; DOI=10.1016/j.devcel.2006.03.010; RA Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.; RT "PP2A is required for centromeric localization of Sgo1 and proper RT chromosome segregation."; RL Dev. Cell 10:575-585(2006). RN [10] RP INTERACTION WITH TP53. RX PubMed=17245430; DOI=10.1038/sj.emboj.7601519; RA Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.; RT "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage- RT induced dephosphorylation of p53 at Thr55."; RL EMBO J. 26:402-411(2007). RN [11] RP INTERACTION WITH PLA2G16. RX PubMed=17374643; DOI=10.1242/jcs.000018; RA Nazarenko I., Schafer R., Sers C.; RT "Mechanisms of the HRSL3 tumor suppressor function in ovarian RT carcinoma cells."; RL J. Cell Sci. 120:1393-1404(2007). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP INTERACTION WITH CTTNBP2NL. RX PubMed=18782753; DOI=10.1074/mcp.M800266-MCP200; RA Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., RA Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., RA Aebersold R., Raught B., Gingras A.C.; RT "A PP2A phosphatase high density interaction network identifies a RT novel striatin-interacting phosphatase and kinase complex linked to RT the cerebral cavernous malformation 3 (CCM3) protein."; RL Mol. Cell. Proteomics 8:157-171(2009). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=9989501; DOI=10.1016/S0092-8674(00)80963-0; RA Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D.; RT "The structure of the protein phosphatase 2A PR65/A subunit reveals RT the conformation of its 15 tandemly repeated HEAT motifs."; RL Cell 96:99-110(1999). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 9-589 IN COMPLEX WITH WITH RP PPP2CA AND PPME1. RX PubMed=18394995; DOI=10.1016/j.cell.2008.02.041; RA Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y.; RT "Structural mechanism of demethylation and inactivation of protein RT phosphatase 2A."; RL Cell 133:154-163(2008). CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit. Required for proper CC chromosome segregation and for centromeric localization of SGOL1 CC in mitosis. CC -!- SUBUNIT: Found in a complex with at least ARL2, PPP2CB, PPP2R1A, CC PPP2R2A, PPP2R5E and TBCD. Interacts with FOXO1; the interaction CC dephosphorylates FOXO1 on AKT-mediated phosphoylation sites (By CC similarity). PP2A consists of a common heterodimeric core enzyme, CC composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and CC PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), CC that associates with a variety of regulatory subunits. Proteins CC that associate with the core dimer include three families of CC regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 CC and R5/B'/B56 families), the 48 kDa variable regulatory subunit, CC viral proteins, and cell signaling molecules. Interacts with IPO9. CC Interacts with TP53 and SGOL1. Interacts with PLA2G16; this CC interaction might decrease PP2A activity. Interacts with CC CTTNBP2NL. CC -!- INTERACTION: CC P03081:- (xeno); NbExp=3; IntAct=EBI-302388, EBI-1266256; CC P31749:AKT1; NbExp=2; IntAct=EBI-302388, EBI-296087; CC P03129:E7 (xeno); NbExp=3; IntAct=EBI-302388, EBI-866453; CC P04020:E7 (xeno); NbExp=2; IntAct=EBI-302388, EBI-7005254; CC Q8TCG1:KIAA1524; NbExp=4; IntAct=EBI-302388, EBI-1379376; CC P97346:Nxn (xeno); NbExp=2; IntAct=EBI-302388, EBI-309684; CC P53816:PLA2G16; NbExp=7; IntAct=EBI-302388, EBI-746318; CC P67775:PPP2CA; NbExp=14; IntAct=EBI-302388, EBI-712311; CC P63151:PPP2R2A; NbExp=8; IntAct=EBI-302388, EBI-1048931; CC Q00005:PPP2R2B; NbExp=5; IntAct=EBI-302388, EBI-1052159; CC Q15172:PPP2R5A; NbExp=3; IntAct=EBI-302388, EBI-641666; CC Q13362:PPP2R5C; NbExp=6; IntAct=EBI-302388, EBI-1266156; CC Q13362-1:PPP2R5C; NbExp=5; IntAct=EBI-302388, EBI-1266170; CC Q13362-2:PPP2R5C; NbExp=2; IntAct=EBI-302388, EBI-1266173; CC Q60996-3:Ppp2r5c (xeno); NbExp=2; IntAct=EBI-302388, EBI-1369292; CC Q14738:PPP2R5D; NbExp=4; IntAct=EBI-302388, EBI-396563; CC Q16537:PPP2R5E; NbExp=3; IntAct=EBI-302388, EBI-968374; CC P60510:PPP4C; NbExp=3; IntAct=EBI-302388, EBI-1046072; CC P53041:PPP5C; NbExp=3; IntAct=EBI-302388, EBI-716663; CC Q04206:RELA; NbExp=2; IntAct=EBI-302388, EBI-73886; CC O43815:STRN; NbExp=4; IntAct=EBI-302388, EBI-1046642; CC P04637:TP53; NbExp=2; IntAct=EBI-302388, EBI-366083; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Chromosome, CC centromere. Note=Centromeric localization requires the presence of CC BUB1. CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M31786; AAA35531.1; -; mRNA. DR EMBL; J02902; AAA36399.1; -; mRNA. DR EMBL; CR450340; CAG29336.1; -; mRNA. DR EMBL; BC001537; AAH01537.1; -; mRNA. DR CCDS; CCDS12849.1; -. DR PIR; A34541; A34541. DR RefSeq; NP_055040.2; NM_014225.5. DR UniGene; Hs.467192; -. DR PDB; 1B3U; X-ray; 2.30 A; A/B=2-589. DR PDB; 2IE3; X-ray; 2.80 A; A=1-589. DR PDB; 2IE4; X-ray; 2.60 A; A=1-589. DR PDB; 2NPP; X-ray; 3.30 A; A/D=1-589. DR PDB; 2NYL; X-ray; 3.80 A; A/D=8-589. DR PDB; 2NYM; X-ray; 3.60 A; A/D=8-589. DR PDB; 2PKG; X-ray; 3.30 A; A/B=10-589. DR PDB; 3C5W; X-ray; 2.80 A; A=9-589. DR PDB; 3DW8; X-ray; 2.85 A; A/D=9-589. DR PDB; 3K7V; X-ray; 2.85 A; A=1-589. DR PDB; 3K7W; X-ray; 2.96 A; A=1-589. DR PDB; 4I5L; X-ray; 2.43 A; A/D=6-589. DR PDB; 4I5N; X-ray; 2.80 A; A/D=6-589. DR PDB; 4LAC; X-ray; 2.82 A; A=404-589. DR PDBsum; 1B3U; -. DR PDBsum; 2IE3; -. DR PDBsum; 2IE4; -. DR PDBsum; 2NPP; -. DR PDBsum; 2NYL; -. DR PDBsum; 2NYM; -. DR PDBsum; 2PKG; -. DR PDBsum; 3C5W; -. DR PDBsum; 3DW8; -. DR PDBsum; 3K7V; -. DR PDBsum; 3K7W; -. DR PDBsum; 4I5L; -. DR PDBsum; 4I5N; -. DR PDBsum; 4LAC; -. DR ProteinModelPortal; P30153; -. DR SMR; P30153; 2-589. DR BioGrid; 111510; 143. DR DIP; DIP-29394N; -. DR IntAct; P30153; 116. DR MINT; MINT-1141071; -. DR STRING; 9606.ENSP00000324804; -. DR PhosphoSite; P30153; -. DR DMDM; 143811355; -. DR OGP; P30153; -. DR REPRODUCTION-2DPAGE; IPI00554737; -. DR MaxQB; P30153; -. DR PaxDb; P30153; -. DR PRIDE; P30153; -. DR DNASU; 5518; -. DR Ensembl; ENST00000322088; ENSP00000324804; ENSG00000105568. DR GeneID; 5518; -. DR KEGG; hsa:5518; -. DR UCSC; uc002pyp.3; human. DR CTD; 5518; -. DR GeneCards; GC19P052693; -. DR HGNC; HGNC:9302; PPP2R1A. DR HPA; CAB018599; -. DR MIM; 605983; gene. DR neXtProt; NX_P30153; -. DR PharmGKB; PA33666; -. DR eggNOG; NOG247268; -. DR HOGENOM; HOG000078539; -. DR HOVERGEN; HBG000011; -. DR InParanoid; P30153; -. DR KO; K03456; -. DR OMA; RNLCQDD; -. DR OrthoDB; EOG764722; -. DR PhylomeDB; P30153; -. DR TreeFam; TF105552; -. DR BioCyc; MetaCyc:ENSG00000105568-MONOMER; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_21257; Metabolism of RNA. DR Reactome; REACT_21300; Mitotic M-M/G1 phases. DR Reactome; REACT_604; Hemostasis. DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines. DR Reactome; REACT_6900; Immune System. DR Reactome; REACT_71; Gene Expression. DR SignaLink; P30153; -. DR EvolutionaryTrace; P30153; -. DR GeneWiki; PPP2R1A; -. DR GenomeRNAi; 5518; -. DR NextBio; 21342; -. DR PMAP-CutDB; P30153; -. DR PRO; PR:P30153; -. DR ArrayExpress; P30153; -. DR Bgee; P30153; -. DR CleanEx; HS_PPP2R1A; -. DR Genevestigator; P30153; -. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; NAS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; NAS:UniProtKB. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB. DR GO; GO:0003823; F:antigen binding; IPI:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB. DR GO; GO:0008601; F:protein phosphatase type 2A regulator activity; TAS:UniProtKB. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; TAS:UniProtKB. DR GO; GO:0006672; P:ceramide metabolic process; NAS:UniProtKB. DR GO; GO:0007059; P:chromosome segregation; IDA:UniProtKB. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0000188; P:inactivation of MAPK activity; NAS:UniProtKB. DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome. DR GO; GO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome. DR GO; GO:0016071; P:mRNA metabolic process; TAS:Reactome. DR GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB. DR GO; GO:0042518; P:negative regulation of tyrosine phosphorylation of Stat3 protein; NAS:UniProtKB. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome. DR GO; GO:0070262; P:peptidyl-serine dephosphorylation; IEA:Ensembl. DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl. DR GO; GO:0006461; P:protein complex assembly; TAS:UniProtKB. DR GO; GO:0006470; P:protein dephosphorylation; TAS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; NAS:UniProtKB. DR GO; GO:0045595; P:regulation of cell differentiation; NAS:UniProtKB. DR GO; GO:0006275; P:regulation of DNA replication; NAS:UniProtKB. DR GO; GO:0040008; P:regulation of growth; NAS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB. DR GO; GO:0030111; P:regulation of Wnt signaling pathway; NAS:UniProtKB. DR GO; GO:0010033; P:response to organic substance; NAS:UniProtKB. DR GO; GO:0016070; P:RNA metabolic process; TAS:Reactome. DR GO; GO:0008380; P:RNA splicing; NAS:UniProtKB. DR GO; GO:0019932; P:second-messenger-mediated signaling; NAS:UniProtKB. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000357; HEAT. DR InterPro; IPR021133; HEAT_type_2. DR Pfam; PF02985; HEAT; 2. DR SUPFAM; SSF48371; SSF48371; 1. DR PROSITE; PS50077; HEAT_REPEAT; 11. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Centromere; Chromosome; KW Chromosome partition; Complete proteome; Cytoplasm; KW Direct protein sequencing; Reference proteome; Repeat. FT INIT_MET 1 1 Removed. FT CHAIN 2 589 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A alpha FT isoform. FT /FTId=PRO_0000071400. FT REPEAT 8 46 HEAT 1. FT REPEAT 47 84 HEAT 2. FT REPEAT 85 123 HEAT 3. FT REPEAT 124 161 HEAT 4. FT REPEAT 162 200 HEAT 5. FT REPEAT 201 239 HEAT 6. FT REPEAT 240 278 HEAT 7. FT REPEAT 279 321 HEAT 8. FT REPEAT 322 360 HEAT 9. FT REPEAT 361 399 HEAT 10. FT REPEAT 400 438 HEAT 11. FT REPEAT 439 477 HEAT 12. FT REPEAT 478 516 HEAT 13. FT REPEAT 517 555 HEAT 14. FT REPEAT 556 589 HEAT 15. FT REGION 8 399 PP2A subunit B binding. FT REGION 47 321 Polyoma small and medium T antigens FT Binding. FT REGION 85 239 SV40 small T antigen binding. FT REGION 400 589 PP2A subunit C binding. FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 280 280 N6-acetyllysine. FT CONFLICT 130 130 P -> A (in Ref. 1; AAA35531). FT CONFLICT 258 258 R -> A (in Ref. 2; AAA36399). FT CONFLICT 272 272 K -> R (in Ref. 6; AA sequence). FT CONFLICT 551 551 L -> P (in Ref. 3; CAG29336). FT TURN 6 8 FT HELIX 11 19 FT HELIX 25 33 FT HELIX 35 41 FT HELIX 44 49 FT HELIX 51 57 FT HELIX 63 73 FT HELIX 78 80 FT HELIX 83 89 FT HELIX 90 96 FT STRAND 99 101 FT HELIX 102 116 FT HELIX 121 126 FT HELIX 128 136 FT STRAND 138 140 FT HELIX 141 147 FT HELIX 148 150 FT HELIX 151 154 FT TURN 155 157 FT HELIX 160 174 FT HELIX 179 194 FT HELIX 198 203 FT HELIX 205 213 FT HELIX 218 221 FT HELIX 224 234 FT HELIX 237 239 FT HELIX 240 243 FT HELIX 245 252 FT HELIX 257 265 FT HELIX 267 274 FT HELIX 276 281 FT HELIX 283 291 FT HELIX 296 311 FT TURN 315 317 FT HELIX 318 324 FT HELIX 326 334 FT HELIX 339 346 FT HELIX 349 352 FT HELIX 353 356 FT HELIX 358 364 FT HELIX 366 373 FT HELIX 378 385 FT HELIX 389 394 FT HELIX 397 412 FT HELIX 417 434 FT HELIX 436 438 FT HELIX 441 449 FT HELIX 450 452 FT HELIX 456 473 FT HELIX 475 481 FT HELIX 483 488 FT TURN 489 491 FT HELIX 495 520 FT HELIX 522 527 FT HELIX 528 530 FT HELIX 534 547 FT HELIX 548 550 FT HELIX 553 567 FT HELIX 573 585 SQ SEQUENCE 589 AA; 65309 MW; 5174EBE94D537836 CRC64; MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA AASHKVKEFC ENLSADCREN VIMSQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA // ID 2AAB_HUMAN Reviewed; 601 AA. AC P30154; A8MY67; B0YJ69; B4DGQ6; B4DK91; B4DWW5; F8W8G1; O75620; AC Q8NHV8; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 09-JUL-2014, entry version 140. DE RecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform; DE AltName: Full=PP2A subunit A isoform PR65-beta; DE AltName: Full=PP2A subunit A isoform R1-beta; GN Name=PPP2R1B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9795170; DOI=10.1016/S0378-1119(98)00350-3; RA Baysal B.E., Farr J.E., Goss J.R., Devlin B., Richard C.W. III; RT "Genomic organization and precise physical location of protein RT phosphatase 2A regulatory subunit A beta isoform gene on chromosome RT band 11q23."; RL Gene 217:107-116(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-8; SER-65; RP ASP-90; PRO-101; GLU-343; ALA-448; GLY-504 AND ALA-545. RX PubMed=9765152; DOI=10.1126/science.282.5387.284; RA Wang S.S., Esplin E.D., Li J.L., Huang L., Gazdar A., Minna J., RA Evans G.A.; RT "Alterations of the PPP2R1B gene in human lung and colon cancer."; RL Science 282:284-287(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11313745; DOI=10.1038/sj/ejhg/5200585; RA Baysal B.E., Willett-Brozick J.E., Taschner P.E.M., Dauwerse J.G., RA Devilee P., Devlin B.; RT "A high-resolution integrated map spanning the SDHD gene at 11q23: a RT 1.1-Mb BAC contig, a partial transcript map and 15 new repeat RT polymorphisms in a tumour-suppressor region."; RL Eur. J. Hum. Genet. 9:121-129(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5). RC TISSUE=Brain, Testis, and Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-601 (ISOFORM 1). RX PubMed=2159327; DOI=10.1021/bi00465a002; RA Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., RA Merlevede W., Hofsteenge J., Stone S.R.; RT "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A RT have a similar 39 amino acid repeating structure."; RL Biochemistry 29:3166-3173(1990). RN [10] RP INTERACTION WITH RAF1. RX PubMed=10801873; DOI=10.1074/jbc.M003259200; RA Abraham D., Podar K., Pacher M., Kubicek M., Welzel N., Hemmings B.A., RA Dilworth S.M., Mischak H., Kolch W., Baccarini M.; RT "Raf-1-associated protein phosphatase 2A as a positive regulator of RT kinase activation."; RL J. Biol. Chem. 275:22300-22304(2000). RN [11] RP INTERACTION WITH IPO9. RX PubMed=12670497; DOI=10.1016/S0006-291X(03)00434-0; RA Lubert E.J., Sarge K.D.; RT "Interaction between protein phosphatase 2A and members of the RT importin beta superfamily."; RL Biochem. Biophys. Res. Commun. 303:908-913(2003). RN [12] RP INTERACTION WITH SGOL1. RX PubMed=16541025; DOI=10.1038/nature04663; RA Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., RA Kawashima S.A., Watanabe Y.; RT "Shugoshin collaborates with protein phosphatase 2A to protect RT cohesin."; RL Nature 441:46-52(2006). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP VARIANT ASP-90. RX PubMed=10597236; DOI=10.1038/sj.onc.1203070; RA Campbell I.G., Manolitsas T.; RT "Absence of PPP2R1B gene alterations in primary ovarian cancers."; RL Oncogene 18:6367-6369(1999). RN [16] RP VARIANTS ALA-15; PRO-365; GLU-498; ILE-499 AND GLY-500. RX PubMed=10896920; DOI=10.1136/gut.47.2.268; RA Takagi Y., Futamura M., Yamaguchi K., Aoki S., Takahashi T., Saji S.; RT "Alterations of the PPP2R1B gene located at 11q23 in human colorectal RT cancers."; RL Gut 47:268-271(2000). RN [17] RP VARIANT ASP-90. RX PubMed=11996789; DOI=10.1016/S0165-4608(01)00597-0; RA Hemmer S., Wasenius V.M., Haglund C., Zhu Y., Knuutila S., RA Franssila K., Joensuu H.; RT "Alterations in the suppressor gene PPP2R1B in parathyroid RT hyperplasias and adenomas."; RL Cancer Genet. Cytogenet. 134:13-17(2002). CC -!- FUNCTION: The PR65 subunit of protein phosphatase 2A serves as a CC scaffolding molecule to coordinate the assembly of the catalytic CC subunit and a variable regulatory B subunit. CC -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, CC composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa CC constant regulatory subunit (PR65 or subunit A), that associates CC with a variety of regulatory subunits. Proteins that associate CC with the core dimer include three families of regulatory subunits CC B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 CC families), the 48 kDa variable regulatory subunit, viral proteins, CC and cell signaling molecules. Interacts with IPO9. Interacts with CC SGOL1. Interacts with RAF1. CC -!- INTERACTION: CC O08785:Clock (xeno); NbExp=2; IntAct=EBI-357094, EBI-79859; CC P67775:PPP2CA; NbExp=7; IntAct=EBI-357094, EBI-712311; CC P63151:PPP2R2A; NbExp=2; IntAct=EBI-357094, EBI-1048931; CC Q15172:PPP2R5A; NbExp=2; IntAct=EBI-357094, EBI-641666; CC Q13362:PPP2R5C; NbExp=2; IntAct=EBI-357094, EBI-1266156; CC Q14738:PPP2R5D; NbExp=2; IntAct=EBI-357094, EBI-396563; CC Q16537:PPP2R5E; NbExp=3; IntAct=EBI-357094, EBI-968374; CC P11233:RALA; NbExp=6; IntAct=EBI-357094, EBI-1036803; CC O08722:Unc5b (xeno); NbExp=4; IntAct=EBI-357094, EBI-4404185; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P30154-1; Sequence=Displayed; CC Name=2; CC IsoId=P30154-2; Sequence=VSP_036460; CC Name=3; CC IsoId=P30154-3; Sequence=VSP_043379, VSP_036460; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=P30154-4; Sequence=VSP_045275; CC Note=No experimental confirmation available; CC Name=5; CC IsoId=P30154-5; Sequence=VSP_046684; CC -!- DOMAIN: Each HEAT repeat appears to consist of two alpha helices CC joined by a hydrophilic region, the intrarepeat loop. The repeat CC units may be arranged laterally to form a rod-like structure. CC -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A CC family. CC -!- SIMILARITY: Contains 15 HEAT repeats. CC -!- SEQUENCE CAUTION: CC Sequence=AAA59983.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part; CC Sequence=BAG59103.1; Type=Frameshift; Positions=540; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF083439; AAC63525.1; -; Genomic_DNA. DR EMBL; AF083425; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083426; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083427; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083428; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083429; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083430; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083431; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083432; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083433; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083434; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083435; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083436; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083437; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF083438; AAC63525.1; JOINED; Genomic_DNA. DR EMBL; AF087438; AAC69624.1; -; mRNA. DR EMBL; AF163473; AAG39644.1; -; mRNA. DR EMBL; AK294716; BAG57867.1; -; mRNA. DR EMBL; AK296455; BAG59103.1; ALT_FRAME; mRNA. DR EMBL; AK301705; BAG63177.1; -; mRNA. DR EMBL; EF445011; ACA06046.1; -; Genomic_DNA. DR EMBL; EF445011; ACA06047.1; -; Genomic_DNA. DR EMBL; AP000925; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001781; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471065; EAW67150.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67151.1; -; Genomic_DNA. DR EMBL; BC027596; AAH27596.1; -; mRNA. DR EMBL; M65254; AAA59983.1; ALT_SEQ; mRNA. DR CCDS; CCDS53706.1; -. [P30154-3] DR CCDS; CCDS53707.1; -. [P30154-5] DR CCDS; CCDS53708.1; -. [P30154-4] DR CCDS; CCDS8348.1; -. [P30154-2] DR CCDS; CCDS8349.1; -. [P30154-1] DR PIR; B34541; B34541. DR RefSeq; NP_001171033.1; NM_001177562.1. [P30154-4] DR RefSeq; NP_001171034.1; NM_001177563.1. [P30154-5] DR RefSeq; NP_002707.3; NM_002716.4. [P30154-1] DR RefSeq; NP_859050.1; NM_181699.2. [P30154-2] DR RefSeq; NP_859051.1; NM_181700.1. [P30154-3] DR UniGene; Hs.269128; -. DR UniGene; Hs.584790; -. DR ProteinModelPortal; P30154; -. DR SMR; P30154; 19-601. DR BioGrid; 111511; 56. DR IntAct; P30154; 64. DR MINT; MINT-1150161; -. DR STRING; 9606.ENSP00000311344; -. DR PhosphoSite; P30154; -. DR DMDM; 116241236; -. DR MaxQB; P30154; -. DR PaxDb; P30154; -. DR PRIDE; P30154; -. DR DNASU; 5519; -. DR Ensembl; ENST00000311129; ENSP00000311344; ENSG00000137713. [P30154-2] DR Ensembl; ENST00000341980; ENSP00000343317; ENSG00000137713. [P30154-4] DR Ensembl; ENST00000393055; ENSP00000376775; ENSG00000137713. [P30154-5] DR Ensembl; ENST00000426998; ENSP00000410671; ENSG00000137713. [P30154-3] DR Ensembl; ENST00000527614; ENSP00000437193; ENSG00000137713. [P30154-1] DR Ensembl; ENST00000571902; ENSP00000459644; ENSG00000262764. [P30154-3] DR Ensembl; ENST00000571959; ENSP00000459838; ENSG00000262764. [P30154-2] DR Ensembl; ENST00000573946; ENSP00000459456; ENSG00000262764. [P30154-5] DR Ensembl; ENST00000575443; ENSP00000459827; ENSG00000262764. [P30154-4] DR Ensembl; ENST00000576276; ENSP00000461254; ENSG00000262764. [P30154-1] DR GeneID; 5519; -. DR KEGG; hsa:5519; -. DR UCSC; uc001plw.1; human. [P30154-2] DR UCSC; uc001plx.1; human. [P30154-1] DR UCSC; uc010rwi.1; human. [P30154-3] DR CTD; 5519; -. DR GeneCards; GC11M111642; -. DR HGNC; HGNC:9303; PPP2R1B. DR HPA; CAB004034; -. DR HPA; HPA018908; -. DR MIM; 603113; gene. DR neXtProt; NX_P30154; -. DR PharmGKB; PA33667; -. DR eggNOG; NOG247268; -. DR HOGENOM; HOG000078539; -. DR HOVERGEN; HBG000011; -. DR KO; K03456; -. DR OMA; NREQIIM; -. DR OrthoDB; EOG764722; -. DR PhylomeDB; P30154; -. DR TreeFam; TF105552; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_21300; Mitotic M-M/G1 phases. DR Reactome; REACT_604; Hemostasis. DR Reactome; REACT_6782; TRAF6 Mediated Induction of proinflammatory cytokines. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; PPP2R1B; human. DR GeneWiki; PPP2R1B; -. DR GenomeRNAi; 5519; -. DR NextBio; 21346; -. DR PRO; PR:P30154; -. DR ArrayExpress; P30154; -. DR Bgee; P30154; -. DR CleanEx; HS_PPP2R1B; -. DR Genevestigator; P30154; -. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; IMP:UniProtKB. DR GO; GO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IMP:UniProtKB. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000357; HEAT. DR InterPro; IPR021133; HEAT_type_2. DR Pfam; PF02985; HEAT; 2. DR SUPFAM; SSF48371; SSF48371; 1. DR PROSITE; PS50077; HEAT_REPEAT; 12. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Polymorphism; KW Reference proteome; Repeat. FT INIT_MET 1 1 Removed. FT CHAIN 2 601 Serine/threonine-protein phosphatase 2A FT 65 kDa regulatory subunit A beta isoform. FT /FTId=PRO_0000071403. FT REPEAT 20 58 HEAT 1. FT REPEAT 59 96 HEAT 2. FT REPEAT 97 135 HEAT 3. FT REPEAT 136 173 HEAT 4. FT REPEAT 174 212 HEAT 5. FT REPEAT 213 251 HEAT 6. FT REPEAT 252 290 HEAT 7. FT REPEAT 291 333 HEAT 8. FT REPEAT 334 372 HEAT 9. FT REPEAT 373 411 HEAT 10. FT REPEAT 412 450 HEAT 11. FT REPEAT 451 489 HEAT 12. FT REPEAT 490 528 HEAT 13. FT REPEAT 529 567 HEAT 14. FT REPEAT 568 601 HEAT 15. FT MOD_RES 2 2 N-acetylalanine. FT VAR_SEQ 39 102 Missing (in isoform 3). FT /FTId=VSP_043379. FT VAR_SEQ 103 229 Missing (in isoform 5). FT /FTId=VSP_046684. FT VAR_SEQ 344 388 Missing (in isoform 4). FT /FTId=VSP_045275. FT VAR_SEQ 598 601 LALA -> VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTV FT PGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD (in FT isoform 2 and isoform 3). FT /FTId=VSP_036460. FT VARIANT 8 8 G -> R (in a lung cancer patient; FT dbSNP:rs142771326). FT /FTId=VAR_022895. FT VARIANT 15 15 G -> A (in a colorectal cancer patient). FT /FTId=VAR_022896. FT VARIANT 65 65 P -> S (in a lung cancer patient). FT /FTId=VAR_022897. FT VARIANT 90 90 G -> D (in a lung cancer patient; FT dbSNP:rs1805076). FT /FTId=VAR_006384. FT VARIANT 101 101 L -> P (in a colon adenocarcinoma). FT /FTId=VAR_022898. FT VARIANT 343 343 K -> E (in a lung cancer patient). FT /FTId=VAR_022899. FT VARIANT 365 365 S -> P (in a colorectal cancer patient). FT /FTId=VAR_022900. FT VARIANT 448 448 V -> A (in a colon adenocarcinoma). FT /FTId=VAR_022901. FT VARIANT 498 498 V -> E (in a colorectal cancer patient). FT /FTId=VAR_022902. FT VARIANT 499 499 L -> I (in a colorectal cancer patient). FT /FTId=VAR_022903. FT VARIANT 500 500 V -> G (in a colorectal cancer patient). FT /FTId=VAR_022904. FT VARIANT 504 504 D -> G (in a lung cancer patient). FT /FTId=VAR_022905. FT VARIANT 545 545 V -> A (in a colon adenocarcinoma). FT /FTId=VAR_022906. FT CONFLICT 74 74 E -> V (in Ref. 9; AAA59983). FT CONFLICT 178 178 I -> T (in Ref. 1; AAC63525, 3; AAG39644 FT and 9; AAA59983). FT CONFLICT 211 211 D -> G (in Ref. 4; BAG57867). FT CONFLICT 411 411 Q -> R (in Ref. 9; AAA59983). FT CONFLICT 503 503 N -> S (in Ref. 4; BAG57867). SQ SEQUENCE 601 AA; 66214 MW; 86AB20D7505210B0 CRC64; MAGASELGTG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI ALALGVERTR SELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC LLPPLENLAT VEETVVRDKA VESLRQISQE HTPVALEAYF VPLVKRLASG DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ QFRSLCSDDT PMVRRAAASK LGEFAKVLEL DSVKSEIVPL FTSLASDEQD SVRLLAVEAC VSIAQLLSQD DLETLVMPTL RQAAEDKSWR VRYMVADRFS ELQKAMGPKI TLNDLIPAFQ NLLKDCEAEV RAAAAHKVKE LGENLPIEDR ETIIMNQILP YIKELVSDTN QHVKSALASV IMGLSTILGK ENTIEHLLPL FLAQLKDECP DVRLNIISNL DCVNEVIGIR QLSQSLLPAI VELAEDAKWR VRLAIIEYMP LLAGQLGVEF FDEKLNSLCM AWLVDHVYAI REAATNNLMK LVQKFGTEWA QNTIVPKVLV MANDPNYLHR MTTLFCINAL SEACGQEITT KQMLPIVLKM AGDQVANVRF NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL A // ID 2B11_HUMAN Reviewed; 266 AA. AC P04229; A4F5N0; A8K098; O62869; P13758; Q06662; Q30116; Q30117; AC Q5Y7E9; Q7M2H4; Q95461; Q9BCL7; Q9GIK5; Q9MXZ0; Q9MXZ5; Q9TQ91; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 2. DT 09-JUL-2014, entry version 143. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-1 beta chain; DE AltName: Full=MHC class II antigen DRB1*1; DE Short=DR-1; DE Short=DR1; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01). RX PubMed=2998758; RA Tonnelle C., Demars R., Long E.O.; RT "DO beta: a new beta chain gene in HLA-D with a distinct regulation of RT expression."; RL EMBO J. 4:2839-2847(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01). RX PubMed=3858829; DOI=10.1073/pnas.82.10.3405; RA Bell J.I., Estess P., St John T., Saiki R., Watling D.L., Erlich H.A., RA McDevitt H.O.; RT "DNA sequence and characterization of human class II major RT histocompatibility complex beta chains from the DR1 haplotype."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3405-3409(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:03). RX PubMed=1688595; RA Coppin H.L., Avoustin P., Fabron J., Huchenq A., Garnier J.-M., RA Thomsen M., De Preval C.; RT "Evolution of the HLA-DR1 gene family. Structural and functional RT analysis of the new allele 'DR-BON'."; RL J. Immunol. 144:984-989(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*01:01), AND VARIANT RP ARG-262. RX PubMed=17345114; DOI=10.1007/s00251-007-0196-8; RA von Salome J., Gyllensten U., Bergstroem T.F.; RT "Full-length sequence analysis of the HLA-DRB1 locus suggests a recent RT origin of alleles."; RL Immunogenetics 59:261-271(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. RC TISSUE=B-cell; RX PubMed=8462990; DOI=10.1007/BF00216386; RA Louis P., Eliaou J.F., Kerlan-Candon S., Pinet V., Vincent R., RA Clot J.; RT "Polymorphism in the regulatory region of HLA-DRB genes correlating RT with haplotype evolution."; RL Immunogenetics 38:21-26(1993). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*01:04). RA Middleton D., Versluis L.F., Tilanus M.G.J.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 30-64. RC TISSUE=B-cell; RX PubMed=6600932; DOI=10.1021/bi00270a027; RA Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J., RA Reisfeld R.A.; RT "N-terminal amino acid sequences of the alpha and beta chains of HLA- RT DR1 and HLA-DR2 antigens."; RL Biochemistry 22:185-188(1983). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:06). RX PubMed=10203026; DOI=10.1034/j.1399-0039.1999.530313.x; RA Palou E., Mongay L., Arias M.T., Isart F., Suarez B., Masso M., RA Fabregat V., Martorell J., Gaya A.; RT "Identification of a novel DRB1-allele (DRB1*0106) by sequence-based RT typing."; RL Tissue Antigens 53:308-310(1999). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07). RX PubMed=12753659; DOI=10.1034/j.1399-0039.2003.00034.x; RA Voorter C.E.M., Hepkema B.G., Lems S.P.M., van den Berg-Loonen E.M.; RT "Identification of three new DRB1 alleles, DRB1*0107, *0425 and *13012 RT and confirmation of DRB4*01033."; RL Tissue Antigens 61:398-402(2003). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:05). RA Kashiwase K., Akaza T., Juji T.; RT "HLA-DRB1 new alleles."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07). RA Dormoy A., Froelich N., Leisenbach R., Tongio M.M.; RT "A new HLA-DRB1*01 allele."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB1*01:02). RC TISSUE=Blood; RA Hashemi S., Couture C., Cole R., Buyse I.; RT "Identification and sequencing of a novel DRB1*01 allele."; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-266 (ALLELE DRB1*01:02). RX PubMed=2453563; RA Hurley C.K., Ziff B.L., Silver J., Gregersen P.K., Hartzman R., RA Johnson A.H.; RT "Polymorphism of the HLA-DR1 haplotype in American blacks. RT Identification of a DR1 beta-chain determinant recognized in the mixed RT lymphocyte reaction."; RL J. Immunol. 140:4019-4023(1988). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115 (ALLELES DRB1*01:01 AND RP DRB1*01:02). RC TISSUE=Blood; RA Arnaiz-Villena A.; RT "HLA class II polymorphism."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [17] RP DISEASE. RX PubMed=14508706; DOI=10.1086/378097; RA Rossman M.D., Thompson B., Frederick M., Maliarik M., Iannuzzi M.C., RA Rybicki B.A., Pandey J.P., Newman L.S., Magira E., Beznik-Cizman B., RA Monos D.; RT "HLA-DRB1*1101: a significant risk factor for sarcoidosis in blacks RT and whites."; RL Am. J. Hum. Genet. 73:720-735(2003). RN [18] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [19] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [20] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [21] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [23] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [24] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [25] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219. RX PubMed=8316295; DOI=10.1038/364033a0; RA Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G., RA Strominger J.L., Wiley D.C.; RT "Three-dimensional structure of the human class II histocompatibility RT antigen HLA-DR1."; RL Nature 364:33-39(1993). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219. RX PubMed=8145819; DOI=10.1038/368215a0; RA Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G., RA Strominger J.L., Wiley D.C.; RT "Crystal structure of the human class II MHC protein HLA-DR1 complexed RT with an influenza virus peptide."; RL Nature 368:215-221(1994). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH SEB. RX PubMed=8152483; DOI=10.1038/368711a0; RA Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., RA Chi Y.I., Stauffacher C., Strominger J.L., Wiley D.C.; RT "Three-dimensional structure of a human class II histocompatibility RT molecule complexed with superantigen."; RL Nature 368:711-718(1994). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II (Probable). CC -!- POLYMORPHISM: The following alleles of DRB1-1 are known: CC DRB1*01:01; DRB1*01:02; DRB1*01:03; DRB1*01:04; DRB1*01:05; CC DRB1*01:06; DRB1*01:07; DRB1*01:08; DRB1*01:09; DRB1*01:10; CC DRB1*01:11; DRB1*01:12; DRB1*01:13; DRB1*01:14; DRB1*01:15; CC DRB1*01:16; DRB1*01:17; DRB1*01:18; DRB1*01:19; DRB1*01:20 and CC DRB1*01:21. The sequence shown is that of DRB1*01:01. CC -!- DISEASE: Sarcoidosis 1 (SS1) [MIM:181000]: An idiopathic, CC systemic, inflammatory disease characterized by the formation of CC immune granulomas in involved organs. Granulomas predominantly CC invade the lungs and the lymphatic system, but also skin, liver, CC spleen, eyes and other organs may be involved. Note=Disease CC susceptibility is associated with variations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X03069; CAA26873.1; -; mRNA. DR EMBL; M11161; AAA59781.1; -; mRNA. DR EMBL; M33600; AAA59782.1; -; mRNA. DR EMBL; AY663400; AAU87993.1; -; Genomic_DNA. DR EMBL; AM419948; CAL99240.1; -; Genomic_DNA. DR EMBL; AK289463; BAF82152.1; -; mRNA. DR EMBL; X64547; CAA45845.1; -; Genomic_DNA. DR EMBL; X99896; CAA68171.1; -; mRNA. DR EMBL; AF089723; AAD51131.1; -; Genomic_DNA. DR EMBL; AJ276206; CAC27123.1; -; Genomic_DNA. DR EMBL; AB015184; BAA28761.1; -; Genomic_DNA. DR EMBL; AJ303118; CAC19693.1; -; Genomic_DNA. DR EMBL; Z50871; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M21008; AAA59780.1; -; mRNA. DR EMBL; AF029288; AAF65497.1; -; Genomic_DNA. DR EMBL; AF029293; AAF65502.1; -; Genomic_DNA. DR PIR; A19197; A19197. DR PIR; D24669; HLHU1B. DR PIR; I56072; I56072. DR PIR; PH0147; PH0147. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR PDB; 1AQD; X-ray; 2.45 A; B/E/H/K=30-227. DR PDB; 1DLH; X-ray; 2.80 A; B/E=32-219. DR PDB; 1FYT; X-ray; 2.60 A; B=30-221. DR PDB; 1HXY; X-ray; 2.60 A; B=30-219. DR PDB; 1JWM; X-ray; 2.70 A; B=30-219. DR PDB; 1JWS; X-ray; 2.60 A; B=30-219. DR PDB; 1JWU; X-ray; 2.30 A; B=30-219. DR PDB; 1KG0; X-ray; 2.65 A; B=32-219. DR PDB; 1KLG; X-ray; 2.40 A; B=30-219. DR PDB; 1KLU; X-ray; 1.93 A; B=30-219. DR PDB; 1LO5; X-ray; 3.20 A; B=30-219. DR PDB; 1PYW; X-ray; 2.10 A; B=30-219. DR PDB; 1R5I; X-ray; 2.60 A; B/F=30-219. DR PDB; 1SEB; X-ray; 2.70 A; B/F=30-221. DR PDB; 1SJE; X-ray; 2.45 A; B=30-219. DR PDB; 1SJH; X-ray; 2.25 A; B=30-219. DR PDB; 1T5W; X-ray; 2.40 A; B/E=30-219. DR PDB; 1T5X; X-ray; 2.50 A; B=30-219. DR PDB; 2FSE; X-ray; 3.10 A; B/D=33-219. DR PDB; 2G9H; X-ray; 2.00 A; B=30-219. DR PDB; 2IAM; X-ray; 2.80 A; B=30-219. DR PDB; 2IAN; X-ray; 2.80 A; B/G/L/Q=30-219. DR PDB; 2ICW; X-ray; 2.41 A; B/E=30-219. DR PDB; 2IPK; X-ray; 2.30 A; B=30-219. DR PDB; 2OJE; X-ray; 3.00 A; B/F=30-219. DR PDB; 2XN9; X-ray; 2.30 A; E=30-219. DR PDB; 3L6F; X-ray; 2.10 A; B=30-221. DR PDB; 3PDO; X-ray; 1.95 A; B=30-227. DR PDB; 3PGC; X-ray; 2.66 A; B/E=30-227. DR PDB; 3PGD; X-ray; 2.72 A; B/E=30-227. DR PDB; 3QXA; X-ray; 2.71 A; B/E=30-219. DR PDB; 3QXD; X-ray; 2.30 A; B/E=30-219. DR PDB; 3S4S; X-ray; 2.40 A; B/E=30-221. DR PDB; 3S5L; X-ray; 2.10 A; B/E=30-221. DR PDB; 4AEN; X-ray; 2.20 A; B=30-227. DR PDB; 4AH2; X-ray; 2.36 A; B=30-227. DR PDB; 4E41; X-ray; 2.60 A; B/G=30-219. DR PDB; 4FQX; X-ray; 2.60 A; B=30-221. DR PDB; 4GBX; X-ray; 3.00 A; B=30-220. DR PDB; 4I5B; X-ray; 2.12 A; B/E=31-222. DR PDBsum; 1AQD; -. DR PDBsum; 1DLH; -. DR PDBsum; 1FYT; -. DR PDBsum; 1HXY; -. DR PDBsum; 1JWM; -. DR PDBsum; 1JWS; -. DR PDBsum; 1JWU; -. DR PDBsum; 1KG0; -. DR PDBsum; 1KLG; -. DR PDBsum; 1KLU; -. DR PDBsum; 1LO5; -. DR PDBsum; 1PYW; -. DR PDBsum; 1R5I; -. DR PDBsum; 1SEB; -. DR PDBsum; 1SJE; -. DR PDBsum; 1SJH; -. DR PDBsum; 1T5W; -. DR PDBsum; 1T5X; -. DR PDBsum; 2FSE; -. DR PDBsum; 2G9H; -. DR PDBsum; 2IAM; -. DR PDBsum; 2IAN; -. DR PDBsum; 2ICW; -. DR PDBsum; 2IPK; -. DR PDBsum; 2OJE; -. DR PDBsum; 2XN9; -. DR PDBsum; 3L6F; -. DR PDBsum; 3PDO; -. DR PDBsum; 3PGC; -. DR PDBsum; 3PGD; -. DR PDBsum; 3QXA; -. DR PDBsum; 3QXD; -. DR PDBsum; 3S4S; -. DR PDBsum; 3S5L; -. DR PDBsum; 4AEN; -. DR PDBsum; 4AH2; -. DR PDBsum; 4E41; -. DR PDBsum; 4FQX; -. DR PDBsum; 4GBX; -. DR PDBsum; 4I5B; -. DR ProteinModelPortal; P04229; -. DR SMR; P04229; 30-219. DR DIP; DIP-6143N; -. DR IntAct; P04229; 6. DR MINT; MINT-203282; -. DR BindingDB; P04229; -. DR ChEMBL; CHEMBL1943; -. DR DrugBank; DB05259; Glatiramer Acetate. DR PhosphoSite; P04229; -. DR DMDM; 34395916; -. DR PaxDb; P04229; -. DR PRIDE; P04229; -. DR Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126. DR GeneCards; GC06M032546; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; CAB015400; -. DR HPA; CAB034021; -. DR MIM; 142857; gene. DR MIM; 181000; phenotype. DR neXtProt; NX_P04229; -. DR Orphanet; 703; Bullous pemphigoid. DR Orphanet; 555; Celiac disease. DR Orphanet; 243377; Diabetes mellitus type 1. DR Orphanet; 220393; Diffuse cutaneous systemic sclerosis. DR Orphanet; 545; Follicular lymphoma. DR Orphanet; 220402; Limited cutaneous systemic sclerosis. DR Orphanet; 220407; Limited systemic sclerosis. DR Orphanet; 802; Multiple sclerosis. DR Orphanet; 83465; Narcolepsy without cataplexy. DR Orphanet; 2073; Narcolepsy-cataplexy. DR Orphanet; 284130; Rheumatoid arthritis. DR Orphanet; 797; Sarcoidosis. DR Orphanet; 536; Systemic lupus erythematosus. DR eggNOG; NOG68200; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P04229; -. DR OrthoDB; EOG7PS1GV; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-DRB1; human. DR EvolutionaryTrace; P04229; -. DR PRO; PR:P04229; -. DR ArrayExpress; P04229; -. DR Bgee; P04229; -. DR CleanEx; HS_HLA-DRB1; -. DR Genevestigator; P04229; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProt. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISS:UniProtKB. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB. DR GO; GO:2001179; P:regulation of interleukin-10 secretion; ISS:UniProtKB. DR GO; GO:0032673; P:regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Endosome; Glycoprotein; Golgi apparatus; Immunity; Isopeptide bond; KW Lysosome; Membrane; MHC II; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-1 beta chain. FT /FTId=PRO_0000018949. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Helical; (Potential). FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 5 5 K -> R (in dbSNP:rs9270305). FT /FTId=VAR_056527. FT VARIANT 13 13 T -> A (in dbSNP:rs1059553). FT /FTId=VAR_033377. FT VARIANT 29 29 A -> S (in dbSNP:rs9270299). FT /FTId=VAR_033378. FT VARIANT 33 33 R -> K (in dbSNP:rs34716432). FT /FTId=VAR_033379. FT VARIANT 33 33 R -> Q (in dbSNP:rs34716432). FT /FTId=VAR_033380. FT VARIANT 39 39 Q -> E (in allele DRB1*01:07). FT /FTId=VAR_016740. FT VARIANT 66 66 S -> Y (in dbSNP:rs16822820). FT /FTId=VAR_033381. FT VARIANT 74 74 G -> R (in allele DRB1*01:05). FT /FTId=VAR_016741. FT VARIANT 76 76 Y -> F (in dbSNP:rs1060346). FT /FTId=VAR_033382. FT VARIANT 89 89 Y -> S (in dbSNP:rs36074728). FT /FTId=VAR_033383. FT VARIANT 96 96 L -> I (in allele DRB1*01:03). FT /FTId=VAR_016710. FT VARIANT 99 99 Q -> D (in allele DRB1*01:03; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016711. FT VARIANT 99 99 Q -> E (in dbSNP:rs17881965). FT /FTId=VAR_033384. FT VARIANT 99 99 Q -> H (in dbSNP:rs17879599). FT /FTId=VAR_033385. FT VARIANT 100 100 R -> A (in allele DRB1*01:06; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016742. FT VARIANT 100 100 R -> E (in allele DRB1*01:03; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016712. FT VARIANT 102 102 A -> G (in dbSNP:rs17878857). FT /FTId=VAR_033386. FT VARIANT 103 103 A -> E (in dbSNP:rs16822805). FT /FTId=VAR_033387. FT VARIANT 106 106 T -> N (in allele DRB1*01:04; FT dbSNP:rs16822752). FT /FTId=VAR_016713. FT VARIANT 107 107 Y -> H (in dbSNP:rs16822512). FT /FTId=VAR_033388. FT VARIANT 114 114 V -> A (in allele DRB1*01:02; FT dbSNP:rs17424145). FT /FTId=VAR_016714. FT VARIANT 115 115 G -> V (in allele DRB1*01:02, allele FT DRB1*01:04 and allele DRB1*01:06; FT dbSNP:rs2230810). FT /FTId=VAR_016715. FT VARIANT 164 164 G -> D (in dbSNP:rs1059633). FT /FTId=VAR_033389. FT VARIANT 169 169 A -> T (in dbSNP:rs2308768). FT /FTId=VAR_033390. FT VARIANT 171 171 V -> M (in dbSNP:rs701829). FT /FTId=VAR_033391. FT VARIANT 178 178 Q -> H (in dbSNP:rs701830). FT /FTId=VAR_033392. FT VARIANT 195 195 R -> Q (in dbSNP:rs3205588). FT /FTId=VAR_033393. FT VARIANT 210 210 T -> I (in dbSNP:rs17423930). FT /FTId=VAR_033394. FT VARIANT 236 236 V -> M (in dbSNP:rs2230816). FT /FTId=VAR_033395. FT VARIANT 253 253 Q -> E (in allele DRB1*01:02). FT /FTId=VAR_016716. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_056528. FT CONFLICT 25 25 P -> R (in Ref. 2; AAA59781). FT CONFLICT 36 36 F -> S (in Ref. 9; AA sequence). FT CONFLICT 58 59 RC -> LF (in Ref. 9; AA sequence). FT CONFLICT 80 80 T -> E (in Ref. 2; AAA59781). FT CONFLICT 100 103 RRAA -> KRGQ (in Ref. 2; AAA59781). FT CONFLICT 192 192 T -> I (in Ref. 2; AAA59781). FT STRAND 36 47 FT TURN 48 51 FT STRAND 52 63 FT STRAND 65 70 FT TURN 71 73 FT STRAND 75 80 FT HELIX 81 83 FT HELIX 84 91 FT HELIX 94 106 FT HELIX 108 115 FT HELIX 116 118 FT TURN 119 121 FT STRAND 127 132 FT STRAND 135 139 FT STRAND 142 154 FT STRAND 157 162 FT STRAND 165 167 FT STRAND 169 173 FT STRAND 180 182 FT STRAND 184 192 FT STRAND 199 205 FT STRAND 213 218 SQ SEQUENCE 266 AA; 29914 MW; CC9CC7E2D0DD036C CRC64; MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQL KFECHFFNGT ERVRLLERCI YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQR RAAVDTYCRH NYGVGESFTV QRRVEPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B13_HUMAN Reviewed; 266 AA. AC P01912; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 09-JUL-2014, entry version 130. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-3 chain; DE AltName: Full=Clone P2-beta-3; DE AltName: Full=MHC class II antigen DRB1*3; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*03:01). RX PubMed=6589154; RA Peterson P.A., Gustafsson K., Wiman K.G., Emmoth E., Larhammar D., RA Boehme J., Hyldig-Nielsen J.J., Ronne H., Rask L.; RT "Mutations and selection in the generation of class II RT histocompatibility antigen polymorphism."; RL EMBO J. 3:1655-1660(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*03:01). RX PubMed=6415003; DOI=10.1016/0198-8859(83)90087-3; RA Larhammar D., Andersson G., Andersson M., Bill P., Boehme J., RA Claesson L., Denaro M., Emmoth E., Gustafsson K., Hammarling U., RA Heldin E., Hyldig-Nielsen J.-J., Lind P., Schenning L., Servenius B., RA Widmark E., Rask L., Peterson P.A.; RT "Molecular analysis of human class II transplantation antigens and RT their genes."; RL Hum. Immunol. 8:95-103(1983). RN [3] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [4] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [5] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [6] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [7] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [8] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [9] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 34-220 OF HLA-DRA/HLA-DRB1 RP HETERODIMER IN COMPLEX WITH CD74 PEPTIDE (CLIP), SUBUNIT, AND RP DISULFIDE BONDS. RX PubMed=7477400; DOI=10.1038/378457a0; RA Ghosh P., Amaya M., Mellins E., Wiley D.C.; RT "The structure of an intermediate in class II MHC maturation: CLIP RT bound to HLA-DR3."; RL Nature 378:457-462(1995). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II (Probable). CC -!- POLYMORPHISM: The following alleles of DRB1-3 are known: CC DRB1*03:01; DRB1*03:02; DRB1*03:03; DRB1*03:04; DRB1*03:05; CC DRB1*03:06; DRB1*03:07; DRB1*03:08; DRB1*03:09; DRB1*03:10; CC DRB1*03:11; DRB1*03:12; DRB1*03:13; DRB1*03:14; DRB1*03:15; CC DRB1*03:16; DRB1*03:17; DRB1*03:18; DRB1*03:19; DRB1*03:20; CC DRB1*03:21; DRB1*03:22; DRB1*03:23; DRB1*03:24; DRB1*03:25; CC DRB1*03:26; DRB1*03:27; DRB1*03:28; DRB1*03:29; DRB1*03:30; CC DRB1*03:31; DRB1*03:32; DRB1*03:33; DRB1*03:34; DRB1*03:35; CC DRB1*03:36; DRB1*03:37; DRB1*03:38; DRB1*03:39; DRB1*03:40 and CC DRB1*03:41. The sequence shown is that of DRB1*03:01. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X00699; CAA25295.1; -; mRNA. DR PIR; I37546; HLHU3D. DR RefSeq; NP_001230894.1; NM_001243965.1. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR PDB; 1A6A; X-ray; 2.75 A; B=34-220. DR PDBsum; 1A6A; -. DR ProteinModelPortal; P01912; -. DR SMR; P01912; 34-220. DR BioGrid; 109368; 15. DR DIP; DIP-6064N; -. DR IntAct; P01912; 8. DR MINT; MINT-1505391; -. DR DMDM; 1708116; -. DR PRIDE; P01912; -. DR DNASU; 3123; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR GeneID; 3123; -. DR KEGG; hsa:3123; -. DR UCSC; uc011eri.2; human. DR CTD; 3123; -. DR GeneCards; GC06M032546; -. DR GeneCards; GC06Mj32477; -. DR GeneCards; GC06Mn32480; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR neXtProt; NX_P01912; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; NGMERVR; -. DR PhylomeDB; P01912; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-DRB1; human. DR EvolutionaryTrace; P01912; -. DR GenomeRNAi; 3123; -. DR NextBio; 12394; -. DR CleanEx; HS_HLA-DRB1; -. DR Genevestigator; P01912; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProt. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProt. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IDA:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; IDA:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProt. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-3 chain. FT /FTId=PRO_0000018965. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Helical; (Potential). FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 123 Beta-1. FT REGION 124 217 Beta-2. FT REGION 218 227 Connecting peptide. FT CARBOHYD 48 48 N-linked (GlcNAc...). FT DISULFID 44 108 FT DISULFID 146 202 FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 55 55 Y -> F (in dbSNP:rs16822516). FT /FTId=VAR_050371. FT VARIANT 106 106 N -> T (in dbSNP:rs9269941). FT /FTId=VAR_050372. FT VARIANT 164 164 G -> S (in dbSNP:rs1059633). FT /FTId=VAR_050373. FT VARIANT 169 169 T -> A (in dbSNP:rs2308768). FT /FTId=VAR_050374. FT VARIANT 236 236 V -> M (in dbSNP:rs2230816). FT /FTId=VAR_056545. FT STRAND 37 47 FT TURN 48 51 FT STRAND 52 61 FT STRAND 64 70 FT TURN 71 73 FT STRAND 75 80 FT HELIX 81 83 FT HELIX 84 92 FT HELIX 94 101 FT HELIX 103 106 FT HELIX 108 115 FT TURN 116 121 FT STRAND 127 134 FT STRAND 138 140 FT STRAND 143 150 FT STRAND 152 154 FT STRAND 157 162 FT STRAND 180 182 FT STRAND 184 187 FT STRAND 189 191 FT STRAND 199 205 FT STRAND 213 218 SQ SEQUENCE 266 AA; 30120 MW; 37329B097C6BEEB4 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRYLDRYF HNQEENVRFD SDVGEFRAVT ELGRPDAEYW NSQKDLLEQK RGRVDNYCRH NYGVVESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B14_HUMAN Reviewed; 266 AA. AC P13760; O19717; O19739; P13759; Q29875; Q30145; Q9GIX9; Q9GIY4; AC Q9MY13; Q9XRY5; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 09-JUL-2014, entry version 142. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-4 beta chain; DE AltName: Full=MHC class II antigen DRB1*4; DE Short=DR-4; DE Short=DR4; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*04:01). RX PubMed=3036826; RA Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A., RA Rask L.; RT "Class II genes of the human major histocompatibility complex. RT Organization and evolutionary relationship of the DR beta genes."; RL J. Biol. Chem. 262:8748-8758(1987). RN [2] RP ERRATUM, AND SEQUENCE REVISION. RA Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A., RA Rask L.; RL J. Biol. Chem. 263:8551-8551(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB1*04:01). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*04:01). RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:01). RX PubMed=3860851; DOI=10.1073/pnas.82.15.5165; RA Spies T., Sorrentino R., Boss J.M., Okada K., Strominger J.L.; RT "Structural organization of the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 82:5165-5169(1985). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:01). RX PubMed=9098937; DOI=10.1111/j.1399-0039.1997.tb02751.x; RA Thonnard J., Gervais T., Heusterpreute M., Mersch G., De Canck I., RA De Greef C., Demanet C., Van Waeyenberge C.; RT "A new silent mutation at codon 35 in exon 2 yielding a DRB1*04012 RT allele."; RL Tissue Antigens 49:274-276(1997). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:02). RX PubMed=12358860; DOI=10.1046/j.1365-2370.2002.00354.x; RA Ramon D., Corell A., Cox S.T., Soteriou B., Madrigal J.A., RA Marsh S.G.E.; RT "Complete cDNA sequences of the HLA-DRB1*0402 and DRB1*11041 RT alleles."; RL Eur. J. Immunogenet. 29:453-455(2002). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115 (ALLELE DRB1*04:03). RC TISSUE=Blood; RA Arnaiz-Villena A.; RT "HLA class II polymorphism."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-122 (ALLELE DRB1*04:03). RA Greville W.D., van Eijck A., Dunckley H.; RT "New HLA class II (DRB1) alleles detected by sequencing-based RT typing."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:03). RA Guttridge M.G., Hammond L.; RT "Confirmatory sequence of HLA-DRB1*04032."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:04). RX PubMed=3875800; DOI=10.1038/317166a0; RA Cairns J.S., Curtsinger J.M., Dahl C.A., Freeman S., Alter B.J., RA Bach F.H.; RT "Sequence polymorphism of HLA DR beta 1 alleles relating to T-cell- RT recognized determinants."; RL Nature 317:166-168(1985). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-123 (ALLELE DRB1*04:04). RX PubMed=3458223; DOI=10.1073/pnas.83.8.2642; RA Gregersen P.K., Shen M., Song Q.-L., Merryman P., Degar S., Seki T., RA Maccari J., Goldberg D., Murphy H., Schwenzer J., Wang C.Y., RA Winchester R.J., Nepom G.T., Silver J.; RT "Molecular diversity of HLA-DR4 haplotypes."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2642-2646(1986). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:11). RA Zhao W., Fernandez-Vina M.A., Stastny P.; RT "Full cDNA sequence of HLA-DRB1*0411."; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [14] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [15] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [16] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [17] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [18] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [19] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [20] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH A COLLAGEN RP PEPTIDE. RX PubMed=9354468; DOI=10.1016/S1074-7613(00)80369-6; RA Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.; RT "X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed RT with a peptide from human collagen II."; RL Immunity 7:473-481(1997). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II (Probable). CC -!- POLYMORPHISM: The following alleles of DRB1-4 are known: CC DRB1*04:01, DRB1*04:02, DRB1*04:03, DRB1*04:04, DRB1*04:05, CC DRB1*04:06, DRB1*04:07, DRB1*04:08, DRB1*04:09, DRB1*04:10, CC DRB1*04:11, DRB1*04:12, DRB1*04:13, DRB1*04:14, DRB1*04:15, CC DRB1*04:16, DRB1*04:17, DRB1*04:18, DRB1*04:19, DRB1*04:20, CC DRB1*04:21, DRB1*04:22, DRB1*04:23, DRB1*04:24, DRB1*04:25, CC DRB1*04:26, DRB1*04:27, DRB1*04:28, DRB1*04:29, DRB1*04:30, CC DRB1*04:31, DRB1*04:32, DRB1*04:33, DRB1*04:34, DRB1*04:35, CC DRB1*04:36, DRB1*04:37, DRB1*04:38, DRB1*04:39, DRB1*04:40, CC DRB1*04:41, DRB1*04:42, DRB1*04:43, DRB1*04:44, DRB1*04:45, CC DRB1*04:46, DRB1*04:47, DRB1*04:48, DRB1*04:49, DRB1*04:50, CC DRB1*04:51, DRB1*04:52, DRB1*04:53, DRB1*04:54, DRB1*04:55, CC DRB1*04:56, DRB1*04:57, DRB1*04:58, DRB1*04:59, DRB1*04:60, CC DRB1*04:61, DRB1*04:62, DRB1*04:63, DRB1*04:64, DRB1*04:65, CC DRB1*04:66, DRB1*04:67, DRB1*04:68, DRB1*04:69, DRB1*04:70, CC DRB1*04:71, DRB1*04:72, DRB1*04:73, DRB1*04:74, DRB1*04:75, CC DRB1*04:76, DRB1*04:77 and DRB1*04:78. The sequence shown is that CC of DRB1*04:01. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M20548; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M20549; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M20550; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137064; CAC19360.1; -; Genomic_DNA. DR EMBL; M17381; AAA59805.1; -; mRNA. DR EMBL; K02776; AAA59808.1; -; Genomic_DNA. DR EMBL; X96851; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ297586; CAC08826.2; -; mRNA. DR EMBL; AF029269; AAF65479.1; -; Genomic_DNA. DR EMBL; AF112876; AAD29581.1; -; Genomic_DNA. DR EMBL; AJ295845; CAC08181.1; -; Genomic_DNA. DR EMBL; X02902; CAA26660.1; -; mRNA. DR EMBL; M15069; AAA59809.1; -; mRNA. DR EMBL; L42143; AAA67104.1; -; mRNA. DR PIR; A94681; A29310. DR PIR; I79419; I79419. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR UniGene; Hs.736560; -. DR PDB; 1D5M; X-ray; 2.00 A; B=30-221. DR PDB; 1D5X; X-ray; 2.45 A; B=30-221. DR PDB; 1D5Z; X-ray; 2.00 A; B=30-221. DR PDB; 1D6E; X-ray; 2.45 A; B=30-221. DR PDB; 1J8H; X-ray; 2.40 A; B=30-221. DR PDB; 2SEB; X-ray; 2.50 A; B=30-221. DR PDB; 3O6F; X-ray; 2.80 A; B/F=31-221. DR PDB; 3T0E; X-ray; 4.00 A; B=30-221. DR PDB; 4IS6; X-ray; 2.50 A; B=30-221. DR PDB; 4MCY; X-ray; 2.30 A; B=30-219. DR PDB; 4MCZ; X-ray; 2.41 A; B=30-219. DR PDB; 4MD0; X-ray; 2.19 A; B=30-219. DR PDB; 4MD4; X-ray; 1.95 A; B=30-219. DR PDB; 4MD5; X-ray; 1.65 A; B=30-219. DR PDB; 4MDI; X-ray; 2.00 A; B=30-219. DR PDB; 4MDJ; X-ray; 1.70 A; B=30-219. DR PDBsum; 1D5M; -. DR PDBsum; 1D5X; -. DR PDBsum; 1D5Z; -. DR PDBsum; 1D6E; -. DR PDBsum; 1J8H; -. DR PDBsum; 2SEB; -. DR PDBsum; 3O6F; -. DR PDBsum; 3T0E; -. DR PDBsum; 4IS6; -. DR PDBsum; 4MCY; -. DR PDBsum; 4MCZ; -. DR PDBsum; 4MD0; -. DR PDBsum; 4MD4; -. DR PDBsum; 4MD5; -. DR PDBsum; 4MDI; -. DR PDBsum; 4MDJ; -. DR ProteinModelPortal; P13760; -. DR SMR; P13760; 31-219. DR IntAct; P13760; 6. DR PhosphoSite; P13760; -. DR DMDM; 122253; -. DR MaxQB; P13760; -. DR PaxDb; P13760; -. DR PRIDE; P13760; -. DR Ensembl; ENST00000419393; ENSP00000403458; ENSG00000228080. DR GeneCards; GC06M032546; -. DR GeneCards; GC06Mo32593; -. DR H-InvDB; HIX0207659; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR neXtProt; NX_P13760; -. DR eggNOG; NOG68200; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P13760; -. DR PhylomeDB; P13760; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-DRB1; human. DR EvolutionaryTrace; P13760; -. DR PRO; PR:P13760; -. DR CleanEx; HS_HLA-DRB1; -. DR Genevestigator; P13760; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProt. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISS:UniProtKB. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IDA:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IDA:UniProtKB. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProt. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB. DR GO; GO:2001179; P:regulation of interleukin-10 secretion; ISS:UniProtKB. DR GO; GO:0032673; P:regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-4 beta chain. FT /FTId=PRO_0000018950. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Helical; (Potential). FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 5 5 K -> R (in dbSNP:rs9270305). FT /FTId=VAR_056529. FT VARIANT 86 86 D -> S (in allele DRB1*04:11; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016673. FT VARIANT 96 96 L -> I (in allele DRB1*04:02). FT /FTId=VAR_016674. FT VARIANT 99 99 Q -> D (in allele DRB1*04:02; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016675. FT VARIANT 100 100 K -> E (in allele DRB1*04:02). FT /FTId=VAR_016676. FT VARIANT 100 100 K -> R (in allele DRB1*04:03, allele FT DRB1*04:04 and allele DRB1*04:11). FT /FTId=VAR_016677. FT VARIANT 103 103 A -> E (in allele DRB1*04:03 and allele FT DRB1*04:11). FT /FTId=VAR_016678. FT VARIANT 115 115 G -> V (in allele DRB1*04:02, allele FT DRB1*04:03, allele DRB1*04:04 and allele FT DRB1*04:11). FT /FTId=VAR_016679. FT VARIANT 236 236 V -> M (in dbSNP:rs2230816). FT /FTId=VAR_056530. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_056531. FT CONFLICT 154 154 G -> A (in Ref. 4; AAA59805). FT STRAND 36 47 FT TURN 48 51 FT STRAND 52 61 FT STRAND 64 70 FT TURN 71 73 FT STRAND 74 80 FT HELIX 81 83 FT HELIX 84 91 FT HELIX 94 106 FT HELIX 108 115 FT HELIX 116 118 FT TURN 119 121 FT STRAND 127 133 FT STRAND 143 154 FT STRAND 157 162 FT STRAND 165 167 FT STRAND 171 173 FT STRAND 180 182 FT STRAND 184 191 FT STRAND 199 205 FT STRAND 213 218 SQ SEQUENCE 266 AA; 30112 MW; 8116E91DA38294E5 CRC64; MVCLKFPGGS CMAALTVTLM VLSSPLALAG DTRPRFLEQV KHECHFFNGT ERVRFLDRYF YHQEEYVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQK RAAVDTYCRH NYGVGESFTV QRRVYPEVTV YPAKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKTG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSLT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B18_HUMAN Reviewed; 266 AA. AC Q30134; O19718; O19788; Q29968; Q30108; Q30115; Q9BCP0; Q9BCP1; AC Q9BCP2; Q9BD33; Q9TQ37; Q9UIM9; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 2. DT 16-APR-2014, entry version 108. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-8 beta chain; DE AltName: Full=MHC class II antigen DRB1*8; DE Short=DR-8; DE Short=DR8; DE Short=DRw8; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*08:02). RX PubMed=2497068; DOI=10.1007/BF00352840; RA Jonsson A.K., Andersson L., Rask L.; RT "A cellular and functional split in the DRw8 haplotype is due to a RT single amino acid replacement (DR beta ser 57- asp 57)."; RL Immunogenetics 29:308-316(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. RX PubMed=8106268; DOI=10.1016/0198-8859(93)90531-5; RA Emery P., Mach B., Reith W.; RT "The different level of expression of HLA-DRB1 and -DRB3 genes is RT controlled by conserved isotypic differences in promoter sequence."; RL Hum. Immunol. 38:137-147(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-115 (ALLELE DRB1*08:01). RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123. RX PubMed=1979063; RA Van Kerckhove C., Melin-Aldana H., Elma M.S., Luyrink L., Donnelly P., RA Taylor J., Maksymowych W.P., Lovell D.J., Choi E., Glass D.N.; RT "A distinct HLA-DRw8 haplotype characterizes patients with juvenile RT rheumatoid arthritis."; RL Immunogenetics 32:304-308(1990). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*08:01). RA Dormoy A., Froelich N., Weschler B., Tongio M.M.; RT "A new DRB1*08 allele."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*08:04). RC TISSUE=Blood; RA Hurley C.K., Tang T., Li L.; RT "Human leukocyte antigen class II DRB1*0804 variant."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-208 (ALLELE DRB1*08:01). RA Greville W.D.; RT "SBT of DRB1*0801, exons two and three."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-115 (ALLELE DRB1*08:03). RX PubMed=2592019; DOI=10.1007/BF02421173; RA Abe A., Ito I., Ohkubo M., Kaneko T., Ito K., Kato H., Kashiwagi N., RA Obata F.; RT "Two distinct subtypes of the HLA-DRw12 haplotypes in the Japanese RT population detected by nucleotide sequence analysis and RT oligonucleotide genotyping."; RL Immunogenetics 30:422-426(1989). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-120 (ALLELE DRB1*08:01). RA Eberle M., Asu U., Taylor M., Hunter J.B., Fuller T.C., Maurer D.; RT "Identification of a putative DR8 founder haplotype containing a novel RT DRB1*08 allele."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-122 (ALLELE DRB1*08:04). RC TISSUE=Blood; RX PubMed=8023844; RA Titus-Trachtenberg E.A., Rickards O., De Stefano G.F., Erlich H.A.; RT "Analysis of HLA class II haplotypes in the Cayapa Indians of Ecuador: RT a novel DRB1 allele reveals evidence for convergent evolution and RT balancing selection at position 86."; RL Am. J. Hum. Genet. 55:160-167(1994). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-217. RX PubMed=2471740; RA Gorski J.; RT "HLA-DR beta-chain polymorphism. Second domain polymorphism reflects RT evolutionary relatedness of alleles and may explain public serologic RT epitopes."; RL J. Immunol. 143:329-333(1989). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 256-266. RX PubMed=3458223; DOI=10.1073/pnas.83.8.2642; RA Gregersen P.K., Shen M., Song Q.-L., Merryman P., Degar S., Seki T., RA Maccari J., Goldberg D., Murphy H., Schwenzer J., Wang C.Y., RA Winchester R.J., Nepom G.T., Silver J.; RT "Molecular diversity of HLA-DR4 haplotypes."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2642-2646(1986). RN [13] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [14] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [15] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [16] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [17] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [18] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [19] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II (Probable). CC -!- POLYMORPHISM: The following alleles of DRB1-8 are known: CC DRB1*08:01 (Dw8.1), DRB1*08:02 (Dw8.2; DRB1L), DRB1*08:03 (Dw8.3); CC DRB1*08:04; DRB1*08:05, DRB1*08:06, DRB1*08:07, DRB1*08:08, CC DRB1*08:09, DRB1*08:10, DRB1*08:11, DRB1*08:12, DRB1*08:13, CC DRB1*08:14, DRB1*08:15, DRB1*08:16, DRB1*08:17, DRB1*08:18, CC DRB1*08:19, DRB1*08:20, DRB1*08:21, DRB1*08:22, DRB1*08:23, CC DRB1*08:24, DRB1*08:25, DRB1*08:26, DRB1*08:27, DRB1*08:28, CC DRB1*08:29, DRB1*08:30, DRB1*08:31, DRB1*08:32, DRB1*08:33, CC DRB1*08:34, DRB1*08:35 and DRB1*08:36. The sequence shown is that CC of DRB1*08:01. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M26038; AAA59794.1; -; mRNA. DR EMBL; S69987; AAD14052.1; -; Genomic_DNA. DR EMBL; M17386; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M60216; AAA36298.1; -; Genomic_DNA. DR EMBL; AJ249626; CAB56284.1; -; Genomic_DNA. DR EMBL; AF330103; AAK08504.1; -; Genomic_DNA. DR EMBL; AH010612; AAK31608.1; -; Genomic_DNA. DR EMBL; AH010613; AAK31609.1; -; Genomic_DNA. DR EMBL; AH010614; AAK31610.1; -; Genomic_DNA. DR EMBL; M27511; AAA59817.1; -; Genomic_DNA. DR EMBL; AF144105; AAD38374.1; -; Genomic_DNA. DR EMBL; L10402; AAA51400.1; -; Genomic_DNA. DR EMBL; M15074; AAA59810.1; -; mRNA. DR PIR; A45856; A45856. DR PIR; F60748; F60748. DR PIR; I51875; I51875. DR PIR; I54473; I54473. DR PIR; I68778; I68778. DR PIR; PH0160; PH0160. DR PIR; PT0161; PT0161. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q30134; -. DR SMR; Q30134; 34-220. DR DMDM; 34395492; -. DR PaxDb; Q30134; -. DR PRIDE; Q30134; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR GeneCards; GC06M032546; -. DR GeneCards; GC06Mj32477; -. DR GeneCards; GC06Mn32480; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR neXtProt; NX_Q30134; -. DR eggNOG; NOG68200; -. DR HOVERGEN; HBG012730; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-DRB1; human. DR PRO; PR:Q30134; -. DR CleanEx; HS_HLA-DRB1; -. DR Genevestigator; Q30134; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-8 beta chain. FT /FTId=PRO_0000018952. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 250 Helical; (Potential). FT TOPO_DOM 251 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 44 108 By similarity. FT DISULFID 146 202 By similarity. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 86 86 S -> D (in allele DRB1*08:02 and allele FT DRB1*08:04; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016683. FT VARIANT 96 96 F -> I (in allele DRB1*08:03). FT /FTId=VAR_016684. FT VARIANT 115 115 G -> V (in allele DRB1*08:04). FT /FTId=VAR_016685. FT VARIANT 236 236 V -> M (in dbSNP:rs2230816). FT /FTId=VAR_056535. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_056536. SQ SEQUENCE 266 AA; 30004 MW; D452D1C3A75CEA31 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TGECYFFNGT ERVRFLDRYF YNQEEYVRFD SDVGEYRAVT ELGRPSAEYW NSQKDFLEDR RALVDTYCRH NYGVGESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWSAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B1C_HUMAN Reviewed; 266 AA. AC Q95IE3; A7LA26; B0LUZ6; B6VCX2; B7UDB2; O19585; Q19AF2; Q29771; AC Q2L9H4; Q2MZ92; Q5EER6; Q5NDB9; Q5UT58; Q5Y7G0; Q768U4; Q7YP04; AC Q861H8; Q95IT6; Q9BD40; DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 16-APR-2014, entry version 94. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-12 beta chain; DE AltName: Full=MHC class II antigen DRB1*12; DE Short=DR-12; DE Short=DR12; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*12:01). RX PubMed=12028552; DOI=10.1034/j.1399-0039.2002.590221.x; RA Zanone R., Bettens F., Tiercy J.M.; RT "Sequence of a new DR12 allele with two silent mutations that affect RT PCR-SSP typing."; RL Tissue Antigens 59:165-167(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*12:10). RX PubMed=15361134; DOI=10.1111/j.1399-0039.2004.00309.x; RA Kim E., Lee E.J., Lim Y.H., Lee J.Y., Koh I.S., Kimm K., Ji G.E., RA Kwack K.; RT "Identification of a novel HLA-DRB1*12 allele (DRB1*1210) in the RT Korean population."; RL Tissue Antigens 64:518-519(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*12:17). RX PubMed=19493243; DOI=10.1111/j.1399-0039.2009.01224.x; RA Park M.H., Kim Y., Lee J.Y.; RT "Identification of a novel HLA-DRB1 allele, HLA-DRB1*1217, in a Korean RT individual."; RL Tissue Antigens 73:627-628(2009). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-262 (ALLELE DRB1*12:01). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-208 (ALLELE DRB1*12:07). RX PubMed=12028551; DOI=10.1034/j.1399-0039.2002.590220.x; RA Dunckley H., Le T., Dodd R., Hogbin J.P., Strickland J., Chapman G., RA Greville W.D.; RT "Description of a novel HLA-DRB1 allele, DRB1*1207."; RL Tissue Antigens 59:162-164(2002). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:11). RC TISSUE=Peripheral blood; RX PubMed=16690413; DOI=10.1016/j.humimm.2005.05.002; RA Horn P.A., DeLuca D.S., Jindra P., Blasczyk R.; RT "The replacement mutation in HLA-DRB1*1211 affects a likely keystone RT position."; RL Hum. Immunol. 66:1254-1257(2005). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:08). RX PubMed=12144630; DOI=10.1034/j.1399-0039.2002.590513.x; RA Sheldon M.H., Bunce M., Dunn P.P., Day S., Lee G.D., Park Y.J., RA Bang B.K., Kim B.K., Oh E.J.; RT "Identification of two new alleles in a single Korean individual, HLA- RT B*1568 and HLA-DRB1*1208."; RL Tissue Antigens 59:430-432(2002). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:15). RX PubMed=19046299; DOI=10.1111/j.1744-313X.2008.00785.x; RA Lee H.L., Chu C.C., Trejaut J.A., Yang K.L., Lin M.; RT "Identification of two novel HLA-DRB1 alleles, HLA-DRB1*1214 and HLA- RT DRB1*1215, in two Taiwanese individuals."; RL Int. J. Immunogenet. 35:423-426(2008). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:19). RX PubMed=19624612; DOI=10.1111/j.1399-0039.2009.01316.x; RA Nie X.M., Fang Y.H., Zhang Y., He W.D., Zhu C.F.; RT "A novel HLA-DRB1 allele, DRB1*1219, was identified by sequence-based RT typing in a Chinese leukaemia family."; RL Tissue Antigens 74:352-354(2009). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:18). RX PubMed=19508407; DOI=10.1111/j.1399-0039.2009.01294.x; RA Gao S.Q., Deng Z.H., Xu Y.P.; RT "Identification of a novel HLA-DRB1*12 allele, DRB1*1218, in Chinese RT population."; RL Tissue Antigens 74:265-267(2009). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:05). RA Kashiwase K., Tokunaga K., Akaza T., Tadokoro K., Juji T.; RT "Sequence of new allele."; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:09). RA Ono A.; RT "A new HLA-DR12V allele detected by PCR-RFLP."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:04). RA Gedil M.A., Steiner N.K., Hurley C.K.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:12). RA Zhu F., Lu Q., Zhang W.; RT "Identification a novel HLA-DRB1*12 in Chinese by sequence-based RT typed."; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:13). RA Hur S.S., Lee M.N., Park S.Y., Kwon O.J.; RT "Novel HLA-DRB1*120201 variant allele."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:14). RA Chu C.-C.; RT "A novel HLA-DRB1 allele."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:16). RA Zhang C., Liu J.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB1*12:03). RX PubMed=8851733; DOI=10.1111/j.1399-0039.1996.tb02532.x; RA Hashemi S., Couture C., Buyse I., Cole R., Aye M.T.; RT "Sequence analysis of three novel HLA-DRB1 alleles: DRB1*1113, RT DRB1*1114 and DRB1*12032."; RL Tissue Antigens 47:155-158(1996). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELE DRB1*12:02). RA Lo B.; RT "HLA class II DRB1*120201 confirmatory sequence."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] OF 88-197 (ALLELE DRB1*12:06). RX PubMed=10372549; DOI=10.1034/j.1399-0039.1999.530510.x; RA Maeng C.Y., Kim K.H., Kang J.H., Han H., Kim K.L.; RT "A novel HLA-DR12 allele (DRB1*1206) found in a Korean B-cell line."; RL Tissue Antigens 53:516-518(1999). RN [21] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [22] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [23] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [24] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [25] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [26] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [27] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II (Probable). CC -!- POLYMORPHISM: The following alleles of DRB1-12 are known: CC DRB1*12:01, DRB1*12:02, DRB1*12:03, DRB1*12:04, DRB1*12:05, CC DRB1*12:06, DRB1*12:07, DRB1*12:08, DRB1*12:09, DRB1*12:10, CC DRB1*12:11, DRB1*12:12, DRB1*12:13, DRB1*12:14, DRB1*12:15, CC DRB1*12:16, DRB1*12:17, DRB1*12:18 and DRB1*12:19. The sequence CC shown is that of DRB1*12:01. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ302075; CAC44379.1; -; mRNA. DR EMBL; AY626551; AAV34808.1; -; mRNA. DR EMBL; EU375850; ABY78039.1; -; mRNA. DR EMBL; AY663396; AAU87983.1; -; Genomic_DNA. DR EMBL; AH010330; AAK07563.1; -; Genomic_DNA. DR EMBL; AJ870921; CAI35044.1; -; Genomic_DNA. DR EMBL; AY033428; AAK55114.1; -; Genomic_DNA. DR EMBL; DQ533486; ABF74752.1; -; Genomic_DNA. DR EMBL; FJ374889; ACJ09136.1; -; Genomic_DNA. DR EMBL; FJ481086; ACK77491.1; -; Genomic_DNA. DR EMBL; D86503; BAA13098.1; -; Genomic_DNA. DR EMBL; AB112911; BAD02942.1; -; Genomic_DNA. DR EMBL; AY339246; AAQ18913.1; -; Genomic_DNA. DR EMBL; AY899825; AAW82078.1; -; Genomic_DNA. DR EMBL; DQ250650; ABC59072.1; -; Genomic_DNA. DR EMBL; DQ343834; ABC70992.1; -; Genomic_DNA. DR EMBL; EF688603; ABS11697.1; -; Genomic_DNA. DR EMBL; X83455; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY174091; AAO20088.1; -; Genomic_DNA. DR EMBL; AF017439; AAB70553.1; -; mRNA. DR PIR; C60748; C60748. DR PIR; F60748; F60748. DR PIR; PH0154; PH0154. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q95IE3; -. DR SMR; Q95IE3; 34-220. DR DMDM; 74760669; -. DR PRIDE; Q95IE3; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR Ensembl; ENST00000412634; ENSP00000408795; ENSG00000228080. DR Ensembl; ENST00000415796; ENSP00000412168; ENSG00000206306. DR Ensembl; ENST00000419393; ENSP00000403458; ENSG00000228080. DR Ensembl; ENST00000428566; ENSP00000392280; ENSG00000206240. DR GeneCards; GC06M032546; -. DR GeneCards; GC06Mj32477; -. DR GeneCards; GC06Mn32480; -. DR GeneCards; GC06Mo32593; -. DR HGNC; HGNC:4948; HLA-DRB1. DR neXtProt; NX_Q95IE3; -. DR HOVERGEN; HBG012730; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-DRB1; human. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 Potential. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-12 beta chain. FT /FTId=PRO_0000391832. FT TRANSMEM 228 248 Helical; (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 146 202 By similarity. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 5 5 R -> K (in allele DRB1*12:17). FT /FTId=VAR_062818. FT VARIANT 13 13 A -> T (in allele DRB1*12:17). FT /FTId=VAR_062819. FT VARIANT 14 14 V -> A (in allele DRB1*12:17). FT /FTId=VAR_062820. FT VARIANT 14 14 V -> I (in allele DRB1*12:10). FT /FTId=VAR_062821. FT VARIANT 54 54 R -> L (in allele DRB1*12:13). FT /FTId=VAR_062822. FT VARIANT 55 55 L -> F (in allele DRB1*12:08). FT /FTId=VAR_062823. FT VARIANT 66 66 L -> F (in allele DRB1*12:05, allele FT DRB1*12:14 and allele DRB1*12:15). FT /FTId=VAR_062824. FT VARIANT 67 67 L -> V (in allele DRB1*12:14). FT /FTId=VAR_062825. FT VARIANT 76 76 F -> L (in allele DRB1*12:11). FT /FTId=VAR_062826. FT VARIANT 86 86 V -> D (in allele DRB1*12:04 and allele FT DRB1*12:09). FT /FTId=VAR_062827. FT VARIANT 87 87 A -> E (in allele DRB1*12:04). FT /FTId=VAR_062828. FT VARIANT 88 88 E -> Q (in allele DRB1*12:18). FT /FTId=VAR_062829. FT VARIANT 89 89 S -> Y (in allele DRB1*12:04 and allele FT DRB1*12:09). FT /FTId=VAR_062830. FT VARIANT 96 96 I -> F (in allele DRB1*12:02, allele FT DRB1*12:13, allele DRB1*12:15, allele FT DRB1*12:16, allele DRB1*12:18 and allele FT DRB1*12:19). FT /FTId=VAR_062831. FT VARIANT 96 96 I -> L (in allele DRB1*12:12). FT /FTId=VAR_062832. FT VARIANT 98 98 E -> G (in allele DRB1*12:07). FT /FTId=VAR_062833. FT VARIANT 114 114 A -> V (in allele DRB1*12:03, allele FT DRB1*12:16 and allele DRB1*12:19). FT /FTId=VAR_062834. FT VARIANT 115 115 V -> G (in allele DRB1*12:16). FT /FTId=VAR_062835. FT VARIANT 125 125 H -> E (in allele DRB1*12:17; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062836. FT VARIANT 169 169 T -> A (in allele DRB1*12:17). FT /FTId=VAR_062837. FT VARIANT 178 178 H -> Q (in allele DRB1*12:06 and allele FT DRB1*12:17). FT /FTId=VAR_062838. FT VARIANT 262 262 R -> T (in allele DRB1*12:17; FT dbSNP:rs9269744). FT /FTId=VAR_062839. SQ SEQUENCE 266 AA; 29878 MW; FFDD0001C2F0BAF9 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TGECYFFNGT ERVRLLERHF HNQEELLRFD SDVGEFRAVT ELGRPVAESW NSQKDILEDR RAAVDTYCRH NYGAVESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B1D_HUMAN Reviewed; 266 AA. AC Q5Y7A7; A0MWF2; A2ICT1; A4ZXA5; A4ZXA6; A7UHG2; A7X5K7; A8YQE9; AC B0BK85; B3VTQ3; B5A8Y2; B5A8Y3; B5B9V6; B5QSK8; C0LAB5; O02930; AC O62889; O78047; P79545; Q14280; Q14QT2; Q19K86; Q1G0Z9; Q1KLJ6; AC Q29673; Q29720; Q29722; Q29806; Q29833; Q29874; Q29886; Q2MF40; AC Q2YHQ2; Q30112; Q3LA93; Q3LA94; Q3LA95; Q3LA96; Q3LA97; Q3LA98; AC Q3LA99; Q3LAA0; Q3LAA1; Q3LAA2; Q3MQ60; Q53IG1; Q56FP2; Q56FP3; AC Q58F52; Q5K3W2; Q5UBA2; Q5W3L4; Q6REE2; Q6U387; Q701T1; Q70Q85; AC Q768U2; Q7YP03; Q7YQ26; Q7YQA3; Q860E5; Q860H8; Q860Z3; Q861G6; AC Q861H0; Q861H4; Q8HWQ6; Q8WMA0; Q95389; Q95HL1; Q96HZ9; Q9BCP5; AC Q9BD21; Q9GIP3; Q9GJ25; Q9GJ60; Q9GJF8; Q9GJF9; Q9GJG0; Q9MY45; AC Q9MY56; Q9TPW3; Q9TPW9; Q9TPX4; Q9UBY1; Q9UIN0; Q9XRX1; Q9Y453; DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 14-MAY-2014, entry version 86. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-13 beta chain; DE AltName: Full=MHC class II antigen DRB1*13; DE Short=DR-13; DE Short=DR13; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*13:01 AND DRB1*13:02). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*13:05). RX PubMed=15896200; DOI=10.1111/j.1399-0039.2005.00407.x; RA Vilches C., Sepulveda S., Balas A., Solis R., Aviles M.J., RA Estefania E., Gomez-Lozano N., Vicario J.L., DePablo R.; RT "Complete coding sequences and haplotypic associations of HLA-B*0707, RT -B*1524, -B*4405, -B*4802, -DRB1*0409, -DRB1*0411, -DRB1*1115, - RT DRB1*1305, and the novel allele -DRB1*0709. Group-specific RT amplification of cDNA from DRB1 alleles associated to DRB3 and DRB4."; RL Tissue Antigens 65:529-538(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*13:27 AND DRB1*13:56). RX PubMed=17174751; DOI=10.1016/j.humimm.2006.09.002; RA Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P., RA de Pablo R., Garcia-Sanchez F., Vicario J.L.; RT "Group-specific amplification of cDNA from DRB1 genes. Complete coding RT sequences of partially defined alleles and identification of the new RT alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113."; RL Hum. Immunol. 67:1008-1016(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*13:02). RC TISSUE=Blood; RA Arnaiz-Villena A., Martinez-Quiles N., De Juan-Echavarri D., RA Martin-Villa M., Martinez-Laso J.; RT "New complete sequences of MHC-DR in Spanish family with systemic RT lupus erythematosus."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB1*13:01). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB1*13:02). RC TISSUE=B-cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-148 (ALLELE DRB1*13:21). RC TISSUE=Leukocyte; RA Maurer D.H.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-123 (ALLELE DRB1*13:19). RC TISSUE=Blood; RX PubMed=7652736; DOI=10.1111/j.1399-0039.1995.tb02458.x; RA Robbins F., Tang T., Yao H., Ng J., Hartzman R.J., Hurley C.K.; RT "Direct sequencing of SSP-PCR-amplified cDNA to identify new alleles RT in the DR52-associated DRB1 group: identification of DRB1*1115, RT DRB1*1117 and DRB1*1319."; RL Tissue Antigens 45:302-308(1995). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-130 (ALLELE DRB1*13:04). RX PubMed=2212675; RA Lee K.W., Johnson A.H., Hurley C.K.; RT "Two divergent routes of evolution gave rise to the DRw13 RT haplotypes."; RL J. Immunol. 145:3119-3125(1990). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB1*13:87). RA Ogrzewalla K., Tillmann G., Scheibelhut N., Lauber J., Enczmann J.; RT "A novel HLA-DRB1*13 allele identified by sequence-based typing."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-216 (ALLELES DRB1*13:03; RP DRB1*13:06; DRB1*13:08; DRB1*13:10; DRB1*13:11; DRB1*13:14; RP DRB1*13:17; DRB1*13:20; DRB1*13:29 AND DRB1*13:36). RC TISSUE=Peripheral blood; RX PubMed=17767557; DOI=10.1111/j.1399-0039.2007.00918.x; RA Horn P.A., Albis-Camps M., Verboom M., Bunce M., Yousaf K., RA Williams S., Blasczyk R.; RT "The nature of diversity of HLA-DRB1 exon 3."; RL Tissue Antigens 70:335-337(2007). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-124 (ALLELE DRB1*13:12). RA Hu C.J.; RT "DR variant with a DR5-like-haplotype found in Taiwan."; RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:18). RX PubMed=8575826; DOI=10.1007/s002510050054; RA Dormoy A., Delbosc A., Galy-Floc'h M., Tongio M.M.; RT "A new HLA-DRB1(*)13 allele (DRB1(*)1318) with a short DRB1(*)08 RT sequence."; RL Immunogenetics 43:240-241(1996). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:22). RX PubMed=9271638; DOI=10.1007/s002510050302; RA Duran K.J., Maeda H., Otten H.G., Vries R.D., Schreuder G.M., RA Tilanus M.G.; RT "Two newly identified HLA-DRB1 alleles: DRB1*1322 and DRB1*1327."; RL Immunogenetics 46:442-443(1997). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*13:42 AND RP DRB1*13:43), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELES RP DRB1*13:35; DRB1*13:37 AND DRB1*13:49), AND NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 35-115 (ALLELE DRB1*13:38). RX PubMed=11972885; DOI=10.1034/j.1399-0039.2002.590115.x; RA Tang T.F., Lin Y.-S., Robbins F.M., Li L., Sintasath D., RA Coquillard G., Huang A., Heine U., Ng J., Hartzman R.J., Hurley C.K.; RT "Description of fourteen new DRB alleles found in a stem cell donor RT registry."; RL Tissue Antigens 59:63-65(2002). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:46). RX PubMed=12028548; DOI=10.1034/j.1399-0039.2002.590217.x; RA Greville W.D., Chapman G., Hogbin J.-P., Kennedy A., Dunckley H.; RT "Novel HLA-DRB1 alleles discovered during routine sequencing based RT typing, DRB1*03052, DRB1*04032, DRB1*1139 and DRB1*1346."; RL Tissue Antigens 59:154-156(2002). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:44). RX PubMed=12028549; DOI=10.1034/j.1399-0039.2002.590218.x; RA Kennedy A., Le T., Chapman G., Greville W.D., Dunckley H.; RT "Identification of two new HLA-DRB1 alleles, DRB1*1138 and RT DRB1*1344."; RL Tissue Antigens 59:157-158(2002). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:60). RX PubMed=15140048; DOI=10.1111/j.0001-2815.2004.00226.x; RA Testa G.V., Bunce M., Sheldon M.H., Dunn P.P., Day S., Marques S.B.; RT "Identification of a new allele, HLA-DRB1*1360, on a DRB5 haplotype in RT a Brazilian individual."; RL Tissue Antigens 63:617-618(2004). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:57). RX PubMed=15245379; DOI=10.1111/j.1399-0039.2004.00261.x; RA Danzer M., Leitner D., Gangl E., Fae I., Fischer G.F., Gabriel C.; RT "A novel HLA-DRB1*13 allele (DRB1*1357) identified by polymerase chain RT reaction with sequence-specific primers and direct sequencing."; RL Tissue Antigens 64:213-214(2004). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:50). RX PubMed=15304013; DOI=10.1111/j.0001-2815.2004.00282.x; RA Chen Z.X., Tsan S.G., Dang C.W., Chu C.C., Lin M., Lee Y.J.; RT "Identification of two new HLA-DRB1 alleles: HLA-DRB1*1350 and RT DRB1*140502."; RL Tissue Antigens 64:300-303(2004). RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:51). RX PubMed=15304015; DOI=10.1111/j.0001-2815.2004.00275.x; RA Chu C.C., Lee H.L., Hsieh N.K., Trejaut J., Lin M.; RT "Two novel HLA-DRB1 alleles identified using a sequence-based typing: RT HLA-DRB1*1443 and HLA-DRB1*1351*."; RL Tissue Antigens 64:308-310(2004). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:66). RX PubMed=15982265; DOI=10.1111/j.1399-0039.2005.00427.x; RA Milia S., Lai S., Valentini T., Testi M., Cappai L., Moscetti A., RA Mariani M., Alba F., Carcassi C.; RT "Identification of a new allele, HLA-DRB1*1366*."; RL Tissue Antigens 66:69-71(2005). RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:64). RC TISSUE=Peripheral blood; RX PubMed=16029439; DOI=10.1111/j.1399-0039.2005.00440.x; RA Czachurski D., Scollo A., Skambraks A., Perichon A.M., Scherer S., RA Tran T.H., Opelz G., Grappiolo I., Mytilineos J.; RT "Description and characterization of two new HLA alleles, B*4051 and RT DRB1*1364, identified by sequence-based typing."; RL Tissue Antigens 66:151-155(2005). RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:68). RX PubMed=16101838; DOI=10.1111/j.1399-0039.2005.00451.x; RA Caggiari L., Simula M.P., Marzotto A., Caragnano A., Luchetti M., RA Gabrielli A., De Re V.; RT "Identification of a novel human DRB1*13 allele by sequence-based DRB RT typing."; RL Tissue Antigens 66:246-247(2005). RN [25] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:70). RC TISSUE=Peripheral blood; RX PubMed=16634878; DOI=10.1111/j.1399-0039.2006.00580.x; RA Horn P.A., Zingsem J., Eckstein R., Blasczyk R.; RT "Novel HLA-DRB1*1370 allele identified in a cord blood donor and her RT mother."; RL Tissue Antigens 67:345-347(2006). RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:77). RC TISSUE=Blood; RA Tavoularis S., Conrod V., Ribeiro E.; RT "Identification of three novel DRB1 alleles."; RL Hum. Immunol. 68:S63-S63(2007). RN [27] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:75). RX PubMed=17257328; DOI=10.1111/j.1399-0039.2006.00750.x; RA Sanchez-Gordo F., Balas A., Ortiz M., Prat I., Vicario J.L.; RT "A new human leukocyte antigen DRB1 allele, HLA-DRB1*1375."; RL Tissue Antigens 69:204-205(2007). RN [28] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:71). RX PubMed=17493158; DOI=10.1111/j.1399-0039.2006.00753.x; RA McWhinnie A.J., Shah A., Peat J., Tavarozzi F., Little A.M.; RT "Description of HLA-DRB1*1371 allele, which has the 3' intron 1 RT sequence and HLA-DQB1 association normally seen with a DRB1*0301 RT allele."; RL Tissue Antigens 69:284-285(2007). RN [29] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:76). RX PubMed=17498272; DOI=10.1111/j.1399-0039.2007.00835.x; RA Abdeen H., McErlean C., Moraes M.E., Torres M., Campiotto S., RA Galvao S., Gouvea C., Middleton D.; RT "Identification of three novel alleles of HLA-DRB1 and HLA-A in the RT Brazilian population."; RL Tissue Antigens 69:607-610(2007). RN [30] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:82). RC TISSUE=Blood; RX PubMed=19744147; DOI=10.1111/j.1399-0039.2009.01334.x; RA Anholts J.D., Aneq M., Dirks H.L., Tas A., Verduyn W., Oudshoorn M.; RT "Thirty-six novel HLA alleles: 7 HLA-A, 11 HLA-B, 15 HLA-C and 3 HLA- RT DRB1."; RL Tissue Antigens 74:424-428(2009). RN [31] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:32). RC TISSUE=Peripheral blood; RA Lester S., Laham N., Humphreys I., McCluskey J.; RT "A new DRB1*13 allele detected by PCR-SSOP and confirmed by RT sequencing."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [32] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:34). RA Erne G., Schmid C., Schwarz K., Woelpl A.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [33] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:39). RA Park M.H., Whang D.H., Kang S.J.; RT "A new HLA-DRB1*13 allele in a Korean individual."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [34] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:14). RC TISSUE=Peripheral blood; RA Guttridge M.G.; RT "Sequence confirmation of HLA-DRB1*1314."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [35] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:41). RA Bois M., Dormoy A., Alcalay D.; RT "Characterization of a new HLA-DRB1*13 class II allele."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [36] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:48). RC TISSUE=Peripheral blood; RA Moine A.; RT "A new HLA DRB1* allele close to DRB1*1304."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [37] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:47). RA Kashiwase K., Shimizu M., Juji T., Tanaka H., Ishikawa Y.; RT "HLA-DRB1-1307V for exon2."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [38] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:07). RA Tamouza R., Keyhani M., Poirier J.C., Schaeffer V., Fortier C., RA Labie D., Charron D.; RT "New HLA-DRB1*13."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [39] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:01). RA Voorter C.E., van den Berg-Loonen E.M.; RT "New HLA DRB1*13 allele identified by sequence-based typing."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [40] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*13:01 AND RP DRB1*13:16). RA Rizzo M., Gedil M.A., Steiner N.K., Hurley C.K.; RT "Complete exon 2 sequence for HLA-DRB1*1316."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [41] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:69). RA Rodriguez-Marino S., Coquillard G.J.; RT "Novel HLA-DRB1*1301 Variant."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [42] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:58). RA Chen D.-F., Dong L., Janzen M., Rabson A., Fraser P.; RT "Novel HLA-DRB1*13 alleles detected by PCR-SSOP and confirmed by RT single allele specific sequencing."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [43] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:54). RA Ono A.; RT "A new HLA-DR12V allele detected by PCR-RFLP."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [44] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:61). RA Lazaro A.M., Gedil M.A., Rizzo M., Hurley C.K.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [45] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*13:62 AND RP DRB1*13:63). RA Hirv K., Krauss A., Schwarz K.; RT "Characterization of a new HLA-DRB1 allele by direct sequencing."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [46] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:59). RA Bendukidze N.; RT "Rare DRB1*1359 alleles confirmatory testing."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [47] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:65). RA Czachurski D.; RT "Hochaufloesende Typisierung von HLA-Klasse I und Klasse II mittels RT Sequenzanalyse. Einfluss auf das Transplantatueberleben."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [48] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:67). RC TISSUE=Peripheral blood; RA Binder T.M.C., Mosebach M., Kuehnl P., Heim M.U., Blasczyk R., RA Eiermann T.H.; RT "A new HLA-DRB1*13 variant similar to DRB1*130201 and DRB3*020101."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [49] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:74). RC TISSUE=Peripheral blood; RA Dunne C., Crowley J.; RT "Sequence of new HLA-DRB1*13 allele DRB1*13XX."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [50] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:79). RC TISSUE=Blood; RA Duignan P., Varney M., Holdsworth R.; RT "New DRB1*13 allele found in cord blood."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [51] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:78). RA Moore J., Bowman S., Varney M., Tait B.; RT "New HLA DR13 sequence found in bone marrow donor."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [52] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:83). RA Horn P.A., Blasczyk R.; RT "A novel HLA-DRB1*13 allele."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [53] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*13:31; RP DRB1*13:72; DRB1*13:73; DRB1*13:80; DRB1*13:81; DRB1*13:84; RP DRB1*13:85; DRB1*13:86 AND DRB1*13:88). RA Lazaro A.M., Xiao Y., Cao K., Shan X., Zhang B., Masaberg C., RA Hurley C.K.; RT "Novel HLA-class II allele."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [54] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELES DRB1*13:23 AND RP DRB1*13:24). RX PubMed=9243754; DOI=10.1111/j.1399-0039.1997.tb02832.x; RA Ellis J.M., Robbins F., Wang J., Tang T., Heine U., Mason J.M., RA Sese D., Milford E., Hurley C.K.; RT "Identification of four new DR52-associated DRB1 alleles: DRB1*1424, RT *1425, *1323 and *1324."; RL Tissue Antigens 50:42-46(1997). RN [55] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-120 (ALLELE DRB1*13:13). RC TISSUE=Blood; RA Hurley C.K., Noreen H., Lin Y.S.; RT "DRB1*1313."; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [56] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-120 (ALLELE DRB1*13:52). RA Rodriguez-Marino S., Coquillard G.; RT "Characterization of a new DRB1*13011 variant allele."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [57] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-116 (ALLELE DRB1*13:25). RX PubMed=9008317; DOI=10.1111/j.1399-0039.1996.tb02698.x; RA Poli F., Bianchi P., Crespiatico L., Sirchia G.; RT "Identification of a new DRB1 allele (DRB1*1325) by PCR-SSP and DNA RT sequencing."; RL Tissue Antigens 48:714-716(1996). RN [58] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB1*13:33). RC TISSUE=Blood; RX PubMed=9694360; DOI=10.1111/j.1399-0039.1998.tb03010.x; RA Buyse I.M., Ouellet S., Hashemi-Tavoularis S.; RT "Identification of novel DRB1*13 (DRB1*1333), DRB1*04 (DRB1*0426) and RT DRB5* (DRB5*0109) alleles."; RL Tissue Antigens 51:658-662(1998). RN [59] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELE DRB1*13:40). RC TISSUE=Cervix; RX PubMed=11019927; DOI=10.1034/j.1399-0039.2000.560218.x; RA Maciag P.C., Junes K.S., Villa L.L., Petzl-Erler M.L.; RT "Identification of a novel allele, DRB1*1340, in two Brazilian RT individuals."; RL Tissue Antigens 56:194-196(2000). RN [60] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELE DRB1*13:53). RC TISSUE=Peripheral blood; RA Poli F., Longhi E., Frison S.; RT "Identification of a new HLA DRB1*13 by SBT."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [61] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELES DRB1*13:15 AND RP DRB1*13:55). RA Lo B.; RT "Confirmatory Sequence of HLA Class II DRB1*1315."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [62] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-120 (ALLELE DRB1*13:09). RC TISSUE=Blood; RX PubMed=8023320; DOI=10.1111/j.1399-0039.1994.tb02298.x; RA Yunis J.J., Kineke E., Yunis E.J.; RT "Characterization of a new DRB1 allele, DRB1*1309, by PCR-SSOP and RT sequencing."; RL Tissue Antigens 43:54-57(1994). RN [63] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-119 (ALLELE DRB1*13:30). RA Greville W.D., Bowman S.; RT "New HLA class II (DRB1) allele from Melbourne BTS."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [64] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-119 (ALLELE DRB1*13:28). RA Varney M.D., Tait B.D.; RT "Identification of a novel DPB allele."; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [65] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB1*13:26). RX PubMed=9027974; DOI=10.1111/j.1399-0039.1997.tb02718.x; RA Voorter C.E.M., de Bruyn-Geraets D., Verduyn W., Schreuder G.M.T., RA van den Berg-Loonen E.M.; RT "Identification of a new HLA-DRB1*13 allele (DRB1*1326) with a short RT DRB1*16 sequence."; RL Tissue Antigens 49:88-91(1997). RN [66] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB1*13:45). RX PubMed=12028550; DOI=10.1034/j.1399-0039.2002.590219.x; RA Bengtsson M., Jansson I.E., Danielsson F., Henrysson H., Kallsten K.; RT "Identification of a novel HLA DRB1 exon 2 sequence, DRB1*1345."; RL Tissue Antigens 59:159-161(2002). RN [67] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [68] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [69] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [70] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [71] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [72] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [73] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II (Probable). CC -!- POLYMORPHISM: The following alleles of DRB1-13 are known: CC DRB1*13:01, DRB1*13:02, DRB1*13:03, DRB1*13:04, DRB1*13:05, CC DRB1*13:06, DRB1*13:07, DRB1*13:08, DRB1*13:09, DRB1*13:10, CC DRB1*13:11, DRB1*13:12, DRB1*13:13, DRB1*13:14, DRB1*13:15, CC DRB1*13:16, DRB1*13:17, DRB1*13:18, DRB1*13:19, DRB1*13:20, CC DRB1*13:21, DRB1*13:22, DRB1*13:23, DRB1*13:24, DRB1*13:25, CC DRB1*13:26, DRB1*13:27, DRB1*13:28, DRB1*13:29, DRB1*13:30, CC DRB1*13:31, DRB1*13:32, DRB1*13:33, DRB1*13:34, DRB1*13:35, CC DRB1*13:36, DRB1*13:37, DRB1*13:38, DRB1*13:39, DRB1*13:40, CC DRB1*13:41, DRB1*13:42, DRB1*13:43, DRB1*13:44, DRB1*13:45, CC DRB1*13:46, DRB1*13:47, DRB1*13:48, DRB1*13:49, DRB1*13:50, CC DRB1*13:51, DRB1*13:52, DRB1*13:53, DRB1*13:54, DRB1*13:55, CC DRB1*13:56, DRB1*13:57, DRB1*13:58, DRB1*13:59, DRB1*13:60, CC DRB1*13:61, DRB1*13:62, DRB1*13:63, DRB1*13:64, DRB1*13:65, CC DRB1*13:66, DRB1*13:67, DRB1*13:68, DRB1*13:69, DRB1*13:70, CC DRB1*13:71, DRB1*13:72, DRB1*13:73, DRB1*13:74, DRB1*13:75, CC DRB1*13:76, DRB1*13:77, DRB1*13:78, DRB1*13:79, DRB1*13:80, CC DRB1*13:81, DRB1*13:82, DRB1*13:83, DRB1*13:84, DRB1*13:85, CC DRB1*13:86, DRB1*13:87 and DRB1*13:88. The sequence shown is that CC of DRB1*13:01. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC -!- SEQUENCE CAUTION: CC Sequence=CAB40418.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY663413; AAU88029.1; -; Genomic_DNA. DR EMBL; AY663415; AAU88035.1; -; Genomic_DNA. DR EMBL; AJ697893; CAG27026.1; -; mRNA. DR EMBL; AY961069; AAX63457.1; -; mRNA. DR EMBL; AY961070; AAX63458.2; -; mRNA. DR EMBL; L76133; AAL40069.1; -; mRNA. DR EMBL; AK293020; BAF85709.1; -; mRNA. DR EMBL; BC007920; AAH07920.1; -; mRNA. DR EMBL; L41992; AAA65914.1; -; Genomic_DNA. DR EMBL; U17381; AAC50167.1; -; mRNA. DR EMBL; M59803; AAA64237.1; -; mRNA. DR EMBL; FM196526; CAQ86517.1; -; Genomic_DNA. DR EMBL; AM109988; CAJ33595.1; -; Genomic_DNA. DR EMBL; AM109989; CAJ33596.1; -; Genomic_DNA. DR EMBL; AM109990; CAJ33597.1; -; Genomic_DNA. DR EMBL; AM109991; CAJ33598.1; -; Genomic_DNA. DR EMBL; AM109992; CAJ33599.1; -; Genomic_DNA. DR EMBL; AM109993; CAJ33600.1; -; Genomic_DNA. DR EMBL; AM109994; CAJ33601.1; -; Genomic_DNA. DR EMBL; AM109995; CAJ33602.1; -; Genomic_DNA. DR EMBL; AM109996; CAJ33603.1; -; Genomic_DNA. DR EMBL; AM109997; CAJ33604.1; -; Genomic_DNA. DR EMBL; D29836; BAA06216.1; -; Genomic_DNA. DR EMBL; Z48631; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X86326; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF136155; AAD27646.1; -; Genomic_DNA. DR EMBL; AF164346; AAD47814.1; -; Genomic_DNA. DR EMBL; AF169239; AAD51315.1; -; Genomic_DNA. DR EMBL; AF243537; AAG00414.1; -; Genomic_DNA. DR EMBL; AF243538; AAG00415.1; -; Genomic_DNA. DR EMBL; AF352295; AAK27712.1; -; Genomic_DNA. DR EMBL; AF306862; AAG42258.1; -; Genomic_DNA. DR EMBL; AF247533; AAF99607.1; -; Genomic_DNA. DR EMBL; AY178845; AAO18733.1; -; Genomic_DNA. DR EMBL; AJ555156; CAD87537.1; -; Genomic_DNA. DR EMBL; AY048687; AAL12226.1; -; Genomic_DNA. DR EMBL; AF441789; AAL35834.1; -; Genomic_DNA. DR EMBL; AY765349; AAV35213.1; -; Genomic_DNA. DR EMBL; AJ634529; CAG25408.1; -; Genomic_DNA. DR EMBL; AY963587; AAX51706.1; -; Genomic_DNA. DR EMBL; AM086025; CAJ30431.1; -; Genomic_DNA. DR EMBL; AM494414; CAM36736.1; -; Genomic_DNA. DR EMBL; EF053230; ABK33462.1; -; Genomic_DNA. DR EMBL; AM158254; CAJ43560.1; -; Genomic_DNA. DR EMBL; EF196873; ABM69041.1; -; Genomic_DNA. DR EMBL; AM904556; CAP17407.1; -; Genomic_DNA. DR EMBL; U97554; AAB58309.1; -; Genomic_DNA. DR EMBL; AF048688; AAC05271.1; -; Genomic_DNA. DR EMBL; AF170582; AAD50971.1; -; Genomic_DNA. DR EMBL; AJ245717; CAB53346.1; -; Genomic_DNA. DR EMBL; AJ249591; CAB56840.1; -; Genomic_DNA. DR EMBL; AJ401236; CAB96577.1; -; Genomic_DNA. DR EMBL; AB049459; BAB16298.1; -; Genomic_DNA. DR EMBL; AF305212; AAG22826.1; -; Genomic_DNA. DR EMBL; AJ271206; CAC27122.1; -; Genomic_DNA. DR EMBL; AY178184; AAO21939.1; -; Genomic_DNA. DR EMBL; AY277392; AAP34696.1; -; Genomic_DNA. DR EMBL; AY225520; AAO67727.1; -; Genomic_DNA. DR EMBL; AY259126; AAP21612.1; -; Genomic_DNA. DR EMBL; AB112913; BAD02944.1; -; Genomic_DNA. DR EMBL; AY339247; AAQ18914.1; -; Genomic_DNA. DR EMBL; AY379480; AAQ85128.1; -; Genomic_DNA. DR EMBL; AY502108; AAR89455.1; -; Genomic_DNA. DR EMBL; AJ627565; CAF28889.1; -; Genomic_DNA. DR EMBL; AJ783982; CAH04455.1; -; Genomic_DNA. DR EMBL; AJ853708; CAH68606.1; -; Genomic_DNA. DR EMBL; AM279417; CAK50561.1; -; Genomic_DNA. DR EMBL; EF493833; ABP68561.1; -; Genomic_DNA. DR EMBL; EF493832; ABP68560.1; -; Genomic_DNA. DR EMBL; AM931066; CAP62371.1; -; Genomic_DNA. DR EMBL; DQ473293; ABF18979.1; -; Genomic_DNA. DR EMBL; DQ514602; ABF60565.1; -; Genomic_DNA. DR EMBL; DQ525629; ABF74594.1; -; Genomic_DNA. DR EMBL; EU029803; ABU86862.1; -; Genomic_DNA. DR EMBL; EU071684; ABS87343.1; -; Genomic_DNA. DR EMBL; EU812541; ACE88700.1; -; Genomic_DNA. DR EMBL; EU826130; ACF36162.1; -; Genomic_DNA. DR EMBL; EU826129; ACF36161.1; -; Genomic_DNA. DR EMBL; FJ688163; ACN56340.1; -; Genomic_DNA. DR EMBL; U36827; AAC51629.1; -; Genomic_DNA. DR EMBL; U36825; AAC51628.1; -; Genomic_DNA. DR EMBL; U79025; AAB52235.1; -; Genomic_DNA. DR EMBL; AF499445; AAP68877.1; -; Genomic_DNA. DR EMBL; X93924; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ001254; CAA04628.1; -; Genomic_DNA. DR EMBL; AJ237964; CAB40418.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ488066; CAD32373.1; -; Genomic_DNA. DR EMBL; AY174182; AAO17054.1; -; Genomic_DNA. DR EMBL; AY179366; AAO23237.1; -; Genomic_DNA. DR EMBL; L23534; AAA62591.1; -; Genomic_DNA. DR EMBL; U72264; AAB17276.1; -; Genomic_DNA. DR EMBL; X97407; CAA66060.1; -; Genomic_DNA. DR EMBL; X96396; CAA65260.1; -; Genomic_DNA. DR EMBL; AJ276873; CAB82169.1; -; Genomic_DNA. DR PIR; D25239; D25239. DR PIR; I38899; I38899. DR PIR; I59647; I59647. DR PIR; I72484; I72484. DR PIR; PH0155; PH0155. DR PIR; S03439; S03439. DR UniGene; Hs.485130; -. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q5Y7A7; -. DR SMR; Q5Y7A7; 34-220. DR DMDM; 74757225; -. DR MaxQB; Q5Y7A7; -. DR PRIDE; Q5Y7A7; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR Ensembl; ENST00000415796; ENSP00000412168; ENSG00000206306. DR Ensembl; ENST00000428566; ENSP00000392280; ENSG00000206240. DR GeneCards; GC06M032546; -. DR GeneCards; GC06Mj32477; -. DR GeneCards; GC06Mn32480; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MIM; 142857; gene. DR neXtProt; NX_Q5Y7A7; -. DR HOVERGEN; HBG012730; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-DRB1; human. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 Potential. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-13 beta chain. FT /FTId=PRO_0000392290. FT TRANSMEM 228 248 Helical; (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 146 202 By similarity. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 39 39 Y -> L (in allele DRB1*13:67; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062866. FT VARIANT 40 40 S -> L (in allele DRB1*13:67). FT /FTId=VAR_062867. FT VARIANT 41 41 T -> K (in allele DRB1*13:67). FT /FTId=VAR_062868. FT VARIANT 42 42 S -> G (in allele DRB1*13:17). FT /FTId=VAR_062869. FT VARIANT 45 45 H -> Q (in allele DRB1*13:72). FT /FTId=VAR_062871. FT VARIANT 45 45 H -> Y (in allele DRB1*13:17). FT /FTId=VAR_062870. FT VARIANT 54 54 R -> L (in allele DRB1*13:73). FT /FTId=VAR_062872. FT VARIANT 55 55 F -> Y (in allele DRB1*13:27, allele FT DRB1*13:41 and allele DRB1*13:71). FT /FTId=VAR_062873. FT VARIANT 56 56 L -> Q (in allele DRB1*13:59). FT /FTId=VAR_062874. FT VARIANT 57 57 D -> E (in allele DRB1*13:15, allele FT DRB1*13:19, allele DRB1*13:26, allele FT DRB1*13:53, allele DRB1*13:57, allele FT DRB1*13:85 and allele DRB1*13:86). FT /FTId=VAR_062875. FT VARIANT 61 61 H -> Y (in allele DRB1*13:03, allele FT DRB1*13:07, allele DRB1*13:04, allele FT DRB1*13:11, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:14, allele FT DRB1*13:17, allele DRB1*13:21, allele FT DRB1*13:22, allele DRB1*13:23, allele FT DRB1*13:24, allele DRB1*13:25, allele FT DRB1*13:30, allele DRB1*13:33, allele FT DRB1*13:37, allele DRB1*13:38, allele FT DRB1*13:44, allele DRB1*13:45, allele FT DRB1*13:46, allele DRB1*13:47, allele FT DRB1*13:48, allele DRB1*13:49, allele FT DRB1*13:50, allele DRB1*13:54, allele FT DRB1*13:55, allele DRB1*13:58, allele FT DRB1*13:60, allele DRB1*13:62, allele FT DRB1*13:66, allele DRB1*13:69, allele FT DRB1*13:70, allele DRB1*13:75, allele FT DRB1*13:81, allele DRB1*13:82, allele FT DRB1*13:86 and allele DRB1*13:88). FT /FTId=VAR_062876. FT VARIANT 66 66 N -> D (in allele DRB1*13:62 and allele FT DRB1*13:68). FT /FTId=VAR_062880. FT VARIANT 66 66 N -> F (in allele DRB1*13:08, allele FT DRB1*13:19, allele DRB1*13:57, allele FT DRB1*13:64, allele DRB1*13:72, allele FT DRB1*13:76 and allele DRB1*13:83; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062878. FT VARIANT 66 66 N -> I (in allele DRB1*13:87). FT /FTId=VAR_062881. FT VARIANT 66 66 N -> S (in allele DRB1*13:60 and allele FT DRB1*13:84). FT /FTId=VAR_062879. FT VARIANT 66 66 N -> Y (in allele DRB1*13:03, allele FT DRB1*13:07, allele DRB1*13:04, allele FT DRB1*13:11, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:14, allele FT DRB1*13:17, allele DRB1*13:21, allele FT DRB1*13:22, allele DRB1*13:23, allele FT DRB1*13:24, allele DRB1*13:25, allele FT DRB1*13:30, allele DRB1*13:33, allele FT DRB1*13:37, allele DRB1*13:38, allele FT DRB1*13:44, allele DRB1*13:45, allele FT DRB1*13:46, allele DRB1*13:47, allele FT DRB1*13:48, allele DRB1*13:49, allele FT DRB1*13:52, allele DRB1*13:54, allele FT DRB1*13:55, allele DRB1*13:58, allele FT DRB1*13:66, allele DRB1*13:70, allele FT DRB1*13:75, allele DRB1*13:81, allele FT DRB1*13:82, allele DRB1*13:86 and allele FT DRB1*13:88). FT /FTId=VAR_062877. FT VARIANT 67 67 V -> L (in allele DRB1*13:34, allele FT DRB1*13:62 and allele DRB1*13:64). FT /FTId=VAR_062882. FT VARIANT 76 76 F -> Y (in allele DRB1*13:03, allele FT DRB1*13:07, allele DRB1*13:08, allele FT DRB1*13:12, allele DRB1*13:13, allele FT DRB1*13:19, allele DRB1*13:26, allele FT DRB1*13:32, allele DRB1*13:33, allele FT DRB1*13:36, allele DRB1*13:37, allele FT DRB1*13:38, allele DRB1*13:40, allele FT DRB1*13:47, allele DRB1*13:48, allele FT DRB1*13:49, allele DRB1*13:53, allele FT DRB1*13:55, allele DRB1*13:58, allele FT DRB1*13:60, allele DRB1*13:65, allele FT DRB1*13:70, allele DRB1*13:72, allele FT DRB1*13:76, allele DRB1*13:81, allele FT DRB1*13:84, allele DRB1*13:85 and allele FT DRB1*13:88). FT /FTId=VAR_062883. FT VARIANT 77 77 R -> L (in allele DRB1*13:35). FT /FTId=VAR_062884. FT VARIANT 77 77 R -> W (in allele DRB1*13:80). FT /FTId=VAR_062885. FT VARIANT 79 79 V -> L (in allele DRB1*13:51). FT /FTId=VAR_062886. FT VARIANT 86 86 D -> A (in allele DRB1*13:43 and allele FT DRB1*13:45). FT /FTId=VAR_062889. FT VARIANT 86 86 D -> S (in allele DRB1*13:03, allele FT DRB1*13:04, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:21, allele FT DRB1*13:30, allele DRB1*13:32, allele FT DRB1*13:33, allele DRB1*13:38, allele FT DRB1*13:48, allele DRB1*13:49, allele FT DRB1*13:55, allele DRB1*13:58, allele FT DRB1*13:65, allele DRB1*13:66, allele FT DRB1*13:75, allele DRB1*13:81 and allele FT DRB1*13:88; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062887. FT VARIANT 86 86 D -> V (in allele DRB1*13:31, allele FT DRB1*13:46, allele DRB1*13:54 and allele FT DRB1*13:77). FT /FTId=VAR_062888. FT VARIANT 89 89 Y -> H (in allele DRB1*13:43 and allele FT DRB1*13:45). FT /FTId=VAR_062891. FT VARIANT 89 89 Y -> S (in allele DRB1*13:39, allele FT DRB1*13:54, allele DRB1*13:77, allele FT DRB1*13:78 and allele DRB1*13:79). FT /FTId=VAR_062890. FT VARIANT 96 96 I -> F (in allele DRB1*13:07, allele FT DRB1*13:05, allele DRB1*13:11, allele FT DRB1*13:14, allele DRB1*13:18, allele FT DRB1*13:21, allele DRB1*13:24, allele FT DRB1*13:26, allele DRB1*13:42, allele FT DRB1*13:46, allele DRB1*13:47, allele FT DRB1*13:49, allele DRB1*13:50, allele FT DRB1*13:54, allele DRB1*13:55, allele FT DRB1*13:62, allele DRB1*13:63 and allele FT DRB1*13:75). FT /FTId=VAR_062892. FT VARIANT 96 96 I -> L (in allele DRB1*13:20, allele FT DRB1*13:25, allele DRB1*13:29, allele FT DRB1*13:43, allele DRB1*13:44, allele FT DRB1*13:56, allele DRB1*13:60, allele FT DRB1*13:71, allele DRB1*13:78, allele FT DRB1*13:86 and allele DRB1*13:88). FT /FTId=VAR_062893. FT VARIANT 97 97 L -> R (in allele DRB1*13:74). FT /FTId=VAR_062894. FT VARIANT 99 99 D -> Q (in allele DRB1*13:09, allele FT DRB1*13:44 and allele DRB1*13:86; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062895. FT VARIANT 100 100 E -> A (in allele DRB1*13:09). FT /FTId=VAR_062898. FT VARIANT 100 100 E -> K (in allele DRB1*13:03, allele FT DRB1*13:10, allele DRB1*13:33, allele FT DRB1*13:37, allele DRB1*13:66, allele FT DRB1*13:81, allele DRB1*13:85 and allele FT DRB1*13:88). FT /FTId=VAR_062897. FT VARIANT 100 100 E -> R (in allele DRB1*13:07, allele FT DRB1*13:05, allele DRB1*13:06, allele FT DRB1*13:11, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:14, allele FT DRB1*13:18, allele DRB1*13:21, allele FT DRB1*13:25, allele DRB1*13:26, allele FT DRB1*13:30, allele DRB1*13:42, allele FT DRB1*13:44, allele DRB1*13:46, allele FT DRB1*13:47, allele DRB1*13:49, allele FT DRB1*13:50, allele DRB1*13:55, allele FT DRB1*13:56, allele DRB1*13:58, allele FT DRB1*13:60, allele DRB1*13:62, allele FT DRB1*13:77, allele DRB1*13:82 and allele FT DRB1*13:86; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062896. FT VARIANT 103 103 A -> E (in allele DRB1*13:76). FT /FTId=VAR_062900. FT VARIANT 103 103 A -> L (in allele DRB1*13:13, allele FT DRB1*13:18, allele DRB1*13:47 and allele FT DRB1*13:55; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062899. FT VARIANT 106 106 T -> N (in allele DRB1*13:33 and allele FT DRB1*13:61). FT /FTId=VAR_062901. FT VARIANT 113 113 G -> R (in allele DRB1*13:28). FT /FTId=VAR_062902. FT VARIANT 114 114 V -> A (in allele DRB1*13:58 and allele FT DRB1*13:81). FT /FTId=VAR_062903. FT VARIANT 115 115 V -> D (in allele DRB1*13:16). FT /FTId=VAR_062905. FT VARIANT 115 115 V -> G (in allele DRB1*13:02, allele FT DRB1*13:03, allele DRB1*13:07, allele FT DRB1*13:05, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:14, allele FT DRB1*13:21, allele DRB1*13:23, allele FT DRB1*13:25, allele DRB1*13:26, allele FT DRB1*13:29, allele DRB1*13:30, allele FT DRB1*13:31, allele DRB1*13:33, allele FT DRB1*13:34, allele DRB1*13:36, allele FT DRB1*13:37, allele DRB1*13:38, allele FT DRB1*13:39, allele DRB1*13:41, allele FT DRB1*13:45, allele DRB1*13:46, allele FT DRB1*13:47, allele DRB1*13:49, allele FT DRB1*13:50, allele DRB1*13:55, allele FT DRB1*13:56, allele DRB1*13:60, allele FT DRB1*13:62, allele DRB1*13:63, allele FT DRB1*13:65, allele DRB1*13:66, allele FT DRB1*13:67, allele DRB1*13:73, allele FT DRB1*13:74, allele DRB1*13:82, allele FT DRB1*13:85, allele DRB1*13:86 and allele FT DRB1*13:88). FT /FTId=VAR_062904. FT CONFLICT 104 104 V -> L (in Ref. 46; CAA04628). FT CONFLICT 121 121 Q -> H (in Ref. 25; AAC05271). FT CONFLICT 124 124 V -> G (in Ref. 11; BAA06216). SQ SEQUENCE 266 AA; 30008 MW; 17731F784445CC39 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRFLDRYF HNQEENVRFD SDVGEFRAVT ELGRPDAEYW NSQKDILEDE RAAVDTYCRH NYGVVESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B1E_HUMAN Reviewed; 266 AA. AC Q9GIY3; A0N0W1; A2TGX3; A4ZY86; A5H000; A5HKN8; A7DZP9; A7X5B1; AC A7X5B7; A7X5E0; A7X5E6; A7X5H8; A9JPG0; B1GWE7; B2CR03; B2LVF9; AC B2NJ29; B2ZCY1; B3VTP8; B5B8U0; B5B9V5; B5LZ25; B6VEL9; B9VRA4; AC B9X248; O02876; O46793; O77969; O78210; Q0PQ39; Q155F7; Q1AP33; AC Q1JRP3; Q27PR6; Q27PR7; Q29734; Q29770; Q29772; Q29800; Q2A120; AC Q2HZE5; Q2LE76; Q2MJA6; Q2VQU1; Q307W5; Q31636; Q3LA87; Q3LA88; AC Q3LA89; Q3LA90; Q3LA91; Q3LA92; Q3T919; Q4PRC3; Q4PRC5; Q4VZY7; AC Q56FP1; Q5BM92; Q5U9W6; Q683P7; Q70GL2; Q7YNY9; Q7YQA5; Q860D8; AC Q860D9; Q860S0; Q861H5; Q861H7; Q8MH59; Q8MH60; Q8WLU3; Q95348; AC Q95HK1; Q95HL0; Q95IG2; Q9GIL5; Q9GIL6; Q9GIY0; Q9GIY1; Q9GIY2; AC Q9GJ56; Q9GJ57; Q9GJ58; Q9TPB6; Q9TPW1; Q9XRY4; Q9Y4H7; DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 16-APR-2014, entry version 96. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-14 beta chain; DE AltName: Full=MHC class II antigen DRB1*14; DE Short=DR-14; DE Short=DR14; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*14:05). RX PubMed=12652907; DOI=10.1080/1042517021000041822; RA Kohsaka H., Nasu K., Matsushita S., Miyasaka N.; RT "Complete cDNA coding sequence of the HLA-DRB1*1405 allele."; RL DNA Seq. 13:359-361(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*14:01 AND DRB1*14:04), RP AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-264 (ALLELES DRB1*14:02 AND RP DRB1*14:03). RX PubMed=11972886; DOI=10.1034/j.1399-0039.2002.590116.x; RA Corell A., Cox S.T., Soteriou B., Ramon D., Madrigal J.A., RA Marsh S.G.E.; RT "Complete cDNA sequences of the HLA-DRB1*14011, *1402, *1403 and *1404 RT alleles."; RL Tissue Antigens 59:66-69(2002). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*14:05). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*14:11), AND NUCLEOTIDE RP SEQUENCE [MRNA] OF 1-265 (ALLELE DRB1*14:46). RX PubMed=17174751; DOI=10.1016/j.humimm.2006.09.002; RA Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P., RA de Pablo R., Garcia-Sanchez F., Vicario J.L.; RT "Group-specific amplification of cDNA from DRB1 genes. Complete coding RT sequences of partially defined alleles and identification of the new RT alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113."; RL Hum. Immunol. 67:1008-1016(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217 (ALLELE DRB1*14:57). RX PubMed=17026471; DOI=10.1111/j.1399-0039.2006.00669.x; RA Chen Q., Zou H., Xu X.H., Luo M., Wang J., Zuo Y.Q., Chen Y.H., RA Chen X.H., Chen X.L., Yao Z.Q., Song N., Zeng J., Mi X.Y., Sun S.X., RA Wang J.X., Zhao T.M.; RT "Characterization of HLA-B*5516, -B*1313, -B*9512, and -DRB1*1457 RT alleles identified in a southwest Chinese population."; RL Tissue Antigens 68:339-343(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208 (ALLELE DRB1*14:54). RX PubMed=19284446; DOI=10.1111/j.1744-313X.2008.00826.x; RA Yang K.L., Chen M.J., Lee S.K., Lin C.C., Tsai M.J., Chiu H.M., RA Jiang S., Chao Y.C., Chen S.P., Lin S., Shyr M.H., Lin P.Y.; RT "New allele name of some HLA-DRB1*1401: HLA-DRB1*1454."; RL Int. J. Immunogenet. 36:119-120(2009). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-123 (ALLELE DRB1*14:19). RX PubMed=8560458; DOI=10.1111/j.1399-0039.1995.tb02506.x; RA Loeffler D., Woelpl A., Kern P., Eiermann T.H.; RT "A novel HLA-DR allele, DRB1*1419."; RL Tissue Antigens 46:343-344(1995). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB1*14:82). RA Ogrzewalla K., Tillmann G., Scheibelhut N., Lauber J., Enczmann J.; RT "A novel HLA-DRB1*14 allele identified by sequence-based typing."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-216 (ALLELES DRB1*14:06; RP DRB1*14:07; DRB1*14:10; DRB1*14:13; DRB1*14:14 AND DRB1*14:21). RC TISSUE=Peripheral blood; RX PubMed=17767557; DOI=10.1111/j.1399-0039.2007.00918.x; RA Horn P.A., Albis-Camps M., Verboom M., Bunce M., Yousaf K., RA Williams S., Blasczyk R.; RT "The nature of diversity of HLA-DRB1 exon 3."; RL Tissue Antigens 70:335-337(2007). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-124 (ALLELE DRB1*14:85). RA Maruya E., Matsushita M., Saji H., Ounuma T., Futagami T., Kojima H., RA Tujino T., Hayashi K., Kusunoki Y., Yoshida T., Maekawajiri S.; RT "HLA-DR new allele related with DRB1*1403."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:22). RX PubMed=8575830; DOI=10.1007/s002510050058; RA Adami N., Aubert V., Jeannet M., Tiercy J.M.; RT "Sequencing of a new HLA-DR14 allele (DRB1(*)1422)."; RL Immunogenetics 43:248-249(1996). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:36). RX PubMed=10321590; DOI=10.1034/j.1399-0039.1999.530421.x; RA Bodmer J., Marsh S., Albert E., Bodmer W.; RT "Nomenclature for factors of the HLA system, 1998."; RL Tissue Antigens 53:407-446(1999). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:37). RC TISSUE=Blood; RX PubMed=11380954; DOI=10.1034/j.1399-0039.2001.057004384.x; RA Wu S., Shiao Y.M., Lai C.Y., Lai S.M., Chen S.P., Sidebottom D.A., RA Hildebrand W.H., Tilanus M.G.J., Chou F.C., Tsai M.F.; RT "Polymorphism of human HLA-DRB1 antigens generated by genetic exchange RT between DR2 (DRB1*15011) and DR6 (DRB1*1405) alleles: a novel DRB1 RT allele (DRB1*1437) identified in a Paiwan tribe member of Taiwan."; RL Tissue Antigens 57:384-387(2001). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:41), AND RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-123 (ALLELE DRB1*14:42). RX PubMed=12144619; DOI=10.1034/j.1399-0039.2002.590502.x; RA Gans C.P., Tang T.F., Slack R., Ng J., Hartzman R.J., Hurley C.K.; RT "DRB1*14 diversity and DRB3 associations in four major population RT groups in the United States."; RL Tissue Antigens 59:364-369(2002). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:43). RX PubMed=15304015; DOI=10.1111/j.0001-2815.2004.00275.x; RA Chu C.C., Lee H.L., Hsieh N.K., Trejaut J., Lin M.; RT "Two novel HLA-DRB1 alleles identified using a sequence-based typing: RT HLA-DRB1*1443 and HLA-DRB1*1351*."; RL Tissue Antigens 64:308-310(2004). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*14:47 AND RP DRB1*14:48). RX PubMed=16185331; DOI=10.1111/j.1399-0039.2005.00459.x; RA Lazaro A.M., Steiner N.K., Moraes M.E., Moraes J.R., Ng J., RA Hartzman R.J., Hurley C.K.; RT "Ten novel HLA-DRB1 alleles and one novel DRB3 allele."; RL Tissue Antigens 66:327-329(2005). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:50). RC TISSUE=Peripheral blood; RX PubMed=16185333; DOI=10.1111/j.1399-0039.2005.00472a.x; RA Tijssen H.J., Zeeuw van der S.C., Joosten I.; RT "Exon 2 sequence analysis of a novel HLA-DRB1 allele, DRB1*1450."; RL Tissue Antigens 66:332-333(2005). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:49). RX PubMed=16426240; DOI=10.1111/j.1744-313X.2005.00557.x; RA Miao K.R., Xue M., Zhou X.Y., Xu R., Fei X.M., Pan Q.Q., Zhang J.W., RA Zhao X., Fan S., Kukuruga D., Xu A.L., Wang C.Y.; RT "Characterization of a novel DRB1*14 allele (DRB1*1449) in the Han- RT Chinese population."; RL Int. J. Immunogenet. 33:33-35(2006). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:56). RX PubMed=16774552; DOI=10.1111/j.1399-0039.2006.00612.x; RA Baek J.Y., Yun H.S., Hur S.S., Kwon O.J., Kwack K.; RT "Identification of a novel HLA-DRB1*14 allele, DRB1*1456, in the cord RT blood of a Korean baby."; RL Tissue Antigens 68:97-98(2006). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:60). RC TISSUE=Peripheral blood; RX PubMed=17026474; DOI=10.1111/j.1399-0039.2006.00675.x; RA Tijssen H.J., van den Dungen-Toet J.H.G., van Houwelingen K.P., RA Allebes W.A., Joosten I.; RT "Exon 2 sequence analysis of a novel HLA-DRB1 allele, DRB1*1460."; RL Tissue Antigens 68:346-347(2006). RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:65). RX PubMed=17498272; DOI=10.1111/j.1399-0039.2007.00835.x; RA Abdeen H., McErlean C., Moraes M.E., Torres M., Campiotto S., RA Galvao S., Gouvea C., Middleton D.; RT "Identification of three novel alleles of HLA-DRB1 and HLA-A in the RT Brazilian population."; RL Tissue Antigens 69:607-610(2007). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:74). RX PubMed=18179646; DOI=10.1111/j.1399-0039.2007.00993.x; RA Rahal M., Kervaire B., Villard J., Tiercy J.M.; RT "DNA typing by microbead arrays and PCR-SSP: apparent false-negative RT or -positive hybridization or amplification signals disclose new HLA-B RT and -DRB1 alleles."; RL Tissue Antigens 71:238-241(2008). RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:67). RC TISSUE=Blood; RX PubMed=18643964; DOI=10.1111/j.1399-0039.2008.01089.x; RA Yan L.N., Li S.Y., Dong Z., Dong L., Xie J.H., An S.P., Yuan Y.H.; RT "Sequence-based typing reveals the novel HLA-DRB1*1467 allele in a RT Chinese individual."; RL Tissue Antigens 72:409-410(2008). RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:75). RX PubMed=18937796; DOI=10.1111/j.1399-0039.2008.01116.x; RA Schuett S., Geflitter A., von Baehr V.; RT "Sequence-based typing of a novel HLA-DRB1*14 allele, DRB1*1475, in a RT Caucasian woman."; RL Tissue Antigens 72:501-502(2008). RN [25] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:61). RX PubMed=19000132; DOI=10.1111/j.1399-0039.2008.01135.x; RA Wang Z., Shan X., Zhang Z.; RT "Identification of a novel HLA-DRB allele, HLA-DRB1*1461."; RL Tissue Antigens 72:603-604(2008). RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:78). RX PubMed=19140840; DOI=10.1111/j.1399-0039.2008.01175.x; RA Han S.H., Jung S.M., Park S.R., Chung S.Y., Han H.; RT "Identification of a new HLA-DRB1*14 variant, HLA-DRB1*1478, in a RT Korean individual."; RL Tissue Antigens 73:81-83(2009). RN [27] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*14:26; RP DRB1*14:27 AND DRB1*14:29). RA Kashiwase K., Tokunaga K., Akaza T., Tadokoro K., Juji T.; RT "Sequence of new allele."; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [28] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:32). RA Blasczyk R.; RT "A new HLA-DRB1*14 variant."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [29] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:34). RA Whidborne R.S., Sayer D.C., Christiansen F.T.; RT "Novel DRB1*14 and 15 alleles in the Western Australian population."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [30] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:17). RA Gervais T.G., Latinne D.; RT "Confirmatory sequence for HLA-DRB1*1417 gene obtained by sequence RT based typing."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [31] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:18). RA Rizzo M., Steiner N.K., Nichol L., Hurley C.K.; RT "Complete exon 2 sequence for HLA-DRB1*1418."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [32] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:15). RA Kervaire B., Villard J., Tiercy J.M.; RT "An unusual HLA-DR/DQ haplotype carrying a new DR8 variant and the RT DRB3*0202 allele."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [33] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:23). RC TISSUE=Blood; RA Velickovic Z.M.; RT "Novel HLA-DRB1*11 allele."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [34] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:12). RA Oh H.B., Byun E.K., Hong S.A., Lee M.N., Kwon O.J.; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [35] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:01). RA Lee T.D.; RT "Identification of a novel HLA-DRB1*14 allele."; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [36] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:53). RA Dormoy A.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [37] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:55). RC TISSUE=Leukocyte; RA Hirv K., Krauss A., Mytilineos J.; RT "Characterization of a new HLA-DRB1*14 allele."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [38] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:58). RA Karvunidis T., Jindra P., Fischer G., Koza V.; RT "Identification of a new HLA-DRB1*14 allele by sequence-based RT typing."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [39] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:59). RA Dormoy A., Weschler B., Leinsenbach R.; RT "A new DRB1*14 allele close to the DRB1*1418 allele is different for 3 RT substitutions at nucleotide positions 84, 152 and 174 leading to the RT change of 2 amino acids at positions 28 and 51."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [40] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:63). RA Ye S., Liu M., Qi J.; RT "Identification a novel HLA-DRB1*14 new allele."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [41] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:30). RA Greville W.D., Dunckley H.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [42] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:76). RC TISSUE=Blood; RA Tavoularis S., Rebeiro E., Sayer D.; RT "Identification of a novel DRB1 allele."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [43] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:77). RC TISSUE=Blood; RA Yan L.N., An S.P., Li S.Y., Xie J.H., Dong L., Dong Z., Yuan Y.H.; RT "A new allele of HLA-DRB1*14 detected with SBT."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [44] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*14:38; RP DRB1*14:39; DRB1*14:40; DRB1*14:44; DRB1*14:45 AND DRB1*14:80). RA Juji T., Shimizu M., Kashiwase K., Nakajima F., Tadokoro K., RA Tanaka H.; RT "HLA-DRB1*1401V1M, HLA-DRB1*1401V2, HLA-DRB1*1403V2, HLA-DRB1*1405V1, RT HLA-DRB1*1405V2, HLA-DRB1*1406V1."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [45] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*14:51; RP DRB1*14:52; DRB1*14:62; DRB1*14:64; DRB1*14:68; DRB1*14:69; RP DRB1*14:70; DRB1*14:71; DRB1*14:72; DRB1*14:73; DRB1*14:79; DRB1*14:81 RP AND DRB1*14:83). RA Lazaro A.M., Cao K., Xiao Y., Lebeck L., Hurley C.K.; RT "Novel class II allele."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [46] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:24). RA Dormoy A., Weschler B.; RT "The HLA-DRB1*14New allele has 3 nucleotide changes from the DRB1*1402 RT allele at positions 286, 298 and 299 of exon 2 where: C286->A286 RT (codon 72 (CTC->ATC)) resulting in a change of amino acid: Leu->Ile RT A298->G298 + G299->C299 (codon 76 (AGG->GCG)) resulting in a change of RT amino acid: Arg->Ala."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [47] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:84). RC TISSUE=Peripheral blood; RA Lee T.-D., Chien W.-C.; RT "A new DR14-related DRB1 allele, identified by sequence-based RT typing."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [48] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB1*14:35). RX PubMed=11532019; DOI=10.1046/j.1365-2370.2001.00243.x; RA Trejaut J., Kennedy A., Hobart D., Le T., Greville W.D., Ng G., RA Taverniti A., Dunckley H.; RT "PCR-RFLP typing detects new HLA-DRB1 alleles: DRB1*13022, DRB1*1336 RT and DRB1*1435."; RL Eur. J. Immunogenet. 28:441-447(2001). RN [49] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB1*14:28). RC TISSUE=Blood; RX PubMed=9243765; DOI=10.1111/j.1399-0039.1997.tb02843.x; RA Hashemi-Tavoularis S., Couture C., Buyse I.M.; RT "Identification of new DRB1*01 (DRB1*01022), DRB1*14 (DRB1*1428) and RT DRB3* (DRB3*0206) alleles."; RL Tissue Antigens 50:89-93(1997). RN [50] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB1*14:01). RC TISSUE=Peripheral blood; RX PubMed=15104685; DOI=10.1111/j.0001-2815.2004.00186.x; RA Tavoularis S., Couture C., Ribeiro-Barros E.; RT "Identification of three novel alleles: DRB3*0110, DRB1*1140, and RT DRB1*140102."; RL Tissue Antigens 63:496-500(2004). RN [51] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELES DRB1*14:09 AND RP DRB1*14:25). RA Vayntrub T., Lo B.; RT "Confirmatory sequence of HLA class II DRB1*1409 and DRB1*1425."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [52] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-122 (ALLELE DRB1*14:08). RC TISSUE=Blood; RX PubMed=1644450; DOI=10.1007/BF00215663; RA Gao X., Veale A., Serjeantson S.W.; RT "HLA class II diversity in Australian aborigines: unusual HLA-DRB1 RT alleles."; RL Immunogenetics 36:333-337(1992). RN [53] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-119 (ALLELE DRB1*14:31). RX PubMed=10599892; DOI=10.1034/j.1399-0039.1999.540510.x; RA Panigoro R., Greville W.D., Kennedy A., Trejaut J., Dunckley H.; RT "New HLA class II alleles in the Indonesian population."; RL Tissue Antigens 54:521-523(1999). RN [54] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-122 (ALLELE DRB1*14:33). RA Greville W.D., van Eijck A., Dunckley H.; RT "New HLA class II (DRB1) alleles detected by sequencing-based RT typing."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [55] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB1*14:20). RX PubMed=8883296; DOI=10.1111/j.1399-0039.1996.tb02611.x; RA Verduyn W., Anholts J.D., Versluis L.F., Parlevliet J., Drabbels J., RA De Meester J., Tilanus M.G., Doxiadis I.I., Giphart M.J., RA Schreuder G.M.; RT "Six newly identified HLA-DRB alleles: DRB1*1121, *1419, *1420, *1421, RT DRB3*0203 and DRB5*0103."; RL Tissue Antigens 48:80-86(1996). RN [56] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-131 (ALLELE DRB1*14:24). RC TISSUE=B-cell; RA Hurley C.K.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [57] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-120 (ALLELE DRB1*14:16). RA Gervais T.G., Latinne D.; RT "Confirmatory typing for exon 2 of HLA-DRB1*1416 gene, obtained by RT sequence-based typing."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [58] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [59] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [60] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [61] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [62] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [63] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [64] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II (Probable). CC -!- POLYMORPHISM: The following alleles of DRB1-14 are known: CC DRB1*14:01, DRB1*14:02, DRB1*14:03, DRB1*14:04, DRB1*14:05, CC DRB1*14:06, DRB1*14:07, DRB1*14:08, DRB1*14:09, DRB1*14:10, CC DRB1*14:11, DRB1*14:12, DRB1*14:13, DRB1*14:14, DRB1*14:15, CC DRB1*14:16, DRB1*14:17, DRB1*14:18, DRB1*14:19, DRB1*14:20, CC DRB1*14:21, DRB1*14:22, DRB1*14:23, DRB1*14:24, DRB1*14:25, CC DRB1*14:26, DRB1*14:27, DRB1*14:28, DRB1*14:29, DRB1*14:30, CC DRB1*14:31, DRB1*14:32, DRB1*14:33, DRB1*14:34, DRB1*14:35, CC DRB1*14:36, DRB1*14:37, DRB1*14:38, DRB1*14:39, DRB1*14:40, CC DRB1*14:41, DRB1*14:42, DRB1*14:43, DRB1*14:44, DRB1*14:45, CC DRB1*14:46, DRB1*14:47, DRB1*14:48, DRB1*14:49, DRB1*14:50, CC DRB1*14:51, DRB1*14:52, DRB1*14:53, DRB1*14:54, DRB1*14:55, CC DRB1*14:56, DRB1*14:57, DRB1*14:58, DRB1*14:59, DRB1*14:60, CC DRB1*14:61, DRB1*14:62, DRB1*14:63, DRB1*14:64, DRB1*14:65, CC DRB1*14:67, DRB1*14:68, DRB1*14:69, DRB1*14:70, DRB1*14:71, CC DRB1*14:72, DRB1*14:73, DRB1*14:74, DRB1*14:75, DRB1*14:76, CC DRB1*14:77, DRB1*14:78, DRB1*14:79, DRB1*14:80, DRB1*14:81, CC DRB1*14:82, DRB1*14:83, DRB1*14:84 and DRB1*14:85. The sequence CC shown is that of DRB1*14:01. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC -!- SEQUENCE CAUTION: CC Sequence=CAB45249.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB062112; BAB84521.2; -; mRNA. DR EMBL; AJ297582; CAC08822.1; -; mRNA. DR EMBL; AJ297583; CAC08823.1; -; mRNA. DR EMBL; AJ297584; CAC08824.1; -; mRNA. DR EMBL; AJ297585; CAC08825.1; -; mRNA. DR EMBL; AY663408; AAU88014.1; -; Genomic_DNA. DR EMBL; AY935719; AAX33315.1; -; mRNA. DR EMBL; AY961071; AAX63459.2; -; mRNA. DR EMBL; DQ235685; ABB52004.1; -; Genomic_DNA. DR EMBL; DQ390459; ABD60300.1; -; Genomic_DNA. DR EMBL; DQ390460; ABD60301.1; -; Genomic_DNA. DR EMBL; FJ379259; ACJ06537.1; -; Genomic_DNA. DR EMBL; Z38072; CAA86217.1; -; Genomic_DNA. DR EMBL; FM196525; CAQ86516.1; -; Genomic_DNA. DR EMBL; AM109998; CAJ33605.1; -; Genomic_DNA. DR EMBL; AM109999; CAJ33606.1; -; Genomic_DNA. DR EMBL; AM110000; CAJ33607.1; -; Genomic_DNA. DR EMBL; AM110001; CAJ33608.1; -; Genomic_DNA. DR EMBL; AM110002; CAJ33609.1; -; Genomic_DNA. DR EMBL; AM110003; CAJ33610.1; -; Genomic_DNA. DR EMBL; AB485773; BAH23562.1; -; Genomic_DNA. DR EMBL; Z50730; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ242985; CAB45249.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ251985; CAC19086.1; -; Genomic_DNA. DR EMBL; AY050186; AAL23547.1; -; Genomic_DNA. DR EMBL; AY054375; AAL15169.1; -; mRNA. DR EMBL; AF400066; AAK85431.1; -; Genomic_DNA. DR EMBL; AY267905; AAP32696.1; -; Genomic_DNA. DR EMBL; AY267906; AAP32697.1; -; Genomic_DNA. DR EMBL; AJ969417; CAI94542.1; -; Genomic_DNA. DR EMBL; AY912075; AAY17288.1; -; Genomic_DNA. DR EMBL; DQ333353; ABC59115.1; -; Genomic_DNA. DR EMBL; AM259285; CAJ90660.1; -; Genomic_DNA. DR EMBL; EF199810; ABM90423.1; -; Genomic_DNA. DR EMBL; AM774161; CAO81738.1; -; Genomic_DNA. DR EMBL; EF495154; ABP38039.1; -; Genomic_DNA. DR EMBL; AM922324; CAP58300.1; -; Genomic_DNA. DR EMBL; DQ494324; ABF50050.1; -; Genomic_DNA. DR EMBL; EU588391; ACB97664.1; -; Genomic_DNA. DR EMBL; D86502; BAA13097.1; -; Genomic_DNA. DR EMBL; D86504; BAA13099.1; -; Genomic_DNA. DR EMBL; D88310; BAA13587.1; -; Genomic_DNA. DR EMBL; AJ010982; CAA09450.1; -; Genomic_DNA. DR EMBL; AF172071; AAD51970.1; -; Genomic_DNA. DR EMBL; AJ543433; CAD65908.1; -; Genomic_DNA. DR EMBL; AY277390; AAP34694.1; -; Genomic_DNA. DR EMBL; AJ581744; CAE46451.1; -; Genomic_DNA. DR EMBL; AJ812566; CAH23708.1; -; Genomic_DNA. DR EMBL; AY770520; AAV37191.1; -; Genomic_DNA. DR EMBL; DQ021915; AAY85747.1; -; Genomic_DNA. DR EMBL; AM084908; CAJ29895.1; -; Genomic_DNA. DR EMBL; DQ327711; ABC59293.1; -; Genomic_DNA. DR EMBL; DQ358688; ABC84557.1; -; Genomic_DNA. DR EMBL; AM233907; CAJ80873.1; -; Genomic_DNA. DR EMBL; DQ643390; ABG25965.1; -; Genomic_DNA. DR EMBL; U95115; AAB58397.2; -; Genomic_DNA. DR EMBL; AM933133; CAP69806.1; -; Genomic_DNA. DR EMBL; EU545181; ACB30275.1; -; Genomic_DNA. DR EMBL; AB049830; BAB16682.1; -; Genomic_DNA. DR EMBL; AB049831; BAB16683.1; -; Genomic_DNA. DR EMBL; AB049832; BAB16684.1; -; Genomic_DNA. DR EMBL; AB087875; BAC02938.1; -; Genomic_DNA. DR EMBL; AB087876; BAC02939.1; -; Genomic_DNA. DR EMBL; AB436778; BAG32234.1; -; Genomic_DNA. DR EMBL; EF078986; ABK56696.1; -; Genomic_DNA. DR EMBL; EF536016; ABQ08747.1; -; Genomic_DNA. DR EMBL; EU029787; ABU86846.1; -; Genomic_DNA. DR EMBL; EU029788; ABU86847.1; -; Genomic_DNA. DR EMBL; EU029792; ABU86851.1; -; Genomic_DNA. DR EMBL; EU029793; ABU86852.1; -; Genomic_DNA. DR EMBL; EU029798; ABU86857.1; -; Genomic_DNA. DR EMBL; EU643616; ACD01094.1; -; Genomic_DNA. DR EMBL; EU812536; ACE88696.1; -; Genomic_DNA. DR EMBL; EU924810; ACH57405.1; -; Genomic_DNA. DR EMBL; DQ060439; AAY59541.1; -; Genomic_DNA. DR EMBL; DQ060441; AAY59543.1; -; Genomic_DNA. DR EMBL; DQ782331; ABG91054.1; -; Genomic_DNA. DR EMBL; FM179681; CAQ77159.1; -; Genomic_DNA. DR EMBL; FJ594768; ACM47962.1; -; Genomic_DNA. DR EMBL; AF177215; AAD53910.1; -; Genomic_DNA. DR EMBL; X99839; CAA68150.1; -; Genomic_DNA. DR EMBL; AJ289123; CAC19015.1; -; Genomic_DNA. DR EMBL; AY174092; AAO20089.1; -; Genomic_DNA. DR EMBL; AY174181; AAO17053.1; -; Genomic_DNA. DR EMBL; M77673; AAA73131.1; -; Genomic_DNA. DR EMBL; AF028010; AAB94612.1; -; Genomic_DNA. DR EMBL; AF112879; AAD29584.1; -; Genomic_DNA. DR EMBL; X86974; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U41489; AAA86242.1; -; Genomic_DNA. DR EMBL; AJ508388; CAD48196.1; -; Genomic_DNA. DR PIR; B33287; B33287. DR PIR; C33287; C33287. DR PIR; C60748; C60748. DR PIR; F60748; F60748. DR PIR; PH0157; PH0157. DR PIR; PH0158; PH0158. DR PIR; S03440; S03440. DR UniGene; Hs.485130; -. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q9GIY3; -. DR SMR; Q9GIY3; 34-220. DR IntAct; Q9GIY3; 1. DR DMDM; 74761361; -. DR PRIDE; Q9GIY3; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR Ensembl; ENST00000412634; ENSP00000408795; ENSG00000228080. DR Ensembl; ENST00000415796; ENSP00000412168; ENSG00000206306. DR Ensembl; ENST00000419393; ENSP00000403458; ENSG00000228080. DR Ensembl; ENST00000428566; ENSP00000392280; ENSG00000206240. DR GeneCards; GC06M032546; -. DR GeneCards; GC06Mj32477; -. DR GeneCards; GC06Mn32480; -. DR GeneCards; GC06Mo32593; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; CAB015400; -. DR HPA; CAB034021; -. DR MIM; 142857; gene. DR neXtProt; NX_Q9GIY3; -. DR HOVERGEN; HBG012730; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-DRB1; human. DR ArrayExpress; Q9GIY3; -. DR Bgee; Q9GIY3; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 Potential. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-14 beta chain. FT /FTId=PRO_5000066676. FT TRANSMEM 228 248 Helical; (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 146 202 By similarity. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 39 39 Y -> L (in allele DRB1*14:46; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062907. FT VARIANT 39 39 Y -> Q (in allele DRB1*14:10 and allele FT DRB1*14:57; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062906. FT VARIANT 40 40 S -> P (in allele DRB1*14:39). FT /FTId=VAR_062910. FT VARIANT 40 40 S -> R (in allele DRB1*14:46). FT /FTId=VAR_062908. FT VARIANT 40 40 S -> V (in allele DRB1*14:10 and allele FT DRB1*14:57; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062909. FT VARIANT 41 41 T -> K (in allele DRB1*14:10, allele FT DRB1*14:46 and allele DRB1*14:57). FT /FTId=VAR_062911. FT VARIANT 42 42 S -> G (in allele DRB1*14:04, allele FT DRB1*14:11, allele DRB1*14:15, allele FT DRB1*14:28, allele DRB1*14:31, allele FT DRB1*14:50, allele DRB1*14:52, allele FT DRB1*14:61, allele DRB1*14:68, allele FT DRB1*14:71, allele DRB1*14:73, allele FT DRB1*14:76 and allele DRB1*14:79). FT /FTId=VAR_062913. FT VARIANT 42 42 S -> H (in allele DRB1*14:10 and allele FT DRB1*14:57; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062912. FT VARIANT 45 45 H -> Q (in allele DRB1*14:05, allele FT DRB1*14:37, allele DRB1*14:43, allele FT DRB1*14:44, allele DRB1*14:45, allele FT DRB1*14:56 and allele DRB1*14:84). FT /FTId=VAR_062915. FT VARIANT 45 45 H -> Y (in allele DRB1*14:04, allele FT DRB1*14:11, allele DRB1*14:15, allele FT DRB1*14:28, allele DRB1*14:31, allele FT DRB1*14:50, allele DRB1*14:52, allele FT DRB1*14:68, allele DRB1*14:71, allele FT DRB1*14:73, allele DRB1*14:76 and allele FT DRB1*14:79). FT /FTId=VAR_062914. FT VARIANT 54 54 R -> Q (in allele DRB1*14:26). FT /FTId=VAR_062916. FT VARIANT 55 55 F -> Y (in allele DRB1*14:82). FT /FTId=VAR_062917. FT VARIANT 56 56 L -> M (in allele DRB1*14:83). FT /FTId=VAR_062918. FT VARIANT 57 57 D -> E (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:06, allele FT DRB1*14:12, allele DRB1*14:13, allele FT DRB1*14:18, allele DRB1*14:19, allele FT DRB1*14:20, allele DRB1*14:24, allele FT DRB1*14:27, allele DRB1*14:29, allele FT DRB1*14:40, allele DRB1*14:41, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:48, allele DRB1*14:49, allele FT DRB1*14:51, allele DRB1*14:52, allele FT DRB1*14:63, allele DRB1*14:67, allele FT DRB1*14:77, allele DRB1*14:78, allele FT DRB1*14:81, allele DRB1*14:83 and allele FT DRB1*14:85). FT /FTId=VAR_062919. FT VARIANT 59 59 Y -> H (in allele DRB1*14:70). FT /FTId=VAR_062920. FT VARIANT 61 61 H -> Y (in allele DRB1*14:25, allele FT DRB1*14:42, allele DRB1*14:53, allele FT DRB1*14:58 and allele DRB1*14:69). FT /FTId=VAR_062921. FT VARIANT 66 66 F -> N (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:06, allele FT DRB1*14:09, allele DRB1*14:12, allele FT DRB1*14:13, allele DRB1*14:17, allele FT DRB1*14:18, allele DRB1*14:19, allele FT DRB1*14:21, allele DRB1*14:24, allele FT DRB1*14:27, allele DRB1*14:29, allele FT DRB1*14:30, allele DRB1*14:33, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:48, allele DRB1*14:51, allele FT DRB1*14:52, allele DRB1*14:59, allele FT DRB1*14:63, allele DRB1*14:64, allele FT DRB1*14:67, allele DRB1*14:78, allele FT DRB1*14:80, allele DRB1*14:81, allele FT DRB1*14:83 and allele DRB1*14:85; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062923. FT VARIANT 66 66 F -> Y (in allele DRB1*14:25, allele FT DRB1*14:42, allele DRB1*14:53, allele FT DRB1*14:58 and allele DRB1*14:69). FT /FTId=VAR_062922. FT VARIANT 67 67 V -> L (in allele DRB1*14:41 and allele FT DRB1*14:77). FT /FTId=VAR_062924. FT VARIANT 74 74 G -> R (in allele DRB1*14:36 and allele FT DRB1*14:60). FT /FTId=VAR_062925. FT VARIANT 76 76 Y -> F (in allele DRB1*14:17, allele FT DRB1*14:21, allele DRB1*14:30, allele FT DRB1*14:33, allele DRB1*14:35, allele FT DRB1*14:42, allele DRB1*14:53, allele FT DRB1*14:64, allele DRB1*14:65 and allele FT DRB1*14:72). FT /FTId=VAR_062926. FT VARIANT 80 80 T -> R (in allele DRB1*14:59). FT /FTId=VAR_062927. FT VARIANT 86 86 A -> D (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:05, allele FT DRB1*14:06, allele DRB1*14:08, allele FT DRB1*14:09, allele DRB1*14:11, allele FT DRB1*14:12, allele DRB1*14:14, allele FT DRB1*14:15, allele DRB1*14:17, allele FT DRB1*14:18, allele DRB1*14:19, allele FT DRB1*14:20, allele DRB1*14:21, allele FT DRB1*14:23, allele DRB1*14:24, allele FT DRB1*14:27, allele DRB1*14:29, allele FT DRB1*14:30, allele DRB1*14:33, allele FT DRB1*14:34, allele DRB1*14:36, allele FT DRB1*14:37, allele DRB1*14:40, allele FT DRB1*14:41, allele DRB1*14:42, allele FT DRB1*14:43, allele DRB1*14:44, allele FT DRB1*14:45, allele DRB1*14:46, allele FT DRB1*14:47, allele DRB1*14:51, allele FT DRB1*14:52, allele DRB1*14:56, allele FT DRB1*14:59, allele DRB1*14:64, allele FT DRB1*14:67, allele DRB1*14:72, allele FT DRB1*14:77, allele DRB1*14:80, allele FT DRB1*14:81, allele DRB1*14:83 and allele FT DRB1*14:84). FT /FTId=VAR_062928. FT VARIANT 86 86 A -> S (in allele DRB1*14:13, allele FT DRB1*14:63, allele DRB1*14:65, allele FT DRB1*14:78 and allele DRB1*14:85). FT /FTId=VAR_062929. FT VARIANT 86 86 A -> T (in allele DRB1*14:62). FT /FTId=VAR_062930. FT VARIANT 86 86 A -> V (in allele DRB1*14:48). FT /FTId=VAR_062931. FT VARIANT 87 87 A -> E (in allele DRB1*14:11). FT /FTId=VAR_062932. FT VARIANT 89 89 H -> S (in allele DRB1*14:48 and allele FT DRB1*14:64; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062934. FT VARIANT 89 89 H -> Y (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:05, allele FT DRB1*14:06, allele DRB1*14:09, allele FT DRB1*14:11, allele DRB1*14:12, allele FT DRB1*14:13, allele DRB1*14:14, allele FT DRB1*14:15, allele DRB1*14:17, allele FT DRB1*14:18, allele DRB1*14:19, allele FT DRB1*14:20, allele DRB1*14:21, allele FT DRB1*14:23, allele DRB1*14:24, allele FT DRB1*14:27, allele DRB1*14:29, allele FT DRB1*14:30, allele DRB1*14:33, allele FT DRB1*14:36, allele DRB1*14:37, allele FT DRB1*14:40, allele DRB1*14:41, allele FT DRB1*14:42, allele DRB1*14:43, allele FT DRB1*14:44, allele DRB1*14:45, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:51, allele DRB1*14:52, allele FT DRB1*14:56, allele DRB1*14:57, allele FT DRB1*14:59, allele DRB1*14:63, allele FT DRB1*14:65, allele DRB1*14:67, allele FT DRB1*14:76, allele DRB1*14:77, allele FT DRB1*14:78, allele DRB1*14:80, allele FT DRB1*14:81, allele DRB1*14:83, allele FT DRB1*14:84 and allele DRB1*14:85). FT /FTId=VAR_062933. FT VARIANT 96 96 L -> F (in allele DRB1*14:15, allele FT DRB1*14:22, allele DRB1*14:25, allele FT DRB1*14:27, allele DRB1*14:53 and allele FT DRB1*14:73). FT /FTId=VAR_062935. FT VARIANT 96 96 L -> I (in allele DRB1*14:16, allele FT DRB1*14:24, allele DRB1*14:37, allele FT DRB1*14:45, allele DRB1*14:57, allele FT DRB1*14:63, allele DRB1*14:67 and allele FT DRB1*14:78). FT /FTId=VAR_062936. FT VARIANT 99 99 R -> D (in allele DRB1*14:03, allele FT DRB1*14:12, allele DRB1*14:15, allele FT DRB1*14:16, allele DRB1*14:22, allele FT DRB1*14:25, allele DRB1*14:27, allele FT DRB1*14:40, allele DRB1*14:53, allele FT DRB1*14:57, allele DRB1*14:63, allele FT DRB1*14:67, allele DRB1*14:69, allele FT DRB1*14:73, allele DRB1*14:74, allele FT DRB1*14:77, allele DRB1*14:78, allele FT DRB1*14:84 and allele DRB1*14:85; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062938. FT VARIANT 99 99 R -> Q (in allele DRB1*14:02, allele FT DRB1*14:06, allele DRB1*14:09, allele FT DRB1*14:13, allele DRB1*14:17, allele FT DRB1*14:19, allele DRB1*14:20, allele FT DRB1*14:21, allele DRB1*14:24, allele FT DRB1*14:29, allele DRB1*14:30, allele FT DRB1*14:33, allele DRB1*14:37, allele FT DRB1*14:41, allele DRB1*14:46, allele FT DRB1*14:47, allele DRB1*14:48, allele FT DRB1*14:49, allele DRB1*14:51, allele FT DRB1*14:52, allele DRB1*14:76, allele FT DRB1*14:79, allele DRB1*14:80 and allele FT DRB1*14:83). FT /FTId=VAR_062937. FT VARIANT 100 100 R -> A (in allele DRB1*14:24 and allele FT DRB1*14:37; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062941. FT VARIANT 100 100 R -> E (in allele DRB1*14:16 and allele FT DRB1*14:57; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062940. FT VARIANT 100 100 R -> K (in allele DRB1*14:19, allele FT DRB1*14:21, allele DRB1*14:76 and allele FT DRB1*14:79). FT /FTId=VAR_062939. FT VARIANT 102 102 A -> G (in allele DRB1*14:76 and allele FT DRB1*14:79). FT /FTId=VAR_062943. FT VARIANT 102 102 A -> S (in allele DRB1*14:56). FT /FTId=VAR_062942. FT VARIANT 103 103 E -> A (in allele DRB1*14:02, allele FT DRB1*14:06, allele DRB1*14:09, allele FT DRB1*14:13, allele DRB1*14:16, allele FT DRB1*14:17, allele DRB1*14:19, allele FT DRB1*14:20, allele DRB1*14:21, allele FT DRB1*14:22, allele DRB1*14:24, allele FT DRB1*14:25, allele DRB1*14:29, allele FT DRB1*14:30, allele DRB1*14:31, allele FT DRB1*14:32, allele DRB1*14:34, allele FT DRB1*14:37, allele DRB1*14:41, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:48, allele DRB1*14:49, allele FT DRB1*14:52, allele DRB1*14:53, allele FT DRB1*14:57, allele DRB1*14:65, allele FT DRB1*14:69, allele DRB1*14:74, allele FT DRB1*14:80, allele DRB1*14:81 and allele FT DRB1*14:83). FT /FTId=VAR_062944. FT VARIANT 103 103 E -> L (in allele DRB1*14:03, allele FT DRB1*14:12, allele DRB1*14:15, allele FT DRB1*14:27, allele DRB1*14:40, allele FT DRB1*14:55, allele DRB1*14:63, allele FT DRB1*14:67, allele DRB1*14:77, allele FT DRB1*14:78, allele DRB1*14:84 and allele FT DRB1*14:85; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062945. FT VARIANT 103 103 E -> R (in allele DRB1*14:76 and allele FT DRB1*14:79; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062946. FT VARIANT 106 106 T -> A (in allele DRB1*14:43). FT /FTId=VAR_062948. FT VARIANT 106 106 T -> N (in allele DRB1*14:38, allele FT DRB1*14:47, allele DRB1*14:50, allele FT DRB1*14:76 and allele DRB1*14:79). FT /FTId=VAR_062947. FT VARIANT 110 110 H -> Y (in allele DRB1*14:75). FT /FTId=VAR_062949. FT VARIANT 114 114 V -> A (in allele DRB1*14:28 and allele FT DRB1*14:29). FT /FTId=VAR_062950. FT VARIANT 115 115 V -> G (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:07, allele FT DRB1*14:09, allele DRB1*14:13, allele FT DRB1*14:14, allele DRB1*14:19, allele FT DRB1*14:22, allele DRB1*14:24, allele FT DRB1*14:25, allele DRB1*14:27, allele FT DRB1*14:30, allele DRB1*14:36, allele FT DRB1*14:40, allele DRB1*14:41, allele FT DRB1*14:42, allele DRB1*14:44, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:48, allele DRB1*14:49, allele FT DRB1*14:51, allele DRB1*14:53, allele FT DRB1*14:63, allele DRB1*14:67, allele FT DRB1*14:68, allele DRB1*14:69, allele FT DRB1*14:77 and allele DRB1*14:85). FT /FTId=VAR_062951. FT VARIANT 115 115 V -> M (in allele DRB1*14:71). FT /FTId=VAR_062952. FT VARIANT 141 141 Y -> H (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:04, allele FT DRB1*14:05, allele DRB1*14:06, allele FT DRB1*14:07, allele DRB1*14:10, allele FT DRB1*14:11, allele DRB1*14:13, allele FT DRB1*14:14, allele DRB1*14:21, allele FT DRB1*14:46, allele DRB1*14:54, allele FT DRB1*14:57 and allele DRB1*14:82). FT /FTId=VAR_062953. FT CONFLICT 124 124 V -> G (in Ref. 10; BAH23562). SQ SEQUENCE 266 AA; 30139 MW; FA4BE90DFAB4FA55 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRFLDRYF HNQEEFVRFD SDVGEYRAVT ELGRPAAEHW NSQKDLLERR RAEVDTYCRH NYGVVESFTV QRRVHPKVTV YPSKTQPLQH YNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B1F_HUMAN Reviewed; 266 AA. AC P01911; Q29790; Q29975; Q30142; Q30166; Q32MY7; Q56FN9; Q5Y7B0; AC Q5Y7B9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 09-JUL-2014, entry version 122. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-15 beta chain; DE AltName: Full=DW2.2/DR2.2; DE AltName: Full=MHC class II antigen DRB1*15; DE Flags: Precursor; GN Name=HLA-DRB1; Synonyms=HLA-DRB2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*15:01). RC TISSUE=B-cell; RX PubMed=3259543; DOI=10.1007/BF00364432; RA Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.; RT "MHC class II sequences of an HLA-DR2 narcoleptic."; RL Immunogenetics 27:449-455(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*15:01; DRB1*15:02 AND RP DRB1*15:03). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*15:03 AND DRB1*15:04). RC TISSUE=Blood; RX PubMed=17174751; DOI=10.1016/j.humimm.2006.09.002; RA Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P., RA de Pablo R., Garcia-Sanchez F., Vicario J.L.; RT "Group-specific amplification of cDNA from DRB1 genes. Complete coding RT sequences of partially defined alleles and identification of the new RT alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113."; RL Hum. Immunol. 67:1008-1016(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB1*15:01). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRB1*15:01 AND RP DRB1*15:02). RC TISSUE=Leukocyte; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-266 (ALLELE DRB1*15:02). RC TISSUE=Lymphoblast; RX PubMed=3571980; RA Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.; RT "cDNA cloning and sequencing reveals that the electrophoretically RT constant DR beta 2 molecules, as well as the variable DR beta 1 RT molecules, from HLA-DR2 subtypes have different amino acid sequences RT including a hypervariable region for a functionally important RT epitope."; RL J. Immunol. 138:2953-2959(1987). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01). RC TISSUE=Lymphoblast; RX PubMed=2885840; DOI=10.1073/pnas.84.13.4591; RA Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.; RT "HLA-DR2 subtypes form an additional supertypic family of DR beta RT alleles."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01). RC TISSUE=Lymphoblast; RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [9] RP PROTEIN SEQUENCE OF 30-228. RC TISSUE=Lymphoblast; RX PubMed=6947956; RA Kratzin H., Yang C.-Y., Gotz H., Pauly E., Kolbel S., Egert G., RA Thinnes F.P., Wernet P., Altevogt P., Hilschmann N.; RT "Primary structure of class II human histocompatibility antigens. 1st RT communication. Amino acid sequence of the N-terminal 198 residues of RT the beta chain of a HLA-Dw2,2;DR2,2-alloantigen."; RL Hoppe-Seyler's Z. Physiol. Chem. 362:1665-1669(1981). RN [10] RP PROTEIN SEQUENCE OF 30-64. RC TISSUE=B-cell; RX PubMed=6600932; DOI=10.1021/bi00270a027; RA Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J., RA Reisfeld R.A.; RT "N-terminal amino acid sequences of the alpha and beta chains of HLA- RT DR1 and HLA-DR2 antigens."; RL Biochemistry 22:185-188(1983). RN [11] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [12] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [13] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [14] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [15] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [16] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [17] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 30-227. RX PubMed=15821740; DOI=10.1038/ni1187; RA Hahn M., Nicholson M.J., Pyrdol J., Wucherpfennig K.W.; RT "Unconventional topology of self peptide-major histocompatibility RT complex binding by a human autoimmune T cell receptor."; RL Nat. Immunol. 6:490-496(2005). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II (Probable). CC -!- POLYMORPHISM: The following alleles of DRB1-15 are known: CC DRB1*15:01, DRB1*15:02, DRB1*15:03, DRB1*15:04, DRB1*15:05, CC DRB1*15:06, DRB1*15:07, DRB1*15:08, DRB1*15:09, DRB1*15:10, CC DRB1*15:11, DRB1*15:12, DRB1*15:13, DRB1*15:14, DRB1*15:15, CC DRB1*15:16, DRB1*15:18, DRB1*15:19, DRB1*15:20, DRB1*15:21, CC DRB1*15:22, DRB1*15:23, DRB1*15:24, DRB1*15:25, DRB1*15:26, CC DRB1*15:27, DRB1*15:28, DRB1*15:29, DRB1*15:30, DRB1*15:31 and CC DRB1*15:32. The sequence shown is that of DRB1*15:01. CC -!- MISCELLANEOUS: The chain shown constituted about 70% of a pool of CC at least seven similar beta chains. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M20430; AAA59831.1; -; mRNA. DR EMBL; AY663395; AAU87979.1; -; Genomic_DNA. DR EMBL; AY663406; AAU88008.1; -; Genomic_DNA. DR EMBL; AY663411; AAU88023.1; -; Genomic_DNA. DR EMBL; AY663414; AAU88033.1; -; Genomic_DNA. DR EMBL; AY961072; AAX63460.1; -; mRNA. DR EMBL; AY961073; AAX63461.1; -; mRNA. DR EMBL; AL713966; CAI18081.1; -; Genomic_DNA. DR EMBL; BC033827; AAH33827.1; -; mRNA. DR EMBL; BC108922; AAI08923.1; -; mRNA. DR EMBL; M28584; AAA59681.1; -; mRNA. DR EMBL; M16957; AAA36279.1; -; mRNA. DR EMBL; M17378; AAA59801.1; -; mRNA. DR CCDS; CCDS47409.1; -. DR PIR; I68734; HLHUWB. DR RefSeq; NP_002115.2; NM_002124.3. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR PDB; 1BX2; X-ray; 2.60 A; B/E=32-222. DR PDB; 1YMM; X-ray; 3.50 A; B=30-227. DR PDB; 2WBJ; X-ray; 3.00 A; B/F=30-227. DR PDBsum; 1BX2; -. DR PDBsum; 1YMM; -. DR PDBsum; 2WBJ; -. DR ProteinModelPortal; P01911; -. DR SMR; P01911; 32-222. DR BioGrid; 109368; 15. DR IntAct; P01911; 1. DR DMDM; 166214928; -. DR MaxQB; P01911; -. DR PRIDE; P01911; -. DR DNASU; 3123; -. DR Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126. DR GeneID; 3123; -. DR KEGG; hsa:3123; -. DR UCSC; uc003obp.4; human. DR CTD; 3123; -. DR GeneCards; GC06M032546; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; CAB015400; -. DR HPA; CAB034021; -. DR MIM; 142857; gene. DR neXtProt; NX_P01911; -. DR PharmGKB; PA35072; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P01911; -. DR KO; K06752; -. DR OMA; ERISCGI; -. DR PhylomeDB; P01911; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-DRB1; human. DR EvolutionaryTrace; P01911; -. DR GeneWiki; HLA-DRB1; -. DR GenomeRNAi; 3123; -. DR NextBio; 12394; -. DR PRO; PR:P01911; -. DR ArrayExpress; P01911; -. DR Bgee; P01911; -. DR CleanEx; HS_HLA-DRB1; -. DR Genevestigator; P01911; -. DR GO; GO:0009986; C:cell surface; IDA:UniProt. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProt. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProt. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProt. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0002506; P:polysaccharide assembly with MHC class II protein complex; IDA:UniProt. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Endosome; Glycoprotein; Golgi apparatus; Immunity; Isopeptide bond; KW Lysosome; Membrane; MHC II; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-15 beta chain. FT /FTId=PRO_0000080744. FT TOPO_DOM 30 227 Extracellular (Potential). FT TRANSMEM 228 248 Helical; (Potential). FT TOPO_DOM 249 266 Cytoplasmic (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...). FT DISULFID 44 108 FT DISULFID 146 202 FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 5 5 K -> R (in dbSNP:rs9270305). FT /FTId=VAR_050364. FT VARIANT 55 55 F -> Y (in dbSNP:rs16822516). FT /FTId=VAR_050365. FT VARIANT 59 59 Y -> H (in allele DRB1*15:03). FT /FTId=VAR_038162. FT VARIANT 96 96 I -> F (in allele DRB1*15:04; FT dbSNP:rs17886918). FT /FTId=VAR_038163. FT VARIANT 106 106 T -> N (in dbSNP:rs9269941). FT /FTId=VAR_050366. FT VARIANT 115 115 V -> G (in allele DRB1*15:02; FT dbSNP:rs17885482). FT /FTId=VAR_038164. FT VARIANT 164 164 G -> S (in dbSNP:rs1059633). FT /FTId=VAR_050367. FT VARIANT 169 169 A -> T (in dbSNP:rs2308768). FT /FTId=VAR_050368. FT VARIANT 236 236 V -> M (in dbSNP:rs2230816). FT /FTId=VAR_050369. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_050370. FT CONFLICT 119 119 T -> A (in Ref. 5; AAI08923). FT CONFLICT 154 154 G -> A (in Ref. 8; AAA59801). FT CONFLICT 171 171 M -> G (in Ref. 9; AA sequence). FT CONFLICT 179 180 NG -> D (in Ref. 9; AA sequence). FT STRAND 36 47 FT TURN 48 51 FT STRAND 52 61 FT STRAND 64 70 FT TURN 71 73 FT STRAND 75 80 FT HELIX 81 83 FT HELIX 84 92 FT HELIX 94 106 FT HELIX 108 115 FT TURN 116 121 FT STRAND 127 134 FT STRAND 142 154 FT STRAND 157 162 FT STRAND 165 167 FT STRAND 169 173 FT STRAND 180 182 FT STRAND 184 192 FT STRAND 199 205 FT STRAND 209 211 FT STRAND 213 218 SQ SEQUENCE 266 AA; 29966 MW; 3B5912820A4654BE CRC64; MVCLKLPGGS CMTALTVTLM VLSSPLALSG DTRPRFLWQP KRECHFFNGT ERVRFLDRYF YNQEESVRFD SDVGEFRAVT ELGRPDAEYW NSQKDILEQA RAAVDTYCRH NYGVVESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FLNGQEEKAG MVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B1G_HUMAN Reviewed; 266 AA. AC Q29974; A7X5J4; O98212; Q0PGR5; Q29792; Q30120; Q30159; Q30200; AC Q3HUP9; Q3KTM1; Q3LA84; Q6T865; Q95383; DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-APR-2014, entry version 107. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-16 beta chain; DE AltName: Full=MHC class II antigen DRB1*16; DE Short=DR-16; DE Short=DR16; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*16:01). RX PubMed=3571980; RA Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.; RT "cDNA cloning and sequencing reveals that the electrophoretically RT constant DR beta 2 molecules, as well as the variable DR beta 1 RT molecules, from HLA-DR2 subtypes have different amino acid sequences RT including a hypervariable region for a functionally important RT epitope."; RL J. Immunol. 138:2953-2959(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*16:02). RX PubMed=3129499; RA Liu C.P., Bach F.H., Wu S.K.; RT "Molecular studies of a rare DR2/LD-5a/DQw3 HLA class II haplotype. RT Multiple genetic mechanisms in the generation of polymorphic HLA class RT II genes."; RL J. Immunol. 140:3631-3639(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*16:03). RC TISSUE=Blood; RX PubMed=8436426; DOI=10.1007/BF00222476; RA Rosenlicht J.W., Hartung K., Deicher H., Frey J.; RT "A novel HLA-DRB1-DR2 allele associated with HLA mistyping."; RL Immunogenetics 37:479-479(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB1*16:01). RC TISSUE=Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*16:01). RX PubMed=2885840; DOI=10.1073/pnas.84.13.4591; RA Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.; RT "HLA-DR2 subtypes form an additional supertypic family of DR beta RT alleles."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-216 (ALLELE DRB1*16:04). RC TISSUE=Peripheral blood; RX PubMed=17767557; DOI=10.1111/j.1399-0039.2007.00918.x; RA Horn P.A., Albis-Camps M., Verboom M., Bunce M., Yousaf K., RA Williams S., Blasczyk R.; RT "The nature of diversity of HLA-DRB1 exon 3."; RL Tissue Antigens 70:335-337(2007). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:08). RX PubMed=9271639; DOI=10.1007/s002510050303; RA Reviron D., Dormoy A., Andre M., Froelich N., Roudier J., Tongio M.M., RA Mercier P.; RT "HLA-DRB1*1608: a new HLA-DRB1*16 allele with a short DRB1*03 RT sequence."; RL Immunogenetics 46:444-445(1997). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:09). RX PubMed=16101839; DOI=10.1111/j.1399-0039.2005.00443.x; RA Miao K.R., Pan Q.Q., Xue M., Zhou X.Y., Fei X.M., Tang Y.H., Xu R., RA Zhang J.W., Zhao X., Osowski L., Shi W.X., Xu A.L., Wang C.Y., RA Kukuruga D.; RT "A novel HLA allele, DRB1*1609, identified in the Chinese Han RT population*."; RL Tissue Antigens 66:248-250(2005). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:11). RX PubMed=19500310; DOI=10.1111/j.1399-0039.2009.01260.x; RA Chu C.-C., Lee H.-L., Lin M.; RT "A novel HLA-DRB1 allele, DRB*1611, is identified in two Taiwanese RT individuals."; RL Tissue Antigens 74:175-176(2009). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:05). RA Gedil M.A., Steiner N.K., Hurley C.K.; RT "Novel HLA-DRB1 allele."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:10). RA Yan L., Zhu F., He J.; RT "Identification a novel HLA-DRB1*16 allele by sequence based typing in RT Chinese."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:12). RA Lazaro A.M., Xiao Y., Hurley C.K.; RT "Novel HLA class II allele."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DRB1*16:01). RC TISSUE=Blood; RX PubMed=10551425; DOI=10.1034/j.1399-0039.1999.540411.x; RA Lin Y.S., Tang T.F., Ng J., Hartzman R., Hurley C.K.; RT "Two DR2-associated novel alleles arose from the silent mutation of RT codon 72: DRB1*16012, DRB5*01012."; RL Tissue Antigens 54:405-408(1999). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-120 (ALLELE DRB1*16:07). RA Brautbar C., Israel S., Safirman C., Smith A.G.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [15] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [16] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [17] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [18] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [19] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [20] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [21] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II (Probable). CC -!- POLYMORPHISM: The following alleles of DRB1-16 are known: CC DRB1*16:01; DRB1*16:02; DRB1*16:03; DRB1*16:04; DRB1*16:05; CC DRB1*16:07; DRB1*16:08; DRB1*16:09; DRB1*16:10; DRB1*16:11 and CC DRB1*16:12. The sequence shown is that of DRB1*16:02. CC -!- SIMILARITY: Belongs to the MHC class II family. CC -!- SIMILARITY: Contains 1 Ig-like C1-type (immunoglobulin-like) CC domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M28583; AAA59680.1; -; mRNA. DR EMBL; M20504; AAA59827.1; -; mRNA. DR EMBL; L02545; AAA59777.1; -; mRNA. DR EMBL; AK291987; BAF84676.1; -; mRNA. DR EMBL; M16959; AAA36281.1; -; mRNA. DR EMBL; AM110006; CAJ33613.1; -; Genomic_DNA. DR EMBL; Z72424; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY912074; AAY17287.1; -; Genomic_DNA. DR EMBL; DQ837166; ABH05946.1; -; Genomic_DNA. DR EMBL; AY428805; AAR07616.1; -; Genomic_DNA. DR EMBL; DQ192647; ABA39176.1; -; Genomic_DNA. DR EMBL; EU029801; ABU86860.1; -; Genomic_DNA. DR EMBL; U59686; AAB52230.1; -; Genomic_DNA. DR EMBL; U26659; AAD09441.1; -; Genomic_DNA. DR PIR; B27618; B27618. DR PIR; D25239; D25239. DR PIR; F27060; F27060. DR PIR; I54509; I54509. DR RefSeq; NP_002115.2; NM_002124.3. DR UniGene; Hs.485130; -. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q29974; -. DR SMR; Q29974; 32-222. DR BioGrid; 109368; 15. DR DMDM; 74762149; -. DR PRIDE; Q29974; -. DR DNASU; 3123; -. DR Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126. DR GeneID; 3123; -. DR KEGG; hsa:3123; -. DR CTD; 3123; -. DR GeneCards; GC06M032546; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; CAB015400; -. DR HPA; CAB034021; -. DR MIM; 142857; gene. DR neXtProt; NX_Q29974; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR TreeFam; TF336626; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; HLA-DRB1; human. DR GenomeRNAi; 3123; -. DR NextBio; 12394; -. DR ArrayExpress; Q29974; -. DR Bgee; Q29974; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISS:UniProtKB. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB. DR GO; GO:2001179; P:regulation of interleukin-10 secretion; ISS:UniProtKB. DR GO; GO:0032673; P:regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0031295; P:T cell costimulation; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 Potential. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-16 beta chain. FT /FTId=PRO_0000391833. FT TRANSMEM 228 248 Helical; (Potential). FT DOMAIN 126 214 Ig-like C1-type. FT CARBOHYD 48 48 N-linked (GlcNAc...) (Potential). FT DISULFID 146 202 By similarity. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) (By FT similarity). FT VARIANT 42 42 R -> K (in allele DRB1*16:12). FT /FTId=VAR_062840. FT VARIANT 43 43 E -> K (in allele DRB1*16:11). FT /FTId=VAR_062841. FT VARIANT 56 56 L -> P (in allele DRB1*16:07). FT /FTId=VAR_062842. FT VARIANT 66 66 S -> N (in allele DRB1*16:08). FT /FTId=VAR_062843. FT VARIANT 76 76 Y -> F (in allele DRB1*16:09 and allele FT DRB1*16:10). FT /FTId=VAR_062844. FT VARIANT 96 96 F -> I (in allele DRB1*16:05 and allele FT DRB1*16:07). FT /FTId=VAR_062845. FT VARIANT 96 96 F -> L (in allele DRB1*16:02, allele FT DRB1*16:10, allele DRB1*16:11 and allele FT DRB1*16:12). FT /FTId=VAR_062846. FT VARIANT 101 101 R -> A (in allele DRB1*16:03; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062847. FT VARIANT 103 103 A -> L (in allele DRB1*16:04; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062848. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_062849. SQ SEQUENCE 266 AA; 30030 MW; 871CC341692ECA4D CRC64; MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQP KRECHFFNGT ERVRFLDRYF YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDFLEDR RAAVDTYCRH NYGVGESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FLNGQEEKAG MVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 3BHS2_HUMAN Reviewed; 372 AA. AC P26439; A2RRA5; Q16010; Q53GD4; Q6AI10; Q6LDB9; Q99890; Q9UD08; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-JUL-2014, entry version 154. DE RecName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2; DE AltName: Full=3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type II; DE Short=3-beta-HSD II; DE AltName: Full=3-beta-HSD adrenal and gonadal type; DE Includes: DE RecName: Full=3-beta-hydroxy-Delta(5)-steroid dehydrogenase; DE EC=1.1.1.145; DE AltName: Full=3-beta-hydroxy-5-ene steroid dehydrogenase; DE AltName: Full=Progesterone reductase; DE Includes: DE RecName: Full=Steroid Delta-isomerase; DE EC=5.3.3.1; DE AltName: Full=Delta-5-3-ketosteroid isomerase; GN Name=HSD3B2; Synonyms=HSDB3B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1741954; DOI=10.1089/dna.1991.10.701; RA Lachance Y., Luu-The V., Verreault H., Dumont M., Rheaume E., RA Leblanc G., Labrie F.; RT "Structure of the human type II 3 beta-hydroxysteroid RT dehydrogenase/delta 5-delta 4 isomerase (3 beta-HSD) gene: adrenal and RT gonadal specificity."; RL DNA Cell Biol. 10:701-711(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Adrenal gland; RX PubMed=1944309; DOI=10.1210/mend-5-8-1147; RA Rheaume E., Lachance Y., Zhao H.-F., Breton N., Dumont M., RA de Launoit Y., Trudel C., Luu-The V., Simard J., Labrie F.; RT "Structure and expression of a new complementary DNA encoding the RT almost exclusive 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4- RT isomerase in human adrenals and gonads."; RL Mol. Endocrinol. 5:1147-1157(1991). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP GLN-94. RC TISSUE=Adrenal gland; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Small intestine; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 49-102. RX PubMed=7588414; RA Russell A.J., McCartin S., Corcao G., Burridge S.M., McBride M.W., RA McNicol A.M., Hawes C.S., Mason J.I., Sutcliffe R.G.; RT "Variation in the expression of human 3 beta-hydroxysteroid RT dehydrogenase."; RL Endocr. Res. 21:485-494(1995). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-205. RX PubMed=1363812; DOI=10.1038/ng0792-239; RA Rheaume E., Simard J., Morel Y., Mebarki F., Zachmann M., Forest M.G., RA New M.I., Labrie F.; RT "Congenital adrenal hyperplasia due to point mutations in the type II RT 3 beta-hydroxysteroid dehydrogenase gene."; RL Nat. Genet. 1:239-245(1992). RN [10] RP POSSIBLE INVOLVEMENT IN INSULIN-RESISTANT POLYCYSTIC OVARY SYNDROME. RX PubMed=14764797; DOI=10.1210/jc.2003-030934; RA Carbunaru G., Prasad P., Scoccia B., Shea P., Hopwood N., Ziai F., RA Chang Y.T., Myers S.E., Mason J.I., Pang S.; RT "The hormonal phenotype of nonclassic 3 beta-hydroxysteroid RT dehydrogenase (HSD3B) deficiency in hyperandrogenic females is RT associated with insulin-resistant polycystic ovary syndrome and is not RT a variant of inherited HSD3B2 deficiency."; RL J. Clin. Endocrinol. Metab. 89:783-794(2004). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP VARIANTS AH2 LYS-142; PRO-245 AND ASN-253. RX PubMed=8316254; DOI=10.1210/me.7.5.716; RA Simard J., Rheaume E., Sanchez R., Laflamme N., de Launoit Y., RA Luu-The V., van Seters A.P., Gordon R.D., Bettendorf M., Heinrich U., RA Moshang T., New M.I., Labrie F.; RT "Molecular basis of congenital adrenal hyperplasia due to 3 beta- RT hydroxysteroid dehydrogenase deficiency."; RL Mol. Endocrinol. 7:716-728(1993). RN [13] RP VARIANTS AH2 TRP-108 AND LEU-186. RX PubMed=7833923; DOI=10.1093/hmg/3.9.1639; RA Sanchez R., Mebarki F., Rheaume E., Laflamme N., Forest M.G., RA Bey-Omar F., David M., Morel Y., Labrie F., Simard J.; RT "Functional characterization of the novel L108W and P186L mutations RT detected in the type II 3 beta-hydroxysteroid dehydrogenase gene of a RT male pseudohermaphrodite with congenital adrenal hyperplasia."; RL Hum. Mol. Genet. 3:1639-1645(1994). RN [14] RP VARIANT AH2 ASP-254. RX PubMed=8126127; DOI=10.1210/jc.78.3.561; RA Sanchez R., Rheaume E., Laflamme N., Rosenfield R.L., Labrie F., RA Simard J.; RT "Detection and functional characterization of the novel missense RT mutation Y254D in type II 3 beta-hydroxysteroid dehydrogenase (3 beta RT HSD) gene of a female patient with nonsalt-losing 3 beta HSD RT deficiency."; RL J. Clin. Endocrinol. Metab. 78:561-567(1994). RN [15] RP VARIANT AH2 ARG-129. RX PubMed=7962268; DOI=10.1210/jc.79.4.1012; RA Rheaume E., Sanchez R., Simard J., Chang Y.T., Wang J., Pang S., RA Labrie F.; RT "Molecular basis of congenital adrenal hyperplasia in two siblings RT with classical nonsalt-losing 3 beta-hydroxysteroid dehydrogenase RT deficiency."; RL J. Clin. Endocrinol. Metab. 79:1012-1018(1994). RN [16] RP VARIANT AH2 THR-82. RX PubMed=8185809; DOI=10.1677/jme.0.0120119; RA Mendonca B.B., Russell A.J., Vasconcelos-Leite M., Arnhold I.J., RA Bloise W., Wajchenberg B.L., Nicolau W., Sutcliffe R.G., Wallace A.M.; RT "Mutation in 3 beta-hydroxysteroid dehydrogenase type II associated RT with pseudohermaphroditism in males and premature pubarche or cryptic RT expression in females."; RL J. Mol. Endocrinol. 12:119-122(1994). RN [17] RP VARIANT AH2 ARG-173. RX PubMed=8060486; DOI=10.1677/jme.0.0120225; RA Russell A.J., Wallace A.M., Forest M.G., Donaldson M.D., Edwards C.R., RA Sutcliffe R.G.; RT "Mutation in the human gene for 3 beta-hydroxysteroid dehydrogenase RT type II leading to male pseudohermaphroditism without salt loss."; RL J. Mol. Endocrinol. 12:225-237(1994). RN [18] RP VARIANT AH2 ASP-15. RX PubMed=7893703; DOI=10.1021/bi00009a020; RA Rheaume E., Sanchez R., Mebarki F., Gagnon E., Carel J.-C., RA Chaussain J.-L., Morel Y., Labrie F., Simard J.; RT "Identification and characterization of the G15D mutation found in a RT male patient with 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) RT deficiency: alteration of the putative NAD-binding domain of type II 3 RT beta-HSD."; RL Biochemistry 34:2893-2900(1995). RN [19] RP VARIANT AH2 PRO-205. RX PubMed=7633426; DOI=10.1093/hmg/4.4.745; RA Katsumata N., Tanae A., Yasunaga T., Horikawa R., Tanaka T., Hibi I.; RT "A novel missense mutation in the type II 3 beta-hydroxysteroid RT dehydrogenase gene in a family with classical salt-wasting congenital RT adrenal hyperplasia due to 3 beta-hydroxysteroid dehydrogenase RT deficiency."; RL Hum. Mol. Genet. 4:745-746(1995). RN [20] RP VARIANT AH2 ARG-259. RX PubMed=7633460; DOI=10.1093/hmg/4.5.969; RA Tajima T., Fujieda K., Nakae J., Shinohara N., Yoshimoto M., Baba T., RA Kinoshita E., Igarashi Y., Oomura T.; RT "Molecular analysis of type II 3 beta-hydroxysteroid dehydrogenase RT gene in Japanese patients with classical 3 beta-hydroxysteroid RT dehydrogenase deficiency."; RL Hum. Mol. Genet. 4:969-971(1995). RN [21] RP VARIANT AH2 SER-100. RX PubMed=7608265; DOI=10.1210/jc.80.7.2127; RA Mebarki F., Sanchez R., Rheaume E., Laflamme N., Simard J., RA Forest M.G., Bey-Omar F., David M., Labrie F., Morel Y.; RT "Nonsalt-losing male pseudohermaphroditism due to the novel homozygous RT N100S mutation in the type II 3 beta-hydroxysteroid dehydrogenase RT gene."; RL J. Clin. Endocrinol. Metab. 80:2127-2134(1995). RN [22] RP VARIANT AH2 SER-236. RX PubMed=9719627; DOI=10.1006/mgme.1998.2715; RA Nayak S., Lee P.A., Witchel S.F.; RT "Variants of the type II 3beta-hydroxysteroid dehydrogenase gene in RT children with premature pubic hair and hyperandrogenic adolescents."; RL Mol. Genet. Metab. 64:184-192(1998). RN [23] RP VARIANTS AH2 GLU-10; VAL-10; ASP-15; THR-82; SER-100; TRP-108; RP ARG-129; LYS-142; LEU-155; VAL-167; ARG-173; LEU-186; PRO-205; RP GLY-213; GLU-216; GLN-222; HIS-222; SER-236; PRO-245; ASN-253; RP ASP-254; ARG-259; MET-259 AND VAL-294. RX PubMed=10599696; DOI=10.1210/jc.84.12.4410; RA Moisan A.M., Ricketts M.L., Tardy V., Desrochers M., Mebarki F., RA Chaussain J.-L., Cabrol S., Raux-Demay M.C., Forest M.G., RA Sippell W.G., Peter M., Morel Y., Simard J.; RT "New insight into the molecular basis of 3beta-hydroxysteroid RT dehydrogenase deficiency: identification of eight mutations in the RT HSD3B2 gene in eleven patients from seven new families and comparison RT of the functional properties of twenty-five mutant enzymes."; RL J. Clin. Endocrinol. Metab. 84:4410-4425(1999). RN [24] RP VARIANTS AH2 ARG-129; GLN-222 AND MET-259. RX PubMed=10651755; DOI=10.1046/j.1365-2265.2000.00873.x; RA Marui S., Castro M., Latronico A.C., Elias L.L., Arnhold I.J., RA Moreira A.C., Mendonca B.B.; RT "Mutations in the type II 3beta-hydroxysteroid dehydrogenase (HSD3B2) RT gene can cause premature pubarche in girls."; RL Clin. Endocrinol. (Oxf.) 52:67-75(2000). RN [25] RP VARIANT AH2 GLU-10. RX PubMed=10843183; DOI=10.1210/jc.85.5.1968; RA Alos N., Moisan A.M., Ward L., Desrochers M., Legault L., Leboeuf G., RA van Vliet G., Simard J.; RT "A novel A10E homozygous mutation in the HSD3B2 gene causing severe RT salt-wasting 3beta-hydroxysteroid dehydrogenase deficiency in 46,XX RT and 46,XY French-Canadians: evaluation of gonadal function after RT puberty."; RL J. Clin. Endocrinol. Metab. 85:1968-1974(2000). RN [26] RP VARIANTS AH2 LYS-142 AND THR-222. RX PubMed=12050213; DOI=10.1210/jc.87.6.2556; RA Pang S., Wang W., Rich B., David R., Chang Y.T., Carbunaru G., RA Myers S.E., Howie A.F., Smillie K.J., Mason J.I.; RT "A novel nonstop mutation in the stop codon and a novel missense RT mutation in the type II 3-beta-hydroxysteroid dehydrogenase (3-beta- RT HSD) gene causing, respectively, nonclassic and classic 3-beta-HSD RT deficiency congenital adrenal hyperplasia."; RL J. Clin. Endocrinol. Metab. 87:2556-2563(2002). RN [27] RP VARIANT AH2 LEU-341, AND CHARACTERIZATION OF VARIANT AH2 LEU-341. RX PubMed=18252794; DOI=10.1210/jc.2007-1874; RA Welzel M., Wustemann N., Simic-Schleicher G., Dorr H.G., Schulze E., RA Shaikh G., Clayton P., Grotzinger J., Holterhus P.M., Riepe F.G.; RT "Carboxyl-terminal mutations in 3beta-hydroxysteroid dehydrogenase RT type II cause severe salt-wasting congenital adrenal hyperplasia."; RL J. Clin. Endocrinol. Metab. 93:1418-1425(2008). RN [28] RP VARIANT AH2 PRO-82. RX PubMed=22579964; DOI=10.1016/j.gene.2012.04.080; RA Rabbani B., Mahdieh N., Haghi Ashtiani M.T., Setoodeh A., Rabbani A.; RT "In silico structural, functional and pathogenicity evaluation of a RT novel mutation: an overview of HSD3B2 gene mutations."; RL Gene 503:215-221(2012). CC -!- FUNCTION: 3-beta-HSD is a bifunctional enzyme, that catalyzes the CC oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and CC the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic CC system plays a crucial role in the biosynthesis of all classes of CC hormonal steroids. CC -!- CATALYTIC ACTIVITY: A 3-beta-hydroxy-Delta(5)-steroid + NAD(+) = a CC 3-oxo-Delta(5)-steroid + NADH. CC -!- CATALYTIC ACTIVITY: A 3-oxo-Delta(5)-steroid = a 3-oxo-Delta(4)- CC steroid. CC -!- PATHWAY: Lipid metabolism; steroid biosynthesis. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein. Mitochondrion membrane; Single-pass membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P26439-1; Sequence=Displayed; CC Name=2; CC IsoId=P26439-2; Sequence=VSP_037399, VSP_037400; CC -!- TISSUE SPECIFICITY: Expressed in adrenal gland, testis and ovary. CC -!- DISEASE: Adrenal hyperplasia 2 (AH2) [MIM:201810]: A form of CC congenital adrenal hyperplasia, a common recessive disease due to CC defective synthesis of cortisol. Congenital adrenal hyperplasia is CC characterized by androgen excess leading to ambiguous genitalia in CC affected females, rapid somatic growth during childhood in both CC sexes with premature closure of the epiphyses and short adult CC stature. Four clinical types: 'salt wasting' (SW, the most severe CC type), 'simple virilizing' (SV, less severely affected patients), CC with normal aldosterone biosynthesis, 'non-classic form' or late- CC onset (NC or LOAH)and 'cryptic' (asymptomatic). In AH2, CC virilization is much less marked or does not occur. AH2 is CC frequently lethal in early life. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Note=Mild HSD3B2 deficiency in hyperandrogenic females is CC associated with characteristic traits of polycystic ovary CC syndrome, such as insulin resistance and luteinizing hormone CC hypersecretion. CC -!- SIMILARITY: Belongs to the 3-beta-HSD family. CC -!- SEQUENCE CAUTION: CC Sequence=AAC60600.1; Type=Frameshift; Positions=186; Note=The frameshift is caused by a single nucleotide insertion which is found in AH2; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M77144; AAA36014.1; -; Genomic_DNA. DR EMBL; M67466; AAA36016.1; -; mRNA. DR EMBL; CR627415; CAH10504.1; -; mRNA. DR EMBL; AK222997; BAD96717.1; -; mRNA. DR EMBL; AL359553; CAC19799.1; -; Genomic_DNA. DR EMBL; CH471122; EAW56700.1; -; Genomic_DNA. DR EMBL; BC038419; AAH38419.1; -; mRNA. DR EMBL; BC131488; AAI31489.1; -; mRNA. DR EMBL; S80140; AAD14329.1; -; Genomic_DNA. DR EMBL; S60309; AAC60599.1; -; Genomic_DNA. DR EMBL; S60310; AAC60600.1; ALT_FRAME; Genomic_DNA. DR CCDS; CCDS902.1; -. [P26439-1] DR PIR; A39488; DEHUH2. DR RefSeq; NP_000189.1; NM_000198.3. [P26439-1] DR RefSeq; NP_001159592.1; NM_001166120.1. [P26439-1] DR UniGene; Hs.654399; -. DR ProteinModelPortal; P26439; -. DR SMR; P26439; 6-158. DR BioGrid; 109517; 1. DR STRING; 9606.ENSP00000358424; -. DR BindingDB; P26439; -. DR ChEMBL; CHEMBL3670; -. DR DrugBank; DB00157; NADH. DR DrugBank; DB01108; Trilostane. DR PhosphoSite; P26439; -. DR DMDM; 112770; -. DR PaxDb; P26439; -. DR PRIDE; P26439; -. DR DNASU; 3284; -. DR Ensembl; ENST00000369416; ENSP00000358424; ENSG00000203859. [P26439-1] DR Ensembl; ENST00000543831; ENSP00000445122; ENSG00000203859. [P26439-1] DR GeneID; 3284; -. DR KEGG; hsa:3284; -. DR UCSC; uc001ehs.3; human. [P26439-1] DR UCSC; uc001ehu.3; human. [P26439-2] DR CTD; 3284; -. DR GeneCards; GC01P119957; -. DR HGNC; HGNC:5218; HSD3B2. DR MIM; 201810; phenotype. DR MIM; 613890; gene. DR neXtProt; NX_P26439; -. DR Orphanet; 90791; Congenital adrenal hyperplasia due to 3-beta-hydroxysteroid dehydrogenase deficiency. DR Orphanet; 3185; Polycystic ovary syndrome. DR PharmGKB; PA29487; -. DR eggNOG; COG0451; -. DR HOVERGEN; HBG000014; -. DR InParanoid; P26439; -. DR KO; K00070; -. DR OMA; TTEWLAS; -. DR PhylomeDB; P26439; -. DR TreeFam; TF343138; -. DR BioCyc; MetaCyc:HS10943-MONOMER; -. DR BRENDA; 1.1.1.145; 2681. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_15493; Steroid hormones. DR UniPathway; UPA00062; -. DR GeneWiki; HSD3B2; -. DR GenomeRNAi; 3284; -. DR NextBio; 13035; -. DR PRO; PR:P26439; -. DR ArrayExpress; P26439; -. DR Bgee; P26439; -. DR CleanEx; HS_HSD3B2; -. DR Genevestigator; P26439; -. DR GO; GO:0005783; C:endoplasmic reticulum; NAS:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB. DR GO; GO:0031966; C:mitochondrial membrane; NAS:UniProtKB. DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISS:UniProtKB. DR GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0004769; F:steroid delta-isomerase activity; IDA:UniProtKB. DR GO; GO:0006702; P:androgen biosynthetic process; TAS:Reactome. DR GO; GO:0006704; P:glucocorticoid biosynthetic process; TAS:Reactome. DR GO; GO:0006705; P:mineralocorticoid biosynthetic process; TAS:Reactome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006694; P:steroid biosynthetic process; IDA:UniProtKB. DR GO; GO:0008202; P:steroid metabolic process; TAS:Reactome. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01073; 3Beta_HSD; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; KW Congenital adrenal hyperplasia; Disease mutation; KW Endoplasmic reticulum; Isomerase; Membrane; Mitochondrion; KW Multifunctional enzyme; NAD; Oxidoreductase; Polymorphism; KW Reference proteome; Steroidogenesis; Transmembrane; KW Transmembrane helix. FT CHAIN 1 372 3 beta-hydroxysteroid dehydrogenase/Delta FT 5-->4-isomerase type 2. FT /FTId=PRO_0000087775. FT TRANSMEM 287 307 Helical; (Potential). FT ACT_SITE 154 154 Proton acceptor (By similarity). FT BINDING 158 158 NAD (By similarity). FT VAR_SEQ 103 222 GTQLLLEACVQASVPVFIYTSSIEVAGPNSYKEIIQNGHEE FT EPLENTWPTPYPYSKKLAEKAVLAANGWNLKNGDTLYTCAL FT RPTYIYGEGGPFLSASINEALNNNGILSSVGKFSTVNP -> FT ELQNKIKLTVLEGDILDEPFLKRACQDVSVVIHTACIIDVF FT GVTHRQSIMNVNVKGRVAWGGDKARWGNEDQKEGQEGKRSL FT SIEHLLCSGPSDFADHYQLGELKAAIFSFIDEKTRTEQ FT (in isoform 2). FT /FTId=VSP_037399. FT VAR_SEQ 223 372 Missing (in isoform 2). FT /FTId=VSP_037400. FT VARIANT 10 10 A -> E (in AH2; activity abolished; FT dbSNP:rs28934880). FT /FTId=VAR_010517. FT VARIANT 10 10 A -> V (in AH2; nonsalt-wasting form). FT /FTId=VAR_010518. FT VARIANT 15 15 G -> D (in AH2; activity abolished). FT /FTId=VAR_010519. FT VARIANT 74 74 D -> N (in dbSNP:rs4986954). FT /FTId=VAR_048099. FT VARIANT 82 82 A -> P (in AH2). FT /FTId=VAR_070028. FT VARIANT 82 82 A -> T (in AH2). FT /FTId=VAR_010520. FT VARIANT 94 94 E -> Q (in dbSNP:rs6211). FT /FTId=VAR_014818. FT VARIANT 100 100 N -> S (in AH2; nonsalt-wasting form). FT /FTId=VAR_010521. FT VARIANT 108 108 L -> W (in AH2; activity abolished). FT /FTId=VAR_010522. FT VARIANT 129 129 G -> R (in AH2; nonsalt-wasting form). FT /FTId=VAR_010523. FT VARIANT 142 142 E -> K (in AH2; activity abolished). FT /FTId=VAR_000006. FT VARIANT 155 155 P -> L (in AH2; nonsalt-wasting form). FT /FTId=VAR_010524. FT VARIANT 167 167 A -> V (in AH2; late onset; almost normal FT activity; dbSNP:rs35486059). FT /FTId=VAR_010525. FT VARIANT 173 173 L -> R (in AH2; nonsalt-wasting form). FT /FTId=VAR_010526. FT VARIANT 186 186 P -> L (in AH2; activity abolished). FT /FTId=VAR_010527. FT VARIANT 205 205 L -> P (in AH2). FT /FTId=VAR_000007. FT VARIANT 213 213 S -> G (in AH2; late onset; partial loss FT of activity). FT /FTId=VAR_010528. FT VARIANT 216 216 K -> E (in AH2; late onset; partial loss FT of activity). FT /FTId=VAR_010529. FT VARIANT 222 222 P -> H (in AH2; nonsalt-wasting form; FT activity abolished). FT /FTId=VAR_010530. FT VARIANT 222 222 P -> Q (in AH2; activity abolished). FT /FTId=VAR_010531. FT VARIANT 222 222 P -> T (in AH2). FT /FTId=VAR_015411. FT VARIANT 231 238 Missing (in AH2; activity abolished). FT /FTId=VAR_010532. FT VARIANT 236 236 L -> S (in AH2; mild; 100% of activity; FT dbSNP:rs35887327). FT /FTId=VAR_010533. FT VARIANT 245 245 A -> P (in AH2; loss of 88% of activity). FT /FTId=VAR_000008. FT VARIANT 253 253 Y -> N (in AH2; activity abolished). FT /FTId=VAR_000009. FT VARIANT 254 254 Y -> D (in AH2; activity abolished). FT /FTId=VAR_000010. FT VARIANT 259 259 T -> M (in AH2; activity abolished). FT /FTId=VAR_010534. FT VARIANT 259 259 T -> R (in AH2; activity abolished). FT /FTId=VAR_000011. FT VARIANT 294 294 G -> V (in AH2; nonsalt-wasting form; FT activity abolished). FT /FTId=VAR_010535. FT VARIANT 341 341 P -> L (in AH2; strongly reduced FT activity). FT /FTId=VAR_065665. FT CONFLICT 52 53 RT -> KI (in Ref. 8; AAD14329). FT CONFLICT 92 94 HRE -> RRQ (in Ref. 8; AAD14329). FT CONFLICT 232 232 H -> L (in Ref. 4; BAD96717). SQ SEQUENCE 372 AA; 42052 MW; 8E0D933488988451 CRC64; MGWSCLVTGA GGLLGQRIVR LLVEEKELKE IRALDKAFRP ELREEFSKLQ NRTKLTVLEG DILDEPFLKR ACQDVSVVIH TACIIDVFGV THRESIMNVN VKGTQLLLEA CVQASVPVFI YTSSIEVAGP NSYKEIIQNG HEEEPLENTW PTPYPYSKKL AEKAVLAANG WNLKNGDTLY TCALRPTYIY GEGGPFLSAS INEALNNNGI LSSVGKFSTV NPVYVGNVAW AHILALRALR DPKKAPSVRG QFYYISDDTP HQSYDNLNYI LSKEFGLRLD SRWSLPLTLM YWIGFLLEVV SFLLSPIYSY QPPFNRHTVT LSNSVFTFSY KKAQRDLAYK PLYSWEEAKQ KTVEWVGSLV DRHKETLKSK TQ // ID 3BP2_HUMAN Reviewed; 561 AA. AC P78314; A6NNC2; B2R5R6; B4DT04; D3DVR0; D6R919; O00500; O15373; AC P78315; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 09-JUL-2014, entry version 131. DE RecName: Full=SH3 domain-binding protein 2; DE Short=3BP-2; GN Name=SH3BP2; Synonyms=3BP2; ORFNames=RES4-23; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Tonsil; RA Gokemeijer J., Deligiannidis K.E., Ligris K., Ernst T.J.; RT "3BP2 binds to phosphatidylinositols; linking the hemopoietic tyrosine RT kinase c-FES to the cytoplasmic membrane in a phosphorylation RT dependent mechanism."; RL Blood 88:473A-473A(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=9299232; DOI=10.1006/geno.1997.4849; RA Bell S.M., Shaw M., Jou Y.-S., Myers R.M., Knowles M.A.; RT "Identification and characterization of the human homologue of SH3BP2, RT an SH3 binding domain protein within a common region of deletion at RT 4p16.3 involved in bladder cancer."; RL Genomics 44:163-170(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=9734812; DOI=10.1093/dnares/5.3.177; RA Hadano S., Ishida Y., Ikeda J.-E.; RT "The primary structure and genomic organization of five novel RT transcripts located close to the Huntington's disease gene on human RT chromosome 4p16.3."; RL DNA Res. 5:177-186(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP STRUCTURE BY NMR OF 444-558. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH2 domain of human SH3BP2 protein."; RL Submitted (NOV-2005) to the PDB data bank. RN [11] RP VARIANTS CRBM GLN-415; PRO-415; ARG-418; HIS-418; LEU-418; ARG-420 AND RP GLU-420. RX PubMed=11381256; DOI=10.1038/88832; RA Ueki Y., Tiziani V., Santanna C., Fukai N., Maulik C., Garfinkle J., RA Ninomiya C., doAmaral C., Peters H., Habal M., Rhee-Morris L., RA Doss J.B., Kreiborg S., Olsen B.R., Reichenberger E.; RT "Mutations in the gene encoding c-Abl-binding protein SH3BP2 cause RT cherubism."; RL Nat. Genet. 28:125-126(2001). RN [12] RP VARIANT CRBM ARG-420. RX PubMed=12900899; DOI=10.1002/ajmg.a.20226; RA Lo B., Faiyaz-Ul-Haque M., Kennedy S., Aviv R., Tsui L.-C., RA Teebi A.S.; RT "Novel mutation in the gene encoding c-Abl-binding protein SH3BP2 RT causes cherubism."; RL Am. J. Med. Genet. A 121:37-40(2003). RN [13] RP VARIANT CRBM ARG-418. RX PubMed=14577811; DOI=10.1597/1545-1569(2003)040<0632:AMMITS>2.0.CO;2; RA Imai Y., Kanno K., Moriya T., Kayano S., Seino H., Matsubara Y., RA Yamada A.; RT "A missense mutation in the SH3BP2 gene on chromosome 4p16.3 found in RT a case of nonfamilial cherubism."; RL Cleft Palate Craniofac. J. 40:632-638(2003). CC -!- FUNCTION: Binds differentially to the SH3 domains of certain CC proteins of signal transduction pathways. Binds to CC phosphatidylinositols; linking the hemopoietic tyrosine kinase fes CC to the cytoplasmic membrane in a phosphorylation dependent CC mechanism. CC -!- INTERACTION: CC Q9UJU6:DBNL; NbExp=7; IntAct=EBI-727062, EBI-751783; CC P10721:KIT; NbExp=3; IntAct=EBI-727062, EBI-1379503; CC Q96B97:SH3KBP1; NbExp=8; IntAct=EBI-727062, EBI-346595; CC Q9H2K2:TNKS2; NbExp=5; IntAct=EBI-727062, EBI-4398527; CC P15498:VAV1; NbExp=8; IntAct=EBI-727062, EBI-625518; CC P52735:VAV2; NbExp=4; IntAct=EBI-727062, EBI-297549; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Long; CC IsoId=P78314-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P78314-2; Sequence=VSP_004085, VSP_004086; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay; CC Name=3; CC IsoId=P78314-3; Sequence=VSP_043636; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=P78314-4; Sequence=VSP_055046; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in a variety of tissues including CC lung, liver, skeletal muscle, kidney and pancreas. CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-448 may stimulate the CC activity of the LYN kinase (By similarity). CC -!- DISEASE: Cherubism (CRBM) [MIM:118400]: An autosomal dominant CC syndrome characterized by excessive bone degradation of the upper CC and lower jaws, which often begins around three years of age. It CC is followed by development of fibrous tissue masses, which causes CC a characteristic facial swelling. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SIMILARITY: Contains 1 SH2 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF000936; AAB59973.1; -; mRNA. DR EMBL; U56386; AAB72034.1; -; mRNA. DR EMBL; AB000462; BAA19119.1; -; mRNA. DR EMBL; AB000463; BAA19120.1; -; mRNA. DR EMBL; AK299996; BAG61816.1; -; mRNA. DR EMBL; AK312286; BAG35213.1; -; mRNA. DR EMBL; AL121750; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471131; EAW82509.1; -; Genomic_DNA. DR EMBL; CH471131; EAW82510.1; -; Genomic_DNA. DR EMBL; CH471131; EAW82511.1; -; Genomic_DNA. DR EMBL; CH471131; EAW82512.1; -; Genomic_DNA. DR EMBL; BC022996; AAH22996.1; -; mRNA. DR CCDS; CCDS33944.1; -. [P78314-1] DR CCDS; CCDS54715.1; -. [P78314-3] DR RefSeq; NP_001116153.1; NM_001122681.1. [P78314-1] DR RefSeq; NP_001139327.1; NM_001145855.1. [P78314-3] DR RefSeq; NP_001139328.1; NM_001145856.1. DR RefSeq; NP_003014.3; NM_003023.4. [P78314-1] DR RefSeq; XP_005248056.1; XM_005247999.2. [P78314-1] DR UniGene; Hs.167679; -. DR PDB; 2CR4; NMR; -; A=446-558. DR PDB; 3TWR; X-ray; 1.55 A; E/F/G/H=410-425. DR PDBsum; 2CR4; -. DR PDBsum; 3TWR; -. DR ProteinModelPortal; P78314; -. DR SMR; P78314; 27-122, 444-560. DR BioGrid; 112350; 17. DR IntAct; P78314; 19. DR MINT; MINT-254189; -. DR STRING; 9606.ENSP00000348685; -. DR PhosphoSite; P78314; -. DR DMDM; 3023207; -. DR MaxQB; P78314; -. DR PaxDb; P78314; -. DR PRIDE; P78314; -. DR Ensembl; ENST00000356331; ENSP00000348685; ENSG00000087266. [P78314-1] DR Ensembl; ENST00000389838; ENSP00000374488; ENSG00000087266. [P78314-2] DR Ensembl; ENST00000435136; ENSP00000403231; ENSG00000087266. [P78314-1] DR Ensembl; ENST00000442312; ENSP00000388152; ENSG00000087266. [P78314-3] DR Ensembl; ENST00000452765; ENSP00000409746; ENSG00000087266. [P78314-1] DR Ensembl; ENST00000503393; ENSP00000422168; ENSG00000087266. DR Ensembl; ENST00000511747; ENSP00000424846; ENSG00000087266. [P78314-1] DR Ensembl; ENST00000513020; ENSP00000424072; ENSG00000087266. [P78314-2] DR Ensembl; ENST00000515737; ENSP00000422605; ENSG00000087266. [P78314-2] DR GeneID; 6452; -. DR KEGG; hsa:6452; -. DR UCSC; uc003gfi.4; human. [P78314-1] DR UCSC; uc011bvp.2; human. [P78314-3] DR CTD; 6452; -. DR GeneCards; GC04P002831; -. DR GeneReviews; SH3BP2; -. DR HGNC; HGNC:10825; SH3BP2. DR HPA; HPA036790; -. DR MIM; 118400; phenotype. DR MIM; 602104; gene. DR neXtProt; NX_P78314; -. DR Orphanet; 184; Cherubism. DR PharmGKB; PA35733; -. DR eggNOG; NOG42035; -. DR HOVERGEN; HBG000016; -. DR InParanoid; P78314; -. DR KO; K07984; -. DR OMA; DFPRRER; -. DR OrthoDB; EOG7DRJ2X; -. DR PhylomeDB; P78314; -. DR SignaLink; P78314; -. DR ChiTaRS; SH3BP2; human. DR EvolutionaryTrace; P78314; -. DR GenomeRNAi; 6452; -. DR NextBio; 25079; -. DR PRO; PR:P78314; -. DR ArrayExpress; P78314; -. DR Bgee; P78314; -. DR CleanEx; HS_SH3BP2; -. DR Genevestigator; P78314; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc. DR GO; GO:0009967; P:positive regulation of signal transduction; TAS:GOC. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR Gene3D; 2.30.29.30; -; 1. DR Gene3D; 3.30.505.10; -; 1. DR InterPro; IPR011993; PH_like_dom. DR InterPro; IPR001849; Pleckstrin_homology. DR InterPro; IPR000980; SH2. DR Pfam; PF00169; PH; 1. DR Pfam; PF00017; SH2; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00252; SH2; 1. DR SUPFAM; SSF55550; SSF55550; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50001; SH2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; KW Disease mutation; Phosphoprotein; Reference proteome; SH2 domain; KW SH3-binding. FT CHAIN 1 561 SH3 domain-binding protein 2. FT /FTId=PRO_0000064365. FT DOMAIN 26 130 PH. FT DOMAIN 457 555 SH2. FT MOTIF 201 210 SH3-binding. FT COMPBIAS 205 212 Poly-Pro. FT COMPBIAS 236 240 Poly-Pro. FT MOD_RES 174 174 Phosphotyrosine; by SYK (By similarity). FT MOD_RES 183 183 Phosphotyrosine; by SYK (By similarity). FT MOD_RES 278 278 Phosphoserine. FT MOD_RES 448 448 Phosphotyrosine; by SYK (By similarity). FT VAR_SEQ 1 1 M -> MASLGPRTPAPSRSRGRRAMCWVSTISFM (in FT isoform 3). FT /FTId=VSP_043636. FT VAR_SEQ 1 1 M -> MAGSGPRPRSWGRREAGARDEAAAAGGRGPGPCRCS FT QGRRAWIAPGKPAMPAAWTPFM (in isoform 4). FT /FTId=VSP_055046. FT VAR_SEQ 81 97 VMRAAEETTSNNVFPFK -> QPRPQPAQALSQTEAGP FT (in isoform 2). FT /FTId=VSP_004085. FT VAR_SEQ 98 561 Missing (in isoform 2). FT /FTId=VSP_004086. FT VARIANT 415 415 R -> P (in CRBM). FT /FTId=VAR_013257. FT VARIANT 415 415 R -> Q (in CRBM). FT /FTId=VAR_013258. FT VARIANT 418 418 P -> H (in CRBM). FT /FTId=VAR_013259. FT VARIANT 418 418 P -> L (in CRBM). FT /FTId=VAR_013260. FT VARIANT 418 418 P -> R (in CRBM). FT /FTId=VAR_013261. FT VARIANT 420 420 G -> E (in CRBM; dbSNP:rs28938171). FT /FTId=VAR_013262. FT VARIANT 420 420 G -> R (in CRBM; dbSNP:rs28938170). FT /FTId=VAR_013263. FT CONFLICT 27 27 V -> L (in Ref. 3; AAB59973). FT CONFLICT 224 224 H -> N (in Ref. 3; AAB59973). FT CONFLICT 249 249 L -> R (in Ref. 3; AAB59973). FT CONFLICT 251 251 A -> P (in Ref. 3; AAB59973). FT TURN 455 457 FT HELIX 464 474 FT STRAND 485 489 FT STRAND 496 501 FT TURN 503 505 FT STRAND 506 508 FT STRAND 514 516 FT STRAND 519 525 FT STRAND 527 530 FT HELIX 531 538 FT STRAND 544 548 FT STRAND 553 556 SQ SEQUENCE 561 AA; 62244 MW; 69E6846A4F6D8F15 CRC64; MAAEEMHWPV PMKAIGAQNL LTMPGGVAKA GYLHKKGGTQ LQLLKWPLRF VIIHKRCVYY FKSSTSASPQ GAFSLSGYNR VMRAAEETTS NNVFPFKIIH ISKKHRTWFF SASSEEERKS WMALLRREIG HFHEKKDLPL DTSDSSSDTD SFYGAVERPV DISLSPYPTD NEDYEHDDED DSYLEPDSPE PGRLEDALMH PPAYPPPPVP TPRKPAFSDM PRAHSFTSKG PGPLLPPPPP KHGLPDVGLA AEDSKRDPLC PRRAEPCPRV PATPRRMSDP PLSTMPTAPG LRKPPCFRES ASPSPEPWTP GHGACSTSSA AIMATATSRN CDKLKSFHLS PRGPPTSEPP PVPANKPKFL KIAEEDPPRE AAMPGLFVPP VAPRPPALKL PVPEAMARPA VLPRPEKPQL PHLQRSPPDG QSFRSFSFEK PRQPSQADTG GDDSDEDYEK VPLPNSVFVN TTESCEVERL FKATSPRGEP QDGLYCIRNS STKSGKVLVV WDETSNKVRN YRIFEKDSKF YLEGEVLFVS VGSMVEHYHT HVLPSHQSLL LRHPYGYTGP R // ID 3MG_HUMAN Reviewed; 298 AA. AC P29372; G5E9E2; Q13770; Q15275; Q15961; Q5J9I4; Q96BZ6; Q96S33; AC Q9NNX5; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 3. DT 09-JUL-2014, entry version 159. DE RecName: Full=DNA-3-methyladenine glycosylase; DE EC=3.2.2.21; DE AltName: Full=3-alkyladenine DNA glycosylase; DE AltName: Full=3-methyladenine DNA glycosidase; DE AltName: Full=ADPG; DE AltName: Full=N-methylpurine-DNA glycosylase; DE Flags: Precursor; GN Name=MPG; Synonyms=AAG, ANPG, MID1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=1924375; DOI=10.1073/pnas.88.20.9127; RA Samson L., Derfler B., Boosalis M., Call K.; RT "Cloning and characterization of a 3-methyladenine DNA glycosylase RT cDNA from human cells whose gene maps to chromosome 16."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9127-9131(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=8475094; DOI=10.1073/pnas.90.8.3437; RA Vickers M.A., Vyas P., Harris P.C., Simmons D.L., Higgs D.R.; RT "Structure of the human 3-methyladenine DNA glycosylase gene and RT localization close to the 16p telomere."; RL Proc. Natl. Acad. Sci. U.S.A. 90:3437-3441(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RA Kim J.W.; RT "Identification of a human cell proliferation gene 11."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-22; HIS-71; RP VAL-258 AND SER-298. RG NIEHS SNPs program; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., RA Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 RT Mb of the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-298 (ISOFORMS 1/2). RX PubMed=1874728; RA Chakravarti D., Ibeanu G.C., Tano K., Mitra S.; RT "Cloning and expression in Escherichia coli of a human cDNA encoding RT the DNA repair protein N-methylpurine-DNA glycosylase."; RL J. Biol. Chem. 266:15710-15715(1991). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-298 (ISOFORMS 1/2). RX PubMed=1645538; DOI=10.1016/0006-291X(91)90408-Y; RA O'Connor T.R., Laval J.; RT "Human cDNA expressing a functional DNA glycosylase excising 3- RT methyladenine and 7-methylguanine."; RL Biochem. Biophys. Res. Commun. 176:1170-1177(1991). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 230-298 (ISOFORMS 1/2). RX PubMed=8318735; DOI=10.1007/BF00357090; RA Kielman M.F., Smits R., Devi T.S., Fodde R., Bernini L.F.; RT "Homology of a 130-kb region enclosing the alpha-globin gene cluster, RT the alpha-locus controlling region, and two non-globin genes in human RT and mouse."; RL Mamm. Genome 4:314-323(1993). RN [12] RP INTERACTION WITH MBD1. RX PubMed=14555760; DOI=10.1073/pnas.2131819100; RA Watanabe S., Ichimura T., Fujita N., Tsuruzoe S., Ohki I., RA Shirakawa M., Kawasuji M., Nakao M.; RT "Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link RT transcriptional repression and DNA repair in chromatin."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12859-12864(2003). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP SUBCELLULAR LOCATION, INTERACTION WITH SSBP1, AND ENZYME REGULATION. RX PubMed=23290262; DOI=10.1016/j.dnarep.2012.11.009; RA van Loon B., Samson L.D.; RT "Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and RT interacts with mitochondrial single-stranded binding protein RT (mtSSB)."; RL DNA Repair 12:177-187(2013). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 80-199. RX PubMed=9790531; DOI=10.1016/S0092-8674(00)81755-9; RA Lau A.Y., Scharer O.D., Samson L., Verdine G.L., Ellenberger T.; RT "Crystal structure of a human alkylbase-DNA repair enzyme complexed to RT DNA: mechanisms for nucleotide flipping and base excision."; RL Cell 95:249-258(1998). CC -!- FUNCTION: Hydrolysis of the deoxyribose N-glycosidic bond to CC excise 3-methyladenine, and 7-methylguanine from the damaged DNA CC polymer formed by alkylation lesions. CC -!- CATALYTIC ACTIVITY: Hydrolysis of alkylated DNA, releasing 3- CC methyladenine, 3-methylguanine, 7-methylguanine and 7- CC methyladenine. CC -!- ENZYME REGULATION: Binding to SSBP1 in mitochondria inhibits CC glycosylase activity in the context of a single-stranded DNA CC (ssDNA), but not a double-stranded DNA (dsDNA) substrates. CC -!- SUBUNIT: Binds MBD1. Binds SSBP1. CC -!- INTERACTION: CC P04156:PRNP; NbExp=4; IntAct=EBI-1043398, EBI-977302; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion matrix, CC mitochondrion nucleoid. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; CC IsoId=P29372-1; Sequence=Displayed; CC Name=2; CC IsoId=P29372-2; Sequence=VSP_003249, VSP_035485; CC Name=3; CC IsoId=P29372-4; Sequence=VSP_003249; CC Name=4; CC IsoId=P29372-5; Sequence=VSP_046678; CC Note=Gene prediction based on EST data; CC -!- SIMILARITY: Belongs to the DNA glycosylase MPG family. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/mpg/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M74905; AAA58627.1; -; mRNA. DR EMBL; L10752; AAF77073.1; -; mRNA. DR EMBL; AY258284; AAP82229.1; -; mRNA. DR EMBL; AY305873; AAQ95215.1; -; mRNA. DR EMBL; AF499437; AAM14628.1; -; Genomic_DNA. DR EMBL; AE006462; AAK61213.1; -; Genomic_DNA. DR EMBL; Z69720; CAA93540.1; -; Genomic_DNA. DR EMBL; Z69720; CAI95610.1; -; Genomic_DNA. DR EMBL; CH471112; EAW85871.1; -; Genomic_DNA. DR EMBL; BC014991; AAH14991.1; -; mRNA. DR EMBL; S51033; AAB19537.1; -; mRNA. DR EMBL; X56528; CAA39875.1; -; mRNA. DR EMBL; M71215; AAA58369.1; -; mRNA. DR EMBL; M99626; AAB46421.1; -; mRNA. DR CCDS; CCDS32345.1; -. [P29372-4] DR CCDS; CCDS32346.1; -. [P29372-1] DR CCDS; CCDS42087.1; -. [P29372-5] DR PIR; A40798; A40798. DR PIR; A41230; A41230. DR PIR; A47471; A47471. DR PIR; JN0062; JN0062. DR RefSeq; NP_001015052.1; NM_001015052.2. [P29372-4] DR RefSeq; NP_001015054.1; NM_001015054.2. [P29372-5] DR RefSeq; NP_002425.2; NM_002434.3. [P29372-1] DR UniGene; Hs.459596; -. DR PDB; 1BNK; X-ray; 2.70 A; A=80-295. DR PDB; 1EWN; X-ray; 2.10 A; A=80-298. DR PDB; 1F4R; X-ray; 2.40 A; A=80-298. DR PDB; 1F6O; X-ray; 2.40 A; A=80-298. DR PDB; 3QI5; X-ray; 2.20 A; A/B=84-298. DR PDB; 3UBY; X-ray; 2.00 A; A/B=84-298. DR PDBsum; 1BNK; -. DR PDBsum; 1EWN; -. DR PDBsum; 1F4R; -. DR PDBsum; 1F6O; -. DR PDBsum; 3QI5; -. DR PDBsum; 3UBY; -. DR ProteinModelPortal; P29372; -. DR SMR; P29372; 82-293. DR BioGrid; 110490; 56. DR IntAct; P29372; 3. DR MINT; MINT-135511; -. DR STRING; 9606.ENSP00000219431; -. DR PhosphoSite; P29372; -. DR MaxQB; P29372; -. DR PaxDb; P29372; -. DR PRIDE; P29372; -. DR DNASU; 4350; -. DR Ensembl; ENST00000219431; ENSP00000219431; ENSG00000103152. [P29372-1] DR Ensembl; ENST00000356432; ENSP00000348809; ENSG00000103152. [P29372-4] DR Ensembl; ENST00000397817; ENSP00000380918; ENSG00000103152. [P29372-5] DR GeneID; 4350; -. DR KEGG; hsa:4350; -. DR UCSC; uc002cfm.4; human. [P29372-1] DR UCSC; uc002cfo.4; human. DR CTD; 4350; -. DR GeneCards; GC16P000127; -. DR HGNC; HGNC:7211; MPG. DR HPA; HPA006531; -. DR MIM; 156565; gene. DR neXtProt; NX_P29372; -. DR PharmGKB; PA30917; -. DR eggNOG; COG2094; -. DR HOGENOM; HOG000224224; -. DR HOVERGEN; HBG000019; -. DR InParanoid; P29372; -. DR KO; K03652; -. DR OMA; TIYVYPI; -. DR PhylomeDB; P29372; -. DR TreeFam; TF331768; -. DR Reactome; REACT_216; DNA Repair. DR ChiTaRS; MPG; human. DR EvolutionaryTrace; P29372; -. DR GeneWiki; MPG_(gene); -. DR GenomeRNAi; 4350; -. DR NextBio; 17110; -. DR PRO; PR:P29372; -. DR ArrayExpress; P29372; -. DR Bgee; P29372; -. DR CleanEx; HS_MID1; -. DR CleanEx; HS_MPG; -. DR Genevestigator; P29372; -. DR GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc. DR GO; GO:0008725; F:DNA-3-methyladenine glycosylase activity; IEA:UniProtKB-EC. DR GO; GO:0052822; F:DNA-3-methylguanine glycosylase activity; IEA:UniProtKB-EC. DR GO; GO:0052821; F:DNA-7-methyladenine glycosylase activity; IEA:UniProtKB-EC. DR GO; GO:0043916; F:DNA-7-methylguanine glycosylase activity; IEA:UniProtKB-EC. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006284; P:base-excision repair; TAS:Reactome. DR GO; GO:0006285; P:base-excision repair, AP site formation; TAS:Reactome. DR GO; GO:0045007; P:depurination; TAS:Reactome. DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; TAS:ProtInc. DR GO; GO:0006281; P:DNA repair; TAS:Reactome. DR Gene3D; 3.10.300.10; -; 1. DR HAMAP; MF_00527; 3MGH; 1. DR InterPro; IPR011034; Formyl_transferase_C-like. DR InterPro; IPR003180; PurDNA_glycsylse. DR PANTHER; PTHR10429; PTHR10429; 1. DR Pfam; PF02245; Pur_DNA_glyco; 1. DR SUPFAM; SSF50486; SSF50486; 1. DR TIGRFAMs; TIGR00567; 3mg; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW DNA damage; DNA repair; Hydrolase; Mitochondrion; KW Mitochondrion nucleoid; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Transit peptide. FT TRANSIT 1 17 Mitochondrion (Potential). FT CHAIN 18 298 DNA-3-methyladenine glycosylase. FT /FTId=PRO_0000100065. FT MOD_RES 78 78 Phosphoserine. FT VAR_SEQ 1 17 Missing (in isoform 4). FT /FTId=VSP_046678. FT VAR_SEQ 1 12 MVTPALQMKKPK -> MPARSGA (in isoform 2 and FT isoform 3). FT /FTId=VSP_003249. FT VAR_SEQ 195 196 QL -> HV (in isoform 2). FT /FTId=VSP_035485. FT VARIANT 22 22 K -> Q (in dbSNP:rs3176383). FT /FTId=VAR_019138. FT VARIANT 64 64 P -> L (in dbSNP:rs2308315). FT /FTId=VAR_014831. FT VARIANT 71 71 Y -> H (in dbSNP:rs2266607). FT /FTId=VAR_014832. FT VARIANT 93 93 Q -> R (in dbSNP:rs25671). FT /FTId=VAR_050096. FT VARIANT 120 120 R -> C (in dbSNP:rs2308313). FT /FTId=VAR_014833. FT VARIANT 141 141 R -> Q (in dbSNP:rs2308312). FT /FTId=VAR_014834. FT VARIANT 258 258 A -> V (in dbSNP:rs769193). FT /FTId=VAR_014835. FT VARIANT 298 298 A -> S (in dbSNP:rs2234949). FT /FTId=VAR_014836. FT CONFLICT 13 13 Q -> QV (in Ref. 5; AAK61213). FT CONFLICT 29 31 GQP -> ARA (in Ref. 9; AAB19537). FT CONFLICT 44 44 Q -> R (in Ref. 9; AAB19537). FT CONFLICT 69 71 GPY -> SKD (in Ref. 10; AAA58369/ FT CAA39875). FT CONFLICT 82 82 H -> L (in Ref. 10; AAA58369/CAA39875). FT CONFLICT 134 134 A -> P (in Ref. 1; AAA58627). FT CONFLICT 287 287 V -> E (in Ref. 10; AAA58369). FT HELIX 82 84 FT HELIX 88 91 FT HELIX 95 101 FT TURN 102 104 FT STRAND 106 110 FT STRAND 116 127 FT STRAND 129 131 FT HELIX 138 140 FT HELIX 145 150 FT STRAND 155 161 FT TURN 162 164 FT STRAND 165 171 FT STRAND 178 188 FT HELIX 190 199 FT HELIX 211 213 FT STRAND 214 217 FT HELIX 218 224 FT HELIX 229 231 FT TURN 236 238 FT STRAND 240 245 FT HELIX 253 255 FT STRAND 256 259 FT TURN 268 272 FT STRAND 276 279 FT TURN 290 292 SQ SEQUENCE 298 AA; 32869 MW; BEA8C4CB250D572B CRC64; MVTPALQMKK PKQFCRRMGQ KKQRPARAGQ PHSSSDAAQA PAEQPHSSSD AAQAPCPRER CLGPPTTPGP YRSIYFSSPK GHLTRLGLEF FDQPAVPLAR AFLGQVLVRR LPNGTELRGR IVETEAYLGP EDEAAHSRGG RQTPRNRGMF MKPGTLYVYI IYGMYFCMNI SSQGDGACVL LRALEPLEGL ETMRQLRSTL RKGTASRVLK DRELCSGPSK LCQALAINKS FDQRDLAQDE AVWLERGPLE PSEPAVVAAA RVGVGHAGEW ARKPLRFYVR GSPWVSVVDR VAEQDTQA // ID 41_HUMAN Reviewed; 864 AA. AC P11171; B1ALH8; B1ALH9; D3DPM9; D3DPN0; P11176; Q14245; Q5TB35; AC Q5VXN8; Q8IXV9; Q9Y578; Q9Y579; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 4. DT 09-JUL-2014, entry version 172. DE RecName: Full=Protein 4.1; DE Short=P4.1; DE AltName: Full=4.1R; DE AltName: Full=Band 4.1; DE AltName: Full=EPB4.1; GN Name=EPB41; Synonyms=E41P; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND PROTEIN SEQUENCE OF RP 378-393. RC TISSUE=Reticulocyte; RX PubMed=3467321; DOI=10.1073/pnas.83.24.9512; RA Conboy J.G., Kan Y.W., Shohet S.B., Mohandas N.; RT "Molecular cloning of protein 4.1, a major structural element of the RT human erythrocyte membrane skeleton."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9512-9516(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6). RX PubMed=3223413; RA Tang T.K., Leto T.L., Marchesi V.T., Benz E.J. Jr.; RT "Expression of specific isoforms of protein 4.1 in erythroid and non- RT erythroid tissues."; RL Adv. Exp. Med. Biol. 241:81-95(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6). RX PubMed=3375238; DOI=10.1073/pnas.85.11.3713; RA Tang T.K., Leto T.L., Correas I., Alonso M.A., Marchesi V.T., RA Benz E.J. Jr.; RT "Selective expression of an erythroid-specific isoform of protein RT 4.1."; RL Proc. Natl. Acad. Sci. U.S.A. 85:3713-3717(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX PubMed=2022644; RA Conboy J.G., Chan J.Y.C., Chasis J.A., Kan Y.W., Mohandas N.; RT "Tissue- and development-specific alternative RNA splicing regulates RT expression of multiple isoforms of erythroid membrane protein 4.1."; RL J. Biol. Chem. 266:8273-8280(1991). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Huang S.C., Wang C., Lichtenauer U., Vortmeyer A., Zhuang Z.; RT "Sequence of protein 4.1 from a human neuroblastoma cell line: LAN5."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 157-227, AND VARIANT ILE-214. RA Lichtenauer U., Huang S.C., Vortmeyer A., Zhuang Z.; RT "Valine to isoleucine polymorphism in exon 4 of human protein 4.1."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE OF 669-864 (ISOFORM 4), AND ALTERNATIVE SPLICING. RX PubMed=3194408; DOI=10.1073/pnas.85.23.9062; RA Conboy J.G., Chan J., Mohandas N., Kan Y.W.; RT "Multiple protein 4.1 isoforms produced by alternative splicing in RT human erythroid cells."; RL Proc. Natl. Acad. Sci. U.S.A. 85:9062-9065(1988). RN [11] RP PROTEIN SEQUENCE OF 534-541; 693-701 AND 793-794, AND PHOSPHORYLATION RP AT SER-540 AND SER-709. RX PubMed=2171679; DOI=10.1016/0167-4889(90)90095-U; RA Horne W.C., Prinz W.C., Tang E.K.; RT "Identification of two cAMP-dependent phosphorylation sites on RT erythrocyte protein 4.1."; RL Biochim. Biophys. Acta 1055:87-92(1990). RN [12] RP PROTEIN SEQUENCE OF 648-714. RX PubMed=3531202; RA Correas I., Speicher D.W., Marchesi V.T.; RT "Structure of the spectrin-actin binding site of erythrocyte protein RT 4.1."; RL J. Biol. Chem. 261:13362-13366(1986). RN [13] RP STRUCTURE OF CARBOHYDRATES. RX PubMed=2808371; RA Inaba M., Maede Y.; RT "O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple RT protein 4.1 isoforms regulated by alternative pathways."; RL J. Biol. Chem. 264:18149-18155(1989). RN [14] RP PHOSPHORYLATION AT TYR-660 BY EGFR. RX PubMed=1647028; DOI=10.1073/pnas.88.12.5222; RA Subrahmanyan G., Bertics P.J., Anderson R.A.; RT "Phosphorylation of protein 4.1 on tyrosine-418 modulates its function RT in vitro."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5222-5226(1991). RN [15] RP INTERACTION WITH DLG1. RX PubMed=7937897; DOI=10.1073/pnas.91.21.9818; RA Lue R.A., Marfatia S.M., Branton D., Chishti A.H.; RT "Cloning and characterization of hdlg: the human homologue of the RT Drosophila discs large tumor suppressor binds to protein 4.1."; RL Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994). RN [16] RP INTERACTION WITH CALMODULIN. RX PubMed=10692436; DOI=10.1074/jbc.275.9.6360; RA Nunomura W., Takakuwa Y., Parra M., Conboy J.G., Mohandas N.; RT "Ca(2+)-dependent and Ca(2+)-independent calmodulin binding sites in RT erythrocyte protein 4.1. Implications for regulation of protein 4.1 RT interactions with transmembrane proteins."; RL J. Biol. Chem. 275:6360-6367(2000). RN [17] RP INTERACTION WITH CENPJ. RX PubMed=11003675; DOI=10.1128/MCB.20.20.7813-7825.2000; RA Hung L.-Y., Tang C.J., Tang T.K.; RT "Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) RT which is associated with the gamma-tubulin complex."; RL Mol. Cell. Biol. 20:7813-7825(2000). RN [18] RP CHARACTERIZATION OF C-TERMINAL DOMAIN. RX PubMed=11432737; DOI=10.1046/j.1432-1327.2001.02276.x; RA Scott C., Phillips G.W., Baines A.J.; RT "Properties of the C-terminal domain of 4.1 proteins."; RL Eur. J. Biochem. 268:3709-3717(2001). RN [19] RP SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING. RX PubMed=12427749; DOI=10.1074/jbc.M201521200; RA Luque C.M., Perez-Ferreiro C.M., Perez-Gonzalez A., Englmeier L., RA Koffa M.D., Correas I.; RT "An alternative domain containing a leucine-rich sequence regulates RT nuclear cytoplasmic localization of protein 4.1R."; RL J. Biol. Chem. 278:2686-2691(2003). RN [20] RP MUTAGENESIS OF THR-60 AND SER-712, AND PHOSPHORYLATION AT THR-60 AND RP SER-712. RX PubMed=15525677; DOI=10.1091/mbc.E04-05-0426; RA Huang S.-C., Liu E.S., Chan S.-H., Munagala I.D., Cho H.T., RA Jagadeeswaran R., Benz E.J. Jr.; RT "Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 RT kinase."; RL Mol. Biol. Cell 16:117-127(2005). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-191; SER-555 RP AND SER-712, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-85; SER-188 AND RP SER-712, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-149; SER-151 AND RP SER-152, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 210-488. RX PubMed=11017195; DOI=10.1038/82819; RA Han B.-G., Nunomura W., Takakuwa Y., Mohandas N., Jap B.K.; RT "Protein 4.1R core domain structure and insights into regulation of RT cytoskeletal organization."; RL Nat. Struct. Biol. 7:871-875(2000). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes. CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin, CENPJ and DLG1. Also found to CC associate with contractile apparatus and tight junctions. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell CC cortex. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=P11171-1; Sequence=Displayed; CC Name=2; CC IsoId=P11171-2; Sequence=VSP_000470; CC Name=3; CC IsoId=P11171-3; Sequence=VSP_000468, VSP_000471; CC Name=4; Synonyms=Erythroid; CC IsoId=P11171-4; Sequence=VSP_000468, VSP_000470, VSP_000473; CC Name=5; Synonyms=Non-erythroid A; CC IsoId=P11171-5; Sequence=VSP_000469, VSP_000470, VSP_000472; CC Name=6; Synonyms=Non-erythroid B; CC IsoId=P11171-6; Sequence=VSP_000468, VSP_000469, VSP_000470, CC VSP_000472; CC Name=7; CC IsoId=P11171-7; Sequence=VSP_000471, VSP_012872, VSP_012873; CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions. CC -!- PTM: Phosphorylation on Tyr-660 reduces the ability of 4.1 to CC promote the assembly of the spectrin/actin/4.1 ternary complex. CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in CC the C-terminal domain. CC -!- DISEASE: Elliptocytosis 1 (EL1) [MIM:611804]: A Rhesus-linked form CC of hereditary elliptocytosis, a genetically heterogeneous, CC autosomal dominant hematologic disorder. It is characterized by CC variable hemolytic anemia and elliptical or oval red cell shape. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Hereditary pyropoikilocytosis (HPP) [MIM:266140]: CC Autosomal recessive hematologic disorder characterized by CC hemolytic anemia, microspherocytosis, poikilocytosis, and an CC unusual thermal sensitivity of red cells. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Contains 1 FERM domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M14993; AAA35795.1; -; mRNA. DR EMBL; J03796; AAA35793.1; -; mRNA. DR EMBL; J03796; AAA35794.1; -; mRNA. DR EMBL; M61733; AAA35797.1; -; mRNA. DR EMBL; AF156225; AAD42222.1; -; mRNA. DR EMBL; AL138785; CAI21967.1; -; Genomic_DNA. DR EMBL; AL357500; CAI21967.1; JOINED; Genomic_DNA. DR EMBL; AL138785; CAI21966.1; -; Genomic_DNA. DR EMBL; AL357500; CAI21966.1; JOINED; Genomic_DNA. DR EMBL; AL138785; CAI21968.1; -; Genomic_DNA. DR EMBL; AL138785; CAI21969.1; -; Genomic_DNA. DR EMBL; AL357500; CAI21969.1; JOINED; Genomic_DNA. DR EMBL; AL138785; CAI21970.1; -; Genomic_DNA. DR EMBL; AL357500; CAI21970.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71636.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71636.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71637.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71637.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71638.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71638.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71639.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71639.1; JOINED; Genomic_DNA. DR EMBL; CH471059; EAX07663.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07665.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07667.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07668.1; -; Genomic_DNA. DR EMBL; BC039079; AAH39079.1; -; mRNA. DR EMBL; AF156226; AAD42223.1; -; Genomic_DNA. DR CCDS; CCDS330.1; -. [P11171-5] DR CCDS; CCDS331.1; -. [P11171-4] DR CCDS; CCDS332.1; -. [P11171-3] DR CCDS; CCDS53288.1; -. [P11171-1] DR CCDS; CCDS53289.1; -. [P11171-7] DR PIR; A39810; MMHUE4. DR RefSeq; NP_001159477.1; NM_001166005.1. [P11171-1] DR RefSeq; NP_001159478.1; NM_001166006.1. [P11171-7] DR RefSeq; NP_004428.1; NM_004437.3. [P11171-4] DR RefSeq; NP_976217.1; NM_203342.2. [P11171-3] DR RefSeq; XP_005245818.1; XM_005245761.1. [P11171-1] DR RefSeq; XP_005245821.1; XM_005245764.1. [P11171-2] DR UniGene; Hs.175437; -. DR UniGene; Hs.708933; -. DR UniGene; Hs.712722; -. DR PDB; 1GG3; X-ray; 2.80 A; A/B/C=210-488. DR PDB; 2RQ1; NMR; -; A=292-396. DR PDB; 3QIJ; X-ray; 1.80 A; A/B=211-488. DR PDBsum; 1GG3; -. DR PDBsum; 2RQ1; -. DR PDBsum; 3QIJ; -. DR DisProt; DP00678; -. DR ProteinModelPortal; P11171; -. DR SMR; P11171; 208-519. DR BioGrid; 108349; 24. DR DIP; DIP-17032N; -. DR IntAct; P11171; 5. DR MINT; MINT-1208648; -. DR TCDB; 8.A.25.1.2; the ezrin/radixin/moesin (ezrin) family. DR PhosphoSite; P11171; -. DR UniCarbKB; P11171; -. DR DMDM; 90101808; -. DR MaxQB; P11171; -. DR PaxDb; P11171; -. DR PRIDE; P11171; -. DR DNASU; 2035; -. DR Ensembl; ENST00000343067; ENSP00000345259; ENSG00000159023. [P11171-1] DR Ensembl; ENST00000347529; ENSP00000290100; ENSG00000159023. [P11171-5] DR Ensembl; ENST00000349460; ENSP00000317597; ENSG00000159023. [P11171-3] DR Ensembl; ENST00000356093; ENSP00000348397; ENSG00000159023. [P11171-2] DR Ensembl; ENST00000373797; ENSP00000362903; ENSG00000159023. [P11171-7] DR Ensembl; ENST00000373798; ENSP00000362904; ENSG00000159023. [P11171-1] DR Ensembl; ENST00000373800; ENSP00000362906; ENSG00000159023. [P11171-4] DR GeneID; 2035; -. DR KEGG; hsa:2035; -. DR UCSC; uc001brg.2; human. [P11171-3] DR UCSC; uc001brh.2; human. [P11171-4] DR UCSC; uc001bri.2; human. [P11171-5] DR UCSC; uc001brk.3; human. [P11171-7] DR UCSC; uc001brl.2; human. [P11171-2] DR UCSC; uc001brm.2; human. [P11171-1] DR UCSC; uc009vtm.2; human. [P11171-6] DR CTD; 2035; -. DR GeneCards; GC01P029213; -. DR HGNC; HGNC:3377; EPB41. DR HPA; HPA028414; -. DR MIM; 130500; gene. DR MIM; 266140; phenotype. DR MIM; 611804; phenotype. DR neXtProt; NX_P11171; -. DR Orphanet; 98864; Common hereditary elliptocytosis. DR Orphanet; 98865; Homozygous hereditary elliptocytosis. DR PharmGKB; PA27810; -. DR eggNOG; NOG242913; -. DR HOVERGEN; HBG007777; -. DR InParanoid; P11171; -. DR KO; K06107; -. DR OMA; HEDLTKN; -. DR OrthoDB; EOG7Z69BP; -. DR PhylomeDB; P11171; -. DR TreeFam; TF351626; -. DR ChiTaRS; EPB41; human. DR EvolutionaryTrace; P11171; -. DR GeneWiki; EPB41; -. DR GenomeRNAi; 2035; -. DR NextBio; 8259; -. DR PMAP-CutDB; B1ALH9; -. DR PRO; PR:P11171; -. DR ArrayExpress; P11171; -. DR Bgee; P11171; -. DR CleanEx; HS_EPB41; -. DR Genevestigator; P11171; -. DR GO; GO:0030863; C:cortical cytoskeleton; IDA:UniProtKB. DR GO; GO:0019898; C:extrinsic component of membrane; IEA:InterPro. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0043234; C:protein complex; IDA:UniProtKB. DR GO; GO:0008091; C:spectrin; TAS:ProtInc. DR GO; GO:0014731; C:spectrin-associated cytoskeleton; TAS:BHF-UCL. DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0030507; F:spectrin binding; TAS:BHF-UCL. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc. DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB. DR GO; GO:0008015; P:blood circulation; TAS:ProtInc. DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro. DR GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL. DR Gene3D; 1.20.80.10; -; 1. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR008379; Band_4.1_C. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR019750; Band_41_fam. DR InterPro; IPR021187; Band_41_protein. DR InterPro; IPR000798; Ez/rad/moesin_like. DR InterPro; IPR014847; FERM-adjacent. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR019747; FERM_CS. DR InterPro; IPR000299; FERM_domain. DR InterPro; IPR018979; FERM_N. DR InterPro; IPR018980; FERM_PH-like_C. DR InterPro; IPR011993; PH_like_dom. DR InterPro; IPR007477; SAB_dom. DR InterPro; IPR029071; Ubiquitin-rel_dom. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF08736; FA; 1. DR Pfam; PF09380; FERM_C; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF09379; FERM_N; 1. DR Pfam; PF04382; SAB; 1. DR PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR SUPFAM; SSF47031; SSF47031; 1. DR SUPFAM; SSF54236; SSF54236; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Actin-binding; Alternative splicing; Calmodulin-binding; KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW Elliptocytosis; Glycoprotein; Hereditary hemolytic anemia; Nucleus; KW Phosphoprotein; Polymorphism; Pyropoikilocytosis; Reference proteome. FT CHAIN 1 864 Protein 4.1. FT /FTId=PRO_0000219390. FT DOMAIN 210 491 FERM. FT REGION 494 614 Hydrophilic. FT REGION 615 713 Spectrin--actin-binding. FT REGION 714 864 C-terminal (CTD). FT MOD_RES 14 14 Phosphoserine. FT MOD_RES 60 60 Phosphothreonine; by CDK1. FT MOD_RES 84 84 Phosphoserine. FT MOD_RES 85 85 Phosphoserine. FT MOD_RES 149 149 Phosphoserine. FT MOD_RES 151 151 Phosphoserine. FT MOD_RES 152 152 Phosphoserine. FT MOD_RES 188 188 Phosphoserine. FT MOD_RES 191 191 Phosphoserine. FT MOD_RES 222 222 Phosphotyrosine (By similarity). FT MOD_RES 540 540 Phosphoserine. FT MOD_RES 542 542 Phosphoserine (By similarity). FT MOD_RES 555 555 Phosphoserine. FT MOD_RES 660 660 Phosphotyrosine; by EGFR. FT MOD_RES 709 709 Phosphoserine. FT MOD_RES 712 712 Phosphoserine; by CDK1. FT VAR_SEQ 1 209 Missing (in isoform 3, isoform 4 and FT isoform 6). FT /FTId=VSP_000468. FT VAR_SEQ 228 262 Missing (in isoform 5 and isoform 6). FT /FTId=VSP_000469. FT VAR_SEQ 616 648 Missing (in isoform 2, isoform 4, isoform FT 5 and isoform 6). FT /FTId=VSP_000470. FT VAR_SEQ 635 648 Missing (in isoform 3 and isoform 7). FT /FTId=VSP_000471. FT VAR_SEQ 649 669 Missing (in isoform 5 and isoform 6). FT /FTId=VSP_000472. FT VAR_SEQ 729 734 PPLVKT -> VSTLST (in isoform 7). FT /FTId=VSP_012872. FT VAR_SEQ 735 864 Missing (in isoform 7). FT /FTId=VSP_012873. FT VAR_SEQ 772 805 Missing (in isoform 4). FT /FTId=VSP_000473. FT VARIANT 214 214 V -> I (in dbSNP:rs111642750). FT /FTId=VAR_009122. FT MUTAGEN 60 60 T->A: Loss of CDK1-mediated FT phosphorylation. Abolishes targeting onto FT the mitotic spindle; when associated with FT A-712. FT MUTAGEN 712 712 S->A: Loss of CDK1-mediated FT phosphorylation. Abolishes targeting onto FT the mitotic spindle; when associated with FT A-60. FT CONFLICT 51 51 Q -> H (in Ref. 5; AAD42222). FT CONFLICT 76 76 S -> N (in Ref. 5; AAD42222). FT CONFLICT 168 168 F -> S (in Ref. 9; AAD42223). FT CONFLICT 259 259 A -> T (in Ref. 5; AAD42222). FT CONFLICT 665 665 N -> S (in Ref. 5; AAD42222). FT CONFLICT 669 669 E -> K (in Ref. 10; no nucleotide entry). FT CONFLICT 679 679 K -> E (in Ref. 5; AAD42222). FT CONFLICT 802 802 Q -> K (in Ref. 2; no nucleotide entry FT and 3; AAA35793/AAA35794). FT CONFLICT 852 852 K -> L (in Ref. 10; no nucleotide entry). FT CONFLICT 863 863 D -> E (in Ref. 10; no nucleotide entry). FT STRAND 211 215 FT STRAND 221 225 FT HELIX 232 243 FT HELIX 248 250 FT STRAND 251 258 FT STRAND 261 264 FT HELIX 271 274 FT TURN 275 277 FT STRAND 281 288 FT HELIX 293 295 FT HELIX 299 314 FT HELIX 322 337 FT HELIX 342 345 FT HELIX 350 352 FT STRAND 356 358 FT HELIX 361 372 FT HELIX 379 390 FT TURN 394 397 FT STRAND 399 404 FT STRAND 410 415 FT STRAND 417 424 FT STRAND 427 433 FT HELIX 434 436 FT STRAND 437 443 FT STRAND 446 451 FT STRAND 454 458 FT STRAND 461 466 FT HELIX 470 486 SQ SEQUENCE 864 AA; 97017 MW; B466E7A9D7FBF12B CRC64; MTTEKSLVTE AENSQHQQKE EGEEAINSGQ QEPQQEESCQ TAAEGDNWCE QKLKASNGDT PTHEDLTKNK ERTSESRGLS RLFSSFLKRP KSQVSEEEGK EVESDKEKGE GGQKEIEFGT SLDEEIILKA PIAAPEPELK TDPSLDLHSL SSAETQPAQE ELREDPDFEI KEGEGLEECS KIEVKEESPQ SKAETELKAS QKPIRKHRNM HCKVSLLDDT VYECVVEKHA KGQDLLKRVC EHLNLLEEDY FGLAIWDNAT SKTWLDSAKE IKKQVRGVPW NFTFNVKFYP PDPAQLTEDI TRYYLCLQLR QDIVAGRLPC SFATLALLGS YTIQSELGDY DPELHGVDYV SDFKLAPNQT KELEEKVMEL HKSYRSMTPA QADLEFLENA KKLSMYGVDL HKAKDLEGVD IILGVCSSGL LVYKDKLRIN RFPWPKVLKI SYKRSSFFIK IRPGEQEQYE STIGFKLPSY RAAKKLWKVC VEHHTFFRLT STDTIPKSKF LALGSKFRYS GRTQAQTRQA SALIDRPAPH FERTASKRAS RSLDGAAAVD SADRSPRPTS APAITQGQVA EGGVLDASAK KTVVPKAQKE TVKAEVKKED EPPEQAEPEP TEAWKVEKTH IEVTVPTSNG DQTQKLAEKT EDLIRMRKKK RERLDGENIY IRHSNLMLED LDKSQEEIKK HHASISELKK NFMESVPEPR PSEWDKRLST HSPFRTLNIN GQIPTGEGPP LVKTQTVTIS DNANAVKSEI PTKDVPIVHT ETKTITYEAA QTDDNSGDLD PGVLLTAQTI TSETPSSTTT TQITKTVKGG ISETRIEKRI VITGDADIDH DQVLVQAIKE AKEQHPDMSV TKVVVHQETE IADE // ID 4EBP1_HUMAN Reviewed; 118 AA. AC Q13541; B2R502; D3DSW8; Q6IBN3; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-JUL-2014, entry version 136. DE RecName: Full=Eukaryotic translation initiation factor 4E-binding protein 1; DE Short=4E-BP1; DE Short=eIF4E-binding protein 1; DE AltName: Full=Phosphorylated heat- and acid-stable protein regulated by insulin 1; DE Short=PHAS-I; GN Name=EIF4EBP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EIF4E, AND RP PHOSPHORYLATION. RC TISSUE=Placenta; RX PubMed=7935836; DOI=10.1038/371762a0; RA Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., RA Lawrence J.C. Jr., Sonenberg N.; RT "Insulin-dependent stimulation of protein synthesis by phosphorylation RT of a regulator of 5'-cap function."; RL Nature 371:762-767(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Ito M., Shichijo S., Tsuda N., Ochi M., Harashima N., Saito N., RA Itoh K.; RT "Identification of multiple genes and immunogenic epitopes of RT pancreatic cancer cells."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 2-13, AND ACETYLATION AT SER-2. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [9] RP INTERACTION WITH EIF4E AND EIF4G. RX PubMed=8521827; RA Haghighat A., Mader S., Pause A., Sonenberg N.; RT "Repression of cap-dependent translation by 4E-binding protein 1: RT competition with p220 for binding to eukaryotic initiation factor- RT 4E."; RL EMBO J. 14:5701-5709(1995). RN [10] RP PHOSPHORYLATION BY MTOR. RX PubMed=9465032; DOI=10.1073/pnas.95.4.1432; RA Burnett P.E., Barrow R.K., Cohen N.A., Snyder S.H., Sabatini D.M.; RT "RAFT1 phosphorylation of the translational regulators p70 S6 kinase RT and 4E-BP1."; RL Proc. Natl. Acad. Sci. U.S.A. 95:1432-1437(1998). RN [11] RP INTERACTION WITH RPTOR. RX PubMed=12150926; DOI=10.1016/S0092-8674(02)00833-4; RA Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S., RA Tokunaga C., Avruch J., Yonezawa K.; RT "Raptor, a binding partner of target of rapamycin (TOR), mediates TOR RT action."; RL Cell 110:177-189(2002). RN [12] RP INTERACTION WITH RPTOR, AND PHOSPHORYLATION AT THR-37; THR-46; SER-65 RP AND THR-70 BY MTOR. RX PubMed=12747827; DOI=10.1016/S0960-9822(03)00329-4; RA Schalm S.S., Fingar D.C., Sabatini D.M., Blenis J.; RT "TOS motif-mediated raptor binding regulates 4E-BP1 multisite RT phosphorylation and function."; RL Curr. Biol. 13:797-806(2003). RN [13] RP PHOSPHORYLATION AT SER-65; SER-101 AND SER-112, PROTEIN SEQUENCE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12588975; DOI=10.1128/MCB.23.5.1546-1557.2003; RA Wang X., Li W., Parra J.L., Beugnet A., Proud C.G.; RT "The C terminus of initiation factor 4E-binding protein 1 contains RT multiple regulatory features that influence its function and RT phosphorylation."; RL Mol. Cell. Biol. 23:1546-1557(2003). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate RT cancer cells: identification of phosphoproteins in the LNCaP cell RT line."; RL Electrophoresis 28:2027-2034(2007). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-50; THR-70 AND SER-101, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; THR-41; THR-46; RP THR-50; TYR-54; SER-65; THR-70 AND SER-83, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND THR-46, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37 AND THR-70, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70 AND SER-112, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [24] RP FUNCTION, INTERACTION WITH EIF4E, UBIQUITINATION AT LYS-57, RP PHOSPHORYLATION AT THR-37; THR-46; SER-65 AND THR-70, AND MUTAGENESIS RP OF THR-37; THR-46; LYS-57; 59-LEU-MET-60; SER-65; LYS-69; THR-70 AND RP LYS-105. RX PubMed=22578813; DOI=10.1016/j.molcel.2012.04.004; RA Yanagiya A., Suyama E., Adachi H., Svitkin Y.V., Aza-Blanc P., RA Imataka H., Mikami S., Martineau Y., Ronai Z.A., Sonenberg N.; RT "Translational homeostasis via the mRNA cap-binding protein, eIF4E."; RL Mol. Cell 46:847-858(2012). RN [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [26] RP STRUCTURE BY NMR OF 4-118. RX PubMed=9684899; DOI=10.1002/pro.5560070720; RA Fletcher C.M., Wagner G.; RT "The interaction of eIF4E with 4E-BP1 is an induced fit to a RT completely disordered protein."; RL Protein Sci. 7:1639-1642(1998). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-70 IN COMPLEX WITH EIF4E RP AND MRNA CAP ANALOG. RX PubMed=16271312; DOI=10.1016/j.bbapap.2005.07.023; RA Tomoo K., Matsushita Y., Fujisaki H., Abiko F., Shen X., Taniguchi T., RA Miyagawa H., Kitamura K., Miura K., Ishida T.; RT "Structural basis for mRNA cap-binding regulation of eukaryotic RT initiation factor 4E by 4E-binding protein, studied by spectroscopic, RT X-ray crystal structural, and molecular dynamics simulation methods."; RL Biochim. Biophys. Acta 1753:191-208(2005). RN [28] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 51-67 IN COMPLEX WITH EIF4E2 RP AND MRNA CAP ANALOG. RX PubMed=17368478; DOI=10.1016/j.jmb.2007.02.019; RA Rosettani P., Knapp S., Vismara M.-G., Rusconi L., Cameron A.D.; RT "Structures of the human eIF4E homologous protein, h4EHP, in its RT m7GTP-bound and unliganded forms."; RL J. Mol. Biol. 368:691-705(2007). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 51-64 IN COMPLEX WITH EIF4E RP AND MRNA CAP ANALOG. RX PubMed=17631896; DOI=10.1016/j.jmb.2007.06.033; RA Brown C.J., McNae I., Fischer P.M., Walkinshaw M.D.; RT "Crystallographic and mass spectrometric characterisation of eIF4E RT with N7-alkylated cap derivatives."; RL J. Mol. Biol. 372:7-15(2007). CC -!- FUNCTION: Regulates eIF4E activity by preventing its assembly into CC the eIF4F complex: hypophosphorylated form competes with CC EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress CC translation. Mediates the regulation of protein translation by CC hormones, growth factors and other stimuli that signal through the CC MAP kinase and mTORC1 pathways. CC -!- SUBUNIT: Hypophosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 CC to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and CC MAPK3) or mTORC1 phosphorylation of EIF4EBP1 causes dissociation CC of the complex allowing EIF4G1/EIF4G3 to bind and consequent CC initiation of translation. Interacts with RPTOR. CC -!- INTERACTION: CC Q9UKV8:AGO2; NbExp=2; IntAct=EBI-74090, EBI-528269; CC P06730:EIF4E; NbExp=8; IntAct=EBI-74090, EBI-73440; CC P42345:MTOR; NbExp=2; IntAct=EBI-74090, EBI-359260; CC Q9JLN9:Mtor (xeno); NbExp=2; IntAct=EBI-74090, EBI-1571628; CC Q8N122:RPTOR; NbExp=5; IntAct=EBI-74090, EBI-1567928; CC -!- PTM: Phosphorylated on serine and threonine residues in response CC to insulin, EGF and PDGF. Phosphorylation at Thr-37, Thr-46, Ser- CC 65 and Thr-70, corresponding to the hyperphosphorylated form, is CC regulated by mTORC1 and abolishes binding to EIF4E. CC -!- PTM: Ubiquitinated: when eIF4E levels are low, hypophosphorylated CC form is ubiquitinated by the BCR(KLHL25) complex, leading to its CC degradation and serving as a homeostatic mechanism to maintain CC translation and prevent eIF4E inhibition when eIF4E levels are CC low. Not ubiquitinated when hyperphosphorylated (at Thr-37, Thr- CC 46, Ser-65 and Thr-70) or associated with eIF4E. CC -!- SIMILARITY: Belongs to the eIF4E-binding protein family. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/EIF4EBP1ID40432ch8p12.html"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L36055; AAA62269.1; -; mRNA. DR EMBL; AB044548; BAB18650.1; -; mRNA. DR EMBL; BT007162; AAP35826.1; -; mRNA. DR EMBL; CR456769; CAG33050.1; -; mRNA. DR EMBL; AK312011; BAG34949.1; -; mRNA. DR EMBL; CH471080; EAW63341.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63342.1; -; Genomic_DNA. DR EMBL; BC004459; AAH04459.1; -; mRNA. DR EMBL; BC058073; AAH58073.1; -; mRNA. DR CCDS; CCDS6100.1; -. DR PIR; S50866; S50866. DR RefSeq; NP_004086.1; NM_004095.3. DR UniGene; Hs.411641; -. DR PDB; 1EJ4; X-ray; 2.25 A; B=51-64. DR PDB; 1WKW; X-ray; 2.10 A; B=47-66. DR PDB; 2JGB; X-ray; 1.70 A; B=51-67. DR PDB; 2JGC; X-ray; 2.40 A; B=51-67. DR PDB; 2V8W; X-ray; 2.30 A; B/F=51-64. DR PDB; 2V8X; X-ray; 2.30 A; B/F=51-64. DR PDB; 2V8Y; X-ray; 2.10 A; B/F=51-64. DR PDB; 3HXG; X-ray; 2.10 A; C=51-67. DR PDB; 3HXI; X-ray; 1.80 A; C=51-67. DR PDB; 3M93; X-ray; 2.90 A; C=51-67. DR PDB; 3M94; X-ray; 2.05 A; C=51-67. DR PDB; 3U7X; X-ray; 2.10 A; C/D=47-66. DR PDBsum; 1EJ4; -. DR PDBsum; 1WKW; -. DR PDBsum; 2JGB; -. DR PDBsum; 2JGC; -. DR PDBsum; 2V8W; -. DR PDBsum; 2V8X; -. DR PDBsum; 2V8Y; -. DR PDBsum; 3HXG; -. DR PDBsum; 3HXI; -. DR PDBsum; 3M93; -. DR PDBsum; 3M94; -. DR PDBsum; 3U7X; -. DR DisProt; DP00028; -. DR ProteinModelPortal; Q13541; -. DR BioGrid; 108293; 25. DR DIP; DIP-30944N; -. DR IntAct; Q13541; 14. DR MINT; MINT-210160; -. DR STRING; 9606.ENSP00000340691; -. DR PhosphoSite; Q13541; -. DR DMDM; 34921508; -. DR MaxQB; Q13541; -. DR PaxDb; Q13541; -. DR PeptideAtlas; Q13541; -. DR PRIDE; Q13541; -. DR DNASU; 1978; -. DR Ensembl; ENST00000338825; ENSP00000340691; ENSG00000187840. DR GeneID; 1978; -. DR KEGG; hsa:1978; -. DR UCSC; uc003xks.3; human. DR CTD; 1978; -. DR GeneCards; GC08P037888; -. DR HGNC; HGNC:3288; EIF4EBP1. DR HPA; CAB005032; -. DR HPA; CAB005039; -. DR HPA; HPA023501; -. DR MIM; 602223; gene. DR neXtProt; NX_Q13541; -. DR PharmGKB; PA27715; -. DR eggNOG; NOG78084; -. DR HOGENOM; HOG000231190; -. DR HOVERGEN; HBG050425; -. DR InParanoid; Q13541; -. DR KO; K07205; -. DR OMA; NHLRNSP; -. DR OrthoDB; EOG7B31Q1; -. DR PhylomeDB; Q13541; -. DR TreeFam; TF101530; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_17015; Metabolism of proteins. DR Reactome; REACT_71; Gene Expression. DR SignaLink; Q13541; -. DR EvolutionaryTrace; Q13541; -. DR GeneWiki; EIF4EBP1; -. DR GenomeRNAi; 1978; -. DR NextBio; 8003; -. DR PMAP-CutDB; Q13541; -. DR PRO; PR:Q13541; -. DR Bgee; Q13541; -. DR CleanEx; HS_EIF4EBP1; -. DR Genevestigator; Q13541; -. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0043234; C:protein complex; IEA:Ensembl. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0030371; F:translation repressor activity; IDA:UniProtKB. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0031333; P:negative regulation of protein complex assembly; IEA:Ensembl. DR GO; GO:0045947; P:negative regulation of translational initiation; IDA:UniProtKB. DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl. DR GO; GO:0031929; P:TOR signaling; IDA:UniProtKB. DR GO; GO:0006412; P:translation; TAS:Reactome. DR GO; GO:0006413; P:translational initiation; TAS:Reactome. DR InterPro; IPR008606; EIF4EBP. DR Pfam; PF05456; eIF_4EBP; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; KW Direct protein sequencing; Isopeptide bond; Phosphoprotein; KW Protein synthesis inhibitor; Reference proteome; KW Translation regulation; Ubl conjugation. FT INIT_MET 1 1 Removed. FT CHAIN 2 118 Eukaryotic translation initiation factor FT 4E-binding protein 1. FT /FTId=PRO_0000190513. FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 37 37 Phosphothreonine; by MTOR. FT MOD_RES 41 41 Phosphothreonine. FT MOD_RES 46 46 Phosphothreonine; by MTOR. FT MOD_RES 50 50 Phosphothreonine. FT MOD_RES 54 54 Phosphotyrosine. FT MOD_RES 65 65 Phosphoserine; by DYRK2, MAPK1, MAPK3 and FT MTOR. FT MOD_RES 70 70 Phosphothreonine; by MTOR. FT MOD_RES 83 83 Phosphoserine. FT MOD_RES 101 101 Phosphoserine; by DYRK2. FT MOD_RES 112 112 Phosphoserine. FT CROSSLNK 57 57 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) FT (Probable). FT MUTAGEN 37 37 T->A: Abolishes phosphorylation by MTOR FT and increased ubiquitination by the FT BCR(KLHL25) complex; when associated with FT A-46; A-65 and A-70. FT MUTAGEN 46 46 T->A: Abolishes phosphorylation by MTOR FT and increased ubiquitination by the FT BCR(KLHL25) complex; when associated with FT A-37; A-65 and A-70. FT MUTAGEN 57 57 K->R: Impaired ubiquitination by the FT BCR(KLHL25) complex. FT MUTAGEN 59 60 LM->AA: Abolishes eIF4E-binding. FT Increased ubiquitination by the FT BCR(KLHL25) complex. FT MUTAGEN 65 65 S->A: Abolishes phosphorylation by MTOR FT and increased ubiquitination by the FT BCR(KLHL25) complex; when associated with FT A-37; A-46 and A-70. FT MUTAGEN 69 69 K->R: Does not affect ubiquitination by FT the BCR(KLHL25) complex. FT MUTAGEN 70 70 T->A: Abolishes phosphorylation by MTOR FT and increased ubiquitination by the FT BCR(KLHL25) complex; when associated with FT A-37; A-46 and A-65. FT MUTAGEN 105 105 K->R: Does not affect ubiquitination by FT the BCR(KLHL25) complex. FT HELIX 56 61 FT HELIX 62 64 SQ SEQUENCE 118 AA; 12580 MW; 1682A6BA74132966 CRC64; MSGGSSCSQT PSRAIPATRR VVLGDGVQLP PGDYSTTPGG TLFSTTPGGT RIIYDRKFLM ECRNSPVTKT PPRDLPTIPG VTSPSSDEPP MEASQSHLRN SPEDKRAGGE ESQFEMDI // ID 4ET_HUMAN Reviewed; 985 AA. AC Q9NRA8; B1AKL2; B1AKL3; B2RBF1; Q8NCF2; Q9H708; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2002, sequence version 2. DT 09-JUL-2014, entry version 121. DE RecName: Full=Eukaryotic translation initiation factor 4E transporter; DE Short=4E-T; DE Short=eIF4E transporter; DE AltName: Full=Eukaryotic translation initiation factor 4E nuclear import factor 1; GN Name=EIF4ENIF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, RP PHOSPHORYLATION, AND MUTAGENESIS OF TYR-30 AND 195-ARG-ARG-196. RC TISSUE=Fetal brain; RX PubMed=10856257; DOI=10.1093/emboj/19.12.3142; RA Dostie J., Ferraiuolo M., Pause A., Adam S.A., Sonenberg N.; RT "A novel shuttling protein, 4E-T, mediates the nuclear import of the RT mRNA 5' cap-binding protein, eIF4E."; RL EMBO J. 19:3142-3156(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Colon, Placenta, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH APOBEC3G. RX PubMed=16699599; DOI=10.1371/journal.ppat.0020041; RA Wichroski M.J., Robb G.B., Rana T.M.; RT "Human retroviral host restriction factors APOBEC3G and APOBEC3F RT localize to mRNA processing bodies."; RL PLoS Pathog. 2:E41-E41(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-136; SER-138; RP SER-345; SER-564 AND SER-951, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-564; SER-587 AND RP SER-693, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-486, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-301; SER-513; RP SER-564 AND SER-951, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-951, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP SUBCELLULAR LOCATION. RX PubMed=22090346; DOI=10.1091/mbc.E11-05-0415; RA Marnef A., Weil D., Standart N.; RT "RNA-related nuclear functions of human Pat1b, the P-body mRNA decay RT factor."; RL Mol. Biol. Cell 23:213-224(2012). CC -!- FUNCTION: Nucleoplasmic shuttling protein. Mediates the nuclear CC import of EIF4E by a piggy-back mechanism. CC -!- SUBUNIT: Interacts with EIF4E. Interacts with importin beta only CC in the presence of importin alpha, suggesting a direct interaction CC with importin alpha. Interacts with APOBEC3G in an RNA-dependent CC manner. CC -!- INTERACTION: CC Q9WMX2:- (xeno); NbExp=3; IntAct=EBI-301024, EBI-6863741; CC P06730:EIF4E; NbExp=6; IntAct=EBI-301024, EBI-73440; CC O60573:EIF4E2; NbExp=3; IntAct=EBI-301024, EBI-398610; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Nucleus, PML body. CC Nucleus speckle. Note=Predominantly cytoplasmic. Shuttles between CC the nucleus and the cytoplasm in a CRM1-dependent manner. CC Localization to nuclear foci and speckles requires active CC transcription. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9NRA8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NRA8-2; Sequence=VSP_003783, VSP_003784, VSP_047042; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q9NRA8-3; Sequence=VSP_047042; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15092.1; Type=Erroneous initiation; CC Sequence=BAC11194.1; Type=Erroneous initiation; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF240775; AAF81693.1; -; mRNA. DR EMBL; CR456386; CAG30272.1; -; mRNA. DR EMBL; AK025254; BAB15092.1; ALT_INIT; mRNA. DR EMBL; AK074768; BAC11194.1; ALT_INIT; mRNA. DR EMBL; AK314636; BAG37198.1; -; mRNA. DR EMBL; AL096701; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471095; EAW59977.1; -; Genomic_DNA. DR EMBL; BC032941; AAH32941.1; -; mRNA. DR EMBL; BC033028; AAH33028.1; -; mRNA. DR CCDS; CCDS13898.1; -. [Q9NRA8-1] DR CCDS; CCDS54520.1; -. [Q9NRA8-2] DR RefSeq; NP_001157973.1; NM_001164501.1. [Q9NRA8-1] DR RefSeq; NP_001157974.1; NM_001164502.1. [Q9NRA8-2] DR RefSeq; NP_062817.2; NM_019843.3. [Q9NRA8-1] DR RefSeq; XP_005261743.1; XM_005261686.1. [Q9NRA8-3] DR RefSeq; XP_005261744.1; XM_005261687.1. [Q9NRA8-3] DR RefSeq; XP_005261745.1; XM_005261688.1. [Q9NRA8-3] DR UniGene; Hs.517559; -. DR ProteinModelPortal; Q9NRA8; -. DR BioGrid; 121148; 10. DR IntAct; Q9NRA8; 15. DR MINT; MINT-1956064; -. DR STRING; 9606.ENSP00000328103; -. DR PhosphoSite; Q9NRA8; -. DR DMDM; 22095430; -. DR MaxQB; Q9NRA8; -. DR PaxDb; Q9NRA8; -. DR PRIDE; Q9NRA8; -. DR DNASU; 56478; -. DR Ensembl; ENST00000330125; ENSP00000328103; ENSG00000184708. [Q9NRA8-1] DR Ensembl; ENST00000344710; ENSP00000342927; ENSG00000184708. [Q9NRA8-2] DR Ensembl; ENST00000397525; ENSP00000380659; ENSG00000184708. [Q9NRA8-1] DR GeneID; 56478; -. DR KEGG; hsa:56478; -. DR UCSC; uc003aky.2; human. [Q9NRA8-1] DR CTD; 56478; -. DR GeneCards; GC22M031835; -. DR H-InvDB; HIX0016395; -. DR HGNC; HGNC:16687; EIF4ENIF1. DR HPA; HPA001619; -. DR HPA; HPA002078; -. DR MIM; 607445; gene. DR neXtProt; NX_Q9NRA8; -. DR Orphanet; 619; Primary ovarian failure. DR PharmGKB; PA38410; -. DR eggNOG; NOG43453; -. DR HOGENOM; HOG000232370; -. DR HOVERGEN; HBG023298; -. DR InParanoid; Q9NRA8; -. DR OMA; HQVPLVP; -. DR OrthoDB; EOG7GFB42; -. DR PhylomeDB; Q9NRA8; -. DR TreeFam; TF101531; -. DR ChiTaRS; EIF4ENIF1; human. DR GeneWiki; EIF4ENIF1; -. DR GenomeRNAi; 56478; -. DR NextBio; 62017; -. DR PRO; PR:Q9NRA8; -. DR ArrayExpress; Q9NRA8; -. DR Bgee; Q9NRA8; -. DR CleanEx; HS_EIF4ENIF1; -. DR Genevestigator; Q9NRA8; -. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008565; F:protein transporter activity; TAS:ProtInc. DR InterPro; IPR018862; eIF4E_transporter. DR Pfam; PF10477; EIF4E-T; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm; KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; KW Transport. FT CHAIN 1 985 Eukaryotic translation initiation factor FT 4E transporter. FT /FTId=PRO_0000064381. FT REGION 30 36 EIF4E-binding. FT MOTIF 195 211 Nuclear localization signal. FT MOTIF 438 447 Nuclear export signal. FT MOTIF 613 638 Nuclear export signal. FT COMPBIAS 148 210 Arg-rich. FT MOD_RES 5 5 Phosphoserine. FT MOD_RES 120 120 Phosphoserine. FT MOD_RES 136 136 Phosphoserine. FT MOD_RES 138 138 Phosphoserine. FT MOD_RES 301 301 Phosphoserine. FT MOD_RES 345 345 Phosphoserine. FT MOD_RES 486 486 N6-acetyllysine. FT MOD_RES 513 513 Phosphoserine. FT MOD_RES 564 564 Phosphoserine. FT MOD_RES 587 587 Phosphoserine. FT MOD_RES 693 693 Phosphoserine. FT MOD_RES 920 920 Phosphoserine. FT MOD_RES 951 951 Phosphoserine. FT VAR_SEQ 100 262 Missing (in isoform 2). FT /FTId=VSP_003783. FT VAR_SEQ 493 504 Missing (in isoform 2). FT /FTId=VSP_003784. FT VAR_SEQ 616 616 Q -> QQ (in isoform 2 and isoform 3). FT /FTId=VSP_047042. FT MUTAGEN 30 30 Y->A: Abolishes interaction with EIF4E. FT MUTAGEN 195 196 RR->NS: Abolishes the nuclear FT localization. FT CONFLICT 114 114 L -> F (in Ref. 1; AAF81693). FT CONFLICT 825 825 Q -> R (in Ref. 6; AAH33028). SQ SEQUENCE 985 AA; 108201 MW; 4C898E0488903C04 CRC64; MDRRSMGETE SGDAFLDLKK PPASKCPHRY TKEELLDIKE LPHSKQRPSC LSEKYDSDGV WDPEKWHASL YPASGRSSPV ESLKKELDTD RPSLVRRIVD PRERVKEDDL DVVLSPQRRS FGGGCHVTAA VSSRRSGSPL EKDSDGLRLL GGRRIGSGRI ISARTFEKDH RLSDKDLRDL RDRDRERDFK DKRFRREFGD SKRVFGERRR NDSYTEEEPE WFSAGPTSQS ETIELTGFDD KILEEDHKGR KRTRRRTASV KEGIVECNGG VAEEDEVEVI LAQEPAADQE VPRDAVLPEQ SPGDFDFNEF FNLDKVPCLA SMIEDVLGEG SVSASRFSRW FSNPSRSGSR SSSLGSTPHE ELERLAGLEQ AILSPGQNSG NYFAPIPLED HAENKVDILE MLQKAKVDLK PLLSSLSANK EKLKESSHSG VVLSVEEVEA GLKGLKVDQQ VKNSTPFMAE HLEETLSAVT NNRQLKKDGD MTAFNKLVST MKASGTLPSQ PKVSRNLESH LMSPAEIPGQ PVPKNILQEL LGQPVQRPAS SNLLSGLMGS LEPTTSLLGQ RAPSPPLSQV FQTRAASADY LRPRIPSPIG FTPGPQQLLG DPFQGMRKPM SPITAQMSQL ELQQAALEGL ALPHDLAVQA ANFYQPGFGK PQVDRTRDGF RNRQQRVTKS PAPVHRGNSS SPAPAASITS MLSPSFTPTS VIRKMYESKE KSKEEPASGK AALGDSKEDT QKASEENLLS SSSVPSADRD SSPTTNSKLS ALQRSSCSTP LSQANRYTKE QDYRPKATGR KTPTLASPVP TTPFLRPVHQ VPLVPHVPMV RPAHQLHPGL VQRMLAQGVH PQHLPSLLQT GVLPPGMDLS HLQGISGPIL GQPFYPLPAA SHPLLNPRPG TPLHLAMVQQ QLQRSVLHPP GSGSHAAAVS VQTTPQNVPS RSGLPHMHSQ LEHRPSQRSS SPVGLAKWFG SDVLQQPLPS MPAKVISVDE LEYRQ // ID 4F2_HUMAN Reviewed; 630 AA. AC P08195; Q13543; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 3. DT 09-JUL-2014, entry version 168. DE RecName: Full=4F2 cell-surface antigen heavy chain; DE Short=4F2hc; DE AltName: Full=4F2 heavy chain antigen; DE AltName: Full=Lymphocyte activation antigen 4F2 large subunit; DE AltName: Full=Solute carrier family 3 member 2; DE AltName: CD_antigen=CD98; GN Name=SLC3A2; Synonyms=MDU1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=3476959; DOI=10.1073/pnas.84.18.6526; RA Quackenbush E., Clabby M., Gottesdiener K.M., Barbosa J., Jones N.H., RA Strominger J.L., Speck S., Leiden J.M.; RT "Molecular cloning of complementary DNAs encoding the heavy chain of RT the human 4F2 cell-surface antigen: a type II membrane glycoprotein RT involved in normal and neoplastic cell growth."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6526-6530(1987). RN [2] RP ERRATUM, AND SEQUENCE REVISION. RA Quackenbush E., Clabby M., Gottesdiener K.M., Barbosa J., Jones N.H., RA Strominger J.L., Speck S., Leiden J.M.; RL Proc. Natl. Acad. Sci. U.S.A. 84:8618-8618(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=3036867; RA Teixeira S., di Grandi S., Kuehn L.C.; RT "Primary structure of the human 4F2 antigen heavy chain predicts a RT transmembrane protein with a cytoplasmic NH2 terminus."; RL J. Biol. Chem. 262:9574-9580(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND RP INDUCTION. RC TISSUE=Fibroblast; RX PubMed=3480538; DOI=10.1073/pnas.84.24.9204; RA Lumadue J.A., Glick A.B., Ruddle F.H.; RT "Cloning, sequence analysis, and expression of the large subunit of RT the human lymphocyte activation antigen 4F2."; RL Proc. Natl. Acad. Sci. U.S.A. 84:9204-9208(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=3265470; RA Gottesdiener K.M., Karpinski B.A., Lindsten T., Strominger J.L., RA Jones N.H., Thompson C.B., Leiden J.M.; RT "Isolation and structural characterization of the human 4F2 heavy- RT chain gene, an inducible gene involved in T-lymphocyte activation."; RL Mol. Cell. Biol. 8:3809-3819(1988). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, AND TISSUE RP SPECIFICITY. RC TISSUE=Placenta; RX PubMed=11557028; DOI=10.1016/S0005-2736(01)00384-4; RA Yanagida O., Kanai Y., Chairoungdua A., Kim D.K., Segawa H., Nii T., RA Cha S.H., Matsuo H., Fukushima J., Fukasawa Y., Tani Y., Taketani Y., RA Uchino H., Kim J.Y., Inatomi J., Okayasu I., Miyamoto K., Takeda E., RA Goya T., Endou H.; RT "Human L-type amino acid transporter 1 (LAT1): characterization of RT function and expression in tumor cell lines."; RL Biochim. Biophys. Acta 1514:291-302(2001). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE RP SPLICING (ISOFORM 4). RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Lung, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 1-17; 146-171; 227-245; 304-313; 440-451; 511-525 RP AND 593-630, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V., Lao L., Ryan K.L.; RL Submitted (OCT-2009) to UniProtKB. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 83-209 (ISOFORM 4). RC TISSUE=Lung carcinoma; RA Strausberg R.L.; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [11] RP PROTEIN SEQUENCE OF 112-122; 148-160; 227-245; 248-255; 288-298; RP 304-313; 440-451; 511-524 AND 593-625, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (MAR-2005) to UniProtKB. RN [12] RP FUNCTION, SUBUNIT, INHIBITION, AND MUTAGENESIS OF CYS-210 AND CYS-431. RX PubMed=9829974; DOI=10.1074/jbc.273.49.32437; RA Torrents D., Estevez R., Pineda M., Fernandez E., Lloberas J., RA Shi Y.-B., Zorzano A., Palacin M.; RT "Identification and characterization of a membrane protein (y+L amino RT acid transporter-1) that associates with 4F2hc to encode the amino RT acid transport activity y+L. A candidate gene for lysinuric protein RT intolerance."; RL J. Biol. Chem. 273:32437-32445(1998). RN [13] RP FUNCTION, AND SUBUNIT. RX PubMed=9751058; DOI=10.1038/26246; RA Mastroberardino L., Spindler B., Pfeiffer R., Skelly P.J., Loffing J., RA Shoemaker C.B., Verrey F.; RT "Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a RT permease family."; RL Nature 395:288-291(1998). RN [14] RP FUNCTION, AND SUBUNIT. RX PubMed=9878049; DOI=10.1093/emboj/18.1.49; RA Pfeiffer R., Rossier G., Spindler B., Meier C., Kuehn L.C., Verrey F.; RT "Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and RT members of the glycoprotein-associated amino acid transporter RT family."; RL EMBO J. 18:49-57(1999). RN [15] RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10903140; RA Broeer A., Wagner C.A., Lang F., Broeer S.; RT "The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates RT arginine efflux in exchange with glutamine."; RL Biochem. J. 349:787-795(2000). RN [16] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=11311135; RA Broeer A., Friedrich B., Wagner C.A., Fillon S., Ganapathy V., RA Lang F., Broeer S.; RT "Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires RT different domains."; RL Biochem. J. 355:725-731(2001). RN [17] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=11389679; DOI=10.1042/0264-6021:3560719; RA Ritchie J.W.A., Taylor P.M.; RT "Role of the System L permease LAT1 in amino acid and iodothyronine RT transport in placenta."; RL Biochem. J. 356:719-725(2001). RN [18] RP SUBUNIT, INTERACTION WITH BETA-1 INTEGRINS, AND MUTAGENESIS OF CYS-210 RP AND CYS-431. RX PubMed=11696247; DOI=10.1186/1472-2091-2-10; RA Kolesnikova T.V., Mannion B.A., Berditchevski F., Hemler M.E.; RT "Beta1 integrins show specific association with CD98 protein in low RT density membranes."; RL BMC Biochem. 2:10-10(2001). RN [19] RP FUNCTION, AND SUBUNIT. RX PubMed=11564694; DOI=10.1210/en.142.10.4339; RA Friesema E.C.H., Docter R., Moerings E.P.C.M., Verrey F., RA Krenning E.P., Hennemann G., Visser T.J.; RT "Thyroid hormone transport by the heterodimeric human system L amino RT acid transporter."; RL Endocrinology 142:4339-4348(2001). RN [20] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=11742812; RA Okamoto Y., Sakata M., Ogura K., Yamamoto T., Yamaguchi M., Tasaka K., RA Kurachi H., Tsurudome M., Murata Y.; RT "Expression and regulation of 4F2hc and hLAT1 in human trophoblasts."; RL Am. J. Physiol. 282:C196-C204(2002). RN [21] RP INTERACTION WITH FAM57A/CT120. RX PubMed=12270127; DOI=10.1016/S0006-291X(02)02227-1; RA He X.H., Di Y., Li J., Xie Y., Tang Y., Zhang F., Wei L., Zhang Y., RA Qin W.X., Huo K., Li Y., Wan D.F., Gu J.R.; RT "Molecular cloning and characterization of CT120, a novel membrane- RT associated gene involved in amino acid transport and glutathione RT metabolism."; RL Biochem. Biophys. Res. Commun. 297:528-536(2002). RN [22] RP FUNCTION. RX PubMed=12117417; DOI=10.1042/BJ20020841; RA Simmons-Willis T.A., Koh A.S., Clarkson T.W., Ballatori N.; RT "Transport of a neurotoxicant by molecular mimicry: the methylmercury- RT L-cysteine complex is a substrate for human L-type large neutral amino RT acid transporter (LAT) 1 and LAT2."; RL Biochem. J. 367:239-246(2002). RN [23] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=12225859; DOI=10.1016/S0005-2736(02)00516-3; RA Kim D.K., Kanai Y., Choi H.W., Tangtrongsup S., Chairoungdua A., RA Babu E., Tachampa K., Anzai N., Iribe Y., Endou H.; RT "Characterization of the system L amino acid transporter in T24 human RT bladder carcinoma cells."; RL Biochim. Biophys. Acta 1565:112-121(2002). RN [24] RP MASS SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=11840567; RX DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H; RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., RA Zvelebil M.J.; RT "Cluster analysis of an extensive human breast cancer cell line RT protein expression map database."; RL Proteomics 2:212-223(2002). RN [25] RP FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY. RX PubMed=14603368; DOI=10.1113/eph8802647; RA Arancibia-Garavilla Y., Toledo F., Casanello P., Sobrevia L.; RT "Nitric oxide synthesis requires activity of the cationic and neutral RT amino acid transport system y+L in human umbilical vein endothelium."; RL Exp. Physiol. 88:699-710(2003). RN [26] RP FUNCTION, SUBUNIT, INTERACTION WITH ICAM1, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=12716892; DOI=10.1074/jbc.M302777200; RA Liu X., Charrier L., Gewirtz A., Sitaraman S., Merlin D.; RT "CD98 and intracellular adhesion molecule I regulate the activity of RT amino acid transporter LAT-2 in polarized intestinal epithelia."; RL J. Biol. Chem. 278:23672-23677(2003). RN [27] RP GLYCOSYLATION AT ASN-365; ASN-381 AND ASN-424. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [28] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15980244; DOI=10.1167/iovs.04-1175; RA Tomi M., Mori M., Tachikawa M., Katayama K., Terasaki T., Hosoya K.; RT "L-type amino acid transporter 1-mediated L-leucine transport at the RT inner blood-retinal barrier."; RL Invest. Ophthalmol. Vis. Sci. 46:2522-2530(2005). RN [29] RP FUNCTION, AND SUBUNIT. RX PubMed=15769744; DOI=10.1074/jbc.M413164200; RA Li S., Whorton A.R.; RT "Identification of stereoselective transporters for S-nitroso-L- RT cysteine: role of LAT1 and LAT2 in biological activity of S- RT nitrosothiols."; RL J. Biol. Chem. 280:20102-20110(2005). RN [30] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-381 AND ASN-424. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [32] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16496379; DOI=10.1002/ijc.21866; RA Nawashiro H., Otani N., Shinomiya N., Fukui S., Ooigawa H., Shima K., RA Matsuo H., Kanai Y., Endou H.; RT "L-type amino acid transporter 1 as a potential molecular target in RT human astrocytic tumors."; RL Int. J. Cancer 119:484-492(2006). RN [33] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [34] RP PHOSPHORYLATION AT SER-406; SER-408; SER-410; SER-527 AND SER-531. RX PubMed=19065266; DOI=10.1371/journal.pone.0003895; RA Nguyen H.T.T., Dalmasso G., Yan Y., Obertone T.S., Sitaraman S.V., RA Merlin D.; RT "Ecto-phosphorylation of CD98 regulates cell-cell interactions."; RL PLoS ONE 3:E3895-E3895(2008). RN [35] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [36] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-365; ASN-381 AND ASN-506. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [37] RP GLYCOSYLATION AT ASN-424. RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [38] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-365; ASN-381; ASN-424 AND RP ASN-506. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [39] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [40] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [41] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-134, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [42] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [43] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [44] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 212-630, SUBUNIT, MUTAGENESIS RP OF CYS-210, SUBCELLULAR LOCATION, AND DISULFIDE BOND. RX PubMed=17724034; DOI=10.1074/jbc.M704524200; RA Fort J., de la Ballina L.R., Burghardt H.E., Ferrer-Costa C., RA Turnay J., Ferrer-Orta C., Uson I., Zorzano A., Fernandez-Recio J., RA Orozco M., Lizarbe M.A., Fita I., Palacin M.; RT "The structure of human 4F2hc ectodomain provides a model for RT homodimerization and electrostatic interaction with plasma membrane."; RL J. Biol. Chem. 282:31444-31452(2007). CC -!- FUNCTION: Required for the function of light chain amino-acid CC transporters. Involved in sodium-independent, high-affinity CC transport of large neutral amino acids such as phenylalanine, CC tyrosine, leucine, arginine and tryptophan. Involved in guiding CC and targeting of LAT1 and LAT2 to the plasma membrane. When CC associated with SLC7A6 or SLC7A7 acts as an arginine/glutamine CC exchanger, following an antiport mechanism for amino acid CC transport, influencing arginine release in exchange for CC extracellular amino acids. Plays a role in nitric oxide synthesis CC in human umbilical vein endothelial cells (HUVECs) via transport CC of L-arginine. Required for normal and neoplastic cell growth. CC When associated with SLC7A5/LAT1, is also involved in the CC transport of L-DOPA across the blood-brain barrier, and that of CC thyroid hormones triiodothyronine (T3) and thyroxine (T4) across CC the cell membrane in tissues such as placenta. Involved in the CC uptake of methylmercury (MeHg) when administered as the L-cysteine CC or D,L-homocysteine complexes, and hence plays a role in metal ion CC homeostasis and toxicity. When associated with SLC7A5 or SLC7A8, CC involved in the cellular activity of small molecular weight CC nitrosothiols, via the stereoselective transport of L- CC nitrosocysteine (L-CNSO) across the transmembrane. Together with CC ICAM1, regulates the transport activity LAT2 in polarized CC intestinal cells, by generating and delivering intracellular CC signals. When associated with SLC7A5, plays an important role in CC transporting L-leucine from the circulating blood to the retina CC across the inner blood-retinal barrier. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=295 uM for glutamine (in the presence of NaCl); CC KM=236 uM for leucine (in the presence of NaCl); CC KM=120 uM for arginine (in the presence of NaCl); CC KM=138 uM for arginine (in the absence of NaCl); CC -!- SUBUNIT: Disulfide-linked heterodimer of a glycosylated heavy CC chain and a non-glycosylated light chain (SLC7A5, SLC7A6, SLCA7A7, CC SLC7A8, SLC7A10 or SLCA7A11). Colocalizes with cadherins (By CC similarity). Interacts with FAM57A/CT120 and ICAM1. Constitutively CC and specifically associates with beta-1 integrins (alpha-2/beta-1, CC alpha-3/beta-1, alpha-5/beta-1 and alpha-6/beta-1), but minimally CC with alpha-4/beta-1. CC -!- SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II CC membrane protein. Melanosome. Note=Identified by mass spectrometry CC in melanosome fractions from stage I to stage IV. Localized to the CC plasma membrane when associated with SLC7A5 or SLC7A8. Localized CC to the placental apical membrane. Located selectively at cell-cell CC adhesion sites (By similarity). Colocalized with SLC7A8/LAT2 at CC the basolateral membrane of kidney proximal tubules and small CC intestine epithelia. Expressed in both luminal and abluminal CC membranes of brain capillary endothelial cells (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=P08195-1; Sequence=Displayed; CC Name=2; CC IsoId=P08195-2; Sequence=VSP_037907; CC Name=3; CC IsoId=P08195-3; Sequence=VSP_037908; CC Name=4; CC IsoId=P08195-4; Sequence=VSP_037909; CC -!- TISSUE SPECIFICITY: Expressed ubiquitously in all tissues tested CC with highest levels detected in kidney, placenta and testis and CC weakest level in thymus. During gestation, expression in the CC placenta was significantly stronger at full-term than at the mid- CC trimester stage. Expressed in HUVECS and at low levels in resting CC peripheral blood T-lymphocytes and quiescent fibroblasts. Also CC expressed in fetal liver and in the astrocytic process of primary CC astrocytic gliomas. Expressed in retinal endothelial cells and in CC the intestinal epithelial cell line C2BBe1. CC -!- INDUCTION: Expression is induced in resting peripheral blood T- CC lymphocytes following PHA stimulation. Expression increases at the CC time of maximal DNA synthesis, in fibroblasts stimulated to CC divide. Expression and the uptake of leucine is stimulated in CC mononuclear, cytotrophoblast-like choriocarcinoma cells by CC combined treatment with PMA and calcium ionophore. CC -!- PTM: Phosphorylation on Ser-406; Ser-408 or Ser-410 and on Ser-527 CC or Ser-531 by ecto-protein kinases favors heterotypic cell-cell CC interactions. CC -!- MASS SPECTROMETRY: Mass=57944.93; Method=MALDI; Range=1-529; CC Source=PubMed:11840567; CC -!- MISCELLANEOUS: Arginine uptake is inhibited by increasing CC concentrations of leucine in the presence of Na(+). CC -!- SIMILARITY: Belongs to the SLC3A transporter family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; J02939; AAA52497.1; -; mRNA. DR EMBL; J02769; AAA51540.1; -; mRNA. DR EMBL; J03569; AAA35536.1; -; mRNA. DR EMBL; M21904; AAA35489.1; -; Genomic_DNA. DR EMBL; M21898; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21899; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21900; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21901; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21902; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; M21903; AAA35489.1; JOINED; Genomic_DNA. DR EMBL; AB018010; BAA84649.1; -; mRNA. DR EMBL; AP001160; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001061; AAH01061.2; -; mRNA. DR EMBL; BC003000; AAH03000.2; -; mRNA. DR EMBL; BE794697; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS31589.1; -. [P08195-3] DR CCDS; CCDS31590.1; -. [P08195-2] DR CCDS; CCDS8039.2; -. [P08195-1] DR PIR; A28455; SAHU4F. DR RefSeq; NP_001012680.1; NM_001012662.2. DR RefSeq; NP_001012682.1; NM_001012664.2. [P08195-3] DR RefSeq; NP_001013269.1; NM_001013251.2. [P08195-2] DR RefSeq; NP_002385.3; NM_002394.5. [P08195-1] DR UniGene; Hs.502769; -. DR PDB; 2DH2; X-ray; 2.10 A; A=212-630. DR PDB; 2DH3; X-ray; 2.80 A; A/B=212-630. DR PDBsum; 2DH2; -. DR PDBsum; 2DH3; -. DR ProteinModelPortal; P08195; -. DR SMR; P08195; 212-630. DR BioGrid; 112411; 29. DR IntAct; P08195; 11. DR MINT; MINT-4999018; -. DR STRING; 9606.ENSP00000367124; -. DR CAZy; GH13; Glycoside Hydrolase Family 13. DR TCDB; 8.A.9.2.2; the rbat transport accessory protein (rbat) family. DR PhosphoSite; P08195; -. DR DMDM; 257051063; -. DR MaxQB; P08195; -. DR PaxDb; P08195; -. DR PRIDE; P08195; -. DR DNASU; 6520; -. DR Ensembl; ENST00000338663; ENSP00000340815; ENSG00000168003. [P08195-2] DR Ensembl; ENST00000377889; ENSP00000367121; ENSG00000168003. [P08195-3] DR Ensembl; ENST00000377890; ENSP00000367122; ENSG00000168003. [P08195-1] DR Ensembl; ENST00000377892; ENSP00000367124; ENSG00000168003. [P08195-4] DR GeneID; 6520; -. DR KEGG; hsa:6520; -. DR UCSC; uc001nwd.3; human. [P08195-1] DR UCSC; uc001nwf.3; human. [P08195-3] DR CTD; 6520; -. DR GeneCards; GC11P062623; -. DR HGNC; HGNC:11026; SLC3A2. DR HPA; CAB010455; -. DR HPA; HPA017980; -. DR MIM; 158070; gene. DR neXtProt; NX_P08195; -. DR PharmGKB; PA35894; -. DR eggNOG; COG0366; -. DR HOGENOM; HOG000233529; -. DR HOVERGEN; HBG000023; -. DR InParanoid; P08195; -. DR KO; K06519; -. DR OMA; NMTVKGQ; -. DR OrthoDB; EOG7ZSHSV; -. DR PhylomeDB; P08195; -. DR BioCyc; MetaCyc:ENSG00000168003-MONOMER; -. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR Reactome; REACT_19419; Amino acid and oligopeptide SLC transporters. DR Reactome; REACT_604; Hemostasis. DR SABIO-RK; P08195; -. DR ChiTaRS; SLC3A2; human. DR EvolutionaryTrace; P08195; -. DR GeneWiki; SLC3A2; -. DR GenomeRNAi; 6520; -. DR NextBio; 25353; -. DR PRO; PR:P08195; -. DR ArrayExpress; P08195; -. DR Bgee; P08195; -. DR CleanEx; HS_SLC3A2; -. DR Genevestigator; P08195; -. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0005432; F:calcium:sodium antiporter activity; TAS:UniProtKB. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0043169; F:cation binding; IEA:InterPro. DR GO; GO:0003725; F:double-stranded RNA binding; IDA:MGI. DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0006865; P:amino acid transport; TAS:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0006816; P:calcium ion transport; NAS:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0016049; P:cell growth; NAS:UniProtKB. DR GO; GO:0006811; P:ion transport; TAS:Reactome. DR GO; GO:0060356; P:leucine import; ISS:UniProtKB. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0043330; P:response to exogenous dsRNA; IMP:MGI. DR GO; GO:0035725; P:sodium ion transmembrane transport; TAS:GOC. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0015827; P:tryptophan transport; ISS:UniProtKB. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR015902; Glyco_hydro_13. DR InterPro; IPR013780; Glyco_hydro_13_b. DR InterPro; IPR006047; Glyco_hydro_13_cat_dom. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR10357; PTHR10357; 1. DR Pfam; PF00128; Alpha-amylase; 2. DR SUPFAM; SSF51445; SSF51445; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Amino-acid transport; KW Cell membrane; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Isopeptide bond; Membrane; KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix; Transport; Ubl conjugation. FT CHAIN 1 630 4F2 cell-surface antigen heavy chain. FT /FTId=PRO_0000064383. FT TOPO_DOM 102 184 Cytoplasmic (Potential). FT TRANSMEM 185 205 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 206 630 Extracellular (Potential). FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 103 103 Phosphoserine. FT MOD_RES 134 134 Phosphoserine. FT MOD_RES 165 165 Phosphoserine. FT MOD_RES 406 406 Phosphoserine (Probable). FT MOD_RES 408 408 Phosphoserine (Probable). FT MOD_RES 410 410 Phosphoserine (Probable). FT MOD_RES 527 527 Phosphoserine (Probable). FT MOD_RES 531 531 Phosphoserine (Probable). FT CARBOHYD 365 365 N-linked (GlcNAc...). FT CARBOHYD 381 381 N-linked (GlcNAc...). FT CARBOHYD 424 424 N-linked (GlcNAc...) (complex). FT CARBOHYD 506 506 N-linked (GlcNAc...). FT DISULFID 210 210 Interchain (with light chain). FT CROSSLNK 147 147 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VAR_SEQ 1 101 Missing (in isoform 2). FT /FTId=VSP_037907. FT VAR_SEQ 38 99 Missing (in isoform 3). FT /FTId=VSP_037908. FT VAR_SEQ 98 98 V -> VTETGFHHVSQADIEFLTSIDPTASASGSAGI (in FT isoform 4). FT /FTId=VSP_037909. FT MUTAGEN 210 210 C->S: Abolishes dimerization, leucine FT uptake and interaction with beta-1 FT integrins. FT MUTAGEN 431 431 C->S: No effect on dimerization, leucine FT uptake or interaction with beta-1 FT integrins. FT CONFLICT 137 137 G -> E (in Ref. 4; AAA35536). FT CONFLICT 158 158 A -> P (in Ref. 3; AAA51540). FT CONFLICT 223 223 A -> P (in Ref. 4; AAA35536). FT CONFLICT 315 315 E -> D (in Ref. 4; AAA35536). FT CONFLICT 320 320 S -> F (in Ref. 5; AAA35489). FT CONFLICT 372 372 E -> G (in Ref. 4; AAA35536). FT CONFLICT 412 413 GE -> PQ (in Ref. 4; AAA35536). FT CONFLICT 465 465 V -> L (in Ref. 4; AAA35536). FT CONFLICT 481 481 G -> P (in Ref. 4; AAA35536). FT CONFLICT 549 549 G -> E (in Ref. 5; AAA35489). FT CONFLICT 609 609 L -> P (in Ref. 4; AAA35536). FT CONFLICT 612 612 E -> G (in Ref. 4; AAA35536). FT HELIX 218 220 FT STRAND 224 227 FT HELIX 230 234 FT HELIX 241 245 FT HELIX 248 253 FT STRAND 257 261 FT STRAND 265 267 FT STRAND 275 280 FT HELIX 282 284 FT HELIX 287 299 FT STRAND 303 307 FT TURN 310 313 FT STRAND 314 316 FT STRAND 319 321 FT HELIX 323 340 FT STRAND 344 347 FT HELIX 350 352 FT HELIX 356 370 FT STRAND 375 379 FT HELIX 385 391 FT TURN 392 394 FT STRAND 399 401 FT TURN 404 407 FT HELIX 412 426 FT STRAND 437 439 FT HELIX 441 443 FT HELIX 447 449 FT HELIX 450 457 FT STRAND 460 467 FT HELIX 470 472 FT HELIX 476 478 FT STRAND 479 481 FT STRAND 484 486 FT HELIX 493 495 FT HELIX 500 502 FT HELIX 505 507 FT HELIX 509 513 FT HELIX 519 532 FT HELIX 534 538 FT STRAND 540 545 FT STRAND 550 556 FT STRAND 562 568 FT STRAND 570 572 FT STRAND 581 583 FT HELIX 585 587 FT STRAND 591 603 FT STRAND 607 610 FT HELIX 611 613 FT STRAND 621 626 SQ SEQUENCE 630 AA; 67994 MW; AE427F8204CC10B0 CRC64; MELQPPEASI AVVSIPRQLP GSHSEAGVQG LSAGDDSELG SHCVAQTGLE LLASGDPLPS ASQNAEMIET GSDCVTQAGL QLLASSDPPA LASKNAEVTG TMSQDTEVDM KEVELNELEP EKQPMNAASG AAMSLAGAEK NGLVKIKVAE DEAEAAAAAK FTGLSKEELL KVAGSPGWVR TRWALLLLFW LGWLGMLAGA VVIIVRAPRC RELPAQKWWH TGALYRIGDL QAFQGHGAGN LAGLKGRLDY LSSLKVKGLV LGPIHKNQKD DVAQTDLLQI DPNFGSKEDF DSLLQSAKKK SIRVILDLTP NYRGENSWFS TQVDTVATKV KDALEFWLQA GVDGFQVRDI ENLKDASSFL AEWQNITKGF SEDRLLIAGT NSSDLQQILS LLESNKDLLL TSSYLSDSGS TGEHTKSLVT QYLNATGNRW CSWSLSQARL LTSFLPAQLL RLYQLMLFTL PGTPVFSYGD EIGLDAAALP GQPMEAPVML WDESSFPDIP GAVSANMTVK GQSEDPGSLL SLFRRLSDQR SKERSLLHGD FHAFSAGPGL FSYIRHWDQN ERFLVVLNFG DVGLSAGLQA SDLPASASLP AKADLLLSTQ PGREEGSPLE LERLKLEPHE GLLLRFPYAA // ID 5HT1A_HUMAN Reviewed; 422 AA. AC P08908; Q6LAE7; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 3. DT 09-JUL-2014, entry version 146. DE RecName: Full=5-hydroxytryptamine receptor 1A; DE Short=5-HT-1A; DE Short=5-HT1A; DE AltName: Full=G-21; DE AltName: Full=Serotonin receptor 1A; GN Name=HTR1A; Synonyms=ADRB2RL1, ADRBRL1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=3041227; DOI=10.1038/329075a0; RA Kobilka B.K., Frielle T., Collins S., Yang-Feng T.L., Kobilka T.S., RA Francke U., Lefkowitz R.J., Caron M.G.; RT "An intronless gene encoding a potential member of the family of RT receptors coupled to guanine nucleotide regulatory proteins."; RL Nature 329:75-79(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Saltzman A.G., Morse B., Felder S.; RT "Nucleotide and deduced amino acid sequence of the human serotonin 5- RT HT1a receptor gene."; RL Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Levy F.O., Gudermann T., Birnbaumer M., Kaumann A.J., Birnbaumer L.; RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15014171; DOI=10.1093/molbev/msh100; RA Kitano T., Liu Y.-H., Ueda S., Saitou N.; RT "Human-specific amino acid changes found in 103 protein-coding RT genes."; RL Mol. Biol. Evol. 21:936-944(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. RX PubMed=1766875; DOI=10.1093/nar/19.25.7155; RA Parks C.L., Chang L.S., Shenk T.; RT "A polymerase chain reaction mediated by a single primer: cloning of RT genomic sequences adjacent to a serotonin receptor protein coding RT region."; RL Nucleic Acids Res. 19:7155-7160(1991). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 200-365, FUNCTION, SUBCELLULAR LOCATION, RP AND TISSUE SPECIFICITY. RX PubMed=8393041; RA Aune T.M., McGrath K.M., Sarr T., Bombara M.P., Kelley K.A.; RT "Expression of 5HT1a receptors on activated human T cells. Regulation RT of cyclic AMP levels and T cell proliferation by 5- RT hydroxytryptamine."; RL J. Immunol. 151:1175-1183(1993). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=3138543; DOI=10.1038/335358a0; RA Fargin A., Raymond J.R., Lohse M.L., Kobilka B.K., Caron M.G., RA Lefkowitz R.J.; RT "The genomic clone G-21 which resembles a beta-adrenergic receptor RT sequence encodes the 5-HT1A receptor."; RL Nature 335:358-360(1988). RN [10] RP FUNCTION. RX PubMed=8138923; RA Harrington M.A., Shaw K., Zhong P., Ciaranello R.D.; RT "Agonist-induced desensitization and loss of high-affinity binding RT sites of stably expressed human 5-HT1A receptors."; RL J. Pharmacol. Exp. Ther. 268:1098-1106(1994). RN [11] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-334. RC TISSUE=Lung adenocarcinoma; RX PubMed=17203973; DOI=10.1021/pr060438j; RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., RA Haines D.S., Figeys D.; RT "The proteomic reactor facilitates the analysis of affinity-purified RT proteins by mass spectrometry: application for identifying RT ubiquitinated proteins in human cells."; RL J. Proteome Res. 6:298-305(2007). RN [12] RP REVIEW. RX PubMed=18476671; DOI=10.1021/cr078224o; RA Nichols D.E., Nichols C.D.; RT "Serotonin receptors."; RL Chem. Rev. 108:1614-1641(2008). RN [13] RP REVIEW. RX PubMed=20363322; DOI=10.1016/j.cellsig.2010.03.019; RA Polter A.M., Li X.; RT "5-HT1A receptor-regulated signal transduction pathways in brain."; RL Cell. Signal. 22:1406-1412(2010). RN [14] RP REVIEW. RX PubMed=20945968; RA Pytliak M., Vargova V., Mechirova V., Felsoci M.; RT "Serotonin receptors - from molecular biology to clinical RT applications."; RL Physiol. Res. 60:15-25(2011). RN [15] RP INVOLVEMENT IN PFMC. RX PubMed=21990073; DOI=10.1002/humu.21622; RA Jiang Y.C., Wu H.M., Cheng K.H., Sunny Sun H.; RT "Menstrual cycle-dependent febrile episode mediated by sequence- RT specific repression of poly(ADP-ribose) polymerase-1 on the RT transcription of the human serotonin receptor 1A gene."; RL Hum. Mutat. 33:209-217(2012). RN [16] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22957663; DOI=10.1111/jnc.12008; RA Singh P., Paila Y.D., Chattopadhyay A.; RT "Role of glycosphingolipids in the function of human serotonin(1)A RT receptors."; RL J. Neurochem. 123:716-724(2012). RN [17] RP SUBUNIT. RX PubMed=23300088; DOI=10.1074/jbc.M112.412478; RA Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.; RT "Post-synaptic density-95 (PSD-95) binding capacity of G-protein- RT coupled receptor 30 (GPR30), an estrogen receptor that can be RT identified in hippocampal dendritic spines."; RL J. Biol. Chem. 288:6438-6450(2013). RN [18] RP VARIANTS SER-22 AND VAL-28. RX PubMed=7755630; DOI=10.1006/bbrc.1995.1692; RA Nakhai B., Nielsen D.A., Linnoila M., Goldman D.; RT "Two naturally occurring amino acid substitutions in the human 5-HT1A RT receptor: glycine 22 to serine 22 and isoleucine 28 to valine 28."; RL Biochem. Biophys. Res. Commun. 210:530-536(1995). RN [19] RP VARIANTS LEU-16 AND ASP-273. RX PubMed=9754630; RX DOI=10.1002/(SICI)1096-8628(19980907)81:5<434::AID-AJMG13>3.0.CO;2-D; RA Kawanishi Y., Harada S., Tachikawa H., Okubo T., Shiraishi H.; RT "Novel mutations in the promoter and coding region of the human 5-HT1A RT receptor gene and association analysis in schizophrenia."; RL Am. J. Med. Genet. 81:434-439(1998). CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine CC (serotonin). Also functions as a receptor for various drugs and CC psychoactive substances. Ligand binding causes a conformation CC change that triggers signaling via guanine nucleotide-binding CC proteins (G proteins) and modulates the activity of down-stream CC effectors, such as adenylate cyclase. Beta-arrestin family members CC inhibit signaling via G proteins and mediate activation of CC alternative signaling pathways. Signaling inhibits adenylate CC cyclase activity and activates a phosphatidylinositol-calcium CC second messenger system that regulates the release of Ca(2+) ions CC from intracellular stores. Plays a role in the regulation of 5- CC hydroxytryptamine release and in the regulation of dopamine and 5- CC hydroxytryptamine metabolism. Plays a role in the regulation of CC dopamine and 5-hydroxytryptamine levels in the brain, and thereby CC affects neural activity, mood and behavior. Plays a role in the CC response to anxiogenic stimuli. CC -!- SUBUNIT: Heterodimer; heterodimerizes with GPER1. CC -!- INTERACTION: CC P11362:FGFR1; NbExp=11; IntAct=EBI-6570214, EBI-1028277; CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Detected in lymph nodes, thymus and spleen. CC Detected in activated T-cells, but not in resting T-cells. CC -!- DISEASE: Periodic fever, menstrual cycle-dependent (PFMC) CC [MIM:614674]: A condition characterized by recurrent fevers up to CC 40 degrees Celsius associated with the luteal phase of the CC menstrual cycle. Women show menstrual cycle-dependent physiologic CC changes in relation to sex hormone levels. Because ovulation CC triggers a significant change in the hormonal milieu that is CC similar to local inflammation, a 0.5 to 1.0 degree Celsius CC increase in basal body temperature after ovulation is commonly CC associated with progesterone secretion and is believed to be CC triggered by the induction of several inflammatory cytokines. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 5- CC hydroxytryptamine receptor subfamily. HTR1A sub-subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M28269; AAA36440.1; -; Genomic_DNA. DR EMBL; X13556; CAA31908.1; -; Genomic_DNA. DR EMBL; X57829; CAA40962.1; -; Genomic_DNA. DR EMBL; M83181; AAA66493.1; -; Genomic_DNA. DR EMBL; AB041403; BAA94488.1; -; Genomic_DNA. DR EMBL; AF498978; AAM21125.1; -; mRNA. DR EMBL; BC069159; AAH69159.1; -; mRNA. DR EMBL; Z11168; CAA77560.1; -; Genomic_DNA. DR CCDS; CCDS34168.1; -. DR PIR; I38209; I38209. DR RefSeq; NP_000515.2; NM_000524.3. DR UniGene; Hs.247940; -. DR ProteinModelPortal; P08908; -. DR SMR; P08908; 31-418. DR BioGrid; 109582; 6. DR IntAct; P08908; 4. DR STRING; 9606.ENSP00000316244; -. DR BindingDB; P08908; -. DR ChEMBL; CHEMBL2096904; -. DR DrugBank; DB00866; Alprenolol. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB00490; Buspirone. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB00216; Eletriptan. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB00176; Fluvoxamine. DR DrugBank; DB00589; Lisuride. DR DrugBank; DB00247; Methysergide. DR DrugBank; DB00370; Mirtazapine. DR DrugBank; DB00960; Pindolol. DR DrugBank; DB00571; Propranolol. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB01104; Sertraline. DR DrugBank; DB01079; Tegaserod. DR DrugBank; DB00656; Trazodone. DR DrugBank; DB00285; Venlafaxine. DR DrugBank; DB00246; Ziprasidone. DR GuidetoPHARMACOLOGY; 1; -. DR PhosphoSite; P08908; -. DR DMDM; 231454; -. DR PaxDb; P08908; -. DR PRIDE; P08908; -. DR DNASU; 3350; -. DR Ensembl; ENST00000323865; ENSP00000316244; ENSG00000178394. DR GeneID; 3350; -. DR KEGG; hsa:3350; -. DR UCSC; uc011cqt.3; human. DR CTD; 3350; -. DR GeneCards; GC05M063292; -. DR HGNC; HGNC:5286; HTR1A. DR HPA; HPA018073; -. DR MIM; 109760; gene. DR MIM; 614674; phenotype. DR neXtProt; NX_P08908; -. DR PharmGKB; PA192; -. DR eggNOG; NOG249628; -. DR HOGENOM; HOG000239242; -. DR HOVERGEN; HBG106962; -. DR InParanoid; P08908; -. DR KO; K04153; -. DR OMA; TGAPCAN; -. DR PhylomeDB; P08908; -. DR TreeFam; TF316350; -. DR Reactome; REACT_111102; Signal Transduction. DR GenomeRNAi; 3350; -. DR NextBio; 13248; -. DR PRO; PR:P08908; -. DR ArrayExpress; P08908; -. DR Bgee; P08908; -. DR CleanEx; HS_HTR1A; -. DR Genevestigator; P08908; -. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004993; F:serotonin receptor activity; IDA:UniProtKB. DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0001662; P:behavioral fear response; ISS:UniProtKB. DR GO; GO:0008283; P:cell proliferation; IEA:InterPro. DR GO; GO:0035640; P:exploration behavior; ISS:UniProtKB. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc. DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro. DR GO; GO:0042053; P:regulation of dopamine metabolic process; ISS:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro. DR GO; GO:0014062; P:regulation of serotonin secretion; ISS:UniProtKB. DR GO; GO:0042428; P:serotonin metabolic process; ISS:UniProtKB. DR GO; GO:0007210; P:serotonin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro. DR Gene3D; 1.20.1070.10; -; 2. DR InterPro; IPR000610; 5HT1A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24247:SF20; PTHR24247:SF20; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00512; 5HT1ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW Behavior; Cell membrane; Complete proteome; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Isopeptide bond; Membrane; KW Polymorphism; Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT CHAIN 1 422 5-hydroxytryptamine receptor 1A. FT /FTId=PRO_0000068903. FT TOPO_DOM 1 36 Extracellular (By similarity). FT TRANSMEM 37 62 Helical; Name=1; (By similarity). FT TOPO_DOM 63 73 Cytoplasmic (By similarity). FT TRANSMEM 74 98 Helical; Name=2; (By similarity). FT TOPO_DOM 99 110 Extracellular (By similarity). FT TRANSMEM 111 132 Helical; Name=3; (By similarity). FT TOPO_DOM 133 152 Cytoplasmic (By similarity). FT TRANSMEM 153 178 Helical; Name=4; (By similarity). FT TOPO_DOM 179 191 Extracellular (By similarity). FT TRANSMEM 192 217 Helical; Name=5; (By similarity). FT TOPO_DOM 218 345 Cytoplasmic (By similarity). FT TRANSMEM 346 367 Helical; Name=6; (By similarity). FT TOPO_DOM 368 378 Extracellular (By similarity). FT TRANSMEM 379 403 Helical; Name=7; (By similarity). FT TOPO_DOM 404 422 Cytoplasmic (By similarity). FT REGION 112 121 Agonist binding (By similarity). FT REGION 358 362 Agonist binding (By similarity). FT MOTIF 133 135 DRY motif; important for ligand-induced FT conformation changes (By similarity). FT MOTIF 396 400 NPxxY motif; important for ligand-induced FT conformation changes and signaling (By FT similarity). FT CARBOHYD 10 10 N-linked (GlcNAc...) (Potential). FT CARBOHYD 11 11 N-linked (GlcNAc...) (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT DISULFID 109 187 By similarity. FT CROSSLNK 334 334 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VARIANT 16 16 P -> L (in dbSNP:rs1800041). FT /FTId=VAR_003446. FT VARIANT 22 22 G -> S (in dbSNP:rs1799920). FT /FTId=VAR_011826. FT VARIANT 28 28 I -> V (in dbSNP:rs1799921). FT /FTId=VAR_011827. FT VARIANT 184 184 P -> L (in dbSNP:rs1800043). FT /FTId=VAR_011828. FT VARIANT 220 220 R -> L (in dbSNP:rs1800044). FT /FTId=VAR_011829. FT VARIANT 273 273 G -> D (in dbSNP:rs1800042). FT /FTId=VAR_011830. FT CONFLICT 152 154 RAA -> PR (in Ref. 1; AAA36440/CAA31908). FT CONFLICT 172 172 M -> I (in Ref. 1; AAA36440/CAA31908). FT CONFLICT 200 202 TFG -> RPR (in Ref. 8; no nucleotide FT entry). FT CONFLICT 228 228 K -> R (in Ref. 8; no nucleotide entry). FT CONFLICT 244 244 A -> AA (in Ref. 8; no nucleotide entry). FT CONFLICT 355 355 I -> T (in Ref. 8; no nucleotide entry). FT CONFLICT 363 365 IVA -> MRP (in Ref. 8; no nucleotide FT entry). FT CONFLICT 418 418 K -> N (in Ref. 1; AAA36440/CAA31908). SQ SEQUENCE 422 AA; 46107 MW; 762664FCF62CFD8F CRC64; MDVLSPGQGN NTTSPPAPFE TGGNTTGISD VTVSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKTGADT RHGASPAPQP KKSVNGESGS RNWRLGVESK AGGALCANGA VRQGDDGAAL EVIEVHRVGN SKEHLPLPSE AGPTPCAPAS FERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC RQ // ID 5HT1B_HUMAN Reviewed; 390 AA. AC P28222; Q4VAY7; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 09-JUL-2014, entry version 137. DE RecName: Full=5-hydroxytryptamine receptor 1B; DE Short=5-HT-1B; DE Short=5-HT1B; DE AltName: Full=S12; DE AltName: Full=Serotonin 1D beta receptor; DE Short=5-HT-1D-beta; DE AltName: Full=Serotonin receptor 1B; GN Name=HTR1B; Synonyms=HTR1DB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=1315531; DOI=10.1016/0006-291X(92)90654-4; RA Hamblin M.W., Metcalf M.A., McGuffin R.W., Karpells S.; RT "Molecular cloning and functional characterization of a human 5-HT1B RT serotonin receptor: a homologue of the rat 5-HT1B receptor with 5- RT HT1D-like pharmacological specificity."; RL Biochem. Biophys. Res. Commun. 184:752-759(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=1610347; DOI=10.1016/0006-291X(92)91655-A; RA Mochizuki D., Yuyama Y., Tsujita R., Komaki H., Sagai H.; RT "Cloning and expression of the human 5-HT1B-type receptor gene."; RL Biochem. Biophys. Res. Commun. 185:517-523(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=1348246; RA Jin H., Oksenberg D., Ashkenazi A., Peroutka S.J., Duncan A.M.V., RA Rozmahel R., Yang Y., Mengod G., Palacios J.M., O'Dowd B.F.; RT "Characterization of the human 5-hydroxytryptamine1B receptor."; RL J. Biol. Chem. 267:5735-5738(1992). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=1559993; RA Levy F.O., Gudermann T., Perez-Reyes E., Birnbaumer M., Kaumann A.J., RA Birnbaumer L.; RT "Molecular cloning of a human serotonin receptor (S12) with a RT pharmacological profile resembling that of the 5-HT1D subtype."; RL J. Biol. Chem. 267:7553-7562(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Placenta; RX PubMed=1565658; DOI=10.1073/pnas.89.8.3630; RA Weinshank R.L., Zgombick J.M., Macchi M.J., Branchek T.A., RA Hartig P.R.; RT "Human serotonin 1D receptor is encoded by a subfamily of two distinct RT genes: 5-HT1D alpha and 5-HT1D beta."; RL Proc. Natl. Acad. Sci. U.S.A. 89:3630-3634(1992). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=1351684; DOI=10.1073/pnas.89.12.5522; RA Demchyshyn L., Sunahara R.K., Miller K., Teitler M., Hoffman B.J., RA Kennedy J.L., Seeman P., van Tol H.H.M., Niznik H.B.; RT "A human serotonin 1D receptor variant (5HT1D beta) encoded by an RT intronless gene on chromosome 6."; RL Proc. Natl. Acad. Sci. U.S.A. 89:5522-5526(1992). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=1328844; RA Veldman S.A., Bienkowski M.J.; RT "Cloning and pharmacological characterization of a novel human 5- RT hydroxytryptamine1D receptor subtype."; RL Mol. Pharmacol. 42:439-444(1992). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15014171; DOI=10.1093/molbev/msh100; RA Kitano T., Liu Y.-H., Ueda S., Saitou N.; RT "Human-specific amino acid changes found in 103 protein-coding RT genes."; RL Mol. Biol. Evol. 21:936-944(2004). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kopatz S.A., Aronstam R.S., Sharma S.V.; RT "Isolation of complete coding sequence for 5-hydroxytryptamine RT (serotonin) receptor 1B (HTR1B)."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP PALMITOYLATION, PHOSPHORYLATION, AND FUNCTION. RX PubMed=8218242; DOI=10.1021/bi00094a032; RA Ng G.Y.K., George S.R., Zastawny R.L., Caron M., Bouvier M., RA Dennis M., O'Dowd B.F.; RT "Human serotonin1B receptor expression in Sf9 cells: phosphorylation, RT palmitoylation, and adenylyl cyclase inhibition."; RL Biochemistry 32:11727-11733(1993). RN [13] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=10452531; DOI=10.1016/S0014-5793(99)00918-7; RA Xie Z., Lee S.P., O'Dowd B.F., George S.R.; RT "Serotonin 5-HT1B and 5-HT1D receptors form homodimers when expressed RT alone and heterodimers when co-expressed."; RL FEBS Lett. 456:63-67(1999). RN [14] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15853772; DOI=10.1042/CS20050016; RA Edvinsson L., Uddman E., Wackenfors A., Davenport A., Longmore J., RA Malmsjo M.; RT "Triptan-induced contractile (5-HT1B receptor) responses in human RT cerebral and coronary arteries: relationship to clinical effect."; RL Clin. Sci. 109:335-342(2005). RN [15] RP REVIEW. RX PubMed=18476671; DOI=10.1021/cr078224o; RA Nichols D.E., Nichols C.D.; RT "Serotonin receptors."; RL Chem. Rev. 108:1614-1641(2008). RN [16] RP REVIEW. RX PubMed=20945968; RA Pytliak M., Vargova V., Mechirova V., Felsoci M.; RT "Serotonin receptors - from molecular biology to clinical RT applications."; RL Physiol. Res. 60:15-25(2011). RN [17] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23519215; DOI=10.1126/science.1232808; RA Wacker D., Wang C., Katritch V., Han G.W., Huang X.P., Vardy E., RA McCorvy J.D., Jiang Y., Chu M., Siu F.Y., Liu W., Xu H.E., RA Cherezov V., Roth B.L., Stevens R.C.; RT "Structural features for functional selectivity at serotonin RT receptors."; RL Science 340:615-619(2013). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 33-390 IN COMPLEXES WITH RP ERGOTAMINE AND DIHYDROERGOTAMINE, FUNCTION, SUBCELLULAR LOCATION, RP MEMBRANE TOPOLOGY, DOMAIN, DISULFIDE BOND, AND MUTAGENESIS OF LEU-126; RP ASP-129; ILE-130; CYS-133; THR-134; VAL-200; VAL-201; THR-203; RP THR-209; SER-212; ALA-216; TRP-327; PHE-330; PHE-331; SER-334; RP MET-337; PHE-351; ASP-352; THR-355 AND TYR-359. RX PubMed=23519210; DOI=10.1126/science.1232807; RA Wang C., Jiang Y., Ma J., Wu H., Wacker D., Katritch V., Han G.W., RA Liu W., Huang X.P., Vardy E., McCorvy J.D., Gao X., Zhou X.E., RA Melcher K., Zhang C., Bai F., Yang H., Yang L., Jiang H., Roth B.L., RA Cherezov V., Stevens R.C., Xu H.E.; RT "Structural basis for molecular recognition at serotonin receptors."; RL Science 340:610-614(2013). RN [19] RP VARIANT CYS-124. RX PubMed=7802650; DOI=10.1006/bbrc.1994.2792; RA Nothen M.M., Erdmann J., Shimron-Abarbanell D., Propping P.; RT "Identification of genetic variation in the human serotonin 1D beta RT receptor gene."; RL Biochem. Biophys. Res. Commun. 205:1194-1200(1994). CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine CC (serotonin). Also functions as a receptor for ergot alkaloid CC derivatives, various anxiolytic and antidepressant drugs and other CC psychoactive substances, such as lysergic acid diethylamide (LSD). CC Ligand binding causes a conformation change that triggers CC signaling via guanine nucleotide-binding proteins (G proteins) and CC modulates the activity of down-stream effectors, such as adenylate CC cyclase. Signaling inhibits adenylate cyclase activity. Arrestin CC family members inhibit signaling via G proteins and mediate CC activation of alternative signaling pathways. Regulates the CC release of 5-hydroxytryptamine, dopamine and acetylcholine in the CC brain, and thereby affects neural activity, nociceptive CC processing, pain perception, mood and behavior. Besides, plays a CC role in vasoconstriction of cerebral arteries. CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1D. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Detected in cerebral artery smooth muscle CC cells (at protein level). Detected in brain cortex, striatum, CC amygdala, medulla, hippocampus, caudate nucleus and putamen. CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the CC transmembrane helices. CC -!- PTM: Phosphorylated. Desensitization of the receptor may be CC mediated by its phosphorylation. CC -!- PTM: Palmitoylated. CC -!- MISCELLANEOUS: A residue in the 7th transmembrane region (Thr-355 CC in human, 'Asn-351' in mouse and rat) is important for species- CC specific sensitivity to various agonists. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M89478; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; D10995; BAA01763.1; -; Genomic_DNA. DR EMBL; M83180; AAA36029.1; -; Genomic_DNA. DR EMBL; L09732; AAA36030.1; -; Genomic_DNA. DR EMBL; M81590; AAA60316.1; -; mRNA. DR EMBL; M75128; AAA58675.1; -; Genomic_DNA. DR EMBL; AB041370; BAA94455.1; -; Genomic_DNA. DR EMBL; AY225227; AAO67712.1; -; Genomic_DNA. DR EMBL; AL049595; CAB51537.1; -; Genomic_DNA. DR EMBL; BC069065; AAH69065.1; -; mRNA. DR EMBL; BC096206; AAH96206.1; -; mRNA. DR EMBL; BC096207; AAH96207.1; -; mRNA. DR EMBL; BC096208; AAH96208.1; -; mRNA. DR CCDS; CCDS4986.1; -. DR PIR; JN0268; JN0268. DR RefSeq; NP_000854.1; NM_000863.1. DR UniGene; Hs.123016; -. DR PDB; 2G1X; Model; -; A=1-390. DR PDB; 4IAQ; X-ray; 2.80 A; A=33-239, A=304-390. DR PDB; 4IAR; X-ray; 2.70 A; A=33-239, A=306-390. DR PDBsum; 2G1X; -. DR PDBsum; 4IAQ; -. DR PDBsum; 4IAR; -. DR ProteinModelPortal; P28222; -. DR SMR; P28222; 38-387. DR BioGrid; 109583; 3. DR IntAct; P28222; 1. DR STRING; 9606.ENSP00000358963; -. DR BindingDB; P28222; -. DR ChEMBL; CHEMBL2095230; -. DR DrugBank; DB00918; Almotriptan. DR DrugBank; DB01191; Dexfenfluramine. DR DrugBank; DB00320; Dihydroergotamine. DR DrugBank; DB00216; Eletriptan. DR DrugBank; DB00696; Ergotamine. DR DrugBank; DB00998; Frovatriptan. DR DrugBank; DB00952; Naratriptan. DR DrugBank; DB00960; Pindolol. DR DrugBank; DB00571; Propranolol. DR DrugBank; DB00953; Rizatriptan. DR DrugBank; DB00669; Sumatriptan. DR DrugBank; DB00285; Venlafaxine. DR DrugBank; DB00315; Zolmitriptan. DR GuidetoPHARMACOLOGY; 2; -. DR TCDB; 9.A.14.3.6; the g-protein-coupled receptor (gpcr) family. DR PhosphoSite; P28222; -. DR DMDM; 112821; -. DR PaxDb; P28222; -. DR PRIDE; P28222; -. DR DNASU; 3351; -. DR Ensembl; ENST00000369947; ENSP00000358963; ENSG00000135312. DR GeneID; 3351; -. DR KEGG; hsa:3351; -. DR UCSC; uc003pil.1; human. DR CTD; 3351; -. DR GeneCards; GC06M078171; -. DR HGNC; HGNC:5287; HTR1B. DR HPA; HPA049046; -. DR MIM; 182131; gene. DR neXtProt; NX_P28222; -. DR PharmGKB; PA29549; -. DR eggNOG; NOG249628; -. DR HOGENOM; HOG000239242; -. DR HOVERGEN; HBG106962; -. DR InParanoid; P28222; -. DR KO; K04153; -. DR OMA; IALPWKV; -. DR OrthoDB; EOG7NCV3Q; -. DR PhylomeDB; P28222; -. DR TreeFam; TF316350; -. DR Reactome; REACT_111102; Signal Transduction. DR GeneWiki; 5-HT1B_receptor; -. DR GenomeRNAi; 3351; -. DR NextBio; 13252; -. DR PRO; PR:P28222; -. DR Bgee; P28222; -. DR CleanEx; HS_HTR1B; -. DR Genevestigator; P28222; -. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008144; F:drug binding; IEA:Ensembl. DR GO; GO:0051378; F:serotonin binding; IEA:Ensembl. DR GO; GO:0004993; F:serotonin receptor activity; IDA:UniProtKB. DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0046849; P:bone remodeling; IEA:Ensembl. DR GO; GO:0071312; P:cellular response to alkaloid; IDA:UniProtKB. DR GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB. DR GO; GO:0071502; P:cellular response to temperature stimulus; IEA:Ensembl. DR GO; GO:0042756; P:drinking behavior; IEA:Ensembl. DR GO; GO:0002031; P:G-protein coupled receptor internalization; IEA:Ensembl. DR GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc. DR GO; GO:0030818; P:negative regulation of cAMP biosynthetic process; IDA:UniProtKB. DR GO; GO:0014063; P:negative regulation of serotonin secretion; ISS:UniProtKB. DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IEA:Ensembl. DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IEA:Ensembl. DR GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl. DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro. DR GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl. DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0051385; P:response to mineralocorticoid; IEA:Ensembl. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro. DR Gene3D; 1.20.1070.10; -; 2. DR InterPro; IPR002147; 5HT1B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24247:SF16; PTHR24247:SF16; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00513; 5HT1BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Behavior; Cell membrane; Complete proteome; KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Lipoprotein; KW Membrane; Palmitate; Phosphoprotein; Polymorphism; Receptor; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1 390 5-hydroxytryptamine receptor 1B. FT /FTId=PRO_0000068916. FT TOPO_DOM 1 49 Extracellular. FT TRANSMEM 50 75 Helical; Name=1. FT TOPO_DOM 76 84 Cytoplasmic. FT TRANSMEM 85 110 Helical; Name=2. FT TOPO_DOM 111 123 Extracellular. FT TRANSMEM 124 145 Helical; Name=3. FT TOPO_DOM 146 165 Cytoplasmic. FT TRANSMEM 166 187 Helical; Name=4. FT TOPO_DOM 188 205 Extracellular. FT TRANSMEM 206 228 Helical; Name=5. FT TOPO_DOM 229 315 Cytoplasmic. FT TRANSMEM 316 336 Helical; Name=6. FT TOPO_DOM 337 349 Extracellular. FT TRANSMEM 350 371 Helical; Name=7. FT TOPO_DOM 372 390 Cytoplasmic. FT REGION 125 134 Agonist binding. FT REGION 327 331 Agonist binding. FT MOTIF 146 148 DRY motif; important for ligand-induced FT conformation changes and signaling. FT MOTIF 365 369 NPxxY motif; important for ligand-induced FT conformation changes and signaling. FT SITE 355 355 Important for species-specific agonist FT sensitivity. FT LIPID 388 388 S-palmitoyl cysteine (Potential). FT CARBOHYD 24 24 N-linked (GlcNAc...) (Potential). FT CARBOHYD 32 32 N-linked (GlcNAc...) (Potential). FT DISULFID 122 199 FT VARIANT 124 124 F -> C (in dbSNP:rs130060). FT /FTId=VAR_011715. FT VARIANT 219 219 F -> L (in dbSNP:rs130061). FT /FTId=VAR_011831. FT VARIANT 367 367 I -> V (in dbSNP:rs130063). FT /FTId=VAR_011832. FT VARIANT 374 374 E -> K (in dbSNP:rs130064). FT /FTId=VAR_011833. FT MUTAGEN 126 126 L->A: No effect on agonist binding. FT MUTAGEN 129 129 D->A: Abolishes agonist binding. FT MUTAGEN 130 130 I->A: Abolishes agonist binding. FT MUTAGEN 133 133 C->A: Abolishes agonist binding. FT MUTAGEN 134 134 T->A: Slightly decreases agonist binding. FT MUTAGEN 200 200 V->A: No effect on agonist binding. FT MUTAGEN 201 201 V->A: No effect on agonist binding. FT MUTAGEN 203 203 T->A: No effect on agonist binding. FT MUTAGEN 209 209 T->A: No effect on agonist binding. FT MUTAGEN 212 212 S->A: No effect on agonist binding. FT MUTAGEN 216 216 A->S: No effect on agonist binding. FT MUTAGEN 327 327 W->A: Abolishes agonist binding. FT MUTAGEN 330 330 F->A: Abolishes agonist binding. FT MUTAGEN 331 331 F->A: No effect on agonist binding. FT MUTAGEN 334 334 S->A: No effect on agonist binding. FT MUTAGEN 337 337 M->A: No effect on agonist binding. FT MUTAGEN 351 351 F->A: No effect on agonist binding. FT MUTAGEN 352 352 D->A: No effect on agonist binding. FT MUTAGEN 355 355 T->A: No effect on agonist binding. FT MUTAGEN 359 359 Y->A: No effect on agonist binding. FT HELIX 40 43 FT HELIX 46 76 FT HELIX 78 80 FT HELIX 83 101 FT HELIX 104 112 FT HELIX 118 152 FT HELIX 154 158 FT HELIX 163 181 FT HELIX 206 216 FT HELIX 218 239 FT HELIX 311 336 FT HELIX 349 372 FT HELIX 374 383 SQ SEQUENCE 390 AA; 43568 MW; CD874DC7EB44CF12 CRC64; MEEPGAQCAP PPPAGSETWV PQANLSSAPS QNCSAKDYIY QDSISLPWKV LLVMLLALIT LATTLSNAFV IATVYRTRKL HTPANYLIAS LAVTDLLVSI LVMPISTMYT VTGRWTLGQV VCDFWLSSDI TCCTASILHL CVIALDRYWA ITDAVEYSAK RTPKRAAVMI ALVWVFSISI SLPPFFWRQA KAEEEVSECV VNTDHILYTV YSTVGAFYFP TLLLIALYGR IYVEARSRIL KQTPNRTGKR LTRAQLITDS PGSTSSVTSI NSRVPDVPSE SGSPVYVNQV KVRVSDALLE KKKLMAARER KATKTLGIIL GAFIVCWLPF FIISLVMPIC KDACWFHLAI FDFFTWLGYL NSLINPIIYT MSNEDFKQAF HKLIRFKCTS // ID 5HT2A_HUMAN Reviewed; 471 AA. AC P28223; B2RAC5; B4DZ79; F5GWE8; Q5T8C0; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 09-JUL-2014, entry version 148. DE RecName: Full=5-hydroxytryptamine receptor 2A; DE Short=5-HT-2; DE Short=5-HT-2A; DE AltName: Full=Serotonin receptor 2A; GN Name=HTR2A; Synonyms=HTR2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain stem; RX PubMed=1722404; DOI=10.1016/0006-291X(91)92105-S; RA Saltzman A.G., Morse B., Whitman M.M., Ivanshchenko Y., Jaye M., RA Felder S.; RT "Cloning of the human serotonin 5-HT2 and 5-HT1C receptor subtypes."; RL Biochem. Biophys. Res. Commun. 181:1469-1478(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1323014; DOI=10.1016/0169-328X(92)90005-V; RA Chen K., Yang W., Grimsby J., Shih J.C.; RT "The human 5-HT2 receptor is encoded by a multiple intron-exon gene."; RL Brain Res. Mol. Brain Res. 14:20-26(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Platelet; RX PubMed=8035173; RA Cook E.H. Jr., Fletcher K.E., Wainwright M., Marks N., Yan S.Y., RA Leventhal B.L.; RT "Primary structure of the human platelet serotonin 5-HT2A receptor: RT identify with frontal cortex serotonin 5-HT2A receptor."; RL J. Neurochem. 63:465-469(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis, and Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T., RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-464 (ISOFORM 1). RC TISSUE=Brain; RA Tritch R.J., Robinson D.L., Sahagan B.G., Horlick R.A.; RT "Cloning and nucleotide sequence of the human(5HT) type 2 receptor."; RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-218, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=1330647; DOI=10.1016/0922-4106(92)90123-D; RA Stam N.J., van Huizen F., van Alebeek C., Brands J., Dijkema R., RA Tonnaer J.A., Olijve W.; RT "Genomic organization, coding sequence and functional expression of RT human 5-HT2 and 5-HT1A receptor genes."; RL Eur. J. Pharmacol. 227:153-162(1992). RN [11] RP INTERACTION WITH MPDZ. RX PubMed=11150294; DOI=10.1074/jbc.M008089200; RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., RA Luebbert H., Ullmer C.; RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with RT PDZ10 of the multi-PDZ domain protein MUPP1."; RL J. Biol. Chem. 276:12974-12982(2001). RN [12] RP INTERACTION WITH INADL; MPP3; PRDX6; DLG4; DLG1; CASK; APBA1 AND RP MAGI2, AND MUTAGENESIS OF GLY-463; ASN-465; CYS-470 AND VAL-471. RX PubMed=14988405; DOI=10.1074/jbc.M312106200; RA Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., RA Dumuis A., Bockaert J., Marin P.; RT "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets RT of PDZ proteins."; RL J. Biol. Chem. 279:20257-20266(2004). RN [13] RP REVIEW. RX PubMed=18476671; DOI=10.1021/cr078224o; RA Nichols D.E., Nichols C.D.; RT "Serotonin receptors."; RL Chem. Rev. 108:1614-1641(2008). RN [14] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18703043; DOI=10.1016/j.ejphar.2008.07.040; RA Cussac D., Boutet-Robinet E., Ailhaud M.C., Newman-Tancredi A., RA Martel J.C., Danty N., Rauly-Lestienne I.; RT "Agonist-directed trafficking of signalling at serotonin 5-HT2A, 5- RT HT2B and 5-HT2C-VSV receptors mediated Gq/11 activation and calcium RT mobilisation in CHO cells."; RL Eur. J. Pharmacol. 594:32-38(2008). RN [15] RP INTERACTION WITH GRM2, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=18297054; DOI=10.1038/nature06612; RA Gonzalez-Maeso J., Ang R.L., Yuen T., Chan P., Weisstaub N.V., RA Lopez-Gimenez J.F., Zhou M., Okawa Y., Callado L.F., Milligan G., RA Gingrich J.A., Filizola M., Meana J.J., Sealfon S.C.; RT "Identification of a serotonin/glutamate receptor complex implicated RT in psychosis."; RL Nature 452:93-97(2008). RN [16] RP FUNCTION. RX PubMed=19057895; DOI=10.1007/s00210-008-0378-4; RA Knauer C.S., Campbell J.E., Chio C.L., Fitzgerald L.W.; RT "Pharmacological characterization of mitogen-activated protein kinase RT activation by recombinant human 5-HT2C, 5-HT2A, and 5-HT2B RT receptors."; RL Naunyn Schmiedebergs Arch. Pharmacol. 379:461-471(2009). RN [17] RP INTERACTION WITH DRD2, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21645528; DOI=10.1016/j.neuropharm.2011.05.023; RA Albizu L., Holloway T., Gonzalez-Maeso J., Sealfon S.C.; RT "Functional crosstalk and heteromerization of serotonin 5-HT2A and RT dopamine D2 receptors."; RL Neuropharmacology 61:770-777(2011). RN [18] RP REVIEW. RX PubMed=20945968; RA Pytliak M., Vargova V., Mechirova V., Felsoci M.; RT "Serotonin receptors - from molecular biology to clinical RT applications."; RL Physiol. Res. 60:15-25(2011). RN [19] RP INTERACTION WITH GRM2, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22300836; DOI=10.1016/j.neuropharm.2012.01.010; RA Delille H.K., Becker J.M., Burkhardt S., Bleher B., Terstappen G.C., RA Schmidt M., Meyer A.H., Unger L., Marek G.J., Mezler M.; RT "Heterocomplex formation of 5-HT2A-mGlu2 and its relevance for RT cellular signaling cascades."; RL Neuropharmacology 62:2184-2191(2012). RN [20] RP VARIANTS ASN-25 AND TYR-452. RX PubMed=8655141; DOI=10.1007/BF02281871; RA Erdmann J., Shimron-Abarbanell D., Rietschel M., Albus M., Maier W., RA Koerner J., Bondy B., Chen K., Shih J.C., Knapp M., Propping P., RA Noethen M.M.; RT "Systematic screening for mutations in the human serotonin-2A (5-HT2A) RT receptor gene: identification of two naturally occurring receptor RT variants and association analysis in schizophrenia."; RL Hum. Genet. 97:614-619(1996). RN [21] RP VARIANTS ASN-25 AND TYR-452. RX PubMed=10581480; RX DOI=10.1002/(SICI)1096-8628(19991215)88:6<621::AID-AJMG9>3.0.CO;2-H; RA Marshall S.E., Bird T.G., Hart K., Welsh K.I.; RT "Unified approach to the analysis of genetic variation in serotonergic RT pathways."; RL Am. J. Med. Genet. 88:621-627(1999). RN [22] RP VARIANTS VAL-197; VAL-447 AND TYR-452. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [23] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine CC (serotonin). Also functions as a receptor for various drugs and CC psychoactive substances, including mescaline, psilocybin, 1-(2,5- CC dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid CC diethylamide (LSD). Ligand binding causes a conformation change CC that triggers signaling via guanine nucleotide-binding proteins (G CC proteins) and modulates the activity of down-stream effectors. CC Beta-arrestin family members inhibit signaling via G proteins and CC mediate activation of alternative signaling pathways. Signaling CC activates phospholipase C and a phosphatidylinositol-calcium CC second messenger system that modulates the activity of CC phosphatidylinositol 3-kinase and promotes the release of Ca(2+) CC ions from intracellular stores. Affects neural activity, CC perception, cognition and mood. Plays a role in the regulation of CC behavior, including responses to anxiogenic situations and CC psychoactive substances. Plays a role in intestinal smooth muscle CC contraction, and may play a role in arterial vasoconstriction. CC -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3, CC PRDX6, DLG4, DLG1, CASK, APBA1 and MAGI2. Interacts with GRM2 and CC DRD2; this may affect signaling. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC Cell projection, dendrite (By similarity). Cell projection, axon CC (By similarity). Cytoplasmic vesicle (By similarity). Membrane, CC caveola (By similarity). Note=Localizes to the postsynaptic CC thickening of axo-dendritic synapses (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P28223-1; Sequence=Displayed; CC Name=2; CC IsoId=P28223-2; Sequence=VSP_046663; CC Note=Ref.5 (BAG63991) sequence is in conflict in position: CC 49:D->N; CC -!- TISSUE SPECIFICITY: Detected in brain cortex (at protein level). CC Detected in blood platelets. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with INADL, CASK, APBA1, DLG1 and DLG4. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and CC polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HTR2A"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X57830; CAA40963.1; -; mRNA. DR EMBL; S42168; AAB22791.2; -; Genomic_DNA. DR EMBL; S42165; AAB22791.2; JOINED; Genomic_DNA. DR EMBL; S42167; AAB22791.2; JOINED; Genomic_DNA. DR EMBL; S71229; AAB31320.1; -; mRNA. DR EMBL; AF498982; AAM21129.1; -; mRNA. DR EMBL; AK302787; BAG63991.1; -; mRNA. DR EMBL; AK314132; BAG36822.1; -; mRNA. DR EMBL; AL160397; CAI16877.1; -; Genomic_DNA. DR EMBL; AL136958; CAI16877.1; JOINED; Genomic_DNA. DR EMBL; AL136958; CAI12227.1; -; Genomic_DNA. DR EMBL; AL160397; CAI12227.1; JOINED; Genomic_DNA. DR EMBL; CH471075; EAX08770.1; -; Genomic_DNA. DR EMBL; BC069356; AAH69356.1; -; mRNA. DR EMBL; BC069576; AAH69576.1; -; mRNA. DR EMBL; BC074848; AAH74848.1; -; mRNA. DR EMBL; BC074849; AAH74849.1; -; mRNA. DR EMBL; BC096839; AAH96839.1; -; mRNA. DR EMBL; M86841; AAA58354.1; -; mRNA. DR EMBL; S50130; AAB24166.2; -; Genomic_DNA. DR EMBL; S49737; AAB24166.2; JOINED; Genomic_DNA. DR EMBL; S50113; AAB24166.2; JOINED; Genomic_DNA. DR CCDS; CCDS53867.1; -. [P28223-2] DR CCDS; CCDS9405.1; -. [P28223-1] DR PIR; A43956; A43956. DR RefSeq; NP_000612.1; NM_000621.4. [P28223-1] DR RefSeq; NP_001159419.1; NM_001165947.2. [P28223-2] DR UniGene; Hs.72630; -. DR ProteinModelPortal; P28223; -. DR SMR; P28223; 38-406. DR BioGrid; 109588; 4. DR DIP; DIP-41844N; -. DR MINT; MINT-443877; -. DR STRING; 9606.ENSP00000367959; -. DR BindingDB; P28223; -. DR ChEMBL; CHEMBL2096662; -. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB01239; Chlorprothixene. DR DrugBank; DB00604; Cisapride. DR DrugBank; DB01242; Clomipramine. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB00924; Cyclobenzaprine. DR DrugBank; DB00434; Cyproheptadine. DR DrugBank; DB00320; Dihydroergotamine. DR DrugBank; DB00843; Donepezil. DR DrugBank; DB00751; Epinastine. DR DrugBank; DB00696; Ergotamine. DR DrugBank; DB00176; Fluvoxamine. DR DrugBank; DB00933; Mesoridazine. DR DrugBank; DB00247; Methysergide. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB00805; Minaprine. DR DrugBank; DB00370; Mirtazapine. DR DrugBank; DB01149; Nefazodone. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB01267; Paliperidone. DR DrugBank; DB00715; Paroxetine. DR DrugBank; DB00433; Prochlorperazine. DR DrugBank; DB00420; Promazine. DR DrugBank; DB01069; Promethazine. DR DrugBank; DB00777; Propiomazine. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB00734; Risperidone. DR DrugBank; DB06144; Sertindole. DR DrugBank; DB00372; Thiethylperazine. DR DrugBank; DB00679; Thioridazine. DR DrugBank; DB00752; Tranylcypromine. DR DrugBank; DB00656; Trazodone. DR DrugBank; DB00285; Venlafaxine. DR DrugBank; DB00246; Ziprasidone. DR GuidetoPHARMACOLOGY; 6; -. DR PhosphoSite; P28223; -. DR DMDM; 543727; -. DR PaxDb; P28223; -. DR PRIDE; P28223; -. DR Ensembl; ENST00000378688; ENSP00000367959; ENSG00000102468. [P28223-1] DR Ensembl; ENST00000542664; ENSP00000437737; ENSG00000102468. [P28223-1] DR Ensembl; ENST00000543956; ENSP00000441861; ENSG00000102468. [P28223-2] DR GeneID; 3356; -. DR KEGG; hsa:3356; -. DR UCSC; uc010acr.4; human. [P28223-1] DR CTD; 3356; -. DR GeneCards; GC13M047407; -. DR HGNC; HGNC:5293; HTR2A. DR HPA; HPA014011; -. DR MIM; 182135; gene. DR neXtProt; NX_P28223; -. DR PharmGKB; PA193; -. DR eggNOG; NOG247243; -. DR HOGENOM; HOG000240378; -. DR HOVERGEN; HBG107487; -. DR InParanoid; P28223; -. DR KO; K04157; -. DR OMA; CTMVALG; -. DR OrthoDB; EOG70ZZN5; -. DR PhylomeDB; P28223; -. DR TreeFam; TF316350; -. DR Reactome; REACT_111102; Signal Transduction. DR SignaLink; P28223; -. DR GeneWiki; 5-HT2A_receptor; -. DR GenomeRNAi; 3356; -. DR NextBio; 13270; -. DR PRO; PR:P28223; -. DR ArrayExpress; P28223; -. DR Bgee; P28223; -. DR CleanEx; HS_HTR2A; -. DR Genevestigator; P28223; -. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0070852; C:cell body fiber; IEA:Ensembl. DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0071886; F:1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding; IDA:UniProtKB. DR GO; GO:0008144; F:drug binding; IDA:UniProtKB. DR GO; GO:0051378; F:serotonin binding; IDA:UniProtKB. DR GO; GO:0004993; F:serotonin receptor activity; IDA:UniProtKB. DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl. DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl. DR GO; GO:0008219; P:cell death; IEA:Ensembl. DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB. DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl. DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR GO; GO:0043267; P:negative regulation of potassium ion transport; IEA:Ensembl. DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IEA:Ensembl. DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB. DR GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl. DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IDA:UniProtKB. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl. DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro. DR GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl. DR GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB. DR GO; GO:0042493; P:response to drug; IDA:UniProtKB. DR GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0030431; P:sleep; IEA:Ensembl. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl. DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IEA:Ensembl. DR Gene3D; 1.20.1070.10; -; 1. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24247:SF30; PTHR24247:SF30; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Behavior; Cell membrane; Cell projection; KW Complete proteome; Cytoplasmic vesicle; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; KW Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1 471 5-hydroxytryptamine receptor 2A. FT /FTId=PRO_0000068946. FT TOPO_DOM 1 75 Extracellular (By similarity). FT TRANSMEM 76 99 Helical; Name=1; (By similarity). FT TOPO_DOM 100 110 Cytoplasmic (By similarity). FT TRANSMEM 111 132 Helical; Name=2; (By similarity). FT TOPO_DOM 133 148 Extracellular (By similarity). FT TRANSMEM 149 171 Helical; Name=3; (By similarity). FT TOPO_DOM 172 191 Cytoplasmic (By similarity). FT TRANSMEM 192 215 Helical; Name=4; (By similarity). FT TOPO_DOM 216 233 Extracellular (By similarity). FT TRANSMEM 234 254 Helical; Name=5; (By similarity). FT TOPO_DOM 255 324 Cytoplasmic (By similarity). FT TRANSMEM 325 346 Helical; Name=6; (By similarity). FT TOPO_DOM 347 362 Extracellular (By similarity). FT TRANSMEM 363 384 Helical; Name=7; (By similarity). FT TOPO_DOM 385 471 Cytoplasmic (By similarity). FT REGION 155 160 Agonist binding (By similarity). FT REGION 336 340 Agonist binding (By similarity). FT MOTIF 172 174 DRY motif; important for ligand-induced FT conformation changes (By similarity). FT MOTIF 376 380 NPxxY motif; important for ligand-induced FT conformation changes and signaling (By FT similarity). FT MOTIF 469 471 PDZ-binding. FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential). FT CARBOHYD 38 38 N-linked (GlcNAc...) (Potential). FT CARBOHYD 44 44 N-linked (GlcNAc...) (Potential). FT CARBOHYD 51 51 N-linked (GlcNAc...) (Potential). FT CARBOHYD 54 54 N-linked (GlcNAc...) (Potential). FT DISULFID 148 227 By similarity. FT DISULFID 349 353 By similarity. FT VAR_SEQ 1 138 MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSD FT AFNWTVDSENRTNLSCEGCLSPSCLSLLHLQEKNWSALLTA FT VVIILTIAGNILVIMAVSLEKKLQNATNYFLMSLAIADMLL FT GFLVMPVSMLTILYG -> MQFLKSAKQKPNYYHIMLVEDQ FT EEGTLHQFNYCERCSESQNNKCISCVDPEDKW (in FT isoform 2). FT /FTId=VSP_046663. FT VARIANT 25 25 T -> N (in dbSNP:rs1805055). FT /FTId=VAR_003448. FT VARIANT 197 197 I -> V (in dbSNP:rs6304). FT /FTId=VAR_013901. FT VARIANT 447 447 A -> V (in dbSNP:rs6308). FT /FTId=VAR_013902. FT VARIANT 452 452 H -> Y (in dbSNP:rs6314). FT /FTId=VAR_003449. FT MUTAGEN 463 463 G->V: Loss of interaction with INADL. FT MUTAGEN 465 465 N->S: No effect on interaction with FT INADL. Acquires the binding properties of FT HTR2C; when associated with S-470. FT MUTAGEN 470 470 C->S: No effect on interaction with FT INADL. Acquires the binding properties of FT HTR2C; when associated with S-465. FT MUTAGEN 471 471 V->A: Loss of interaction with INADL, FT CASK, APBA1, DLG1 and DLG4. SQ SEQUENCE 471 AA; 52603 MW; EF8AAC0BC5379DA2 CRC64; MDILCEENTS LSSTTNSLMQ LNDDTRLYSN DFNSGEANTS DAFNWTVDSE NRTNLSCEGC LSPSCLSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VSFFIPLTIM VITYFLTIKS LQKEATLCVS DLGTRAKLAS FSFLPQSSLS SEKLFQRSIH REPGSYTGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNEDVIGA LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENKKPLQLIL VNTIPALAYK SSQLQMGQKK NSKQDAKTTD NDCSMVALGK QHSEEASKDN SDGVNEKVSC V // ID 5HT2B_HUMAN Reviewed; 481 AA. AC P41595; B2R9D5; Q53TI1; Q62221; Q6P523; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JUL-2014, entry version 139. DE RecName: Full=5-hydroxytryptamine receptor 2B; DE Short=5-HT-2B; DE Short=5-HT2B; DE AltName: Full=Serotonin receptor 2B; GN Name=HTR2B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=8143856; DOI=10.1016/0014-5793(94)80590-3; RA Schmuck K., Ullmer C., Engels P., Luebbert H.; RT "Cloning and functional characterization of the human 5-HT2B serotonin RT receptor."; RL FEBS Lett. 342:85-90(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=7926008; DOI=10.1016/0014-5793(94)00968-6; RA Choi D.S., Birraux G., Launay J.-M., Maroteaux L.; RT "The human serotonin 5-HT2B receptor: pharmacological link between 5- RT HT2 and 5-HT1D receptors."; RL FEBS Lett. 352:393-399(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Uterus; RX PubMed=8078486; RA Kursar J.D., Nelson D.L., Wainscott D.B., Baez M.; RT "Molecular cloning, functional expression, and mRNA tissue RT distribution of the human 5-hydroxytryptamine2B receptor."; RL Mol. Pharmacol. 46:227-234(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10722792; DOI=10.1006/mcpr.1999.0281; RA Kim S.J., Veenstra-VanderWeele J., Hanna G.L., Gonen D., RA Leventhal B.L., Cook E.H. Jr.; RT "Mutation screening of human 5-HT(2B) receptor gene in early-onset RT obsessive-compulsive disorder."; RL Mol. Cell. Probes 14:47-52(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=8882600; DOI=10.1111/j.1476-5381.1996.tb16700.x; RA Ullmer C., Boddeke H.G., Schmuck K., Lubbert H.; RT "5-HT2B receptor-mediated calcium release from ryanodine-sensitive RT intracellular stores in human pulmonary artery endothelial cells."; RL Br. J. Pharmacol. 117:1081-1088(1996). RN [11] RP INTERACTION WITH MPDZ. RX PubMed=11150294; DOI=10.1074/jbc.M008089200; RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., RA Luebbert H., Ullmer C.; RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with RT PDZ10 of the multi-PDZ domain protein MUPP1."; RL J. Biol. Chem. 276:12974-12982(2001). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12970106; DOI=10.1038/sj.bjp.0705437; RA Schaerlinger B., Hickel P., Etienne N., Guesnier L., Maroteaux L.; RT "Agonist actions of dihydroergotamine at 5-HT2B and 5-HT2C receptors RT and their possible relevance to antimigraine efficacy."; RL Br. J. Pharmacol. 140:277-284(2003). RN [13] RP REVIEW. RX PubMed=18476671; DOI=10.1021/cr078224o; RA Nichols D.E., Nichols C.D.; RT "Serotonin receptors."; RL Chem. Rev. 108:1614-1641(2008). RN [14] RP FUNCTION. RX PubMed=18703043; DOI=10.1016/j.ejphar.2008.07.040; RA Cussac D., Boutet-Robinet E., Ailhaud M.C., Newman-Tancredi A., RA Martel J.C., Danty N., Rauly-Lestienne I.; RT "Agonist-directed trafficking of signalling at serotonin 5-HT2A, 5- RT HT2B and 5-HT2C-VSV receptors mediated Gq/11 activation and calcium RT mobilisation in CHO cells."; RL Eur. J. Pharmacol. 594:32-38(2008). RN [15] RP INVOLVEMENT IN IMPULSIVE BEHAVIOR, TISSUE SPECIFICITY, POLYMORPHISM, RP AND VARIANTS GLU-45; LEU-173 AND TRP-388. RX PubMed=21179162; DOI=10.1038/nature09629; RA Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T., RA Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., RA Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., RA Peltonen L., Virkkunen M., Goldman D.; RT "A population-specific HTR2B stop codon predisposes to severe RT impulsivity."; RL Nature 468:1061-1066(2010). RN [16] RP REVIEW. RX PubMed=20945968; RA Pytliak M., Vargova V., Mechirova V., Felsoci M.; RT "Serotonin receptors - from molecular biology to clinical RT applications."; RL Physiol. Res. 60:15-25(2011). RN [17] RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-132; ASP-135; RP VAL-136; SER-139; THR-140; VAL-208; LEU-209; LYS-211; PHE-217; RP MET-218; ALA-225; TRP-337; PHE-340; ASN-344; LEU-347; VAL-348; RP LEU-362; GLU-363; VAL-366 AND TYR-370. RX PubMed=23519210; DOI=10.1126/science.1232807; RA Wang C., Jiang Y., Ma J., Wu H., Wacker D., Katritch V., Han G.W., RA Liu W., Huang X.P., Vardy E., McCorvy J.D., Gao X., Zhou X.E., RA Melcher K., Zhang C., Bai F., Yang H., Yang L., Jiang H., Roth B.L., RA Cherezov V., Stevens R.C., Xu H.E.; RT "Structural basis for molecular recognition at serotonin receptors."; RL Science 340:610-614(2013). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-405 IN COMPLEX WITH THE RP AGONIST ERGOTAMINE, FUNCTION, ROLE IN ARRESTIN-MEDIATED SIGNALING AND RP CALCIUM RELEASE, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, AND RP DISULFIDE BONDS. RX PubMed=23519215; DOI=10.1126/science.1232808; RA Wacker D., Wang C., Katritch V., Han G.W., Huang X.P., Vardy E., RA McCorvy J.D., Jiang Y., Chu M., Siu F.Y., Liu W., Xu H.E., RA Cherezov V., Roth B.L., Stevens R.C.; RT "Structural features for functional selectivity at serotonin RT receptors."; RL Science 340:615-619(2013). CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine CC (serotonin). Also functions as a receptor for various ergot CC alkaloid derivatives and psychoactive substances. Ligand binding CC causes a conformation change that triggers signaling via guanine CC nucleotide-binding proteins (G proteins) and modulates the CC activity of down-stream effectors. Beta-arrestin family members CC inhibit signaling via G proteins and mediate activation of CC alternative signaling pathways. Signaling activates a CC phosphatidylinositol-calcium second messenger system that CC modulates the activity of phosphatidylinositol 3-kinase and down- CC stream signaling cascades and promotes the release of Ca(2+) ions CC from intracellular stores. Plays a role in the regulation of CC dopamine and 5-hydroxytryptamine release, 5-hydroxytryptamine CC uptake and in the regulation of extracellular dopamine and 5- CC hydroxytryptamine levels, and thereby affects neural activity. May CC play a role in the perception of pain. Plays a role in the CC regulation of behavior, including impulsive behavior. Required for CC normal proliferation of embryonic cardiac myocytes and normal CC heart development. Protects cardiomyocytes against apoptosis. CC Plays a role in the adaptation of pulmonary arteries to chronic CC hypoxia. Plays a role in vasoconstriction. Required for normal CC osteoblast function and proliferation, and for maintaining normal CC bone density. Required for normal proliferation of the CC interstitial cells of Cajal in the intestine. CC -!- SUBUNIT: Interacts with MPDZ. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC Cell junction, synapse, synaptosome (By similarity). CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in liver, kidney, heart, CC pulmonary artery, and intestine. Detected at lower levels in CC blood, placenta and brain, especially in cerebellum, occipital CC cortex and frontal cortex. CC -!- DOMAIN: Ligands are bound in a hydrophobic pocket formed by the CC transmembrane helices. CC -!- POLYMORPHISM: A variation at a single nucleotide base, which CC results in an erroneous stop codon and affects Gln-20, triggers CC non-sense mediated RNA decay, such that no HTR2B-receptor protein CC is expressed. It is associated with impulsive behavior and co- CC segregates with disorders characterized by impulsivity. However, CC the presence of this variant is not in itself sufficient to cause CC impulsive behavior: male sex, testosterone level, alcohol and CC stress exposure are other factors playing important roles. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=On the spur of a whim - CC Issue 127 of March 2011; CC URL="http://web.expasy.org/spotlight/back_issues/127"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X77307; CAA54513.1; -; mRNA. DR EMBL; Z36748; CAA85319.1; -; mRNA. DR EMBL; AF156160; AAD39259.1; -; Genomic_DNA. DR EMBL; AF156158; AAD39259.1; JOINED; Genomic_DNA. DR EMBL; AF156159; AAD39259.1; JOINED; Genomic_DNA. DR EMBL; AY136751; AAN01277.1; -; mRNA. DR EMBL; AC009407; AAX93128.1; -; Genomic_DNA. DR EMBL; AK313741; BAG36482.1; -; mRNA. DR EMBL; CH471063; EAW70949.1; -; Genomic_DNA. DR EMBL; BC063123; AAH63123.1; -; mRNA. DR CCDS; CCDS2483.1; -. DR PIR; S43687; S43687. DR PIR; S49442; S49442. DR RefSeq; NP_000858.3; NM_000867.4. DR UniGene; Hs.421649; -. DR PDB; 4IB4; X-ray; 2.70 A; A=36-248, A=314-405. DR PDB; 4NC3; X-ray; 2.80 A; A=36-248, A=314-405. DR PDBsum; 4IB4; -. DR PDBsum; 4NC3; -. DR ProteinModelPortal; P41595; -. DR SMR; P41595; 48-400. DR BioGrid; 109589; 3. DR MINT; MINT-444010; -. DR STRING; 9606.ENSP00000258400; -. DR BindingDB; P41595; -. DR ChEMBL; CHEMBL2111466; -. DR DrugBank; DB01239; Chlorprothixene. DR DrugBank; DB00216; Eletriptan. DR DrugBank; DB00574; Fenfluramine. DR DrugBank; DB01403; Methotrimeprazine. DR DrugBank; DB00805; Minaprine. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB00669; Sumatriptan. DR DrugBank; DB01079; Tegaserod. DR DrugBank; DB00508; Triflupromazine. DR GuidetoPHARMACOLOGY; 7; -. DR TCDB; 9.A.14.3.7; the g-protein-coupled receptor (gpcr) family. DR PhosphoSite; P41595; -. DR DMDM; 1168220; -. DR PaxDb; P41595; -. DR PRIDE; P41595; -. DR DNASU; 3357; -. DR Ensembl; ENST00000258400; ENSP00000258400; ENSG00000135914. DR GeneID; 3357; -. DR KEGG; hsa:3357; -. DR UCSC; uc002vro.3; human. DR CTD; 3357; -. DR GeneCards; GC02M231936; -. DR HGNC; HGNC:5294; HTR2B. DR HPA; CAB011448; -. DR HPA; HPA012867; -. DR MIM; 601122; gene. DR neXtProt; NX_P41595; -. DR PharmGKB; PA29554; -. DR eggNOG; NOG247243; -. DR HOGENOM; HOG000240378; -. DR HOVERGEN; HBG107487; -. DR InParanoid; P41595; -. DR KO; K04157; -. DR OMA; CDSCNQT; -. DR OrthoDB; EOG70ZZN5; -. DR PhylomeDB; P41595; -. DR TreeFam; TF316350; -. DR Reactome; REACT_111102; Signal Transduction. DR GeneWiki; 5-HT2B_receptor; -. DR GenomeRNAi; 3357; -. DR NextBio; 13274; -. DR PRO; PR:P41595; -. DR ArrayExpress; P41595; -. DR Bgee; P41595; -. DR CleanEx; HS_HTR2B; -. DR Genevestigator; P41595; -. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045202; C:synapse; IEA:UniProtKB-KW. DR GO; GO:0008144; F:drug binding; IDA:UniProtKB. DR GO; GO:0001965; F:G-protein alpha-subunit binding; IMP:UniProtKB. DR GO; GO:0005099; F:Ras GTPase activator activity; ISS:UniProtKB. DR GO; GO:0051378; F:serotonin binding; IDA:UniProtKB. DR GO; GO:0004993; F:serotonin receptor activity; IDA:UniProtKB. DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB. DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW. DR GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB. DR GO; GO:0003300; P:cardiac muscle hypertrophy; ISS:UniProtKB. DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB. DR GO; GO:0071502; P:cellular response to temperature stimulus; ISS:UniProtKB. DR GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB. DR GO; GO:0048598; P:embryonic morphogenesis; ISS:UniProtKB. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:UniProtKB. DR GO; GO:0002031; P:G-protein coupled receptor internalization; IEA:Ensembl. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB. DR GO; GO:0014827; P:intestine smooth muscle contraction; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0010507; P:negative regulation of autophagy; IMP:UniProtKB. DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB. DR GO; GO:0014033; P:neural crest cell differentiation; ISS:UniProtKB. DR GO; GO:0001755; P:neural crest cell migration; ISS:UniProtKB. DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IMP:UniProtKB. DR GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB. DR GO; GO:0050715; P:positive regulation of cytokine secretion; ISS:UniProtKB. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB. DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IDA:UniProtKB. DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IDA:UniProtKB. DR GO; GO:0070528; P:protein kinase C signaling; IMP:UniProtKB. DR GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0050795; P:regulation of behavior; IMP:UniProtKB. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB. DR GO; GO:0042493; P:response to drug; IDA:UniProtKB. DR GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0042310; P:vasoconstriction; IMP:UniProtKB. DR Gene3D; 1.20.1070.10; -; 2. DR InterPro; IPR000482; 5HT2B_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24247:SF31; PTHR24247:SF31; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00651; 5HT2BRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Behavior; Cell junction; Cell membrane; KW Complete proteome; Disulfide bond; G-protein coupled receptor; KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Polymorphism; KW Receptor; Reference proteome; Synapse; Synaptosome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1 481 5-hydroxytryptamine receptor 2B. FT /FTId=PRO_0000068953. FT TOPO_DOM 1 56 Extracellular. FT TRANSMEM 57 79 Helical; Name=1. FT TOPO_DOM 80 90 Cytoplasmic. FT TRANSMEM 91 113 Helical; Name=2. FT TOPO_DOM 114 129 Extracellular. FT TRANSMEM 130 151 Helical; Name=3. FT TOPO_DOM 152 171 Cytoplasmic. FT TRANSMEM 172 192 Helical; Name=4. FT TOPO_DOM 193 216 Extracellular. FT TRANSMEM 217 239 Helical; Name=5. FT TOPO_DOM 240 324 Cytoplasmic. FT TRANSMEM 325 345 Helical; Name=6. FT TOPO_DOM 346 360 Extracellular. FT TRANSMEM 361 382 Helical; Name=7. FT TOPO_DOM 383 481 Cytoplasmic. FT REGION 135 140 Agonist binding. FT REGION 337 341 Agonist binding. FT MOTIF 152 154 DRY motif; important for ligand-induced FT conformation changes. FT MOTIF 212 215 [DE]RFG motif; may stabilize a FT conformation that preferentially FT activates signaling via beta-arrestin FT family members. FT MOTIF 376 380 NPxxY motif; important for ligand-induced FT conformation changes and signaling. FT MOTIF 479 481 PDZ-binding. FT LIPID 397 397 S-palmitoyl cysteine (Potential). FT CARBOHYD 30 30 N-linked (GlcNAc...) (Potential). FT DISULFID 128 207 FT DISULFID 350 353 FT VARIANT 45 45 Q -> E (in dbSNP:rs78484969). FT /FTId=VAR_064574. FT VARIANT 173 173 F -> L (in dbSNP:rs77570025). FT /FTId=VAR_064575. FT VARIANT 388 388 R -> W (in dbSNP:rs77982984). FT /FTId=VAR_064576. FT VARIANT 421 421 M -> V (in dbSNP:rs6736017). FT /FTId=VAR_055907. FT MUTAGEN 132 132 L->A: No effect on agonist binding. FT MUTAGEN 135 135 D->A: Abolishes agonist binding. FT MUTAGEN 136 136 V->A: Slightly decreases agonist binding. FT MUTAGEN 139 139 S->A: Slightly decreases agonist binding. FT MUTAGEN 140 140 T->A: Slightly decreases agonist binding. FT MUTAGEN 208 208 V->A: No effect on agonist binding. FT MUTAGEN 209 209 L->A: No effect on agonist binding. FT MUTAGEN 211 211 K->A: Impairs protein folding and FT stability. Strongly reduced cell surface FT expression. FT MUTAGEN 217 217 F->A: Slightly decreases agonist binding. FT MUTAGEN 218 218 M->A: No effect on agonist binding. FT MUTAGEN 225 225 A->S: No effect on agonist binding. FT MUTAGEN 337 337 W->A: Slightly decreases agonist binding. FT MUTAGEN 340 340 F->A: Slightly decreases agonist binding. FT MUTAGEN 344 344 N->A: Slightly decreases agonist binding. FT MUTAGEN 347 347 L->A: No effect on agonist binding. FT MUTAGEN 348 348 V->A: No effect on agonist binding. FT MUTAGEN 362 362 L->A: No effect on agonist binding. FT MUTAGEN 363 363 E->A: No effect on agonist binding. FT MUTAGEN 366 366 V->A: No effect on agonist binding. FT MUTAGEN 370 370 Y->A: Slightly decreases agonist binding. FT CONFLICT 452 452 T -> P (in Ref. 2; CAA85319). FT CONFLICT 477 477 Q -> R (in Ref. 9; AAH63123). FT HELIX 54 63 FT HELIX 65 81 FT HELIX 83 85 FT HELIX 88 106 FT HELIX 108 111 FT HELIX 113 116 FT HELIX 127 158 FT HELIX 165 187 FT HELIX 189 193 FT HELIX 211 225 FT HELIX 227 248 FT HELIX 314 349 FT STRAND 351 353 FT HELIX 355 381 FT HELIX 385 394 FT TURN 395 397 SQ SEQUENCE 481 AA; 54298 MW; CDA4447ECDBA3B46 CRC64; MALSYRVSEL QSTIPEHILQ STFVHVISSN WSGLQTESIP EEMKQIVEEQ GNKLHWAALL ILMVIIPTIG GNTLVILAVS LEKKLQYATN YFLMSLAVAD LLVGLFVMPI ALLTIMFEAM WPLPLVLCPA WLFLDVLFST ASIMHLCAIS VDRYIAIKKP IQANQYNSRA TAFIKITVVW LISIGIAIPV PIKGIETDVD NPNNITCVLT KERFGDFMLF GSLAAFFTPL AIMIVTYFLT IHALQKKAYL VKNKPPQRLT WLTVSTVFQR DETPCSSPEK VAMLDGSRKD KALPNSGDET LMRRTSTIGK KSVQTISNEQ RASKVLGIVF FLFLLMWCPF FITNITLVLC DSCNQTTLQM LLEIFVWIGY VSSGVNPLVY TLFNKTFRDA FGRYITCNYR ATKSVKTLRK RSSKIYFRNP MAENSKFFKK HGIRNGINPA MYQSPMRLRS STIQSSSIIL LDTLLLTENE GDKTEEQVSY V // ID 5HT2C_HUMAN Reviewed; 458 AA. AC P28335; B1AMW4; Q5VUF8; Q9NP28; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 09-JUL-2014, entry version 152. DE RecName: Full=5-hydroxytryptamine receptor 2C; DE Short=5-HT-2C; DE Short=5-HT2C; DE Short=5-HTR2C; DE AltName: Full=5-hydroxytryptamine receptor 1C; DE Short=5-HT-1C; DE Short=5-HT1C; DE AltName: Full=Serotonin receptor 2C; DE Flags: Precursor; GN Name=HTR2C; Synonyms=HTR1C; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=1722404; DOI=10.1016/0006-291X(91)92105-S; RA Saltzman A.G., Morse B., Whitman M.M., Ivanshchenko Y., Jaye M., RA Felder S.; RT "Cloning of the human serotonin 5-HT2 and 5-HT1C receptor subtypes."; RL Biochem. Biophys. Res. Commun. 181:1469-1478(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Hippocampus, and Placenta; RX PubMed=7895773; DOI=10.1016/0922-4106(94)90042-6; RA Stam N.J., Vanderheyden P., Van Alebeek C., Klomp J., De Boer T., RA Van Delft A.M.L., Olijve W.; RT "Genomic organisation and functional expression of the gene encoding RT the human serotonin 5-HT2C receptor."; RL Eur. J. Pharmacol. 269:339-348(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=8812491; DOI=10.1006/geno.1996.0397; RA Xie E., Zhao L., Levine A.J., Shenk T., Chang L.-S.; RT "The human serotonin 5-HT2C receptor: complete cDNA, genomic RT structure, and alternatively spliced variant."; RL Genomics 35:551-561(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND RNA EDITING OF POSITIONS RP 156; 158 AND 160. RC TISSUE=Brain; RX PubMed=9928237; DOI=10.1111/j.1749-6632.1998.tb10171.x; RA Niswender C.M., Sanders-Bush E., Emeson R.B.; RT "Identification and characterization of RNA editing events within the RT 5-HT2C receptor."; RL Ann. N. Y. Acad. Sci. 861:38-48(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP INTERACTION WITH MPDZ, DOMAIN, MUTAGENESIS OF SER-456; SER-457 AND RP VAL-458, AND GLYCOSYLATION. RX PubMed=11150294; DOI=10.1074/jbc.M008089200; RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., RA Luebbert H., Ullmer C.; RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with RT PDZ10 of the multi-PDZ domain protein MUPP1."; RL J. Biol. Chem. 276:12974-12982(2001). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12970106; DOI=10.1038/sj.bjp.0705437; RA Schaerlinger B., Hickel P., Etienne N., Guesnier L., Maroteaux L.; RT "Agonist actions of dihydroergotamine at 5-HT2B and 5-HT2C receptors RT and their possible relevance to antimigraine efficacy."; RL Br. J. Pharmacol. 140:277-284(2003). RN [11] RP INTERACTION WITH ARRB2, AND MUTAGENESIS OF PRO-159. RX PubMed=16319069; DOI=10.1074/jbc.M508074200; RA Marion S., Oakley R.H., Kim K.-M., Caron M.G., Barak L.S.; RT "A beta-arrestin binding determinant common to the second RT intracellular loops of rhodopsin family G protein-coupled receptors."; RL J. Biol. Chem. 281:2932-2938(2006). RN [12] RP REVIEW. RX PubMed=18476671; DOI=10.1021/cr078224o; RA Nichols D.E., Nichols C.D.; RT "Serotonin receptors."; RL Chem. Rev. 108:1614-1641(2008). RN [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18703043; DOI=10.1016/j.ejphar.2008.07.040; RA Cussac D., Boutet-Robinet E., Ailhaud M.C., Newman-Tancredi A., RA Martel J.C., Danty N., Rauly-Lestienne I.; RT "Agonist-directed trafficking of signalling at serotonin 5-HT2A, 5- RT HT2B and 5-HT2C-VSV receptors mediated Gq/11 activation and calcium RT mobilisation in CHO cells."; RL Eur. J. Pharmacol. 594:32-38(2008). RN [14] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19057895; DOI=10.1007/s00210-008-0378-4; RA Knauer C.S., Campbell J.E., Chio C.L., Fitzgerald L.W.; RT "Pharmacological characterization of mitogen-activated protein kinase RT activation by recombinant human 5-HT2C, 5-HT2A, and 5-HT2B RT receptors."; RL Naunyn Schmiedebergs Arch. Pharmacol. 379:461-471(2009). RN [15] RP REVIEW. RX PubMed=20945968; RA Pytliak M., Vargova V., Mechirova V., Felsoci M.; RT "Serotonin receptors - from molecular biology to clinical RT applications."; RL Physiol. Res. 60:15-25(2011). RN [16] RP SIGNAL SEQUENCE CLEAVAGE SITE, AND VARIANT SER-23. RX PubMed=22497996; DOI=10.1016/j.ejphar.2012.03.043; RA Jahnsen J.A., Uhlen S.; RT "The N-terminal region of the human 5-HT(2)C receptor has as a RT cleavable signal peptide."; RL Eur. J. Pharmacol. 684:44-50(2012). RN [17] RP VARIANT SER-23. RX PubMed=7557992; DOI=10.1006/geno.1995.1042; RA Lappalainen J., Zhang L., Dean M., Oz M., Ozaki N., Yu D., RA Virkkunen M., Weight F., Linnoila M., Goldman D.; RT "Identification, expression, and pharmacology of a Cys23-Ser23 RT substitution in the human 5-HT2c receptor gene (HTR2C)."; RL Genomics 27:274-279(1995). RN [18] RP VARIANT SER-23. RX PubMed=10206230; RX DOI=10.1002/(SICI)1096-8628(19990416)88:2<126::AID-AJMG6>3.3.CO;2-D; RA Samochowiec J., Smolka M., Winterer G., Rommelspacher H., RA Schmidt L.G., Sander T.; RT "Association analysis between a Cys23Ser substitution polymorphism of RT the human 5-HT2c receptor gene and neuronal hyperexcitability."; RL Am. J. Med. Genet. 88:126-130(1999). RN [19] RP VARIANT SER-23. RX PubMed=10581480; RX DOI=10.1002/(SICI)1096-8628(19991215)88:6<621::AID-AJMG9>3.0.CO;2-H; RA Marshall S.E., Bird T.G., Hart K., Welsh K.I.; RT "Unified approach to the analysis of genetic variation in serotonergic RT pathways."; RL Am. J. Med. Genet. 88:621-627(1999). RN [20] RP VARIANT SER-23. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [21] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine CC (serotonin). Also functions as a receptor for various drugs and CC psychoactive substances, including ergot alkaloid derivatives, 1- CC 2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid CC diethylamide (LSD). Ligand binding causes a conformation change CC that triggers signaling via guanine nucleotide-binding proteins (G CC proteins) and modulates the activity of down-stream effectors. CC Beta-arrestin family members inhibit signaling via G proteins and CC mediate activation of alternative signaling pathways. Signaling CC activates a phosphatidylinositol-calcium second messenger system CC that modulates the activity of phosphatidylinositol 3-kinase and CC down-stream signaling cascades and promotes the release of Ca(2+) CC ions from intracellular stores. Regulates neuronal activity via CC the activation of short transient receptor potential calcium CC channels in the brain, and thereby modulates the activation of CC pro-opiomelacortin neurons and the release of CRH that then CC regulates the release of corticosterone. Plays a role in the CC regulation of appetite and eating behavior, responses to CC anxiogenic stimuli and stress. Plays a role in insulin sensitivity CC and glucose homeostasis. CC -!- SUBUNIT: Interacts with MPDZ. Interacts with ARRB2. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P28335-1; Sequence=Displayed; CC Name=2; CC IsoId=P28335-2; Sequence=VSP_045171; CC -!- TISSUE SPECIFICITY: Detected in brain. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the CC interaction with MPDZ. CC -!- PTM: N-glycosylated. CC -!- RNA EDITING: Modified_positions=156, 158, 160; Note=Partially CC edited. RNA editing generates receptor isoforms that differ in CC their ability to interact with the phospholipase C signaling CC cascade in a transfected cell line, suggesting that this RNA CC processing event may contribute to the modulation of serotonergic CC neurotransmission in the central nervous system. CC -!- POLYMORPHISM: Position 23 is polymorphic; the frequencies in CC unrelated Caucasians are 0.87 for Cys and 0.13 for Ser. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M81778; AAA60317.1; -; mRNA. DR EMBL; X80763; CAB59978.1; -; Genomic_DNA. DR EMBL; U49516; AAB40898.1; -; mRNA. DR EMBL; AF208053; AAF35842.1; -; mRNA. DR EMBL; AF498983; AAM21130.1; -; mRNA. DR EMBL; AK295753; BAG58583.1; -; mRNA. DR EMBL; AC007022; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007025; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL591402; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL355812; CAI41334.1; -; Genomic_DNA. DR EMBL; AC004822; CAI41334.1; JOINED; Genomic_DNA. DR EMBL; AL590097; CAI41334.1; JOINED; Genomic_DNA. DR EMBL; AC004822; AAC71658.1; -; Genomic_DNA. DR EMBL; AL355812; CAI41335.1; -; Genomic_DNA. DR EMBL; AL590097; CAI41335.1; JOINED; Genomic_DNA. DR EMBL; AC004822; CAI41335.1; JOINED; Genomic_DNA. DR EMBL; AL590097; CAH70193.1; -; Genomic_DNA. DR EMBL; AC004822; CAH70193.1; JOINED; Genomic_DNA. DR EMBL; AL355812; CAH70193.1; JOINED; Genomic_DNA. DR EMBL; BC095543; AAH95543.1; -; mRNA. DR CCDS; CCDS14564.1; -. [P28335-1] DR CCDS; CCDS59174.1; -. [P28335-2] DR PIR; JS0616; JS0616. DR RefSeq; NP_000859.1; NM_000868.2. [P28335-1] DR RefSeq; NP_001243689.1; NM_001256760.1. [P28335-1] DR RefSeq; NP_001243690.1; NM_001256761.1. [P28335-2] DR UniGene; Hs.149037; -. DR ProteinModelPortal; P28335; -. DR SMR; P28335; 54-388. DR BioGrid; 109590; 7. DR IntAct; P28335; 1. DR MINT; MINT-443944; -. DR STRING; 9606.ENSP00000276198; -. DR BindingDB; P28335; -. DR ChEMBL; CHEMBL2111466; -. DR DrugBank; DB01239; Chlorprothixene. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB01191; Dexfenfluramine. DR DrugBank; DB00574; Fenfluramine. DR DrugBank; DB00247; Methysergide. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB00805; Minaprine. DR DrugBank; DB00370; Mirtazapine. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB00420; Promazine. DR DrugBank; DB00777; Propiomazine. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB06144; Sertindole. DR DrugBank; DB00372; Thiethylperazine. DR DrugBank; DB00193; Tramadol. DR DrugBank; DB00246; Ziprasidone. DR GuidetoPHARMACOLOGY; 8; -. DR PhosphoSite; P28335; -. DR DMDM; 112816; -. DR PaxDb; P28335; -. DR PRIDE; P28335; -. DR Ensembl; ENST00000276198; ENSP00000276198; ENSG00000147246. [P28335-1] DR Ensembl; ENST00000371950; ENSP00000361018; ENSG00000147246. [P28335-2] DR Ensembl; ENST00000371951; ENSP00000361019; ENSG00000147246. [P28335-1] DR GeneID; 3358; -. DR KEGG; hsa:3358; -. DR UCSC; uc004epu.1; human. [P28335-1] DR UCSC; uc004epv.1; human. DR CTD; 3358; -. DR GeneCards; GC0XP113818; -. DR HGNC; HGNC:5295; HTR2C. DR HPA; CAB006857; -. DR HPA; HPA003133; -. DR MIM; 312861; gene. DR neXtProt; NX_P28335; -. DR PharmGKB; PA194; -. DR eggNOG; NOG247243; -. DR HOGENOM; HOG000240378; -. DR HOVERGEN; HBG107487; -. DR InParanoid; P28335; -. DR KO; K04157; -. DR OMA; CCKRNTD; -. DR OrthoDB; EOG70ZZN5; -. DR PhylomeDB; P28335; -. DR TreeFam; TF316350; -. DR Reactome; REACT_111102; Signal Transduction. DR SignaLink; P28335; -. DR GeneWiki; 5-HT2C_receptor; -. DR GenomeRNAi; 3358; -. DR NextBio; 13278; -. DR PRO; PR:P28335; -. DR ArrayExpress; P28335; -. DR Bgee; P28335; -. DR CleanEx; HS_HTR2C; -. DR Genevestigator; P28335; -. DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0071886; F:1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding; IDA:UniProtKB. DR GO; GO:0008144; F:drug binding; IDA:UniProtKB. DR GO; GO:0001587; F:Gq/11-coupled serotonin receptor activity; IDA:UniProtKB. DR GO; GO:0051378; F:serotonin binding; IDA:UniProtKB. DR GO; GO:0004993; F:serotonin receptor activity; IDA:MGI. DR GO; GO:0001662; P:behavioral fear response; ISS:UniProtKB. DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB. DR GO; GO:0006182; P:cGMP biosynthetic process; IDA:UniProtKB. DR GO; GO:0007631; P:feeding behavior; ISS:UniProtKB. DR GO; GO:0007626; P:locomotory behavior; IEA:InterPro. DR GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway; ISS:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB. DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IDA:UniProtKB. DR GO; GO:0032098; P:regulation of appetite; ISS:UniProtKB. DR GO; GO:0043397; P:regulation of corticotropin-releasing hormone secretion; ISS:UniProtKB. DR GO; GO:0031644; P:regulation of neurological system process; ISS:UniProtKB. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB. DR GO; GO:0042493; P:response to drug; IDA:UniProtKB. DR GO; GO:0007210; P:serotonin receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR Gene3D; 1.20.1070.10; -; 2. DR InterPro; IPR000377; 5HT2C_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24247:SF32; PTHR24247:SF32; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00517; 5HT2CRECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; Behavior; Cell membrane; Complete proteome; KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane; KW Polymorphism; Receptor; Reference proteome; RNA editing; Signal; KW Transducer; Transmembrane; Transmembrane helix. FT SIGNAL 1 32 FT CHAIN 33 458 5-hydroxytryptamine receptor 2C. FT /FTId=PRO_0000068958. FT TOPO_DOM 33 52 Extracellular (By similarity). FT TRANSMEM 53 78 Helical; Name=1; (By similarity). FT TOPO_DOM 79 89 Cytoplasmic (By similarity). FT TRANSMEM 90 110 Helical; Name=2; (By similarity). FT TOPO_DOM 111 127 Extracellular (By similarity). FT TRANSMEM 128 150 Helical; Name=3; (By similarity). FT TOPO_DOM 151 170 Cytoplasmic (By similarity). FT TRANSMEM 171 193 Helical; Name=4; (By similarity). FT TOPO_DOM 194 213 Extracellular (By similarity). FT TRANSMEM 214 235 Helical; Name=5; (By similarity). FT TOPO_DOM 236 311 Cytoplasmic (By similarity). FT TRANSMEM 312 333 Helical; Name=6; (By similarity). FT TOPO_DOM 334 348 Extracellular (By similarity). FT TRANSMEM 349 371 Helical; Name=7; (By similarity). FT TOPO_DOM 372 458 Cytoplasmic (By similarity). FT REGION 134 139 Agonist binding (By similarity). FT REGION 324 328 Agonist binding (By similarity). FT MOTIF 151 153 DRY motif; important for ligand-induced FT conformation changes (By similarity). FT MOTIF 364 368 NPxxY motif; important for ligand-induced FT conformation changes and signaling (By FT similarity). FT MOTIF 456 458 PDZ-binding. FT CARBOHYD 39 39 N-linked (GlcNAc...) (Probable). FT DISULFID 127 207 By similarity. FT DISULFID 337 341 By similarity. FT VAR_SEQ 153 458 YVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIG FT LRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITY FT CLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEE FT NSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIV FT FFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIG FT YVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQI FT PRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVE FT NLELPVNPSSVVSERISSV -> CISSYPCDWTEGRRKGVR FT EQHDVRAQRPKFRSYWVLRSFLHTADDYGDYVLPDHLRSAP FT TSFDVTARPHRGTAWTKSGFPEVLQEEYGRGRELCKP (in FT isoform 2). FT /FTId=VSP_045171. FT VARIANT 23 23 C -> S (in dbSNP:rs6318). FT /FTId=VAR_003450. FT VARIANT 156 156 I -> V (in RNA edited version). FT /FTId=VAR_010166. FT VARIANT 158 158 N -> S (in RNA edited version). FT /FTId=VAR_010167. FT VARIANT 160 160 I -> V (in RNA edited version). FT /FTId=VAR_010168. FT MUTAGEN 159 159 P->A: Decreases interaction with ARRB2. FT MUTAGEN 456 456 S->A: Loss of interaction with MPDZ. FT MUTAGEN 456 456 S->T: No effect on interaction with MPDZ. FT MUTAGEN 457 457 S->A: No effect on interaction with MPDZ. FT MUTAGEN 458 458 V->A: Loss of interaction with MPDZ. SQ SEQUENCE 458 AA; 51821 MW; 9E76B3FFD3E09C93 CRC64; MVNLRNAVHS FLVHLIGLLV WQCDISVSPV AAIVTDIFNT SDGGRFKFPD GVQNWPALSI VIIIIMTIGG NILVIMAVSM EKKLHNATNY FLMSLAIADM LVGLLVMPLS LLAILYDYVW PLPRYLCPVW ISLDVLFSTA SIMHLCAISL DRYVAIRNPI EHSRFNSRTK AIMKIAIVWA ISIGVSVPIP VIGLRDEEKV FVNNTTCVLN DPNFVLIGSF VAFFIPLTIM VITYCLTIYV LRRQALMLLH GHTEEPPGLS LDFLKCCKRN TAEEENSANP NQDQNARRRK KKERRPRGTM QAINNERKAS KVLGIVFFVF LIMWCPFFIT NILSVLCEKS CNQKLMEKLL NVFVWIGYVC SGINPLVYTL FNKIYRRAFS NYLRCNYKVE KKPPVRQIPR VAATALSGRE LNVNIYRHTN EPVIEKASDN EPGIEMQVEN LELPVNPSSV VSERISSV // ID 5HT3A_HUMAN Reviewed; 478 AA. AC P46098; B4DSY6; G5E986; O60854; Q7KZM7; Q99918; Q9BSZ9; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JUL-2014, entry version 148. DE RecName: Full=5-hydroxytryptamine receptor 3A; DE Short=5-HT3-A; DE Short=5-HT3A; DE AltName: Full=5-hydroxytryptamine receptor 3; DE Short=5-HT-3; DE Short=5-HT3R; DE AltName: Full=Serotonin receptor 3A; DE AltName: Full=Serotonin-gated ion channel receptor; DE Flags: Precursor; GN Name=HTR3A; Synonyms=5HT3R, HTR3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Hippocampus; RX PubMed=7565620; RA Miyake A., Mochizuki S., Takemoto Y., Akuzawa S.; RT "Molecular cloning of human 5-hydroxytryptamine3 receptor: RT heterogeneity in distribution and function among species."; RL Mol. Pharmacol. 48:407-416(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Amygdala; RX PubMed=8848005; RA Belelli D., Balcarek J.M., Hope A.G., Peters J.A., Lambert J.J., RA Blackburn T.P.; RT "Cloning and functional expression of a human 5-hydroxytryptamine type RT 3AS receptor subunit."; RL Mol. Pharmacol. 48:1054-1062(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, and Hippocampus; RX PubMed=9928262; DOI=10.1111/j.1749-6632.1998.tb10196.x; RA Bruess M., Goethert M., Hayer M., Bonisch H.; RT "Molecular cloning of alternatively spliced human 5HT3 receptor RT cDNAs."; RL Ann. N. Y. Acad. Sci. 861:234-235(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Blood; RX PubMed=10670426; DOI=10.1016/S0028-3908(99)00116-1; RA Bruess M., Eucker T., Goethert M., Bonisch H.; RT "Exon-intron organization of the human 5-HT3A receptor gene."; RL Neuropharmacology 39:308-315(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction RT sequenced by the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RX PubMed=15028279; DOI=10.1016/j.ygeno.2003.09.023; RA Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., RA Au-Young J., Stuve L.L.; RT "PCR isolation and cloning of novel splice variant mRNAs from known RT drug target genes."; RL Genomics 83:566-571(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP FUNCTION, AND SUBUNIT. RX PubMed=9950429; DOI=10.1038/16941; RA Davies P.A., Pistis M., Hanna M.C., Peters J.A., Lambert J.J., RA Hales T.G., Kirkness E.F.; RT "The 5-HT3B subunit is a major determinant of serotonin-receptor RT function."; RL Nature 397:359-363(1999). RN [13] RP SUBUNIT, AND TISSUE SPECIFICITY. RC TISSUE=Small intestine; RX PubMed=10521471; DOI=10.1074/jbc.274.43.30799; RA Dubin A.E., Huvar R., D'Andrea M.R., Pyati J., Zhu J.Y., Joy K.C., RA Wilson S.J., Galindo J.E., Glass C.A., Luo L., Jackson M.R., RA Lovenberg T.W., Erlander M.G.; RT "The pharmacological and functional characteristics of the serotonin RT 5-HT(3A) receptor are specifically modified by a 5-HT(3B) receptor RT subunit."; RL J. Biol. Chem. 274:30799-30810(1999). RN [14] RP FUNCTION, REGION, AND MUTAGENESIS OF ARG-432; ARG-436 AND ARG-440. RX PubMed=12867984; DOI=10.1038/nature01788; RA Kelley S.P., Dunlop J.I., Kirkness E.F., Lambert J.J., Peters J.A.; RT "A cytoplasmic region determines single-channel conductance in 5-HT3 RT receptors."; RL Nature 424:321-324(2003). RN [15] RP INTERACTION WITH RIC3. RX PubMed=15809299; DOI=10.1074/jbc.M414341200; RA Cheng A., McDonald N.A., Connolly C.N.; RT "Cell surface expression of 5-hydroxytryptamine type 3 receptors is RT promoted by RIC-3."; RL J. Biol. Chem. 280:22502-22507(2005). RN [16] RP SUBUNIT, AND MUTAGENESIS OF TRP-178. RX PubMed=17392525; DOI=10.1124/mol.106.032144; RA Niesler B., Walstab J., Combrink S., Moeller D., Kapeller J., RA Rietdorf J., Boenisch H., Goethert M., Rappold G., Bruess M.; RT "Characterization of the novel human serotonin receptor subunits 5- RT HT3C, 5-HT3D, and 5-HT3E."; RL Mol. Pharmacol. 72:8-17(2007). RN [17] RP VARIANT THR-33. RX PubMed=15293096; DOI=10.1007/s10067-004-0927-2; RA Frank B., Niesler B., Bondy B., Spaeth M., Pongratz D.E., RA Ackenheil M., Fischer C., Rappold G.; RT "Mutational analysis of serotonin receptor genes: HTR3A and HTR3B in RT fibromyalgia patients."; RL Clin. Rheumatol. 23:338-344(2004). RN [18] RP VARIANTS HIS-344; ARG-391 AND GLN-409. RX PubMed=16487942; DOI=10.1016/j.biopsych.2005.11.008; RA Yamada K., Hattori E., Iwayama Y., Ohnishi T., Ohba H., Toyota T., RA Takao H., Minabe Y., Nakatani N., Higuchi T., Detera-Wadleigh S.D., RA Yoshikawa T.; RT "Distinguishable haplotype blocks in the HTR3A and HTR3B region in the RT Japanese reveal evidence of association of HTR3B with female major RT depression."; RL Biol. Psychiatry 60:192-201(2006). CC -!- FUNCTION: This is one of the several different receptors for 5- CC hydroxytryptamine (serotonin), a biogenic hormone that functions CC as a neurotransmitter, a hormone, and a mitogen. This receptor is CC a ligand-gated ion channel, which when activated causes fast, CC depolarizing responses in neurons. It is a cation-specific, but CC otherwise relatively nonselective, ion channel. CC -!- SUBUNIT: Forms pentahomomeric complex as well as pentaheteromeric CC complex with HTR3B or HTR3C or HTR3D or HTR3E; homomeric complex CC is functional but exhibits low conductance with modified voltage CC dependence, and decreased agonist and antagonist affinity. CC Interacts with RIC3. CC -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell CC membrane; Multi-pass membrane protein. Cell membrane; Multi-pass CC membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=5-HT3R-AS; CC IsoId=P46098-1; Sequence=Displayed; CC Name=2; Synonyms=5-HT3R-AL; CC IsoId=P46098-2; Sequence=VSP_000078; CC Name=3; CC IsoId=P46098-3; Sequence=VSP_042214; CC Name=4; CC IsoId=P46098-4; Sequence=VSP_043484; CC Note=No experimental confirmation available; CC Name=5; CC IsoId=P46098-5; Sequence=VSP_043484, VSP_000078; CC Note=No experimental confirmation available. Ref.7 (CD014118) CC sequence is in conflict in position: 342:C->W; CC -!- TISSUE SPECIFICITY: Expressed in cerebral cortex, amygdala, CC hippocampus, and testis. Detected in monocytes of the spleen and CC tonsil, in small and large intestine, uterus, prostate, ovary and CC placenta. CC -!- MISCELLANEOUS: The HA-stretch region of HTR3A seems to be CC responsible for the low conductance of HTR3A homomers compared to CC that of HTR3A/HTR3B heteromers. CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) CC family. 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3A CC sub-subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D49394; BAA08387.1; -; mRNA. DR EMBL; S82612; AAB37533.2; -; mRNA. DR EMBL; AJ003078; CAA05851.1; -; mRNA. DR EMBL; AJ003079; CAA05852.1; -; mRNA. DR EMBL; AJ005205; CAA06442.3; -; Genomic_DNA. DR EMBL; AF498984; AAM21131.1; -; mRNA. DR EMBL; BT007204; AAP35868.1; -; mRNA. DR EMBL; CD014118; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK299973; BAG61798.1; -; mRNA. DR EMBL; AP000908; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471065; EAW67238.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67240.1; -; Genomic_DNA. DR EMBL; BC002354; AAH02354.1; -; mRNA. DR EMBL; BC004453; AAH04453.2; -; mRNA. DR CCDS; CCDS53710.1; -. [P46098-3] DR CCDS; CCDS8365.2; -. [P46098-4] DR CCDS; CCDS8366.2; -. [P46098-5] DR RefSeq; NP_000860.2; NM_000869.5. [P46098-4] DR RefSeq; NP_001155244.1; NM_001161772.2. [P46098-3] DR RefSeq; NP_998786.2; NM_213621.3. [P46098-5] DR UniGene; Hs.413899; -. DR ProteinModelPortal; P46098; -. DR SMR; P46098; 37-316. DR STRING; 9606.ENSP00000347754; -. DR BindingDB; P46098; -. DR ChEMBL; CHEMBL2094132; -. DR DrugBank; DB00969; Alosetron. DR DrugBank; DB01161; Chloroprocaine. DR DrugBank; DB00604; Cisapride. DR DrugBank; DB00757; Dolasetron. DR DrugBank; DB00889; Granisetron. DR DrugBank; DB00370; Mirtazapine. DR DrugBank; DB00904; Ondansetron. DR DrugBank; DB00377; Palonosetron. DR DrugBank; DB00721; Procaine. DR DrugBank; DB01199; Tubocurarine. DR GuidetoPHARMACOLOGY; 373; -. DR TCDB; 1.A.9.2.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family. DR PhosphoSite; P46098; -. DR DMDM; 1168222; -. DR PaxDb; P46098; -. DR PRIDE; P46098; -. DR DNASU; 3359; -. DR Ensembl; ENST00000299961; ENSP00000299961; ENSG00000166736. [P46098-3] DR Ensembl; ENST00000355556; ENSP00000347754; ENSG00000166736. [P46098-5] DR Ensembl; ENST00000375498; ENSP00000364648; ENSG00000166736. [P46098-4] DR Ensembl; ENST00000504030; ENSP00000424189; ENSG00000166736. [P46098-1] DR Ensembl; ENST00000506841; ENSP00000424776; ENSG00000166736. [P46098-2] DR GeneID; 3359; -. DR KEGG; hsa:3359; -. DR UCSC; uc010rxa.2; human. [P46098-4] DR UCSC; uc010rxb.2; human. DR UCSC; uc010rxc.2; human. [P46098-3] DR CTD; 3359; -. DR GeneCards; GC11P113879; -. DR HGNC; HGNC:5297; HTR3A. DR MIM; 182139; gene. DR neXtProt; NX_P46098; -. DR PharmGKB; PA29555; -. DR eggNOG; NOG302526; -. DR HOGENOM; HOG000241519; -. DR HOVERGEN; HBG106638; -. DR KO; K04819; -. DR OMA; FIVRLVH; -. DR OrthoDB; EOG7KDF9H; -. DR PhylomeDB; P46098; -. DR TreeFam; TF315605; -. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR GeneWiki; HTR3A; -. DR GenomeRNAi; 3359; -. DR NextBio; 13282; -. DR PRO; PR:P46098; -. DR ArrayExpress; P46098; -. DR Bgee; P46098; -. DR CleanEx; HS_HTR3A; -. DR Genevestigator; P46098; -. DR GO; GO:0030424; C:axon; IEA:Ensembl. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004872; F:receptor activity; TAS:ProtInc. DR GO; GO:0051378; F:serotonin binding; IDA:MGI. DR GO; GO:0004993; F:serotonin receptor activity; IDA:MGI. DR GO; GO:0005232; F:serotonin-activated cation-selective channel activity; TAS:ProtInc. DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:Ensembl. DR GO; GO:0006812; P:cation transport; TAS:GOC. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl. DR GO; GO:0007586; P:digestion; TAS:ProtInc. DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome. DR GO; GO:0042220; P:response to cocaine; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0007210; P:serotonin receptor signaling pathway; IDA:GOC. DR GO; GO:0007268; P:synaptic transmission; TAS:ProtInc. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0006810; P:transport; TAS:ProtInc. DR Gene3D; 1.20.120.370; -; 2. DR Gene3D; 2.70.170.10; -; 1. DR InterPro; IPR008132; 5HT3_rcpt. DR InterPro; IPR008133; 5HT3_rcpt_A. DR InterPro; IPR027361; Acetylcholine_rcpt_TM. DR InterPro; IPR006202; Neur_chan_lig-bd. DR InterPro; IPR006201; Neur_channel. DR InterPro; IPR006029; Neurotrans-gated_channel_TM. DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS. DR PANTHER; PTHR18945; PTHR18945; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR01709; 5HT3ARECEPTR. DR PRINTS; PR01708; 5HT3RECEPTOR. DR PRINTS; PR00252; NRIONCHANNEL. DR SUPFAM; SSF63712; SSF63712; 1. DR SUPFAM; SSF90112; SSF90112; 1. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell membrane; Complete proteome; KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; KW Ligand-gated ion channel; Membrane; Polymorphism; KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; KW Synapse; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1 23 Potential. FT CHAIN 24 478 5-hydroxytryptamine receptor 3A. FT /FTId=PRO_0000000408. FT TOPO_DOM 24 241 Extracellular (Potential). FT TRANSMEM 242 268 Helical; Name=1; (Potential). FT TOPO_DOM 269 273 Cytoplasmic (Potential). FT TRANSMEM 274 292 Helical; Name=2; (Potential). FT TOPO_DOM 293 302 Extracellular (Potential). FT TRANSMEM 303 321 Helical; Name=3; (Potential). FT TOPO_DOM 322 455 Cytoplasmic (Potential). FT TRANSMEM 456 475 Helical; Name=4; (Potential). FT TOPO_DOM 476 478 Extracellular (Potential). FT REGION 414 450 HA-stretch. FT CARBOHYD 28 28 N-linked (GlcNAc...) (Potential). FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT CARBOHYD 170 170 N-linked (GlcNAc...) (Potential). FT CARBOHYD 186 186 N-linked (GlcNAc...) (Potential). FT DISULFID 157 171 By similarity. FT VAR_SEQ 1 22 MLLWVQQALLALLLPTLLAQGE -> MHRSFLQ (in FT isoform 3). FT /FTId=VSP_042214. FT VAR_SEQ 1 1 M -> MLGKLAM (in isoform 4 and isoform FT 5). FT /FTId=VSP_043484. FT VAR_SEQ 306 306 G -> GKAPPGSRAQSGEKPAPSHLLHVSLASALGCTG FT (in isoform 2 and isoform 5). FT /FTId=VSP_000078. FT VARIANT 33 33 A -> T (in dbSNP:rs117793058). FT /FTId=VAR_037398. FT VARIANT 253 253 S -> N (in dbSNP:rs4938063). FT /FTId=VAR_037399. FT VARIANT 344 344 R -> H (in dbSNP:rs35815285). FT /FTId=VAR_037400. FT VARIANT 391 391 P -> R. FT /FTId=VAR_037401. FT VARIANT 409 409 R -> Q. FT /FTId=VAR_037402. FT MUTAGEN 178 178 W->S: Abolished ligand binding to the FT heteromeric receptor. FT MUTAGEN 432 432 R->Q: Little effect on conductance. FT Massive increase of conductance; when FT associated with D-436 and A-440. FT MUTAGEN 436 436 R->D: Increased conductance. Massive FT increase of conductance; when associated FT with Q-432 and A-440. FT MUTAGEN 440 440 R->A: Increased conductance. Massive FT increase of conductance; when associated FT with Q-432 and D-436. FT CONFLICT 46 46 R -> T (in Ref. 2; AAB37533). FT CONFLICT 125 125 F -> L (in Ref. 2; AAB37533). FT CONFLICT 321 321 A -> T (in Ref. 2; AAB37533). FT CONFLICT 386 386 S -> T (in Ref. 2; AAB37533). SQ SEQUENCE 478 AA; 55280 MW; 24CA9A232286FBC9 CRC64; MLLWVQQALL ALLLPTLLAQ GEARRSRNTT RPALLRLSDY LLTNYRKGVR PVRDWRKPTT VSIDVIVYAI LNVDEKNQVL TTYIWYRQYW TDEFLQWNPE DFDNITKLSI PTDSIWVPDI LINEFVDVGK SPNIPYVYIR HQGEVQNYKP LQVVTACSLD IYNFPFDVQN CSLTFTSWLH TIQDINISLW RLPEKVKSDR SVFMNQGEWE LLGVLPYFRE FSMESSNYYA EMKFYVVIRR RPLFYVVSLL LPSIFLMVMD IVGFYLPPNS GERVSFKITL LLGYSVFLII VSDTLPATAI GTPLIGVYFV VCMALLVISL AETIFIVRLV HKQDLQQPVP AWLRHLVLER IAWLLCLREQ STSQRPPATS QATKTDDCSA MGNHCSHMGG PQDFEKSPRD RCSPPPPPRE ASLAVCGLLQ ELSSIRQFLE KRDEIREVAR DWLRVGSVLD KLLFHIYLLA VLAYSITLVM LWSIWQYA // ID 5NT3A_HUMAN Reviewed; 336 AA. AC Q9H0P0; A8K253; B2RAA5; B8ZZC4; Q6IPZ1; Q6NXS6; Q7L3G6; Q9P0P5; AC Q9UC42; Q9UC43; Q9UC44; Q9UC45; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 3. DT 09-JUL-2014, entry version 123. DE RecName: Full=Cytosolic 5'-nucleotidase 3A; DE EC=3.1.3.5; DE AltName: Full=Cytosolic 5'-nucleotidase 3; DE AltName: Full=Cytosolic 5'-nucleotidase III; DE Short=cN-III; DE AltName: Full=Pyrimidine 5'-nucleotidase 1; DE Short=P5'N-1; DE Short=P5N-1; DE Short=PN-I; DE AltName: Full=Uridine 5'-monophosphate hydrolase 1; DE AltName: Full=p36; GN Name=NT5C3A; Synonyms=NT5C3, P5N1, UMPH1; ORFNames=HSPC233; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Placenta; RX PubMed=10942414; RA Amici A., Emanuelli M., Raffaelli N., Ruggieri S., Saccucci F., RA Magni G.; RT "Human erythrocyte pyrimidine 5'-nucleotidase, PN-I, is identical to RT p36, a protein associated to lupus inclusion formation in response to RT alpha-interferon."; RL Blood 96:1596-1598(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND RP VARIANT P5N DEFICIENCY VAL-137. RX PubMed=11369620; DOI=10.1182/blood.V97.11.3327; RA Marinaki A.M., Escuredo E., Duley J.A., Simmonds H.A., Amici A., RA Naponelli V., Magni G., Seip M., Ben-Bassat I., Harley E.H., RA Thein S.L., Rees D.C.; RT "Genetic basis of hemolytic anemia caused by pyrimidine 5' RT nucleotidase deficiency."; RL Blood 97:3327-3332(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, VARIANTS RP P5N DEFICIENCY PRO-181 AND ARG-280, AND CHARACTERIZATION OF VARIANTS RP P5N DEFICIENCY PRO-181 AND ARG-280. RX PubMed=15238149; DOI=10.1111/j.1365-2141.2004.05029.x; RA Kanno H., Takizawa T., Miwa S., Fujii H.; RT "Molecular basis of Japanese variants of pyrimidine 5'-nucleotidase RT deficiency."; RL Br. J. Haematol. 126:265-271(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Kidney; RX PubMed=11230166; DOI=10.1101/gr.GR1547R; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D., RA Wambutt R., Korn B., Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and RT analysis of 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Brain cortex, and Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, Lung, Muscle, and Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-336 (ISOFORM 2). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [11] RP PROTEIN SEQUENCE OF 83-95; 131-147; 226-240; 268-296 AND 311-329, RP INDUCTION, AND SUBCELLULAR LOCATION. RX PubMed=8557639; DOI=10.1074/jbc.271.20.11595; RA Rich S.A., Bose M., Tempst P., Rudofsky U.H.; RT "Purification, microsequencing, and immunolocalization of p36, a new RT interferon-alpha-induced protein that is associated with human lupus RT inclusions."; RL J. Biol. Chem. 271:1118-1126(1996). RN [12] RP PROTEIN SEQUENCE OF 1-11, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, RP CHARACTERIZATION OF VARIANTS P5N DEFICIENCY VAL-137; PRO-181; SER-229 RP AND ARG-280, AND MUTAGENESIS OF ASP-88; PHE-89; ASP-90; GLU-135 AND RP PHE-233. RX PubMed=15968458; DOI=10.1007/s00018-005-5135-y; RA Amici A., Ciccioli K., Naponelli V., Raffaelli N., Magni G.; RT "Evidence for essential catalytic determinants for human erythrocyte RT pyrimidine 5'-nucleotidase."; RL Cell. Mol. Life Sci. 62:1613-1620(2005). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 64-336 IN COMPLEX WITH RP PHOSPHATE AND MAGNESIUM IONS. RX PubMed=17405878; DOI=10.1074/jbc.M700917200; RA Wallden K., Stenmark P., Nyman T., Flodin S., Graeslund S., RA Loppnau P., Bianchi V., Nordlund P.; RT "Crystal structure of human cytosolic 5'-nucleotidase II: insights RT into allosteric regulation and substrate recognition."; RL J. Biol. Chem. 282:17828-17836(2007). RN [16] RP VARIANT P5N DEFICIENCY SER-229. RX PubMed=12930399; DOI=10.1046/j.1365-2141.2003.04532.x; RA Bianchi P., Fermo E., Alfinito F., Vercellati C., Baserga M., RA Ferraro F., Guzzo I., Rotoli B., Zanella A.; RT "Molecular characterization of six unrelated Italian patients affected RT by pyrimidine 5'-nucleotidase deficiency."; RL Br. J. Haematol. 122:847-851(2003). CC -!- FUNCTION: Can act both as nucleotidase and as phosphotransferase. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=66 uM for CMP; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). CC -!- SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=2; CC IsoId=Q9H0P0-4; Sequence=Displayed; CC Name=1; CC IsoId=Q9H0P0-1; Sequence=VSP_021565; CC Name=3; CC IsoId=Q9H0P0-2; Sequence=VSP_015623; CC Name=4; Synonyms=P5N-R; CC IsoId=Q9H0P0-3; Sequence=VSP_015624; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in CC reticulocytes and lymphocytes. Isoform 4 is expressed only in CC reticulocytes. CC -!- INDUCTION: Isoform 2 is induced by interferon alpha in Raji cells CC in association with lupus inclusions. CC -!- DISEASE: P5N deficiency (P5ND) [MIM:266120]: Autosomal recessive CC condition causing hemolytic anemia characterized by marked CC basophilic stippling and the accumulation of high concentrations CC of pyrimidine nucleotides within the erythrocyte. It is implicated CC in the anemia of lead poisoning and is possibly associated with CC learning difficulties. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the pyrimidine 5'-nucleotidase family. CC -!- SEQUENCE CAUTION: CC Sequence=AAF36153.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAG33630.1; Type=Frameshift; Positions=Several; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF312735; AAG33630.1; ALT_SEQ; mRNA. DR EMBL; AL136716; CAB66650.1; -; mRNA. DR EMBL; AK290118; BAF82807.1; -; mRNA. DR EMBL; AK314109; BAG36802.1; -; mRNA. DR EMBL; CR533518; CAG38549.1; -; mRNA. DR EMBL; AC074338; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC083863; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471073; EAW94007.1; -; Genomic_DNA. DR EMBL; CH471073; EAW94008.1; -; Genomic_DNA. DR EMBL; BC013292; AAH13292.2; -; mRNA. DR EMBL; BC015856; AAH15856.2; -; mRNA. DR EMBL; BC066914; AAH66914.1; -; mRNA. DR EMBL; BC071652; AAH71652.2; -; mRNA. DR EMBL; AF151067; AAF36153.1; ALT_INIT; mRNA. DR CCDS; CCDS34616.1; -. [Q9H0P0-4] DR CCDS; CCDS34617.1; -. [Q9H0P0-1] DR CCDS; CCDS55101.1; -. [Q9H0P0-3] DR RefSeq; NP_001002009.1; NM_001002009.2. [Q9H0P0-1] DR RefSeq; NP_001002010.1; NM_001002010.2. [Q9H0P0-4] DR RefSeq; NP_001159590.1; NM_001166118.2. [Q9H0P0-3] DR RefSeq; NP_057573.2; NM_016489.12. [Q9H0P0-1] DR UniGene; Hs.487933; -. DR PDB; 2CN1; X-ray; 2.67 A; A=64-336. DR PDB; 2JGA; X-ray; 3.01 A; A=64-336. DR PDB; 2VKQ; X-ray; 2.50 A; A=64-336. DR PDBsum; 2CN1; -. DR PDBsum; 2JGA; -. DR PDBsum; 2VKQ; -. DR ProteinModelPortal; Q9H0P0; -. DR SMR; Q9H0P0; 64-336. DR BioGrid; 119408; 6. DR IntAct; Q9H0P0; 3. DR MINT; MINT-3065844; -. DR PhosphoSite; Q9H0P0; -. DR DMDM; 117949804; -. DR MaxQB; Q9H0P0; -. DR PaxDb; Q9H0P0; -. DR PRIDE; Q9H0P0; -. DR DNASU; 51251; -. DR Ensembl; ENST00000242210; ENSP00000242210; ENSG00000122643. [Q9H0P0-4] DR Ensembl; ENST00000381626; ENSP00000371039; ENSG00000122643. [Q9H0P0-3] DR Ensembl; ENST00000396152; ENSP00000379456; ENSG00000122643. [Q9H0P0-1] DR Ensembl; ENST00000405342; ENSP00000385261; ENSG00000122643. [Q9H0P0-1] DR Ensembl; ENST00000409467; ENSP00000387166; ENSG00000122643. [Q9H0P0-3] DR GeneID; 51251; -. DR KEGG; hsa:51251; -. DR UCSC; uc003tdi.4; human. [Q9H0P0-1] DR UCSC; uc003tdk.4; human. [Q9H0P0-4] DR CTD; 51251; -. DR GeneCards; GC07M033056; -. DR HGNC; HGNC:17820; NT5C3A. DR HPA; HPA029058; -. DR MIM; 266120; phenotype. DR MIM; 606224; gene. DR neXtProt; NX_Q9H0P0; -. DR Orphanet; 35120; Hemolytic anemia due to pyrimidine 5' nucleotidase deficiency. DR PharmGKB; PA31802; -. DR eggNOG; NOG266578; -. DR HOVERGEN; HBG059750; -. DR InParanoid; Q9H0P0; -. DR KO; K01081; -. DR OMA; NTEYFKQ; -. DR PhylomeDB; Q9H0P0; -. DR TreeFam; TF314663; -. DR Reactome; REACT_111217; Metabolism. DR SABIO-RK; Q9H0P0; -. DR EvolutionaryTrace; Q9H0P0; -. DR GeneWiki; NT5C3; -. DR GenomeRNAi; 51251; -. DR NextBio; 54391; -. DR PRO; PR:Q9H0P0; -. DR Bgee; Q9H0P0; -. DR Genevestigator; Q9H0P0; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0008665; F:2'-phosphotransferase activity; NAS:UniProtKB. DR GO; GO:0008253; F:5'-nucleotidase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; NAS:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0046085; P:adenosine metabolic process; IEA:Ensembl. DR GO; GO:0016311; P:dephosphorylation; IDA:GOC. DR GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; TAS:Reactome. DR GO; GO:0046135; P:pyrimidine nucleoside catabolic process; TAS:Reactome. DR GO; GO:0006213; P:pyrimidine nucleoside metabolic process; NAS:UniProtKB. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006434; Pyrimidine_nucleotidase_eu. DR PANTHER; PTHR13045; PTHR13045; 1. DR Pfam; PF05822; UMPH-1; 1. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01544; HAD-SF-IE; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; Disease mutation; Endoplasmic reticulum; KW Hydrolase; Magnesium; Metal-binding; Nucleotide metabolism; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 336 Cytosolic 5'-nucleotidase 3A. FT /FTId=PRO_0000064387. FT REGION 203 204 Substrate binding. FT ACT_SITE 88 88 Nucleophile. FT ACT_SITE 90 90 Proton donor. FT METAL 88 88 Magnesium. FT METAL 90 90 Magnesium; via carbonyl oxygen. FT METAL 277 277 Magnesium. FT BINDING 252 252 Substrate. FT VAR_SEQ 1 51 Missing (in isoform 4). FT /FTId=VSP_015624. FT VAR_SEQ 1 50 MRAPSMDRAAVARVGAVASASVCALVAGVVLAQYIFTLKRK FT TGRKTKIIE -> MTNQESAVHVK (in isoform 1). FT /FTId=VSP_021565. FT VAR_SEQ 1 50 Missing (in isoform 3). FT /FTId=VSP_015623. FT VARIANT 137 137 D -> V (in P5N deficiency; may alter FT protein structure). FT /FTId=VAR_023511. FT VARIANT 181 181 L -> P (in P5N deficiency; may alter FT protein structure and markedly decreases FT activity). FT /FTId=VAR_023512. FT VARIANT 229 229 N -> S (in P5N deficiency; markedly FT decreases activity). FT /FTId=VAR_023513. FT VARIANT 280 280 G -> R (in P5N deficiency; markedly FT decreases activity). FT /FTId=VAR_023514. FT MUTAGEN 88 88 D->N: Loss of nucleotidase and FT phosphotransferase activity. FT MUTAGEN 89 89 F->A: Increases Km for CMP 45-fold. FT Reduces nucleotidase and FT phosphotransferase activity by 99%. FT MUTAGEN 90 90 D->N: Loss of nucleotidase and FT phosphotransferase activity. FT MUTAGEN 135 135 E->D: No effect on nucleotidase activity. FT Reduces phosphotransferase activity by FT 99%. FT MUTAGEN 233 233 F->A: Reduces nucleotidase and FT phosphotransferase activity by 97%. FT CONFLICT 95 95 R -> K (in Ref. 11; AA sequence). FT CONFLICT 144 144 E -> Q (in Ref. 11; AA sequence). FT CONFLICT 329 329 N -> R (in Ref. 11; AA sequence). FT HELIX 65 78 FT HELIX 80 82 FT STRAND 83 87 FT TURN 90 92 FT STRAND 96 98 FT HELIX 106 111 FT HELIX 118 135 FT STRAND 138 140 FT HELIX 142 163 FT HELIX 167 169 FT HELIX 170 175 FT HELIX 185 194 FT STRAND 199 206 FT HELIX 207 216 FT STRAND 224 229 FT STRAND 231 233 FT STRAND 237 242 FT HELIX 252 258 FT HELIX 260 264 FT TURN 265 268 FT STRAND 271 279 FT HELIX 280 283 FT TURN 284 287 FT STRAND 292 300 FT HELIX 304 312 FT STRAND 315 320 FT HELIX 326 335 SQ SEQUENCE 336 AA; 37948 MW; C5D75CCF1BB61021 CRC64; MRAPSMDRAA VARVGAVASA SVCALVAGVV LAQYIFTLKR KTGRKTKIIE MMPEFQKSSV RIKNPTRVEE IICGLIKGGA AKLQIITDFD MTLSRFSYKG KRCPTCHNII DNCKLVTDEC RKKLLQLKEK YYAIEVDPVL TVEEKYPYMV EWYTKSHGLL VQQALPKAKL KEIVAESDVM LKEGYENFFD KLQQHSIPVF IFSAGIGDVL EEVIRQAGVY HPNVKVVSNF MDFDETGVLK GFKGELIHVF NKHDGALRNT EYFNQLKDNS NIILLGDSQG DLRMADGVAN VEHILKIGYL NDRVDELLEK YMDSYDIVLV QDESLEVANS ILQKIL // ID 8ODP_HUMAN Reviewed; 197 AA. AC P36639; A4D205; Q6LES7; Q6P0Y6; Q7Z7N6; Q8IV95; Q9UBM0; Q9UBM9; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 3. DT 09-JUL-2014, entry version 139. DE RecName: Full=7,8-dihydro-8-oxoguanine triphosphatase; DE EC=3.6.1.55; DE AltName: Full=2-hydroxy-dATP diphosphatase; DE EC=3.6.1.56; DE AltName: Full=8-oxo-dGTPase; DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 1; DE Short=Nudix motif 1; DE Flags: Precursor; GN Name=NUDT1; Synonyms=MTH1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), PARTIAL PROTEIN SEQUENCE, RP AND CATALYTIC ACTIVITY. RX PubMed=8226881; RA Sakumi K., Furuichi M., Tsuzuki T., Kakuma T., Kawabata S., Maki H., RA Sekiguchi M.; RT "Cloning and expression of cDNA for a human enzyme that hydrolyzes 8- RT oxo-dGTP, a mutagenic substrate for DNA synthesis."; RL J. Biol. Chem. 268:23524-23530(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7713500; DOI=10.1006/geno.1994.1657; RA Furuichi M., Yoshida M.C., Oda H., Tajiri T., Nakabeppu Y., RA Tsuzuki T., Sekiguchi M.; RT "Genomic structure and chromosome location of the human mutT homologue RT gene MTH1 encoding 8-oxo-dGTPase for prevention of A:T to C:G RT transversion."; RL Genomics 24:485-490(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P18), TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND VARIANT MET-124. RX PubMed=9211940; DOI=10.1074/jbc.272.28.17843; RA Oda H., Nakabeppu Y., Furuichi M., Sekiguchi M.; RT "Regulation of expression of the human MTH1 gene encoding 8-oxo- RT dGTPase. Alternative splicing of transcription products."; RL J. Biol. Chem. 272:17843-17850(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P18/P21/P22/P26), AND ALTERNATIVE RP INITIATION. RX PubMed=10536140; DOI=10.1093/nar/27.22.4335; RA Oda H., Taketomi A., Maruyama R., Itoh R., Nishioka K., Yakushiji H., RA Suzuki T., Sekiguchi M., Nakabeppu Y.; RT "Multi-forms of human MTH1 polypeptides produced by alternative RT translation initiation and single nucleotide polymorphism."; RL Nucleic Acids Res. 27:4335-4343(1999). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P18). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS P18 AND P22), AND RP VARIANT MET-124. RC TISSUE=Bone, Lymph, Mammary gland, and Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP SUBCELLULAR LOCATION. RX PubMed=7782328; DOI=10.1074/jbc.270.24.14659; RA Kang D., Nishida J., Iyama A., Nakabeppu Y., Furuichi M., Fujiwara T., RA Sekiguchi M., Takeshige K.; RT "Intracellular localization of 8-oxo-dGTPase in human cells, with RT special reference to the role of the enzyme in mitochondria."; RL J. Biol. Chem. 270:14659-14665(1995). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10373420; DOI=10.1074/jbc.274.26.18201; RA Fujikawa K., Kamiya H., Yakushiji H., Fujii Y., Nakabeppu Y., RA Kasai H.; RT "The oxidized forms of dATP are substrates for the human MutT RT homologue, the hMTH1 protein."; RL J. Biol. Chem. 274:18201-18205(1999). RN [13] RP MUTAGENESIS OF GLY-77; GLY-78; VAL-80; GLN-81; GLY-83; ILE-86; ASP-88; RP GLY-89; ALA-90; LEU-94; GLN-95; GLU-96; GLU-97 AND SER-98, FUNCTION, RP AND CATALYTIC ACTIVITY. RX PubMed=10608900; DOI=10.1074/jbc.274.53.38251; RA Fujii Y., Shimokawa H., Sekiguchi M., Nakabeppu Y.; RT "Functional significance of the conserved residues for the 23-residue RT module among MTH1 and MutT family proteins."; RL J. Biol. Chem. 274:38251-38259(1999). RN [14] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=11139615; DOI=10.1093/nar/29.2.449; RA Fujikawa K., Kamiya H., Yakushiji H., Nakabeppu Y., Kasai H.; RT "Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy- RT ATP."; RL Nucleic Acids Res. 29:449-454(2001). RN [15] RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-68; TRP-158; ASP-160; RP LEU-191; ARG-192; GLU-193; VAL-194; ASP-195; THR-196; VAL-197; RP 192-ARG--VAL-197; 193-GLU--VAL-197; 194-VAL-VAL-197 AND RP 195-ASP--VAL-197. RX PubMed=11756418; DOI=10.1074/jbc.M110566200; RA Sakai Y., Furuichi M., Takahashi M., Mishima M., Iwai S., RA Shirakawa M., Nakabeppu Y.; RT "A molecular basis for the selective recognition of 2-hydroxy-dATP and RT 8-oxo-dGTP by human MTH1."; RL J. Biol. Chem. 277:8579-8587(2002). RN [16] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12857738; DOI=10.1074/jbc.M306201200; RA Yoshimura D., Sakumi K., Ohno M., Sakai Y., Furuichi M., Iwai S., RA Nakabeppu Y.; RT "An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell RT death caused by oxidative stress."; RL J. Biol. Chem. 278:37965-37973(2003). RN [17] RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=16607562; DOI=10.1007/s00109-006-0053-5; RA Sakai Y., Oda H., Yoshimura D., Furuichi M., Kang D., Iwai S., RA Hara T., Nakabeppu Y.; RT "The GT to GC single nucleotide polymorphism at the beginning of an RT alternative exon 2C of human MTH1 gene confers an amino terminal RT extension that functions as a mitochondrial targeting signal."; RL J. Mol. Med. 84:660-670(2006). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22556419; DOI=10.1074/jbc.M112.363010; RA Takagi Y., Setoyama D., Ito R., Kamiya H., Yamagata Y., Sekiguchi M.; RT "Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine RT and deoxyguanosine diphosphates: comparison with MTH1 and MTH2."; RL J. Biol. Chem. 287:21541-21549(2012). RN [20] RP STRUCTURE BY NMR OF 42-197, SUBUNIT, COFACTOR, AND SUBSTRATE BINDING RP SITE. RX PubMed=15133035; DOI=10.1074/jbc.M402393200; RA Mishima M., Sakai Y., Itoh N., Kamiya H., Furuichi M., Takahashi M., RA Yamagata Y., Iwai S., Nakabeppu Y., Shirakawa M.; RT "Structure of human MTH1, a Nudix family hydrolase that selectively RT degrades oxidized purine nucleoside triphosphates."; RL J. Biol. Chem. 279:33806-33815(2004). RN [21] RP CRYSTALLIZATION, AND PRELIMINARY X-RAY CRYSTALLOGRAPHY (1.95 RP ANGSTROMS). RX PubMed=17142918; DOI=10.1107/S1744309106049529; RA Nakamura T., Kitaguchi Y., Miyazawa M., Kamiya H., Toma S., RA Ikemizu S., Shirakawa M., Nakabeppu Y., Yamagata Y.; RT "Crystallization and preliminary X-ray analysis of human MTH1 RT complexed with two oxidized nucleotides, 8-oxo-dGMP and 2-oxo-dATP."; RL Acta Crystallogr. F 62:1283-1285(2006). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197 IN COMPLEX WITH RP 8-OXO-DGMP, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=21787772; DOI=10.1016/j.febslet.2011.07.017; RA Svensson L.M., Jemth A.S., Desroses M., Loseva O., Helleday T., RA Hogbom M., Stenmark P.; RT "Crystal structure of human MTH1 and the 8-oxo-dGMP product complex."; RL FEBS Lett. 585:2617-2621(2011). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 42-197. RG Structural genomics consortium (SGC); RA Tresaugues L., Siponen M.I., Arrowsmith C.H., Berglund H., Bountra C., RA Collins R., Edwards A.M., Ekblad T., Flodin S., Flores A., RA Graslund S., Hammarstrom M., Johansson I., Karlberg T., Kol S., RA Kotenyova T., Kouznetsova E., Moche M., Nyman T., Persson C., RA Schuler H., Schutz P., Thorsell A.G., Van Der Berg S., Wahlberg E., RA Weigelt J., Welin M., Nordlund P.; RT "Crystal Structure of Human 8-oxo-dGTPase (MTH1)."; RL Submitted (JAN-2011) to the PDB data bank. RN [24] RP VARIANT MET-124. RX PubMed=15516784; DOI=10.1507/endocrj.51.493; RA Miyako K., Kohno H., Ihara K., Kuromaru R., Matsuura N., Hara T.; RT "Association study of human MTH1 gene polymorphisms with type 1 RT diabetes mellitus."; RL Endocr. J. 51:493-498(2004). RN [25] RP VARIANT MET-124. RX PubMed=16774934; DOI=10.1093/carcin/bgl095; RA Kohno T., Sakiyama T., Kunitoh H., Goto K., Nishiwaki Y., Saito D., RA Hirose H., Eguchi T., Yanagitani N., Saito R., Sasaki-Matsumura R., RA Mimaki S., Toyama K., Yamamoto S., Kuchiba A., Sobue T., Ohta T., RA Ohki M., Yokota J.; RT "Association of polymorphisms in the MTH1 gene with small cell lung RT carcinoma risk."; RL Carcinogenesis 27:2448-2454(2006). CC -!- FUNCTION: Antimutagenic. Acts as a sanitizing enzyme for oxidized CC nucleotide pools, thus suppressing cell dysfunction and death CC induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and CC 2-OH-dATP, thus preventing misincorporation of oxidized purine CC nucleoside triphosphates into DNA and subsequently preventing A:T CC to C:G and G:C to T:A transversions. Able to hydrolyze also the CC corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP. CC Does not play a role in U8 snoRNA decapping activity. Binds U8 CC snoRNA. CC -!- CATALYTIC ACTIVITY: 8-oxo-dGTP + H(2)O = 8-oxo-dGMP + diphosphate. CC -!- CATALYTIC ACTIVITY: 2-hydroxy-dATP + H(2)O = 2-hydroxy-dAMP + CC diphosphate. CC -!- COFACTOR: Binds 1 magnesium ion per subunit (Probable). CC -!- ENZYME REGULATION: 2-hydroxy-dATPase activity is inhibited by 2- CC OH-dADP, 8-OH-dGDP and 8-OH-dGTP. 8-OH-dGTPase activity is CC inhibited by 8-OH-dGDP, 2-OH-dADP and 2-OH-dATP. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=8.3 uM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 8.0, CC PubMed:11139615); CC KM=5.7 uM for 2-hydroxy-dATP (at 30 degrees Celsius and pH 7.2, CC PubMed:11139615); CC KM=4.3 uM for 2-hydroxy-rATP (at 30 degrees Celsius and pH 8.0, CC PubMed:11139615); CC KM=13.9 uM for 8-hydroxy-dATP (at 30 degrees Celsius and pH 8.0, CC PubMed:11139615); CC KM=51.0 uM for 8-hydroxy-rATP (at 30 degrees Celsius and pH 8.0, CC PubMed:11139615); CC KM=15.2 uM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 8.0, CC PubMed:11139615); CC KM=12.8 uM for 8-hydroxy-dGTP (at 30 degrees Celsius and pH 7.2, CC PubMed:11139615); CC KM=13.2 uM for 8-hydroxy-dGTP (at 22 degrees Celsius and pH 7.5, CC PubMed:21787772); CC KM=55.0 uM for 8-hydroxy-rGTP (at 30 degrees Celsius and pH 8.0, CC PubMed:11139615); CC KM=258 uM for dGTP (at 30 degrees Celsius and pH 8.0, CC PubMed:11139615); CC Note=The kinetic constants are determined for the recombinant CC enzyme expressed in E.coli. 2-hydroxy-rATP shows the best CC catalytic efficiency; CC pH dependence: CC Optimum pH is 7.8-8.2 with 8-hydroxy-dGTP as substrate, and 8.0- CC 8.5 with 2-hydroxy-dATP as substrate; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Isoform p18: Cytoplasm. Mitochondrion CC matrix. Nucleus. Note=Mostly present in cytoplasm. Variant Met-124 CC has decreased efficiency in translocation to mitochondria. CC -!- SUBCELLULAR LOCATION: Isoform p26: Cytoplasm. Mitochondrion CC matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=4; CC Name=p26; CC IsoId=P36639-1; Sequence=Displayed; CC Note=Derived from a B-type mRNA with a polymorphic alteration CC (GU-->GC) at the beginning of exon 2c that converts an in-frame CC UGA to CGA yielding another in-frame AUG further upstream; CC Name=p22; CC IsoId=P36639-2; Sequence=VSP_018812; CC Name=p21; CC IsoId=P36639-3; Sequence=VSP_018813; CC Name=p18; CC IsoId=P36639-4; Sequence=VSP_018814; CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in CC thymus, testis, embryo and proliferating blood lymphocytes. CC -!- DEVELOPMENTAL STAGE: In peripheral blood lymphocytes, expressed at CC much higher levels in proliferating cells than in resting cells. CC -!- PTM: The N-terminus is blocked. CC -!- POLYMORPHISM: A polymorphism between Met-1 and Met-19 removes a CC stop codon before the initiation codon for isoform p22 and gives CC rise to the production of isoform p26. The allele frequency of CC isoform p26 is about 20%. The allele may be associated with an CC increased risk for small cell lung carcinoma (SCLC). CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/nudt1/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D16581; BAA04013.1; -; mRNA. DR EMBL; D38594; BAA07601.1; -; Genomic_DNA. DR EMBL; AB025233; BAA83791.1; -; mRNA. DR EMBL; AB025234; BAA83792.1; -; mRNA. DR EMBL; AB025235; BAA83793.1; -; mRNA. DR EMBL; AB025236; BAA83794.1; -; mRNA. DR EMBL; AB025237; BAA83795.1; -; mRNA. DR EMBL; AB025238; BAA83796.1; -; mRNA. DR EMBL; AB025239; BAA83797.1; -; mRNA. DR EMBL; AB025240; BAA83798.1; -; mRNA. DR EMBL; AB025241; BAA83799.1; -; mRNA. DR EMBL; AB025242; BAA83800.1; -; mRNA. DR EMBL; DQ230907; ABB02181.1; -; Genomic_DNA. DR EMBL; CH236953; EAL23948.1; -; Genomic_DNA. DR EMBL; CH236953; EAL23949.1; -; Genomic_DNA. DR EMBL; CR407655; CAG28583.1; -; mRNA. DR EMBL; CH471144; EAW87225.1; -; Genomic_DNA. DR EMBL; CH471144; EAW87227.1; -; Genomic_DNA. DR EMBL; AC004971; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014618; AAH14618.1; -; mRNA. DR EMBL; BC040144; AAH40144.2; -; mRNA. DR EMBL; BC051375; AAH51375.2; -; mRNA. DR EMBL; BC065367; AAH65367.1; -; mRNA. DR CCDS; CCDS5329.1; -. [P36639-2] DR CCDS; CCDS5330.1; -. [P36639-4] DR RefSeq; NP_002443.3; NM_002452.3. [P36639-4] DR RefSeq; NP_945186.1; NM_198948.1. [P36639-4] DR RefSeq; NP_945187.1; NM_198949.1. [P36639-2] DR RefSeq; NP_945188.1; NM_198950.1. [P36639-4] DR RefSeq; NP_945190.1; NM_198952.1. [P36639-2] DR RefSeq; NP_945191.1; NM_198953.1. [P36639-4] DR RefSeq; NP_945192.1; NM_198954.1. [P36639-2] DR UniGene; Hs.534331; -. DR PDB; 1IRY; NMR; -; A=42-197. DR PDB; 3Q93; X-ray; 1.80 A; A/B=42-197. DR PDB; 3WHW; X-ray; 2.70 A; A/B=42-197. DR PDB; 3ZR0; X-ray; 1.80 A; A/B=42-197. DR PDB; 3ZR1; X-ray; 1.90 A; A/B=42-197. DR PDB; 4C9W; X-ray; 1.65 A; A=42-197. DR PDB; 4C9X; X-ray; 1.20 A; A=42-197. DR PDB; 4N1T; X-ray; 1.60 A; A=42-197. DR PDB; 4N1U; X-ray; 1.60 A; A/B=42-196. DR PDBsum; 1IRY; -. DR PDBsum; 3Q93; -. DR PDBsum; 3WHW; -. DR PDBsum; 3ZR0; -. DR PDBsum; 3ZR1; -. DR PDBsum; 4C9W; -. DR PDBsum; 4C9X; -. DR PDBsum; 4N1T; -. DR PDBsum; 4N1U; -. DR ProteinModelPortal; P36639; -. DR SMR; P36639; 44-197. DR BioGrid; 110621; 11. DR IntAct; P36639; 4. DR STRING; 9606.ENSP00000339503; -. DR PhosphoSite; P36639; -. DR DMDM; 254763430; -. DR MaxQB; P36639; -. DR PaxDb; P36639; -. DR PRIDE; P36639; -. DR DNASU; 4521; -. DR Ensembl; ENST00000339737; ENSP00000343439; ENSG00000106268. [P36639-4] DR Ensembl; ENST00000343985; ENSP00000339503; ENSG00000106268. [P36639-2] DR Ensembl; ENST00000356714; ENSP00000349148; ENSG00000106268. [P36639-4] DR Ensembl; ENST00000397046; ENSP00000380239; ENSG00000106268. [P36639-4] DR Ensembl; ENST00000397048; ENSP00000380241; ENSG00000106268. [P36639-2] DR Ensembl; ENST00000397049; ENSP00000380242; ENSG00000106268. [P36639-2] DR GeneID; 4521; -. DR KEGG; hsa:4521; -. DR UCSC; uc003slp.1; human. [P36639-1] DR CTD; 4521; -. DR GeneCards; GC07P002248; -. DR HGNC; HGNC:8048; NUDT1. DR HPA; HPA012636; -. DR MIM; 600312; gene. DR neXtProt; NX_P36639; -. DR PharmGKB; PA31830; -. DR eggNOG; COG0494; -. DR HOGENOM; HOG000261970; -. DR HOVERGEN; HBG000032; -. DR InParanoid; P36639; -. DR KO; K17816; -. DR OMA; WFPLMLQ; -. DR OrthoDB; EOG7BS4BT; -. DR PhylomeDB; P36639; -. DR TreeFam; TF106348; -. DR BioCyc; MetaCyc:HS02879-MONOMER; -. DR Reactome; REACT_111217; Metabolism. DR EvolutionaryTrace; P36639; -. DR GeneWiki; NUDT1; -. DR GenomeRNAi; 4521; -. DR NextBio; 17452; -. DR PRO; PR:P36639; -. DR ArrayExpress; P36639; -. DR Bgee; P36639; -. DR CleanEx; HS_NUDT1; -. DR Genevestigator; P36639; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IDA:UniProtKB. DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IDA:UniProtKB. DR GO; GO:0047693; F:ATP diphosphatase activity; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030515; F:snoRNA binding; ISS:UniProtKB. DR GO; GO:0006200; P:ATP catabolic process; IDA:UniProtKB. DR GO; GO:0046061; P:dATP catabolic process; IDA:UniProtKB. DR GO; GO:0006203; P:dGTP catabolic process; IDA:UniProtKB. DR GO; GO:0042262; P:DNA protection; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IC:UniProtKB. DR GO; GO:0006184; P:GTP catabolic process; IDA:UniProtKB. DR GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; TAS:Reactome. DR GO; GO:0055086; P:nucleobase-containing small molecule metabolic process; TAS:Reactome. DR GO; GO:0006195; P:purine nucleotide catabolic process; IDA:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR InterPro; IPR003563; OxG-triPHTase. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR01403; 8OXTPHPHTASE. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Complete proteome; Cytoplasm; KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding; KW Mitochondrion; Nucleus; Polymorphism; Reference proteome; RNA-binding; KW Transit peptide. FT TRANSIT 1 18 Mitochondrion (Potential). FT CHAIN 19 197 7,8-dihydro-8-oxoguanine triphosphatase. FT /FTId=PRO_0000019944. FT DOMAIN 44 173 Nudix hydrolase. FT REGION 76 79 Substrate binding (Probable). FT REGION 158 161 Substrate binding. FT MOTIF 78 99 Nudix box. FT METAL 78 78 Magnesium; via carbonyl oxygen (By FT similarity). FT METAL 93 93 Magnesium (By similarity). FT METAL 96 96 Magnesium (By similarity). FT METAL 97 97 Magnesium (By similarity). FT BINDING 49 49 Substrate; via carbonyl oxygen. FT BINDING 68 68 Substrate. FT BINDING 74 74 Substrate. FT SITE 68 68 Important for 2-OH-dATPase and 8-oxo- FT dGTPase activities. FT SITE 158 158 Essential for 2-OH-dATPase and 8-oxo- FT dGTPase activities. FT SITE 160 160 Essential for 2-OH-dATPase activity and FT important for 8-oxo-dGTPase activity. FT VAR_SEQ 1 41 Missing (in isoform p18). FT /FTId=VSP_018814. FT VAR_SEQ 1 26 Missing (in isoform p21). FT /FTId=VSP_018813. FT VAR_SEQ 1 18 Missing (in isoform p22). FT /FTId=VSP_018812. FT VARIANT 77 77 G -> W (in dbSNP:rs11547459). FT /FTId=VAR_068715. FT VARIANT 124 124 V -> M (associated with type I diabetes FT in Japanese female population; may be FT associated with an increased risk for FT small cell lung carcinoma (SCLC); FT dbSNP:rs4866). FT /FTId=VAR_013757. FT MUTAGEN 68 68 F->A: Reduces 2-OH-dATPase and 8-oxo- FT dGTPase activities. FT MUTAGEN 77 77 G->R: Reduces activity by 97%. FT MUTAGEN 78 78 G->F: Loss of activity. FT MUTAGEN 80 80 V->E: Loss of activity. FT MUTAGEN 81 81 Q->P: Reduces activity by 97%. FT MUTAGEN 83 83 G->I: Reduces activity by 60%. FT MUTAGEN 86 86 I->K: Loss of activity. FT MUTAGEN 88 88 D->P: Loss of activity. FT MUTAGEN 89 89 G->M: Loss of activity. FT MUTAGEN 90 90 A->P: Loss of activity. FT MUTAGEN 94 94 L->P: Loss of activity. FT MUTAGEN 95 95 Q->P: Loss of activity. FT MUTAGEN 96 96 E->G: Loss of activity. FT MUTAGEN 97 97 E->Y: Loss of activity. FT MUTAGEN 98 98 S->R: Loss of activity. FT MUTAGEN 158 158 W->A: Greatly reduces or abolishes 2-OH- FT dATPase and 8-oxo-dGTPase activities. FT MUTAGEN 158 158 W->Y: Enhances 2-OH-dATPase activity and FT greatly reduces 8-oxo-dGTPase activity. FT MUTAGEN 160 160 D->A,N: Loss of 2-OH-dATPase activity, FT reduces 8-oxo-dGTPase activity. FT MUTAGEN 191 191 L->A: Reduces 2-OH-dATPase and 8-oxo- FT dGTPase activities and increases FT thermolability. FT MUTAGEN 192 197 Missing: Almost abolishes 2-OH-dATPase FT and 8-oxo-dGTPase activities and FT increases thermolability. FT MUTAGEN 192 192 R->A: Reduces 2-OH-dATPase and 8-oxo- FT dGTPase activities and increases FT thermolability. FT MUTAGEN 193 197 Missing: Greatly reduces 2-OH-dATPase and FT 8-oxo-dGTPase activities and increases FT thermolability. FT MUTAGEN 193 193 E->A: Reduces 2-OH-dATPase and 8-oxo- FT dGTPase activities and increases FT thermolability. FT MUTAGEN 194 197 Missing: Reduces 2-OH-dATPase and 8-oxo- FT dGTPase activities and increases FT thermolability. FT MUTAGEN 194 194 V->A: Reduces 2-OH-dATPase and 8-oxo- FT dGTPase activities and increases FT thermolability. FT MUTAGEN 195 197 Missing: Slightly enhances 2-OH-dATPase FT and 8-oxo-dGTPase activities and FT increases thermolability. FT MUTAGEN 195 195 D->A: Enhances 2-OH-dATPase and 8-oxo- FT dGTPase activities and increases FT thermolability. FT MUTAGEN 196 196 T->A: Reduces 2-OH-dATPase and 8-oxo- FT dGTPase activities and increases FT thermolability. FT MUTAGEN 197 197 V->A: Slightly reduces 2-OH-dATPase and FT 8-oxo-dGTPase activities and increases FT thermolability. FT STRAND 45 54 FT STRAND 56 64 FT TURN 68 71 FT STRAND 72 74 FT STRAND 76 79 FT HELIX 86 98 FT STRAND 101 103 FT STRAND 106 115 FT STRAND 121 130 FT STRAND 132 134 FT STRAND 140 148 FT HELIX 149 151 FT HELIX 154 156 FT HELIX 161 169 FT STRAND 173 181 FT TURN 182 184 FT STRAND 185 195 SQ SEQUENCE 197 AA; 22520 MW; 82AFF5E1CE287957 CRC64; MYWSNQITRR LGERVQGFMS GISPQQMGEP EGSWSGKNPG TMGASRLYTL VLVLQPQRVL LGMKKRGFGA GRWNGFGGKV QEGETIEDGA RRELQEESGL TVDALHKVGQ IVFEFVGEPE LMDVHVFCTD SIQGTPVESD EMRPCWFQLD QIPFKDMWPD DSYWFPLLLQ KKKFHGYFKF QGQDTILDYT LREVDTV // ID A16L1_HUMAN Reviewed; 607 AA. AC Q676U5; A3EXK9; A3EXL0; B6ZDH0; Q6IPN1; Q6UXW4; Q6ZVZ5; Q8NCY2; AC Q96JV5; Q9H619; DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 2. DT 09-JUL-2014, entry version 111. DE RecName: Full=Autophagy-related protein 16-1; DE AltName: Full=APG16-like 1; GN Name=ATG16L1; Synonyms=APG16L; ORFNames=UNQ9393/PRO34307; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-300. RC TISSUE=Fetal brain; RX PubMed=15620219; DOI=10.1080/10425170400004104; RA Zheng H., Ji C., Li J., Jiang H., Ren M., Lu Q., Gu S., Mao Y., RA Xie Y.; RT "Cloning and analysis of human Apg16L."; RL DNA Seq. 15:303-305(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), AND ASSOCIATION OF RP VARIANT ALA-300 WITH SUSCEPTIBILITY TO IBD10. RX PubMed=17200669; DOI=10.1038/ng1954; RA Hampe J., Franke A., Rosenstiel P., Till A., Teuber M., Huse K., RA Albrecht M., Mayr G., De La Vega F.M., Briggs J., Guenther S., RA Prescott N.J., Onnie C.M., Haesler R., Sipos B., Foelsch U.R., RA Lengauer T., Platzer M., Mathew C.G., Krawczak M., Schreiber S.; RT "A genome-wide association scan of nonsynonymous SNPs identifies a RT susceptibility variant for Crohn disease in ATG16L1."; RL Nat. Genet. 39:207-211(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 55-607 (ISOFORM 2). RC TISSUE=Brain, Placenta, and Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 114-607 (ISOFORM 2). RC TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 513-607. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-287, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP FUNCTION, AND INTERACTION WITH TMEM59; TLR2 AND NOD2. RX PubMed=23376921; DOI=10.1038/emboj.2013.8; RA Boada-Romero E., Letek M., Fleischer A., Pallauf K., Ramon-Barros C., RA Pimentel-Muinos F.X.; RT "TMEM59 defines a novel ATG16L1-binding motif that promotes local RT activation of LC3."; RL EMBO J. 32:566-582(2013). RN [12] RP ASSOCIATION OF VARIANT ALA-300 WITH SUSCEPTIBILITY TO IBD10. RX PubMed=17435756; DOI=10.1038/ng2032; RA Rioux J.D., Xavier R.J., Taylor K.D., Silverberg M.S., Goyette P., RA Huett A., Green T., Kuballa P., Barmada M.M., Datta L.W., RA Shugart Y.Y., Griffiths A.M., Targan S.R., Ippoliti A.F., RA Bernard E.-J., Mei L., Nicolae D.L., Regueiro M., Schumm L.P., RA Steinhart A.H., Rotter J.I., Duerr R.H., Cho J.H., Daly M.J., RA Brant S.R.; RT "Genome-wide association study identifies new susceptibility loci for RT Crohn disease and implicates autophagy in disease pathogenesis."; RL Nat. Genet. 39:596-604(2007). RN [13] RP FUNCTION IN AUTOPHAGY, CLEAVAGE BY CASP3, CHARACTERIZATION OF VARIANT RP ALA-300, AND MUTAGENESIS OF ASP-299. RX PubMed=24553140; DOI=10.1038/nature13044; RA Murthy A., Li Y., Peng I., Reichelt M., Katakam A.K., Noubade R., RA Roose-Girma M., Devoss J., Diehl L., Graham R.R., RA van Lookeren Campagne M.; RT "A Crohn's disease variant in Atg16l1 enhances its degradation by RT caspase 3."; RL Nature 506:456-462(2014). CC -!- FUNCTION: Plays an essential role in autophagy: interacts with CC ATG12-ATG5 to mediate the conjugation of phosphatidylethanolamine CC (PE) to LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C), to produce a CC membrane-bound activated form of LC3 named LC3-II. Thereby, CC controls the elongation of the nascent autophagosomal membrane. CC -!- SUBUNIT: Homooligomer. Interacts with ATG5. Part of either the CC minor and major complexes respectively composed of 4 sets of CC ATG12-ATG5 and ATG16L1 (400 kDa) or 8 sets of ATG12-ATG5 and CC ATG16L1 (800 kDa) (By similarity). Interacts with RAB33B (By CC similarity). Interacts with TMEM59, TLR2 and NOD2. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-535909, EBI-535909; CC P60520:GABARAPL2; NbExp=2; IntAct=EBI-535909, EBI-720116; CC Q9GZQ8:MAP1LC3B; NbExp=2; IntAct=EBI-535909, EBI-373144; CC Q9BXW4:MAP1LC3C; NbExp=4; IntAct=EBI-535909, EBI-2603996; CC Q8TDY2:RB1CC1; NbExp=5; IntAct=EBI-535909, EBI-1047793; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Preautophagosomal CC structure membrane; Peripheral membrane protein (By similarity). CC Note=Localized to preautophagosomal structure (PAS) where it is CC involved in the membrane targeting of ATG5 (By similarity). CC Localizes also to discrete punctae along the ciliary axoneme (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=APG16L beta; CC IsoId=Q676U5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q676U5-2; Sequence=VSP_013386; CC Name=3; CC IsoId=Q676U5-3; Sequence=VSP_013387, VSP_013388; CC Note=No experimental confirmation available. May be produced at CC very low levels due to a premature stop codon in the mRNA, CC leading to nonsense-mediated mRNA decay; CC Name=4; CC IsoId=Q676U5-4; Sequence=VSP_013389, VSP_013390; CC Note=No experimental confirmation available; CC Name=5; CC IsoId=Q676U5-5; Sequence=VSP_013389, VSP_013386; CC Note=No experimental confirmation available; CC -!- PTM: Proteolytic cleavage by activated CASP3 leads to degradation CC and may regulate autophagy upon cellular stress and apoptotic CC stimuli. CC -!- DISEASE: Inflammatory bowel disease 10 (IBD10) [MIM:611081]: A CC chronic, relapsing inflammation of the gastrointestinal tract with CC a complex etiology. It is subdivided into Crohn disease and CC ulcerative colitis phenotypes. Crohn disease may affect any part CC of the gastrointestinal tract from the mouth to the anus, but most CC frequently it involves the terminal ileum and colon. Bowel CC inflammation is transmural and discontinuous; it may contain CC granulomas or be associated with intestinal or perianal fistulas. CC In contrast, in ulcerative colitis, the inflammation is continuous CC and limited to rectal and colonic mucosal layers; fistulas and CC granulomas are not observed. Both diseases include extraintestinal CC inflammation of the skin, eyes, or joints. Note=Disease CC susceptibility is associated with variations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the WD repeat ATG16 family. CC -!- SIMILARITY: Contains 7 WD repeats. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15448.1; Type=Erroneous translation; Note=Wrong choice of CDS; CC Sequence=BAB55412.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY398617; AAR32130.1; -; mRNA. DR EMBL; EF079889; ABN48554.1; -; mRNA. DR EMBL; EF079890; ABN48555.1; -; mRNA. DR EMBL; AY358182; AAQ88549.1; -; mRNA. DR EMBL; AK026330; BAB15448.1; ALT_SEQ; mRNA. DR EMBL; AK027854; BAB55412.1; ALT_INIT; mRNA. DR EMBL; AK123876; BAC85713.1; -; mRNA. DR EMBL; AC013726; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471063; EAW71034.1; -; Genomic_DNA. DR EMBL; BC071846; AAH71846.1; -; mRNA. DR EMBL; AL834526; CAD39182.1; -; mRNA. DR CCDS; CCDS2502.2; -. [Q676U5-2] DR CCDS; CCDS2503.2; -. [Q676U5-1] DR CCDS; CCDS54438.1; -. [Q676U5-5] DR RefSeq; NP_001177195.1; NM_001190266.1. DR RefSeq; NP_001177196.1; NM_001190267.1. DR RefSeq; NP_060444.3; NM_017974.3. [Q676U5-2] DR RefSeq; NP_110430.5; NM_030803.6. [Q676U5-1] DR RefSeq; NP_942593.2; NM_198890.2. [Q676U5-5] DR UniGene; Hs.529322; -. DR PDB; 4GDK; X-ray; 2.70 A; C/F=11-43. DR PDB; 4GDL; X-ray; 2.88 A; C=11-43. DR PDB; 4NAW; X-ray; 2.20 A; C/G/K/O=11-43. DR PDBsum; 4GDK; -. DR PDBsum; 4GDL; -. DR PDBsum; 4NAW; -. DR ProteinModelPortal; Q676U5; -. DR SMR; Q676U5; 11-43, 312-604. DR BioGrid; 120375; 28. DR DIP; DIP-27552N; -. DR DIP; DIP-50290N; -. DR IntAct; Q676U5; 25. DR MINT; MINT-1141152; -. DR STRING; 9606.ENSP00000375872; -. DR PhosphoSite; Q676U5; -. DR DMDM; 62510482; -. DR MaxQB; Q676U5; -. DR PaxDb; Q676U5; -. DR PRIDE; Q676U5; -. DR DNASU; 55054; -. DR Ensembl; ENST00000347464; ENSP00000318259; ENSG00000085978. [Q676U5-5] DR Ensembl; ENST00000373525; ENSP00000362625; ENSG00000085978. [Q676U5-4] DR Ensembl; ENST00000392017; ENSP00000375872; ENSG00000085978. [Q676U5-1] DR Ensembl; ENST00000392020; ENSP00000375875; ENSG00000085978. [Q676U5-2] DR GeneID; 55054; -. DR KEGG; hsa:55054; -. DR UCSC; uc002vtx.2; human. [Q676U5-5] DR UCSC; uc002vty.3; human. [Q676U5-1] DR UCSC; uc002vtz.3; human. [Q676U5-4] DR UCSC; uc002vua.3; human. [Q676U5-2] DR CTD; 55054; -. DR GeneCards; GC02P234118; -. DR HGNC; HGNC:21498; ATG16L1. DR HPA; HPA012577; -. DR MIM; 610767; gene. DR MIM; 611081; phenotype. DR neXtProt; NX_Q676U5; -. DR Orphanet; 206; Crohn disease. DR PharmGKB; PA134902949; -. DR eggNOG; COG2319; -. DR HOGENOM; HOG000112569; -. DR HOVERGEN; HBG050534; -. DR KO; K17890; -. DR OrthoDB; EOG70CR6M; -. DR PhylomeDB; Q676U5; -. DR TreeFam; TF315541; -. DR SignaLink; Q676U5; -. DR GeneWiki; ATG16L1; -. DR GenomeRNAi; 55054; -. DR NextBio; 58531; -. DR PRO; PR:Q676U5; -. DR ArrayExpress; Q676U5; -. DR Bgee; Q676U5; -. DR CleanEx; HS_ATG16L1; -. DR Genevestigator; Q676U5; -. DR GO; GO:0005776; C:autophagic vacuole; ISS:UniProtKB. DR GO; GO:0000421; C:autophagic vacuole membrane; IEA:Ensembl. DR GO; GO:0005930; C:axoneme; ISS:UniProtKB. DR GO; GO:0034045; C:pre-autophagosomal structure membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0000045; P:autophagic vacuole assembly; NAS:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; NAS:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR013923; Autophagy-rel_prot_16. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_dom. DR Pfam; PF08614; ATG16; 1. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; SSF50978; 1. DR PROSITE; PS00678; WD_REPEATS_1; 3. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Autophagy; Coiled coil; KW Complete proteome; Cytoplasm; Membrane; Phosphoprotein; Polymorphism; KW Protein transport; Reference proteome; Repeat; Transport; WD repeat. FT CHAIN 1 607 Autophagy-related protein 16-1. FT /FTId=PRO_0000050848. FT REPEAT 320 359 WD 1. FT REPEAT 364 403 WD 2. FT REPEAT 406 445 WD 3. FT REPEAT 447 484 WD 4. FT REPEAT 486 525 WD 5. FT REPEAT 532 573 WD 6. FT REPEAT 575 607 WD 7. FT COILED 78 230 Potential. FT MOTIF 296 299 Caspase cleavage. FT MOD_RES 269 269 Phosphoserine. FT MOD_RES 287 287 Phosphoserine. FT VAR_SEQ 70 213 Missing (in isoform 4 and isoform 5). FT /FTId=VSP_013389. FT VAR_SEQ 266 284 Missing (in isoform 2 and isoform 5). FT /FTId=VSP_013386. FT VAR_SEQ 334 368 Missing (in isoform 4). FT /FTId=VSP_013390. FT VAR_SEQ 443 470 IKTVFAGSSCNDIVCTEQCVMSGHFDKK -> EEIQSLCLC FT ICLDVSVEVCVCTSEPAFM (in isoform 3). FT /FTId=VSP_013387. FT VAR_SEQ 471 607 Missing (in isoform 3). FT /FTId=VSP_013388. FT VARIANT 300 300 T -> A (associated with susceptibility to FT IBD10; has no effect on the stability of FT the protein; enhances the cleavage and FT the degradation mediated by activated FT CASP3; results in reduced autophagy and FT defective clearance of intestinal FT pathogens; dbSNP:rs2241880). FT /FTId=VAR_021834. FT VARIANT 307 307 E -> K (in dbSNP:rs1866878). FT /FTId=VAR_053386. FT MUTAGEN 299 299 D->E: Prevents cleavage by activated FT CASP3. FT CONFLICT 151 151 K -> R (in Ref. 6; BAB55412). FT CONFLICT 328 328 V -> A (in Ref. 6; BAB55412). FT CONFLICT 529 529 P -> T (in Ref. 6; BAB55412). FT HELIX 12 28 FT HELIX 30 42 SQ SEQUENCE 607 AA; 68265 MW; 5A5816AE2CF03CA0 CRC64; MSSGLRAADF PRWKRHISEQ LRRRDRLQRQ AFEEIILQYN KLLEKSDLHS VLAQKLQAEK HDVPNRHEIS PGHDGTWNDN QLQEMAQLRI KHQEELTELH KKRGELAQLV IDLNNQMQRK DREMQMNEAK IAECLQTISD LETECLDLRT KLCDLERANQ TLKDEYDALQ ITFTALEGKL RKTTEENQEL VTRWMAEKAQ EANRLNAENE KDSRRRQARL QKELAEAAKE PLPVEQDDDI EVIVDETSDH TEETSPVRAI SRAATKRLSQ PAGGLLDSIT NIFGRRSVSS FPVPQDNVDT HPGSGKEVRV PATALCVFDA HDGEVNAVQF SPGSRLLATG GMDRRVKLWE VFGEKCEFKG SLSGSNAGIT SIEFDSAGSY LLAASNDFAS RIWTVDDYRL RHTLTGHSGK VLSAKFLLDN ARIVSGSHDR TLKLWDLRSK VCIKTVFAGS SCNDIVCTEQ CVMSGHFDKK IRFWDIRSES IVREMELLGK ITALDLNPER TELLSCSRDD LLKVIDLRTN AIKQTFSAPG FKCGSDWTRV VFSPDGSYVA AGSAEGSLYI WSVLTGKVEK VLSKQHSSSI NAVAWSPSGS HVVSVDKGCK AVLWAQY // ID A1AG1_HUMAN Reviewed; 201 AA. AC P02763; B7ZKQ5; Q5T539; Q5U067; Q8TC16; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 09-JUL-2014, entry version 162. DE RecName: Full=Alpha-1-acid glycoprotein 1; DE Short=AGP 1; DE AltName: Full=Orosomucoid-1; DE Short=OMD 1; DE Flags: Precursor; GN Name=ORM1; Synonyms=AGP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2822385; RA Dente L., Pizza M.G., Metspalu A., Cortese R.; RT "Structure and expression of the genes coding for human alpha 1-acid RT glycoprotein."; RL EMBO J. 6:2289-2296(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3770479; DOI=10.1016/0378-1119(86)90051-X; RA Board P.G., Jones I.M., Bentley A.K.; RT "Molecular cloning and nucleotide sequence of human alpha 1 acid RT glycoprotein cDNA."; RL Gene 44:127-131(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2409529; DOI=10.1093/nar/13.11.3941; RA Dente L., Ciliberto G., Cortese R.; RT "Structure of the human alpha 1-acid glycoprotein gene: sequence RT homology with other human acute phase protein genes."; RL Nucleic Acids Res. 13:3941-3952(1985). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-38. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-38. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-38; CYS-167 RP AND MET-174. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 19-129, AND PYROGLUTAMATE FORMATION AT GLN-19. RX PubMed=4711474; DOI=10.1021/bi00738a026; RA Schmid K., Kaufmann H., Isemura S., Bauer F., Emura J., Motoyama T., RA Ishiguro M., Nanno S.; RT "Structure of alpha 1-acid glycoprotein. The complete amino acid RT sequence, multiple amino acid substitutions, and homology with the RT immunoglobulins."; RL Biochemistry 12:2711-2724(1973). RN [10] RP PROTEIN SEQUENCE OF 129-201. RX PubMed=4561179; DOI=10.1021/bi00770a022; RA Ikenaka T., Ishiguro M., Emura J., Kaufmann H., Isemura S., Bauer W., RA Schmid K.; RT "Isolation and partial characterization of the cyanogen bromide RT fragments of alpha 1-acid glycoprotein and the elucidation of the RT amino acid sequence of the carboxyl-terminal cyanogen bromide RT fragment."; RL Biochemistry 11:3817-3829(1972). RN [11] RP DISULFIDE BONDS. RX PubMed=4603214; DOI=10.1021/bi00710a006; RA Schmid K., Buergi W., Collins J.H., Nanno S.; RT "The disulfide bonds of alpha1-acid glycoprotein."; RL Biochemistry 13:2694-2697(1974). RN [12] RP GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103. RX PubMed=1567356; RA Treuheit M.J., Costello C.E., Halsall H.B.; RT "Analysis of the five glycosylation sites of human alpha 1-acid RT glycoprotein."; RL Biochem. J. 283:105-112(1992). RN [13] RP GLYCOSYLATION AT ASN-33. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [14] RP GLYCOSYLATION AT ASN-33; ASN-72 AND ASN-93, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=15253437; DOI=10.1021/pr034112b; RA Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.; RT "A new strategy for identification of N-glycosylated proteins and RT unambiguous assignment of their glycosylation sites using HILIC RT enrichment and partial deglycosylation."; RL J. Proteome Res. 3:556-566(2004). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-93. RC TISSUE=Bile; RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200; RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; RT "A proteomic analysis of human bile."; RL Mol. Cell. Proteomics 3:715-728(2004). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 RP AND ASN-103. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [17] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 RP AND ASN-103. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [18] RP FUNCTION. RX PubMed=17008009; DOI=10.1016/j.bbagen.2006.08.015; RA Fitos I., Visy J., Zsila F., Mady G., Simonyi M.; RT "Selective binding of imatinib to the genetic variants of human RT alpha1-acid glycoprotein."; RL Biochim. Biophys. Acta 1760:1704-1712(2006). RN [19] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93. RC TISSUE=Saliva; RX PubMed=16740002; DOI=10.1021/pr050492k; RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., RA Loo J.A.; RT "Identification of N-linked glycoproteins in human saliva by RT glycoprotein capture and mass spectrometry."; RL J. Proteome Res. 5:1493-1503(2006). RN [20] RP FUNCTION. RX PubMed=17321687; DOI=10.1016/j.bbagen.2007.01.009; RA Zsila F., Iwao Y.; RT "The drug binding site of human alpha1-acid glycoprotein: insight from RT induced circular dichroism and electronic absorption spectra."; RL Biochim. Biophys. Acta 1770:797-809(2007). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93 AND ASN-103. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33 AND ASN-72, AND RP STRUCTURE OF CARBOHYDRATES. RC TISSUE=Cerebrospinal fluid; RX PubMed=19838169; DOI=10.1038/nmeth.1392; RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., RA Brinkmalm G., Larson G.; RT "Enrichment of glycopeptides for glycan structure and attachment site RT identification."; RL Nat. Methods 6:809-811(2009). RN [23] RP GLYCOSYLATION AT ASN-33, STRUCTURE OF CARBOHYDRATES, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.M111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of RT N-and O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 0:0-0(2011). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 20-201, DOMAIN, AND DISULFIDE RP BONDS. RX PubMed=18823996; DOI=10.1016/j.jmb.2008.09.020; RA Schonfeld D.L., Ravelli R.B., Mueller U., Skerra A.; RT "The 1.8-A crystal structure of alpha1-acid glycoprotein (Orosomucoid) RT solved by UV RIP reveals the broad drug-binding activity of this human RT plasma lipocalin."; RL J. Mol. Biol. 384:393-405(2008). RN [25] RP VARIANTS ARG-38 AND MET-174. RX PubMed=9050929; DOI=10.1007/s004390050378; RA Yuasa I., Umetsu K., Vogt U., Nakamura H., Nanba E., Tamaki N., RA Irizawa Y.; RT "Human orosomucoid polymorphism: molecular basis of the three common RT ORM1 alleles, ORM1*F1, ORM1*F2, and ORM1*S."; RL Hum. Genet. 99:393-398(1997). CC -!- FUNCTION: Functions as transport protein in the blood stream. CC Binds various ligands in the interior of its beta-barrel domain. CC Also binds synthetic drugs and influences their distribution and CC availability in the body. Appears to function in modulating the CC activity of the immune system during the acute-phase reaction. CC -!- INTERACTION: CC P05121:SERPINE1; NbExp=4; IntAct=EBI-976767, EBI-953978; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- INDUCTION: Synthesis is controlled by glucocorticoids, CC interleukin-1 and interleukin-6, It increases 5- to 50-fold upon CC inflammation. CC -!- DOMAIN: Contains a beta-barrel that binds various ligands in its CC interior. CC -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 CC (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor). CC -!- POLYMORPHISM: Three common alleles of ORM1 are known. ORM1*F1 has CC Gln-38/Val-174; ORM1*F2 has Gln-38/Met-174 and ORM1*S has Arg- CC 38/Val-174. The sequence shown is that of allele ORM1*F1. CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family. CC -!- SEQUENCE CAUTION: CC Sequence=CAA29229.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X02544; CAA26397.1; -; mRNA. DR EMBL; M13692; AAA35515.1; -; mRNA. DR EMBL; X05779; CAA29229.1; ALT_SEQ; Genomic_DNA. DR EMBL; X05780; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X05781; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X05782; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X05783; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X05784; CAA29229.1; JOINED; Genomic_DNA. DR EMBL; X06676; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X06680; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BT019790; AAV38593.1; -; mRNA. DR EMBL; AK312035; BAG34972.1; -; mRNA. DR EMBL; AL356796; CAI16859.1; -; Genomic_DNA. DR EMBL; CH471090; EAW87416.1; -; Genomic_DNA. DR EMBL; BC104818; AAI04819.1; -; mRNA. DR EMBL; BC104820; AAI04821.1; -; mRNA. DR EMBL; BC143313; AAI43314.1; -; mRNA. DR EMBL; BC143314; AAI43315.1; -; mRNA. DR EMBL; BC026238; AAH26238.1; -; mRNA. DR CCDS; CCDS6803.1; -. DR PIR; A28346; OMHU1. DR RefSeq; NP_000598.2; NM_000607.2. DR UniGene; Hs.522356; -. DR PDB; 3KQ0; X-ray; 1.80 A; A=19-201. DR PDBsum; 3KQ0; -. DR ProteinModelPortal; P02763; -. DR SMR; P02763; 19-193. DR BioGrid; 111046; 7. DR IntAct; P02763; 7. DR MINT; MINT-202382; -. DR STRING; 9606.ENSP00000259396; -. DR BindingDB; P02763; -. DR ChEMBL; CHEMBL4285; -. DR DrugBank; DB01418; Acenocoumarol. DR DrugBank; DB00802; Alfentanil. DR DrugBank; DB01429; Aprindine. DR DrugBank; DB00280; Disopyramide. DR DrugBank; DB01359; Penbutolol. DR DrugBank; DB00946; Phenprocoumon. DR DrugBank; DB00908; Quinidine. DR DrugBank; DB00706; Tamsulosin. DR PhosphoSite; P02763; -. DR UniCarbKB; P02763; -. DR DMDM; 112877; -. DR SWISS-2DPAGE; P02763; -. DR MaxQB; P02763; -. DR PaxDb; P02763; -. DR PeptideAtlas; P02763; -. DR PRIDE; P02763; -. DR DNASU; 5004; -. DR Ensembl; ENST00000259396; ENSP00000259396; ENSG00000229314. DR GeneID; 5004; -. DR KEGG; hsa:5004; -. DR UCSC; uc004bik.4; human. DR CTD; 5004; -. DR GeneCards; GC09P117085; -. DR HGNC; HGNC:8498; ORM1. DR HPA; CAB006265; -. DR HPA; HPA046438; -. DR MIM; 138600; gene. DR neXtProt; NX_P02763; -. DR PharmGKB; PA260; -. DR eggNOG; NOG41523; -. DR HOGENOM; HOG000125170; -. DR HOVERGEN; HBG000035; -. DR InParanoid; P02763; -. DR KO; K17308; -. DR OrthoDB; EOG7B5WXT; -. DR PhylomeDB; P02763; -. DR TreeFam; TF343791; -. DR ChiTaRS; ORM1; human. DR EvolutionaryTrace; P02763; -. DR GeneWiki; ORM1; -. DR GenomeRNAi; 5004; -. DR NextBio; 19272; -. DR PRO; PR:P02763; -. DR ArrayExpress; P02763; -. DR Bgee; P02763; -. DR CleanEx; HS_ORM1; -. DR Genevestigator; P02763; -. DR GO; GO:0072562; C:blood microparticle; IDA:UniProt. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006953; P:acute-phase response; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0002682; P:regulation of immune system process; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 2.40.128.20; -; 1. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin-like. DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom. DR PANTHER; PTHR11967; PTHR11967; 1. DR Pfam; PF00061; Lipocalin; 1. DR PIRSF; PIRSF036899; AGP; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR SUPFAM; SSF50814; SSF50814; 1. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Polymorphism; KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal; KW Transport. FT SIGNAL 1 18 FT CHAIN 19 201 Alpha-1-acid glycoprotein 1. FT /FTId=PRO_0000017860. FT MOD_RES 19 19 Pyrrolidone carboxylic acid. FT CARBOHYD 33 33 N-linked (GlcNAc...) (complex). FT CARBOHYD 56 56 N-linked (GlcNAc...). FT CARBOHYD 72 72 N-linked (GlcNAc...) (complex). FT CARBOHYD 93 93 N-linked (GlcNAc...). FT CARBOHYD 103 103 N-linked (GlcNAc...). FT /FTId=CAR_000170. FT DISULFID 23 165 FT DISULFID 90 183 FT VARIANT 38 38 Q -> R (in allele ORM1*S). FT /FTId=VAR_013840. FT VARIANT 167 167 R -> C (in dbSNP:rs3182034). FT /FTId=VAR_056166. FT VARIANT 174 174 V -> M (in allele ORM1*F2; FT dbSNP:rs1126801). FT /FTId=VAR_013841. FT CONFLICT 170 170 K -> R (in Ref. 8; AAI43315). FT CONFLICT 182 182 Missing (in Ref. 10; AA sequence). FT CONFLICT 193 193 Missing (in Ref. 10; AA sequence). FT HELIX 24 26 FT HELIX 33 39 FT STRAND 41 52 FT HELIX 53 59 FT STRAND 62 72 FT TURN 73 76 FT STRAND 77 86 FT STRAND 89 100 FT TURN 101 104 FT STRAND 105 110 FT STRAND 113 121 FT STRAND 127 132 FT HELIX 137 139 FT STRAND 141 149 FT TURN 153 156 FT HELIX 157 166 FT HELIX 170 172 FT HELIX 178 180 FT HELIX 184 192 SQ SEQUENCE 201 AA; 23512 MW; 63292233AD6EAD8B CRC64; MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDQIT GKWFYIASAF RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQDQC IYNTTYLNVQ RENGTISRYV GGQEHFAHLL ILRDTKTYML AFDVNDEKNW GLSVYADKPE TTKEQLGEFY EALDCLRIPK SDVVYTDWKK DKCEPLEKQH EKERKQEEGE S // ID A1AG2_HUMAN Reviewed; 201 AA. AC P19652; B2R5L2; Q16571; Q5T538; Q6IB74; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 2. DT 09-JUL-2014, entry version 151. DE RecName: Full=Alpha-1-acid glycoprotein 2; DE Short=AGP 2; DE AltName: Full=Orosomucoid-2; DE Short=OMD 2; DE Flags: Precursor; GN Name=ORM2; Synonyms=AGP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2822385; RA Dente L., Pizza M.G., Metspalu A., Cortese R.; RT "Structure and expression of the genes coding for human alpha 1-acid RT glycoprotein."; RL EMBO J. 6:2289-2296(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2970990; DOI=10.1016/0378-1119(88)90228-4; RA Merritt C.M., Board P.G.; RT "Structure and characterisation of a duplicated human alpha 1 acid RT glycoprotein gene."; RL Gene 66:97-106(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP DISULFIDE BONDS. RX PubMed=4603214; DOI=10.1021/bi00710a006; RA Schmid K., Buergi W., Collins J.H., Nanno S.; RT "The disulfide bonds of alpha1-acid glycoprotein."; RL Biochemistry 13:2694-2697(1974). RN [9] RP GLYCOSYLATION AT ASN-33; ASN-56; ASN-72; ASN-93 AND ASN-103. RX PubMed=1567356; RA Treuheit M.J., Costello C.E., Halsall H.B.; RT "Analysis of the five glycosylation sites of human alpha 1-acid RT glycoprotein."; RL Biochem. J. 283:105-112(1992). RN [10] RP PYROGLUTAMATE FORMATION AT GLN-19, GLYCOSYLATION AT ASN-33 AND ASN-93, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15253437; DOI=10.1021/pr034112b; RA Hagglund P., Bunkenborg J., Elortza F., Jensen O.N., Roepstorff P.; RT "A new strategy for identification of N-glycosylated proteins and RT unambiguous assignment of their glycosylation sites using HILIC RT enrichment and partial deglycosylation."; RL J. Proteome Res. 3:556-566(2004). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33. RC TISSUE=Bile; RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200; RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; RT "A proteomic analysis of human bile."; RL Mol. Cell. Proteomics 3:715-728(2004). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72 AND RP ASN-93. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-72; ASN-93 RP AND ASN-103. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-56; ASN-93 AND RP ASN-103. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33, AND STRUCTURE OF RP CARBOHYDRATES. RC TISSUE=Cerebrospinal fluid; RX PubMed=19838169; DOI=10.1038/nmeth.1392; RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., RA Brinkmalm G., Larson G.; RT "Enrichment of glycopeptides for glycan structure and attachment site RT identification."; RL Nat. Methods 6:809-811(2009). RN [16] RP GLYCOSYLATION AT ASN-33, STRUCTURE OF CARBOHYDRATES, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.M111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of RT N-and O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 0:0-0(2011). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 19-201 OF VARIANT ARG-167 IN RP COMPLEXES WITH DISOPYRAMIDE; AMITRIPTYLINE AND CHLORPROMAZINE, RP FUNCTION, DISULFIDE BONDS, AND DOMAIN. RX PubMed=21349832; DOI=10.1074/jbc.M110.208926; RA Nishi K., Ono T., Nakamura T., Fukunaga N., Izumi M., Watanabe H., RA Suenaga A., Maruyama T., Yamagata Y., Curry S., Otagiri M.; RT "Structural insights into differences in drug-binding selectivity RT between two forms of human {alpha}1-acid glycoprotein genetic RT variants, the A and F1*S forms."; RL J. Biol. Chem. 286:14427-14434(2011). CC -!- FUNCTION: Functions as transport protein in the blood stream. CC Binds various hydrophobic ligands in the interior of its beta- CC barrel domain. Also binds synthetic drugs and influences their CC distribution and availability. Appears to function in modulating CC the activity of the immune system during the acute-phase reaction. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- INDUCTION: Synthesis is controlled by glucocorticoids, CC interleukin-1 and interleukin-6, It increases 5- to 50-fold upon CC inflammation. CC -!- DOMAIN: Contains a beta-barrel that binds various ligands in its CC interior. CC -!- PTM: N-glycosylated. N-glycan heterogeneity at Asn-33: Hex5HexNAc4 CC (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor). CC -!- POLYMORPHISM: Many different variants of ORM2 are known. CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family. CC -!- SEQUENCE CAUTION: CC Sequence=CAA29873.2; Type=Erroneous gene model prediction; CC Sequence=CAA29874.1; Type=Erroneous gene model prediction; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X06675; CAA29874.1; ALT_SEQ; Genomic_DNA. DR EMBL; X05780; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X06674; CAA29873.2; ALT_SEQ; Genomic_DNA. DR EMBL; X06676; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06677; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06678; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06679; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X06680; CAA29873.2; JOINED; Genomic_DNA. DR EMBL; X05784; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M21540; AAA51549.1; -; Genomic_DNA. DR EMBL; AK312226; BAG35159.1; -; mRNA. DR EMBL; CR456930; CAG33211.1; -; mRNA. DR EMBL; AL356796; CAI16860.1; -; Genomic_DNA. DR EMBL; CH471090; EAW87417.1; -; Genomic_DNA. DR EMBL; BC015964; AAH15964.1; -; mRNA. DR EMBL; BC056239; AAH56239.1; -; mRNA. DR CCDS; CCDS6804.1; -. DR PIR; JT0326; OMHU2. DR RefSeq; NP_000599.1; NM_000608.2. DR UniGene; Hs.719954; -. DR PDB; 3APU; X-ray; 2.10 A; A/B=19-201. DR PDB; 3APV; X-ray; 2.15 A; A/B=19-201. DR PDB; 3APW; X-ray; 2.20 A; A/B=19-201. DR PDB; 3APX; X-ray; 2.20 A; A=19-201. DR PDBsum; 3APU; -. DR PDBsum; 3APV; -. DR PDBsum; 3APW; -. DR PDBsum; 3APX; -. DR ProteinModelPortal; P19652; -. DR SMR; P19652; 19-196. DR BioGrid; 111047; 3. DR IntAct; P19652; 3. DR STRING; 9606.ENSP00000394936; -. DR ChEMBL; CHEMBL5958; -. DR PhosphoSite; P19652; -. DR UniCarbKB; P19652; -. DR DMDM; 231458; -. DR DOSAC-COBS-2DPAGE; P19652; -. DR SWISS-2DPAGE; P19652; -. DR MaxQB; P19652; -. DR PeptideAtlas; P19652; -. DR PRIDE; P19652; -. DR DNASU; 5005; -. DR Ensembl; ENST00000431067; ENSP00000394936; ENSG00000228278. DR GeneID; 5005; -. DR KEGG; hsa:5005; -. DR UCSC; uc004bil.3; human. DR CTD; 5005; -. DR GeneCards; GC09P117092; -. DR HGNC; HGNC:8499; ORM2. DR HPA; HPA046438; -. DR MIM; 138610; gene. DR neXtProt; NX_P19652; -. DR PharmGKB; PA32818; -. DR HOGENOM; HOG000125170; -. DR HOVERGEN; HBG000035; -. DR InParanoid; P19652; -. DR KO; K17308; -. DR OMA; SKEHMEE; -. DR OrthoDB; EOG7B5WXT; -. DR PhylomeDB; P19652; -. DR TreeFam; TF343791; -. DR EvolutionaryTrace; P19652; -. DR GenomeRNAi; 5005; -. DR NextBio; 19276; -. DR PRO; PR:P19652; -. DR ArrayExpress; P19652; -. DR Bgee; P19652; -. DR Genevestigator; P19652; -. DR GO; GO:0072562; C:blood microparticle; IDA:UniProt. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0006953; P:acute-phase response; TAS:ProtInc. DR GO; GO:0002682; P:regulation of immune system process; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 2.40.128.20; -; 1. DR InterPro; IPR001500; A1A_glycop. DR InterPro; IPR012674; Calycin. DR InterPro; IPR011038; Calycin-like. DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom. DR PANTHER; PTHR11967; PTHR11967; 1. DR Pfam; PF00061; Lipocalin; 1. DR PIRSF; PIRSF036899; AGP; 1. DR PRINTS; PR00708; A1AGLPROTEIN. DR SUPFAM; SSF50814; SSF50814; 1. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Complete proteome; Disulfide bond; KW Glycoprotein; Polymorphism; Pyrrolidone carboxylic acid; KW Reference proteome; Secreted; Signal; Transport. FT SIGNAL 1 18 FT CHAIN 19 201 Alpha-1-acid glycoprotein 2. FT /FTId=PRO_0000017861. FT MOD_RES 19 19 Pyrrolidone carboxylic acid. FT CARBOHYD 33 33 N-linked (GlcNAc...) (complex). FT CARBOHYD 56 56 N-linked (GlcNAc...). FT CARBOHYD 72 72 N-linked (GlcNAc...). FT CARBOHYD 93 93 N-linked (GlcNAc...). FT CARBOHYD 103 103 N-linked (GlcNAc...). FT /FTId=CAR_000171. FT DISULFID 23 165 FT DISULFID 90 183 FT VARIANT 38 38 R -> Q (in dbSNP:rs17650). FT /FTId=VAR_014667. FT VARIANT 99 99 V -> A (in dbSNP:rs2636889). FT /FTId=VAR_050172. FT VARIANT 141 141 G -> R (in dbSNP:rs12685968). FT /FTId=VAR_050173. FT VARIANT 167 167 C -> R (in dbSNP:rs1126777). FT /FTId=VAR_050174. FT VARIANT 174 174 M -> V (in dbSNP:rs2636890). FT /FTId=VAR_050175. FT CONFLICT 32 32 T -> I (in Ref. 4; CAG33211). FT CONFLICT 102 102 E -> D (in Ref. 3; BAG35159). FT CONFLICT 125 125 T -> I (in Ref. 3; BAG35159). FT CONFLICT 162 162 A -> V (in Ref. 3; BAG35159). FT CONFLICT 189 189 Q -> H (in Ref. 3; BAG35159). FT TURN 20 23 FT HELIX 24 26 FT HELIX 33 39 FT STRAND 41 51 FT HELIX 53 60 FT STRAND 62 72 FT TURN 73 76 FT STRAND 77 86 FT STRAND 89 100 FT TURN 101 104 FT STRAND 105 110 FT STRAND 113 120 FT STRAND 127 133 FT TURN 137 139 FT STRAND 141 150 FT HELIX 153 165 FT HELIX 170 172 FT HELIX 178 180 FT HELIX 184 191 SQ SEQUENCE 201 AA; 23603 MW; 49167ABCC22933B9 CRC64; MALSWVLTVL SLLPLLEAQI PLCANLVPVP ITNATLDRIT GKWFYIASAF RNEEYNKSVQ EIQATFFYFT PNKTEDTIFL REYQTRQNQC FYNSSYLNVQ RENGTVSRYE GGREHVAHLL FLRDTKTLMF GSYLDDEKNW GLSFYADKPE TTKEQLGEFY EALDCLCIPR SDVMYTDWKK DKCEPLEKQH EKERKQEEGE S // ID A1AT_HUMAN Reviewed; 418 AA. AC P01009; A6PX14; B2RDQ8; Q0PVP5; Q13672; Q53XB8; Q5U0M1; Q7M4R2; AC Q86U18; Q86U19; Q96BF9; Q96ES1; Q9P1P0; Q9UCE6; Q9UCM3; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 3. DT 09-JUL-2014, entry version 207. DE RecName: Full=Alpha-1-antitrypsin; DE AltName: Full=Alpha-1 protease inhibitor; DE AltName: Full=Alpha-1-antiproteinase; DE AltName: Full=Serpin A1; DE Contains: DE RecName: Full=Short peptide from AAT; DE Short=SPAAT; DE Flags: Precursor; GN Name=SERPINA1; Synonyms=AAT, PI; ORFNames=PRO0684, PRO2209; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=6319097; DOI=10.1089/dna.1983.2.255; RA Bollen A., Herzog A., Cravador A., Herion P., Chuchana P., RA van der Straten A., Loriau R., Jacobs P., van Elsen A.; RT "Cloning and expression in Escherichia coli of full-length RT complementary DNA coding for human alpha 1-antitrypsin."; RL DNA 2:255-264(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6093867; DOI=10.1021/bi00316a003; RA Long G.L., Chandra T., Woo S.L.C., Davie E.W., Kurachi K.; RT "Complete sequence of the cDNA for human alpha 1-antitrypsin and the RT gene for the S variant."; RL Biochemistry 23:4828-4837(1984). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS OF MET-382. RX PubMed=6387509; DOI=10.1038/312077a0; RA Rosenberg S., Barr P.J., Najarian R.C., Hallewell R.A.; RT "Synthesis in yeast of a functional oxidation-resistant mutant of RT human alpha-antitrypsin."; RL Nature 312:77-80(1984). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2985281; DOI=10.1016/S0092-8674(85)80026-X; RA Ciliberto G., Dente L., Cortese R.; RT "Cell-specific expression of a transfected human alpha 1-antitrypsin RT gene."; RL Cell 41:531-540(1985). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION OF VARIANT Z. RX PubMed=3491072; RA Nukiwa T., Satoh K., Brantly M.L., Ogushi F., Fells G.A., Courtney M., RA Crystal R.G.; RT "Identification of a second mutation in the protein-coding sequence of RT the Z type alpha 1-antitrypsin gene."; RL J. Biol. Chem. 261:15989-15994(1986). RN [6] RP ERRATUM. RA Nukiwa T., Satoh K., Brantly M.L., Ogushi F., Fells G.A., Courtney M., RA Crystal R.G.; RL J. Biol. Chem. 262:10412-10412(1987). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ALA-237 AND RP ASP-400. RC TISSUE=Liver; RX PubMed=17650587; RA Shasany A.K., Shukla A.K., Darokar M.P., Saraiya M., Chaturvedi N., RA Tewari L., Khanuja S.P.; RT "An alpha-1 antitrypsin genetic variant from India."; RL Indian J. Biochem. Biophys. 44:176-178(2007). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-172; ALA-237 AND RP LYS-366. RC TISSUE=Lymphocyte; RA Balduyck M., Porchet N., Aubert J.-P., Zerimech F., Douchain F., RA Verchain S.; RT "Characterization of a new variant of alpha1 antitrypsin M Lille RT (p.Gly148Trp)."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., RA Zhou W., Bi J., Zhang Y., Liu M., He F.; RT "Functional prediction of the coding sequences of 32 new genes deduced RT by analysis of cDNA clones from human fetal liver."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). RC TISSUE=Fetal liver, and Placenta; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Synovium; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ALA-237. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon, and Ovary; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67; 196-255 AND 387-418. RX PubMed=6979715; DOI=10.1038/297655a0; RA Leicht M., Long G.L., Chandra T., Kurachi K., Kidd V.J., Mace M. Jr., RA Davie E.W., Woo S.L.C.; RT "Sequence homology and structural comparison between the chromosomal RT human alpha 1-antitrypsin and chicken ovalbumin genes."; RL Nature 297:655-659(1982). RN [15] RP PRELIMINARY PROTEIN SEQUENCE OF 25-418 (ISOFORM 1). RA Chan S.K.; RT "The covalent structure of human alpha1-protease inhibitor."; RL Fed. Proc. 41:1016-1016(1982). RN [16] RP PROTEIN SEQUENCE OF 25-418 (ISOFORM 1). RX PubMed=7045697; DOI=10.1038/298329a0; RA Carrell R.W., Jeppsson J.-O., Laurell C.-B., Brennan S.O., Owen M.C., RA Vaughan L., Boswell D.R.; RT "Structure and variation of human alpha 1-antitrypsin."; RL Nature 298:329-334(1982). RN [17] RP PROTEIN SEQUENCE OF 25-418 (ISOFORM 1), VARIANTS ABERRANT FORM RP 190-GLY--ARG-198 AND VAL-288, AND FUNCTION. RC TISSUE=Blood; RA Sinha A.K., Girish G.V.; RT "Appearance of an aberrant form of alpha-antitrypsin in the RT circulation of chronic cigarette smokers and its effect on the insulin RT induced NO synthesis in blood platelets."; RL Submitted (AUG-2007) to UniProtKB. RN [18] RP PROTEIN SEQUENCE OF 25-39, AND FUNCTION. RC TISSUE=Ascites; RX PubMed=1906855; RA Tanaka N., Sekiya S., Takamizawa H., Kato N., Moriyama Y., RA Fujimura S.; RT "Characterization of a 54 kDa, alpha 1-antitrypsin-like protein RT isolated from ascitic fluid of an endometrial cancer patient."; RL Jpn. J. Cancer Res. 82:693-700(1991). RN [19] RP PROTEIN SEQUENCE OF 30-48 AND 248-257 (ISOFORMS 1/2/3), GLYCOSYLATION RP AT ASN-70; ASN-107 AND ASN-271, STRUCTURE OF CARBOHYDRATES, RP CYSTEINE-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16622833; DOI=10.1002/pmic.200500751; RA Kolarich D., Weber A., Turecek P.L., Schwarz H.P., Altmann F.; RT "Comprehensive glyco-proteomic analysis of human alpha1-antitrypsin RT and its charge isoforms."; RL Proteomics 6:3369-3380(2006). RN [20] RP PROTEIN SEQUENCE OF 47-66. RC TISSUE=Urine; RX PubMed=8323530; DOI=10.1006/bbrc.1993.1731; RA Umekawa T., Kohri K., Amasaki N., Yamate T., Yoshida K., Yamamoto K., RA Suzuki Y., Sinohara H., Kurita T.; RT "Sequencing of a urinary stone protein, identical to alpha-one RT antitrypsin, which lacks 22 amino acids."; RL Biochem. Biophys. Res. Commun. 193:1049-1053(1993). RN [21] RP PROTEIN SEQUENCE OF 50-63 AND 161-178 (ISOFORMS 1/2/3), AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [22] RP NUCLEOTIDE SEQUENCE [MRNA] OF 292-418 (ISOFORM 1). RX PubMed=3876243; DOI=10.1016/0014-5793(85)81056-5; RA Riley J.H., Bathurst I.C., Edbrooke M.R., Carrell R.W., Craig R.K.; RT "Alpha 1-antitrypsin and serum albumin mRNA accumulation in normal, RT acute phase and ZZ human liver."; RL FEBS Lett. 189:361-366(1985). RN [23] RP NUCLEOTIDE SEQUENCE [MRNA] OF 350-418 (ISOFORM 1). RX PubMed=7031661; DOI=10.1073/pnas.78.11.6826; RA Kurachi K., Chandra T., Friezner Degen S.J., White T.T., RA Marchioro T.L., Woo S.L.C., Davie E.W.; RT "Cloning and sequence of cDNA coding for alpha 1-antitrypsin."; RL Proc. Natl. Acad. Sci. U.S.A. 78:6826-6830(1981). RN [24] RP PROTEIN SEQUENCE OF 375-414, IDENTIFICATION OF SPAAT, FUNCTION, AND RP SUBCELLULAR LOCATION. RC TISSUE=Placenta; RX PubMed=1406456; RA Niemann M.A., Narkates A.J., Miller E.J.; RT "Isolation and serine protease inhibitory activity of the 44-residue, RT C-terminal fragment of alpha 1-antitrypsin from human placenta."; RL Matrix 12:233-241(1992). RN [25] RP NUCLEOTIDE SEQUENCE [MRNA] OF 387-418 (ISOFORM 1). RX PubMed=3873938; RA Coutelle C., Speer A., Rogers J., Kalsheker N., Humphries S., RA Williamson R.; RT "Construction and partial characterization of a human liver cDNA RT library."; RL Biomed. Biochim. Acta 44:421-431(1985). RN [26] RP GLYCOSYLATION AT ASN-70 AND ASN-271. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [27] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271. RC TISSUE=Bile; RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200; RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; RT "A proteomic analysis of human bile."; RL Mol. Cell. Proteomics 3:715-728(2004). RN [28] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-271. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [29] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [30] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70. RC TISSUE=Platelet; RX PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200; RA Lewandrowski U., Moebius J., Walter U., Sickmann A.; RT "Elucidation of N-glycosylation sites on human platelet proteins: a RT glycoproteomic approach."; RL Mol. Cell. Proteomics 5:226-233(2006). RN [31] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [32] RP GLYCOSYLATION AT ASN-107 AND ASN-271. RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [33] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-107 AND ASN-271, RP AND STRUCTURE OF CARBOHYDRATES. RC TISSUE=Cerebrospinal fluid; RX PubMed=19838169; DOI=10.1038/nmeth.1392; RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., RA Brinkmalm G., Larson G.; RT "Enrichment of glycopeptides for glycan structure and attachment site RT identification."; RL Nat. Methods 6:809-811(2009). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [35] RP GLYCOSYLATION AT ASN-70 AND ASN-271, STRUCTURE OF CARBOHYDRATES, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.M111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of RT N-and O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 0:0-0(2011). RN [36] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=6332197; DOI=10.1016/0022-2836(84)90298-5; RA Loebermann H., Tokuoka R., Deisenhofer J., Huber R.; RT "Human alpha 1-proteinase inhibitor. Crystal structure analysis of two RT crystal modifications, molecular model and preliminary analysis of the RT implications for function."; RL J. Mol. Biol. 177:531-556(1984). RN [37] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=2785270; DOI=10.1093/protein/2.6.407; RA Engh R., Loebermann H., Schneider M., Wiegand G., Huber R., RA Laurell C.-B.; RT "The S variant of human alpha 1-antitrypsin, structure and RT implications for function and metabolism."; RL Protein Eng. 2:407-415(1989). RN [38] RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 25-418. RX PubMed=8543039; DOI=10.1016/0014-5793(95)01331-8; RA Song H.K., Lee K.N., Kwon K.-S., Yu M.-H., Suh S.W.; RT "Crystal structure of an uncleaved alpha 1-antitrypsin reveals the RT conformation of its inhibitory reactive loop."; RL FEBS Lett. 377:150-154(1995). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418. RX PubMed=8756325; DOI=10.1038/nsb0896-676; RA Elliott P.R., Lomas D.A., Carrell R.W., Abrahams J.P.; RT "Inhibitory conformation of the reactive loop of alpha 1- RT antitrypsin."; RL Nat. Struct. Biol. 3:676-681(1996). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 45-418. RX PubMed=8939743; DOI=10.1016/S0969-2126(96)00126-8; RA Ryu S.-E., Choi H.-J., Kwon K.-S., Lee K.N., Yu M.-H.; RT "The native strains in the hydrophobic core and flexible reactive loop RT of a serine protease inhibitor: crystal structure of an uncleaved RT alpha1-antitrypsin at 2.7 A."; RL Structure 4:1181-1192(1996). RN [41] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-418. RX PubMed=9466920; DOI=10.1006/jmbi.1997.1458; RA Elliott P.R., Abrahams J.P., Lomas D.A.; RT "Wild-type alpha 1-antitrypsin is in the canonical inhibitory RT conformation."; RL J. Mol. Biol. 275:419-425(1998). RN [42] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 48-418 IN COMPLEX WITH BOVINE RP TRYPSIN. RX PubMed=11057674; DOI=10.1038/35038119; RA Huntington J.A., Read R.J., Carrell R.W.; RT "Structure of a serpin-protease complex shows inhibition by RT deformation."; RL Nature 407:923-926(2000). RN [43] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 44-418. RX PubMed=10716194; DOI=10.1110/ps.9.2.417; RA Dunstone M.A., Dai W., Whisstock J.C., Rossjohn J., Pike R.N., RA Feil S.C., Le Bonniec B.F., Parker M.W., Bottomley S.P.; RT "Cleaved antitrypsin polymers at atomic resolution."; RL Protein Sci. 9:417-420(2000). RN [44] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=10933492; DOI=10.1110/ps.9.7.1274; RA Elliott P.R., Pei X.Y., Dafforn T.R., Lomas D.A.; RT "Topography of a 2.0 A structure of alpha1-antitrypsin reveals targets RT for rational drug design to prevent conformational disease."; RL Protein Sci. 9:1274-1281(2000). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-418. RX PubMed=11178897; DOI=10.1006/jmbi.2000.4357; RA Kim S.-J., Woo J.-R., Seo E.J., Yu M.-H., Ryu S.-E.; RT "A 2.1 A resolution structure of an uncleaved alpha(1)-antitrypsin RT shows variability of the reactive center and other loops."; RL J. Mol. Biol. 306:109-119(2001). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-418. RX PubMed=12244055; DOI=10.1074/jbc.M207682200; RA Im H., Woo M.-S., Hwang K.Y., Yu M.-H.; RT "Interactions causing the kinetic trap in serpin protein folding."; RL J. Biol. Chem. 277:46347-46354(2002). RN [47] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-418 OF VARIANT PITTSBURGH RP ARG-382. RX PubMed=12860985; DOI=10.1074/jbc.M305195200; RA Dementiev A., Simonovic M., Volz K., Gettins P.G.; RT "Canonical inhibitor-like interactions explain reactivity of alpha1- RT proteinase inhibitor Pittsburgh and antithrombin with proteinases."; RL J. Biol. Chem. 278:37881-37887(2003). RN [48] RP REVIEW. RX PubMed=2669992; DOI=10.1007/BF01115992; RA Kalsheker N.; RT "Alpha 1-antitrypsin: structure, function and molecular biology of the RT gene."; RL Biosci. Rep. 9:129-138(1989). RN [49] RP REVIEW. RX PubMed=1859394; DOI=10.1002/bies.950130404; RA Wu Y., Foreman R.C.; RT "The molecular genetics of alpha 1 antitrypsin deficiency."; RL Bioessays 13:163-169(1991). RN [50] RP CHARACTERIZATION OF VARIANT M2. RX PubMed=2901226; RA Nukiwa T., Brantly M.L., Ogushi F., Fells G.A., Crystal R.G.; RT "Characterization of the gene and protein of the common alpha 1- RT antitrypsin normal M2 allele."; RL Am. J. Hum. Genet. 43:322-330(1988). RN [51] RP VARIANT M3 ASP-400. RX PubMed=2394452; DOI=10.1007/BF00206766; RA Graham A., Hayes K., Weidinger S., Newton C.R., Markham A.F., RA Kalsheker N.A.; RT "Characterisation of the alpha-1-antitrypsin M3 gene, a normal RT variant."; RL Hum. Genet. 85:381-382(1990). RN [52] RP VARIANT F CYS-247. RX PubMed=2035534; RA Okayama H., Brantly M., Holmes M., Crystal R.G.; RT "Characterization of the molecular basis of the alpha 1-antitrypsin F RT allele."; RL Am. J. Hum. Genet. 48:1154-1158(1991). RN [53] RP VARIANT M-HEERLEN LEU-393. RX PubMed=2784123; DOI=10.1007/BF00279001; RA Hofker M.H., Nukiwa T., van Paassen H.M.B., Nelen M., Kramps J.A., RA Klasen E.C., Frants R.R., Crystal R.G.; RT "A Pro-->Leu substitution in codon 369 of the alpha-1-antitrypsin RT deficiency variant PI M-Heerlen."; RL Hum. Genet. 81:264-268(1989). RN [54] RP VARIANT M-MALTON PHE-75 DEL. RX PubMed=2786335; RA Fraizer G.C., Harrold T.R., Hofker M.H., Cox D.W.; RT "In-frame single codon deletion in the M-Malton deficiency allele of RT alpha 1-antitrypsin."; RL Am. J. Hum. Genet. 44:894-902(1989). RN [55] RP VARIANT M-MINERAL SPRINGS GLU-91. RX PubMed=1967187; RA Curiel D.T., Vogelmeier C., Hubbard R.C., Stier L.E., Crystal R.G.; RT "Molecular basis of alpha 1-antitrypsin deficiency and emphysema RT associated with the alpha 1-antitrypsin M-Mineral springs allele."; RL Mol. Cell. Biol. 10:47-56(1990). RN [56] RP VARIANT M-NICHINAN PHE-75 DEL. RX PubMed=2309708; RA Matsunaga E., Shiokawa S., Nakamura H., Maruyama T., Tsuda K., RA Fukumaki Y.; RT "Molecular analysis of the gene of the alpha 1-antitrypsin deficiency RT variant, M-Nichinan."; RL Am. J. Hum. Genet. 46:602-612(1990). RN [57] RP VARIANT M-PROCIDA PRO-65. RX PubMed=3262617; RA Takahashi H., Nukiwa T., Satoh K., Ogushi F., Brantly M., Fells G., RA Stier L., Courtney M., Crystal R.G.; RT "Characterization of the gene and protein of the alpha 1-antitrypsin RT 'deficiency' allele M-Procida."; RL J. Biol. Chem. 263:15528-15534(1988). RN [58] RP VARIANT P-DUARTE VAL-280. RX PubMed=8364590; DOI=10.1002/humu.1380020311; RA Hildesheim J., Kinsley G., Bissell M., Pierce J., Brantly M.; RT "Genetic diversity from a limited repertoire of mutations on different RT common allelic backgrounds: alpha 1-antitrypsin deficiency variant P- RT Duarte."; RL Hum. Mutat. 2:221-228(1993). RN [59] RP INVOLVEMENT OF VARIANT PITTSBURGH ARG-382 IN BLEEDING DIATHESIS. RX PubMed=6604220; DOI=10.1056/NEJM198309223091203; RA Owen M.C., Brennan S.O., Lewis J.H., Carrell R.W.; RT "Mutation of antitrypsin to antithrombin. Alpha 1-antitrypsin RT Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder."; RL N. Engl. J. Med. 309:694-698(1983). RN [60] RP INVOLVEMENT IN A1ATD, AND VARIANT S-IIYAMA PHE-77. RX PubMed=1905728; RA Seyama K., Nukiwa T., Takabe K., Takahashi H., Miyake K., Kira S.; RT "Siiyama (serine 53 (TCC) to phenylalanine 53 (TTC)). A new alpha 1- RT antitrypsin-deficient variant with mutation on a predicted conserved RT residue of the serpin backbone."; RL J. Biol. Chem. 266:12627-12632(1991). RN [61] RP VARIANT V-MUNICH ALA-26. RX PubMed=2316526; RA Holmes M.D., Brantly M.L., Curiel D.T., Weidinger S., Crystal R.G.; RT "Characterization of the normal alpha 1-antitrypsin allele V-Munich: a RT variant associated with a unique protein isoelectric focusing RT pattern."; RL Am. J. Hum. Genet. 46:810-816(1990). RN [62] RP INVOLVEMENT IN A1ATD, AND VARIANT W-BETHESDA THR-360. RX PubMed=2390072; DOI=10.1016/0006-291X(90)90493-7; RA Holmes M.D., Brantly M.L., Fells G.A., Crystal R.G.; RT "Alpha 1-antitrypsin W-Bethesda: molecular basis of an unusual alpha RT 1-antitrypsin deficiency variant."; RL Biochem. Biophys. Res. Commun. 170:1013-1020(1990). RN [63] RP VARIANT Z-AUGSBURG LYS-366. RX PubMed=2339709; RA Faber J.-P., Weidinger S., Olek K.; RT "Sequence data of the rare deficient alpha 1-antitrypsin variant PI RT Zaugsburg."; RL Am. J. Hum. Genet. 46:1158-1162(1990). RN [64] RP INVOLVEMENT IN A1ATD, AND VARIANTS Z-WREXHAM LEU-4 AND Q0-NEWPORT RP SER-139. RX PubMed=2227940; DOI=10.1007/BF00194233; RA Graham A., Kalsheker N.A., Bamforth F.J., Newton C.R., Markham A.F.; RT "Molecular characterisation of two alpha-1-antitrypsin deficiency RT variants: proteinase inhibitor (Pi) Null(Newport) (Gly115-->Ser) and RT (Pi) Z Wrexham (Ser-19-->Leu)."; RL Hum. Genet. 85:537-540(1990). RN [65] RP VARIANTS P-CARDIFF VAL-280; I CYS-63 AND M-MALTON PHE-75 DEL. RX PubMed=2606478; DOI=10.1007/BF00210671; RA Graham A., Kalsheker N.A., Newton C.R., Bamforth F.J., Powell S.J., RA Markham A.F.; RT "Molecular characterisation of three alpha-1-antitrypsin deficiency RT variants: proteinase inhibitor (Pi) nullcardiff (Asp256-->Val); PiM- RT Malton (Phe51-->deletion) and PiI (Arg39-->Cys)."; RL Hum. Genet. 84:55-58(1989). RN [66] RP VARIANT QO-LUDWIGSHAFEN ASN-116. RX PubMed=2254451; DOI=10.1172/JCI114919; RA Fraizer G.C., Siewertsen M.A., Hofker M.H., Brubacher M.G., Cox D.W.; RT "A null deficiency allele of alpha 1-antitrypsin, QO-Ludwigshafen, RT with altered tertiary structure."; RL J. Clin. Invest. 86:1878-1884(1990). RN [67] RP VARIANTS. RX PubMed=7977369; RA Faber J.-P., Poller W., Weidinger S., Kirchgesser M., Schwaab R., RA Bidlingmaier F., Olek K.; RT "Identification and DNA sequence analysis of 15 new alpha 1- RT antitrypsin variants, including two PI*Q0 alleles and one deficient RT PI*M allele."; RL Am. J. Hum. Genet. 55:1113-1121(1994). RN [68] RP VARIANT Z-BRISTOL MET-109. RX PubMed=9459000; DOI=10.1017/S0003480097006404; RA Lovegrove J.U., Jeremiah S., Gillett G.T., Temple I.K., Povey S., RA Whitehouse D.B.; RT "A new alpha 1-antitrypsin mutation, Thr-Met 85, (PI ZBristol) RT associated with novel electrophoretic properties."; RL Ann. Hum. Genet. 61:385-391(1997). RN [69] RP VARIANTS Y-BARCELONA VAL-280 AND HIS-415. RX PubMed=10651487; RA Jardi R., Rodriguez F., Miravitlles M., Vidal R., Cotrina M., Quer J., RA Pascual C., Weidinger S.; RT "Identification and molecular characterization of the new alpha-1- RT antitrypsin deficient allele PI YBarcelona (Asp256Val and RT Pro391His)."; RL Hum. Mutat. 12:213-213(1998). RN [70] RP VARIANT SAO TOME HIS-386. RA Seixas S., Trovoada M.J., Santos M.T., Rocha J.; RT "A novel alpha-1-antitrypsin P362H variant found in a population RT sample from Sao Tome e Principe (Gulf of Guinea, West Africa)."; RL Hum. Mutat. 13:414-414(1999). RN [71] RP VARIANT BASQUE ARG-305 DEL. RX PubMed=10612848; RX DOI=10.1002/(SICI)1098-1004(200001)15:1<121::AID-HUMU37>3.0.CO;2-U; RA Seixas S., Garcia O., Amorim A., Rocha J.; RT "A novel alpha-1-antitrypsin r281del variant found in a population RT sample from the Basque country."; RL Hum. Mutat. 15:121-122(2000). RN [72] RP VARIANTS Z ALA-237 AND LYS-366, VARIANT S VAL-288, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND INTERACTION WITH CANX RP AND PDIA3. RX PubMed=23826168; DOI=10.1371/journal.pone.0066889; RA Marques P.I., Ferreira Z., Martins M., Figueiredo J., Silva D.I., RA Castro P., Morales-Hojas R., Simoes-Correia J., Seixas S.; RT "SERPINA2 is a novel gene with a divergent function from SERPINA1."; RL PLoS ONE 8:E66889-E66889(2013). CC -!- FUNCTION: Inhibitor of serine proteases. Its primary target is CC elastase, but it also has a moderate affinity for plasmin and CC thrombin. Irreversibly inhibits trypsin, chymotrypsin and CC plasminogen activator. The aberrant form inhibits insulin-induced CC NO synthesis in platelets, decreases coagulation time and has CC proteolytic activity against insulin and plasmin. CC -!- FUNCTION: Short peptide from AAT: reversible chymotrypsin CC inhibitor. It also inhibits elastase, but not trypsin. Its major CC physiological function is the protection of the lower respiratory CC tract against proteolytic destruction by human leukocyte elastase CC (HLE). CC -!- SUBUNIT: The variants S and Z interact with CANX AND PDIA3. CC -!- INTERACTION: CC Self; NbExp=5; IntAct=EBI-986224, EBI-986224; CC P00760:- (xeno); NbExp=5; IntAct=EBI-986224, EBI-986385; CC P00772:CELA1 (xeno); NbExp=2; IntAct=EBI-986224, EBI-986248; CC P71213:espB (xeno); NbExp=3; IntAct=EBI-986224, EBI-2615322; CC P43307:SSR1; NbExp=4; IntAct=EBI-986224, EBI-714168; CC -!- SUBCELLULAR LOCATION: Secreted. Endoplasmic reticulum. Note=The S CC and Z allele are not secreted effectively and accumulate CC intracellularly in the endoplasmic reticulum. CC -!- SUBCELLULAR LOCATION: Short peptide from AAT: Secreted, CC extracellular space, extracellular matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P01009-1; Sequence=Displayed; CC Name=2; CC IsoId=P01009-2; Sequence=VSP_028889; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=P01009-3; Sequence=VSP_028890; CC Note=No experimental confirmation available. May be produced at CC very low levels due to a premature stop codon in the mRNA, CC leading to nonsense-mediated mRNA decay; CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in leukocytes and CC plasma. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable. CC -!- PTM: N-glycosylated. Differential glycosylation produces a number CC of isoforms. N-linked glycan at Asn-107 is alternatively di- CC antennary, tri-antennary or tetra-antennary. The glycan at Asn-70 CC is di-antennary with trace amounts of tri-antennary. Glycan at CC Asn-271 is exclusively di-antennary. Structure of glycans at Asn- CC 70 and Asn-271 is Hex5HexNAc4. The structure of the antennae is CC Neu5Ac(alpha1-6)Gal(beta1-4)GlcNAc attached to the core structure CC Man(alpha1-6)[Man(alpha1-3)]Man(beta1-4)GlcNAc(beta1-4)GlcNAc. CC Some antennae are fucosylated, which forms a Lewis-X determinant. CC -!- PTM: Proteolytic processing may yield the truncated form that CC ranges from Asp-30 to Lys-418. CC -!- POLYMORPHISM: The sequence shown is that of the M1V allele which CC is the most common form of PI (44 to 49%). Other frequent alleles CC are: M1A 20 to 23%; M2 10 to 11%; M3 14 to 19%. CC -!- DISEASE: Alpha-1-antitrypsin deficiency (A1ATD) [MIM:613490]: A CC disorder whose most common manifestation is emphysema, which CC becomes evident by the third to fourth decade. A less common CC manifestation of the deficiency is liver disease, which occurs in CC children and adults, and may result in cirrhosis and liver CC failure. Environmental factors, particularly cigarette smoking, CC greatly increase the risk of emphysema at an earlier age. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- MISCELLANEOUS: The aberrant form is found in the plasma of chronic CC smokers, and persists after smoking is ceased. It can still be CC found ten years after smoking has ceased. CC -!- SIMILARITY: Belongs to the serpin family. CC -!- SEQUENCE CAUTION: CC Sequence=CAD62334.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=CAD62585.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-1 antitrypsin entry; CC URL="http://en.wikipedia.org/wiki/Alpha_1-antitrypsin"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K01396; AAB59375.1; -; mRNA. DR EMBL; K02212; AAB59495.1; -; Genomic_DNA. DR EMBL; X01683; CAA25838.1; -; mRNA. DR EMBL; M11465; AAA51546.1; -; mRNA. DR EMBL; J02619; AAA51547.1; -; Genomic_DNA. DR EMBL; DQ682455; ABG73380.1; -; mRNA. DR EMBL; AM048838; CAJ15161.1; -; Genomic_DNA. DR EMBL; AF113676; AAF29581.1; -; mRNA. DR EMBL; AF130068; AAG35496.1; -; mRNA. DR EMBL; BX161449; CAD61914.1; -; mRNA. DR EMBL; BX247968; CAD62306.1; -; mRNA. DR EMBL; BX248002; CAD62334.1; ALT_INIT; mRNA. DR EMBL; BX248257; CAD62585.1; ALT_INIT; mRNA. DR EMBL; AK315637; BAG38005.1; -; mRNA. DR EMBL; BT019455; AAV38262.1; -; mRNA. DR EMBL; BC011991; AAH11991.1; -; mRNA. DR EMBL; BC015642; AAH15642.1; -; mRNA. DR EMBL; J00064; AAB59369.1; -; Genomic_DNA. DR EMBL; J00066; AAB59370.1; -; Genomic_DNA. DR EMBL; J00065; AAB59370.1; JOINED; Genomic_DNA. DR EMBL; J00067; AAB59371.1; -; Genomic_DNA. DR EMBL; X02920; CAA26677.1; -; mRNA. DR EMBL; V00496; CAA23755.1; -; mRNA. DR EMBL; M26123; AAA51545.1; -; mRNA. DR CCDS; CCDS9925.1; -. [P01009-1] DR PIR; A21853; ITHU. DR PIR; A61391; A61391. DR RefSeq; NP_000286.3; NM_000295.4. [P01009-1] DR RefSeq; NP_001002235.1; NM_001002235.2. [P01009-1] DR RefSeq; NP_001002236.1; NM_001002236.2. [P01009-1] DR RefSeq; NP_001121172.1; NM_001127700.1. [P01009-1] DR RefSeq; NP_001121173.1; NM_001127701.1. [P01009-1] DR RefSeq; NP_001121174.1; NM_001127702.1. [P01009-1] DR RefSeq; NP_001121175.1; NM_001127703.1. [P01009-1] DR RefSeq; NP_001121176.1; NM_001127704.1. [P01009-1] DR RefSeq; NP_001121177.1; NM_001127705.1. [P01009-1] DR RefSeq; NP_001121178.1; NM_001127706.1. [P01009-1] DR RefSeq; NP_001121179.1; NM_001127707.1. [P01009-1] DR UniGene; Hs.525557; -. DR PDB; 1ATU; X-ray; 2.70 A; A=45-418. DR PDB; 1D5S; X-ray; 3.00 A; A=44-377, B=378-418. DR PDB; 1EZX; X-ray; 2.60 A; A=48-382, B=383-418. DR PDB; 1HP7; X-ray; 2.10 A; A=25-418. DR PDB; 1IZ2; X-ray; 2.20 A; A=25-418. DR PDB; 1KCT; X-ray; 3.46 A; A=25-418. DR PDB; 1OO8; X-ray; 2.65 A; A=26-418. DR PDB; 1OPH; X-ray; 2.30 A; A=26-418. DR PDB; 1PSI; X-ray; 2.92 A; A=26-418. DR PDB; 1QLP; X-ray; 2.00 A; A=26-418. DR PDB; 1QMB; X-ray; 2.60 A; A=49-376, B=377-418. DR PDB; 2D26; X-ray; 3.30 A; A=25-382, B=383-418. DR PDB; 2QUG; X-ray; 2.00 A; A=25-418. DR PDB; 3CWL; X-ray; 2.44 A; A=25-418. DR PDB; 3CWM; X-ray; 2.51 A; A=25-418. DR PDB; 3DRM; X-ray; 2.20 A; A=26-418. DR PDB; 3DRU; X-ray; 3.20 A; A/B/C=26-418. DR PDB; 3NDD; X-ray; 1.50 A; A=46-382, B=383-418. DR PDB; 3NDF; X-ray; 2.70 A; A=46-382, B=383-418. DR PDB; 3NE4; X-ray; 1.81 A; A=48-418. DR PDB; 3T1P; X-ray; 3.90 A; A=48-418. DR PDB; 7API; X-ray; 3.00 A; A=36-382, B=383-418. DR PDB; 8API; X-ray; 3.10 A; A=36-382, B=383-418. DR PDB; 9API; X-ray; 3.00 A; A=36-382, B=383-418. DR PDBsum; 1ATU; -. DR PDBsum; 1D5S; -. DR PDBsum; 1EZX; -. DR PDBsum; 1HP7; -. DR PDBsum; 1IZ2; -. DR PDBsum; 1KCT; -. DR PDBsum; 1OO8; -. DR PDBsum; 1OPH; -. DR PDBsum; 1PSI; -. DR PDBsum; 1QLP; -. DR PDBsum; 1QMB; -. DR PDBsum; 2D26; -. DR PDBsum; 2QUG; -. DR PDBsum; 3CWL; -. DR PDBsum; 3CWM; -. DR PDBsum; 3DRM; -. DR PDBsum; 3DRU; -. DR PDBsum; 3NDD; -. DR PDBsum; 3NDF; -. DR PDBsum; 3NE4; -. DR PDBsum; 3T1P; -. DR PDBsum; 7API; -. DR PDBsum; 8API; -. DR PDBsum; 9API; -. DR ProteinModelPortal; P01009; -. DR SMR; P01009; 48-417. DR BioGrid; 111283; 22. DR DIP; DIP-35493N; -. DR IntAct; P01009; 19. DR MINT; MINT-365327; -. DR DrugBank; DB00058; Alpha-1-proteinase inhibitor. DR MEROPS; I04.001; -. DR PhosphoSite; P01009; -. DR UniCarbKB; P01009; -. DR DMDM; 1703025; -. DR DOSAC-COBS-2DPAGE; P01009; -. DR OGP; P01009; -. DR REPRODUCTION-2DPAGE; IPI00553177; -. DR REPRODUCTION-2DPAGE; P01009; -. DR SWISS-2DPAGE; P01009; -. DR UCD-2DPAGE; P01009; -. DR MaxQB; P01009; -. DR PaxDb; P01009; -. DR PRIDE; P01009; -. DR DNASU; 5265; -. DR Ensembl; ENST00000355814; ENSP00000348068; ENSG00000197249. [P01009-1] DR Ensembl; ENST00000393087; ENSP00000376802; ENSG00000197249. [P01009-1] DR Ensembl; ENST00000393088; ENSP00000376803; ENSG00000197249. [P01009-1] DR Ensembl; ENST00000402629; ENSP00000386094; ENSG00000197249. [P01009-2] DR Ensembl; ENST00000404814; ENSP00000385960; ENSG00000197249. [P01009-1] DR Ensembl; ENST00000437397; ENSP00000408474; ENSG00000197249. [P01009-1] DR Ensembl; ENST00000440909; ENSP00000390299; ENSG00000197249. [P01009-1] DR Ensembl; ENST00000448921; ENSP00000416066; ENSG00000197249. [P01009-1] DR Ensembl; ENST00000449399; ENSP00000416354; ENSG00000197249. [P01009-1] DR Ensembl; ENST00000489769; ENSP00000451525; ENSG00000197249. [P01009-3] DR GeneID; 5265; -. DR KEGG; hsa:5265; -. DR UCSC; uc001ycx.4; human. [P01009-1] DR UCSC; uc001yda.1; human. [P01009-2] DR CTD; 5265; -. DR GeneCards; GC14M094843; -. DR GeneReviews; SERPINA1; -. DR HGNC; HGNC:8941; SERPINA1. DR HPA; CAB013211; -. DR HPA; CAB016648; -. DR HPA; HPA000927; -. DR HPA; HPA001292; -. DR MIM; 107400; gene. DR MIM; 613490; phenotype. DR neXtProt; NX_P01009; -. DR Orphanet; 60; Alpha-1-antitrypsin deficiency. DR Orphanet; 178396; Hemorrhagic disease due to alpha-1-antitrypsin Pittsburgh mutation. DR PharmGKB; PA35509; -. DR eggNOG; COG4826; -. DR HOVERGEN; HBG005957; -. DR InParanoid; P01009; -. DR KO; K03984; -. DR OMA; VVNPTQK; -. DR OrthoDB; EOG7QC7W9; -. DR PhylomeDB; P01009; -. DR TreeFam; TF343201; -. DR Reactome; REACT_604; Hemostasis. DR ChiTaRS; SERPINA1; human. DR EvolutionaryTrace; P01009; -. DR GeneWiki; Alpha_1-antitrypsin; -. DR GenomeRNAi; 5265; -. DR NextBio; 20336; -. DR PMAP-CutDB; P01009; -. DR PRO; PR:P01009; -. DR ArrayExpress; P01009; -. DR Bgee; P01009; -. DR Genevestigator; P01009; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IMP:UniProtKB. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0002020; F:protease binding; IPI:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:RefGenome. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome. DR GO; GO:0030162; P:regulation of proteolysis; IBA:RefGenome. DR GO; GO:0046687; P:response to chromate; IEA:Ensembl. DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0010288; P:response to lead ion; IEA:Ensembl. DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0033986; P:response to methanol; IEA:Ensembl. DR GO; GO:0034014; P:response to triglyceride; IEA:Ensembl. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. DR PANTHER; PTHR11461; PTHR11461; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; SSF56574; 1. DR PROSITE; PS00284; SERPIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Alternative splicing; Blood coagulation; KW Complete proteome; Direct protein sequencing; Endoplasmic reticulum; KW Extracellular matrix; Glycoprotein; Hemostasis; Polymorphism; KW Protease inhibitor; Reference proteome; Secreted; KW Serine protease inhibitor; Signal. FT SIGNAL 1 24 FT CHAIN 25 418 Alpha-1-antitrypsin. FT /FTId=PRO_0000032377. FT PEPTIDE 375 418 Short peptide from AAT. FT /FTId=PRO_0000364030. FT REGION 368 392 RCL. FT SITE 382 383 Reactive bond. FT MOD_RES 256 256 S-cysteinyl cysteine. FT CARBOHYD 70 70 N-linked (GlcNAc...) (complex). FT CARBOHYD 107 107 N-linked (GlcNAc...) (complex). FT CARBOHYD 271 271 N-linked (GlcNAc...) (complex). FT VAR_SEQ 307 418 Missing (in isoform 3). FT /FTId=VSP_028890. FT VAR_SEQ 356 418 AVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVF FT LMIEQNTKSPLFMGKVVNPTQK -> VRSP (in FT isoform 2). FT /FTId=VSP_028889. FT VARIANT 4 4 S -> L (in Z-Wrexham). FT /FTId=VAR_006978. FT VARIANT 26 26 D -> A (in V-Munich). FT /FTId=VAR_006979. FT VARIANT 37 37 T -> A (in dbSNP:rs11558262). FT /FTId=VAR_051938. FT VARIANT 58 58 A -> T (in M5-Karlsruhe). FT /FTId=VAR_006980. FT VARIANT 63 63 R -> C (in I; dbSNP:rs28931570). FT /FTId=VAR_006981. FT VARIANT 65 65 L -> P (in M-Procida; dbSNP:rs28931569). FT /FTId=VAR_006982. FT VARIANT 69 69 S -> F (in M6-Bonn). FT /FTId=VAR_006983. FT VARIANT 75 75 Missing (in M-Malton, M-Nichinan and M- FT Palermo; associated with very low serum FT levels of AAT; homozygosity for allele M- FT Malton may be associated with a risk for FT chronic emphysema or infantile liver FT cirrhosis). FT /FTId=VAR_006984. FT VARIANT 77 77 S -> F (in S-Iiyama; dbSNP:rs55819880). FT /FTId=VAR_006985. FT VARIANT 84 84 A -> T (in M6-Passau). FT /FTId=VAR_006986. FT VARIANT 91 91 G -> E (in M-Mineral springs; causes FT reduced AAT secretion; dbSNP:rs28931568). FT /FTId=VAR_006987. FT VARIANT 92 92 T -> I (in QO-Lisbon; deficient AAT with FT very low serum levels). FT /FTId=VAR_006988. FT VARIANT 109 109 T -> M (in Z-Bristol; deficient AA; FT disrupts the N-glycosylation site N-107). FT /FTId=VAR_011620. FT VARIANT 112 112 P -> T (in M5-Berlin). FT /FTId=VAR_006989. FT VARIANT 116 116 I -> N (in QO-Ludwigshafen; FT dbSNP:rs28931572). FT /FTId=VAR_006990. FT VARIANT 125 125 R -> H (in M2; associated with D-400; FT dbSNP:rs709932). FT /FTId=VAR_006991. FT VARIANT 139 139 G -> S (in QO-Newport; dbSNP:rs11558261). FT /FTId=VAR_006992. FT VARIANT 172 172 G -> R (in V and M-Nichinan). FT /FTId=VAR_006993. FT VARIANT 172 172 G -> W (in M2-Obernburg). FT /FTId=VAR_006994. FT VARIANT 180 180 Q -> E (in L-Frankfurt). FT /FTId=VAR_006995. FT VARIANT 190 198 QGKIVDLVK -> GFQNAILVR (in Aberrant FT form). FT /FTId=VAR_036746. FT VARIANT 228 228 E -> K (in X). FT /FTId=VAR_006996. FT VARIANT 237 237 V -> A (in M1A and Z; associated with K- FT 366 in Z; dbSNP:rs6647). FT /FTId=VAR_006997. FT VARIANT 247 247 R -> C (in F; dbSNP:rs28929470). FT /FTId=VAR_006998. FT VARIANT 280 280 D -> V (in P-Duarte/P-Cardiff/P-Lowell; FT associated with H-415 in Y-Barcelona; FT dbSNP:rs28929472). FT /FTId=VAR_006999. FT VARIANT 288 288 E -> V (in S and T; dbSNP:rs17580). FT /FTId=VAR_007000. FT VARIANT 305 305 Missing (in Basque). FT /FTId=VAR_009216. FT VARIANT 354 354 S -> F (in S-Munich). FT /FTId=VAR_007001. FT VARIANT 360 360 A -> T (in W-Bethesda; dbSNP:rs1802959). FT /FTId=VAR_007002. FT VARIANT 365 365 D -> N (in P-St.Albans/P-Donauwoerth). FT /FTId=VAR_007003. FT VARIANT 366 366 E -> K (in Z/Z-Augsburg/Z-Tun; associated FT with A-237 in Z; dbSNP:rs28929474). FT /FTId=VAR_007004. FT VARIANT 382 382 M -> R (in Pittsburgh; has antithrombin FT activity; causes fatal bleeding FT diathesis). FT /FTId=VAR_007005. FT VARIANT 386 386 P -> H (in Sao Tome). FT /FTId=VAR_007006. FT VARIANT 386 386 P -> T (in L-Offenbach). FT /FTId=VAR_007007. FT VARIANT 387 387 E -> K (in Christchurch; FT dbSNP:rs121912712). FT /FTId=VAR_007008. FT VARIANT 393 393 P -> L (in M-Heerlen). FT /FTId=VAR_007009. FT VARIANT 400 400 E -> D (in M2 and M3; associated with H- FT 125 in M2; dbSNP:rs1303). FT /FTId=VAR_007010. FT VARIANT 415 415 P -> H (in Y-Barcelona; associated with FT V-280). FT /FTId=VAR_007011. FT MUTAGEN 382 382 M->V: Oxidation-resistant inhibitor of FT therapeutic importance. FT CONFLICT 12 12 Missing (in Ref. 4; AAA51546). FT CONFLICT 23 23 L -> P (in Ref. 11; BAG38005). FT CONFLICT 26 26 D -> H (in Ref. 18; AA sequence). FT CONFLICT 39 39 H -> L (in Ref. 18; AA sequence). FT CONFLICT 61 61 L -> P (in Ref. 9; AAF29581). FT CONFLICT 96 96 T -> A (in Ref. 7; ABG73380). FT CONFLICT 139 140 GN -> DG (in Ref. 1; AAB59375). FT CONFLICT 174 174 T -> H (in Ref. 4; AAA51546). FT CONFLICT 229 229 E -> D (in Ref. 4; AAA51546). FT CONFLICT 273 273 T -> N (in Ref. 1; AAB59375). FT CONFLICT 280 280 D -> G (in Ref. 7; ABG73380). FT CONFLICT 326 326 V -> I (in Ref. 3; CAA25838). FT CONFLICT 410 410 G -> L (in Ref. 24; AA sequence). FT CONFLICT 414 414 N -> S (in Ref. 24; AA sequence). FT TURN 48 50 FT HELIX 51 68 FT STRAND 70 72 FT STRAND 74 76 FT HELIX 78 89 FT HELIX 94 103 FT TURN 108 110 FT HELIX 113 127 FT STRAND 135 145 FT STRAND 146 148 FT HELIX 152 162 FT STRAND 164 169 FT STRAND 171 173 FT HELIX 174 188 FT TURN 189 191 FT STRAND 206 220 FT HELIX 224 226 FT STRAND 228 235 FT STRAND 238 256 FT TURN 257 260 FT STRAND 261 279 FT STRAND 280 282 FT HELIX 284 290 FT HELIX 293 301 FT STRAND 306 313 FT STRAND 315 322 FT HELIX 324 329 FT HELIX 334 336 FT TURN 337 339 FT TURN 343 345 FT STRAND 347 349 FT STRAND 351 364 FT STRAND 366 381 FT STRAND 387 389 FT STRAND 394 400 FT TURN 401 403 FT STRAND 406 414 SQ SEQUENCE 418 AA; 46737 MW; 7016555F273B7F16 CRC64; MPSSVSWGIL LLAGLCCLVP VSLAEDPQGD AAQKTDTSHH DQDHPTFNKI TPNLAEFAFS LYRQLAHQSN STNIFFSPVS IATAFAMLSL GTKADTHDEI LEGLNFNLTE IPEAQIHEGF QELLRTLNQP DSQLQLTTGN GLFLSEGLKL VDKFLEDVKK LYHSEAFTVN FGDTEEAKKQ INDYVEKGTQ GKIVDLVKEL DRDTVFALVN YIFFKGKWER PFEVKDTEEE DFHVDQVTTV KVPMMKRLGM FNIQHCKKLS SWVLLMKYLG NATAIFFLPD EGKLQHLENE LTHDIITKFL ENEDRRSASL HLPKLSITGT YDLKSVLGQL GITKVFSNGA DLSGVTEEAP LKLSKAVHKA VLTIDEKGTE AAGAMFLEAI PMSIPPEVKF NKPFVFLMIE QNTKSPLFMG KVVNPTQK // ID A2AP_HUMAN Reviewed; 491 AA. AC P08697; B4E1B7; Q8N5U7; Q9UCG2; Q9UCG3; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 3. DT 09-JUL-2014, entry version 161. DE RecName: Full=Alpha-2-antiplasmin; DE Short=Alpha-2-AP; DE AltName: Full=Alpha-2-plasmin inhibitor; DE Short=Alpha-2-PI; DE AltName: Full=Serpin F2; DE Flags: Precursor; GN Name=SERPINF2; Synonyms=AAP, PLI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=2830248; RA Tone M., Kikuno R., Kume-Iwaki A., Hashimoto-Gotoh T.; RT "Structure of human alpha 2-plasmin inhibitor deduced from the cDNA RT sequence."; RL J. Biochem. 102:1033-1041(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM RP 1). RX PubMed=3166140; DOI=10.1073/pnas.85.18.6836; RA Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.; RT "Organization of the human alpha 2-plasmin inhibitor gene."; RL Proc. Natl. Acad. Sci. U.S.A. 85:6836-6840(1988). RN [3] RP ERRATUM. RA Hirosawa S., Nakamura Y., Miura O., Sumi Y., Aoki N.; RL Proc. Natl. Acad. Sci. U.S.A. 86:1612-1613(1989). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Liver; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-2. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-491 (ISOFORM 1). RX PubMed=2433286; RA Holmes W.E., Nelles L., Lijnen H.R., Collen D.; RT "Primary structure of human alpha 2-antiplasmin, a serine protease RT inhibitor (serpin)."; RL J. Biol. Chem. 262:1659-1664(1987). RN [8] RP PROTEIN SEQUENCE OF 28-58. RC TISSUE=Plasma; RX PubMed=8484741; RA Bangert K., Johnsen A.H., Christensen U., Thorsen S.; RT "Different N-terminal forms of alpha 2-plasmin inhibitor in human RT plasma."; RL Biochem. J. 291:623-625(1993). RN [9] RP PROTEIN SEQUENCE OF 28-52. RC TISSUE=Plasma; RX PubMed=1385210; DOI=10.1016/0014-5793(92)81419-M; RA Christensen S., Sottrup-Jensen L.; RT "Bovine alpha 2-antiplasmin. N-terminal and reactive site sequence."; RL FEBS Lett. 312:100-104(1992). RN [10] RP PROTEIN SEQUENCE OF 40-491. RX PubMed=2440681; DOI=10.1111/j.1432-1033.1987.tb13551.x; RA Lijnen H.R., Holmes W.E., van Hoef B., Wiman B., Rodriguez H., RA Collen D.; RT "Amino-acid sequence of human alpha 2-antiplasmin."; RL Eur. J. Biochem. 166:565-574(1987). RN [11] RP PROTEIN SEQUENCE OF 40-43. RX PubMed=21075; DOI=10.1111/j.1432-1033.1977.tb11709.x; RA Wiman B., Collen D.; RT "Purification and characterization of human antiplasmin, the fast- RT acting plasmin inhibitor in plasma."; RL Eur. J. Biochem. 78:19-26(1977). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 218-491. RX PubMed=3818581; RA Sumi Y., Nakamura Y., Aoki N., Sakai M., Muramatsu M.; RT "Structure of the carboxyl-terminal half of human alpha 2-plasmin RT inhibitor deduced from that of cDNA."; RL J. Biochem. 100:1399-1402(1986). RN [13] RP PROTEIN SEQUENCE OF 481-491, AND SULFATION AT TYR-484. RX PubMed=2434496; RA Hortin G., Fok K.F., Toren P.C., Strauss A.W.; RT "Sulfation of a tyrosine residue in the plasmin-binding domain of RT alpha 2-antiplasmin."; RL J. Biol. Chem. 262:3082-3085(1987). RN [14] RP REACTIVE SITES. RX PubMed=2456616; DOI=10.1126/science.2456616; RA Potempa J., Shieh B.-H., Travis J.; RT "Alpha-2-antiplasmin: a serpin with two separate but overlapping RT reactive sites."; RL Science 241:699-700(1988). RN [15] RP DISULFIDE BOND. RX PubMed=9169621; RA Christensen S., Valnickova Z., Thogersen I.B., Olsen E.H., RA Enghild J.J.; RT "Assignment of a single disulphide bridge in human alpha2-antiplasmin: RT implications for the structural and functional properties."; RL Biochem. J. 323:847-852(1997). RN [16] RP FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, AND RP HETERODIMER WITH TMPRSS7. RX PubMed=15853774; DOI=10.1042/BJ20050299; RA Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.; RT "Matriptase-3 is a novel phylogenetically preserved membrane-anchored RT serine protease with broad serpin reactivity."; RL Biochem. J. 390:231-242(2005). RN [17] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-126; ASN-295 AND ASN-309. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [18] RP VARIANT APLID GLU-176 DEL. RX PubMed=2572590; RA Miura O., Sugahara Y., Aoki N.; RT "Hereditary alpha 2-plasmin inhibitor deficiency caused by a RT transport-deficient mutation (alpha 2-PI-Okinawa). Deletion of Glu137 RT by a trinucleotide deletion blocks intracellular transport."; RL J. Biol. Chem. 264:18213-18219(1989). RN [19] RP VARIANT APLID MET-411, AND VARIANTS VAL-27; TRP-33 AND LYS-434. RX PubMed=10583218; DOI=10.1046/j.1365-2141.1999.01708.x; RA Lind B., Thorsen S.; RT "A novel missense mutation in the human plasmin inhibitor (alpha2- RT antiplasmin) gene associated with a bleeding tendency."; RL Br. J. Haematol. 107:317-322(1999). CC -!- FUNCTION: Serine protease inhibitor. The major targets of this CC inhibitor are plasmin and trypsin, but it also inactivates CC matriptase-3/TMPRSS7 and chymotrypsin. CC -!- SUBUNIT: Forms protease inhibiting heterodimer with TMPRSS7. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P08697-1; Sequence=Displayed; CC Name=2; CC IsoId=P08697-2; Sequence=VSP_043833, VSP_043834; CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- DISEASE: Alpha-2-plasmin inhibitor deficiency (APLID) CC [MIM:262850]: An autosomal recessive disorder resulting in severe CC hemorrhagic diathesis. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the serpin family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D00174; BAA00124.1; -; mRNA. DR EMBL; M20786; AAA51554.1; -; Genomic_DNA. DR EMBL; M20782; AAA51554.1; JOINED; Genomic_DNA. DR EMBL; M20783; AAA51554.1; JOINED; Genomic_DNA. DR EMBL; M20784; AAA51554.1; JOINED; Genomic_DNA. DR EMBL; M20785; AAA51554.1; JOINED; Genomic_DNA. DR EMBL; AK303763; BAG64729.1; -; mRNA. DR EMBL; AC130343; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC031592; AAH31592.1; -; mRNA. DR EMBL; J02654; AAA35543.1; -; mRNA. DR EMBL; D00116; BAA00070.1; -; mRNA. DR CCDS; CCDS11011.1; -. [P08697-1] DR CCDS; CCDS54064.1; -. [P08697-2] DR PIR; A31402; ITHUA2. DR RefSeq; NP_000925.2; NM_000934.3. [P08697-1] DR RefSeq; NP_001159392.1; NM_001165920.1. [P08697-1] DR RefSeq; NP_001159393.1; NM_001165921.1. [P08697-2] DR RefSeq; XP_005256758.1; XM_005256701.2. [P08697-1] DR UniGene; Hs.159509; -. DR ProteinModelPortal; P08697; -. DR SMR; P08697; 74-446. DR BioGrid; 111360; 10. DR IntAct; P08697; 2. DR STRING; 9606.ENSP00000321853; -. DR DrugBank; DB00086; Streptokinase. DR MEROPS; I04.023; -. DR PhosphoSite; P08697; -. DR DMDM; 112907; -. DR SWISS-2DPAGE; P08697; -. DR MaxQB; P08697; -. DR PaxDb; P08697; -. DR PRIDE; P08697; -. DR DNASU; 5345; -. DR Ensembl; ENST00000324015; ENSP00000321853; ENSG00000167711. [P08697-1] DR Ensembl; ENST00000382061; ENSP00000371493; ENSG00000167711. [P08697-1] DR Ensembl; ENST00000450523; ENSP00000403877; ENSG00000167711. [P08697-2] DR GeneID; 5345; -. DR KEGG; hsa:5345; -. DR UCSC; uc002ftk.1; human. [P08697-1] DR UCSC; uc010vqr.1; human. [P08697-2] DR CTD; 5345; -. DR GeneCards; GC17P001593; -. DR H-InvDB; HIX0013407; -. DR HGNC; HGNC:9075; SERPINF2. DR HPA; CAB024863; -. DR HPA; HPA001885; -. DR MIM; 262850; phenotype. DR MIM; 613168; gene. DR neXtProt; NX_P08697; -. DR Orphanet; 79; Congenital alpha2 antiplasmin deficiency. DR PharmGKB; PA35522; -. DR eggNOG; COG4826; -. DR HOGENOM; HOG000231761; -. DR HOVERGEN; HBG000043; -. DR InParanoid; P08697; -. DR KO; K03983; -. DR OMA; RWFLLEQ; -. DR PhylomeDB; P08697; -. DR TreeFam; TF317350; -. DR Reactome; REACT_604; Hemostasis. DR ChiTaRS; SERPINF2; human. DR GeneWiki; Alpha_2-antiplasmin; -. DR GenomeRNAi; 5345; -. DR NextBio; 20714; -. DR PMAP-CutDB; P08697; -. DR PRO; PR:P08697; -. DR ArrayExpress; P08697; -. DR Bgee; P08697; -. DR CleanEx; HS_SERPINF2; -. DR Genevestigator; P08697; -. DR GO; GO:0072562; C:blood microparticle; IDA:UniProt. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0005577; C:fibrinogen complex; IDA:BHF-UCL. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc. DR GO; GO:0002020; F:protease binding; IPI:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; NAS:UniProtKB. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0048514; P:blood vessel morphogenesis; ISS:BHF-UCL. DR GO; GO:0030199; P:collagen fibril organization; ISS:BHF-UCL. DR GO; GO:0042730; P:fibrinolysis; TAS:Reactome. DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:RefGenome. DR GO; GO:0051918; P:negative regulation of fibrinolysis; IDA:BHF-UCL. DR GO; GO:0010757; P:negative regulation of plasminogen activation; IDA:BHF-UCL. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome. DR GO; GO:0045597; P:positive regulation of cell differentiation; IDA:BHF-UCL. DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; TAS:BHF-UCL. DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL. DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:BHF-UCL. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL. DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA:BHF-UCL. DR GO; GO:0002034; P:regulation of blood vessel size by renin-angiotensin; ISS:BHF-UCL. DR GO; GO:0030162; P:regulation of proteolysis; IBA:RefGenome. DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. DR PANTHER; PTHR11461; PTHR11461; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; SSF56574; 1. DR PROSITE; PS00284; SERPIN; 1. PE 1: Evidence at protein level; KW Acute phase; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; KW Glycoprotein; Isopeptide bond; Polymorphism; Protease inhibitor; KW Reference proteome; Secreted; Serine protease inhibitor; Signal; KW Sulfation. FT SIGNAL 1 27 FT PROPEP 28 39 FT /FTId=PRO_0000032511. FT CHAIN 40 491 Alpha-2-antiplasmin. FT /FTId=PRO_0000032512. FT SITE 403 404 Reactive bond for plasmin. FT SITE 404 405 Reactive bond for chymotrypsin. FT MOD_RES 484 484 Sulfotyrosine. FT CARBOHYD 126 126 N-linked (GlcNAc...). FT CARBOHYD 295 295 N-linked (GlcNAc...). FT CARBOHYD 309 309 N-linked (GlcNAc...). FT CARBOHYD 316 316 N-linked (GlcNAc...) (Potential). FT DISULFID 70 143 FT CROSSLNK 41 41 Isoglutamyl lysine isopeptide (Gln-Lys) FT (interchain with K-322 in alpha- FT fibrinogen). FT VAR_SEQ 56 119 Missing (in isoform 2). FT /FTId=VSP_043833. FT VAR_SEQ 120 122 LAL -> VQP (in isoform 2). FT /FTId=VSP_043834. FT VARIANT 2 2 A -> V (in dbSNP:rs2070862). FT /FTId=VAR_047951. FT VARIANT 27 27 A -> V. FT /FTId=VAR_013252. FT VARIANT 33 33 R -> W (in dbSNP:rs2070863). FT /FTId=VAR_013253. FT VARIANT 98 98 A -> G (in dbSNP:rs36021516). FT /FTId=VAR_051956. FT VARIANT 176 176 Missing (in APLID; variant Okinawa; FT probably blocks intracellular transport FT of alpha-2-plasmin inhibitor). FT /FTId=VAR_013254. FT VARIANT 411 411 V -> M (in APLID). FT /FTId=VAR_013255. FT VARIANT 434 434 R -> K (in dbSNP:rs1057335). FT /FTId=VAR_013256. FT VARIANT 451 451 P -> S (in dbSNP:rs57360598). FT /FTId=VAR_061792. FT CONFLICT 49 49 L -> G (in Ref. 10; AA sequence). FT CONFLICT 105 105 N -> D (in Ref. 10; AA sequence). FT CONFLICT 289 289 H -> D (in Ref. 7; AAA35543). FT CONFLICT 408 408 S -> G (in Ref. 10; AA sequence). FT CONFLICT 455 455 D -> N (in Ref. 10; AA sequence). SQ SEQUENCE 491 AA; 54566 MW; 385A1C90E91A63CB CRC64; MALLWGLLVL SWSCLQGPCS VFSPVSAMEP LGRQLTSGPN QEQVSPLTLL KLGNQEPGGQ TALKSPPGVC SRDPTPEQTH RLARAMMAFT ADLFSLVAQT STCPNLILSP LSVALALSHL ALGAQNHTLQ RLQQVLHAGS GPCLPHLLSR LCQDLGPGAF RLAARMYLQK GFPIKEDFLE QSEQLFGAKP VSLTGKQEDD LANINQWVKE ATEGKIQEFL SGLPEDTVLL LLNAIHFQGF WRNKFDPSLT QRDSFHLDEQ FTVPVEMMQA RTYPLRWFLL EQPEIQVAHF PFKNNMSFVV LVPTHFEWNV SQVLANLSWD TLHPPLVWER PTKVRLPKLY LKHQMDLVAT LSQLGLQELF QAPDLRGISE QSLVVSGVQH QSTLELSEVG VEAAAATSIA MSRMSLSSFS VNRPFLFFIF EDTTGLPLFV GSVRNPNPSA PRELKEQQDS PGNKDFLQSL KGFPRGDKLF GPDLKLVPPM EEDYPQFGSP K // ID A2MG_HUMAN Reviewed; 1474 AA. AC P01023; Q13677; Q59F47; Q5QTS0; Q68DN2; Q6PIY3; Q6PN97; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 09-JUL-2014, entry version 172. DE RecName: Full=Alpha-2-macroglobulin; DE Short=Alpha-2-M; DE AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5; DE Flags: Precursor; GN Name=A2M; Synonyms=CPAMD5; ORFNames=FWP007; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASP-639 AND VAL-1000. RX PubMed=2581245; DOI=10.1073/pnas.82.8.2282; RA Kan C.-C., Solomon E., Belt K.T., Chain A.C., Hiorns L.R., Fey G.H.; RT "Nucleotide sequence of cDNA encoding human alpha 2-macroglobulin and RT assignment of the chromosomal locus."; RL Proc. Natl. Acad. Sci. U.S.A. 82:2282-2286(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASP-639 AND VAL-1000. RC TISSUE=Prostate; RX PubMed=15611997; DOI=10.1002/pros.20183; RA Lin V.K., Wang S.-Y., Boetticher N.C., Vazquez D.V., Saboorian H., RA McConnell J.D., Roehrborn C.G.; RT "Alpha(2) macroglobulin, a PSA-binding protein, is expressed in human RT prostate stroma."; RL Prostate 63:299-308(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-639. RC TISSUE=Spleen; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-639 AND RP VAL-1000. RC TISSUE=Liver; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASP-639 AND RP VAL-1000. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. RC TISSUE=Placenta; RX PubMed=1374237; DOI=10.1016/0006-291X(92)90631-T; RA Matthijs G., Devriendt K., Cassiman J.-J., van den Berghe H., RA Marynen P.; RT "Structure of the human alpha-2 macroglobulin gene and its promotor."; RL Biochem. Biophys. Res. Commun. 184:596-603(1992). RN [8] RP PROTEIN SEQUENCE OF 24-1474, SUBUNIT, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DISULFIDE BONDS. RX PubMed=6203908; RA Sottrup-Jensen L., Stepanik T.M., Kristensen T., Wierzbicki D.M., RA Jones C.M., Loenblad P.B., Magnusson S., Petersen T.E.; RT "Primary structure of human alpha 2-macroglobulin. V. The complete RT structure."; RL J. Biol. Chem. 259:8318-8327(1984). RN [9] RP ERRATUM. RA Sottrup-Jensen L., Stepanik T.M., Kristensen T., Wierzbicki D.M., RA Jones C.M., Loenblad P.B., Magnusson S., Petersen T.E.; RL J. Biol. Chem. 260:6500-6500(1985). RN [10] RP PROTEIN SEQUENCE OF 273-286 AND 426-436, AND DISULFIDE BONDS. RX PubMed=2430963; RA Jensen P.E.H., Sottrup-Jensen L.; RT "Primary structure of human alpha 2-macroglobulin. Complete disulfide RT bridge assignment and localization of two interchain bridges in the RT dimeric proteinase binding unit."; RL J. Biol. Chem. 261:15863-15869(1986). RN [11] RP PROTEIN SEQUENCE OF 672-747. RX PubMed=1692292; DOI=10.1016/0014-5793(90)80226-9; RA Marynen P., Devriendt K., van den Berghe H., Cassiman J.-J.; RT "A genetic polymorphism in a functional domain of human pregnancy zone RT protein: the bait region. Genomic structure of the bait domains of RT human pregnancy zone protein and alpha 2 macroglobulin."; RL FEBS Lett. 262:349-352(1990). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 672-746, AND VARIANT TYR-972. RX PubMed=1370808; DOI=10.1007/BF00197266; RA Poller W., Faber J.-P., Klobeck G., Olek K.; RT "Cloning of the human alpha 2-macroglobulin gene and detection of RT mutations in two functional domains: the bait region and the RT thiolester site."; RL Hum. Genet. 88:313-319(1992). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 832-1474. RC TISSUE=Liver; RX PubMed=2408344; DOI=10.1007/BF01534685; RA Bell G.I., Rall L.B., Sanchez-Pescador R., Merryweather J.P., RA Scott J., Eddy R.L., Shows T.B.; RT "Human alpha 2-macroglobulin gene is located on chromosome 12."; RL Somat. Cell Mol. Genet. 11:285-289(1985). RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1208-1474. RC TISSUE=Aorta; RA Liu B., Zhao B., Wang X.Y., Xu Y.Y., Liu Y.Q., Song L., Ye J., RA Sheng H., Gao Y., Zhang C.L., Wei Y.J., Zhang J., Song L., Jiang Y.X., RA Zhao Z.W., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y., Qiang B.Q., RA Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [15] RP INHIBITORY SITE. RX PubMed=6167263; DOI=10.1016/S0006-291X(81)80055-1; RA Hall P.K., Nelles L.P., Travis J., Roberts R.C.; RT "Proteolytic cleavage sites on alpha 2-macroglobulin resulting in RT proteinase binding are different for trypsin and Staphylococcus aureus RT V-8 proteinase."; RL Biochem. Biophys. Res. Commun. 100:8-16(1981). RN [16] RP INHIBITORY SITE. RX PubMed=6165619; DOI=10.1016/0014-5793(81)80197-4; RA Sottrup-Jensen L., Loenblad P.B., Stepanik T.M., Petersen T.E., RA Magnusson S., Joernvall H.; RT "Primary structure of the 'bait' region for proteinases in alpha 2- RT macroglobulin. Nature of the complex."; RL FEBS Lett. 127:167-173(1981). RN [17] RP INHIBITORY SITE. RX PubMed=6172288; DOI=10.1016/0014-5793(81)80804-6; RA Mortensen S.B., Sottrup-Jensen L., Hansen H.F., Petersen T.E., RA Magnusson S.; RT "Primary and secondary cleavage sites in the bait region of alpha 2- RT macroglobulin."; RL FEBS Lett. 135:295-300(1981). RN [18] RP INHIBITORY SITE. RX PubMed=6195065; RA Virca G.D., Salvesen G.S., Travis J.; RT "Human neutrophil elastase and cathepsin G cleavage sites in the bait RT region of alpha 2-macroglobulin. Proposed structural limits of the RT bait region."; RL Hoppe-Seyler's Z. Physiol. Chem. 364:1297-1302(1983). RN [19] RP GLYCOSYLATION AT ASN-991. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-869 AND ASN-1424. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-247; ASN-396; RP ASN-410; ASN-869; ASN-991 AND ASN-1424. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-396; ASN-991 AND ASN-1424. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [23] RP GLYCOSYLATION AT ASN-55 AND ASN-1424. RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [25] RP STRUCTURE BY NMR OF 1337-1474. RX PubMed=9865955; DOI=10.1002/pro.5560071214; RA Huang W., Dolmer K., Liao X., Gettins P.G.W.; RT "Localization of basic residues required for receptor binding to the RT single alpha-helix of the receptor binding domain of human alpha2- RT macroglobulin."; RL Protein Sci. 7:2602-2612(1998). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 126-227, AND DOMAIN RP STRUCTURE. RX PubMed=17608619; DOI=10.1042/BJ20070764; RA Doan N., Gettins P.G.W.; RT "Human alpha2-macroglobulin is composed of multiple domains, as RT predicted by homology with complement component C3."; RL Biochem. J. 407:23-30(2007). RN [27] RP VARIANT VAL-1000. RX PubMed=1707161; DOI=10.1093/nar/19.1.198-a; RA Poller W., Faber J.-P., Olek K.; RT "Sequence polymorphism in the human alpha2-macroglobulin (A2M) gene."; RL Nucleic Acids Res. 19:198-198(1991). CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a CC unique 'trapping' mechanism. This protein has a peptide stretch, CC called the 'bait region' which contains specific cleavage sites CC for different proteinases. When a proteinase cleaves the bait CC region, a conformational change is induced in the protein which CC traps the proteinase. The entrapped enzyme remains active against CC low molecular weight substrates (activity against high molecular CC weight substrates is greatly reduced). Following cleavage in the CC bait region a thioester bond is hydrolyzed and mediates the CC covalent binding of the protein to the proteinase. CC -!- SUBUNIT: Homotetramer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Secreted in plasma. CC -!- DEVELOPMENTAL STAGE: Contrary to the rat protein, which is an CC acute phase protein, this protein is always present at high levels CC in circulation. CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2- CC macroglobulin) family. CC -!- SEQUENCE CAUTION: CC Sequence=AAT02228.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=BAD92851.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-2 macroglobulin entry; CC URL="http://en.wikipedia.org/wiki/Alpha_2-macroglobulin"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M11313; AAA51551.1; -; mRNA. DR EMBL; AY591530; AAT02228.1; ALT_INIT; mRNA. DR EMBL; AB209614; BAD92851.1; ALT_INIT; mRNA. DR EMBL; CR749334; CAH18188.1; -; mRNA. DR EMBL; AC007436; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC026246; AAH26246.1; -; mRNA. DR EMBL; BC040071; AAH40071.1; -; mRNA. DR EMBL; Z11711; CAA77774.1; -; Genomic_DNA. DR EMBL; X68728; CAA48670.1; -; Genomic_DNA. DR EMBL; X68729; CAA48670.1; JOINED; Genomic_DNA. DR EMBL; M36501; AAA51552.1; -; mRNA. DR EMBL; AF109189; AAQ13498.1; -; mRNA. DR CCDS; CCDS44827.1; -. DR PIR; A94033; MAHU. DR RefSeq; NP_000005.2; NM_000014.4. DR UniGene; Hs.212838; -. DR PDB; 1BV8; NMR; -; A=1337-1474. DR PDB; 2P9R; X-ray; 2.30 A; A/B=126-227. DR PDB; 4ACQ; X-ray; 4.30 A; A/B/C/D=24-1474. DR PDBsum; 1BV8; -. DR PDBsum; 2P9R; -. DR PDBsum; 4ACQ; -. DR ProteinModelPortal; P01023; -. DR SMR; P01023; 126-227, 1338-1474. DR BioGrid; 106524; 89. DR DIP; DIP-1118N; -. DR IntAct; P01023; 95. DR MINT; MINT-122288; -. DR STRING; 9606.ENSP00000323929; -. DR DrugBank; DB00626; Bacitracin. DR DrugBank; DB00102; Becaplermin. DR MEROPS; I39.001; -. DR PhosphoSite; P01023; -. DR DMDM; 308153640; -. DR DOSAC-COBS-2DPAGE; P01023; -. DR SWISS-2DPAGE; P01023; -. DR MaxQB; P01023; -. DR PaxDb; P01023; -. DR PeptideAtlas; P01023; -. DR PRIDE; P01023; -. DR Ensembl; ENST00000318602; ENSP00000323929; ENSG00000175899. DR GeneID; 2; -. DR KEGG; hsa:2; -. DR UCSC; uc001qvk.1; human. DR CTD; 2; -. DR GeneCards; GC12M009220; -. DR H-InvDB; HIX0026392; -. DR HGNC; HGNC:7; A2M. DR HPA; CAB017621; -. DR HPA; HPA002265; -. DR MIM; 103950; gene. DR neXtProt; NX_P01023; -. DR PharmGKB; PA24357; -. DR eggNOG; COG2373; -. DR HOVERGEN; HBG000039; -. DR KO; K03910; -. DR OMA; QTVQAHY; -. DR OrthoDB; EOG7DJSKB; -. DR PhylomeDB; P01023; -. DR TreeFam; TF313285; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_118779; Extracellular matrix organization. DR Reactome; REACT_604; Hemostasis. DR ChiTaRS; A2M; human. DR EvolutionaryTrace; P01023; -. DR GenomeRNAi; 2; -. DR NextBio; 5; -. DR PRO; PR:P01023; -. DR ArrayExpress; P01023; -. DR Bgee; P01023; -. DR CleanEx; HS_A2M; -. DR Genevestigator; P01023; -. DR GO; GO:0072562; C:blood microparticle; IDA:UniProt. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0019838; F:growth factor binding; IDA:UniProtKB. DR GO; GO:0019966; F:interleukin-1 binding; IDA:UniProtKB. DR GO; GO:0019959; F:interleukin-8 binding; IPI:UniProtKB. DR GO; GO:0002020; F:protease binding; IPI:BHF-UCL. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0005102; F:receptor binding; IMP:AgBase. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB. DR GO; GO:0043120; F:tumor necrosis factor binding; IDA:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0001869; P:negative regulation of complement activation, lectin pathway; IDA:UniProtKB. DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:GOC. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0048863; P:stem cell differentiation; IEA:Ensembl. DR Gene3D; 1.50.10.20; -; 1. DR Gene3D; 2.60.40.690; -; 1. DR InterPro; IPR009048; A-macroglobulin_rcpt-bd. DR InterPro; IPR011626; A2M_comp. DR InterPro; IPR002890; A2M_N. DR InterPro; IPR011625; A2M_N_2. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR001599; Macroglobln_a2. DR InterPro; IPR019742; MacrogloblnA2_CS. DR InterPro; IPR019565; MacrogloblnA2_thiol-ester-bond. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR InterPro; IPR010916; TonB_box_CS. DR Pfam; PF00207; A2M; 1. DR Pfam; PF07678; A2M_comp; 1. DR Pfam; PF01835; A2M_N; 1. DR Pfam; PF07703; A2M_N_2; 1. DR Pfam; PF07677; A2M_recep; 1. DR Pfam; PF10569; Thiol-ester_cl; 1. DR SUPFAM; SSF48239; SSF48239; 1. DR SUPFAM; SSF49410; SSF49410; 1. DR SUPFAM; SSF81296; SSF81296; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Bait region; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Isopeptide bond; Polymorphism; Protease inhibitor; Reference proteome; KW Secreted; Serine protease inhibitor; Signal; Thioester bond. FT SIGNAL 1 23 FT CHAIN 24 1474 Alpha-2-macroglobulin. FT /FTId=PRO_0000000055. FT REGION 690 728 Bait region. FT REGION 704 709 Inhibitory. FT REGION 719 723 Inhibitory. FT REGION 730 735 Inhibitory. FT CARBOHYD 55 55 N-linked (GlcNAc...) (complex). FT CARBOHYD 70 70 N-linked (GlcNAc...). FT CARBOHYD 247 247 N-linked (GlcNAc...). FT CARBOHYD 396 396 N-linked (GlcNAc...). FT CARBOHYD 410 410 N-linked (GlcNAc...). FT CARBOHYD 869 869 N-linked (GlcNAc...). FT CARBOHYD 991 991 N-linked (GlcNAc...). FT CARBOHYD 1424 1424 N-linked (GlcNAc...) (complex). FT DISULFID 48 86 FT DISULFID 251 299 FT DISULFID 269 287 FT DISULFID 278 278 Interchain (with C-431). FT DISULFID 431 431 Interchain (with C-278). FT DISULFID 470 563 FT DISULFID 595 771 FT DISULFID 642 689 FT DISULFID 821 849 FT DISULFID 847 883 FT DISULFID 921 1321 FT DISULFID 1079 1127 FT DISULFID 1352 1467 FT CROSSLNK 693 693 Isoglutamyl lysine isopeptide (Gln-Lys) FT (interchain with K-? in other proteins) FT (Potential). FT CROSSLNK 694 694 Isoglutamyl lysine isopeptide (Gln-Lys) FT (interchain with K-? in other proteins) FT (Potential). FT CROSSLNK 972 975 Isoglutamyl cysteine thioester (Cys-Gln). FT VARIANT 639 639 N -> D (in dbSNP:rs226405). FT /FTId=VAR_026820. FT VARIANT 704 704 R -> H (in dbSNP:rs1800434). FT /FTId=VAR_000012. FT VARIANT 815 815 L -> Q (in dbSNP:rs3180392). FT /FTId=VAR_026821. FT VARIANT 972 972 C -> Y (probably interferes with the FT activity; dbSNP:rs1800433). FT /FTId=VAR_000013. FT VARIANT 1000 1000 I -> V (in dbSNP:rs669). FT /FTId=VAR_000014. FT CONFLICT 63 63 Missing (in Ref. 8; AA sequence). FT CONFLICT 82 82 D -> V (in Ref. 3; AAT02228). FT CONFLICT 350 353 LSFV -> ACCS (in Ref. 6; AAH26246). FT CONFLICT 563 563 C -> E (in Ref. 8; AA sequence). FT CONFLICT 844 844 A -> V (in Ref. 4; BAD92851). FT CONFLICT 872 872 V -> M (in Ref. 5; CAH18188). FT CONFLICT 1148 1148 A -> D (in Ref. 13; AAA51552). FT CONFLICT 1195 1195 H -> D (in Ref. 13; AAA51552). FT STRAND 128 134 FT STRAND 136 138 FT STRAND 143 151 FT HELIX 153 155 FT STRAND 161 168 FT STRAND 174 182 FT STRAND 187 193 FT STRAND 201 208 FT STRAND 214 221 FT STRAND 1341 1347 FT HELIX 1355 1359 FT STRAND 1360 1369 FT STRAND 1379 1384 FT STRAND 1389 1391 FT HELIX 1393 1400 FT TURN 1401 1403 FT STRAND 1407 1410 FT STRAND 1412 1419 FT STRAND 1427 1434 FT STRAND 1445 1450 FT STRAND 1454 1456 FT STRAND 1459 1463 SQ SEQUENCE 1474 AA; 163291 MW; 0A46DF09EFD3CF40 CRC64; MGKNKLLHPS LVLLLLVLLP TDASVSGKPQ YMVLVPSLLH TETTEKGCVL LSYLNETVTV SASLESVRGN RSLFTDLEAE NDVLHCVAFA VPKSSSNEEV MFLTVQVKGP TQEFKKRTTV MVKNEDSLVF VQTDKSIYKP GQTVKFRVVS MDENFHPLNE LIPLVYIQDP KGNRIAQWQS FQLEGGLKQF SFPLSSEPFQ GSYKVVVQKK SGGRTEHPFT VEEFVLPKFE VQVTVPKIIT ILEEEMNVSV CGLYTYGKPV PGHVTVSICR KYSDASDCHG EDSQAFCEKF SGQLNSHGCF YQQVKTKVFQ LKRKEYEMKL HTEAQIQEEG TVVELTGRQS SEITRTITKL SFVKVDSHFR QGIPFFGQVR LVDGKGVPIP NKVIFIRGNE ANYYSNATTD EHGLVQFSIN TTNVMGTSLT VRVNYKDRSP CYGYQWVSEE HEEAHHTAYL VFSPSKSFVH LEPMSHELPC GHTQTVQAHY ILNGGTLLGL KKLSFYYLIM AKGGIVRTGT HGLLVKQEDM KGHFSISIPV KSDIAPVARL LIYAVLPTGD VIGDSAKYDV ENCLANKVDL SFSPSQSLPA SHAHLRVTAA PQSVCALRAV DQSVLLMKPD AELSASSVYN LLPEKDLTGF PGPLNDQDNE DCINRHNVYI NGITYTPVSS TNEKDMYSFL EDMGLKAFTN SKIRKPKMCP QLQQYEMHGP EGLRVGFYES DVMGRGHARL VHVEEPHTET VRKYFPETWI WDLVVVNSAG VAEVGVTVPD TITEWKAGAF CLSEDAGLGI SSTASLRAFQ PFFVELTMPY SVIRGEAFTL KATVLNYLPK CIRVSVQLEA SPAFLAVPVE KEQAPHCICA NGRQTVSWAV TPKSLGNVNF TVSAEALESQ ELCGTEVPSV PEHGRKDTVI KPLLVEPEGL EKETTFNSLL CPSGGEVSEE LSLKLPPNVV EESARASVSV LGDILGSAMQ NTQNLLQMPY GCGEQNMVLF APNIYVLDYL NETQQLTPEI KSKAIGYLNT GYQRQLNYKH YDGSYSTFGE RYGRNQGNTW LTAFVLKTFA QARAYIFIDE AHITQALIWL SQRQKDNGCF RSSGSLLNNA IKGGVEDEVT LSAYITIALL EIPLTVTHPV VRNALFCLES AWKTAQEGDH GSHVYTKALL AYAFALAGNQ DKRKEVLKSL NEEAVKKDNS VHWERPQKPK APVGHFYEPQ APSAEVEMTS YVLLAYLTAQ PAPTSEDLTS ATNIVKWITK QQNAQGGFSS TQDTVVALHA LSKYGAATFT RTGKAAQVTI QSSGTFSSKF QVDNNNRLLL QQVSLPELPG EYSMKVTGEG CVYLQTSLKY NILPEKEEFP FALGVQTLPQ TCDEPKAHTS FQISLSVSYT GSRSASNMAI VDVKMVSGFI PLKPTVKMLE RSNHVSRTEV SSNHVLIYLD KVSNQTLSLF FTVLQDVPVR DLKPAIVKVY DYYETDEFAI AEYNAPCSKD LGNA // ID A4_HUMAN Reviewed; 770 AA. AC P05067; B2R5V1; B4DII8; D3DSD1; D3DSD2; D3DSD3; P09000; P78438; AC Q13764; Q13778; Q13793; Q16011; Q16014; Q16019; Q16020; Q6GSC0; AC Q8WZ99; Q9BT38; Q9UC33; Q9UCA9; Q9UCB6; Q9UCC8; Q9UCD1; Q9UQ58; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 3. DT 09-JUL-2014, entry version 229. DE RecName: Full=Amyloid beta A4 protein; DE AltName: Full=ABPP; DE AltName: Full=APPI; DE Short=APP; DE AltName: Full=Alzheimer disease amyloid protein; DE AltName: Full=Cerebral vascular amyloid peptide; DE Short=CVAP; DE AltName: Full=PreA4; DE AltName: Full=Protease nexin-II; DE Short=PN-II; DE Contains: DE RecName: Full=N-APP; DE Contains: DE RecName: Full=Soluble APP-alpha; DE Short=S-APP-alpha; DE Contains: DE RecName: Full=Soluble APP-beta; DE Short=S-APP-beta; DE Contains: DE RecName: Full=C99; DE Contains: DE RecName: Full=Beta-amyloid protein 42; DE AltName: Full=Beta-APP42; DE Contains: DE RecName: Full=Beta-amyloid protein 40; DE AltName: Full=Beta-APP40; DE Contains: DE RecName: Full=C83; DE Contains: DE RecName: Full=P3(42); DE Contains: DE RecName: Full=P3(40); DE Contains: DE RecName: Full=C80; DE Contains: DE RecName: Full=Gamma-secretase C-terminal fragment 59; DE AltName: Full=Amyloid intracellular domain 59; DE Short=AICD-59; DE Short=AID(59); DE AltName: Full=Gamma-CTF(59); DE Contains: DE RecName: Full=Gamma-secretase C-terminal fragment 57; DE AltName: Full=Amyloid intracellular domain 57; DE Short=AICD-57; DE Short=AID(57); DE AltName: Full=Gamma-CTF(57); DE Contains: DE RecName: Full=Gamma-secretase C-terminal fragment 50; DE AltName: Full=Amyloid intracellular domain 50; DE Short=AICD-50; DE Short=AID(50); DE AltName: Full=Gamma-CTF(50); DE Contains: DE RecName: Full=C31; DE Flags: Precursor; GN Name=APP; Synonyms=A4, AD1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695). RC TISSUE=Brain; RX PubMed=2881207; DOI=10.1038/325733a0; RA Kang J., Lemaire H.-G., Unterbeck A., Salbaum J.M., Masters C.L., RA Grzeschik K.-H., Multhaup G., Beyreuther K., Mueller-Hill B.; RT "The precursor of Alzheimer's disease amyloid A4 protein resembles a RT cell-surface receptor."; RL Nature 325:733-736(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP751). RC TISSUE=Brain; RX PubMed=2893289; DOI=10.1038/331525a0; RA Ponte P., Gonzalez-Dewhitt P., Schilling J., Miller J., Hsu D., RA Greenberg B., Davis K., Wallace W., Lieberburg I., Fuller F., RA Cordell B.; RT "A new A4 amyloid mRNA contains a domain homologous to serine RT proteinase inhibitors."; RL Nature 331:525-527(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM APP695). RX PubMed=2783775; DOI=10.1093/nar/17.2.517; RA Lemaire H.-G., Salbaum J.M., Multhaup G., Kang J., Bayney R.M., RA Unterbeck A., Beyreuther K., Mueller-Hill B.; RT "The PreA4(695) precursor protein of Alzheimer's disease A4 amyloid is RT encoded by 16 exons."; RL Nucleic Acids Res. 17:517-522(1989). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM APP770). RX PubMed=2110105; DOI=10.1016/0378-1119(90)90310-N; RA Yoshikai S., Sasaki H., Doh-ura K., Furuya H., Sakaki Y.; RT "Genomic organization of the human amyloid beta-protein precursor RT gene."; RL Gene 87:257-263(1990). RN [5] RP ERRATUM. RX PubMed=1908403; DOI=10.1016/0378-1119(91)90093-Q; RA Yoshikai S., Sasaki H., Doh-ura K., Furuya H., Sakaki Y.; RL Gene 102:291-292(1991). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM L-APP733). RC TISSUE=Leukocyte; RX PubMed=1587857; RA Koenig G., Moenning U., Czech C., Prior R., Banati R., RA Schreiter-Gasser U., Bauer J., Masters C.L., Beyreuther K.; RT "Identification and differential expression of a novel alternative RT splice isoform of the beta A4 amyloid precursor protein (APP) mRNA in RT leukocytes and brain microglial cells."; RL J. Biol. Chem. 267:10804-10809(1992). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM APP770). RX PubMed=9108164; DOI=10.1093/nar/25.9.1802; RA Hattori M., Tsukahara F., Furuhata Y., Tanahashi H., Hirose M., RA Saito M., Tsukuni S., Sakaki Y.; RT "A novel method for making nested deletions and its application for RT sequencing of a 300 kb region of human APP locus."; RL Nucleic Acids Res. 25:1802-1808(1997). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP639), AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=12859342; DOI=10.1046/j.1460-9568.2003.02731.x; RA Tang K., Wang C., Shen C., Sheng S., Ravid R., Jing N.; RT "Identification of a novel alternative splicing isoform of human RT amyloid precursor protein gene, APP639."; RL Eur. J. Neurosci. 18:102-108(2003). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS APP770 AND 11). RC TISSUE=Cerebellum, and Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-501. RG NIEHS SNPs program; RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., RA Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS APP305 AND APP751). RC TISSUE=Eye, and Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-10. RC TISSUE=Liver; RX PubMed=3140222; DOI=10.1093/nar/16.19.9351; RA Schon E.A., Mita S., Sadlock J., Herbert J.; RT "A cDNA specifying the human amyloid beta precursor protein (ABPP) RT encodes a 95-kDa polypeptide."; RL Nucleic Acids Res. 16:9351-9351(1988). RN [15] RP ERRATUM, AND SEQUENCE REVISION. RA Schon E.A., Mita S., Sadlock J., Herbert J.; RL Nucleic Acids Res. 16:11402-11402(1988). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-75. RX PubMed=2538123; DOI=10.1016/0006-291X(89)92437-6; RA La Fauci G., Lahiri D.K., Salton S.R., Robakis N.K.; RT "Characterization of the 5'-end region and the first two exons of the RT beta-protein precursor gene."; RL Biochem. Biophys. Res. Commun. 159:297-304(1989). RN [17] RP PROTEIN SEQUENCE OF 18-50. RC TISSUE=Fibroblast; RX PubMed=3597385; RA van Nostrand W.E., Cunningham D.D.; RT "Purification of protease nexin II from human fibroblasts."; RL J. Biol. Chem. 262:8508-8514(1987). RN [18] RP PROTEIN SEQUENCE OF 18-40. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [19] RP NUCLEOTIDE SEQUENCE [MRNA] OF 286-366. RX PubMed=2893290; DOI=10.1038/331528a0; RA Tanzi R.E., McClatchey A.I., Lamperti E.D., Villa-Komaroff L., RA Gusella J.F., Neve R.L.; RT "Protease inhibitor domain encoded by an amyloid protein precursor RT mRNA associated with Alzheimer's disease."; RL Nature 331:528-530(1988). RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] OF 287-367. RX PubMed=2893291; DOI=10.1038/331530a0; RA Kitaguchi N., Takahashi Y., Tokushima Y., Shiojiri S., Ito H.; RT "Novel precursor of Alzheimer's disease amyloid protein shows protease RT inhibitory activity."; RL Nature 331:530-532(1988). RN [21] RP NUCLEOTIDE SEQUENCE [MRNA] OF 507-770. RC TISSUE=Brain cortex; RX PubMed=2893379; DOI=10.1073/pnas.85.3.929; RA Zain S.B., Salim M., Chou W.G., Sajdel-Sulkowska E.M., Majocha R.E., RA Marotta C.A.; RT "Molecular cloning of amyloid cDNA derived from mRNA of the Alzheimer RT disease brain: coding and noncoding regions of the fetal precursor RT mRNA are expressed in the cortex."; RL Proc. Natl. Acad. Sci. U.S.A. 85:929-933(1988). RN [22] RP PROTEIN SEQUENCE OF 523-555, AND DOMAIN COLLAGEN-BINDING. RX PubMed=8576160; DOI=10.1074/jbc.271.3.1613; RA Beher D., Hesse L., Masters C.L., Multhaup G.; RT "Regulation of amyloid protein precursor (APP) binding to collagen and RT mapping of the binding sites on APP and collagen type I."; RL J. Biol. Chem. 271:1613-1620(1996). RN [23] RP NUCLEOTIDE SEQUENCE [MRNA] OF 655-737, AND VARIANTS AD1 GLY-717; RP ILE-717 AND PHE-717. RX PubMed=8476439; DOI=10.1006/bbrc.1993.1386; RA Denman R.B., Rosenzcwaig R., Miller D.L.; RT "A system for studying the effect(s) of familial Alzheimer disease RT mutations on the processing of the beta-amyloid peptide precursor."; RL Biochem. Biophys. Res. Commun. 192:96-103(1993). RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 656-737. RX PubMed=2675837; DOI=10.1016/0006-291X(89)91112-1; RA Johnstone E.M., Chaney M.O., Moore R.E., Ward K.E., Norris F.H., RA Little S.P.; RT "Alzheimer's disease amyloid peptide is encoded by two exons and shows RT similarity to soybean trypsin inhibitor."; RL Biochem. Biophys. Res. Commun. 163:1248-1255(1989). RN [25] RP NUCLEOTIDE SEQUENCE [MRNA] OF 672-723, AND VARIANT AD1 ASN-678. RX PubMed=15201367; DOI=10.1136/jnnp.2003.010611; RA Wakutani Y., Watanabe K., Adachi Y., Wada-Isoe K., Urakami K., RA Ninomiya H., Saido T.C., Hashimoto T., Iwatsubo T., Nakashima K.; RT "Novel amyloid precursor protein gene missense mutation (D678N) in RT probable familial Alzheimer's disease."; RL J. Neurol. Neurosurg. Psych. 75:1039-1042(2004). RN [26] RP PROTEIN SEQUENCE OF 672-713. RC TISSUE=Blood vessel; RX PubMed=8248178; DOI=10.1073/pnas.90.22.10836; RA Roher A.E., Lowenson J.D., Clarke S., Woods A.S., Cotter R.J., RA Gowing E., Ball M.J.; RT "Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid RT deposits: implications for the pathology of Alzheimer disease."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10836-10840(1993). RN [27] RP PROTEIN SEQUENCE OF 672-704, AND TISSUE SPECIFICITY. RX PubMed=1406936; DOI=10.1038/359325a0; RA Seubert P., Vigo-Pelfrey C., Esch F., Lee M., Dovey H., Davis D., RA Sinha S., Schlossmacher M., Whaley J., Swindlehurst C.; RT "Isolation and quantification of soluble Alzheimer's beta-peptide from RT biological fluids."; RL Nature 359:325-327(1992). RN [28] RP PROTEIN SEQUENCE OF 672-701 AND 707-713. RX PubMed=8109908; DOI=10.1002/ana.410350223; RA Wisniewski T., Lalowski M., Levy E., Marques M.R.F., Frangione B.; RT "The amino acid sequence of neuritic plaque amyloid from a familial RT Alzheimer's disease patient."; RL Ann. Neurol. 35:245-246(1994). RN [29] RP PROTEIN SEQUENCE OF 672-701. RC TISSUE=Cerebrospinal fluid; RX PubMed=8229004; DOI=10.1111/j.1471-4159.1993.tb09841.x; RA Vigo-Pelfrey C., Lee D., Keim P., Lieberburg I., Schenk D.B.; RT "Characterization of beta-amyloid peptide from human cerebrospinal RT fluid."; RL J. Neurochem. 61:1965-1968(1993). RN [30] RP PROTEIN SEQUENCE OF 672-681. RC TISSUE=Brain cortex; RX PubMed=3312495; DOI=10.1111/j.1471-4159.1987.tb01005.x; RA Pardridge W.M., Vinters H.V., Yang J., Eisenberg J., Choi T.B., RA Tourtellotte W.W., Huebner V., Shively J.E.; RT "Amyloid angiopathy of Alzheimer's disease: amino acid composition and RT partial sequence of a 4,200-dalton peptide isolated from cortical RT microvessels."; RL J. Neurochem. 49:1394-1401(1987). RN [31] RP NUCLEOTIDE SEQUENCE [MRNA] OF 674-770. RC TISSUE=Brain; RX PubMed=3810169; DOI=10.1126/science.3810169; RA Goldgaber D., Lerman M.I., McBride O.W., Saffiotti U., Gajdusek D.C.; RT "Characterization and chromosomal localization of a cDNA encoding RT brain amyloid of Alzheimer's disease."; RL Science 235:877-880(1987). RN [32] RP NUCLEOTIDE SEQUENCE [MRNA] OF 674-703. RC TISSUE=Fetal brain; RX PubMed=2949367; DOI=10.1126/science.2949367; RA Tanzi R.E., Gusella J.F., Watkins P.C., Bruns G.A., RA St George-Hyslop P.H., Van Keuren M.L., Patterson D., Pagan S., RA Kurnit D.M., Neve R.L.; RT "Amyloid beta protein gene: cDNA, mRNA distribution, and genetic RT linkage near the Alzheimer locus."; RL Science 235:880-884(1987). RN [33] RP PROTEIN SEQUENCE OF 609-713, AND GLYCOSYLATION AT SER-614; SER-623; RP SER-628; SER-679 AND SER-697. RC TISSUE=Cerebrospinal fluid; RX PubMed=22576872; DOI=10.1002/jms.2987; RA Brinkmalm G., Portelius E., Ohrfelt A., Mattsson N., Persson R., RA Gustavsson M.K., Vite C.H., Gobom J., Mansson J.E., Nilsson J., RA Halim A., Larson G., Ruetschi U., Zetterberg H., Blennow K., RA Brinkmalm A.; RT "An online nano-LC-ESI-FTICR-MS method for comprehensive RT characterization of endogenous fragments from amyloid beta and amyloid RT precursor protein in human and cat cerebrospinal fluid."; RL J. Mass Spectrom. 47:591-603(2012). RN [34] RP PROTEIN SEQUENCE OF 691-698, AND CLEAVAGE BY THETA-SECRETASE. RX PubMed=16816112; DOI=10.1096/fj.05-5632com; RA Sun X., He G., Song W.; RT "BACE2, as a novel APP theta-secretase, is not responsible for the RT pathogenesis of Alzheimer's disease in Down syndrome."; RL FASEB J. 20:1369-1376(2006). RN [35] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP751). RC TISSUE=Brain; RX PubMed=2569763; DOI=10.1126/science.2569763; RA de Sauvage F., Octave J.-N.; RT "A novel mRNA of the A4 amyloid precursor gene coding for a possibly RT secreted protein."; RL Science 245:651-653(1989). RN [36] RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695). RC TISSUE=Brain; RX PubMed=3035574; DOI=10.1073/pnas.84.12.4190; RA Robakis N.K., Ramakrishna N., Wolfe G., Wisniewski H.M.; RT "Molecular cloning and characterization of a cDNA encoding the RT cerebrovascular and the neuritic plaque amyloid peptides."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4190-4194(1987). RN [37] RP CHARACTERIZATION OF L-APP733, AND MUTAGENESIS OF SER-656. RX PubMed=7737970; DOI=10.1074/jbc.270.18.10388; RA Pangalos M.N., Efthimiopoulos S., Shioi J., Robakis N.K.; RT "The chondroitin sulfate attachment site of appican is formed by RT splicing out exon 15 of the amyloid precursor gene."; RL J. Biol. Chem. 270:10388-10391(1995). RN [38] RP FUNCTION OF BETA-AMYLOID PEPTIDE AS LIPID PEROXIDATION INHIBITOR, AND RP MUTAGENESIS OF MET-706. RX PubMed=9168929; DOI=10.1006/bbrc.1997.6547; RA Walter M.F., Mason P.E., Mason R.P.; RT "Alzheimer's disease amyloid beta peptide 25-35 inhibits lipid RT peroxidation as a result of its membrane interactions."; RL Biochem. Biophys. Res. Commun. 233:760-764(1997). RN [39] RP REVIEW ON FUNCTION OF BETA-AMYLOID AS ANTIOXIDANT. RX PubMed=11775062; DOI=10.1023/A:1012629603390; RA Kontush A.; RT "Alzheimer's amyloid-beta as a preventive antioxidant for brain RT lipoproteins."; RL Cell. Mol. Neurobiol. 21:299-315(2001). RN [40] RP IDENTITY OF APP WITH NEXIN-II. RX PubMed=2506449; DOI=10.1038/341144a0; RA Oltersdorf T., Fritz L.C., Schenk D.B., Lieberburg I., RA Johnson-Wood K.L., Beattie E.C., Ward P.J., Blacher R.W., Dovey H.F., RA Sinha S.; RT "The secreted form of the Alzheimer's amyloid precursor protein with RT the Kunitz domain is protease nexin-II."; RL Nature 341:144-147(1989). RN [41] RP PROTEASE-SPECIFICITY OF INHIBITOR DOMAIN. RX PubMed=1969731; DOI=10.1016/0006-291X(90)92084-D; RA Kido H., Fukutomi A., Schilling J., Wang Y., Cordell B., Katunuma N.; RT "Protease-specificity of Kunitz inhibitor domain of Alzheimer's RT disease amyloid protein precursor."; RL Biochem. Biophys. Res. Commun. 167:716-721(1990). RN [42] RP EXTRACELLULAR ZINC-BINDING DOMAIN. RX PubMed=8344894; RA Bush A.I., Multhaup G., Moir R.D., Williamson T.G., Small D.H., RA Rumble B., Pollwein P., Beyreuther K., Masters C.L.; RT "A novel zinc(II) binding site modulates the function of the beta A4 RT amyloid protein precursor of Alzheimer's disease."; RL J. Biol. Chem. 268:16109-16112(1993). RN [43] RP INTERACTION WITH G(O). RX PubMed=8446172; DOI=10.1038/362075a0; RA Nishimoto I., Okamoto T., Matsuura Y., Takahashi S., Okamoto T., RA Murayama Y., Ogata E.; RT "Alzheimer amyloid protein precursor complexes with brain GTP-binding RT protein G(o)."; RL Nature 362:75-79(1993). RN [44] RP EXTRACELLULAR COPPER-BINDING DOMAIN, AND MUTAGENESIS OF HIS-137; RP MET-141; CYS-144; HIS-147 AND HIS-151. RX PubMed=7913895; DOI=10.1016/0014-5793(94)00658-X; RA Hesse L., Beher D., Masters C.L., Multhaup G.; RT "The beta A4 amyloid precursor protein binding to copper."; RL FEBS Lett. 349:109-116(1994). RN [45] RP N-TERMINAL HEPARIN-BINDING DOMAIN, AND MUTAGENESIS OF 99-LYS--ARG-102. RX PubMed=8158260; RA Small D.H., Nurcombe V., Reed G., Clarris H., Moir R., Beyreuther K., RA Masters C.L.; RT "A heparin-binding domain in the amyloid protein precursor of RT Alzheimer's disease is involved in the regulation of neurite RT outgrowth."; RL J. Neurosci. 14:2117-2127(1994). RN [46] RP MUTAGENESIS OF VAL-717. RX PubMed=8886002; DOI=10.1006/bbrc.1996.1577; RA Maruyama K., Tomita T., Shinozaki K., Kume H., Asada H., Saido T.C., RA Ishiura S., Iwatsubo T., Obata K.; RT "Familial Alzheimer's disease-linked mutations at Val717 of amyloid RT precursor protein are specific for the increased secretion of A beta RT 42(43)."; RL Biochem. Biophys. Res. Commun. 227:730-735(1996). RN [47] RP INTERACTION WITH APP-BP1. RX PubMed=8626687; DOI=10.1074/jbc.271.19.11339; RA Chow N., Korenberg J.R., Chen X.-N., Neve R.L.; RT "APP-BP1, a novel protein that binds to the carboxyl-terminal region RT of the amyloid precursor protein."; RL J. Biol. Chem. 271:11339-11346(1996). RN [48] RP INTERACTION WITH APBA1 AND APBB1, AND MUTAGENESIS OF TYR-728; TYR-757; RP ASN-759 AND TYR-762. RX PubMed=8887653; RA Borg J.-P., Ooi J., Levy E., Margolis B.; RT "The phosphotyrosine interaction domains of X11 and FE65 bind to RT distinct sites on the YENPTY motif of amyloid precursor protein."; RL Mol. Cell. Biol. 16:6229-6241(1996). RN [49] RP INTERACTION WITH APBB2. RX PubMed=8855266; DOI=10.1073/pnas.93.20.10832; RA Guenette S.Y., Chen J., Jondro P.D., Tanzi R.E.; RT "Association of a novel human FE65-like protein with the cytoplasmic RT domain of the beta-amyloid precursor protein."; RL Proc. Natl. Acad. Sci. U.S.A. 93:10832-10837(1996). RN [50] RP HEPARIN-BINDING DOMAINS. RX PubMed=9357988; DOI=10.1016/S0014-5793(97)01146-0; RA Mok S.S., Sberna G., Heffernan D., Cappai R., Galatis D., RA Clarris H.J., Sawyer W.H., Beyreuther K., Masters C.L., Small D.H.; RT "Expression and analysis of heparin-binding regions of the amyloid RT precursor protein of Alzheimer's disease."; RL FEBS Lett. 415:303-307(1997). RN [51] RP INTERACTION OF BETA-AMYLOID PEPTIDE WITH HADH2. RC TISSUE=Brain; RX PubMed=9338779; DOI=10.1038/39522; RA Yan S.D., Fu J., Soto C., Chen X., Zhu H., Al-Mohanna F., RA Collinson K., Zhu A., Stern E., Saido T., Tohyama M., Ogawa S., RA Roher A., Stern D.; RT "An intracellular protein that binds amyloid-beta peptide and mediates RT neurotoxicity in Alzheimer's disease."; RL Nature 389:689-695(1997). RN [52] RP INTERACTION WITH APPBP2, AND MUTAGENESIS OF TYR-728. RX PubMed=9843960; DOI=10.1073/pnas.95.25.14745; RA Zheng P., Eastman J., Vande Pol S., Pimplikar S.W.; RT "PAT1, a microtubule-interacting protein, recognizes the basolateral RT sorting signal of amyloid precursor protein."; RL Proc. Natl. Acad. Sci. U.S.A. 95:14745-14750(1998). RN [53] RP BETA-AMYLOID ZINC-BINDING, AND MUTAGENESIS OF ARG-676; TYR-681 AND RP HIS-684. RX PubMed=10413512; DOI=10.1021/bi990205o; RA Liu S.T., Howlett G., Barrow C.J.; RT "Histidine-13 is a crucial residue in the zinc ion-induced aggregation RT of the A beta peptide of Alzheimer's disease."; RL Biochemistry 38:9373-9378(1999). RN [54] RP IMPORTANCE OF MET-706 IN FREE RADICAL OXIDATIVE STRESS, AND RP MUTAGENESIS OF MET-706. RX PubMed=10535332; DOI=10.1016/S0361-9230(99)00093-3; RA Varadarajan S., Yatin S., Kanski J., Jahanshahi F., Butterfield D.A.; RT "Methionine residue 35 is important in amyloid beta-peptide-associated RT free radical oxidative stress."; RL Brain Res. Bull. 50:133-141(1999). RN [55] RP INTERACTION WITH APBA2. RX PubMed=9890987; DOI=10.1074/jbc.274.4.2243; RA Tomita S., Ozaki T., Taru H., Oguchi S., Takeda S., Yagi Y., RA Sakiyama S., Kirino Y., Suzuki T.; RT "Interaction of a neuron-specific protein containing PDZ domains with RT Alzheimer's amyloid precursor protein."; RL J. Biol. Chem. 274:2243-2254(1999). RN [56] RP ENDOCYTOSIS SIGNAL, AND MUTAGENESIS OF TYR-728; GLY-756; TYR-757; RP ASN-759; PRO-760 AND TYR-762. RX PubMed=10383380; DOI=10.1074/jbc.274.27.18851; RA Perez R.G., Soriano S., Hayes J.D., Ostaszewski B., Xia W., RA Selkoe D.J., Chen X., Stokin G.B., Koo E.H.; RT "Mutagenesis identifies new signals for beta-amyloid precursor protein RT endocytosis, turnover, and the generation of secreted fragments, RT including Abeta42."; RL J. Biol. Chem. 274:18851-18856(1999). RN [57] RP IMPORTANCE OF CYS-144 IN COPPER REDUCTION, AND MUTAGENESIS OF CYS-144 RP AND 147-HIS--HIS-149. RX PubMed=10461923; DOI=10.1046/j.1471-4159.1999.0731288.x; RA Ruiz F.H., Gonzalez M., Bodini M., Opazo C., Inestrosa N.C.; RT "Cysteine 144 is a key residue in the copper reduction by the beta- RT amyloid precursor protein."; RL J. Neurochem. 73:1288-1292(1999). RN [58] RP INTERACTION OF BETA-AMYLOID WITH APOE. RX PubMed=10816430; DOI=10.1042/0264-6021:3480359; RA Tokuda T., Calero M., Matsubara E., Vidal R., Kumar A., Permanne B., RA Zlokovic B., Smith J.D., Ladu M.J., Rostagno A., Frangione B., RA Ghiso J.; RT "Lipidation of apolipoprotein E influences its isoform-specific RT interaction with Alzheimer's amyloid beta peptides."; RL Biochem. J. 348:359-365(2000). RN [59] RP INTERACTION OF BETA-APP42 WITH CHRNA7. RX PubMed=10681545; DOI=10.1074/jbc.275.8.5626; RA Wang H.-Y., Lee D.H.S., D'Andrea M.R., Peterson P.A., Shank R.P., RA Reitz A.B.; RT "Beta-amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor RT with high affinity. Implications for Alzheimer's disease pathology."; RL J. Biol. Chem. 275:5626-5632(2000). RN [60] RP IDENTIFICATION OF GAMMA-CTFS BY MASS SPECTROMETRY, AND MUTAGENESIS OF RP ASP-739. RX PubMed=12214090; RA Passer B., Pellegrini L., Russo C., Siegel R.M., Lenardo M.J., RA Schettini G., Bachmann M., Tabaton M., D'Adamio L.; RT "Generation of an apoptotic intracellular peptide by gamma-secretase RT cleavage of Alzheimer's amyloid beta protein precursor."; RL J. Alzheimers Dis. 2:289-301(2000). RN [61] RP INTERACTION WITH FPRL1. RX PubMed=11689470; DOI=10.1096/fj.01-0251com; RA Yazawa H., Yu Z.-X., Takeda K., Le Y., Gong W., Ferrans V.J., RA Oppenheim J.J., Li C.C.H., Wang J.M.; RT "Beta amyloid peptide (Abeta42) is internalized via the G-protein- RT coupled receptor FPRL1 and forms fibrillar aggregates in RT macrophages."; RL FASEB J. 15:2454-2462(2001). RN [62] RP INTERACTION WITH BBP. RX PubMed=11278849; DOI=10.1074/jbc.M011161200; RA Kajkowski E.M., Lo C.F., Ning X., Walker S., Sofia H.J., Wang W., RA Edris W., Chanda P., Wagner E., Vile S., Ryan K., McHendry-Rinde B., RA Smith S.C., Wood A., Rhodes K.J., Kennedy J.D., Bard J., RA Jacobsen J.S., Ozenberger B.A.; RT "Beta-amyloid peptide-induced apoptosis regulated by a novel protein RT containing a G protein activation module."; RL J. Biol. Chem. 276:18748-18756(2001). RN [63] RP BETA-AMYLOID COPPER AND ZINC-BINDING. RX PubMed=11274207; DOI=10.1074/jbc.M100175200; RA Curtain C.C., Ali F., Volitakis I., Cherny R.A., Norton R.S., RA Beyreuther K., Barrow C.J., Masters C.L., Bush A.I., Barnham K.J.; RT "Alzheimer's disease amyloid-beta binds copper and zinc to generate an RT allosterically ordered structure containing superoxide dismutase-like RT subunits."; RL J. Biol. Chem. 276:20466-20473(2001). RN [64] RP SUBUNIT. RX PubMed=11438549; DOI=10.1074/jbc.M105410200; RA Scheuermann S., Hambsch B., Hesse L., Stumm J., Schmidt C., Beher D., RA Bayer T.A., Beyreuther K., Multhaup G.; RT "Homodimerization of amyloid precursor protein and its implication in RT the amyloidogenic pathway of Alzheimer's disease."; RL J. Biol. Chem. 276:33923-33929(2001). RN [65] RP INTERACTION WITH APBB1, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11544248; DOI=10.1074/jbc.C100447200; RA Kimberly W.T., Zheng J.B., Guenette S.Y., Selkoe D.J.; RT "The intracellular domain of the beta-amyloid precursor protein is RT stabilized by Fe65 and translocates to the nucleus in a notch-like RT manner."; RL J. Biol. Chem. 276:40288-40292(2001). RN [66] RP INTERACTION WITH FBLN1. RX PubMed=11238726; DOI=10.1046/j.1471-4159.2001.00144.x; RA Ohsawa I., Takamura C., Kohsaka S.; RT "Fibulin-1 binds the amino-terminal head of beta-amyloid precursor RT protein and modulates its physiological function."; RL J. Neurochem. 76:1411-1420(2001). RN [67] RP INTERACTION WITH MAPT, AND FUNCTION. RX PubMed=11943163; DOI=10.1016/S0014-5793(02)02376-1; RA Rank K.B., Pauley A.M., Bhattacharya K., Wang Z., Evans D.B., RA Fleck T.J., Johnston J.A., Sharma S.K.; RT "Direct interaction of soluble human recombinant tau protein with RT Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau RT protein kinase II."; RL FEBS Lett. 514:263-268(2002). RN [68] RP INTERACTION WITH MAPK8IP1, AND MUTAGENESIS OF TYR-757. RX PubMed=11724784; DOI=10.1074/jbc.M108357200; RA Scheinfeld M.H., Roncarati R., Vito P., Lopez P.A., Abdallah M., RA D'Adamio L.; RT "Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the RT cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein RT (APP)."; RL J. Biol. Chem. 277:3767-3775(2002). RN [69] RP COPPER-MEDIATED LIPID PEROXIDATION, AND MUTAGENESIS OF HIS-147 AND RP HIS-151. RX PubMed=11784781; RA White A.R., Multhaup G., Galatis D., McKinstry W.J., Parker M.W., RA Pipkorn R., Beyreuther K., Masters C.L., Cappai R.; RT "Contrasting species-dependent modulation of copper-mediated RT neurotoxicity by the Alzheimer's disease amyloid precursor protein."; RL J. Neurosci. 22:365-376(2002). RN [70] RP REVIEW ON ZINC-BINDING. RX PubMed=12032279; DOI=10.1073/pnas.122249699; RA Bush A.I., Tanzi R.E.; RT "The galvanization of beta-amyloid in Alzheimer's disease."; RL Proc. Natl. Acad. Sci. U.S.A. 99:7317-7319(2002). RN [71] RP SUBCELLULAR LOCATION, AND ASSOCIATION OF AMYLOID FIBRILS WITH GCP1. RX PubMed=15084524; DOI=10.1096/fj.03-1040fje; RA Watanabe N., Araki W., Chui D.H., Makifuchi T., Ihara Y., Tabira T.; RT "Glypican-1 as an Abeta binding HSPG in the human brain: its RT localization in DIG domains and possible roles in the pathogenesis of RT Alzheimer's disease."; RL FASEB J. 18:1013-1015(2004). RN [72] RP INTERACTION WITH ANKS1B. RX PubMed=15347684; DOI=10.1074/jbc.M405329200; RA Ghersi E., Noviello C., D'Adamio L.; RT "Amyloid-beta protein precursor (AbetaPP) intracellular domain- RT associated protein-1 proteins bind to AbetaPP and modulate its RT processing in an isoform-specific manner."; RL J. Biol. Chem. 279:49105-49112(2004). RN [73] RP PHOSPHORYLATION AT THR-743. RX PubMed=8131745; RA Suzuki T., Oishi M., Marshak D.R., Czernik A.J., Nairn A.C., RA Greengard P.; RT "Cell cycle-dependent regulation of the phosphorylation and metabolism RT of the Alzheimer amyloid precursor protein."; RL EMBO J. 13:1114-1122(1994). RN [74] RP PHOSPHORYLATION AT SER-198 AND SER-206 BY CASEIN KINASES, AND RP MUTAGENESIS OF SER-198 AND SER-206. RX PubMed=8999878; DOI=10.1074/jbc.272.3.1896; RA Walter J., Capell A., Hung A.Y., Langen H., Schnoelzer M., RA Thinakaran G., Sisodia S.S., Selkoe D.J., Haass C.; RT "Ectodomain phosphorylation of beta-amyloid precursor protein at two RT distinct cellular locations."; RL J. Biol. Chem. 272:1896-1903(1997). RN [75] RP COPPER-BINDING, AND DISULFIDE BOND FORMATION. RX PubMed=9585534; DOI=10.1021/bi980022m; RA Multhaup G., Ruppert T., Schlicksupp A., Hesse L., Bill E., RA Pipkorn R., Masters C.L., Beyreuther K.; RT "Copper-binding amyloid precursor protein undergoes a site-specific RT fragmentation in the reduction of hydrogen peroxide."; RL Biochemistry 37:7224-7230(1998). RN [76] RP CLEAVAGE BY CASPASES, AND MUTAGENESIS OF ASP-739. RX PubMed=10319819; DOI=10.1016/S0092-8674(00)80748-5; RA Gervais F.G., Xu D., Robertson G.S., Vaillancourt J.P., Zhu Y., RA Huang J., LeBlanc A., Smith D., Rigby M., Shearman M.S., Clarke E.E., RA Zheng H., van der Ploeg L.H.T., Ruffolo S.C., Thornberry N.A., RA Xanthoudakis S., Zamboni R.J., Roy S., Nicholson D.W.; RT "Involvement of caspases in proteolytic cleavage of Alzheimer's RT amyloid-beta precursor protein and amyloidogenic A beta peptide RT formation."; RL Cell 97:395-406(1999). RN [77] RP PHOSPHORYLATION, AND MUTAGENESIS OF THR-743. RX PubMed=10341243; RA Ando K., Oishi M., Takeda S., Iijima K., Isohara T., Nairn A.C., RA Kirino Y., Greengard P., Suzuki T.; RT "Role of phosphorylation of Alzheimer's amyloid precursor protein RT during neuronal differentiation."; RL J. Neurosci. 19:4421-4427(1999). RN [78] RP CHARACTERIZATION OF CASEIN KINASE PHOSPHORYLATION, AND MUTAGENESIS OF RP SER-198 AND SER-206. RX PubMed=10806211; DOI=10.1074/jbc.M002850200; RA Walter J., Schindzielorz A., Hartung B., Haass C.; RT "Phosphorylation of the beta-amyloid precursor protein at the cell RT surface by ectocasein kinases 1 and 2."; RL J. Biol. Chem. 275:23523-23529(2000). RN [79] RP CLEAVAGE BY CASPASES, AND MUTAGENESIS OF ASP-739. RX PubMed=10742146; DOI=10.1038/74656; RA Lu D.C., Rabizadeh S., Chandra S., Shayya R.F., Ellerby L.M., Ye X., RA Salvesen G.S., Koo E.H., Bredesen D.E.; RT "A second cytotoxic proteolytic peptide derived from amyloid beta- RT protein precursor."; RL Nat. Med. 6:397-404(2000). RN [80] RP PHOSPHORYLATION, INTERACTION WITH APBB1, AND MUTAGENESIS OF THR-743. RX PubMed=11517218; DOI=10.1074/jbc.M104059200; RA Ando K., Iijima K., Elliott J.I., Kirino Y., Suzuki T.; RT "Phosphorylation-dependent regulation of the interaction of amyloid RT precursor protein with Fe65 affects the production of beta-amyloid."; RL J. Biol. Chem. 276:40353-40361(2001). RN [81] RP PHOSPHORYLATION BY MAPK10, AND MUTAGENESIS OF THR-743. RX PubMed=11146006; DOI=10.1046/j.1471-4159.2001.00102.x; RA Standen C.L., Brownlees J., Grierson A.J., Kesavapany S., Lau K.-F., RA McLoughlin D.M., Miller C.C.J.; RT "Phosphorylation of thr(668) in the cytoplasmic domain of the RT Alzheimer's disease amyloid precursor protein by stress-activated RT protein kinase 1b (Jun N-terminal kinase-3)."; RL J. Neurochem. 76:316-320(2001). RN [82] RP CLEAVAGE AT LEU-720. RX PubMed=11851430; DOI=10.1021/bi015794o; RA Weidemann A., Eggert S., Reinhard F.B.M., Vogel M., Paliga K., RA Baier G., Masters C.L., Beyreuther K., Evin G.; RT "A novel epsilon-cleavage within the transmembrane domain of the RT Alzheimer amyloid precursor protein demonstrates homology with Notch RT processing."; RL Biochemistry 41:2825-2835(2002). RN [83] RP PHOSPHORYLATION AT TYR-757, INTERACTION WITH SHC1, AND MUTAGENESIS OF RP THR-743 AND TYR-757. RX PubMed=11877420; DOI=10.1074/jbc.M110286200; RA Tarr P.E., Roncarati R., Pelicci G., Pelicci P.G., D'Adamio L.; RT "Tyrosine phosphorylation of the beta-amyloid precursor protein RT cytoplasmic tail promotes interaction with Shc."; RL J. Biol. Chem. 277:16798-16804(2002). RN [84] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-542. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [85] RP SIGNAL SEQUENCE CLEAVAGE SITE, AND TOPOLOGY. RX PubMed=2900137; RA Dyrks T., Weidemann A., Multhaup G., Salbaum J.M., Lemaire H.-G., RA Kang J., Mueller-Hill B., Masters C.L., Beyreuther K.; RT "Identification, transmembrane orientation and biogenesis of the RT amyloid A4 precursor of Alzheimer's disease."; RL EMBO J. 7:949-957(1988). RN [86] RP REVIEW. RX PubMed=12142279; DOI=10.1146/annurev.cellbio.18.020402.142302; RA Annaert W., De Strooper B.; RT "A cell biological perspective on Alzheimer's disease."; RL Annu. Rev. Cell Dev. Biol. 18:25-51(2002). RN [87] RP INTERACTION WITH SORL1, AND SUBCELLULAR LOCATION. RX PubMed=16174740; DOI=10.1073/pnas.0503689102; RA Andersen O.M., Reiche J., Schmidt V., Gotthardt M., Spoelgen R., RA Behlke J., von Arnim C.A., Breiderhoff T., Jansen P., Wu X., RA Bales K.R., Cappai R., Masters C.L., Gliemann J., Mufson E.J., RA Hyman B.T., Paul S.M., Nykjaer A., Willnow T.E.; RT "Neuronal sorting protein-related receptor sorLA/LR11 regulates RT processing of the amyloid precursor protein."; RL Proc. Natl. Acad. Sci. U.S.A. 102:13461-13466(2005). RN [88] RP INTERACTION WITH APBB1. RX PubMed=18468999; DOI=10.1074/jbc.M801827200; RA Nakaya T., Kawai T., Suzuki T.; RT "Regulation of FE65 nuclear translocation and function by amyloid RT beta-protein precursor in osmotically stressed cells."; RL J. Biol. Chem. 283:19119-19131(2008). RN [89] RP INTERACTION WITH ITM2C. RX PubMed=19366692; DOI=10.1074/jbc.M109.006403; RA Matsuda S., Matsuda Y., D'Adamio L.; RT "BRI3 inhibits amyloid precursor protein processing in a RT mechanistically distinct manner from its homologue dementia gene RT BRI2."; RL J. Biol. Chem. 284:15815-15825(2009). RN [90] RP FUNCTION, CLEAVAGE, AND INTERACTION WITH TNFRSF21. RX PubMed=19225519; DOI=10.1038/nature07767; RA Nikolaev A., McLaughlin T., O'Leary D.D.M., Tessier-Lavigne M.; RT "APP binds DR6 to trigger axon pruning and neuron death via distinct RT caspases."; RL Nature 457:981-989(2009). RN [91] RP FUNCTION, AND INTERACTION WITH AGER. RX PubMed=19901339; DOI=10.1073/pnas.0905686106; RA Takuma K., Fang F., Zhang W., Yan S., Fukuzaki E., Du H., Sosunov A., RA McKhann G., Funatsu Y., Nakamichi N., Nagai T., Mizoguchi H., Ibi D., RA Hori O., Ogawa S., Stern D.M., Yamada K., Yan S.S.; RT "RAGE-mediated signaling contributes to intraneuronal transport of RT amyloid-{beta} and neuronal dysfunction."; RL Proc. Natl. Acad. Sci. U.S.A. 106:20021-20026(2009). RN [92] RP INTERACTION WITH GSAP. RX PubMed=20811458; DOI=10.1038/nature09325; RA He G., Luo W., Li P., Remmers C., Netzer W.J., Hendrick J., RA Bettayeb K., Flajolet M., Gorelick F., Wennogle L.P., Greengard P.; RT "Gamma-secretase activating protein is a therapeutic target for RT Alzheimer's disease."; RL Nature 467:95-98(2010). RN [93] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [94] RP GLYCOSYLATION AT THR-633; THR-651; THR-652; SER-656; THR-663 AND RP SER-667 PROTEOLYTIC PROCESSING, STRUCTURE OF CARBOHYDRATES, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=21712440; DOI=10.1073/pnas.1102664108; RA Halim A., Brinkmalm G., Ruetschi U., Westman-Brinkmalm A., RA Portelius E., Zetterberg H., Blennow K., Larson G., Nilsson J.; RT "Site-specific characterization of threonine, serine, and tyrosine RT glycosylations of amyloid precursor protein/amyloid beta-peptides in RT human cerebrospinal fluid."; RL Proc. Natl. Acad. Sci. U.S.A. 108:11848-11853(2011). RN [95] RP INTERACTION WITH S100A9. RX PubMed=22457725; DOI=10.1371/journal.pone.0032953; RA Zhang C., Liu Y., Gilthorpe J., van der Maarel J.R.; RT "MRP14 (S100A9) protein interacts with Alzheimer beta-amyloid peptide RT and induces its fibrillization."; RL PLoS ONE 7:E32953-E32953(2012). RN [96] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 287-344. RX PubMed=2125487; DOI=10.1021/bi00495a002; RA Hynes T.R., Randal M., Kennedy L.A., Eigenbrot C., Kossiakof A.A.; RT "X-ray crystal structure of the protease inhibitor domain of RT Alzheimer's amyloid beta-protein precursor."; RL Biochemistry 29:10018-10022(1990). RN [97] RP STRUCTURE BY NMR OF 289-344. RX PubMed=1718421; DOI=10.1021/bi00107a015; RA Heald S.L., Tilton R.F. Jr., Hammond L.S., Lee A., Bayney R.M., RA Kamarck M.E., Ramabhadran T.V., Dreyer R.N., Davis G., Unterbeck A., RA Tamburini P.P.; RT "Sequential NMR resonance assignment and structure determination of RT the Kunitz-type inhibitor domain of the Alzheimer's beta-amyloid RT precursor protein."; RL Biochemistry 30:10467-10478(1991). RN [98] RP STRUCTURE BY NMR OF 672-699. RX PubMed=7516706; DOI=10.1021/bi00191a006; RA Talafous J., Marcinowski K.J., Klopman G., Zagorski M.G.; RT "Solution structure of residues 1-28 of the amyloid beta-peptide."; RL Biochemistry 33:7788-7796(1994). RN [99] RP STRUCTURE BY NMR OF 672-711. RX PubMed=7588758; DOI=10.1111/j.1432-1033.1995.293_1.x; RA Sticht H., Bayer P., Willbold D., Dames S., Hilbich C., Beyreuther K., RA Frank R.W., Rosch P.; RT "Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease."; RL Eur. J. Biochem. 233:293-298(1995). RN [100] RP STRUCTURE BY NMR OF 696-706. RX PubMed=8973180; DOI=10.1021/bi961598j; RA Kohno T., Kobayashi K., Maeda T., Sato K., Takashima A.; RT "Three-dimensional structures of the amyloid beta peptide (25-35) in RT membrane-mimicking environment."; RL Biochemistry 35:16094-16104(1996). RN [101] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF KUNITZ DOMAIN IN COMPLEX WITH RP CHYMOTRYPSIN; TRYPSIN AND BASIC PANCREATIC TRYPSIN INHIBITOR. RX PubMed=9300481; DOI=10.1002/pro.5560060902; RA Scheidig A.J., Hynes T.R., Pelletier L.A., Wells J.A., RA Kossiakoff A.A.; RT "Crystal structures of bovine chymotrypsin and trypsin complexed to RT the inhibitor domain of Alzheimer's amyloid beta-protein precursor RT (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of RT inhibitors with altered specificities."; RL Protein Sci. 6:1806-1824(1997). RN [102] RP STRUCTURE BY NMR OF 672-711. RX PubMed=9693002; DOI=10.1021/bi972979f; RA Coles M., Bicknell W., Watson A.A., Fairlie D.P., Craik D.J.; RT "Solution structure of amyloid beta-peptide(1-40) in a water-micelle RT environment. Is the membrane-spanning domain where we think it is?"; RL Biochemistry 37:11064-11077(1998). RN [103] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 28-123. RX PubMed=10201399; DOI=10.1038/7562; RA Rossjohn J., Cappai R., Feil S.C., Henry A., McKinstry W.J., RA Galatis D., Hesse L., Multhaup G., Beyreuther K., Masters C.L., RA Parker M.W.; RT "Crystal structure of the N-terminal, growth factor-like domain of RT Alzheimer amyloid precursor protein."; RL Nat. Struct. Biol. 6:327-331(1999). RN [104] RP STRUCTURE OF CAA-APP VARIANTS. RX PubMed=10821838; DOI=10.1074/jbc.M003154200; RA Miravalle L., Tokuda T., Chiarle R., Giaccone G., Bugiani O., RA Tagliavini F., Frangione B., Ghiso J.; RT "Substitutions at codon 22 of Alzheimer's Abeta peptide induce diverse RT conformational changes and apoptotic effects in human cerebral RT endothelial cells."; RL J. Biol. Chem. 275:27110-27116(2000). RN [105] RP STRUCTURE BY NMR OF 681-706. RX PubMed=10940221; DOI=10.1006/jsbi.2000.4288; RA Zhang S., Iwata K., Lachenmann M.J., Peng J.W., Li S., Stimson E.R., RA Lu Y., Felix A.M., Maggio J.E., Lee J.P.; RT "The Alzheimer's peptide a beta adopts a collapsed coil structure in RT water."; RL J. Struct. Biol. 130:130-141(2000). RN [106] RP STRUCTURE BY NMR OF 672-699. RX PubMed=10940222; DOI=10.1006/jsbi.2000.4267; RA Poulsen S.-A., Watson A.A., Craik D.J.; RT "Solution structures in aqueous SDS micelles of two amyloid beta RT peptides of Abeta(1-28) mutated at the alpha-secretase cleavage RT site."; RL J. Struct. Biol. 130:142-152(2000). RN [107] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 346-551, PARTIAL PROTEIN RP SEQUENCE, MUTAGENESIS OF ARG-499 AND LYS-503, AND IDENTIFICATION BY RP MASS SPECTROMETRY. RX PubMed=15304215; DOI=10.1016/j.molcel.2004.06.037; RA Wang Y., Ha Y.; RT "The X-ray structure of an antiparallel dimer of the human amyloid RT precursor protein E2 domain."; RL Mol. Cell 15:343-353(2004). RN [108] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 672-711 IN COMPLEX WITH IDE. RX PubMed=17051221; DOI=10.1038/nature05143; RA Shen Y., Joachimiak A., Rosner M.R., Tang W.-J.; RT "Structures of human insulin-degrading enzyme reveal a new substrate RT recognition mechanism."; RL Nature 443:870-874(2006). RN [109] RP X-RAY CRYSTALLOGRAPHY (0.85 ANGSTROMS) OF 133-189, AND DISULFIDE RP BONDS. RX PubMed=17909280; DOI=10.1107/S1744309107041139; RA Kong G.K., Adams J.J., Cappai R., Parker M.W.; RT "Structure of Alzheimer's disease amyloid precursor protein copper- RT binding domain at atomic resolution."; RL Acta Crystallogr. F 63:819-824(2007). RN [110] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 133-189 IN COMPLEXES WITH RP COPPER IONS, AND DISULFIDE BONDS. RX PubMed=17239395; DOI=10.1016/j.jmb.2006.12.041; RA Kong G.K., Adams J.J., Harris H.H., Boas J.F., Curtain C.C., RA Galatis D., Masters C.L., Barnham K.J., McKinstry W.J., Cappai R., RA Parker M.W.; RT "Structural studies of the Alzheimer's amyloid precursor protein RT copper-binding domain reveal how it binds copper ions."; RL J. Mol. Biol. 367:148-161(2007). RN [111] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 672-679 IN COMPLEX WITH IGG. RX PubMed=17895381; DOI=10.1073/pnas.0705888104; RA Gardberg A.S., Dice L.T., Ou S., Rich R.L., Helmbrecht E., Ko J., RA Wetzel R., Myszka D.G., Patterson P.H., Dealwis C.; RT "Molecular basis for passive immunotherapy of Alzheimer's disease."; RL Proc. Natl. Acad. Sci. U.S.A. 104:15659-15664(2007). RN [112] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 672-678 IN COMPLEXES WITH RP ANTIBODY FAB FRAGMENTS. RX PubMed=19923222; DOI=10.1074/jbc.M109.045187; RA Basi G.S., Feinberg H., Oshidari F., Anderson J., Barbour R., RA Baker J., Comery T.A., Diep L., Gill D., Johnson-Wood K., Goel A., RA Grantcharova K., Lee M., Li J., Partridge A., Griswold-Prenner I., RA Piot N., Walker D., Widom A., Pangalos M.N., Seubert P., RA Jacobsen J.S., Schenk D., Weis W.I.; RT "Structural correlates of antibodies associated with acute reversal of RT amyloid beta-related behavioral deficits in a mouse model of Alzheimer RT disease."; RL J. Biol. Chem. 285:3417-3427(2010). RN [113] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 18-190, PARTIAL PROTEIN RP SEQUENCE, SUBUNIT, DISULFIDE BONDS, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=20212142; DOI=10.1073/pnas.0911326107; RA Dahms S.O., Hoefgen S., Roeser D., Schlott B., Guhrs K.H., Than M.E.; RT "Structure and biochemical analysis of the heparin-induced E1 dimer of RT the amyloid precursor protein."; RL Proc. Natl. Acad. Sci. U.S.A. 107:5381-5386(2010). RN [114] RP REVIEW ON VARIANTS. RX PubMed=1363811; DOI=10.1038/ng0792-233; RA Hardy J.; RT "Framing beta-amyloid."; RL Nat. Genet. 1:233-234(1992). RN [115] RP VARIANT CAA-APP GLN-693. RX PubMed=2111584; DOI=10.1126/science.2111584; RA Levy E., Carman M.D., Fernandez-Madrid I.J., Power M.D., RA Lieberburg I., van Duinen S.G., Bots G.T.A.M., Luyendijk W., RA Frangione B.; RT "Mutation of the Alzheimer's disease amyloid gene in hereditary RT cerebral hemorrhage, Dutch type."; RL Science 248:1124-1126(1990). RN [116] RP VARIANT AD1 ILE-717. RX PubMed=1671712; DOI=10.1038/349704a0; RA Goate A., Chartier-Harlin M.-C., Mullan M., Brown J., Crawford F., RA Fidani L., Giuffra L., Haynes A., Irving N., James L., Mant R., RA Newton P., Rooke K., Roques P., Talbot C., Pericak-Vance M., RA Roses A.D., Williamson R., Rossor M., Owen M., Hardy J.; RT "Segregation of a missense mutation in the amyloid precursor protein RT gene with familial Alzheimer's disease."; RL Nature 349:704-706(1991). RN [117] RP VARIANT AD1 ILE-717. RX PubMed=1908231; DOI=10.1016/0006-291X(91)91011-Z; RA Yoshioka K., Miki T., Katsuya T., Ogihara T., Sakaki Y.; RT "The 717Val-->Ile substitution in amyloid precursor protein is RT associated with familial Alzheimer's disease regardless of ethnic RT groups."; RL Biochem. Biophys. Res. Commun. 178:1141-1146(1991). RN [118] RP VARIANT AD1 ILE-717. RX PubMed=1678058; DOI=10.1016/0140-6736(91)91612-X; RA Naruse S., Igarashi S., Kobayashi H., Aoki K., Inuzuka T., Kaneko K., RA Shimizu T., Iihara K., Kojima T., Miyatake T., Tsuji S.; RT "Mis-sense mutation Val->Ile in exon 17 of amyloid precursor protein RT gene in Japanese familial Alzheimer's disease."; RL Lancet 337:978-979(1991). RN [119] RP VARIANT AD1 GLY-717. RX PubMed=1944558; DOI=10.1038/353844a0; RA Chartier-Harlin M.-C., Crawford F., Houlden H., Warren A., Hughes D., RA Fidani L., Goate A., Rossor M., Roques P., Hardy J., Mullan M.; RT "Early-onset Alzheimer's disease caused by mutations at codon 717 of RT the beta-amyloid precursor protein gene."; RL Nature 353:844-846(1991). RN [120] RP VARIANT AD1 PHE-717. RX PubMed=1925564; DOI=10.1126/science.1925564; RA Murrell J.R., Farlow M., Ghetti B., Benson M.D.; RT "A mutation in the amyloid precursor protein associated with RT hereditary Alzheimer's disease."; RL Science 254:97-99(1991). RN [121] RP VARIANT AD1 GLY-693. RX PubMed=1415269; RA Kamino K., Orr H.T., Payami H., Wijsman E.M., Alonso M.E., Pulst S.M., RA Anderson L., O'Dahl S., Nemens E., White J.A., Sadovnick A.D., RA Ball M.J., Kaye J., Warren A., McInnis M.G., Antonarakis S.E., RA Korenberg J.R., Sharma V., Kukull W., Larson E., Heston L.L., RA Martin G.M., Bird T.D., Schellenberg G.D.; RT "Linkage and mutational analysis of familial Alzheimer disease RT kindreds for the APP gene region."; RL Am. J. Hum. Genet. 51:998-1014(1992). RN [122] RP VARIANT AD1 GLY-692. RX PubMed=1303239; DOI=10.1038/ng0692-218; RA Hendriks L., van Duijn C.M., Cras P., Cruts M., Van Hul W., RA van Harskamp F., Warren A., McInnis M.G., Antonarakis S.E., RA Martin J.J., Hofman A., Van Broeckhoven C.; RT "Presenile dementia and cerebral haemorrhage linked to a mutation at RT codon 692 of the beta-amyloid precursor protein gene."; RL Nat. Genet. 1:218-221(1992). RN [123] RP VARIANT AD1 670-ASN-LEU-671. RX PubMed=1302033; DOI=10.1038/ng0892-345; RA Mullan M., Crawford F., Axelman K., Houlden H., Lilius L., Winblad B., RA Lannfelt L.; RT "A pathogenic mutation for probable Alzheimer's disease in the APP RT gene at the N-terminus of beta-amyloid."; RL Nat. Genet. 1:345-347(1992). RN [124] RP VARIANT VAL-713. RX PubMed=1307241; DOI=10.1038/ng0792-306; RA Jones C.T., Morris S., Yates C.M., Moffoot A., Sharpe C., RA Brock D.J.H., St Clair D.; RT "Mutation in codon 713 of the beta amyloid precursor protein gene RT presenting with schizophrenia."; RL Nat. Genet. 1:306-309(1992). RN [125] RP VARIANT AD1 THR-713. RX PubMed=1303275; DOI=10.1038/ng1292-255; RA Carter D.A., Desmarais E., Bellis M., Campion D., Clerget-Darpoux F., RA Brice A., Agid Y., Jaillard-Serradt A., Mallet J.; RT "More missense in amyloid gene."; RL Nat. Genet. 2:255-256(1992). RN [126] RP VARIANTS AD1 ILE-717 AND PHE-717. RX PubMed=8267572; DOI=10.1006/bbrc.1993.2491; RA Liepnieks J.J., Ghetti B., Farlow M., Roses A.D., Benson M.D.; RT "Characterization of amyloid fibril beta-peptide in familial RT Alzheimer's disease with APP717 mutations."; RL Biochem. Biophys. Res. Commun. 197:386-392(1993). RN [127] RP VARIANT ASP-665. RX PubMed=8154870; DOI=10.1002/ana.410350410; RA Peacock M.L., Murman D.L., Sima A.A.F., Warren J.T. Jr., Roses A.D., RA Fink J.K.; RT "Novel amyloid precursor protein gene mutation (codon 665Asp) in a RT patient with late-onset Alzheimer's disease."; RL Ann. Neurol. 35:432-438(1994). RN [128] RP VARIANT AD1 PHE-717. RX PubMed=8290042; DOI=10.1212/WNL.44.1.105; RA Farlow M., Murrell J., Ghetti B., Unverzagt F., Zeldenrust S., RA Benson M.D.; RT "Clinical characteristics in a kindred with early-onset Alzheimer's RT disease and their linkage to a G-->T change at position 2149 of the RT amyloid precursor protein gene."; RL Neurology 44:105-111(1994). RN [129] RP VARIANT AD1 ILE-717. RX PubMed=8577393; DOI=10.1016/0304-3940(95)12046-7; RA Brooks W.S., Martins R.N., De Voecht J., Nicholson G.A., RA Schofield P.R., Kwok J.B.J., Fisher C., Yeung L.U., RA Van Broeckhoven C.; RT "A mutation in codon 717 of the amyloid precursor protein gene in an RT Australian family with Alzheimer's disease."; RL Neurosci. Lett. 199:183-186(1995). RN [130] RP VARIANT AD1 VAL-716. RX PubMed=9328472; DOI=10.1093/hmg/6.12.2087; RA Eckman C.B., Mehta N.D., Crook R., Perez-Tur J., Prihar G., RA Pfeiffer E., Graff-Radford N., Hinder P., Yager D., Zenk B., RA Refolo L.M., Prada C.M., Younkin S.G., Hutton M., Hardy J.; RT "A new pathogenic mutation in the APP gene (I716V) increases the RT relative proportion of A beta 42(43)."; RL Hum. Mol. Genet. 6:2087-2089(1997). RN [131] RP VARIANT AD1 GLY-692, AND CHARACTERIZATION OF PHENOTYPE. RX PubMed=9754958; DOI=10.1007/s004010050892; RA Cras P., van Harskamp F., Hendriks L., Ceuterick C., van Duijn C.M., RA Stefanko S.Z., Hofman A., Kros J.M., Van Broeckhoven C., Martin J.J.; RT "Presenile Alzheimer dementia characterized by amyloid angiopathy and RT large amyloid core type senile plaques in the APP 692Ala-->Gly RT mutation."; RL Acta Neuropathol. 96:253-260(1998). RN [132] RP VARIANT AD1 MET-715, AND CHARACTERIZATION OF VARIANT AD1 MET-715. RX PubMed=10097173; DOI=10.1073/pnas.96.7.4119; RA Ancolio K., Dumanchin C., Barelli H., Warter J.-M., Brice A., RA Campion D., Frebourg T., Checler F.; RT "Unusual phenotypic alteration of beta amyloid precursor protein RT (betaAPP) maturation by a new Val-715 --> Met betaAPP-770 mutation RT responsible for probable early-onset Alzheimer's disease."; RL Proc. Natl. Acad. Sci. U.S.A. 96:4119-4124(1999). RN [133] RP VARIANT AD1 ILE-717. RX PubMed=10631141; DOI=10.1086/302702; RA Finckh U., Mueller-Thomsen T., Mann U., Eggers C., Marksteiner J., RA Meins W., Binetti G., Alberici A., Hock C., Nitsch R.M., Gal A.; RT "High prevalence of pathogenic mutations in patients with early-onset RT dementia detected by sequence analyses of four different genes."; RL Am. J. Hum. Genet. 66:110-117(2000). RN [134] RP VARIANT AD1 PRO-723. RX PubMed=10665499; RX DOI=10.1002/1531-8249(200002)47:2<249::AID-ANA18>3.0.CO;2-8; RA Kwok J.B.J., Li Q.X., Hallupp M., Whyte S., Ames D., Beyreuther K., RA Masters C.L., Schofield P.R.; RT "Novel Leu723Pro amyloid precursor protein mutation increases amyloid RT beta42(43) peptide levels and induces apoptosis."; RL Ann. Neurol. 47:249-253(2000). RN [135] RP VARIANT AD1 LEU-717. RX PubMed=10867787; DOI=10.1001/archneur.57.6.885; RA Murrell J.R., Hake A.M., Quaid K.A., Farlow M.R., Ghetti B.; RT "Early-onset Alzheimer disease caused by a new mutation (V717L) in the RT amyloid precursor protein gene."; RL Arch. Neurol. 57:885-887(2000). RN [136] RP VARIANT AD1 ILE-714, CHARACTERIZATION OF VARIANT AD1 ILE-714, AND RP MUTAGENESIS OF VAL-717. RX PubMed=11063718; DOI=10.1093/hmg/9.18.2589; RA Kumar-Singh S., De Jonghe C., Cruts M., Kleinert R., Wang R., RA Mercken M., De Strooper B., Vanderstichele H., Loefgren A., RA Vanderhoeven I., Backhovens H., Vanmechelen E., Kroisel P.M., RA Van Broeckhoven C.; RT "Nonfibrillar diffuse amyloid deposition due to a gamma(42)-secretase RT site mutation points to an essential role for N-truncated A beta(42) RT in Alzheimer's disease."; RL Hum. Mol. Genet. 9:2589-2598(2000). RN [137] RP VARIANT CAA-APP ASN-694. RX PubMed=11409420; DOI=10.1002/ana.1009; RA Grabowski T.J., Cho H.S., Vonsattel J.P.G., Rebeck G.W., RA Greenberg S.M.; RT "Novel amyloid precursor protein mutation in an Iowa family with RT dementia and severe cerebral amyloid angiopathy."; RL Ann. Neurol. 49:697-705(2001). RN [138] RP CHARACTERIZATION OF VARIANT AD1 GLY-692. RX PubMed=11311152; RA Walsh D.M., Hartley D.M., Condron M.M., Selkoe D.J., Teplow D.B.; RT "In vitro studies of amyloid beta-protein fibril assembly and toxicity RT provide clues to the aetiology of Flemish variant (Ala692-->Gly) RT Alzheimer's disease."; RL Biochem. J. 355:869-877(2001). RN [139] RP VARIANT AD1 GLY-693. RX PubMed=11528419; DOI=10.1038/nn0901-887; RA Nilsberth C., Westlind-Danielsson A., Eckman C.B., Condron M.M., RA Axelman K., Forsell C., Stenh C., Luthman J., Teplow D.B., RA Younkin S.G., Naeslund J., Lannfelt L.; RT "The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by RT enhanced Abeta protofibril formation."; RL Nat. Neurosci. 4:887-893(2001). RN [140] RP VARIANT AD1 ALA-714. RX PubMed=12034808; DOI=10.1212/WNL.58.10.1574; RA Pasalar P., Najmabadi H., Noorian A.R., Moghimi B., Jannati A., RA Soltanzadeh A., Krefft T., Crook R., Hardy J.; RT "An Iranian family with Alzheimer's disease caused by a novel APP RT mutation (Thr714Ala)."; RL Neurology 58:1574-1575(2002). RN [141] RP VARIANT CAA-APP ASN-694. RX PubMed=12654973; DOI=10.1212/01.WNL.0000050140.10044.A8; RA Greenberg S.M., Shin Y., Grabowski T.J., Cooper G.E., Rebeck G.W., RA Iglesias S., Chapon F., Tournier-Lasserve E., Baron J.-C.; RT "Hemorrhagic stroke associated with the Iowa amyloid precursor protein RT mutation."; RL Neurology 60:1020-1022(2003). RN [142] RP VARIANT AD1 THR-713. RX PubMed=15365148; DOI=10.1212/01.WNL.0000137048.80666.86; RA Rossi G., Giaccone G., Maletta R., Morbin M., Capobianco R., RA Mangieri M., Giovagnoli A.R., Bizzi A., Tomaino C., Perri M., RA Di Natale M., Tagliavini F., Bugiani O., Bruni A.C.; RT "A family with Alzheimer disease and strokes associated with A713T RT mutation of the APP gene."; RL Neurology 63:910-912(2004). RN [143] RP VARIANT CAA-APP VAL-705. RX PubMed=16178030; DOI=10.1002/ana.20571; RA Obici L., Demarchi A., de Rosa G., Bellotti V., Marciano S., RA Donadei S., Arbustini E., Palladini G., Diegoli M., Genovese E., RA Ferrari G., Coverlizza S., Merlini G.; RT "A novel AbetaPP mutation exclusively associated with cerebral amyloid RT angiopathy."; RL Ann. Neurol. 58:639-644(2005). RN [144] RP VARIANT AD1 ILE-714. RX PubMed=15668448; DOI=10.1212/01.WNL.0000149761.70566.3E; RA Edwards-Lee T., Ringman J.M., Chung J., Werner J., Morgan A., RA St George-Hyslop P.H., Thompson P., Dutton R., Mlikotic A., RA Rogaeva E., Hardy J.; RT "An African American family with early-onset Alzheimer disease and an RT APP (T714I) mutation."; RL Neurology 64:377-379(2005). CC -!- FUNCTION: Functions as a cell surface receptor and performs CC physiological functions on the surface of neurons relevant to CC neurite growth, neuronal adhesion and axonogenesis. Involved in CC cell mobility and transcription regulation through protein-protein CC interactions. Can promote transcription activation through binding CC to APBB1-KAT5 and inhibits Notch signaling through interaction CC with Numb. Couples to apoptosis-inducing pathways such as those CC mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By CC similarity). Acts as a kinesin I membrane receptor, mediating the CC axonal transport of beta-secretase and presenilin 1. Involved in CC copper homeostasis/oxidative stress through copper ion reduction. CC In vitro, copper-metallated APP induces neuronal death directly or CC is potentiated through Cu(2+)-mediated low-density lipoprotein CC oxidation. Can regulate neurite outgrowth through binding to CC components of the extracellular matrix such as heparin and CC collagen I and IV. The splice isoforms that contain the BPTI CC domain possess protease inhibitor activity. Induces a AGER- CC dependent pathway that involves activation of p38 MAPK, resulting CC in internalization of amyloid-beta peptide and leading to CC mitochondrial dysfunction in cultured cortical neurons. Provides CC Cu(2+) ions for GPC1 which are required for release of nitric CC oxide (NO) and subsequent degradation of the heparan sulfate CC chains on GPC1. CC -!- FUNCTION: Beta-amyloid peptides are lipophilic metal chelators CC with metal-reducing activity. Bind transient metals such as CC copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to CC Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more CC effective reductant than beta-amyloid 40. Beta-amyloid peptides CC bind to lipoproteins and apolipoproteins E and J in the CSF and to CC HDL particles in plasma, inhibiting metal-catalyzed oxidation of CC lipoproteins. Beta-APP42 may activate mononuclear phagocytes in CC the brain and elicit inflammatory responses. Promotes both tau CC aggregation and TPK II-mediated phosphorylation. Interaction with CC Also bind GPC1 in lipid rafts. CC -!- FUNCTION: Appicans elicit adhesion of neural cells to the CC extracellular matrix and may regulate neurite outgrowth in the CC brain (By similarity). CC -!- FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved CC peptides, including C31, are potent enhancers of neuronal CC apoptosis. CC -!- FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and CC degeneration of both neuronal cell bodies (via caspase-3) and CC axons (via caspase-6). CC -!- SUBUNIT: Binds, via its C-terminus, to the PID domain of several CC cytoplasmic proteins, including APBB family members, the APBA CC family, MAPK8IP1, SHC1 and, NUMB and DAB1 (By similarity). Binding CC to DAB1 inhibits its serine phosphorylation (By similarity). CC Interacts (via NPXY motif) with DAB2 (via PID domain); the CC interaction is impaired by tyrosine phosphorylation of the NPXY CC motif. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, CC IB1, KNS2 (via its TPR domains) (By similarity), APPBP2 (via BaSS) CC and DDB1. In vitro, it binds MAPT via the MT-binding domains (By CC similarity). Associates with microtubules in the presence of ATP CC and in a kinesin-dependent manner (By similarity). Interacts, CC through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CC CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. CC Soluble APP binds, via its N-terminal head, to FBLN1. Interacts CC with CPEB1 and AGER (By similarity). Interacts with ANKS1B and CC TNFRSF21. Interacts with ITM2B. Interacts with ITM2C. Interacts CC with IDE. Can form homodimers; this is promoted by heparin CC binding. Beta-amyloid protein 40 interacts with S100A9. CTF-alpha CC product of APP interacts with GSAP. Interacts with SORL1. CC -!- INTERACTION: CC Self; NbExp=79; IntAct=EBI-77613, EBI-77613; CC Q306T3:- (xeno); NbExp=3; IntAct=EBI-77613, EBI-8294101; CC P31696:AGRN (xeno); NbExp=3; IntAct=EBI-2431589, EBI-457650; CC Q02410:APBA1; NbExp=3; IntAct=EBI-77613, EBI-368690; CC O00213:APBB1; NbExp=5; IntAct=EBI-77613, EBI-81694; CC Q92870:APBB2; NbExp=2; IntAct=EBI-77613, EBI-79277; CC P51693:APLP1; NbExp=2; IntAct=EBI-302641, EBI-74648; CC Q06481:APLP2; NbExp=2; IntAct=EBI-302641, EBI-79306; CC P02647:APOA1; NbExp=5; IntAct=EBI-77613, EBI-701692; CC Q13867:BLMH; NbExp=2; IntAct=EBI-302641, EBI-718504; CC P15253:CALR (xeno); NbExp=3; IntAct=EBI-77613, EBI-9005200; CC Q8K3H7:CALR (xeno); NbExp=2; IntAct=EBI-3894543, EBI-9005068; CC P39060:COL18A1; NbExp=2; IntAct=EBI-821758, EBI-2566375; CC P07339:CTSD; NbExp=2; IntAct=EBI-77613, EBI-2115097; CC O75955:FLOT1; NbExp=5; IntAct=EBI-77613, EBI-603643; CC P01100:FOS; NbExp=3; IntAct=EBI-77613, EBI-852851; CC P46089:GPR3; NbExp=2; IntAct=EBI-302641, EBI-3909653; CC Q9NSC5:HOMER3; NbExp=3; IntAct=EBI-302661, EBI-748420; CC Q99714:HSD17B10; NbExp=4; IntAct=EBI-77613, EBI-79964; CC O43736:ITM2A; NbExp=3; IntAct=EBI-302641, EBI-2431769; CC P05412:JUN; NbExp=2; IntAct=EBI-77613, EBI-852823; CC P10636:MAPT; NbExp=9; IntAct=EBI-77613, EBI-366182; CC Q93074:MED12; NbExp=2; IntAct=EBI-77613, EBI-394357; CC P03897:MT-ND3; NbExp=2; IntAct=EBI-821758, EBI-1246249; CC P21359:NF1; NbExp=3; IntAct=EBI-77613, EBI-1172917; CC P08138:NGFR; NbExp=2; IntAct=EBI-77613, EBI-1387782; CC P07174:Ngfr (xeno); NbExp=2; IntAct=EBI-2431589, EBI-1038810; CC P61457:PCBD1; NbExp=2; IntAct=EBI-77613, EBI-740475; CC Q15113:PCOLCE; NbExp=3; IntAct=EBI-821758, EBI-8869614; CC P30101:PDIA3; NbExp=3; IntAct=EBI-77613, EBI-979862; CC Q13526:PIN1; NbExp=2; IntAct=EBI-302641, EBI-714158; CC P04156:PRNP; NbExp=3; IntAct=EBI-77613, EBI-977302; CC P49768:PSEN1; NbExp=6; IntAct=EBI-77613, EBI-297277; CC P29353:SHC1; NbExp=5; IntAct=EBI-77613, EBI-78835; CC Q92529:SHC3; NbExp=2; IntAct=EBI-77613, EBI-79084; CC Q9NP59:SLC40A1; NbExp=4; IntAct=EBI-77613, EBI-725153; CC Q8BGY9:Slc5a7 (xeno); NbExp=2; IntAct=EBI-77613, EBI-2010752; CC Q9HCB6:SPON1; NbExp=3; IntAct=EBI-302641, EBI-2431846; CC P01137:TGFB1; NbExp=2; IntAct=EBI-77613, EBI-779636; CC P61812:TGFB2; NbExp=6; IntAct=EBI-77613, EBI-779581; CC O75509:TNFRSF21; NbExp=3; IntAct=EBI-77613, EBI-2313231; CC Q13625:TP53BP2; NbExp=3; IntAct=EBI-77613, EBI-77642; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. Membrane, clathrin-coated pit. Note=Cell surface protein CC that rapidly becomes internalized via clathrin-coated pits. During CC maturation, the immature APP (N-glycosylated in the endoplasmic CC reticulum) moves to the Golgi complex where complete maturation CC occurs (O-glycosylated and sulfated). After alpha-secretase CC cleavage, soluble APP is released into the extracellular space and CC the C-terminal is internalized to endosomes and lysosomes. Some CC APP accumulates in secretory transport vesicles leaving the late CC Golgi compartment and returns to the cell surface. Gamma-CTF(59) CC peptide is located to both the cytoplasm and nuclei of neurons. It CC can be translocated to the nucleus through association with APBB1 CC (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and CC the complex is then rapidly internalized. APP sorts to the CC basolateral surface in epithelial cells. During neuronal CC differentiation, the Thr-743 phosphorylated form is located mainly CC in growth cones, moderately in neurites and sparingly in the cell CC body. Casein kinase phosphorylation can occur either at the cell CC surface or within a post-Golgi compartment. Associates with GPC1 CC in perinuclear compartments. Colocalizes with SORL1 in a vesicular CC pattern in cytoplasm and perinuclear regions. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=11; CC Comment=Additional isoforms seem to exist. Experimental CC confirmation may be lacking for some isoforms; CC Name=APP770; Synonyms=PreA4 770; CC IsoId=P05067-1; Sequence=Displayed; CC Note=A major isoform; CC Name=APP305; CC IsoId=P05067-2; Sequence=VSP_000005, VSP_000006; CC Name=L-APP677; CC IsoId=P05067-3; Sequence=VSP_000002, VSP_000004, VSP_000009; CC Note=The L-isoforms are referred to as appicans; CC Name=APP695; Synonyms=PreA4 695; CC IsoId=P05067-4; Sequence=VSP_000002, VSP_000004; CC Note=A major isoform; CC Name=L-APP696; CC IsoId=P05067-5; Sequence=VSP_000002, VSP_000003, VSP_000009; CC Note=The L-isoforms are referred to as appicans; CC Name=APP714; CC IsoId=P05067-6; Sequence=VSP_000002, VSP_000003; CC Name=L-APP733; CC IsoId=P05067-7; Sequence=VSP_000007, VSP_000008, VSP_000009; CC Note=The L-isoforms are referred to as appicans; CC Name=APP751; Synonyms=PreA4 751; CC IsoId=P05067-8; Sequence=VSP_000007, VSP_000008; CC Note=A major isoform; CC Name=L-APP752; CC IsoId=P05067-9; Sequence=VSP_000009; CC Name=APP639; CC IsoId=P05067-10; Sequence=VSP_009116, VSP_009117, VSP_009118; CC Name=11; CC IsoId=P05067-11; Sequence=VSP_045446, VSP_045447; CC -!- TISSUE SPECIFICITY: Expressed in all fetal tissues examined with CC highest levels in brain, kidney, heart and spleen. Weak expression CC in liver. In adult brain, highest expression found in the frontal CC lobe of the cortex and in the anterior perisylvian cortex- CC opercular gyri. Moderate expression in the cerebellar cortex, the CC posterior perisylvian cortex-opercular gyri and the temporal CC associated cortex. Weak expression found in the striate, extra- CC striate and motor cortices. Expressed in cerebrospinal fluid, and CC plasma. Isoform APP695 is the predominant form in neuronal tissue, CC isoform APP751 and isoform APP770 are widely expressed in non- CC neuronal cells. Isoform APP751 is the most abundant form in T- CC lymphocytes. Appican is expressed in astrocytes. CC -!- INDUCTION: Increased levels during neuronal differentiation. CC -!- DOMAIN: The basolateral sorting signal (BaSS) is required for CC sorting of membrane proteins to the basolateral surface of CC epithelial cells. CC -!- DOMAIN: The NPXY sequence motif found in many tyrosine- CC phosphorylated proteins is required for the specific binding of CC the PID domain. However, additional amino acids either N- or C- CC terminal to the NPXY motif are often required for complete CC interaction. The PID domain-containing proteins which bind APP CC require the YENPTY motif for full interaction. These interactions CC are independent of phosphorylation on the terminal tyrosine CC residue. The NPXY site is also involved in clathrin-mediated CC endocytosis. CC -!- PTM: Proteolytically processed under normal cellular conditions. CC Cleavage either by alpha-secretase, beta-secretase or theta- CC secretase leads to generation and extracellular release of soluble CC APP peptides, S-APP-alpha and S-APP-beta, and the retention of CC corresponding membrane-anchored C-terminal fragments, C80, C83 and CC C99. Subsequent processing of C80 and C83 by gamma-secretase CC yields P3 peptides. This is the major secretory pathway and is CC non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated CC gamma-secretase processing of C99 releases the amyloid beta CC proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), CC major components of amyloid plaques, and the cytotoxic C-terminal CC fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59). Many CC other minor beta-amyloid peptides, beta-amyloid 1-X peptides, are CC found in cerebral spinal fluid (CSF) including the beta-amyloid X- CC 15 peptides, produced from the cleavage by alpha-secretase and all CC terminatiing at Gln-686. CC -!- PTM: Proteolytically cleaved by caspases during neuronal CC apoptosis. Cleavage at Asp-739 by either caspase-6, -8 or -9 CC results in the production of the neurotoxic C31 peptide and the CC increased production of beta-amyloid peptides. CC -!- PTM: N- and O-glycosylated. O-glycosylation on Ser and Thr CC residues with core 1 or possibly core 8 glycans. Partial tyrosine CC glycosylation (Tyr-681) is found on some minor, short beta-amyloid CC peptides (beta-amyloid 1-15, 1-16, 1-17, 1-18, 1-19 and 1-20) but CC not found on beta-amyloid 38, beta-amyloid 40 nor on beta-amyloid CC 42. Modification on a tyrosine is unusual and is more prevelant in CC AD patients. Glycans had Neu5AcHex(Neu5Ac)HexNAc-O-Tyr, CC Neu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr and O- CC AcNeu5AcNeu5AcHex(Neu5Ac)HexNAc-O-Tyr structures, where O-Ac is O- CC acetylation of Neu5Ac. Neu5AcNeu5Ac is most likely Neu5Ac CC 2,8Neu5Ac linked. O-glycosylations in the vicinity of the cleavage CC sites may influence the proteolytic processing. Appicans are L-APP CC isoforms with O-linked chondroitin sulfate. CC -!- PTM: Phosphorylation in the C-terminal on tyrosine, threonine and CC serine residues is neuron-specific. Phosphorylation can affect APP CC processing, neuronal differentiation and interaction with other CC proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 CC kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell- CC cycle dependent manner with maximal levels at the G2/M phase and, CC in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a CC conformational change which reduces binding of Fe65 family CC members. Phosphorylation on Tyr-757 is required for SHC binding. CC Phosphorylated in the extracellular domain by casein kinases on CC both soluble and membrane-bound APP. This phosphorylation is CC inhibited by heparin. CC -!- PTM: Extracellular binding and reduction of copper, results in a CC corresponding oxidation of Cys-144 and Cys-158, and the formation CC of a disulfide bond. In vitro, the APP-Cu(+) complex in the CC presence of hydrogen peroxide results in an increased production CC of beta-amyloid-containing peptides. CC -!- PTM: Trophic-factor deprivation triggers the cleavage of surface CC APP by beta-secretase to release sAPP-beta which is further CC cleaved to release an N-terminal fragment of APP (N-APP). CC -!- PTM: Beta-amyloid peptides are degraded by IDE. CC -!- MASS SPECTROMETRY: Mass=6461.6; Method=MALDI; Range=712-767; CC Source=PubMed:12214090; CC -!- MASS SPECTROMETRY: Mass=6451.6; Method=MALDI; Range=714-770; CC Source=PubMed:12214090; CC -!- MASS SPECTROMETRY: Mass=6436.8; Method=MALDI; Range=715-769; CC Source=PubMed:12214090; CC -!- MASS SPECTROMETRY: Mass=5752.5; Method=MALDI; Range=719-767; CC Source=PubMed:12214090; CC -!- DISEASE: Alzheimer disease 1 (AD1) [MIM:104300]: A familial early- CC onset form of Alzheimer disease. It can be associated with CC cerebral amyloid angiopathy. Alzheimer disease is a CC neurodegenerative disorder characterized by progressive dementia, CC loss of cognitive abilities, and deposition of fibrillar amyloid CC proteins as intraneuronal neurofibrillary tangles, extracellular CC amyloid plaques and vascular amyloid deposits. The major CC constituent of these plaques is the neurotoxic amyloid-beta-APP CC 40-42 peptide (s), derived proteolytically from the transmembrane CC precursor protein APP by sequential secretase processing. The CC cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved CC products such as C31 derived from APP, are also implicated in CC neuronal death. Note=The disease is caused by mutations affecting CC the gene represented in this entry. CC -!- DISEASE: Cerebral amyloid angiopathy, APP-related (CAA-APP) CC [MIM:605714]: A hereditary localized amyloidosis due to amyloid- CC beta A4 peptide(s) deposition in the cerebral vessels. The CC principal clinical characteristics are recurrent cerebral and CC cerebellar hemorrhages, recurrent strokes, cerebral ischemia, CC cerebral infarction, and progressive mental deterioration. CC Patients develop cerebral hemorrhage because of the severe CC cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare CC and largely in the form of pre-amyloid lesions or diffuse plaque- CC like structures. They are Congo red negative and lack the dense CC amyloid cores commonly present in Alzheimer disease. Some affected CC individuals manifest progressive aphasic dementia, CC leukoencephalopathy, and occipital calcifications. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- MISCELLANEOUS: Chelation of metal ions, notably copper, iron and CC zinc, can induce histidine-bridging between beta-amyloid molecules CC resulting in beta-amyloid-metal aggregates. The affinity for CC copper is much higher than for other transient metals and is CC increased under acidic conditions. Extracellular zinc-binding CC increases binding of heparin to APP and inhibits collagen-binding. CC -!- SIMILARITY: Belongs to the APP family. CC -!- SIMILARITY: Contains 1 BPTI/Kunitz inhibitor domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAA58727.1; Type=Miscellaneous discrepancy; Note=Contamination by an Alu repeat; CC -!- WEB RESOURCE: Name=Alzheimer Research Forum; Note=APP mutations; CC URL="http://www.alzforum.org/res/com/mut/app/default.asp"; CC -!- WEB RESOURCE: Name=AD mutations; CC URL="http://www.molgen.ua.ac.be/ADmutations/"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/app/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Amyloid beta entry; CC URL="http://en.wikipedia.org/wiki/Amyloid_beta"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y00264; CAA68374.1; -; mRNA. DR EMBL; X13466; CAA31830.1; -; Genomic_DNA. DR EMBL; X13467; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13468; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13469; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13470; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13471; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13472; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13473; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13474; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13475; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13476; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13477; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13478; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13479; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13487; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X13488; CAA31830.1; JOINED; Genomic_DNA. DR EMBL; X06989; CAA30050.1; -; mRNA. DR EMBL; M33112; AAB59502.1; -; Genomic_DNA. DR EMBL; M34862; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34863; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34864; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34865; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34866; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34867; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34868; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34869; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34870; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34871; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34872; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34873; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34874; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34876; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34877; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34878; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34879; AAB59502.1; JOINED; Genomic_DNA. DR EMBL; M34875; AAB59501.1; ALT_TERM; Genomic_DNA. DR EMBL; M34862; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34863; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34864; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34865; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34866; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34867; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34868; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34869; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34870; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34871; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34872; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; M34873; AAB59501.1; JOINED; Genomic_DNA. DR EMBL; D87675; BAA22264.1; -; Genomic_DNA. DR EMBL; AK312326; BAG35248.1; -; mRNA. DR EMBL; AK295621; BAG58500.1; -; mRNA. DR EMBL; AY919674; AAW82435.1; -; Genomic_DNA. DR EMBL; AP001439; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001440; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001441; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001442; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP001443; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09958.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09959.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09960.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09961.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09963.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09965.1; -; Genomic_DNA. DR EMBL; BC004369; AAH04369.1; -; mRNA. DR EMBL; BC065529; AAH65529.1; -; mRNA. DR EMBL; M35675; AAA60163.1; ALT_SEQ; mRNA. DR EMBL; M24547; AAC13654.1; -; Genomic_DNA. DR EMBL; M24546; AAC13654.1; JOINED; Genomic_DNA. DR EMBL; M28373; AAA58727.1; ALT_SEQ; mRNA. DR EMBL; X06982; CAA30042.1; -; mRNA. DR EMBL; X06981; CAA30041.1; -; mRNA. DR EMBL; M18734; AAA51726.1; -; mRNA. DR EMBL; M29270; AAA51768.1; -; Genomic_DNA. DR EMBL; M29269; AAA51768.1; JOINED; Genomic_DNA. DR EMBL; AB066441; BAB71958.2; -; mRNA. DR EMBL; M15533; AAA35540.1; -; mRNA. DR EMBL; M15532; AAA51564.1; -; mRNA. DR EMBL; M37896; AAA51727.1; -; Genomic_DNA. DR EMBL; M37895; AAA51727.1; JOINED; Genomic_DNA. DR EMBL; S45136; AAB23646.1; -; Genomic_DNA. DR EMBL; S60317; AAC60601.2; -; Genomic_DNA. DR EMBL; AF282245; AAQ14327.1; -; mRNA. DR EMBL; S60721; AAB26263.2; -; mRNA. DR EMBL; S61380; AAB26264.2; -; mRNA. DR EMBL; S61383; AAB26265.2; -; mRNA. DR EMBL; M16765; AAA51722.1; -; mRNA. DR CCDS; CCDS13576.1; -. [P05067-1] DR CCDS; CCDS13577.1; -. [P05067-4] DR CCDS; CCDS33523.1; -. [P05067-8] DR CCDS; CCDS46638.1; -. [P05067-10] DR CCDS; CCDS56212.1; -. [P05067-11] DR CCDS; CCDS56213.1; -. [P05067-9] DR PIR; S01442; S01442. DR PIR; S02260; QRHUA4. DR RefSeq; NP_000475.1; NM_000484.3. [P05067-1] DR RefSeq; NP_001129488.1; NM_001136016.3. [P05067-11] DR RefSeq; NP_001129601.1; NM_001136129.2. [P05067-10] DR RefSeq; NP_001129602.1; NM_001136130.2. DR RefSeq; NP_001129603.1; NM_001136131.2. DR RefSeq; NP_001191230.1; NM_001204301.1. [P05067-9] DR RefSeq; NP_001191231.1; NM_001204302.1. [P05067-7] DR RefSeq; NP_001191232.1; NM_001204303.1. [P05067-3] DR RefSeq; NP_958816.1; NM_201413.2. [P05067-8] DR RefSeq; NP_958817.1; NM_201414.2. [P05067-4] DR UniGene; Hs.434980; -. DR PDB; 1AAP; X-ray; 1.50 A; A/B=287-344. DR PDB; 1AMB; NMR; -; A=672-699. DR PDB; 1AMC; NMR; -; A=672-699. DR PDB; 1AML; NMR; -; A=672-711. DR PDB; 1BA4; NMR; -; A=672-711. DR PDB; 1BA6; NMR; -; A=672-711. DR PDB; 1BJB; NMR; -; A=672-699. DR PDB; 1BJC; NMR; -; A=672-699. DR PDB; 1BRC; X-ray; 2.50 A; I=287-342. DR PDB; 1CA0; X-ray; 2.10 A; D/I=289-342. DR PDB; 1HZ3; NMR; -; A=681-706. DR PDB; 1IYT; NMR; -; A=672-713. DR PDB; 1MWP; X-ray; 1.80 A; A=28-123. DR PDB; 1OWT; NMR; -; A=124-189. DR PDB; 1QCM; NMR; -; A=696-706. DR PDB; 1QWP; NMR; -; A=696-706. DR PDB; 1QXC; NMR; -; A=696-706. DR PDB; 1QYT; NMR; -; A=696-706. DR PDB; 1TAW; X-ray; 1.80 A; B=287-344. DR PDB; 1TKN; NMR; -; A=460-569. DR PDB; 1UO7; Model; -; A=672-713. DR PDB; 1UO8; Model; -; A=672-713. DR PDB; 1UOA; Model; -; A=672-713. DR PDB; 1UOI; Model; -; A=672-713. DR PDB; 1X11; X-ray; 2.50 A; C/D=754-766. DR PDB; 1Z0Q; NMR; -; A=672-713. DR PDB; 1ZE7; NMR; -; A=672-687. DR PDB; 1ZE9; NMR; -; A=672-687. DR PDB; 1ZJD; X-ray; 2.60 A; B=289-344. DR PDB; 2BEG; NMR; -; A/B/C/D/E=672-713. DR PDB; 2BOM; Model; -; A/B=681-713. DR PDB; 2BP4; NMR; -; A=672-687. DR PDB; 2FJZ; X-ray; 1.61 A; A=133-189. DR PDB; 2FK1; X-ray; 1.60 A; A=133-189. DR PDB; 2FK2; X-ray; 1.65 A; A=133-189. DR PDB; 2FK3; X-ray; 2.40 A; A/B/C/D/E/F/G/H=133-189. DR PDB; 2FKL; X-ray; 2.50 A; A/B=124-189. DR PDB; 2FMA; X-ray; 0.85 A; A=133-189. DR PDB; 2G47; X-ray; 2.10 A; C/D=672-711. DR PDB; 2IPU; X-ray; 1.65 A; P/Q=672-679. DR PDB; 2LFM; NMR; -; A=672-711. DR PDB; 2LLM; NMR; -; A=686-726. DR PDB; 2LMN; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L=672-711. DR PDB; 2LMO; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L=672-711. DR PDB; 2LMP; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=672-711. DR PDB; 2LMQ; NMR; -; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=672-711. DR PDB; 2LNQ; NMR; -; A/B/C/D/E/F/G/H=672-711. DR PDB; 2LOH; NMR; -; A/B=686-726. DR PDB; 2LP1; NMR; -; A=671-770. DR PDB; 2LZ3; NMR; -; A/B=699-726. DR PDB; 2LZ4; NMR; -; A/B=699-726. DR PDB; 2M4J; NMR; -; A/B/C/D/E/F/G/H/I=672-711. DR PDB; 2M9R; NMR; -; A=672-711. DR PDB; 2M9S; NMR; -; A=672-711. DR PDB; 2OTK; NMR; -; C=672-711. DR PDB; 2R0W; X-ray; 2.50 A; Q=672-679. DR PDB; 2WK3; X-ray; 2.59 A; C/D=672-713. DR PDB; 2Y29; X-ray; 2.30 A; A=687-692. DR PDB; 2Y2A; X-ray; 1.91 A; A=687-692. DR PDB; 2Y3J; X-ray; 1.99 A; A/B/C/D/E/F/G/H=701-706. DR PDB; 2Y3K; X-ray; 1.90 A; A/B/C/D/E/F/G/H=706-713. DR PDB; 2Y3L; X-ray; 2.10 A; A/B/C/G=706-713. DR PDB; 3AYU; X-ray; 2.00 A; B=586-595. DR PDB; 3BAE; X-ray; 1.59 A; A=672-699. DR PDB; 3BKJ; X-ray; 1.59 A; A=672-687. DR PDB; 3DXC; X-ray; 2.10 A; B/D=739-770. DR PDB; 3DXD; X-ray; 2.20 A; B/D=739-770. DR PDB; 3DXE; X-ray; 2.00 A; B/D=739-770. DR PDB; 3GCI; X-ray; 2.04 A; P=707-713. DR PDB; 3IFL; X-ray; 1.50 A; P=672-678. DR PDB; 3IFN; X-ray; 1.50 A; P=672-711. DR PDB; 3IFO; X-ray; 2.15 A; P/Q=672-678. DR PDB; 3IFP; X-ray; 2.95 A; P/Q/R/S=672-678. DR PDB; 3JQ5; X-ray; 2.03 A; B=672-679. DR PDB; 3JQL; X-ray; 1.20 A; B=687-692. DR PDB; 3JTI; X-ray; 1.80 A; B=699-706. DR PDB; 3KTM; X-ray; 2.70 A; A/B/C/D/E/F/G/H=18-190. DR PDB; 3L33; X-ray; 2.48 A; E/F/G/H=290-341. DR PDB; 3L81; X-ray; 1.60 A; B=761-767. DR PDB; 3MOQ; X-ray; 2.05 A; A/B/C/D=689-712. DR PDB; 3MXC; X-ray; 2.00 A; L=754-762. DR PDB; 3MXY; X-ray; 2.30 A; L=754-762. DR PDB; 3NYJ; X-ray; 3.20 A; A=365-567. DR PDB; 3NYL; X-ray; 2.80 A; A=365-570. DR PDB; 3OVJ; X-ray; 1.80 A; A/B/C/D=687-692. DR PDB; 3OW9; X-ray; 1.80 A; A/B=687-692. DR PDB; 3SV1; X-ray; 3.30 A; D/E/F=754-767. DR PDB; 3U0T; X-ray; 2.50 A; E/F=701-711. DR PDB; 3UMH; X-ray; 2.00 A; A=370-575. DR PDB; 3UMI; X-ray; 2.40 A; A=370-575. DR PDB; 3UMK; X-ray; 2.60 A; A=370-575. DR PDB; 4HIX; X-ray; 2.20 A; A=672-699. DR PDB; 4MDR; X-ray; 1.85 A; B=758-767. DR PDB; 4NGE; X-ray; 2.70 A; B/E=672-711. DR PDBsum; 1AAP; -. DR PDBsum; 1AMB; -. DR PDBsum; 1AMC; -. DR PDBsum; 1AML; -. DR PDBsum; 1BA4; -. DR PDBsum; 1BA6; -. DR PDBsum; 1BJB; -. DR PDBsum; 1BJC; -. DR PDBsum; 1BRC; -. DR PDBsum; 1CA0; -. DR PDBsum; 1HZ3; -. DR PDBsum; 1IYT; -. DR PDBsum; 1MWP; -. DR PDBsum; 1OWT; -. DR PDBsum; 1QCM; -. DR PDBsum; 1QWP; -. DR PDBsum; 1QXC; -. DR PDBsum; 1QYT; -. DR PDBsum; 1TAW; -. DR PDBsum; 1TKN; -. DR PDBsum; 1UO7; -. DR PDBsum; 1UO8; -. DR PDBsum; 1UOA; -. DR PDBsum; 1UOI; -. DR PDBsum; 1X11; -. DR PDBsum; 1Z0Q; -. DR PDBsum; 1ZE7; -. DR PDBsum; 1ZE9; -. DR PDBsum; 1ZJD; -. DR PDBsum; 2BEG; -. DR PDBsum; 2BOM; -. DR PDBsum; 2BP4; -. DR PDBsum; 2FJZ; -. DR PDBsum; 2FK1; -. DR PDBsum; 2FK2; -. DR PDBsum; 2FK3; -. DR PDBsum; 2FKL; -. DR PDBsum; 2FMA; -. DR PDBsum; 2G47; -. DR PDBsum; 2IPU; -. DR PDBsum; 2LFM; -. DR PDBsum; 2LLM; -. DR PDBsum; 2LMN; -. DR PDBsum; 2LMO; -. DR PDBsum; 2LMP; -. DR PDBsum; 2LMQ; -. DR PDBsum; 2LNQ; -. DR PDBsum; 2LOH; -. DR PDBsum; 2LP1; -. DR PDBsum; 2LZ3; -. DR PDBsum; 2LZ4; -. DR PDBsum; 2M4J; -. DR PDBsum; 2M9R; -. DR PDBsum; 2M9S; -. DR PDBsum; 2OTK; -. DR PDBsum; 2R0W; -. DR PDBsum; 2WK3; -. DR PDBsum; 2Y29; -. DR PDBsum; 2Y2A; -. DR PDBsum; 2Y3J; -. DR PDBsum; 2Y3K; -. DR PDBsum; 2Y3L; -. DR PDBsum; 3AYU; -. DR PDBsum; 3BAE; -. DR PDBsum; 3BKJ; -. DR PDBsum; 3DXC; -. DR PDBsum; 3DXD; -. DR PDBsum; 3DXE; -. DR PDBsum; 3GCI; -. DR PDBsum; 3IFL; -. DR PDBsum; 3IFN; -. DR PDBsum; 3IFO; -. DR PDBsum; 3IFP; -. DR PDBsum; 3JQ5; -. DR PDBsum; 3JQL; -. DR PDBsum; 3JTI; -. DR PDBsum; 3KTM; -. DR PDBsum; 3L33; -. DR PDBsum; 3L81; -. DR PDBsum; 3MOQ; -. DR PDBsum; 3MXC; -. DR PDBsum; 3MXY; -. DR PDBsum; 3NYJ; -. DR PDBsum; 3NYL; -. DR PDBsum; 3OVJ; -. DR PDBsum; 3OW9; -. DR PDBsum; 3SV1; -. DR PDBsum; 3U0T; -. DR PDBsum; 3UMH; -. DR PDBsum; 3UMI; -. DR PDBsum; 3UMK; -. DR PDBsum; 4HIX; -. DR PDBsum; 4MDR; -. DR PDBsum; 4NGE; -. DR ProteinModelPortal; P05067; -. DR SMR; P05067; 26-192, 287-342, 385-567, 683-728, 741-768. DR BioGrid; 106848; 1971. DR DIP; DIP-574N; -. DR IntAct; P05067; 113. DR MINT; MINT-150767; -. DR BindingDB; P05067; -. DR ChEMBL; CHEMBL2487; -. DR MEROPS; I02.015; -. DR TCDB; 1.C.50.1.2; the amyloid -protein peptide (app) family. DR PhosphoSite; P05067; -. DR UniCarbKB; P05067; -. DR DMDM; 112927; -. DR SWISS-2DPAGE; P05067; -. DR MaxQB; P05067; -. DR PaxDb; P05067; -. DR PRIDE; P05067; -. DR DNASU; 351; -. DR Ensembl; ENST00000346798; ENSP00000284981; ENSG00000142192. [P05067-1] DR Ensembl; ENST00000348990; ENSP00000345463; ENSG00000142192. [P05067-4] DR Ensembl; ENST00000354192; ENSP00000346129; ENSG00000142192. [P05067-10] DR Ensembl; ENST00000357903; ENSP00000350578; ENSG00000142192. [P05067-8] DR Ensembl; ENST00000358918; ENSP00000351796; ENSG00000142192. [P05067-9] DR Ensembl; ENST00000359726; ENSP00000352760; ENSG00000142192. [P05067-6] DR Ensembl; ENST00000440126; ENSP00000387483; ENSG00000142192. [P05067-11] DR GeneID; 351; -. DR KEGG; hsa:351; -. DR UCSC; uc002ylz.3; human. [P05067-1] DR UCSC; uc002yma.3; human. [P05067-8] DR UCSC; uc002ymb.3; human. [P05067-4] DR UCSC; uc010glj.3; human. [P05067-10] DR UCSC; uc010glk.3; human. DR UCSC; uc011acj.2; human. [P05067-2] DR UCSC; uc021whz.1; human. [P05067-9] DR UCSC; uc021wia.1; human. [P05067-7] DR UCSC; uc021wib.1; human. [P05067-3] DR CTD; 351; -. DR GeneCards; GC21M027252; -. DR GeneReviews; APP; -. DR HGNC; HGNC:620; APP. DR HPA; CAB000157; -. DR HPA; HPA001462; -. DR MIM; 104300; phenotype. DR MIM; 104760; gene. DR MIM; 605714; phenotype. DR neXtProt; NX_P05067; -. DR Orphanet; 1020; Early-onset autosomal dominant Alzheimer disease. DR Orphanet; 324723; Hereditary cerebral hemorrhage with amyloidosis, Arctic type. DR Orphanet; 100006; Hereditary cerebral hemorrhage with amyloidosis, Dutch type. DR Orphanet; 324718; Hereditary cerebral hemorrhage with amyloidosis, Flemish type. DR Orphanet; 324708; Hereditary cerebral hemorrhage with amyloidosis, Iowa type. DR Orphanet; 324713; Hereditary cerebral hemorrhage with amyloidosis, Italian type. DR Orphanet; 324703; Hereditary cerebral hemorrhage with amyloidosis, Piedmont type. DR PharmGKB; PA24910; -. DR eggNOG; NOG289770; -. DR HOVERGEN; HBG000051; -. DR InParanoid; P05067; -. DR KO; K04520; -. DR OMA; THAHIVI; -. DR OrthoDB; EOG7RNJZP; -. DR PhylomeDB; P05067; -. DR TreeFam; TF317274; -. DR BioCyc; MetaCyc:ENSG00000142192-MONOMER; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_118779; Extracellular matrix organization. DR Reactome; REACT_604; Hemostasis. DR Reactome; REACT_6900; Immune System. DR SABIO-RK; P05067; -. DR ChiTaRS; app; human. DR EvolutionaryTrace; P05067; -. DR GeneWiki; Amyloid_precursor_protein; -. DR GenomeRNAi; 351; -. DR NextBio; 1445; -. DR PMAP-CutDB; P05067; -. DR PRO; PR:P05067; -. DR ArrayExpress; P05067; -. DR Bgee; P05067; -. DR Genevestigator; P05067; -. DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl. DR GO; GO:0030424; C:axon; ISS:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0035253; C:ciliary rootlet; IEA:Ensembl. DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0043198; C:dendritic shaft; IDA:MGI. DR GO; GO:0043197; C:dendritic spine; IDA:MGI. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0045121; C:membrane raft; IDA:ParkinsonsUK-UCL. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0005641; C:nuclear envelope lumen; IDA:Alzheimers_University_of_Toronto. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProt. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0043235; C:receptor complex; IDA:MGI. DR GO; GO:0051233; C:spindle midzone; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IDA:MGI. DR GO; GO:0033130; F:acetylcholine receptor binding; IPI:UniProtKB. DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0051425; F:PTB domain binding; IPI:BHF-UCL. DR GO; GO:0005102; F:receptor binding; IPI:BHF-UCL. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR GO; GO:0008344; P:adult locomotory behavior; ISS:UniProtKB. DR GO; GO:0008088; P:axon cargo transport; ISS:UniProtKB. DR GO; GO:0016199; P:axon midline choice point recognition; ISS:UniProtKB. DR GO; GO:0007409; P:axonogenesis; ISS:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0006878; P:cellular copper ion homeostasis; ISS:UniProtKB. DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl. DR GO; GO:0048669; P:collateral sprouting in absence of injury; ISS:UniProtKB. DR GO; GO:0016358; P:dendrite development; ISS:UniProtKB. DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB. DR GO; GO:0030198; P:extracellular matrix organization; ISS:UniProtKB. DR GO; GO:0030900; P:forebrain development; IEA:Ensembl. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0007626; P:locomotory behavior; ISS:UniProtKB. DR GO; GO:0007617; P:mating behavior; ISS:UniProtKB. DR GO; GO:0000085; P:mitotic G2 phase; ISS:UniProtKB. DR GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB. DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:GOC. DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl. DR GO; GO:0051402; P:neuron apoptotic process; IMP:UniProtKB. DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB. DR GO; GO:0016322; P:neuron remodeling; ISS:UniProtKB. DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; TAS:Reactome. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome. DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB. DR GO; GO:0007176; P:regulation of epidermal growth factor-activated receptor activity; ISS:UniProtKB. DR GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB. DR GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl. DR GO; GO:0050803; P:regulation of synapse structure and activity; ISS:UniProtKB. DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl. DR GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IEA:Ensembl. DR GO; GO:0001967; P:suckling behavior; IEA:Ensembl. DR GO; GO:0051124; P:synaptic growth at neuromuscular junction; IEA:Ensembl. DR GO; GO:0008542; P:visual learning; ISS:UniProtKB. DR Gene3D; 3.30.1490.140; -; 1. DR Gene3D; 3.90.570.10; -; 1. DR Gene3D; 4.10.230.10; -; 1. DR Gene3D; 4.10.410.10; -; 1. DR InterPro; IPR008155; Amyloid_glyco. DR InterPro; IPR013803; Amyloid_glyco_Abeta. DR InterPro; IPR011178; Amyloid_glyco_Cu-bd. DR InterPro; IPR024329; Amyloid_glyco_E2_domain. DR InterPro; IPR008154; Amyloid_glyco_extra. DR InterPro; IPR019744; Amyloid_glyco_extracell_CS. DR InterPro; IPR015849; Amyloid_glyco_heparin-bd. DR InterPro; IPR019745; Amyloid_glyco_intracell_CS. DR InterPro; IPR028866; APP. DR InterPro; IPR019543; APP_amyloid_C. DR InterPro; IPR002223; Prot_inh_Kunz-m. DR InterPro; IPR020901; Prtase_inh_Kunz-CS. DR PANTHER; PTHR23103:SF7; PTHR23103:SF7; 1. DR Pfam; PF10515; APP_amyloid; 1. DR Pfam; PF12924; APP_Cu_bd; 1. DR Pfam; PF12925; APP_E2; 1. DR Pfam; PF02177; APP_N; 1. DR Pfam; PF03494; Beta-APP; 1. DR Pfam; PF00014; Kunitz_BPTI; 1. DR PRINTS; PR00203; AMYLOIDA4. DR PRINTS; PR00759; BASICPTASE. DR PRINTS; PR00204; BETAAMYLOID. DR SMART; SM00006; A4_EXTRA; 1. DR SMART; SM00131; KU; 1. DR SUPFAM; SSF109843; SSF109843; 1. DR SUPFAM; SSF56491; SSF56491; 1. DR SUPFAM; SSF57362; SSF57362; 1. DR SUPFAM; SSF89811; SSF89811; 1. DR PROSITE; PS00319; A4_EXTRA; 1. DR PROSITE; PS00320; A4_INTRA; 1. DR PROSITE; PS00280; BPTI_KUNITZ_1; 1. DR PROSITE; PS50279; BPTI_KUNITZ_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Alzheimer disease; Amyloid; KW Amyloidosis; Apoptosis; Cell adhesion; Coated pit; Complete proteome; KW Copper; Direct protein sequencing; Disease mutation; Disulfide bond; KW Endocytosis; Glycoprotein; Heparin-binding; Iron; Membrane; KW Metal-binding; Neurodegeneration; Notch signaling pathway; KW Phosphoprotein; Polymorphism; Protease inhibitor; Proteoglycan; KW Reference proteome; Serine protease inhibitor; Signal; Transmembrane; KW Transmembrane helix; Zinc. FT SIGNAL 1 17 FT CHAIN 18 770 Amyloid beta A4 protein. FT /FTId=PRO_0000000088. FT CHAIN 18 687 Soluble APP-alpha. FT /FTId=PRO_0000000089. FT CHAIN 18 671 Soluble APP-beta. FT /FTId=PRO_0000000090. FT CHAIN 18 286 N-APP. FT /FTId=PRO_0000381966. FT CHAIN 672 770 C99. FT /FTId=PRO_0000000091. FT CHAIN 672 713 Beta-amyloid protein 42. FT /FTId=PRO_0000000092. FT CHAIN 672 711 Beta-amyloid protein 40. FT /FTId=PRO_0000000093. FT CHAIN 688 770 C83. FT /FTId=PRO_0000000094. FT PEPTIDE 688 713 P3(42). FT /FTId=PRO_0000000095. FT PEPTIDE 688 711 P3(40). FT /FTId=PRO_0000000096. FT CHAIN 691 770 C80. FT /FTId=PRO_0000384574. FT CHAIN 712 770 Gamma-secretase C-terminal fragment 59. FT /FTId=PRO_0000000097. FT CHAIN 714 770 Gamma-secretase C-terminal fragment 57. FT /FTId=PRO_0000000098. FT CHAIN 721 770 Gamma-secretase C-terminal fragment 50 FT (By similarity). FT /FTId=PRO_0000000099. FT CHAIN 740 770 C31. FT /FTId=PRO_0000000100. FT TOPO_DOM 18 699 Extracellular (Potential). FT TRANSMEM 700 723 Helical; (Potential). FT TOPO_DOM 724 770 Cytoplasmic (Potential). FT DOMAIN 291 341 BPTI/Kunitz inhibitor. FT REGION 96 110 Heparin-binding. FT REGION 181 188 Zinc-binding. FT REGION 391 423 Heparin-binding. FT REGION 491 522 Heparin-binding. FT REGION 523 540 Collagen-binding. FT REGION 732 751 Interaction with G(o)-alpha. FT MOTIF 724 734 Basolateral sorting signal. FT MOTIF 759 762 NPXY motif; contains endocytosis signal. FT COMPBIAS 230 260 Asp/Glu-rich (acidic). FT COMPBIAS 274 280 Poly-Thr. FT METAL 147 147 Copper 1. FT METAL 151 151 Copper 1. FT METAL 168 168 Copper 1. FT METAL 677 677 Copper or zinc 2. FT METAL 681 681 Copper or zinc 2 (Probable). FT METAL 684 684 Copper or zinc 2. FT METAL 685 685 Copper or zinc 2. FT SITE 144 144 Required for Cu(2+) reduction. FT SITE 301 302 Reactive bond. FT SITE 671 672 Cleavage; by beta-secretase. FT SITE 672 673 Cleavage; by caspase-6; when associated FT with variant 670-N-L-671. FT SITE 687 688 Cleavage; by alpha-secretase. FT SITE 690 691 Cleavage; by theta-secretase. FT SITE 704 704 Implicated in free radical propagation FT (By similarity). FT SITE 706 706 Susceptible to oxidation. FT SITE 711 712 Cleavage; by gamma-secretase; site 1. FT SITE 713 714 Cleavage; by gamma-secretase; site 2. FT SITE 720 721 Cleavage; by gamma-secretase; site 3. FT SITE 739 740 Cleavage; by caspase-6, caspase-8 or FT caspase-9. FT MOD_RES 198 198 Phosphoserine; by CK2. FT MOD_RES 206 206 Phosphoserine; by CK1. FT MOD_RES 729 729 Phosphothreonine (By similarity). FT MOD_RES 730 730 Phosphoserine; by APP-kinase I (By FT similarity). FT MOD_RES 743 743 Phosphothreonine; by CDK5 and MAPK10. FT MOD_RES 757 757 Phosphotyrosine. FT CARBOHYD 542 542 N-linked (GlcNAc...). FT CARBOHYD 571 571 N-linked (GlcNAc...) (Probable). FT CARBOHYD 614 614 O-linked (GalNAc...). FT CARBOHYD 623 623 O-linked (GalNAc...). FT CARBOHYD 628 628 O-linked (GalNAc...). FT CARBOHYD 633 633 O-linked (GalNAc...). FT CARBOHYD 651 651 O-linked (GalNAc...). FT CARBOHYD 652 652 O-linked (GalNAc...). FT CARBOHYD 656 656 O-linked (Xyl...) (chondroitin sulfate); FT in L-APP isoforms. FT CARBOHYD 659 659 O-linked (GalNAc...). FT CARBOHYD 663 663 O-linked (GalNAc...) (Probable). FT CARBOHYD 667 667 O-linked (GalNAc...) (Probable). FT CARBOHYD 679 679 O-linked (GalNAc...). FT CARBOHYD 697 697 O-linked (GalNAc...). FT DISULFID 38 62 FT DISULFID 73 117 FT DISULFID 98 105 FT DISULFID 133 187 FT DISULFID 144 174 FT DISULFID 158 186 FT DISULFID 291 341 FT DISULFID 300 324 FT DISULFID 316 337 FT VAR_SEQ 1 19 MLPGLALLLLAAWTARALE -> MDQLEDLLVLFINY (in FT isoform 11). FT /FTId=VSP_045446. FT VAR_SEQ 19 74 Missing (in isoform APP639). FT /FTId=VSP_009116. FT VAR_SEQ 289 363 Missing (in isoform APP639). FT /FTId=VSP_009117. FT VAR_SEQ 289 289 E -> V (in isoform APP695, isoform L- FT APP696, isoform L-APP677 and isoform FT APP714). FT /FTId=VSP_000002. FT VAR_SEQ 290 364 Missing (in isoform APP695 and isoform L- FT APP677). FT /FTId=VSP_000004. FT VAR_SEQ 290 345 Missing (in isoform L-APP696 and isoform FT APP714). FT /FTId=VSP_000003. FT VAR_SEQ 290 305 VCSEQAETGPCRAMIS -> KWYKEVHSGQARWLML (in FT isoform APP305). FT /FTId=VSP_000005. FT VAR_SEQ 306 770 Missing (in isoform APP305). FT /FTId=VSP_000006. FT VAR_SEQ 345 364 MSQSLLKTTQEPLARDPVKL -> I (in isoform FT 11). FT /FTId=VSP_045447. FT VAR_SEQ 345 345 M -> I (in isoform L-APP733 and isoform FT APP751). FT /FTId=VSP_000007. FT VAR_SEQ 346 364 Missing (in isoform L-APP733 and isoform FT APP751). FT /FTId=VSP_000008. FT VAR_SEQ 364 364 L -> V (in isoform APP639). FT /FTId=VSP_009118. FT VAR_SEQ 637 654 Missing (in isoform L-APP677, isoform L- FT APP696, isoform L-APP733 and isoform L- FT APP752). FT /FTId=VSP_000009. FT VARIANT 501 501 E -> K (in dbSNP:rs45588932). FT /FTId=VAR_022315. FT VARIANT 665 665 E -> D (in a patient with late onset FT Alzheimer disease). FT /FTId=VAR_010107. FT VARIANT 670 671 KM -> NL (in AD1). FT /FTId=VAR_000015. FT VARIANT 678 678 D -> N (in AD1). FT /FTId=VAR_044424. FT VARIANT 692 692 A -> G (in AD1; Flemish mutation; FT increases the solubility of processed FT beta-amyloid peptides and increases the FT stability of peptide oligomers). FT /FTId=VAR_000016. FT VARIANT 693 693 E -> G (in AD1). FT /FTId=VAR_014215. FT VARIANT 693 693 E -> K (in CAA-APP; Italian type). FT /FTId=VAR_014216. FT VARIANT 693 693 E -> Q (in CAA-APP; Dutch type). FT /FTId=VAR_000017. FT VARIANT 694 694 D -> N (in CAA-APP; Iowa type). FT /FTId=VAR_014217. FT VARIANT 705 705 L -> V (in CAA-APP; Italian type). FT /FTId=VAR_032276. FT VARIANT 713 713 A -> T (in AD1). FT /FTId=VAR_000019. FT VARIANT 713 713 A -> V (in one chronic schizophrenia FT patient; unknown pathological FT significance; dbSNP:rs1800557). FT /FTId=VAR_000018. FT VARIANT 714 714 T -> A (in AD1). FT /FTId=VAR_032277. FT VARIANT 714 714 T -> I (in AD1; increased beta-APP42/ FT beta-APP40 ratio). FT /FTId=VAR_014218. FT VARIANT 715 715 V -> M (in AD1; decreased beta-APP40/ FT total APP-beta). FT /FTId=VAR_010108. FT VARIANT 716 716 I -> V (in AD1). FT /FTId=VAR_000020. FT VARIANT 717 717 V -> F (in AD1). FT /FTId=VAR_000023. FT VARIANT 717 717 V -> G (in AD1). FT /FTId=VAR_000022. FT VARIANT 717 717 V -> I (in AD1). FT /FTId=VAR_000021. FT VARIANT 717 717 V -> L (in AD1). FT /FTId=VAR_014219. FT VARIANT 723 723 L -> P (in AD1). FT /FTId=VAR_010109. FT MUTAGEN 99 102 KRGR->NQGG: Reduced heparin-binding. FT MUTAGEN 137 137 H->N: Binds copper. Forms dimer. FT MUTAGEN 141 141 M->T: Binds copper. Forms dimer. FT MUTAGEN 144 144 C->S: Binds copper. No dimer formation. FT No copper reducing activity. FT MUTAGEN 147 149 HLH->ALA: 50% decrease in copper reducing FT activity. FT MUTAGEN 147 147 H->A: Some decrease in copper reducing FT activity. FT MUTAGEN 147 147 H->N: Binds copper. Forms dimer. FT MUTAGEN 147 147 H->Y: Greatly reduced copper-mediated FT low-density lipoprotein oxidation. FT MUTAGEN 151 151 H->K: Greatly reduced copper-mediated FT low-density lipoprotein oxidation. FT MUTAGEN 151 151 H->N: Binds copper. Forms dimer. FT MUTAGEN 198 198 S->A: Greatly reduced casein kinase FT phosphorylation. FT MUTAGEN 206 206 S->A: Reduced casein kinase FT phosphorylation. FT MUTAGEN 499 499 R->A: Reduced affinity for heparin; when FT associated with A-503. FT MUTAGEN 503 503 K->A: Reduced affinity for heparin; when FT associated with A-499. FT MUTAGEN 656 656 S->A: Abolishes chondroitin sulfate FT binding in L-APP733 isoform. FT MUTAGEN 676 676 R->G: 60-70% zinc-induced beta-APP (28) FT peptide aggregation. FT MUTAGEN 681 681 Y->F: 60-70% zinc-induced beta-APP (28) FT peptide aggregation. FT MUTAGEN 684 684 H->R: Only 23% zinc-induced beta-APP (28) FT peptide aggregation. FT MUTAGEN 704 704 G->V: Reduced protein oxidation. No FT hippocampal neuron toxicity. FT MUTAGEN 706 706 M->L: Reduced lipid peroxidation FT inhibition. FT MUTAGEN 706 706 M->V: No free radical production. No FT hippocampal neuron toxicity. FT MUTAGEN 717 717 V->C,S: Unchanged beta-APP42/total APP- FT beta ratio. FT MUTAGEN 717 717 V->F,G,I: Increased beta-APP42/beta-APP40 FT ratio. FT MUTAGEN 717 717 V->K: Decreased beta-APP42/total APP-beta FT ratio. FT MUTAGEN 717 717 V->M: Increased beta-APP42/beta-APP40 FT ratio. No change in apoptosis after FT caspase cleavage. FT MUTAGEN 728 728 Y->A: No effect on APBA1 nor APBB1 FT binding. Greatly reduces the binding to FT APPBP2. APP internalization unchanged. No FT change in beta-APP42 secretion. FT MUTAGEN 739 739 D->A: No cleavage by caspases during FT apoptosis. FT MUTAGEN 739 739 D->N: No effect on FADD-induced FT apoptosis. FT MUTAGEN 743 743 T->A: Greatly reduces the binding to SHC1 FT and APBB family members; no effect on FT NGF-stimulated neurite extension. FT MUTAGEN 743 743 T->E: Reduced NGF-stimulated neurite FT extension. No effect on APP maturation. FT MUTAGEN 756 756 G->A: APP internalization unchanged. No FT change in beta-APP42 secretion. FT MUTAGEN 757 757 Y->A: Little APP internalization. Reduced FT beta-APP42 secretion. FT MUTAGEN 757 757 Y->G: Loss of binding to MAPK8IP1, APBA1, FT APBB1, APPBP2 and SHC1. FT MUTAGEN 759 759 N->A: No binding to APBA1, no effect on FT APBB1 binding. Little APP FT internalization. Reduced beta-APP42 FT secretion. FT MUTAGEN 760 760 P->A: Little APP internalization. Reduced FT beta-APP42 secretion. FT MUTAGEN 762 762 Y->A: Loss of binding to APBA1 and APBB1. FT APP internalization unchanged. No change FT in beta-APP42 secretion. FT CONFLICT 15 16 AR -> VW (in Ref. 3; CAA31830). FT CONFLICT 647 647 D -> E (in Ref. 36; AAA51722). FT CONFLICT 724 724 Missing (in Ref. 23; AAB26263/AAB26264). FT CONFLICT 731 731 I -> N (in Ref. 23; AAB26263/AAB26264/ FT AAB26265). FT CONFLICT 757 757 Y -> S (in Ref. 31; AAA35540). FT STRAND 33 35 FT STRAND 43 45 FT TURN 47 49 FT STRAND 52 54 FT HELIX 66 76 FT STRAND 82 87 FT STRAND 92 94 FT STRAND 97 99 FT HELIX 100 102 FT STRAND 103 106 FT STRAND 110 112 FT STRAND 115 119 FT STRAND 134 139 FT HELIX 147 160 FT STRAND 163 174 FT TURN 175 177 FT STRAND 178 188 FT HELIX 288 292 FT STRAND 299 301 FT STRAND 304 310 FT TURN 311 314 FT STRAND 315 321 FT STRAND 323 325 FT STRAND 331 333 FT HELIX 334 341 FT HELIX 374 380 FT HELIX 389 418 FT STRAND 421 423 FT HELIX 425 480 FT STRAND 482 484 FT HELIX 487 518 FT HELIX 520 546 FT HELIX 547 550 FT HELIX 552 566 FT HELIX 673 675 FT STRAND 679 682 FT STRAND 683 685 FT STRAND 688 691 FT HELIX 695 697 FT STRAND 698 700 FT STRAND 702 705 FT STRAND 707 712 FT HELIX 744 754 FT STRAND 755 758 FT STRAND 763 765 SQ SEQUENCE 770 AA; 86943 MW; A12EE761403740F5 CRC64; MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSAMSQSLL KTTQEPLARD PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL QAVPPRPRHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET KTTVELLPVN GEFSLDDLQP WHSFGADSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN // ID AAAD_HUMAN Reviewed; 399 AA. AC P22760; A8K3L3; D3DNJ6; Q8N1A9; DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 5. DT 09-JUL-2014, entry version 133. DE RecName: Full=Arylacetamide deacetylase; DE EC=3.1.1.3; GN Name=AADAC; Synonyms=DAC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT RP ILE-281. RC TISSUE=Liver; RX PubMed=8063807; RA Probst M.R., Beer M., Beer D., Jenoe P., Meyer U.A., Gasser R.; RT "Human liver arylacetamide deacetylase. Molecular cloning of a novel RT esterase involved in the metabolic activation of arylamine carcinogens RT with high sequence similarity to hormone-sensitive lipase."; RL J. Biol. Chem. 269:21650-21656(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-281. RC TISSUE=Heart; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-281. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION. RC TISSUE=Liver; RX PubMed=2043131; DOI=10.1016/0006-291X(91)92005-5; RA Probst M.R., Jenoe P., Meyer U.A.; RT "Purification and characterization of a human liver arylacetamide RT deacetylase."; RL Biochem. Biophys. Res. Commun. 177:453-459(1991). RN [7] RP FUNCTION. RX PubMed=17936933; DOI=10.1002/jbt.20178; RA Ross M.K., Crow J.A.; RT "Human carboxylesterases and their role in xenobiotic and endobiotic RT metabolism."; RL J. Biochem. Mol. Toxicol. 21:187-196(2007). RN [8] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=19339378; DOI=10.1124/dmd.109.026567; RA Watanabe A., Fukami T., Nakajima M., Takamiya M., Aoki Y., Yokoi T.; RT "Human arylacetamide deacetylase is a principal enzyme in flutamide RT hydrolysis."; RL Drug Metab. Dispos. 37:1513-1520(2009). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78 AND ASN-282. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [10] RP BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=22207054; DOI=10.1124/dmd.111.043067; RA Kobayashi Y., Fukami T., Nakajima A., Watanabe A., Nakajima M., RA Yokoi T.; RT "Species differences in tissue distribution and enzyme activities of RT arylacetamide deacetylase in human, rat, and mouse."; RL Drug Metab. Dispos. 40:671-679(2012). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL RP PROPERTIES, VARIANTS ILE-281 AND GLN-399 EXT, AND CHARACTERIZATION OF RP VARIANTS ILE-281 AND GLN-399 EXT. RX PubMed=22415931; DOI=10.1124/dmd.112.044883; RA Shimizu M., Fukami T., Kobayashi Y., Takamiya M., Aoki Y., RA Nakajima M., Yokoi T.; RT "A novel polymorphic allele of human arylacetamide deacetylase leads RT to decreased enzyme activity."; RL Drug Metab. Dispos. 40:1183-1190(2012). RN [12] RP BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-78 AND ASN-282, RP AND MUTAGENESIS OF ASN-78 AND ASN-282. RX PubMed=24125761; DOI=10.1016/j.bcp.2013.10.001; RA Muta K., Fukami T., Nakajima M., Yokoi T.; RT "N-Glycosylation during translation is essential for human RT arylacetamide deacetylase enzyme activity."; RL Biochem. Pharmacol. 87:352-359(2014). RN [13] RP FUNCTION, AND INDUCTION. RX PubMed=23542347; DOI=10.1016/j.jhep.2013.03.022; RA Nourbakhsh M., Douglas D.N., Pu C.H., Lewis J.T., Kawahara T., RA Lisboa L.F., Wei E., Asthana S., Quiroga A.D., Law L.M., Chen C., RA Addison W.R., Nelson R., Houghton M., Lehner R., Kneteman N.M.; RT "Arylacetamide deacetylase: a novel host factor with important roles RT in the lipolysis of cellular triacylglycerol stores, VLDL assembly and RT HCV production."; RL J. Hepatol. 59:336-343(2013). RN [14] RP VARIANT ILE-281. RX PubMed=12721789; DOI=10.1007/s10038-003-0021-7; RA Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., RA Nakamura Y.; RT "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, RT nine esterase genes, and two other genes in the Japanese population."; RL J. Hum. Genet. 48:249-270(2003). CC -!- FUNCTION: Displays cellular triglyceride lipase activity in liver, CC increases the levels of intracellular fatty acids derived from the CC hydrolysis of newly formed triglyceride stores and plays a role in CC very low-density lipoprotein assembly. Displays serine esterase CC activity in liver. Deacetylates a variety of arylacetamide CC substrates, including xenobiotic compounds and procarcinogens, CC converting them to the primary arylamide compounds and increasing CC their toxicity. CC -!- CATALYTIC ACTIVITY: Triacylglycerol + H(2)O = diacylglycerol + a CC carboxylate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.8 mM for flutamide (PubMed:19339378); CC KM=0.6 mM for flutamide (PubMed:22207054); CC KM=0.472 mM for flutamide (PubMed:22415931); CC KM=3.05 mM for phenacetin (PubMed:24125761); CC KM=1.8 mM for phenacetin (PubMed:22207054); CC KM=1.42 mM for phenacetin (PubMed:22415931); CC KM=0.2 mM for rifampicin (PubMed:22207054); CC KM=0.154 mM for rifampicin (PubMed:22415931); CC Vmax=1.1 nmol/min/mg enzyme toward flutamide (PubMed:19339378); CC Vmax=1.1 nmol/min/mg enzyme toward flutamide (PubMed:22207054); CC Vmax=0.617 nmol/min/mg enzyme toward flutamide CC (PubMed:22415931); CC Vmax=1.34 nmol/min/mg enzyme toward phenacetin CC (PubMed:24125761); CC Vmax=6.4 nmol/min/mg enzyme toward phenacetin (PubMed:22207054); CC Vmax=1.42 nmol/min/mg enzyme toward phenacetin CC (PubMed:22415931); CC Vmax=0.149 nmol/min/mg enzyme toward rifampicin CC (PubMed:22207054); CC Vmax=0.060 nmol/min/mg enzyme toward rifampicin CC (PubMed:22415931); CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC type II membrane protein. Microsome membrane; Single-pass type II CC membrane protein. CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level). Mainly CC expressed in liver, small intestine, colon, adrenal gland and CC bladder. CC -!- INDUCTION: Down-regulated following infection with hepatis C virus CC which results in impaired triacylglycerol lipolysis and impaired CC assembly of very low density lipoproteins. This may represent a CC cellular adaptation to infection that is aimed at limiting viral CC production. CC -!- PTM: Glycosylation is required for enzyme activity. CC -!- POLYMORPHISM: Three alleles are known: AADAC*1, AADAC*2 and CC AADAC*3. The sequence shown is that of AADAC*1 which is found in CC European American, African American, Japanese and Korean CC populations at allelic frequencies of 39.3 to 47.4%. The AADAC*2 CC allele is found in European American, African American, Korean, CC and Japanese populations at allelic frequencies of 52.6 to 63.5% CC whereas the AADAC*3 allele is found in European American (1.3%) CC and African American (2.0%) samples but not in Japanese or Korean CC samples. CC -!- MISCELLANEOUS: Can hydrolyze a number of clinical drugs such as CC flutamide, an antiandrogen drug used for the treatment of prostate CC cancer; phenacetin, an analgesic antipyretic which has been CC withdrawn from the market due to its links with renal failure; and CC rifamycins which have been used as antituberculosis drugs. CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family. CC -!- SEQUENCE CAUTION: CC Sequence=AAA35551.1; Type=Frameshift; Positions=53, 56; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L32179; AAA35551.1; ALT_FRAME; mRNA. DR EMBL; AK290628; BAF83317.1; -; mRNA. DR EMBL; AC068647; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471052; EAW78791.1; -; Genomic_DNA. DR EMBL; CH471052; EAW78792.1; -; Genomic_DNA. DR EMBL; BC032309; AAH32309.1; -; mRNA. DR CCDS; CCDS33877.1; -. DR PIR; A53856; A53856. DR RefSeq; NP_001077.2; NM_001086.2. DR RefSeq; XP_005247160.1; XM_005247103.2. DR UniGene; Hs.506908; -. DR ProteinModelPortal; P22760; -. DR SMR; P22760; 69-379. DR BioGrid; 106531; 1. DR STRING; 9606.ENSP00000232892; -. DR MEROPS; S09.991; -. DR PhosphoSite; P22760; -. DR DMDM; 317373587; -. DR PaxDb; P22760; -. DR PRIDE; P22760; -. DR Ensembl; ENST00000232892; ENSP00000232892; ENSG00000114771. DR GeneID; 13; -. DR KEGG; hsa:13; -. DR UCSC; uc003eze.3; human. DR CTD; 13; -. DR GeneCards; GC03P151531; -. DR HGNC; HGNC:17; AADAC. DR HPA; HPA002911; -. DR MIM; 600338; gene. DR neXtProt; NX_P22760; -. DR PharmGKB; PA24363; -. DR eggNOG; COG0657; -. DR HOGENOM; HOG000033738; -. DR HOVERGEN; HBG058974; -. DR InParanoid; P22760; -. DR KO; K13616; -. DR OMA; YVYEPIP; -. DR OrthoDB; EOG7HB599; -. DR PhylomeDB; P22760; -. DR TreeFam; TF314978; -. DR SABIO-RK; P22760; -. DR GeneWiki; AADAC; -. DR GenomeRNAi; 13; -. DR NextBio; 27; -. DR PRO; PR:P22760; -. DR ArrayExpress; P22760; -. DR Bgee; P22760; -. DR CleanEx; HS_AADAC; -. DR Genevestigator; P22760; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; TAS:ProtInc. DR GO; GO:0019213; F:deacetylase activity; IDA:UniProtKB. DR GO; GO:0016298; F:lipase activity; TAS:UniProtKB. DR GO; GO:0017171; F:serine hydrolase activity; IDA:UniProtKB. DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB. DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISS:UniProtKB. DR Gene3D; 3.40.50.1820; -; 2. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR013094; AB_hydrolase_3. DR InterPro; IPR017157; Arylacetamide_deacetylase. DR InterPro; IPR002168; Lipase_GDXG_AS. DR Pfam; PF07859; Abhydrolase_3; 2. DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1. DR SUPFAM; SSF53474; SSF53474; 1. DR PROSITE; PS01174; LIPASE_GDXG_SER; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Disulfide bond; KW Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane; Microsome; KW Polymorphism; Reference proteome; Signal-anchor; Transmembrane; KW Transmembrane helix. FT CHAIN 1 399 Arylacetamide deacetylase. FT /FTId=PRO_0000071542. FT TOPO_DOM 1 5 Cytoplasmic (Potential). FT TRANSMEM 6 23 Helical; Signal-anchor for type II FT membrane protein; (Potential). FT TOPO_DOM 24 399 Lumenal (Potential). FT MOTIF 111 113 Involved in the stabilization of the FT negatively charged intermediate by the FT formation of the oxyanion hole (By FT similarity). FT ACT_SITE 111 111 Potential. FT ACT_SITE 189 189 Potential. FT CARBOHYD 78 78 N-linked (GlcNAc...). FT CARBOHYD 282 282 N-linked (GlcNAc...). FT DISULFID 116 340 By similarity. FT VARIANT 281 281 V -> I (in alleles AADAC*2 and AADAC*3; FT mildly decreased enzyme activity; FT dbSNP:rs1803155). FT /FTId=VAR_014798. FT VARIANT 399 399 L -> LQ (in allele AADAC*3; decreased FT enzyme activity). FT /FTId=VAR_070543. FT MUTAGEN 78 78 N->Q: Abolishes glycosylation at this FT site and causes moderate decrease in FT activity. FT MUTAGEN 282 282 N->Q: Abolishes glycosylation at this FT site and causes substantial decrease in FT activity and reduced substrate affinity. FT CONFLICT 3 3 R -> M (in Ref. 6; AA sequence). FT CONFLICT 55 57 LHH -> VHI (in Ref. 1; AAA35551). SQ SEQUENCE 399 AA; 45734 MW; 34F9CB717DD7417A CRC64; MGRKSLYLLI VGILIAYYIY TPLPDNVEEP WRMMWINAHL KTIQNLATFV ELLGLHHFMD SFKVVGSFDE VPPTSDENVT VTETKFNNIL VRVYVPKRKS EALRRGLFYI HGGGWCVGSA ALSGYDLLSR WTADRLDAVV VSTNYRLAPK YHFPIQFEDV YNALRWFLRK KVLAKYGVNP ERIGISGDSA GGNLAAAVTQ QLLDDPDVKI KLKIQSLIYP ALQPLDVDLP SYQENSNFLF LSKSLMVRFW SEYFTTDRSL EKAMLSRQHV PVESSHLFKF VNWSSLLPER FIKGHVYNNP NYGSSELAKK YPGFLDVRAA PLLADDNKLR GLPLTYVITC QYDLLRDDGL MYVTRLRNTG VQVTHNHVED GFHGAFSFLG LKISHRLINQ YIEWLKENL // ID AAAS_HUMAN Reviewed; 546 AA. AC Q9NRG9; Q5JB47; Q9NWI6; Q9UG19; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-JUL-2014, entry version 132. DE RecName: Full=Aladin; DE AltName: Full=Adracalin; GN Name=AAAS; Synonyms=ADRACALA; ORFNames=GL003; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RX PubMed=11062474; DOI=10.1038/81642; RA Tullio-Pelet A., Salomon R., Hadj-Rabia S., Mugnier C., de Laet M.-H., RA Chaouachi B., Bakiri F., Brottier P., Cattolico L., Penet C., RA Begeot M., Naville D., Nicolino M., Chaussain J.-L., Weissenbach J., RA Munnich A., Lyonnet S.; RT "Mutant WD-repeat protein in triple-A syndrome."; RL Nat. Genet. 26:332-335(2000). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS AAAS LYS-15; ARG-160 RP AND PRO-263. RX PubMed=11159947; DOI=10.1093/hmg/10.3.283; RA Handschug K., Sperling S., Yoon S.-J.K., Hennig S., Clark A.J.L., RA Huebner A.; RT "Triple A syndrome is caused by mutations in AAAS, a new WD-repeat RT protein gene."; RL Hum. Mol. Genet. 10:283-290(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=16022285; DOI=10.1007/s11033-004-6939-9; RA Li X., Ji C., Gu J., Xu J., Jin Z., Sun L., Zou X., Lin Y., Sun R., RA Wang P., Gu S., Mao Y.; RT "Molecular cloning and characterization of AAAS-V2, a novel splice RT variant of human AAAS."; RL Mol. Biol. Rep. 32:127-131(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.; RT "A novel gene expressed in human liver non-tumor tissues."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adipose tissue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 210-546 (ISOFORM 1). RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP SUBCELLULAR LOCATION, AND INTERACTION WITH NDC1. RX PubMed=19782045; DOI=10.1016/j.bbrc.2009.09.080; RA Kind B., Koehler K., Lorenz M., Huebner A.; RT "The nuclear pore complex protein ALADIN is anchored via NDC1 but not RT via POM121 and GP210 in the nuclear envelope."; RL Biochem. Biophys. Res. Commun. 390:205-210(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-495, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT CYS-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Plays a role in the normal development of the peripheral CC and central nervous system. CC -!- SUBUNIT: Interacts with NDC1, the interaction is required for CC nuclear pore localization. CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=AAAS-v1; CC IsoId=Q9NRG9-1; Sequence=Displayed; CC Name=2; Synonyms=AAAS-v2; CC IsoId=Q9NRG9-2; Sequence=VSP_043014; CC Note=Ubiquitously expressed; CC -!- TISSUE SPECIFICITY: Widely expressed. Particularly abundant CC expression is found in cerebellum, corpus callosum, adrenal gland, CC pituitary gland, gastrointestinal structures and fetal lung. CC -!- DISEASE: Achalasia-addisonianism-alacrima syndrome (AAAS) CC [MIM:231550]: An autosomal recessive disorder characterized by CC adreno-corticotropic hormone (ACTH)-resistant adrenal failure, CC achalasia of the esophageal cardia and alacrima. The syndrome is CC associated with variable and progressive neurological impairment CC involving the central, peripheral, and autonomic nervous system. CC Other features such as palmoplantar hyperkeratosis, short stature, CC facial dysmorphy and osteoporosis may also be present. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- SIMILARITY: Contains 4 WD repeats. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ289857; CAC19017.1; -; mRNA. DR EMBL; AJ289841; CAC19038.1; -; Genomic_DNA. DR EMBL; AJ289842; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289843; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289844; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289845; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289846; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289847; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289848; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289849; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289850; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289851; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289852; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289853; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289854; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289855; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ289856; CAC19038.1; JOINED; Genomic_DNA. DR EMBL; AJ297977; CAC17465.1; -; Genomic_DNA. DR EMBL; AY237818; AAP69911.1; -; mRNA. DR EMBL; AF226048; AAF86948.1; -; mRNA. DR EMBL; AK000833; BAA91394.1; -; mRNA. DR EMBL; BT006912; AAP35558.1; -; mRNA. DR EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000659; AAH00659.1; -; mRNA. DR EMBL; AL110160; CAB53665.2; -; mRNA. DR CCDS; CCDS53797.1; -. [Q9NRG9-2] DR CCDS; CCDS8856.1; -. [Q9NRG9-1] DR RefSeq; NP_001166937.1; NM_001173466.1. [Q9NRG9-2] DR RefSeq; NP_056480.1; NM_015665.5. [Q9NRG9-1] DR UniGene; Hs.369144; -. DR ProteinModelPortal; Q9NRG9; -. DR SMR; Q9NRG9; 154-179, 247-273. DR BioGrid; 113759; 3. DR IntAct; Q9NRG9; 1. DR MINT; MINT-3073010; -. DR STRING; 9606.ENSP00000209873; -. DR PhosphoSite; Q9NRG9; -. DR DMDM; 20137527; -. DR MaxQB; Q9NRG9; -. DR PaxDb; Q9NRG9; -. DR PRIDE; Q9NRG9; -. DR DNASU; 8086; -. DR Ensembl; ENST00000209873; ENSP00000209873; ENSG00000094914. [Q9NRG9-1] DR Ensembl; ENST00000394384; ENSP00000377908; ENSG00000094914. [Q9NRG9-2] DR GeneID; 8086; -. DR KEGG; hsa:8086; -. DR UCSC; uc001scr.4; human. [Q9NRG9-1] DR UCSC; uc001scs.4; human. [Q9NRG9-2] DR CTD; 8086; -. DR GeneCards; GC12M053701; -. DR HGNC; HGNC:13666; AAAS. DR HPA; HPA040086; -. DR MIM; 231550; phenotype. DR MIM; 605378; gene. DR neXtProt; NX_Q9NRG9; -. DR Orphanet; 869; Triple A syndrome. DR PharmGKB; PA24361; -. DR eggNOG; NOG314927; -. DR HOGENOM; HOG000033741; -. DR HOVERGEN; HBG026353; -. DR InParanoid; Q9NRG9; -. DR KO; K14320; -. DR OMA; GEGKGCV; -. DR OrthoDB; EOG7JQBN1; -. DR PhylomeDB; Q9NRG9; -. DR TreeFam; TF324412; -. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR Reactome; REACT_21300; Mitotic M-M/G1 phases. DR Reactome; REACT_6900; Immune System. DR SignaLink; Q9NRG9; -. DR ChiTaRS; AAAS; human. DR GeneWiki; AAAS_(gene); -. DR GenomeRNAi; 8086; -. DR NextBio; 30710; -. DR PRO; PR:Q9NRG9; -. DR ArrayExpress; Q9NRG9; -. DR Bgee; Q9NRG9; -. DR CleanEx; HS_AAAS; -. DR Genevestigator; Q9NRG9; -. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005635; C:nuclear envelope; TAS:Reactome. DR GO; GO:0031965; C:nuclear membrane; IDA:HPA. DR GO; GO:0005643; C:nuclear pore; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProt. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome. DR GO; GO:0009566; P:fertilization; IEA:Ensembl. DR GO; GO:0015758; P:glucose transport; TAS:Reactome. DR GO; GO:0008645; P:hexose transport; TAS:Reactome. DR GO; GO:0007612; P:learning; IEA:Ensembl. DR GO; GO:0000278; P:mitotic cell cycle; TAS:Reactome. DR GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome. DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI. DR GO; GO:0010827; P:regulation of glucose transport; TAS:Reactome. DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; NAS:UniProtKB. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0016032; P:viral process; TAS:Reactome. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_dom. DR Pfam; PF00400; WD40; 1. DR SMART; SM00320; WD40; 4. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; KW Disease mutation; mRNA transport; Nuclear pore complex; Nucleus; KW Phosphoprotein; Protein transport; Reference proteome; Repeat; KW Translocation; Transport; WD repeat. FT INIT_MET 1 1 Removed. FT CHAIN 2 546 Aladin. FT /FTId=PRO_0000050828. FT REPEAT 149 188 WD 1. FT REPEAT 191 230 WD 2. FT REPEAT 243 282 WD 3. FT REPEAT 285 324 WD 4. FT MOTIF 544 546 Microbody targeting signal (Potential). FT MOD_RES 2 2 N-acetylcysteine. FT MOD_RES 33 33 Phosphoserine. FT MOD_RES 495 495 Phosphoserine. FT VAR_SEQ 149 182 WSSCCLRVFAWHPHTNKFAVALLDDSVRVYNASS -> C FT (in isoform 2). FT /FTId=VSP_043014. FT VARIANT 15 15 Q -> K (in AAAS). FT /FTId=VAR_012804. FT VARIANT 108 108 K -> M (in dbSNP:rs13330). FT /FTId=VAR_037060. FT VARIANT 160 160 H -> R (in AAAS). FT /FTId=VAR_012805. FT VARIANT 263 263 S -> P (in AAAS; dbSNP:rs121918550). FT /FTId=VAR_012806. FT CONFLICT 122 122 S -> P (in Ref. 5; BAA91394). FT CONFLICT 135 135 R -> K (in Ref. 5; BAA91394). FT CONFLICT 479 479 I -> V (in Ref. 5; BAA91394). SQ SEQUENCE 546 AA; 59574 MW; E0F4E7145D8C192E CRC64; MCSLGLFPPP PPRGQVTLYE HNNELVTGSS YESPPPDFRG QWINLPVLQL TKDPLKTPGR LDHGTRTAFI HHREQVWKRC INIWRDVGLF GVLNEIANSE EEVFEWVKTA SGWALALCRW ASSLHGSLFP HLSLRSEDLI AEFAQVTNWS SCCLRVFAWH PHTNKFAVAL LDDSVRVYNA SSTIVPSLKH RLQRNVASLA WKPLSASVLA VACQSCILIW TLDPTSLSTR PSSGCAQVLS HPGHTPVTSL AWAPSGGRLL SASPVDAAIR VWDVSTETCV PLPWFRGGGV TNLLWSPDGS KILATTPSAV FRVWEAQMWT CERWPTLSGR CQTGCWSPDG SRLLFTVLGE PLIYSLSFPE RCGEGKGCVG GAKSATIVAD LSETTIQTPD GEERLGGEAH SMVWDPSGER LAVLMKGKPR VQDGKPVILL FRTRNSPVFE LLPCGIIQGE PGAQPQLITF HPSFNKGALL SVGWSTGRIA HIPLYFVNAQ FPRFSPVLGR AQEPPAGGGG SIHDLPLFTE TSPTSAPWDP LPGPPPVLPH SPHSHL // ID AAAT_HUMAN Reviewed; 541 AA. AC Q15758; A8K9H5; B4DR77; B4DWS4; B7ZB81; D0EYG6; E9PC01; O95720; AC Q96RL9; Q9BWQ3; Q9UNP2; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2002, sequence version 2. DT 09-JUL-2014, entry version 140. DE RecName: Full=Neutral amino acid transporter B(0); DE Short=ATB(0); DE AltName: Full=Baboon M7 virus receptor; DE AltName: Full=RD114/simian type D retrovirus receptor; DE AltName: Full=Sodium-dependent neutral amino acid transporter type 2; DE AltName: Full=Solute carrier family 1 member 5; GN Name=SLC1A5; Synonyms=ASCT2, M7V1, RDR, RDRC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Choriocarcinoma; RX PubMed=8702519; DOI=10.1074/jbc.271.31.18657; RA Kekuda R., Prasad P.D., Fei Y.-J., Torres-Zamorano V., Sinha S., RA Yang-Feng T.L., Leibach F.H., Ganapathy V.; RT "Cloning of the sodium-dependent, broad-scope, neutral amino acid RT transporter Bo from a human placental choriocarcinoma cell line."; RL J. Biol. Chem. 271:18657-18661(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A VIRAL RP RECEPTOR. RX PubMed=10051606; DOI=10.1073/pnas.96.5.2129; RA Rasko J.E.J., Battini J.L., Gottschalk R.J., Mazo I., Miller A.D.; RT "The RD114/simian type D retrovirus receptor is a neutral amino acid RT transporter."; RL Proc. Natl. Acad. Sci. U.S.A. 96:2129-2134(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A VIRAL RP RECEPTOR. RX PubMed=10196349; RA Tailor C.S., Nouri A., Zhao Y., Takeuchi Y., Kabat D.; RT "A sodium-dependent neutral-amino-acid transporter mediates infections RT of feline and baboon endogenous retroviruses and simian type D RT retroviruses."; RL J. Virol. 73:4470-4474(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Ouyang D.-Y., Xu L.-H., He X.-H., Zha Q.-B., Guo H., Gao Q., RA Zhang Y.-T.; RT "Cloning of ASCT2 cDNA from MCF-7 cells and its expression in B16 RT cells."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND RP VARIANT LEU-512. RC TISSUE=Esophagus, and Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-541 (ISOFORM 1), AND ALTERNATIVE RP INITIATION. RX PubMed=11350958; DOI=10.1074/jbc.M100737200; RA Tailor C.S., Marin M., Nouri A., Kavanaugh M.P., Kabat D.; RT "Truncated forms of the dual function human ASCT2 neutral amino acid RT transporter/retroviral receptor are translationally initiated at RT multiple alternative CUG and GUG codons."; RL J. Biol. Chem. 276:27221-27230(2001). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [11] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., RA Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-535, VARIANT RP [LARGE SCALE ANALYSIS] LEU-512, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Has a broad substrate specificity, a preference for CC zwitterionic amino acids, and a sodium-dependence. It accepts as CC substrates all neutral amino acids, including glutamine, CC asparagine, and branched-chain and aromatic amino acids, and CC excludes methylated amino acids, anionic amino acids, and cationic CC amino acids. Acts as a cell surface receptor for feline endogenous CC virus RD114, baboon M7 endogenous virus and type D simian CC retroviruses. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Probable). Melanosome. Note=Identified by mass spectrometry in CC melanosome fractions from stage I to stage IV. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=3; CC Comment=A number of isoforms are produced by alternative CC initiation. Isoforms start at multiple alternative CUG and GUG CC codons; CC Name=1; CC IsoId=Q15758-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15758-2; Sequence=VSP_046354; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q15758-3; Sequence=VSP_046851; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Placenta, lung, skeletal muscle, kidney, CC pancreas, and intestine. CC -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter CC (TC 2.A.23) family. SLC1A5 subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U53347; AAC50629.1; -; mRNA. DR EMBL; AF102826; AAD09812.1; -; mRNA. DR EMBL; AF105423; AAD27806.1; -; mRNA. DR EMBL; GQ919058; ACX53626.1; -; mRNA. DR EMBL; AK292690; BAF85379.1; -; mRNA. DR EMBL; AK299137; BAG61189.1; -; mRNA. DR EMBL; AK301661; BAG63136.1; -; mRNA. DR EMBL; AK316546; BAH14917.1; -; mRNA. DR EMBL; AC008622; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471126; EAW57446.1; -; Genomic_DNA. DR EMBL; BC000062; AAH00062.1; -; mRNA. DR EMBL; AF334818; AAK77026.1; -; mRNA. DR CCDS; CCDS12692.1; -. [Q15758-1] DR CCDS; CCDS46125.1; -. [Q15758-2] DR CCDS; CCDS46126.1; -. [Q15758-3] DR RefSeq; NP_001138616.1; NM_001145144.1. [Q15758-3] DR RefSeq; NP_001138617.1; NM_001145145.1. [Q15758-2] DR RefSeq; NP_005619.1; NM_005628.2. [Q15758-1] DR UniGene; Hs.631582; -. DR ProteinModelPortal; Q15758; -. DR SMR; Q15758; 59-482. DR BioGrid; 112401; 15. DR IntAct; Q15758; 6. DR MINT; MINT-5001314; -. DR STRING; 9606.ENSP00000303623; -. DR DrugBank; DB00174; L-Asparagine. DR DrugBank; DB00130; L-Glutamine. DR GuidetoPHARMACOLOGY; 874; -. DR TCDB; 2.A.23.3.3; the dicarboxylate/amino acid:cation (na(+) or h(+)) symporter (daacs) family. DR PhosphoSite; Q15758; -. DR DMDM; 21542389; -. DR MaxQB; Q15758; -. DR PaxDb; Q15758; -. DR PeptideAtlas; Q15758; -. DR PRIDE; Q15758; -. DR DNASU; 6510; -. DR Ensembl; ENST00000412532; ENSP00000397924; ENSG00000105281. [Q15758-3] DR Ensembl; ENST00000434726; ENSP00000406532; ENSG00000105281. [Q15758-2] DR Ensembl; ENST00000542575; ENSP00000444408; ENSG00000105281. [Q15758-1] DR GeneID; 6510; -. DR KEGG; hsa:6510; -. DR UCSC; uc002pfr.3; human. [Q15758-1] DR CTD; 6510; -. DR GeneCards; GC19M047278; -. DR H-InvDB; HIX0015262; -. DR HGNC; HGNC:10943; SLC1A5. DR HPA; HPA035239; -. DR HPA; HPA035240; -. DR MIM; 109190; gene. DR neXtProt; NX_Q15758; -. DR PharmGKB; PA35830; -. DR eggNOG; COG1301; -. DR HOVERGEN; HBG000080; -. DR InParanoid; Q15758; -. DR KO; K05616; -. DR OMA; LVRNIFP; -. DR OrthoDB; EOG7RV9G2; -. DR PhylomeDB; Q15758; -. DR TreeFam; TF315206; -. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR Reactome; REACT_19419; Amino acid and oligopeptide SLC transporters. DR ChiTaRS; SLC1A5; human. DR GeneWiki; SLC1A5; -. DR GenomeRNAi; 6510; -. DR NextBio; 25315; -. DR PRO; PR:Q15758; -. DR ArrayExpress; Q15758; -. DR Bgee; Q15758; -. DR CleanEx; HS_SLC1A5; -. DR Genevestigator; Q15758; -. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0015186; F:L-glutamine transmembrane transporter activity; TAS:BHF-UCL. DR GO; GO:0015194; F:L-serine transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; TAS:ProtInc. DR GO; GO:0004872; F:receptor activity; TAS:ProtInc. DR GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0006865; P:amino acid transport; TAS:Reactome. DR GO; GO:0006860; P:extracellular amino acid transport; IEA:Ensembl. DR GO; GO:0006868; P:glutamine transport; TAS:BHF-UCL. DR GO; GO:0006811; P:ion transport; TAS:Reactome. DR GO; GO:0015804; P:neutral amino acid transport; TAS:ProtInc. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR Gene3D; 1.10.3860.10; -; 1. DR InterPro; IPR001991; Na-dicarboxylate_symporter. DR InterPro; IPR018107; Na-dicarboxylate_symporter_CS. DR PANTHER; PTHR11958; PTHR11958; 1. DR Pfam; PF00375; SDF; 1. DR PRINTS; PR00173; EDTRNSPORT. DR SUPFAM; SSF118215; SSF118215; 1. DR PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1. DR PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative initiation; Alternative splicing; KW Complete proteome; Glycoprotein; Host cell receptor for virus entry; KW Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome; KW Symport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 541 Neutral amino acid transporter B(0). FT /FTId=PRO_0000202082. FT TOPO_DOM 1 52 Cytoplasmic (Potential). FT TRANSMEM 53 73 Helical; (Potential). FT TRANSMEM 99 119 Helical; (Potential). FT TRANSMEM 133 153 Helical; (Potential). FT TOPO_DOM 154 224 Extracellular (Potential). FT TRANSMEM 225 245 Helical; (Potential). FT TRANSMEM 266 286 Helical; (Potential). FT TRANSMEM 306 326 Helical; (Potential). FT TRANSMEM 336 356 Helical; (Potential). FT TRANSMEM 377 397 Helical; (Potential). FT TRANSMEM 399 419 Helical; (Potential). FT TRANSMEM 426 446 Helical; (Potential). FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 493 493 Phosphoserine. FT MOD_RES 503 503 Phosphoserine. FT MOD_RES 535 535 Phosphoserine. FT CARBOHYD 163 163 N-linked (GlcNAc...) (Potential). FT CARBOHYD 212 212 N-linked (GlcNAc...). FT VAR_SEQ 1 228 Missing (in isoform 3). FT /FTId=VSP_046851. FT VAR_SEQ 1 203 MVADPPRDSKGLAAAEPTANGGLALASIEDQGAAAGGYCGS FT RDQVRRCLRANLLVLLTVVAVVAGVALGLGVSGAGGALALG FT PERLSAFVFPGELLLRLLRMIILPLVVCSLIGGAASLDPGA FT LGRLGAWALLFFLVTTLLASALGVGLALALQPGAASAAINA FT SVGAAGSAENAPSKEVLDSFLDLARNIFPSNLVSAAFRS FT -> M (in isoform 2). FT /FTId=VSP_046354. FT VARIANT 17 17 P -> A (in dbSNP:rs3027956). FT /FTId=VAR_020439. FT VARIANT 512 512 V -> L (in dbSNP:rs3027961). FT /FTId=VAR_013517. FT CONFLICT 18 24 TANGGLA -> PPTGAWQ (in Ref. 1; AAC50629). FT CONFLICT 44 44 Q -> L (in Ref. 1; AAC50629). FT CONFLICT 84 87 ERLS -> GALE (in Ref. 1; AAC50629). FT CONFLICT 341 341 V -> A (in Ref. 5; BAH14917). FT CONFLICT 453 453 I -> V (in Ref. 2; AAD09812). FT CONFLICT 460 460 D -> G (in Ref. 2; AAD09812). FT CONFLICT 463 463 V -> A (in Ref. 2; AAD09812). FT CONFLICT 508 508 D -> G (in Ref. 2; AAD09812). SQ SEQUENCE 541 AA; 56598 MW; AD61C789CCFFE934 CRC64; MVADPPRDSK GLAAAEPTAN GGLALASIED QGAAAGGYCG SRDQVRRCLR ANLLVLLTVV AVVAGVALGL GVSGAGGALA LGPERLSAFV FPGELLLRLL RMIILPLVVC SLIGGAASLD PGALGRLGAW ALLFFLVTTL LASALGVGLA LALQPGAASA AINASVGAAG SAENAPSKEV LDSFLDLARN IFPSNLVSAA FRSYSTTYEE RNITGTRVKV PVGQEVEGMN ILGLVVFAIV FGVALRKLGP EGELLIRFFN SFNEATMVLV SWIMWYAPVG IMFLVAGKIV EMEDVGLLFA RLGKYILCCL LGHAIHGLLV LPLIYFLFTR KNPYRFLWGI VTPLATAFGT SSSSATLPLM MKCVEENNGV AKHISRFILP IGATVNMDGA ALFQCVAAVF IAQLSQQSLD FVKIITILVT ATASSVGAAG IPAGGVLTLA IILEAVNLPV DHISLILAVD WLVDRSCTVL NVEGDALGAG LLQNYVDRTE SRSTEPELIQ VKSELPLDPL PVPTEEGNPL LKHYRGPAGD ATVASEKESV M // ID AACT_HUMAN Reviewed; 423 AA. AC P01011; B3KVQ7; Q13703; Q2TU87; Q2TU88; Q59GP9; Q6LBY8; Q6LDT7; AC Q6NSC9; Q8N177; Q96DW8; Q9UC47; Q9UNU9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 2. DT 09-JUL-2014, entry version 180. DE RecName: Full=Alpha-1-antichymotrypsin; DE Short=ACT; DE AltName: Full=Cell growth-inhibiting gene 24/25 protein; DE AltName: Full=Serpin A3; DE Contains: DE RecName: Full=Alpha-1-antichymotrypsin His-Pro-less; DE Flags: Precursor; GN Name=SERPINA3; Synonyms=AACT; ORFNames=GIG24, GIG25; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=6606438; DOI=10.1021/bi00291a001; RA Chandra T., Stackhouse R., Kidd V.J., Robson K.J.H., Woo S.L.C.; RT "Sequence homology between human alpha 1-antichymotrypsin, alpha 1- RT antitrypsin, and antithrombin III."; RL Biochemistry 22:5055-5061(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS BOCHUM-1 PRO-78 AND RP BONN-1 ALA-252. RX PubMed=8244391; DOI=10.1006/geno.1993.1396; RA Poller W., Faber J.-P., Weidinger S., Tief K., Scholz S., Fischer M., RA Olek K., Kirchgesser M., Heidtmann H.-H.; RT "A leucine-to-proline substitution causes a defective alpha 1- RT antichymotrypsin allele associated with familial obstructive lung RT disease."; RL Genomics 17:740-743(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-9. RA Kim J.W.; RT "Identification of a human cell growth inhibiting gene."; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-9. RC TISSUE=Urinary bladder; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-9. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND RP VARIANTS THR-9 AND ARG-267. RC TISSUE=Brain, Liver, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-46, AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX PubMed=3257719; DOI=10.1016/0092-8674(88)90462-X; RA Abraham C.R., Selkoe D.J., Potter H.; RT "Immunochemical identification of the serine protease inhibitor alpha RT 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's RT disease."; RL Cell 52:487-501(1988). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-423 (ISOFORM 1), AND TISSUE RP SPECIFICITY. RC TISSUE=Hippocampus; RX PubMed=9880565; DOI=10.1074/jbc.274.3.1821; RA Hwang S.-R., Steineckert B., Kohn A., Palkovits M., Hook V.Y.H.; RT "Molecular studies define the primary structure of alpha1- RT antichymotrypsin (ACT) protease inhibitor in Alzheimer's disease RT brains. Comparison of act in hippocampus and liver."; RL J. Biol. Chem. 274:1821-1827(1999). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-86 AND 130-423 (ISOFORM 1). RA Rubin H.; RL Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases. RN [10] RP PROTEIN SEQUENCE OF 24-34. RX PubMed=2787670; DOI=10.1016/0167-4838(89)90139-8; RA Lindmark B., Hilja H., Alan R., Eriksson S.; RT "The microheterogeneity of desialylated alpha 1-antichymotrypsin: the RT occurrence of two amino-terminal isoforms, one lacking a His-Pro RT dipeptide."; RL Biochim. Biophys. Acta 997:90-95(1989). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-45. RX PubMed=7521171; DOI=10.1515/bchm3.1994.375.5.335; RA Korzus E., Luisetti M., Travis J.; RT "Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase RT inhibitor, and alpha-2-macroglobulin with the fungal enzyme, RT seaprose."; RL Biol. Chem. Hoppe-Seyler 375:335-341(1994). RN [12] RP PROTEIN SEQUENCE OF 41-60. RX PubMed=6687683; DOI=10.1016/0006-291X(83)90325-X; RA Morii M., Travis J.; RT "Structural alterations in alpha 1-antichymotrypsin from normal and RT acute phase human plasma."; RL Biochem. Biophys. Res. Commun. 111:438-443(1983). RN [13] RP PROTEIN SEQUENCE OF 48-68 (ISOFORMS 1/2). RX PubMed=8647626; RX DOI=10.1002/(SICI)1097-0215(19960529)66:5<636::AID-IJC10>3.0.CO;2-2; RA Pinczower G.D., Williams R.P.W., Gianello R.D., Robinson H.C., RA Preston B.N., Linnane A.W.; RT "Characterisation of the tumour-associated carbohydrate epitope RT recognised by monoclonal antibody 4D3."; RL Int. J. Cancer 66:636-644(1996). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 87-129 (ISOFORMS 1/2), AND FUNCTION. RC TISSUE=Liver; RX PubMed=2404007; RA Rubin H., Wang Z., Nickbarg E.B., McLarney S., Naidoo N., RA Schoenberger O.L., Johnson J.L., Cooperman B.S.; RT "Cloning, expression, purification, and biological activity of RT recombinant native and variant human alpha 1-antichymotrypsins."; RL J. Biol. Chem. 265:1199-1207(1990). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-423. RX PubMed=6547997; DOI=10.1038/311175a0; RA Hill R.E., Shaw P.H., Boyd P.A., Baumann H., Hastie N.D.; RT "Plasma protease inhibitors in mouse and man: divergence within the RT reactive centre regions."; RL Nature 311:175-177(1984). RN [16] RP REACTIVE SITE. RX PubMed=6556193; RA Morii M., Travis J.; RT "Amino acid sequence at the reactive site of human alpha 1- RT antichymotrypsin."; RL J. Biol. Chem. 258:12749-12752(1983). RN [17] RP GLYCOSYLATION AT ASN-93 AND ASN-106. RX PubMed=12754519; DOI=10.1038/nbt827; RA Zhang H., Li X.-J., Martin D.B., Aebersold R.; RT "Identification and quantification of N-linked glycoproteins using RT hydrazide chemistry, stable isotope labeling and mass spectrometry."; RL Nat. Biotechnol. 21:660-666(2003). RN [18] RP INTERACTION WITH DNAJC1. RX PubMed=14668352; DOI=10.1074/jbc.M310903200; RA Kroczynska B., Evangelista C.M., Samant S.S., Elguindi E.C., RA Blond S.Y.; RT "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human RT homologue interacts with alpha1-antichymotrypsin and kinetically RT interferes with its serpin inhibitory activity."; RL J. Biol. Chem. 279:11432-11443(2004). RN [19] RP REGION RCL. RX PubMed=15638460; DOI=10.1007/s00239-004-2640-9; RA Horvath A.J., Forsyth S.L., Coughlin P.B.; RT "Expression patterns of murine antichymotrypsin-like genes reflect RT evolutionary divergence at the Serpina3 locus."; RL J. Mol. Evol. 59:488-497(2004). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-93; ASN-106; RP ASN-127; ASN-186 AND ASN-271. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [22] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93; ASN-106; ASN-127 AND RP ASN-271. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [23] RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=23234360; DOI=10.1021/pr300963h; RA Halim A., Ruetschi U., Larson G., Nilsson J.; RT "LC-MS/MS characterization of O-glycosylation sites and glycan RT structures of human cerebrospinal fluid glycoproteins."; RL J. Proteome Res. 12:573-584(2013). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-423. RX PubMed=2016749; DOI=10.1016/0022-2836(91)90704-A; RA Baumann U., Huber R., Bode W., Grosse D., Lesjak M., Laurell C.-B.; RT "Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7-A RT resolution and its comparison with other serpins."; RL J. Mol. Biol. 218:595-606(1991). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370 RP AND ARG-372. RX PubMed=8836107; DOI=10.1038/nsb1096-888; RA Lukacs C.M., Zhong J.Q., Plotnick M.I., Rubin H., Cooperman B.S., RA Christianson D.W.; RT "Arginine substitutions in the hinge region of antichymotrypsin affect RT serpin beta-sheet rearrangement."; RL Nat. Struct. Biol. 3:888-893(1996). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370; RP ARG-372 AND ARG-374. RX PubMed=9521649; DOI=10.1021/bi972359e; RA Lukacs C.M., Rubin H., Christianson D.W.; RT "Engineering an anion-binding cavity in antichymotrypsin modulates the RT 'spring-loaded' serpin-protease interaction."; RL Biochemistry 37:3297-3304(1998). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 26-423. RX PubMed=10618372; DOI=10.1073/pnas.97.1.67; RA Gooptu B., Hazes B., Chang W.-S.W., Dafforn T.R., Carrell R.W., RA Read R.J., Lomas D.A.; RT "Inactive conformation of the serpin alpha(1)-antichymotrypsin RT indicates two-stage insertion of the reactive loop: implications for RT inhibitory function and conformational disease."; RL Proc. Natl. Acad. Sci. U.S.A. 97:67-72(2000). RN [28] RP VARIANT ISEHARA-1 VAL-401. RX PubMed=1618300; DOI=10.1016/0014-5793(92)80590-D; RA Tsuda M., Sei Y., Yamamura M., Yamamoto M., Shinohara Y.; RT "Detection of a new mutant alpha-1-antichymotrypsin in patients with RT occlusive-cerebrovascular disease."; RL FEBS Lett. 304:66-68(1992). RN [29] RP VARIANT BONN-1 ALA-252. RX PubMed=1351206; DOI=10.1016/0140-6736(92)91301-N; RA Poller W., Faber J.-P., Scholz S., Weindinger S., Bartholome K., RA Olek K., Eriksson S.; RT "Mis-sense mutation of alpha 1-antichymotrypsin gene associated with RT chronic lung disease."; RL Lancet 339:1538-1538(1992). RN [30] RP VARIANT VAL-401. RX PubMed=11289720; DOI=10.1007/s100380170125; RA Tachikawa H., Tsuda M., Onoe K., Ueno M., Takagi S., Shinohara Y.; RT "Alpha-1-antichymotrypsin gene A1252G variant (ACT Isehara-1) is RT associated with a lacunar type of ischemic cerebrovascular disease."; RL J. Hum. Genet. 46:45-47(2001). CC -!- FUNCTION: Although its physiological function is unclear, it can CC inhibit neutrophil cathepsin G and mast cell chymase, both of CC which can convert angiotensin-1 to the active angiotensin-2. CC -!- SUBUNIT: Interacts with DNAJC1. CC -!- INTERACTION: CC Q96KC8:DNAJC1; NbExp=3; IntAct=EBI-296557, EBI-296550; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P01011-1; Sequence=Displayed; CC Name=2; CC IsoId=P01011-2; Sequence=VSP_014227, VSP_014228; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=P01011-3; Sequence=VSP_014225, VSP_014226; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Plasma. Synthesized in the liver. Like the CC related alpha-1-antitrypsin, its concentration increases in the CC acute phase of inflammation or infection. Found in the amyloid CC plaques from the hippocampus of Alzheimer disease brains. CC -!- DOMAIN: The reactive center loop (RCL) extends out from the body CC of the protein and directs binding to the target protease. The CC protease cleaves the serpin at the reactive site within the RCL, CC establishing a covalent linkage between the carboxyl group of the CC serpin reactive site and the serine hydroxyl of the protease. The CC resulting inactive serpin-protease complex is highly stable. CC -!- PTM: N- and O-glycosylated. CC -!- MISCELLANEOUS: Alpha-1-antichymotrypsin can bind DNA. CC -!- SIMILARITY: Belongs to the serpin family. CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator. CC -!- SEQUENCE CAUTION: CC Sequence=AAA51543.1; Type=Frameshift; Positions=101, 106, 111, 117, 123, 129, 421; CC Sequence=AAT08029.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=AAT08029.1; Type=Frameshift; Positions=4; CC Sequence=BAD92297.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=CAA48671.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alpha-1 antichymotrypsin entry; CC URL="http://en.wikipedia.org/wiki/Alpha_1-antichymotrypsin"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; K01500; AAA51543.1; ALT_FRAME; mRNA. DR EMBL; X68733; CAA48671.1; ALT_INIT; Genomic_DNA. DR EMBL; X68734; CAA48671.1; JOINED; Genomic_DNA. DR EMBL; X68735; CAA48671.1; JOINED; Genomic_DNA. DR EMBL; X68736; CAA48671.1; JOINED; Genomic_DNA. DR EMBL; X68737; CAA48671.1; JOINED; Genomic_DNA. DR EMBL; AY513275; AAT08028.1; -; mRNA. DR EMBL; AY513276; AAT08029.1; ALT_SEQ; mRNA. DR EMBL; AK123091; BAG53869.1; -; mRNA. DR EMBL; AB209060; BAD92297.1; ALT_INIT; mRNA. DR EMBL; BC003559; AAH03559.3; -; mRNA. DR EMBL; BC010530; AAH10530.1; -; mRNA. DR EMBL; BC013189; AAH13189.1; -; mRNA. DR EMBL; BC034554; AAH34554.1; -; mRNA. DR EMBL; BC070265; AAH70265.1; -; mRNA. DR EMBL; M18906; AAA51559.1; -; mRNA. DR EMBL; AF089747; AAD08810.1; -; mRNA. DR EMBL; J05176; AAA51560.1; -; mRNA. DR EMBL; X00947; CAA25459.1; -; Genomic_DNA. DR CCDS; CCDS32150.1; -. [P01011-1] DR PIR; A90475; ITHUC. DR PIR; S62374; S62374. DR RefSeq; NP_001076.2; NM_001085.4. [P01011-1] DR UniGene; Hs.534293; -. DR UniGene; Hs.710488; -. DR PDB; 1AS4; X-ray; 2.10 A; A=43-383, B=387-423. DR PDB; 1QMN; X-ray; 2.27 A; A=26-423. DR PDB; 2ACH; X-ray; 2.70 A; A=24-383, B=384-423. DR PDB; 3CAA; X-ray; 2.40 A; A=43-383, B=387-423. DR PDB; 3DLW; X-ray; 2.70 A; A=25-423. DR PDB; 4CAA; X-ray; 2.90 A; A=43-383, B=387-423. DR PDBsum; 1AS4; -. DR PDBsum; 1QMN; -. DR PDBsum; 2ACH; -. DR PDBsum; 3CAA; -. DR PDBsum; 3DLW; -. DR PDBsum; 4CAA; -. DR ProteinModelPortal; P01011; -. DR SMR; P01011; 48-422. DR BioGrid; 106530; 11. DR IntAct; P01011; 10. DR ChEMBL; CHEMBL5960; -. DR MEROPS; I04.002; -. DR PhosphoSite; P01011; -. DR UniCarbKB; P01011; -. DR DMDM; 112874; -. DR DOSAC-COBS-2DPAGE; P01011; -. DR SWISS-2DPAGE; P01011; -. DR MaxQB; P01011; -. DR PaxDb; P01011; -. DR PRIDE; P01011; -. DR DNASU; 12; -. DR Ensembl; ENST00000393078; ENSP00000376793; ENSG00000196136. [P01011-1] DR Ensembl; ENST00000393080; ENSP00000376795; ENSG00000196136. [P01011-1] DR Ensembl; ENST00000467132; ENSP00000450540; ENSG00000196136. [P01011-1] DR Ensembl; ENST00000556968; ENSP00000452476; ENSG00000196136. [P01011-2] DR GeneID; 12; -. DR KEGG; hsa:12; -. DR UCSC; uc001ydp.3; human. [P01011-1] DR UCSC; uc021sbb.2; human. [P01011-3] DR CTD; 12; -. DR GeneCards; GC14P095078; -. DR H-InvDB; HIX0079611; -. DR HGNC; HGNC:16; SERPINA3. DR HPA; CAB016647; -. DR HPA; HPA000893; -. DR HPA; HPA002560; -. DR MIM; 107280; gene. DR neXtProt; NX_P01011; -. DR Orphanet; 93594; Alpha-1-antichymotrypsin deficiency. DR PharmGKB; PA35020; -. DR eggNOG; COG4826; -. DR HOVERGEN; HBG005957; -. DR InParanoid; P01011; -. DR KO; K04525; -. DR PhylomeDB; P01011; -. DR TreeFam; TF343201; -. DR ChiTaRS; SERPINA3; human. DR EvolutionaryTrace; P01011; -. DR GeneWiki; Alpha_1-antichymotrypsin; -. DR GenomeRNAi; 12; -. DR NextBio; 23; -. DR PMAP-CutDB; P01011; -. DR PRO; PR:P01011; -. DR ArrayExpress; P01011; -. DR Bgee; P01011; -. DR Genevestigator; P01011; -. DR GO; GO:0072562; C:blood microparticle; IDA:UniProt. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005622; C:intracellular; NAS:UniProtKB. DR GO; GO:0005634; C:nucleus; TAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:UniProtKB. DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB. DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; NAS:UniProtKB. DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:RefGenome. DR GO; GO:0019216; P:regulation of lipid metabolic process; NAS:UniProtKB. DR GO; GO:0030162; P:regulation of proteolysis; IBA:RefGenome. DR InterPro; IPR023795; Serpin_CS. DR InterPro; IPR023796; Serpin_dom. DR InterPro; IPR000215; Serpin_fam. DR PANTHER; PTHR11461; PTHR11461; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR SUPFAM; SSF56574; SSF56574; 1. DR PROSITE; PS00284; SERPIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disease mutation; Glycoprotein; KW Polymorphism; Protease inhibitor; Reference proteome; Secreted; KW Serine protease inhibitor; Signal. FT SIGNAL 1 23 FT CHAIN 24 423 Alpha-1-antichymotrypsin. FT /FTId=PRO_0000032411. FT CHAIN 26 423 Alpha-1-antichymotrypsin His-Pro-less. FT /FTId=PRO_0000032412. FT DNA_BIND 235 237 FT REGION 369 394 RCL. FT REGION 381 389 O-glycosylated at one site. FT SITE 383 384 Reactive bond. FT CARBOHYD 33 33 N-linked (GlcNAc...). FT CARBOHYD 93 93 N-linked (GlcNAc...). FT CARBOHYD 106 106 N-linked (GlcNAc...). FT CARBOHYD 127 127 N-linked (GlcNAc...). FT CARBOHYD 186 186 N-linked (GlcNAc...). FT CARBOHYD 271 271 N-linked (GlcNAc...). FT VAR_SEQ 64 95 LVLKAPDKNVIFSPLSISTALAFLSLGAHNTT -> SPRWS FT IRLCLMYLRRAQKHLLPQQSKSPSFLH (in isoform FT 3). FT /FTId=VSP_014225. FT VAR_SEQ 96 423 Missing (in isoform 3). FT /FTId=VSP_014226. FT VAR_SEQ 215 216 AK -> ER (in isoform 2). FT /FTId=VSP_014227. FT VAR_SEQ 217 423 Missing (in isoform 2). FT /FTId=VSP_014228. FT VARIANT 9 9 A -> T (in dbSNP:rs4934). FT /FTId=VAR_006973. FT VARIANT 78 78 L -> P (in Bochum-1; dbSNP:rs1800463). FT /FTId=VAR_006974. FT VARIANT 167 167 A -> G. FT /FTId=VAR_006975. FT VARIANT 252 252 P -> A (in Bonn-1; dbSNP:rs17473). FT /FTId=VAR_006976. FT VARIANT 267 267 K -> R (in dbSNP:rs17853314). FT /FTId=VAR_037902. FT VARIANT 401 401 M -> V (associated with occlusive- FT cerebrovascular disease; Isehara-1). FT /FTId=VAR_006977. FT VARIANT 407 407 D -> G (in dbSNP:rs10956). FT /FTId=VAR_011742. FT CONFLICT 55 55 D -> S (in Ref. 12; AA sequence). FT CONFLICT 69 69 P -> L (in Ref. 1; AAA51543). FT CONFLICT 101 101 K -> R (in Ref. 5; BAD92297). FT CONFLICT 106 106 N -> Y (in Ref. 3; AAT08028). FT CONFLICT 198 198 D -> N (in Ref. 3; AAT08029). FT CONFLICT 199 199 L -> P (in Ref. 1; AAA51543). FT CONFLICT 234 234 S -> N (in Ref. 3; AAT08029). FT CONFLICT 339 339 S -> G (in Ref. 3; AAT08028). FT CONFLICT 346 346 I -> S (in Ref. 3; AAT08028). FT CONFLICT 361 363 AVL -> VVS (in Ref. 1; AAA51543). FT HELIX 49 67 FT STRAND 69 71 FT STRAND 73 75 FT HELIX 77 88 FT HELIX 93 102 FT TURN 107 109 FT HELIX 112 126 FT STRAND 130 132 FT STRAND 134 144 FT HELIX 151 161 FT STRAND 164 168 FT HELIX 170 172 FT HELIX 173 187 FT TURN 188 190 FT STRAND 203 219 FT HELIX 223 225 FT STRAND 227 234 FT STRAND 237 256 FT TURN 257 260 FT STRAND 261 279 FT TURN 281 283 FT HELIX 284 289 FT HELIX 293 302 FT STRAND 304 314 FT STRAND 316 323 FT HELIX 325 330 FT HELIX 335 337 FT HELIX 344 347 FT STRAND 348 350 FT STRAND 352 365 FT STRAND 367 382 FT STRAND 391 394 FT STRAND 399 405 FT STRAND 412 418 SQ SEQUENCE 423 AA; 47651 MW; B002F946C86A8951 CRC64; MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA SANVDFAFSL YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL KGLKFNLTET SEAEIHQSFQ HLLRTLNQSS DELQLSMGNA MFVKEQLSLL DRFTEDAKRL YGSEAFATDF QDSAAAKKLI NDYVKNGTRG KITDLIKDLD SQTMMVLVNY IFFKAKWEMP FDPQDTHQSR FYLSKKKWVM VPMMSLHHLT IPYFRDEELS CTVVELKYTG NASALFILPD QDKMEEVEAM LLPETLKRWR DSLEFREIGE LYLPKFSISR DYNLNDILLQ LGIEEAFTSK ADLSGITGAR NLAVSQVVHK AVLDVFEEGT EASAATAVKI TLLSALVETR TIVRFNRPFL MIIVPTDTQN IFFMSKVTNP KQA // ID AAK1_HUMAN Reviewed; 961 AA. AC Q2M2I8; Q4ZFZ3; Q53RX6; Q9UPV4; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 3. DT 09-JUL-2014, entry version 91. DE RecName: Full=AP2-associated protein kinase 1; DE EC=2.7.11.1; DE AltName: Full=Adaptor-associated kinase 1; GN Name=AAK1; Synonyms=KIAA1048; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RP CLATHRIN, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=17494869; DOI=10.1091/mbc.E06-09-0831; RA Henderson D.M., Conner S.D.; RT "A novel AAK1 splice variant functions at multiple steps of the RT endocytic pathway."; RL Mol. Biol. Cell 18:2698-2706(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP GLN-509. RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP GLN-509. RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, AND MUTAGENESIS OF LYS-74 AND ASP-176. RX PubMed=12952931; DOI=10.1083/jcb.200304069; RA Conner S.D., Schmid S.L.; RT "Differential requirements for AP-2 in clathrin-mediated RT endocytosis."; RL J. Cell Biol. 162:773-779(2003). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389 AND THR-606, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using RT sequential IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389; THR-441; SER-637 RP AND SER-731, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-234; SER-235; THR-389; RP THR-606; THR-620; SER-623; SER-624 AND SER-637, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP FUNCTION, INTERACTION WITH NUMB, AND MUTAGENESIS OF LYS-74 AND RP ASP-176. RX PubMed=18657069; DOI=10.1111/j.1600-0854.2008.00790.x; RA Sorensen E.B., Conner S.D.; RT "AAK1 regulates Numb function at an early step in clathrin-mediated RT endocytosis."; RL Traffic 9:1791-1800(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-354; THR-389; RP SER-637; SER-650; TYR-687 AND SER-731, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-389; THR-606; SER-637 RP AND THR-653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-620; SER-623; SER-624 RP AND SER-637, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP FUNCTION, INTERACTION WITH EPS15 AND NOTCH1, AND MUTAGENESIS OF LYS-74 RP AND 777-ASP--PHE-779. RX PubMed=21464124; DOI=10.1074/jbc.M110.190769; RA Gupta-Rossi N., Ortica S., Meas-Yedid V., Heuss S., Moretti J., RA Olivo-Marin J.C., Israel A.; RT "The adaptor-associated kinase 1, AAK1, is a positive regulator of the RT Notch pathway."; RL J. Biol. Chem. 286:18720-18730(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606; THR-620; SER-624 RP AND SER-637, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [21] RP VARIANTS [LARGE SCALE ANALYSIS] VAL-59; HIS-533; ALA-603; MET-694; RP THR-725; ARG-771 AND ASP-835. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Regulates clathrin-mediated endocytosis by CC phosphorylating the AP2M1/mu2 subunit of the adaptor protein CC complex 2 (AP-2) which ensures high affinity binding of AP-2 to CC cargo membrane proteins during the initial stages of endocytosis. CC Isoform 1 and isoform 2 display similar levels of kinase activity CC towards AP2M1. Regulates phosphorylation of other AP-2 subunits as CC well as AP-2 localization and AP-2-mediated internalization of CC ligand complexes. Phosphorylates NUMB and regulates its cellular CC localization, promoting NUMB localization to endosomes. Binds to CC and stabilizes the activated form of NOTCH1, increases its CC localization in endosomes and regulates its transcriptional CC activity. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Stimulated by clathrin (By similarity). CC -!- SUBUNIT: Interacts with alpha-adaptin, AP-2, clathrin, NUMB and CC EPS15 isoform 2. Interacts with membrane-bound activated NOTCH1 CC but not with the inactive full-length form of NOTCH1. CC Preferentially interacts with monoubiquitinated activated NOTCH1 CC compared to the non-ubiquitinated form. CC -!- INTERACTION: CC Q9NQ11:ATP13A2; NbExp=2; IntAct=EBI-1383433, EBI-6308763; CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein CC (By similarity). Membrane, clathrin-coated pit (By similarity). CC Note=Active when found in clathrin-coated pits at the plasma CC membrane. In neuronal cells, enriched at presynaptic terminals. In CC non-neuronal cells, enriched at leading edge of migrating cells CC (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=AAK1L; CC IsoId=Q2M2I8-1; Sequence=Displayed; CC Name=2; Synonyms=AAK1S; CC IsoId=Q2M2I8-2; Sequence=VSP_039459; CC -!- TISSUE SPECIFICITY: Detected in brain, heart and liver. Isoform 1 CC is the predominant isoform in brain. CC -!- PTM: Autophosphorylated (By similarity). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr CC protein kinase family. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAA83000.2; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB028971; BAA83000.2; ALT_INIT; mRNA. DR EMBL; AC092431; AAX88861.1; -; Genomic_DNA. DR EMBL; AC079121; AAY14931.1; -; Genomic_DNA. DR EMBL; AC136007; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC104842; AAI04843.1; -; mRNA. DR EMBL; BC111965; AAI11966.1; -; mRNA. DR CCDS; CCDS1893.2; -. [Q2M2I8-1] DR RefSeq; NP_055726.3; NM_014911.3. DR UniGene; Hs.468878; -. DR ProteinModelPortal; Q2M2I8; -. DR SMR; Q2M2I8; 32-356. DR BioGrid; 116520; 3. DR IntAct; Q2M2I8; 3. DR STRING; 9606.ENSP00000386456; -. DR BindingDB; Q2M2I8; -. DR ChEMBL; CHEMBL3830; -. DR GuidetoPHARMACOLOGY; 1921; -. DR PhosphoSite; Q2M2I8; -. DR DMDM; 300669613; -. DR MaxQB; Q2M2I8; -. DR PaxDb; Q2M2I8; -. DR PRIDE; Q2M2I8; -. DR Ensembl; ENST00000406297; ENSP00000385181; ENSG00000115977. [Q2M2I8-2] DR Ensembl; ENST00000409085; ENSP00000386456; ENSG00000115977. [Q2M2I8-1] DR GeneID; 22848; -. DR KEGG; hsa:22848; -. DR UCSC; uc002sfp.2; human. [Q2M2I8-1] DR UCSC; uc010fdk.2; human. [Q2M2I8-2] DR CTD; 22848; -. DR GeneCards; GC02M069685; -. DR H-InvDB; HIX0161871; -. DR HGNC; HGNC:19679; AAK1. DR HPA; HPA017931; -. DR HPA; HPA020289; -. DR neXtProt; NX_Q2M2I8; -. DR PharmGKB; PA134990616; -. DR eggNOG; COG0515; -. DR HOGENOM; HOG000232173; -. DR HOVERGEN; HBG080803; -. DR KO; K08853; -. DR OMA; QLIQNFY; -. DR PhylomeDB; Q2M2I8; -. DR TreeFam; TF317300; -. DR SignaLink; Q2M2I8; -. DR ChiTaRS; AAK1; human. DR GeneWiki; AAK1; -. DR GenomeRNAi; 22848; -. DR NextBio; 43313; -. DR PRO; PR:Q2M2I8; -. DR ArrayExpress; Q2M2I8; -. DR Bgee; Q2M2I8; -. DR CleanEx; HS_AAK1; -. DR Genevestigator; Q2M2I8; -. DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB. DR GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB. DR GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell. DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISS:UniProtKB. DR GO; GO:0043195; C:terminal bouton; ISS:UniProtKB. DR GO; GO:0035612; F:AP-2 adaptor complex binding; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005112; F:Notch binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:UniProtKB. DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB. DR GO; GO:2000369; P:regulation of clathrin-mediated endocytosis; IDA:UniProtKB. DR GO; GO:0032880; P:regulation of protein localization; IDA:UniProtKB. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Cell membrane; KW Coated pit; Complete proteome; Endocytosis; Kinase; Membrane; KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 961 AP2-associated protein kinase 1. FT /FTId=PRO_0000250578. FT DOMAIN 46 315 Protein kinase. FT NP_BIND 52 60 ATP (By similarity). FT COMPBIAS 12 42 Gly-rich. FT COMPBIAS 397 614 Gln-rich. FT COMPBIAS 658 663 Poly-Ala. FT ACT_SITE 176 176 Proton acceptor (By similarity). FT BINDING 74 74 ATP (By similarity). FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 14 14 Phosphoserine. FT MOD_RES 234 234 Phosphotyrosine. FT MOD_RES 235 235 Phosphoserine. FT MOD_RES 354 354 Phosphothreonine. FT MOD_RES 389 389 Phosphothreonine. FT MOD_RES 441 441 Phosphothreonine. FT MOD_RES 606 606 Phosphothreonine. FT MOD_RES 620 620 Phosphothreonine. FT MOD_RES 623 623 Phosphoserine. FT MOD_RES 624 624 Phosphoserine. FT MOD_RES 637 637 Phosphoserine. FT MOD_RES 650 650 Phosphoserine. FT MOD_RES 653 653 Phosphothreonine. FT MOD_RES 687 687 Phosphotyrosine. FT MOD_RES 731 731 Phosphoserine. FT VAR_SEQ 823 961 EKADVAVESLIPGLEPPVPQRLPSQTESVTSNRTDSLTGED FT SLLDCSLLSNPTTDLLEEFAPTAISAPVHKAAEDSNLISGF FT DVPEGSDKVAEDEFDPIPVLITKNPQGGHSRNSSGSSESSL FT PNLARSLLLVDQLIDL -> GKVIISVSSVMHDMCACFKND FT KYLVNQSLGNSPATPEAKAI (in isoform 2). FT /FTId=VSP_039459. FT VARIANT 59 59 I -> V (in dbSNP:rs34535244). FT /FTId=VAR_040348. FT VARIANT 509 509 K -> Q (in dbSNP:rs6715776). FT /FTId=VAR_031129. FT VARIANT 533 533 Q -> H. FT /FTId=VAR_040349. FT VARIANT 603 603 V -> A (in dbSNP:rs56038532). FT /FTId=VAR_040350. FT VARIANT 694 694 T -> M (in dbSNP:rs55889248). FT /FTId=VAR_040351. FT VARIANT 725 725 P -> T (in dbSNP:rs35285785). FT /FTId=VAR_040352. FT VARIANT 771 771 P -> R (in dbSNP:rs34422616). FT /FTId=VAR_040353. FT VARIANT 835 835 G -> D. FT /FTId=VAR_040354. FT MUTAGEN 74 74 K->A: Inhibits autophosphorylation and FT phosphorylation of AP2M1. Does not affect FT NUMB localization. Does not interact with FT monoubiquitinated NOTCH1. FT MUTAGEN 176 176 D->A: Inhibits autophosphorylation and FT phosphorylation of AP2M1. Does not affect FT NUMB localization. FT MUTAGEN 777 779 DPF->AAA: Does not affect interaction FT with NOTCH1 but abolishes interaction FT with ESP15. SQ SEQUENCE 961 AA; 103885 MW; 1FB44D0FDEF6CAD0 CRC64; MKKFFDSRRE QGGSGLGSGS SGGGGSTSGL GSGYIGRVFG IGRQQVTVDE VLAEGGFAIV FLVRTSNGMK CALKRMFVNN EHDLQVCKRE IQIMRDLSGH KNIVGYIDSS INNVSSGDVW EVLILMDFCR GGQVVNLMNQ RLQTGFTENE VLQIFCDTCE AVARLHQCKT PIIHRDLKVE NILLHDRGHY VLCDFGSATN KFQNPQTEGV NAVEDEIKKY TTLSYRAPEM VNLYSGKIIT TKADIWALGC LLYKLCYFTL PFGESQVAIC DGNFTIPDNS RYSQDMHCLI RYMLEPDPDK RPDIYQVSYF SFKLLKKECP IPNVQNSPIP AKLPEPVKAS EAAAKKTQPK ARLTDPIPTT ETSIAPRQRP KAGQTQPNPG ILPIQPALTP RKRATVQPPP QAAGSSNQPG LLASVPQPKP QAPPSQPLPQ TQAKQPQAPP TPQQTPSTQA QGLPAQAQAT PQHQQQLFLK QQQQQQQPPP AQQQPAGTFY QQQQAQTQQF QAVHPATQKP AIAQFPVVSQ GGSQQQLMQN FYQQQQQQQQ QQQQQQLATA LHQQQLMTQQ AALQQKPTMA AGQQPQPQPA AAPQPAPAQE PAIQAPVRQQ PKVQTTPPPA VQGQKVGSLT PPSSPKTQRA GHRRILSDVT HSAVFGVPAS KSTQLLQAAA AEASLNKSKS ATTTPSGSPR TSQQNVYNPS EGSTWNPFDD DNFSKLTAEE LLNKDFAKLG EGKHPEKLGG SAESLIPGFQ STQGDAFATT SFSAGTAEKR KGGQTVDSGL PLLSVSDPFI PLQVPDAPEK LIEGLKSPDT SLLLPDLLPM TDPFGSTSDA VIEKADVAVE SLIPGLEPPV PQRLPSQTES VTSNRTDSLT GEDSLLDCSL LSNPTTDLLE EFAPTAISAP VHKAAEDSNL ISGFDVPEGS DKVAEDEFDP IPVLITKNPQ GGHSRNSSGS SESSLPNLAR SLLLVDQLID L // ID AAKB1_HUMAN Reviewed; 270 AA. AC Q9Y478; Q9UBV0; Q9UE20; Q9UEX2; Q9Y6V8; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 09-JUL-2014, entry version 140. DE RecName: Full=5'-AMP-activated protein kinase subunit beta-1; DE Short=AMPK subunit beta-1; DE Short=AMPKb; GN Name=PRKAB1; Synonyms=AMPK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Carling D.; RT "Non-catalytic beta and gamma subunits isoforms of the AMP-activated RT protein kinase."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=9224708; DOI=10.1016/S0014-5793(97)00569-3; RA Stapleton D., Woollatt E., Mitchelhill K., Nicholl J.K., RA Fernandez C.S., Michell B.J., Witters L.A., Power D.A., RA Sutherland G.R., Kemp B.E.; RT "AMP-activated protein kinase isoenzyme family: subunit structure and RT chromosomal location."; RL FEBS Lett. 409:452-456(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V., RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M., RA Lathrop M., Cox R.D., Bell G.I.; RT "Transcription map of the 5cM region surrounding the hepatocyte RT nuclear factor-1a/MODY3 gene on chromosome 12."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wang X., Yu L., Tu Q.; RT "Cloning and expression of the complete mRNA coding human AMP- RT activated protein kinase."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH FNIP1. RX PubMed=17028174; DOI=10.1073/pnas.0603781103; RA Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L., RA Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III, RA Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr., RA Linehan W.M., Schmidt L.S., Zbar B.; RT "Folliculin encoded by the BHD gene interacts with a binding protein, RT FNIP1, and AMPK, and is involved in AMPK and mTOR signaling."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006). RN [8] RP INTERACTION WITH FNIP2. RX PubMed=18403135; DOI=10.1016/j.gene.2008.02.022; RA Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., RA Valera V.A., Linehan W.M., Schmidt L.S.; RT "Identification and characterization of a novel folliculin-interacting RT protein FNIP2."; RL Gene 415:60-67(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-5; SER-6 AND RP SER-108, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40 AND SER-108, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-40; SER-108 AND RP THR-148, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-108, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-108, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] RP PHOSPHORYLATION BY ULK1. RX PubMed=21460634; DOI=10.4161/auto.7.7.15451; RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.; RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative RT regulatory feedback loop."; RL Autophagy 7:696-706(2011). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP INTERACTION WITH PRKAA1 AND PRKAG1, MUTAGENESIS OF GLY-2, AND RP MYRISTOYLATION AT GLY-2. RX PubMed=21680840; DOI=10.1126/science.1200094; RA Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S., RA Kemp B.E.; RT "AMPK is a direct adenylate charge-regulated protein kinase."; RL Science 332:1433-1435(2011). RN [19] RP REVIEW ON FUNCTION. RX PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05; RA Towler M.C., Hardie D.G.; RT "AMP-activated protein kinase in metabolic control and insulin RT signaling."; RL Circ. Res. 100:328-341(2007). RN [20] RP REVIEW ON FUNCTION. RX PubMed=17712357; DOI=10.1038/nrm2249; RA Hardie D.G.; RT "AMP-activated/SNF1 protein kinases: conserved guardians of cellular RT energy."; RL Nat. Rev. Mol. Cell Biol. 8:774-785(2007). CC -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase CC (AMPK), an energy sensor protein kinase that plays a key role in CC regulating cellular energy metabolism. In response to reduction of CC intracellular ATP levels, AMPK activates energy-producing pathways CC and inhibits energy-consuming processes: inhibits protein, CC carbohydrate and lipid biosynthesis, as well as cell growth and CC proliferation. AMPK acts via direct phosphorylation of metabolic CC enzymes, and by longer-term effects via phosphorylation of CC transcription regulators. Also acts as a regulator of cellular CC polarity by remodeling the actin cytoskeleton; probably by CC indirectly activating myosin. Beta non-catalytic subunit acts as a CC scaffold on which the AMPK complex assembles, via its C-terminus CC that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, CC PRKAG2 or PRKAG3). CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit CC (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non- CC catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with CC FNIP1 and FNIP2. CC -!- INTERACTION: CC O70302:Cidea (xeno); NbExp=4; IntAct=EBI-719769, EBI-7927848; CC P62993:GRB2; NbExp=2; IntAct=EBI-719769, EBI-401755; CC Q13131:PRKAA1; NbExp=5; IntAct=EBI-719769, EBI-1181405; CC P54619:PRKAG1; NbExp=4; IntAct=EBI-719769, EBI-1181439; CC -!- DOMAIN: The glycogen-binding domain may target AMPK to glycogen so CC that other factors like glycogen-bound debranching enzyme or CC protein phosphatases can directly affect AMPK activity (By CC similarity). CC -!- PTM: Phosphorylated when associated with the catalytic subunit CC (PRKAA1 or PRKAA2). Phosphorylated by ULK1; leading to negatively CC regulate AMPK activity and suggesting the existence of a CC regulatory feedback loop between ULK1 and AMPK. CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta CC subunit family. CC -!- SEQUENCE CAUTION: CC Sequence=AAB71326.1; Type=Erroneous gene model prediction; CC Sequence=AAC98897.1; Type=Frameshift; Positions=245; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PRKAB1ID44100ch12q24.html"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ224515; CAA12024.1; -; mRNA. DR EMBL; Y12556; CAA73146.1; -; mRNA. DR EMBL; U83994; AAD09237.1; -; mRNA. DR EMBL; U87276; AAD00625.1; -; Genomic_DNA. DR EMBL; U87271; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; U87272; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; U87273; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; U87274; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; U87275; AAD00625.1; JOINED; Genomic_DNA. DR EMBL; AF022116; AAC98897.1; ALT_FRAME; mRNA. DR EMBL; AC002563; AAB71326.1; ALT_SEQ; Genomic_DNA. DR EMBL; BC001007; AAH01007.1; -; mRNA. DR EMBL; BC001056; AAH01056.1; -; mRNA. DR EMBL; BC001823; AAH01823.1; -; mRNA. DR EMBL; BC017671; AAH17671.1; -; mRNA. DR CCDS; CCDS9191.1; -. DR PIR; T09514; T09514. DR RefSeq; NP_006244.2; NM_006253.4. DR RefSeq; XP_005253966.1; XM_005253909.1. DR UniGene; Hs.741184; -. DR PDB; 4CFE; X-ray; 3.02 A; B/D=1-270. DR PDB; 4CFF; X-ray; 3.92 A; B/D=1-270. DR PDBsum; 4CFE; -. DR PDBsum; 4CFF; -. DR ProteinModelPortal; Q9Y478; -. DR SMR; Q9Y478; 77-270. DR BioGrid; 111551; 28. DR IntAct; Q9Y478; 16. DR MINT; MINT-1400840; -. DR STRING; 9606.ENSP00000229328; -. DR BindingDB; Q9Y478; -. DR ChEMBL; CHEMBL2111345; -. DR DrugBank; DB00131; Adenosine monophosphate. DR DrugBank; DB00331; Metformin. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR PhosphoSite; Q9Y478; -. DR DMDM; 14194425; -. DR MaxQB; Q9Y478; -. DR PaxDb; Q9Y478; -. DR PRIDE; Q9Y478; -. DR Ensembl; ENST00000229328; ENSP00000229328; ENSG00000111725. DR Ensembl; ENST00000541640; ENSP00000441369; ENSG00000111725. DR GeneID; 5564; -. DR KEGG; hsa:5564; -. DR UCSC; uc001txg.3; human. DR CTD; 5564; -. DR GeneCards; GC12P120105; -. DR HGNC; HGNC:9378; PRKAB1. DR HPA; CAB005058; -. DR HPA; HPA004247; -. DR MIM; 602740; gene. DR neXtProt; NX_Q9Y478; -. DR PharmGKB; PA33746; -. DR eggNOG; NOG238368; -. DR HOGENOM; HOG000230597; -. DR HOVERGEN; HBG050430; -. DR InParanoid; Q9Y478; -. DR KO; K07199; -. DR OMA; CKAEERF; -. DR OrthoDB; EOG7SXW3Z; -. DR PhylomeDB; Q9Y478; -. DR TreeFam; TF313827; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_200751; Organelle biogenesis and maintenance. DR SignaLink; Q9Y478; -. DR GeneWiki; PRKAB1; -. DR GenomeRNAi; 5564; -. DR NextBio; 21556; -. DR PRO; PR:Q9Y478; -. DR ArrayExpress; Q9Y478; -. DR Bgee; Q9Y478; -. DR CleanEx; HS_PRKAB1; -. DR Genevestigator; Q9Y478; -. DR GO; GO:0031588; C:AMP-activated protein kinase complex; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0050790; P:regulation of catalytic activity; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR006828; AMP_prot_kin_bsu_interact-dom. DR InterPro; IPR014756; Ig_E-set. DR Pfam; PF04739; AMPKBI; 1. DR SMART; SM01010; AMPKBI; 1. DR SUPFAM; SSF81296; SSF81296; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Lipoprotein; Myristate; Phosphoprotein; Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 270 5'-AMP-activated protein kinase subunit FT beta-1. FT /FTId=PRO_0000204363. FT REGION 68 163 Glycogen-binding domain (By similarity). FT MOD_RES 4 4 Phosphothreonine. FT MOD_RES 5 5 Phosphoserine. FT MOD_RES 6 6 Phosphoserine. FT MOD_RES 19 19 Phosphothreonine. FT MOD_RES 24 24 Phosphoserine; by autocatalysis (By FT similarity). FT MOD_RES 25 25 Phosphoserine; by autocatalysis (By FT similarity). FT MOD_RES 40 40 Phosphoserine. FT MOD_RES 96 96 Phosphoserine. FT MOD_RES 101 101 Phosphoserine (By similarity). FT MOD_RES 108 108 Phosphoserine. FT MOD_RES 148 148 Phosphothreonine. FT MOD_RES 182 182 Phosphoserine (By similarity). FT LIPID 2 2 N-myristoyl glycine. FT MUTAGEN 2 2 G->A: Abolishes myristoylation and AMP- FT enhanced phosphorylation of PRKAA1 or FT PRKAA2. FT CONFLICT 10 10 A -> G (in Ref. 2; CAA73146 and 4; FT AAC98897). FT CONFLICT 15 15 G -> A (in Ref. 1; CAA12024). FT CONFLICT 20 20 P -> A (in Ref. 2; CAA73146 and 4; FT AAC98897). FT CONFLICT 22 22 R -> K (in Ref. 3; AAD09237/AAD00625). FT CONFLICT 56 56 E -> Y (in Ref. 3; AAD09237/AAD00625). FT STRAND 79 84 FT STRAND 91 95 FT TURN 96 100 FT STRAND 112 117 FT STRAND 120 129 FT STRAND 132 134 FT STRAND 141 143 FT STRAND 145 147 FT STRAND 149 155 FT HELIX 157 160 FT HELIX 162 171 FT HELIX 208 211 FT HELIX 214 216 FT STRAND 238 241 FT STRAND 248 257 FT STRAND 260 269 SQ SEQUENCE 270 AA; 30382 MW; F0BCAA94D5BC15FC CRC64; MGNTSSERAA LERHGGHKTP RRDSSGGTKD GDRPKILMDS PEDADLFHSE EIKAPEKEEF LAWQHDLEVN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW SKLPLTRSHN NFVAILDLPE GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN NIIQVKKTDF EVFDALMVDS QKCSDVSELS SSPPGPYHQE PYVCKPEERF RAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY ALSIKDGVMV LSATHRYKKK YVTTLLYKPI // ID AAKB2_HUMAN Reviewed; 272 AA. AC O43741; A8K9V5; Q5VXY0; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 09-JUL-2014, entry version 133. DE RecName: Full=5'-AMP-activated protein kinase subunit beta-2; DE Short=AMPK subunit beta-2; GN Name=PRKAB2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9575201; DOI=10.1074/jbc.273.20.12443; RA Thornton C., Snowden M.A., Carling D.; RT "Identification of a novel AMP-activated protein kinase beta subunit RT isoform that is highly expressed in skeletal muscle."; RL J. Biol. Chem. 273:12443-12450(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12490143; DOI=10.1006/mcpr.2002.0439; RA Prochazka M., Farook V.S., Ossowski V., Wolford J.K., Bogardus C.; RT "Variant screening of PRKAB2, a type 2 diabetes mellitus RT susceptibility candidate gene on 1q in Pima Indians."; RL Mol. Cell. Probes 16:421-427(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-184, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by RT enrichment and fractionation of phosphopeptides with strong anion RT exchange chromatography."; RL Proteomics 8:1346-1361(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP PHOSPHORYLATION BY ULK1 AND ULK2. RX PubMed=21460634; DOI=10.4161/auto.7.7.15451; RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.; RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative RT regulatory feedback loop."; RL Autophagy 7:696-706(2011). RN [15] RP REVIEW ON FUNCTION. RX PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05; RA Towler M.C., Hardie D.G.; RT "AMP-activated protein kinase in metabolic control and insulin RT signaling."; RL Circ. Res. 100:328-341(2007). RN [16] RP REVIEW ON FUNCTION. RX PubMed=17712357; DOI=10.1038/nrm2249; RA Hardie D.G.; RT "AMP-activated/SNF1 protein kinases: conserved guardians of cellular RT energy."; RL Nat. Rev. Mol. Cell Biol. 8:774-785(2007). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 187-272 IN COMPLEX WITH RP PRKAA1 AND PRKAG1. RX PubMed=17851531; DOI=10.1038/nature06161; RA Xiao B., Heath R., Saiu P., Leiper F.C., Leone P., Jing C., RA Walker P.A., Haire L., Eccleston J.F., Davis C.T., Martin S.R., RA Carling D., Gamblin S.J.; RT "Structural basis for AMP binding to mammalian AMP-activated protein RT kinase."; RL Nature 449:496-500(2007). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 187-272 IN COMPLEX WITH RP PRKAA1 AND PRKAG1, AND MUTAGENESIS OF HIS-235. RX PubMed=21399626; DOI=10.1038/nature09932; RA Xiao B., Sanders M.J., Underwood E., Heath R., Mayer F.V., Carmena D., RA Jing C., Walker P.A., Eccleston J.F., Haire L.F., Saiu P., RA Howell S.A., Aasland R., Martin S.R., Carling D., Gamblin S.J.; RT "Structure of mammalian AMPK and its regulation by ADP."; RL Nature 472:230-233(2011). CC -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase CC (AMPK), an energy sensor protein kinase that plays a key role in CC regulating cellular energy metabolism. In response to reduction of CC intracellular ATP levels, AMPK activates energy-producing pathways CC and inhibits energy-consuming processes: inhibits protein, CC carbohydrate and lipid biosynthesis, as well as cell growth and CC proliferation. AMPK acts via direct phosphorylation of metabolic CC enzymes, and by longer-term effects via phosphorylation of CC transcription regulators. Also acts as a regulator of cellular CC polarity by remodeling the actin cytoskeleton; probably by CC indirectly activating myosin. Beta non-catalytic subunit acts as a CC scaffold on which the AMPK complex assembles, via its C-terminus CC that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, CC PRKAG2 or PRKAG3). CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit CC (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non- CC catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-1053424, EBI-1053424; CC Q13131:PRKAA1; NbExp=6; IntAct=EBI-1053424, EBI-1181405; CC P54619:PRKAG1; NbExp=3; IntAct=EBI-1053424, EBI-1181439; CC -!- PTM: Phosphorylated when associated with the catalytic subunit CC (PRKAA1 or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to CC negatively regulate AMPK activity and suggesting the existence of CC a regulatory feedback loop between ULK1, ULK2 and AMPK. CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta CC subunit family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ224538; CAA12030.1; -; mRNA. DR EMBL; AF504543; AAM74153.1; -; Genomic_DNA. DR EMBL; AF504538; AAM74153.1; JOINED; Genomic_DNA. DR EMBL; AF504539; AAM74153.1; JOINED; Genomic_DNA. DR EMBL; AF504540; AAM74153.1; JOINED; Genomic_DNA. DR EMBL; AF504541; AAM74153.1; JOINED; Genomic_DNA. DR EMBL; AF504542; AAM74153.1; JOINED; Genomic_DNA. DR EMBL; AK292820; BAF85509.1; -; mRNA. DR EMBL; AL356378; CAH72644.1; -; Genomic_DNA. DR EMBL; CH471223; EAW50945.1; -; Genomic_DNA. DR EMBL; BC053610; AAH53610.1; -; mRNA. DR CCDS; CCDS925.1; -. DR RefSeq; NP_005390.1; NM_005399.4. DR UniGene; Hs.50732; -. DR PDB; 2F15; X-ray; 2.00 A; A=69-163. DR PDB; 2V8Q; X-ray; 2.10 A; B=187-272. DR PDB; 2V92; X-ray; 2.40 A; B=187-272. DR PDB; 2V9J; X-ray; 2.53 A; B=187-272. DR PDB; 2Y8L; X-ray; 2.50 A; B=187-272. DR PDB; 2Y8Q; X-ray; 2.80 A; B=187-270. DR PDB; 2YA3; X-ray; 2.51 A; B=187-272. DR PDB; 4CFH; X-ray; 3.24 A; B=187-272. DR PDB; 4EAI; X-ray; 2.28 A; B=189-272. DR PDB; 4EAJ; X-ray; 2.61 A; B=189-272. DR PDBsum; 2F15; -. DR PDBsum; 2V8Q; -. DR PDBsum; 2V92; -. DR PDBsum; 2V9J; -. DR PDBsum; 2Y8L; -. DR PDBsum; 2Y8Q; -. DR PDBsum; 2YA3; -. DR PDBsum; 4CFH; -. DR PDBsum; 4EAI; -. DR PDBsum; 4EAJ; -. DR ProteinModelPortal; O43741; -. DR SMR; O43741; 68-272. DR BioGrid; 111552; 40. DR DIP; DIP-39763N; -. DR IntAct; O43741; 32. DR STRING; 9606.ENSP00000254101; -. DR BindingDB; O43741; -. DR ChEMBL; CHEMBL3038453; -. DR DrugBank; DB00131; Adenosine monophosphate. DR CAZy; CBM48; Carbohydrate-Binding Module Family 48. DR PhosphoSite; O43741; -. DR MaxQB; O43741; -. DR PaxDb; O43741; -. DR PeptideAtlas; O43741; -. DR PRIDE; O43741; -. DR DNASU; 5565; -. DR Ensembl; ENST00000254101; ENSP00000254101; ENSG00000131791. DR Ensembl; ENST00000584647; ENSP00000463518; ENSG00000266198. DR GeneID; 5565; -. DR KEGG; hsa:5565; -. DR UCSC; uc001epe.3; human. DR CTD; 5565; -. DR GeneCards; GC01M146627; -. DR HGNC; HGNC:9379; PRKAB2. DR HPA; HPA044342; -. DR MIM; 602741; gene. DR neXtProt; NX_O43741; -. DR PharmGKB; PA33747; -. DR eggNOG; NOG238368; -. DR HOGENOM; HOG000230597; -. DR HOVERGEN; HBG050430; -. DR InParanoid; O43741; -. DR KO; K07199; -. DR OMA; ESKYITV; -. DR PhylomeDB; O43741; -. DR TreeFam; TF313827; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_200751; Organelle biogenesis and maintenance. DR SignaLink; O43741; -. DR ChiTaRS; PRKAB2; human. DR EvolutionaryTrace; O43741; -. DR GeneWiki; PRKAB2; -. DR GenomeRNAi; 5565; -. DR NextBio; 21560; -. DR PRO; PR:O43741; -. DR ArrayExpress; O43741; -. DR Bgee; O43741; -. DR CleanEx; HS_PRKAB2; -. DR Genevestigator; O43741; -. DR GO; GO:0031588; C:AMP-activated protein kinase complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006853; P:carnitine shuttle; TAS:Reactome. DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0006468; P:protein phosphorylation; IDA:GOC. DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR InterPro; IPR006828; AMP_prot_kin_bsu_interact-dom. DR InterPro; IPR014756; Ig_E-set. DR Pfam; PF04739; AMPKBI; 1. DR SMART; SM01010; AMPKBI; 1. DR SUPFAM; SSF81296; SSF81296; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Phosphoprotein; Reference proteome. FT CHAIN 1 272 5'-AMP-activated protein kinase subunit FT beta-2. FT /FTId=PRO_0000204368. FT MOD_RES 39 39 Phosphoserine; by ULK1 (Probable). FT MOD_RES 40 40 Phosphothreonine; by ULK1 (Probable). FT MOD_RES 69 69 Phosphoserine; by ULK1 (By similarity). FT MOD_RES 108 108 Phosphoserine. FT MOD_RES 174 174 Phosphoserine (By similarity). FT MOD_RES 184 184 Phosphoserine. FT MUTAGEN 235 235 H->A: Results in an AMPK enzyme that is FT activable by phosphorylation but has FT significantly increased rate of FT dephosphorylation in phosphatase assays. FT STRAND 76 83 FT STRAND 90 94 FT HELIX 95 97 FT STRAND 112 129 FT STRAND 132 134 FT STRAND 141 143 FT STRAND 149 155 FT TURN 159 162 FT STRAND 201 204 FT HELIX 210 213 FT STRAND 214 217 FT TURN 236 239 FT STRAND 242 244 FT STRAND 250 259 FT STRAND 262 271 SQ SEQUENCE 272 AA; 30302 MW; 42B23BD70B92519C CRC64; MGNTTSDRVS GERHGAKAAR SEGAGGHAPG KEHKIMVGST DDPSVFSLPD SKLPGDKEFV SWQQDLEDSV KPTQQARPTV IRWSEGGKEV FISGSFNNWS TKIPLIKSHN DFVAILDLPE GEHQYKFFVD GQWVHDPSEP VVTSQLGTIN NLIHVKKSDF EVFDALKLDS MESSETSCRD LSSSPPGPYG QEMYAFRSEE RFKSPPILPP HLLQVILNKD TNISCDPALL PEPNHVMLNH LYALSIKDSV MVLSATHRYK KKYVTTLLYK PI // ID AAKG1_HUMAN Reviewed; 331 AA. AC P54619; B4DDT7; Q8N7V9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 09-JUL-2014, entry version 130. DE RecName: Full=5'-AMP-activated protein kinase subunit gamma-1; DE Short=AMPK gamma1; DE Short=AMPK subunit gamma-1; DE Short=AMPKg; GN Name=PRKAG1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Fetal liver; RX PubMed=8621499; DOI=10.1074/jbc.271.15.8675; RA Gao G., Fernandez C.S., Stapleton D., Auster A.S., Widmer J., RA Dyck J.R.B., Kemp B.E., Witters L.A.; RT "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP- RT activated protein kinase."; RL J. Biol. Chem. 271:8675-8681(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Glial tumor, and Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP DOMAIN CBS, AMP-BINDING, AND ATP-BINDING. RX PubMed=14722619; DOI=10.1172/JCI19874; RA Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., RA Scullion G.A., Norman D.G., Hardie D.G.; RT "CBS domains form energy-sensing modules whose binding of adenosine RT ligands is disrupted by disease mutations."; RL J. Clin. Invest. 113:274-284(2004). RN [7] RP INTERACTION WITH FNIP1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17028174; DOI=10.1073/pnas.0603781103; RA Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L., RA Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III, RA Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr., RA Linehan W.M., Schmidt L.S., Zbar B.; RT "Folliculin encoded by the BHD gene interacts with a binding protein, RT FNIP1, and AMPK, and is involved in AMPK and mTOR signaling."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006). RN [8] RP DOMAIN AMPK PSEUDOSUBSTRATE. RX PubMed=17255938; DOI=10.1038/sj.emboj.7601542; RA Scott J.W., Ross F.A., Liu J.K., Hardie D.G.; RT "Regulation of AMP-activated protein kinase by a pseudosubstrate RT sequence on the gamma subunit."; RL EMBO J. 26:806-815(2007). RN [9] RP INTERACTION WITH FNIP2. RX PubMed=18403135; DOI=10.1016/j.gene.2008.02.022; RA Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., RA Valera V.A., Linehan W.M., Schmidt L.S.; RT "Identification and characterization of a novel folliculin-interacting RT protein FNIP2."; RL Gene 415:60-67(2008). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION BY ULK1 AND ULK2. RX PubMed=21460634; DOI=10.4161/auto.7.7.15451; RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.; RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative RT regulatory feedback loop."; RL Autophagy 7:696-706(2011). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP INTERACTION WITH PRKAA1 AND PRKAB1, DOMAIN CBS, ADP-BINDING, RP MUTAGENESIS OF ASP-90; ASP-245 AND ASP-317, AND FUNCTION. RX PubMed=21680840; DOI=10.1126/science.1200094; RA Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S., RA Kemp B.E.; RT "AMPK is a direct adenylate charge-regulated protein kinase."; RL Science 332:1433-1435(2011). RN [14] RP REVIEW ON FUNCTION. RX PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05; RA Towler M.C., Hardie D.G.; RT "AMP-activated protein kinase in metabolic control and insulin RT signaling."; RL Circ. Res. 100:328-341(2007). RN [15] RP REVIEW ON FUNCTION. RX PubMed=17712357; DOI=10.1038/nrm2249; RA Hardie D.G.; RT "AMP-activated/SNF1 protein kinases: conserved guardians of cellular RT energy."; RL Nat. Rev. Mol. Cell Biol. 8:774-785(2007). CC -!- FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase CC (AMPK), an energy sensor protein kinase that plays a key role in CC regulating cellular energy metabolism. In response to reduction of CC intracellular ATP levels, AMPK activates energy-producing pathways CC and inhibits energy-consuming processes: inhibits protein, CC carbohydrate and lipid biosynthesis, as well as cell growth and CC proliferation. AMPK acts via direct phosphorylation of metabolic CC enzymes, and by longer-term effects via phosphorylation of CC transcription regulators. Also acts as a regulator of cellular CC polarity by remodeling the actin cytoskeleton; probably by CC indirectly activating myosin. Gamma non-catalytic subunit mediates CC binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: CC AMP-binding results in allosteric activation of alpha catalytic CC subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and CC preventing dephosphorylation of catalytic subunits. ADP also CC stimulates phosphorylation, without stimulating already CC phosphorylated catalytic subunit. ATP promotes dephosphorylation CC of catalytic subunit, rendering the AMPK enzyme inactive. CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit CC (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non- CC catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with CC FNIP1 and FNIP2. CC -!- INTERACTION: CC Q9Y478:PRKAB1; NbExp=4; IntAct=EBI-1181439, EBI-719769; CC O43741:PRKAB2; NbExp=3; IntAct=EBI-1181439, EBI-1053424; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P54619-1; Sequence=Displayed; CC Name=2; CC IsoId=P54619-2; Sequence=VSP_046711; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=P54619-3; Sequence=VSP_046712; CC Note=No experimental confirmation available. May be due to CC competing acceptor splice site; CC -!- DOMAIN: The AMPK pseudosubstrate motif resembles the sequence CC around sites phosphorylated on target proteins of AMPK, except the CC presence of a non-phosphorylatable residue in place of Ser. In the CC absence of AMP this pseudosubstrate sequence may bind to the CC active site groove on the alpha subunit (PRKAA1 or PRKAA2), CC preventing phosphorylation by the upstream activating kinase CC STK11/LKB1. CC -!- DOMAIN: The CBS domains mediate binding to AMP, ADP and ATP. 2 CC sites bind either AMP or ATP, whereas a third site contains a CC tightly bound AMP that does not exchange. Under physiological CC conditions AMPK mainly exists in its inactive form in complex with CC ATP, which is much more abundant than AMP. CC -!- PTM: Phosphorylated by ULK1 and ULK2; leading to negatively CC regulate AMPK activity and suggesting the existence of a CC regulatory feedback loop between ULK1, ULK2 and AMPK. CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma CC subunit family. CC -!- SIMILARITY: Contains 4 CBS domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U42412; AAC50495.1; -; mRNA. DR EMBL; BT007345; AAP36009.1; -; mRNA. DR EMBL; AK097606; BAC05117.1; -; mRNA. DR EMBL; AK293332; BAG56848.1; -; mRNA. DR EMBL; AC011603; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000358; AAH00358.1; -; mRNA. DR CCDS; CCDS55824.1; -. [P54619-2] DR CCDS; CCDS55825.1; -. [P54619-3] DR CCDS; CCDS8777.1; -. [P54619-1] DR RefSeq; NP_001193638.1; NM_001206709.1. [P54619-3] DR RefSeq; NP_001193639.1; NM_001206710.1. [P54619-2] DR RefSeq; NP_002724.1; NM_002733.4. [P54619-1] DR RefSeq; XP_006719562.1; XM_006719499.1. [P54619-2] DR UniGene; Hs.530862; -. DR PDB; 2UV4; X-ray; 1.33 A; A=182-325. DR PDB; 2UV5; X-ray; 1.69 A; A=182-325. DR PDB; 2UV6; X-ray; 2.00 A; A=182-325. DR PDB; 2UV7; X-ray; 2.00 A; A=182-325. DR PDB; 4CFE; X-ray; 3.02 A; E/F=1-331. DR PDB; 4CFF; X-ray; 3.92 A; E/F=1-331. DR PDBsum; 2UV4; -. DR PDBsum; 2UV5; -. DR PDBsum; 2UV6; -. DR PDBsum; 2UV7; -. DR PDBsum; 4CFE; -. DR PDBsum; 4CFF; -. DR ProteinModelPortal; P54619; -. DR SMR; P54619; 27-325. DR BioGrid; 111558; 19. DR IntAct; P54619; 19. DR MINT; MINT-4649712; -. DR STRING; 9606.ENSP00000323867; -. DR BindingDB; P54619; -. DR ChEMBL; CHEMBL2096907; -. DR PhosphoSite; P54619; -. DR DMDM; 1703037; -. DR MaxQB; P54619; -. DR PaxDb; P54619; -. DR PRIDE; P54619; -. DR DNASU; 5571; -. DR Ensembl; ENST00000316299; ENSP00000323867; ENSG00000181929. [P54619-3] DR Ensembl; ENST00000548065; ENSP00000447433; ENSG00000181929. [P54619-1] DR Ensembl; ENST00000552212; ENSP00000448972; ENSG00000181929. [P54619-2] DR GeneID; 5571; -. DR KEGG; hsa:5571; -. DR UCSC; uc001rsy.3; human. [P54619-1] DR UCSC; uc001rsz.3; human. DR CTD; 5571; -. DR GeneCards; GC12M049396; -. DR HGNC; HGNC:9385; PRKAG1. DR MIM; 602742; gene. DR neXtProt; NX_P54619; -. DR PharmGKB; PA33751; -. DR eggNOG; COG0517; -. DR HOVERGEN; HBG050431; -. DR InParanoid; P54619; -. DR KO; K07200; -. DR OMA; KGGAYDE; -. DR PhylomeDB; P54619; -. DR TreeFam; TF313247; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_200751; Organelle biogenesis and maintenance. DR SignaLink; P54619; -. DR ChiTaRS; PRKAG1; human. DR EvolutionaryTrace; P54619; -. DR GeneWiki; PRKAG1; -. DR GenomeRNAi; 5571; -. DR NextBio; 21596; -. DR PRO; PR:P54619; -. DR ArrayExpress; P54619; -. DR Bgee; P54619; -. DR CleanEx; HS_PRKAG1; -. DR Genevestigator; P54619; -. DR GO; GO:0031588; C:AMP-activated protein kinase complex; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0043531; F:ADP binding; ISS:UniProtKB. DR GO; GO:0016208; F:AMP binding; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB. DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; TAS:ProtInc. DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; TAS:BHF-UCL. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL. DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:0045860; P:positive regulation of protein kinase activity; TAS:BHF-UCL. DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0006110; P:regulation of glycolytic process; TAS:BHF-UCL. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 4. DR SMART; SM00116; CBS; 4. DR PROSITE; PS51371; CBS; 4. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; CBS domain; KW Complete proteome; Direct protein sequencing; Fatty acid biosynthesis; KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; KW Repeat. FT CHAIN 1 331 5'-AMP-activated protein kinase subunit FT gamma-1. FT /FTId=PRO_0000204377. FT DOMAIN 43 103 CBS 1. FT DOMAIN 125 187 CBS 2. FT DOMAIN 198 260 CBS 3. FT DOMAIN 272 329 CBS 4. FT MOTIF 138 159 AMPK pseudosubstrate. FT BINDING 70 70 AMP 1 (By similarity). FT BINDING 70 70 ATP 1 (By similarity). FT BINDING 151 151 AMP 2 (By similarity). FT BINDING 151 151 AMP 3 (By similarity). FT BINDING 151 151 ATP 2 (By similarity). FT BINDING 152 152 ATP 1 (By similarity). FT BINDING 152 152 ATP 2 (By similarity). FT BINDING 170 170 AMP 1 (By similarity). FT BINDING 170 170 ATP 1 (By similarity). FT BINDING 298 298 AMP 3 (By similarity). FT BINDING 299 299 AMP 1 (By similarity). FT BINDING 299 299 ATP 1 (By similarity). FT MOD_RES 261 261 Phosphoserine; by ULK1 (By similarity). FT MOD_RES 263 263 Phosphothreonine; by ULK1 (By FT similarity). FT MOD_RES 270 270 Phosphoserine; by ULK1 (By similarity). FT VAR_SEQ 1 32 Missing (in isoform 2). FT /FTId=VSP_046711. FT VAR_SEQ 83 83 V -> VVLRALSCPL (in isoform 3). FT /FTId=VSP_046712. FT VARIANT 89 89 T -> S (in dbSNP:rs1126930). FT /FTId=VAR_033453. FT VARIANT 329 329 K -> N (in dbSNP:rs34210356). FT /FTId=VAR_033454. FT MUTAGEN 90 90 D->A: Reduced AMP-activation of FT phosphorylation of PRKAA1 or PRKAA2. FT Reduced ADP activation of phosphorylation FT of PRKAA1 or PRKAA2. FT MUTAGEN 245 245 D->A: Reduced AMP-activation of FT phosphorylation of PRKAA1 or PRKAA2. FT Reduced ADP activation of phosphorylation FT of PRKAA1 or PRKAA2. FT MUTAGEN 317 317 D->A: Reduced AMP-activation of FT phosphorylation of PRKAA1 or PRKAA2. Does FT not affect ADP activation of FT phosphorylation of PRKAA1 or PRKAA2. FT HELIX 28 33 FT HELIX 38 41 FT STRAND 44 52 FT HELIX 57 66 FT STRAND 72 76 FT TURN 77 80 FT STRAND 81 86 FT HELIX 88 97 FT STRAND 102 104 FT HELIX 107 111 FT HELIX 114 120 FT HELIX 138 147 FT STRAND 151 156 FT TURN 158 160 FT STRAND 163 168 FT HELIX 169 177 FT TURN 178 182 FT HELIX 186 189 FT HELIX 193 196 FT HELIX 213 223 FT STRAND 226 231 FT STRAND 235 242 FT HELIX 243 251 FT HELIX 262 267 FT HELIX 271 274 FT STRAND 277 279 FT HELIX 285 295 FT STRAND 298 303 FT STRAND 307 314 FT HELIX 315 322 SQ SEQUENCE 331 AA; 37579 MW; 0F22B9CA1DBD87AE CRC64; METVISSDSS PAVENEHPQE TPESNNSVYT SFMKSHRCYD LIPTSSKLVV FDTSLQVKKA FFALVTNGVR AAPLWDSKKQ SFVGMLTITD FINILHRYYK SALVQIYELE EHKIETWREV YLQDSFKPLV CISPNASLFD AVSSLIRNKI HRLPVIDPES GNTLYILTHK RILKFLKLFI TEFPKPEFMS KSLEELQIGT YANIAMVRTT TPVYVALGIF VQHRVSALPV VDEKGRVVDI YSKFDVINLA AEKTYNNLDV SVTKALQHRS HYFEGVLKCY LHETLETIIN RLVEAEVHRL VVVDENDVVK GIVSLSDILQ ALVLTGGEKK P // ID AAKG2_HUMAN Reviewed; 569 AA. AC Q9UGJ0; Q53Y07; Q6NUI0; Q75MP4; Q9NUZ9; Q9UDN8; Q9ULX8; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 09-JUL-2014, entry version 133. DE RecName: Full=5'-AMP-activated protein kinase subunit gamma-2; DE Short=AMPK gamma2; DE Short=AMPK subunit gamma-2; DE AltName: Full=H91620p; GN Name=PRKAG2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RA Hattori A., Seki N., Hayashi A., Kozuma S., Muramatsu M., Saito T.; RT "Human homolog of AMPK gamma-1 chain."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RX PubMed=10698692; DOI=10.1042/0264-6021:3460659; RA Cheung P.C.F., Salt I.P., Davies S.P., Hardie D.G., Carling D.; RT "Characterization of AMP-activated protein kinase gamma-subunit RT isoforms and their role in AMP binding."; RL Biochem. J. 346:659-669(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B). RX PubMed=11112354; DOI=10.1006/geno.2000.6376; RA Lang T.M., Yu L., Qiang T., Jiang J.M., Chen Z., Xin Y.R., Liu G.Y., RA Zhao S.; RT "Molecular cloning, genomic organization, and mapping of PRKAG2, a RT heart abundant gamma-2 subunit of 5'-AMP-activated protein kinase, to RT human chromosome 7q36."; RL Genomics 70:258-263(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS B AND C). RC TISSUE=Brain, and Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP DOMAIN CBS, AMP-BINDING, ATP-BINDING, CHARACTERIZATION OF VARIANTS RP WPWS GLN-302; ARG-383 AND ASN-400, CHARACTERIZATION OF VARIANT WPWS RP GLY-531, AND FUNCTION. RX PubMed=14722619; DOI=10.1172/JCI19874; RA Scott J.W., Hawley S.A., Green K.A., Anis M., Stewart G., RA Scullion G.A., Norman D.G., Hardie D.G.; RT "CBS domains form energy-sensing modules whose binding of adenosine RT ligands is disrupted by disease mutations."; RL J. Clin. Invest. 113:274-284(2004). RN [9] RP DOMAIN AMPK PSEUDOSUBSTRATE, AND MUTAGENESIS OF VAL-387. RX PubMed=17255938; DOI=10.1038/sj.emboj.7601542; RA Scott J.W., Ross F.A., Liu J.K., Hardie D.G.; RT "Regulation of AMP-activated protein kinase by a pseudosubstrate RT sequence on the gamma subunit."; RL EMBO J. 26:806-815(2007). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [13] RP PHOSPHORYLATION BY ULK1. RX PubMed=21460634; DOI=10.4161/auto.7.7.15451; RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.; RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative RT regulatory feedback loop."; RL Autophagy 7:696-706(2011). RN [14] RP REVIEW ON FUNCTION. RX PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05; RA Towler M.C., Hardie D.G.; RT "AMP-activated protein kinase in metabolic control and insulin RT signaling."; RL Circ. Res. 100:328-341(2007). RN [15] RP REVIEW ON FUNCTION. RX PubMed=17712357; DOI=10.1038/nrm2249; RA Hardie D.G.; RT "AMP-activated/SNF1 protein kinases: conserved guardians of cellular RT energy."; RL Nat. Rev. Mol. Cell Biol. 8:774-785(2007). RN [16] RP VARIANT WPWS GLY-531. RX PubMed=11748095; DOI=10.1161/hc5001.102111; RA Gollob M.H., Seger J.J., Gollob T.N., Tapscott T., Gonzales O., RA Bachinski L., Roberts R.; RT "Novel PRKAG2 mutation responsible for the genetic syndrome of RT ventricular preexcitation and conduction system disease with childhood RT onset and absence of cardiac hypertrophy."; RL Circulation 104:3030-3033(2001). RN [17] RP VARIANTS CMH6 LEU-350 INS AND ARG-383. RX PubMed=11371514; DOI=10.1093/hmg/10.11.1215; RA Blair E., Redwood C., Ashrafian H., Oliveira M., Broxholme J., RA Kerr B., Salmon A., Oestman-Smith I., Watkins H.; RT "Mutations in the gamma(2) subunit of AMP-activated protein kinase RT cause familial hypertrophic cardiomyopathy: evidence for the central RT role of energy compromise in disease pathogenesis."; RL Hum. Mol. Genet. 10:1215-1220(2001). RN [18] RP VARIANT WPWS GLN-302. RX PubMed=11407343; DOI=10.1056/NEJM200106143442403; RA Gollob M.H., Green M.S., Tang A.S.-L., Gollob T., Karibe A., RA Al Sayegh A.H., Ahmad F., Lozado R., Shah G., Fananapazir L., RA Bachinski L.L., Roberts R.; RT "Identification of a gene responsible for familial Wolff-Parkinson- RT White syndrome."; RL N. Engl. J. Med. 344:1823-1831(2001). RN [19] RP ERRATUM. RA Gollob M.H., Green M.S., Tang A.S.-L., Gollob T., Karibe A., RA Al Sayegh A.H., Ahmad F., Lozado R., Shah G., Fananapazir L., RA Bachinski L.L., Roberts R.; RL N. Engl. J. Med. 345:552-552(2001). RN [20] RP ERRATUM. RA Gollob M.H., Green M.S., Tang A.S.-L., Gollob T., Karibe A., RA Al Sayegh A.H., Ahmad F., Lozado R., Shah G., Fananapazir L., RA Bachinski L.L., Roberts R.; RL N. Engl. J. Med. 346:300-300(2002). RN [21] RP VARIANTS CMH6 GLN-302; ASN-400 AND ILE-488. RX PubMed=11827995; DOI=10.1172/JCI0214571; RA Arad M., Benson D.W., Perez-Atayde A.R., McKenna W.J., Sparks E.A., RA Kanter R.J., McGarry K., Seidman J.G., Seidman C.E.; RT "Constitutively active AMP kinase mutations cause glycogen storage RT disease mimicking hypertrophic cardiomyopathy."; RL J. Clin. Invest. 109:357-362(2002). RN [22] RP VARIANT GSDH GLN-531, AND CHARACTERIZATION OF VARIANT GSDH GLN-531. RX PubMed=15877279; DOI=10.1086/430840; RA Burwinkel B., Scott J.W., Buehrer C., van Landeghem F.K.H., Cox G.F., RA Wilson C.J., Grahame Hardie D., Kilimann M.W.; RT "Fatal congenital heart glycogenosis caused by a recurrent activating RT R531Q mutation in the gamma 2-subunit of AMP-activated protein kinase RT (PRKAG2), not by phosphorylase kinase deficiency."; RL Am. J. Hum. Genet. 76:1034-1049(2005). CC -!- FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase CC (AMPK), an energy sensor protein kinase that plays a key role in CC regulating cellular energy metabolism. In response to reduction of CC intracellular ATP levels, AMPK activates energy-producing pathways CC and inhibits energy-consuming processes: inhibits protein, CC carbohydrate and lipid biosynthesis, as well as cell growth and CC proliferation. AMPK acts via direct phosphorylation of metabolic CC enzymes, and by longer-term effects via phosphorylation of CC transcription regulators. Also acts as a regulator of cellular CC polarity by remodeling the actin cytoskeleton; probably by CC indirectly activating myosin. Gamma non-catalytic subunit mediates CC binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: CC AMP-binding results in allosteric activation of alpha catalytic CC subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and CC preventing dephosphorylation of catalytic subunits. ADP also CC stimulates phosphorylation, without stimulating already CC phosphorylated catalytic subunit. ATP promotes dephosphorylation CC of catalytic subunit, rendering the AMPK enzyme inactive. CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit CC (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non- CC catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with CC FNIP1 and FNIP2. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=A; CC IsoId=Q9UGJ0-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9UGJ0-2; Sequence=VSP_000261; CC Name=C; CC IsoId=Q9UGJ0-3; Sequence=VSP_015589; CC -!- TISSUE SPECIFICITY: Isoform B is ubiquitously expressed except in CC liver and thymus. The highest level is detected in heart with CC abundant expression in placenta and testis. CC -!- DOMAIN: The AMPK pseudosubstrate motif resembles the sequence CC around sites phosphorylated on target proteins of AMPK, except the CC presence of a non-phosphorylatable residue in place of Ser. In the CC absence of AMP this pseudosubstrate sequence may bind to the CC active site groove on the alpha subunit (PRKAA1 or PRKAA2), CC preventing phosphorylation by the upstream activating kinase CC STK11/LKB1. CC -!- DOMAIN: The CBS domains mediate binding to AMP, ADP and ATP. 2 CC sites bind either AMP or ATP, whereas a third site contains a CC tightly bound AMP that does not exchange. Under physiological CC conditions AMPK mainly exists in its inactive form in complex with CC ATP, which is much more abundant than AMP. CC -!- PTM: Phosphorylated by ULK1; leading to negatively regulate AMPK CC activity and suggesting the existence of a regulatory feedback CC loop between ULK1 and AMPK. CC -!- DISEASE: Wolff-Parkinson-White syndrome (WPWS) [MIM:194200]: A CC supernormal conduction disorder characterized by the presence of CC one or several accessory atrioventricular connections, which can CC lead to episodes of sporadic tachycardia. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 6 (CMH6) CC [MIM:600858]: A hereditary heart disorder characterized by CC ventricular hypertrophy, which is usually asymmetric and often CC involves the interventricular septum. The symptoms include CC dyspnea, syncope, collapse, palpitations, and chest pain. They can CC be readily provoked by exercise. The disorder has inter- and CC intrafamilial variability ranging from benign to malignant forms CC with high risk of cardiac failure and sudden cardiac death. CMH6 CC patients present Wolff-Parkinson-White ventricular preexcitation, CC enlarged myocytes without myofiber disarray, and glycogen- CC containing cytosolic vacuoles within cardiomyocytes. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Glycogen storage disease of heart lethal congenital CC (GSDH) [MIM:261740]: Rare disease which leads to death within a CC few weeks to a few months after birth, through heart failure and CC respiratory compromise. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma CC subunit family. CC -!- SIMILARITY: Contains 4 CBS domains. CC -!- SEQUENCE CAUTION: CC Sequence=AAH20540.2; Type=Erroneous initiation; CC Sequence=AAS02032.1; Type=Erroneous gene model prediction; CC Sequence=BAA84695.1; Type=Frameshift; Positions=228, 233; Note=Frameshifts are upstream of the initiating Met of isoform B; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB025580; BAA84695.1; ALT_FRAME; mRNA. DR EMBL; AJ249976; CAB65116.1; -; mRNA. DR EMBL; AF087875; AAK00413.1; -; mRNA. DR EMBL; AK001887; BAA91962.1; -; mRNA. DR EMBL; BT007127; AAP35791.1; -; mRNA. DR EMBL; AC006358; AAS02032.1; ALT_SEQ; Genomic_DNA. DR EMBL; AC006966; AAF03528.2; -; Genomic_DNA. DR EMBL; AC093583; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020540; AAH20540.2; ALT_INIT; mRNA. DR EMBL; BC068598; AAH68598.1; -; mRNA. DR CCDS; CCDS43683.1; -. [Q9UGJ0-3] DR CCDS; CCDS47752.1; -. [Q9UGJ0-2] DR CCDS; CCDS5928.1; -. [Q9UGJ0-1] DR RefSeq; NP_001035723.1; NM_001040633.1. [Q9UGJ0-3] DR RefSeq; NP_057287.2; NM_016203.3. [Q9UGJ0-1] DR RefSeq; NP_077747.1; NM_024429.1. [Q9UGJ0-2] DR UniGene; Hs.647072; -. DR ProteinModelPortal; Q9UGJ0; -. DR SMR; Q9UGJ0; 260-557. DR BioGrid; 119531; 19. DR IntAct; Q9UGJ0; 15. DR MINT; MINT-4831646; -. DR STRING; 9606.ENSP00000287878; -. DR BindingDB; Q9UGJ0; -. DR ChEMBL; CHEMBL2096907; -. DR PhosphoSite; Q9UGJ0; -. DR DMDM; 14285344; -. DR MaxQB; Q9UGJ0; -. DR PaxDb; Q9UGJ0; -. DR PRIDE; Q9UGJ0; -. DR DNASU; 51422; -. DR Ensembl; ENST00000287878; ENSP00000287878; ENSG00000106617. [Q9UGJ0-1] DR Ensembl; ENST00000392801; ENSP00000376549; ENSG00000106617. [Q9UGJ0-3] DR Ensembl; ENST00000418337; ENSP00000387386; ENSG00000106617. [Q9UGJ0-2] DR GeneID; 51422; -. DR KEGG; hsa:51422; -. DR UCSC; uc003wki.3; human. [Q9UGJ0-1] DR CTD; 51422; -. DR GeneCards; GC07M151253; -. DR GeneReviews; PRKAG2; -. DR HGNC; HGNC:9386; PRKAG2. DR HPA; CAB018641; -. DR HPA; HPA004246; -. DR MIM; 194200; phenotype. DR MIM; 261740; phenotype. DR MIM; 600858; phenotype. DR MIM; 602743; gene. DR neXtProt; NX_Q9UGJ0; -. DR Orphanet; 155; Familial isolated hypertrophic cardiomyopathy. DR Orphanet; 907; Wolff-Parkinson-White syndrome. DR PharmGKB; PA33752; -. DR eggNOG; COG0517; -. DR HOVERGEN; HBG050431; -. DR InParanoid; Q9UGJ0; -. DR KO; K07200; -. DR OMA; GAKQKEN; -. DR OrthoDB; EOG74FF0W; -. DR PhylomeDB; Q9UGJ0; -. DR TreeFam; TF313247; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_200751; Organelle biogenesis and maintenance. DR SignaLink; Q9UGJ0; -. DR ChiTaRS; PRKAG2; human. DR GeneWiki; PRKAG2; -. DR GenomeRNAi; 51422; -. DR NextBio; 54969; -. DR PRO; PR:Q9UGJ0; -. DR ArrayExpress; Q9UGJ0; -. DR Bgee; Q9UGJ0; -. DR CleanEx; HS_PRKAG2; -. DR Genevestigator; Q9UGJ0; -. DR GO; GO:0031588; C:AMP-activated protein kinase complex; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProt. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0043531; F:ADP binding; IDA:BHF-UCL. DR GO; GO:0016208; F:AMP binding; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL. DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IDA:BHF-UCL. DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IMP:BHF-UCL. DR GO; GO:0008607; F:phosphorylase kinase regulator activity; IMP:BHF-UCL. DR GO; GO:0030295; F:protein kinase activator activity; IMP:BHF-UCL. DR GO; GO:0019901; F:protein kinase binding; IDA:BHF-UCL. DR GO; GO:0006754; P:ATP biosynthetic process; TAS:BHF-UCL. DR GO; GO:0006853; P:carnitine shuttle; TAS:Reactome. DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0005977; P:glycogen metabolic process; IMP:BHF-UCL. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0035556; P:intracellular signal transduction; IMP:BHF-UCL. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:BHF-UCL. DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IDA:GOC. DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:BHF-UCL. DR GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:BHF-UCL. DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; TAS:Reactome. DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:BHF-UCL. DR GO; GO:0046320; P:regulation of fatty acid oxidation; TAS:BHF-UCL. DR GO; GO:0046324; P:regulation of glucose import; TAS:BHF-UCL. DR GO; GO:0006110; P:regulation of glycolytic process; IMP:BHF-UCL. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0016126; P:sterol biosynthetic process; TAS:BHF-UCL. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 3. DR SMART; SM00116; CBS; 4. DR PROSITE; PS51371; CBS; 4. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cardiomyopathy; CBS domain; KW Complete proteome; Disease mutation; Fatty acid biosynthesis; KW Fatty acid metabolism; Glycogen storage disease; Lipid biosynthesis; KW Lipid metabolism; Nucleotide-binding; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat. FT CHAIN 1 569 5'-AMP-activated protein kinase subunit FT gamma-2. FT /FTId=PRO_0000204381. FT DOMAIN 275 335 CBS 1. FT DOMAIN 357 415 CBS 2. FT DOMAIN 430 492 CBS 3. FT DOMAIN 504 562 CBS 4. FT MOTIF 370 391 AMPK pseudosubstrate. FT BINDING 302 302 AMP 1 (By similarity). FT BINDING 302 302 ATP 1 (By similarity). FT BINDING 383 383 AMP 2 (By similarity). FT BINDING 383 383 AMP 3 (By similarity). FT BINDING 383 383 ATP 2 (By similarity). FT BINDING 384 384 ATP 1 (By similarity). FT BINDING 384 384 ATP 2 (By similarity). FT BINDING 402 402 AMP 1 (By similarity). FT BINDING 402 402 ATP 1 (By similarity). FT BINDING 530 530 AMP 3 (By similarity). FT BINDING 531 531 AMP 1 (By similarity). FT BINDING 531 531 ATP 1 (By similarity). FT MOD_RES 65 65 Phosphoserine (By similarity). FT MOD_RES 71 71 Phosphoserine (By similarity). FT MOD_RES 73 73 Phosphoserine (By similarity). FT MOD_RES 90 90 Phosphoserine (By similarity). FT MOD_RES 138 138 Phosphoserine (By similarity). FT MOD_RES 143 143 Phosphoserine (By similarity). FT MOD_RES 161 161 Phosphoserine (By similarity). FT MOD_RES 196 196 Phosphoserine (By similarity). FT VAR_SEQ 1 241 Missing (in isoform B). FT /FTId=VSP_000261. FT VAR_SEQ 1 44 Missing (in isoform C). FT /FTId=VSP_015589. FT VARIANT 6 6 M -> L (in dbSNP:rs3207363). FT /FTId=VAR_048250. FT VARIANT 302 302 R -> Q (in WPWS and CMH6; impaired AMP- FT and ATP-binding). FT /FTId=VAR_013264. FT VARIANT 350 350 R -> RL (in CMH6; severe). FT /FTId=VAR_013265. FT VARIANT 383 383 H -> R (in CMH6; severe; impaired AMP- FT and ATP-binding). FT /FTId=VAR_013266. FT VARIANT 400 400 T -> N (in CMH6; severe; impaired AMP- FT and ATP-binding; dbSNP:rs28938173). FT /FTId=VAR_013267. FT VARIANT 488 488 N -> I (in CMH6; severe). FT /FTId=VAR_013268. FT VARIANT 531 531 R -> G (in WPWS; absence of cardiac FT hypertrophy; onset in childhood; impaired FT AMP- and ATP-binding). FT /FTId=VAR_032909. FT VARIANT 531 531 R -> Q (in GSDH; reduction of binding FT affinities for AMP and ATP; loss of FT cooperative binding; enhanced basal FT activity; increased phosphorylation of FT the alpha-subunit). FT /FTId=VAR_013269. FT MUTAGEN 387 387 V->S: Induces phosphorylation by AMPK. SQ SEQUENCE 569 AA; 63066 MW; F51C30668C294089 CRC64; MGSAVMDTKK KKDVSSPGGS GGKKNASQKR RSLRVHIPDL SSFAMPLLDG DLEGSGKHSS RKVDSPFGPG SPSKGFFSRG PQPRPSSPMS APVRPKTSPG SPKTVFPFSY QESPPRSPRR MSFSGIFRSS SKESSPNSNP ATSPGGIRFF SRSRKTSGLS SSPSTPTQVT KQHTFPLESY KHEPERLENR IYASSSPPDT GQRFCPSSFQ SPTRPPLASP THYAPSKAAA LAAALGPAEA GMLEKLEFED EAVEDSESGV YMRFMRSHKC YDIVPTSSKL VVFDTTLQVK KAFFALVANG VRAAPLWESK KQSFVGMLTI TDFINILHRY YKSPMVQIYE LEEHKIETWR ELYLQETFKP LVNISPDASL FDAVYSLIKN KIHRLPVIDP ISGNALYILT HKRILKFLQL FMSDMPKPAF MKQNLDELGI GTYHNIAFIH PDTPIIKALN IFVERRISAL PVVDESGKVV DIYSKFDVIN LAAEKTYNNL DITVTQALQH RSQYFEGVVK CNKLEILETI VDRIVRAEVH RLVVVNEADS IVGIISLSDI LQALILTPAG AKQKETETE // ID AAPK1_HUMAN Reviewed; 559 AA. AC Q13131; A8MTQ6; B2R7E1; O00286; Q5D0E1; Q86VS1; Q9UNQ4; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 4. DT 09-JUL-2014, entry version 158. DE RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-1; DE Short=AMPK subunit alpha-1; DE EC=2.7.11.1; DE AltName: Full=Acetyl-CoA carboxylase kinase; DE Short=ACACA kinase; DE EC=2.7.11.27; DE AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase; DE Short=HMGCR kinase; DE EC=2.7.11.31; DE AltName: Full=Tau-protein kinase PRKAA1; DE EC=2.7.11.26; GN Name=PRKAA1; Synonyms=AMPK1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP LEU-10. RC TISSUE=Brain, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-559 (ISOFORM 1). RC TISSUE=Mammary gland; RA Yano K.; RT "Nucleotide sequence of cDNA for human AMP-activated protein kinase RT alpha-1."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-559 (ISOFORM 1). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-559 (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-209 (ISOFORM 1). RC TISSUE=Intestine; RA Taboada E.N., Hickey D.A.; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 303-559 (ISOFORMS 1/2). RC TISSUE=Liver; RX PubMed=8557660; DOI=10.1074/jbc.271.2.611; RA Stapleton D., Mitchelhill K.I., Gao G., Widmer J., Michell B.J., RA Teh T., House C.M., Fernandez C.S., Cox T., Witters L.A., Kemp B.E.; RT "Mammalian AMP-activated protein kinase subfamily."; RL J. Biol. Chem. 271:611-614(1996). RN [8] RP DOMAIN AIS. RX PubMed=9857077; DOI=10.1074/jbc.273.52.35347; RA Crute B.E., Seefeld K., Gamble J., Kemp B.E., Witters L.A.; RT "Functional domains of the alpha1 catalytic subunit of the AMP- RT activated protein kinase."; RL J. Biol. Chem. 273:35347-35354(1998). RN [9] RP FUNCTION. RX PubMed=11554766; DOI=10.1006/bbrc.2001.5627; RA Imamura K., Ogura T., Kishimoto A., Kaminishi M., Esumi H.; RT "Cell cycle regulation via p53 phosphorylation by a 5'-AMP activated RT protein kinase activator, 5-aminoimidazole-4-carboxamide-1-beta-D- RT ribofuranoside, in a human hepatocellular carcinoma cell line."; RL Biochem. Biophys. Res. Commun. 287:562-567(2001). RN [10] RP FUNCTION IN PHOSPHORYLATION OF EP300. RX PubMed=11518699; DOI=10.1074/jbc.C100316200; RA Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T.; RT "Regulation of transcription by AMP-activated protein kinase: RT phosphorylation of p300 blocks its interaction with nuclear RT receptors."; RL J. Biol. Chem. 276:38341-38344(2001). RN [11] RP ENZYME REGULATION. RX PubMed=11602624; DOI=10.1172/JCI13505; RA Zhou G., Myers R., Li Y., Chen Y., Shen X., Fenyk-Melody J., Wu M., RA Ventre J., Doebber T., Fujii N., Musi N., Hirshman M.F., RA Goodyear L.J., Moller D.E.; RT "Role of AMP-activated protein kinase in mechanism of metformin RT action."; RL J. Clin. Invest. 108:1167-1174(2001). RN [12] RP FUNCTION IN PHOSPHORYLATION OF CFTR. RX PubMed=12519745; DOI=10.1152/ajpcell.00227.2002; RA Hallows K.R., Kobinger G.P., Wilson J.M., Witters L.A., Foskett J.K.; RT "Physiological modulation of CFTR activity by AMP-activated protein RT kinase in polarized T84 cells."; RL Am. J. Physiol. 284:C1297-C1308(2003). RN [13] RP FUNCTION IN PHOSPHORYLATION OF TSC2. RX PubMed=14651849; DOI=10.1016/S0092-8674(03)00929-2; RA Inoki K., Zhu T., Guan K.L.; RT "TSC2 mediates cellular energy response to control cell growth and RT survival."; RL Cell 115:577-590(2003). RN [14] RP PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION. RX PubMed=14976552; DOI=10.1038/sj.emboj.7600110; RA Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A., RA Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G., RA Alessi D.R.; RT "LKB1 is a master kinase that activates 13 kinases of the AMPK RT subfamily, including MARK/PAR-1."; RL EMBO J. 23:833-843(2004). RN [15] RP PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION. RX PubMed=16054095; DOI=10.1016/j.cmet.2005.05.009; RA Hawley S.A., Pan D.A., Mustard K.J., Ross L., Bain J., Edelman A.M., RA Frenguelli B.G., Hardie D.G.; RT "Calmodulin-dependent protein kinase kinase-beta is an alternative RT upstream kinase for AMP-activated protein kinase."; RL Cell Metab. 2:9-19(2005). RN [16] RP PHOSPHORYLATION AT THR-183, AND ENZYME REGULATION. RX PubMed=15980064; DOI=10.1074/jbc.M503824200; RA Hurley R.L., Anderson K.A., Franzone J.M., Kemp B.E., Means A.R., RA Witters L.A.; RT "The Ca2+/calmodulin-dependent protein kinase kinases are AMP- RT activated protein kinase kinases."; RL J. Biol. Chem. 280:29060-29066(2005). RN [17] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15866171; DOI=10.1016/j.molcel.2005.03.027; RA Jones R.G., Plas D.R., Kubek S., Buzzai M., Mu J., Xu Y., RA Birnbaum M.J., Thompson C.B.; RT "AMP-activated protein kinase induces a p53-dependent metabolic RT checkpoint."; RL Mol. Cell 18:283-293(2005). RN [18] RP INTERACTION WITH FNIP1. RX PubMed=17028174; DOI=10.1073/pnas.0603781103; RA Baba M., Hong S.-B., Sharma N., Warren M.B., Nickerson M.L., RA Iwamatsu A., Esposito D., Gillette W.K., Hopkins R.F. III, RA Hartley J.L., Furihata M., Oishi S., Zhen W., Burke T.R. Jr., RA Linehan W.M., Schmidt L.S., Zbar B.; RT "Folliculin encoded by the BHD gene interacts with a binding protein, RT FNIP1, and AMPK, and is involved in AMPK and mTOR signaling."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15552-15557(2006). RN [19] RP DOMAIN AIS, AND MUTAGENESIS OF VAL-307. RX PubMed=17088252; DOI=10.1074/jbc.M605790200; RA Pang T., Xiong B., Li J.Y., Qiu B.Y., Jin G.Z., Shen J.K., Li J.; RT "Conserved alpha-helix acts as autoinhibitory sequence in AMP- RT activated protein kinase alpha subunits."; RL J. Biol. Chem. 282:495-506(2007). RN [20] RP FUNCTION IN PHOSPHORYLATION OF FOXO3. RX PubMed=17711846; DOI=10.1074/jbc.M705325200; RA Greer E.L., Oskoui P.R., Banko M.R., Maniar J.M., Gygi M.P., RA Gygi S.P., Brunet A.; RT "The energy sensor AMP-activated protein kinase directly regulates the RT mammalian FOXO3 transcription factor."; RL J. Biol. Chem. 282:30107-30119(2007). RN [21] RP FUNCTION IN CELL POLARITY. RX PubMed=17486097; DOI=10.1038/nature05828; RA Lee J.H., Koh H., Kim M., Kim Y., Lee S.Y., Karess R.E., Lee S.H., RA Shong M., Kim J.M., Kim J., Chung J.; RT "Energy-dependent regulation of cell structure by AMP-activated RT protein kinase."; RL Nature 447:1017-1020(2007). RN [22] RP FUNCTION IN PHOSPHORYLATION OF HDAC5. RX PubMed=18184930; DOI=10.2337/db07-0843; RA McGee S.L., van Denderen B.J., Howlett K.F., Mollica J., RA Schertzer J.D., Kemp B.E., Hargreaves M.; RT "AMP-activated protein kinase regulates GLUT4 transcription by RT phosphorylating histone deacetylase 5."; RL Diabetes 57:860-867(2008). RN [23] RP INTERACTION WITH FNIP2. RX PubMed=18403135; DOI=10.1016/j.gene.2008.02.022; RA Hasumi H., Baba M., Hong S.-B., Hasumi Y., Huang Y., Yao M., RA Valera V.A., Linehan W.M., Schmidt L.S.; RT "Identification and characterization of a novel folliculin-interacting RT protein FNIP2."; RL Gene 415:60-67(2008). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-382, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [26] RP FUNCTION IN PHOSPHORYLATION OF RPTOR. RX PubMed=18439900; DOI=10.1016/j.molcel.2008.03.003; RA Gwinn D.M., Shackelford D.B., Egan D.F., Mihaylova M.M., Mery A., RA Vasquez D.S., Turk B.E., Shaw R.J.; RT "AMPK phosphorylation of raptor mediates a metabolic checkpoint."; RL Mol. Cell 30:214-226(2008). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [28] RP INTERACTION WITH FNIP2. RX PubMed=18663353; DOI=10.1038/onc.2008.261; RA Takagi Y., Kobayashi T., Shiono M., Wang L., Piao X., Sun G., RA Zhang D., Abe M., Hagiwara Y., Takahashi K., Hino O.; RT "Interaction of folliculin (Birt-Hogg-Dube gene product) with a novel RT Fnip1-like (FnipL/Fnip2) protein."; RL Oncogene 27:5339-5347(2008). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356; SER-486; THR-490 RP AND SER-496, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32 AND SER-467, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-382, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [32] RP FUNCTION IN PHOSPHORYLATION OF KLC1. RX PubMed=20074060; DOI=10.1042/BST0380205; RA McDonald A., Fogarty S., Leclerc I., Hill E.V., Hardie D.G., RA Rutter G.A.; RT "Cell-wide analysis of secretory granule dynamics in three dimensions RT in living pancreatic beta-cells: evidence against a role for AMPK- RT dependent phosphorylation of KLC1 at Ser517/Ser520 in glucose- RT stimulated insulin granule movement."; RL Biochem. Soc. Trans. 38:205-208(2010). RN [33] RP FUNCTION. RX PubMed=20160076; DOI=10.1073/pnas.0913860107; RA Alexander A., Cai S.L., Kim J., Nanez A., Sahin M., MacLean K.H., RA Inoki K., Guan K.L., Shen J., Person M.D., Kusewitt D., Mills G.B., RA Kastan M.B., Walker C.L.; RT "ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response RT to ROS."; RL Proc. Natl. Acad. Sci. U.S.A. 107:4153-4158(2010). RN [34] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [35] RP PHOSPHORYLATION BY ULK1 AND ULK2. RX PubMed=21460634; DOI=10.4161/auto.7.7.15451; RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.; RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative RT regulatory feedback loop."; RL Autophagy 7:696-706(2011). RN [36] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [37] RP FUNCTION IN PHOSPHORYLATION OF ULK1. RX PubMed=21205641; DOI=10.1126/science.1196371; RA Egan D.F., Shackelford D.B., Mihaylova M.M., Gelino S., Kohnz R.A., RA Mair W., Vasquez D.S., Joshi A., Gwinn D.M., Taylor R., Asara J.M., RA Fitzpatrick J., Dillin A., Viollet B., Kundu M., Hansen M., Shaw R.J.; RT "Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase RT connects energy sensing to mitophagy."; RL Science 331:456-461(2011). RN [38] RP INTERACTION WITH PRKAB1 AND PRKAG1, AND ENZYME REGULATION. RX PubMed=21680840; DOI=10.1126/science.1200094; RA Oakhill J.S., Steel R., Chen Z.P., Scott J.W., Ling N., Tam S., RA Kemp B.E.; RT "AMPK is a direct adenylate charge-regulated protein kinase."; RL Science 332:1433-1435(2011). RN [39] RP REVIEW ON FUNCTION. RX PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05; RA Towler M.C., Hardie D.G.; RT "AMP-activated protein kinase in metabolic control and insulin RT signaling."; RL Circ. Res. 100:328-341(2007). RN [40] RP REVIEW ON FUNCTION. RX PubMed=17712357; DOI=10.1038/nrm2249; RA Hardie D.G.; RT "AMP-activated/SNF1 protein kinases: conserved guardians of cellular RT energy."; RL Nat. Rev. Mol. Cell Biol. 8:774-785(2007). RN [41] RP DEPHOSPHORYLATION. RX PubMed=23088624; DOI=10.1042/BJ20121201; RA Chida T., Ando M., Matsuki T., Masu Y., Nagaura Y., RA Takano-Yamamoto T., Tamura S., Kobayashi T.; RT "N-Myristoylation is essential for protein phosphatases PPM1A and RT PPM1B to dephosphorylate their physiological substrates in cells."; RL Biochem. J. 449:741-749(2013). RN [42] RP VARIANT [LARGE SCALE ANALYSIS] ARG-16. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Catalytic subunit of AMP-activated protein kinase CC (AMPK), an energy sensor protein kinase that plays a key role in CC regulating cellular energy metabolism. In response to reduction of CC intracellular ATP levels, AMPK activates energy-producing pathways CC and inhibits energy-consuming processes: inhibits protein, CC carbohydrate and lipid biosynthesis, as well as cell growth and CC proliferation. AMPK acts via direct phosphorylation of metabolic CC enzymes, and by longer-term effects via phosphorylation of CC transcription regulators. Also acts as a regulator of cellular CC polarity by remodeling the actin cytoskeleton; probably by CC indirectly activating myosin. Regulates lipid synthesis by CC phosphorylating and inactivating lipid metabolic enzymes such as CC ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and CC cholesterol synthesis by phosphorylating acetyl-CoA carboxylase CC (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, CC respectively. Regulates insulin-signaling and glycolysis by CC phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose CC uptake in muscle by increasing the translocation of the glucose CC transporter SLC2A4/GLUT4 to the plasma membrane, possibly by CC mediating phosphorylation of TBC1D4/AS160. Regulates transcription CC and chromatin structure by phosphorylating transcription CC regulators involved in energy metabolism such as CRTC2/TORC2, CC FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, CC p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of CC glucose homeostasis in liver by phosphorylating CRTC2/TORC2, CC leading to CRTC2/TORC2 sequestration in the cytoplasm. In response CC to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), CC leading to promote transcription. Acts as a key regulator of cell CC growth and proliferation by phosphorylating TSC2, RPTOR and CC ATG1/ULK1: in response to nutrient limitation, negatively CC regulates the mTORC1 complex by phosphorylating RPTOR component of CC the mTORC1 complex and by phosphorylating and activating TSC2. In CC response to nutrient limitation, promotes autophagy by CC phosphorylating and activating ATG1/ULK1. AMPK also acts as a CC regulator of circadian rhythm by mediating phosphorylation of CC CRY1, leading to destabilize it. May regulate the Wnt signaling CC pathway by phosphorylating CTNNB1, leading to stabilize it. Also CC has tau-protein kinase activity: in response to amyloid beta A4 CC protein (APP) exposure, activated by CAMKK2, leading to CC phosphorylation of MAPT/TAU; however the relevance of such data CC remains unclear in vivo. Also phosphorylates CFTR, EEF2K, KLC1, CC NOS3 and SLC12A1. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein] CC phosphate. CC -!- CATALYTIC ACTIVITY: ATP + [hydroxymethylglutaryl-CoA reductase CC (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] CC phosphate. CC -!- CATALYTIC ACTIVITY: ATP + [acetyl-CoA carboxylase] = ADP + CC [acetyl-CoA carboxylase] phosphate. CC -!- COFACTOR: Magnesium. CC -!- ENZYME REGULATION: Activated by phosphorylation on Thr-183. CC Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or CC PRKAG3) results in allosteric activation, inducing phosphorylation CC on Thr-183. AMP-binding to gamma subunit also sustains activity by CC preventing dephosphorylation of Thr-183. ADP also stimulates Thr- CC 183 phosphorylation, without stimulating already phosphorylated CC AMPK. ATP promotes dephosphorylation of Thr-183, rendering the CC enzyme inactive. Under physiological conditions AMPK mainly exists CC in its inactive form in complex with ATP, which is much more CC abundant than AMP. AMPK is activated by antihyperglycemic drug CC metformin, a drug prescribed to patients with type 2 diabetes: in CC vivo, metformin seems to mainly inhibit liver gluconeogenesis. CC However, metformin can be used to activate AMPK in muscle and CC other cells in culture or ex vivo (PubMed:11602624). Selectively CC inhibited by compound C (6-[4-(2-Piperidin-1-yl-ethoxy)-phenyl)]- CC 3-pyridin-4-yl-pyyrazolo[1,5-a] pyrimidine. Activated by CC resveratrol, a natural polyphenol present in red wine, and S17834, CC a synthetic polyphenol. CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit CC (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non- CC catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with CC FNIP1 and FNIP2. CC -!- INTERACTION: CC P08238:HSP90AB1; NbExp=2; IntAct=EBI-1181405, EBI-352572; CC Q9Y478:PRKAB1; NbExp=5; IntAct=EBI-1181405, EBI-719769; CC O43741:PRKAB2; NbExp=6; IntAct=EBI-1181405, EBI-1053424; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In response to CC stress, recruited by p53/TP53 to specific promoters. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13131-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13131-2; Sequence=VSP_035431; CC -!- DOMAIN: The AIS (autoinhibitory sequence) region shows some CC sequence similarity with the ubiquitin-associated domains and CC represses kinase activity. CC -!- PTM: Ubiquitinated (By similarity). CC -!- PTM: Phosphorylated at Thr-183 by STK11/LKB1 in complex with CC STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also CC phosphorylated at Thr-183 by CAMKK2; triggered by a rise in CC intracellular calcium ions, without detectable changes in the CC AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-183, but at a CC much lower level. Dephosphorylated by protein phosphatase 2A and CC 2C (PP2A and PP2C). Phosphorylated by ULK1 and ULK2; leading to CC negatively regulate AMPK activity and suggesting the existence of CC a regulatory feedback loop between ULK1, ULK2 and AMPK. CC Dephosphorylated by PPM1A and PPM1B. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. SNF1 subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAA64850.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAD43027.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAH37303.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAA36547.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAG35788.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AC008810; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC048980; AAH48980.1; -; mRNA. DR EMBL; AB022017; BAA36547.1; ALT_INIT; mRNA. DR EMBL; AK312947; BAG35788.1; ALT_INIT; mRNA. DR EMBL; BC037303; AAH37303.1; ALT_INIT; mRNA. DR EMBL; AF100763; AAD43027.1; ALT_INIT; mRNA. DR EMBL; U22456; AAA64850.1; ALT_INIT; mRNA. DR EMBL; Y12856; CAA73361.1; -; mRNA. DR CCDS; CCDS3932.2; -. [Q13131-1] DR CCDS; CCDS3933.2; -. [Q13131-2] DR PIR; G01743; G01743. DR RefSeq; NP_006242.5; NM_006251.5. [Q13131-1] DR RefSeq; NP_996790.3; NM_206907.3. [Q13131-2] DR UniGene; Hs.43322; -. DR ProteinModelPortal; Q13131; -. DR SMR; Q13131; 18-559. DR BioGrid; 111549; 253. DR DIP; DIP-39973N; -. DR IntAct; Q13131; 62. DR MINT; MINT-6771251; -. DR STRING; 9606.ENSP00000346148; -. DR BindingDB; Q13131; -. DR ChEMBL; CHEMBL3038451; -. DR DrugBank; DB00131; Adenosine monophosphate. DR DrugBank; DB00171; Adenosine triphosphate. DR DrugBank; DB00914; Phenformin. DR GuidetoPHARMACOLOGY; 1541; -. DR PhosphoSite; Q13131; -. DR DMDM; 254763436; -. DR MaxQB; Q13131; -. DR PaxDb; Q13131; -. DR PRIDE; Q13131; -. DR DNASU; 5562; -. DR Ensembl; ENST00000354209; ENSP00000346148; ENSG00000132356. [Q13131-2] DR Ensembl; ENST00000397128; ENSP00000380317; ENSG00000132356. [Q13131-1] DR GeneID; 5562; -. DR KEGG; hsa:5562; -. DR UCSC; uc003jmb.3; human. [Q13131-2] DR UCSC; uc003jmc.3; human. [Q13131-1] DR CTD; 5562; -. DR GeneCards; GC05M040759; -. DR H-InvDB; HIX0004832; -. DR HGNC; HGNC:9376; PRKAA1. DR HPA; CAB005050; -. DR HPA; HPA035409; -. DR MIM; 602739; gene. DR neXtProt; NX_Q13131; -. DR PharmGKB; PA33744; -. DR eggNOG; COG0515; -. DR HOGENOM; HOG000233016; -. DR HOVERGEN; HBG050432; -. DR KO; K07198; -. DR OMA; MKRATIR; -. DR OrthoDB; EOG7RRF6K; -. DR PhylomeDB; Q13131; -. DR TreeFam; TF314032; -. DR BRENDA; 2.7.11.1; 2681. DR Reactome; REACT_111102; Signal Transduction. DR SignaLink; Q13131; -. DR ChiTaRS; PRKAA1; human. DR GeneWiki; Protein_kinase,_AMP-activated,_alpha_1; -. DR GenomeRNAi; 5562; -. DR NextBio; 21546; -. DR PRO; PR:Q13131; -. DR ArrayExpress; Q13131; -. DR Bgee; Q13131; -. DR CleanEx; HS_PRKAA1; -. DR Genevestigator; Q13131; -. DR GO; GO:0031588; C:AMP-activated protein kinase complex; ISS:UniProtKB. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005622; C:intracellular; IC:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0050405; F:[acetyl-CoA carboxylase] kinase activity; IEA:UniProtKB-EC. DR GO; GO:0047322; F:[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; NAS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0035174; F:histone serine kinase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB. DR GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC. DR GO; GO:0000187; P:activation of MAPK activity; NAS:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome. DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl. DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl. DR GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009631; P:cold acclimation; IEA:Ensembl. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055089; P:fatty acid homeostasis; ISS:UniProtKB. DR GO; GO:0019395; P:fatty acid oxidation; IEA:Ensembl. DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB. DR GO; GO:0006006; P:glucose metabolic process; IEA:Ensembl. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0008610; P:lipid biosynthetic process; ISS:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:2001274; P:negative regulation of glucose import in response to insulin stimulus; IEA:Ensembl. DR GO; GO:0046318; P:negative regulation of glucosylceramide biosynthetic process; NAS:UniProtKB. DR GO; GO:0050995; P:negative regulation of lipid catabolic process; ISS:UniProtKB. DR GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB. DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; NAS:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:0045821; P:positive regulation of glycolytic process; ISS:UniProtKB. DR GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:Ensembl. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0031000; P:response to caffeine; IEA:Ensembl. DR GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; NAS:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR028797; PRKAA1. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24343:SF81; PTHR24343:SF81; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF103243; SSF103243; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Autophagy; Biological rhythms; KW Cholesterol biosynthesis; Cholesterol metabolism; Chromatin regulator; KW Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Kinase; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Serine/threonine-protein kinase; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism; Transcription; Transcription regulation; KW Transferase; Ubl conjugation; Wnt signaling pathway. FT CHAIN 1 559 5'-AMP-activated protein kinase catalytic FT subunit alpha-1. FT /FTId=PRO_0000085589. FT DOMAIN 27 279 Protein kinase. FT NP_BIND 33 41 ATP (By similarity). FT REGION 302 381 AIS. FT ACT_SITE 150 150 Proton acceptor (By similarity). FT BINDING 56 56 ATP (By similarity). FT MOD_RES 32 32 Phosphothreonine. FT MOD_RES 183 183 Phosphothreonine; by LKB1 and CaMKK2 (By FT similarity). FT MOD_RES 269 269 Phosphothreonine (By similarity). FT MOD_RES 356 356 Phosphoserine. FT MOD_RES 360 360 Phosphoserine; by ULK1 (By similarity). FT MOD_RES 368 368 Phosphothreonine; by ULK1 (By FT similarity). FT MOD_RES 382 382 Phosphothreonine. FT MOD_RES 397 397 Phosphoserine; by ULK1 (Probable). FT MOD_RES 467 467 Phosphoserine. FT MOD_RES 486 486 Phosphoserine. FT MOD_RES 488 488 Phosphothreonine; by ULK1 (Probable). FT MOD_RES 490 490 Phosphothreonine. FT MOD_RES 496 496 Phosphoserine. FT VAR_SEQ 121 121 R -> RKSDVPGVVKTGSTKE (in isoform 2). FT /FTId=VSP_035431. FT VARIANT 10 10 M -> L (in dbSNP:rs17855679). FT /FTId=VAR_058401. FT VARIANT 16 16 Q -> R (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035622. FT MUTAGEN 307 307 V->G,Q: Activates the kinase activity. FT CONFLICT 5 5 S -> C (in Ref. 4; BAG35788). FT CONFLICT 9 9 K -> S (in Ref. 5; AAD43027). FT CONFLICT 37 37 T -> A (in Ref. 6; AAA64850). FT CONFLICT 202 202 A -> V (in Ref. 6; AAA64850). FT CONFLICT 208 208 I -> L (in Ref. 6; AAA64850). FT CONFLICT 269 269 T -> S (in Ref. 3; BAA36547). SQ SEQUENCE 559 AA; 64009 MW; ABAE71FBF912947A CRC64; MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG HKVAVKILNR QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG ELFDYICKNG RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG LSNMMSDGEF LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG IFYTPQYLNP SVISLLKHML QVDPMKRATI KDIREHEWFK QDLPKYLFPE DPSYSSTMID DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTYSKMSL QLYQVDSRTY LLDFRSIDDE ITEAKSGTAT PQRSGSVSNY RSCQRSDSDA EAQGKSSEVS LTSSVTSLDS SPVDLTPRPG SHTIEFFEMC ANLIKILAQ // ID AAPK2_HUMAN Reviewed; 552 AA. AC P54646; Q9H1E8; Q9UD43; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 09-JUL-2014, entry version 148. DE RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2; DE Short=AMPK subunit alpha-2; DE EC=2.7.11.1; DE AltName: Full=Acetyl-CoA carboxylase kinase; DE Short=ACACA kinase; DE EC=2.7.11.27; DE AltName: Full=Hydroxymethylglutaryl-CoA reductase kinase; DE Short=HMGCR kinase; DE EC=2.7.11.31; GN Name=PRKAA2; Synonyms=AMPK, AMPK2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC TISSUE=Heart; RX PubMed=7959015; DOI=10.1016/0378-1119(94)90174-0; RA Aguan K., Scott J., See C.G., Sarkar N.H.; RT "Characterization and chromosomal localization of the human homologue RT of a rat AMP-activated protein kinase-encoding gene: a major regulator RT of lipid metabolism in mammals."; RL Gene 149:345-350(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=7988703; DOI=10.1016/0014-5793(94)01247-4; RA Beri R.K., Marley A.E., See C.G., Sopwith W.F., Aguan K., Carling D., RA Scott J., Carey F.; RT "Molecular cloning, expression and chromosomal localisation of human RT AMP-activated protein kinase."; RL FEBS Lett. 356:117-121(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION. RX PubMed=11554766; DOI=10.1006/bbrc.2001.5627; RA Imamura K., Ogura T., Kishimoto A., Kaminishi M., Esumi H.; RT "Cell cycle regulation via p53 phosphorylation by a 5'-AMP activated RT protein kinase activator, 5-aminoimidazole-4-carboxamide-1-beta-D- RT ribofuranoside, in a human hepatocellular carcinoma cell line."; RL Biochem. Biophys. Res. Commun. 287:562-567(2001). RN [6] RP FUNCTION IN PHOSPHORYLATION OF EP300. RX PubMed=11518699; DOI=10.1074/jbc.C100316200; RA Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T.; RT "Regulation of transcription by AMP-activated protein kinase: RT phosphorylation of p300 blocks its interaction with nuclear RT receptors."; RL J. Biol. Chem. 276:38341-38344(2001). RN [7] RP ENZYME REGULATION. RX PubMed=11602624; DOI=10.1172/JCI13505; RA Zhou G., Myers R., Li Y., Chen Y., Shen X., Fenyk-Melody J., Wu M., RA Ventre J., Doebber T., Fujii N., Musi N., Hirshman M.F., RA Goodyear L.J., Moller D.E.; RT "Role of AMP-activated protein kinase in mechanism of metformin RT action."; RL J. Clin. Invest. 108:1167-1174(2001). RN [8] RP FUNCTION IN PHOSPHORYLATION OF CFTR. RX PubMed=12519745; DOI=10.1152/ajpcell.00227.2002; RA Hallows K.R., Kobinger G.P., Wilson J.M., Witters L.A., Foskett J.K.; RT "Physiological modulation of CFTR activity by AMP-activated protein RT kinase in polarized T84 cells."; RL Am. J. Physiol. 284:C1297-C1308(2003). RN [9] RP FUNCTION IN PHOSPHORYLATION OF TSC2. RX PubMed=14651849; DOI=10.1016/S0092-8674(03)00929-2; RA Inoki K., Zhu T., Guan K.L.; RT "TSC2 mediates cellular energy response to control cell growth and RT survival."; RL Cell 115:577-590(2003). RN [10] RP PHOSPHORYLATION AT THR-172, AND ENZYME REGULATION. RX PubMed=15980064; DOI=10.1074/jbc.M503824200; RA Hurley R.L., Anderson K.A., Franzone J.M., Kemp B.E., Means A.R., RA Witters L.A.; RT "The Ca2+/calmodulin-dependent protein kinase kinases are AMP- RT activated protein kinase kinases."; RL J. Biol. Chem. 280:29060-29066(2005). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15866171; DOI=10.1016/j.molcel.2005.03.027; RA Jones R.G., Plas D.R., Kubek S., Buzzai M., Mu J., Xu Y., RA Birnbaum M.J., Thompson C.B.; RT "AMP-activated protein kinase induces a p53-dependent metabolic RT checkpoint."; RL Mol. Cell 18:283-293(2005). RN [12] RP FUNCTION IN PHOSPHORYLATION OF FOXO3. RX PubMed=17711846; DOI=10.1074/jbc.M705325200; RA Greer E.L., Oskoui P.R., Banko M.R., Maniar J.M., Gygi M.P., RA Gygi S.P., Brunet A.; RT "The energy sensor AMP-activated protein kinase directly regulates the RT mammalian FOXO3 transcription factor."; RL J. Biol. Chem. 282:30107-30119(2007). RN [13] RP FUNCTION IN CELL POLARITY. RX PubMed=17486097; DOI=10.1038/nature05828; RA Lee J.H., Koh H., Kim M., Kim Y., Lee S.Y., Karess R.E., Lee S.H., RA Shong M., Kim J.M., Kim J., Chung J.; RT "Energy-dependent regulation of cell structure by AMP-activated RT protein kinase."; RL Nature 447:1017-1020(2007). RN [14] RP FUNCTION IN PHOSPHORYLATION OF HDAC5. RX PubMed=18184930; DOI=10.2337/db07-0843; RA McGee S.L., van Denderen B.J., Howlett K.F., Mollica J., RA Schertzer J.D., Kemp B.E., Hargreaves M.; RT "AMP-activated protein kinase regulates GLUT4 transcription by RT phosphorylating histone deacetylase 5."; RL Diabetes 57:860-867(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [18] RP FUNCTION IN PHOSPHORYLATION OF KLC1. RX PubMed=20074060; DOI=10.1042/BST0380205; RA McDonald A., Fogarty S., Leclerc I., Hill E.V., Hardie D.G., RA Rutter G.A.; RT "Cell-wide analysis of secretory granule dynamics in three dimensions RT in living pancreatic beta-cells: evidence against a role for AMPK- RT dependent phosphorylation of KLC1 at Ser517/Ser520 in glucose- RT stimulated insulin granule movement."; RL Biochem. Soc. Trans. 38:205-208(2010). RN [19] RP FUNCTION. RX PubMed=20160076; DOI=10.1073/pnas.0913860107; RA Alexander A., Cai S.L., Kim J., Nanez A., Sahin M., MacLean K.H., RA Inoki K., Guan K.L., Shen J., Person M.D., Kusewitt D., Mills G.B., RA Kastan M.B., Walker C.L.; RT "ATM signals to TSC2 in the cytoplasm to regulate mTORC1 in response RT to ROS."; RL Proc. Natl. Acad. Sci. U.S.A. 107:4153-4158(2010). RN [20] RP PHOSPHORYLATION BY ULK1. RX PubMed=21460634; DOI=10.4161/auto.7.7.15451; RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.; RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative RT regulatory feedback loop."; RL Autophagy 7:696-706(2011). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP FUNCTION IN PHOSPHORYLATION OF ULK1. RX PubMed=21205641; DOI=10.1126/science.1196371; RA Egan D.F., Shackelford D.B., Mihaylova M.M., Gelino S., Kohnz R.A., RA Mair W., Vasquez D.S., Joshi A., Gwinn D.M., Taylor R., Asara J.M., RA Fitzpatrick J., Dillin A., Viollet B., Kundu M., Hansen M., Shaw R.J.; RT "Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase RT connects energy sensing to mitophagy."; RL Science 331:456-461(2011). RN [23] RP REVIEW ON FUNCTION. RX PubMed=17307971; DOI=10.1161/01.RES.0000256090.42690.05; RA Towler M.C., Hardie D.G.; RT "AMP-activated protein kinase in metabolic control and insulin RT signaling."; RL Circ. Res. 100:328-341(2007). RN [24] RP REVIEW ON FUNCTION. RX PubMed=17712357; DOI=10.1038/nrm2249; RA Hardie D.G.; RT "AMP-activated/SNF1 protein kinases: conserved guardians of cellular RT energy."; RL Nat. Rev. Mol. Cell Biol. 8:774-785(2007). RN [25] RP ENZYME REGULATION BY SALICYLATE. RX PubMed=22517326; DOI=10.1126/science.1215327; RA Hawley S.A., Fullerton M.D., Ross F.A., Schertzer J.D., Chevtzoff C., RA Walker K.J., Peggie M.W., Zibrova D., Green K.A., Mustard K.J., RA Kemp B.E., Sakamoto K., Steinberg G.R., Hardie D.G.; RT "The ancient drug salicylate directly activates AMP-activated protein RT kinase."; RL Science 336:918-922(2012). RN [26] RP DEPHOSPHORYLATION AT THR-172. RX PubMed=23088624; DOI=10.1042/BJ20121201; RA Chida T., Ando M., Matsuki T., Masu Y., Nagaura Y., RA Takano-Yamamoto T., Tamura S., Kobayashi T.; RT "N-Myristoylation is essential for protein phosphatases PPM1A and RT PPM1B to dephosphorylate their physiological substrates in cells."; RL Biochem. J. 449:741-749(2013). RN [27] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 6-279. RX PubMed=20124709; DOI=10.1107/S1744309109052543; RA Littler D.R., Walker J.R., Davis T., Wybenga-Groot L.E., RA Finerty P.J. Jr., Newman E., Mackenzie F., Dhe-Paganon S.; RT "A conserved mechanism of autoinhibition for the AMPK kinase domain: RT ATP-binding site and catalytic loop refolding as a means of RT regulation."; RL Acta Crystallogr. F 66:143-151(2010). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 6-279 OF MUTANT THR-172 IN RP COMPLEX WITH COMPOUND C, AND ENZYME REGULATION. RX PubMed=21543851; DOI=10.1107/S0907444911010201; RA Handa N., Takagi T., Saijo S., Kishishita S., Takaya D., Toyama M., RA Terada T., Shirouzu M., Suzuki A., Lee S., Yamauchi T., RA Okada-Iwabu M., Iwabu M., Kadowaki T., Minokoshi Y., Yokoyama S.; RT "Structural basis for compound C inhibition of the human AMP-activated RT protein kinase alpha2 subunit kinase domain."; RL Acta Crystallogr. D 67:480-487(2011). RN [29] RP VARIANTS [LARGE SCALE ANALYSIS] THR-371 AND GLY-523. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [30] RP VARIANTS [LARGE SCALE ANALYSIS] THR-371 AND GLN-407. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Catalytic subunit of AMP-activated protein kinase CC (AMPK), an energy sensor protein kinase that plays a key role in CC regulating cellular energy metabolism. In response to reduction of CC intracellular ATP levels, AMPK activates energy-producing pathways CC and inhibits energy-consuming processes: inhibits protein, CC carbohydrate and lipid biosynthesis, as well as cell growth and CC proliferation. AMPK acts via direct phosphorylation of metabolic CC enzymes, and by longer-term effects via phosphorylation of CC transcription regulators. Also acts as a regulator of cellular CC polarity by remodeling the actin cytoskeleton; probably by CC indirectly activating myosin. Regulates lipid synthesis by CC phosphorylating and inactivating lipid metabolic enzymes such as CC ACACA, ACACB, GYS1, HMGCR and LIPE; regulates fatty acid and CC cholesterol synthesis by phosphorylating acetyl-CoA carboxylase CC (ACACA and ACACB) and hormone-sensitive lipase (LIPE) enzymes, CC respectively. Regulates insulin-signaling and glycolysis by CC phosphorylating IRS1, PFKFB2 and PFKFB3. AMPK stimulates glucose CC uptake in muscle by increasing the translocation of the glucose CC transporter SLC2A4/GLUT4 to the plasma membrane, possibly by CC mediating phosphorylation of TBC1D4/AS160. Regulates transcription CC and chromatin structure by phosphorylating transcription CC regulators involved in energy metabolism such as CRTC2/TORC2, CC FOXO3, histone H2B, HDAC5, MEF2C, MLXIPL/ChREBP, EP300, HNF4A, CC p53/TP53, SREBF1, SREBF2 and PPARGC1A. Acts as a key regulator of CC glucose homeostasis in liver by phosphorylating CRTC2/TORC2, CC leading to CRTC2/TORC2 sequestration in the cytoplasm. In response CC to stress, phosphorylates 'Ser-36' of histone H2B (H2BS36ph), CC leading to promote transcription. Acts as a key regulator of cell CC growth and proliferation by phosphorylating TSC2, RPTOR and CC ATG1/ULK1: in response to nutrient limitation, negatively CC regulates the mTORC1 complex by phosphorylating RPTOR component of CC the mTORC1 complex and by phosphorylating and activating TSC2. In CC response to nutrient limitation, promotes autophagy by CC phosphorylating and activating ATG1/ULK1. AMPK also acts as a CC regulator of circadian rhythm by mediating phosphorylation of CC CRY1, leading to destabilize it. May regulate the Wnt signaling CC pathway by phosphorylating CTNNB1, leading to stabilize it. Also CC phosphorylates CFTR, EEF2K, KLC1, NOS3 and SLC12A1. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- CATALYTIC ACTIVITY: ATP + [hydroxymethylglutaryl-CoA reductase CC (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] CC phosphate. CC -!- CATALYTIC ACTIVITY: ATP + [acetyl-CoA carboxylase] = ADP + CC [acetyl-CoA carboxylase] phosphate. CC -!- COFACTOR: Magnesium (By similarity). CC -!- ENZYME REGULATION: Activated by phosphorylation on Thr-172. CC Binding of AMP to non-catalytic gamma subunit (PRKAG1, PRKAG2 or CC PRKAG3) results in allosteric activation, inducing phosphorylation CC on Thr-172. AMP-binding to gamma subunit also sustains activity by CC preventing dephosphorylation of Thr-172. ADP also stimulates Thr- CC 172 phosphorylation, without stimulating already phosphorylated CC AMPK. ATP promotes dephosphorylation of Thr-172, rendering the CC enzyme inactive. Under physiological conditions AMPK mainly exists CC in its inactive form in complex with ATP, which is much more CC abundant than AMP. AMPK is activated by antihyperglycemic drug CC metformin, a drug prescribed to patients with type 2 diabetes: in CC vivo, metformin seems to mainly inhibit liver gluconeogenesis. CC However, metformin can be used to activate AMPK in muscle and CC other cells in culture or ex vivo (PubMed:11602624). Selectively CC inhibited by compound C (6-[4-(2-Piperidin-1-yl-ethoxy)-phenyl)]- CC 3-pyridin-4-yl-pyyrazolo[1,5-a] pyrimidine. Activated by CC resveratrol, a natural polyphenol present in red wine, and S17834, CC a synthetic polyphenol. Salicylate/aspirin directly activates CC kinase activity, primarily by inhibiting Thr-172 CC dephosphorylation. CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit CC (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non- CC catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with CC FNIP1 and FNIP2. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus. Note=In CC response to stress, recruited by p53/TP53 to specific promoters. CC -!- DOMAIN: The AIS (autoinhibitory sequence) region shows some CC sequence similarity with the ubiquitin-associated domains and CC represses kinase activity. CC -!- PTM: Ubiquitinated (By similarity). CC -!- PTM: Phosphorylated at Thr-172 by STK11/LKB1 in complex with CC STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Also CC phosphorylated at Thr-172 by CAMKK2; triggered by a rise in CC intracellular calcium ions, without detectable changes in the CC AMP/ATP ratio. CAMKK1 can also phosphorylate Thr-172, but at much CC lower level. Dephosphorylated by protein phosphatase 2A and 2C CC (PP2A and PP2C). Phosphorylated by ULK1; leading to negatively CC regulate AMPK activity and suggesting the existence of a CC regulatory feedback loop between ULK1 and AMPK. Dephosphorylated CC by PPM1A and PPM1B at Thr-172 (mediated by STK11/LKB1). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. SNF1 subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U06454; AAA64745.1; -; mRNA. DR EMBL; AL035705; CAC17574.2; -; Genomic_DNA. DR EMBL; BC069680; AAH69680.1; -; mRNA. DR EMBL; BC069740; AAH69740.1; -; mRNA. DR EMBL; BC069823; AAH69823.1; -; mRNA. DR CCDS; CCDS605.1; -. DR PIR; S51025; S51025. DR RefSeq; NP_006243.2; NM_006252.3. DR UniGene; Hs.437039; -. DR PDB; 2H6D; X-ray; 1.85 A; A=6-279. DR PDB; 2LTU; NMR; -; A=282-339. DR PDB; 2YZA; X-ray; 3.02 A; A=6-279. DR PDB; 3AQV; X-ray; 2.08 A; A=6-279. DR PDB; 4CFE; X-ray; 3.02 A; A/C=1-552. DR PDB; 4CFF; X-ray; 3.92 A; A/C=1-552. DR PDBsum; 2H6D; -. DR PDBsum; 2LTU; -. DR PDBsum; 2YZA; -. DR PDBsum; 3AQV; -. DR PDBsum; 4CFE; -. DR PDBsum; 4CFF; -. DR ProteinModelPortal; P54646; -. DR SMR; P54646; 7-551. DR BioGrid; 111550; 45. DR IntAct; P54646; 34. DR MINT; MINT-2804161; -. DR STRING; 9606.ENSP00000360290; -. DR BindingDB; P54646; -. DR ChEMBL; CHEMBL3038455; -. DR GuidetoPHARMACOLOGY; 1542; -. DR PhosphoSite; P54646; -. DR DMDM; 20178276; -. DR MaxQB; P54646; -. DR PaxDb; P54646; -. DR PRIDE; P54646; -. DR DNASU; 5563; -. DR Ensembl; ENST00000371244; ENSP00000360290; ENSG00000162409. DR GeneID; 5563; -. DR KEGG; hsa:5563; -. DR UCSC; uc001cyk.4; human. DR CTD; 5563; -. DR GeneCards; GC01P057027; -. DR HGNC; HGNC:9377; PRKAA2. DR HPA; CAB013043; -. DR MIM; 600497; gene. DR neXtProt; NX_P54646; -. DR PharmGKB; PA33745; -. DR eggNOG; COG0515; -. DR HOGENOM; HOG000233016; -. DR HOVERGEN; HBG050432; -. DR InParanoid; P54646; -. DR KO; K07198; -. DR OMA; TMHIPPG; -. DR OrthoDB; EOG7RRF6K; -. DR PhylomeDB; P54646; -. DR TreeFam; TF314032; -. DR BRENDA; 2.7.11.1; 2681. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_11123; Membrane Trafficking. DR Reactome; REACT_200751; Organelle biogenesis and maintenance. DR SignaLink; P54646; -. DR EvolutionaryTrace; P54646; -. DR GeneWiki; PRKAA2; -. DR GenomeRNAi; 5563; -. DR NextBio; 21552; -. DR PRO; PR:P54646; -. DR Bgee; P54646; -. DR CleanEx; HS_PRKAA2; -. DR Genevestigator; P54646; -. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0050405; F:[acetyl-CoA carboxylase] kinase activity; IEA:UniProtKB-EC. DR GO; GO:0047322; F:[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004679; F:AMP-activated protein kinase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB. DR GO; GO:0035174; F:histone serine kinase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0006853; P:carnitine shuttle; TAS:Reactome. DR GO; GO:0007050; P:cell cycle arrest; TAS:Reactome. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB. DR GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB. DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0055089; P:fatty acid homeostasis; ISS:UniProtKB. DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0008610; P:lipid biosynthetic process; ISS:UniProtKB. DR GO; GO:0061024; P:membrane organization; TAS:Reactome. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB. DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB. DR GO; GO:0045821; P:positive regulation of glycolytic process; ISS:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB. DR GO; GO:0042304; P:regulation of fatty acid biosynthetic process; TAS:Reactome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006950; P:response to stress; ISS:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR InterPro; IPR028375; KA1/Ssp2_C. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR028783; PRKAA2. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24343:SF82; PTHR24343:SF82; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF103243; SSF103243; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Autophagy; Biological rhythms; KW Cholesterol biosynthesis; Cholesterol metabolism; Chromatin regulator; KW Complete proteome; Cytoplasm; Fatty acid biosynthesis; KW Fatty acid metabolism; Kinase; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Serine/threonine-protein kinase; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism; Transcription; Transcription regulation; KW Transferase; Ubl conjugation; Wnt signaling pathway. FT CHAIN 1 552 5'-AMP-activated protein kinase catalytic FT subunit alpha-2. FT /FTId=PRO_0000085594. FT DOMAIN 16 268 Protein kinase. FT NP_BIND 22 30 ATP (By similarity). FT REGION 291 376 AIS (By similarity). FT ACT_SITE 139 139 Proton acceptor (By similarity). FT BINDING 45 45 ATP (By similarity). FT MOD_RES 172 172 Phosphothreonine; by LKB1 and CaMKK2. FT MOD_RES 258 258 Phosphothreonine (By similarity). FT MOD_RES 377 377 Phosphoserine. FT MOD_RES 491 491 Phosphoserine (By similarity). FT VARIANT 371 371 P -> T (in breast cancer samples; FT infiltrating ductal carcinoma; somatic FT mutation). FT /FTId=VAR_035623. FT VARIANT 407 407 R -> Q (in a gastric adenocarcinoma FT sample; somatic mutation). FT /FTId=VAR_040355. FT VARIANT 523 523 S -> G (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035624. FT MUTAGEN 172 172 T->D: Phosphomimetic mutant. FT CONFLICT 180 180 A -> T (in Ref. 1; AAA64745). FT CONFLICT 271 271 D -> G (in Ref. 1; AAA64745). FT CONFLICT 403 404 HL -> RQ (in Ref. 1; AAA64745). FT STRAND 16 24 FT STRAND 26 35 FT TURN 36 38 FT STRAND 41 48 FT HELIX 49 54 FT HELIX 58 69 FT STRAND 79 84 FT STRAND 86 94 FT HELIX 101 108 FT HELIX 113 133 FT HELIX 142 144 FT STRAND 145 147 FT STRAND 153 155 FT HELIX 160 162 FT HELIX 183 185 FT HELIX 192 209 FT HELIX 219 228 FT HELIX 239 248 FT HELIX 253 255 FT HELIX 259 264 FT HELIX 266 269 FT HELIX 274 276 FT TURN 284 286 FT HELIX 291 294 FT HELIX 304 312 FT HELIX 322 335 FT HELIX 338 341 FT STRAND 403 408 FT HELIX 412 424 FT TURN 425 427 FT STRAND 429 434 FT STRAND 437 443 FT TURN 445 447 FT STRAND 450 460 FT TURN 461 463 FT STRAND 464 471 FT HELIX 535 548 SQ SEQUENCE 552 AA; 62320 MW; C46AAFC1D5104975 CRC64; MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEMEARRLF QQILSAVDYC HRHMVVHRDL KPENVLLDAH MNAKIADFGL SNMMSDGEFL RTSCGSPNYA APEVISGRLY AGPEVDIWSC GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPEYLNRS VATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS FMDDSAMHIP PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KPYDIMAEVY RAMKQLDFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DNRSYLLDFK SIDDEVVEQR SGSSTPQRSC SAAGLHRPRS SFDSTTAESH SLSGSLTGSL TGSTLSSVSP RLGSHTMDFF EMCASLITTL AR // ID AATF_HUMAN Reviewed; 560 AA. AC Q9NY61; A6NCJ6; B3KQ26; Q9P0A4; Q9UNX5; DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-JUL-2014, entry version 110. DE RecName: Full=Protein AATF; DE AltName: Full=Apoptosis-antagonizing transcription factor; DE AltName: Full=Rb-binding protein Che-1; GN Name=AATF; Synonyms=CHE1, DED; ORFNames=HSPC277; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=11027528; DOI=10.1006/bbrc.2000.3480; RA Lindfors K., Halttunen T., Huotari P., Nupponen N., Vihinen M., RA Visakorpi T., Maki M., Kainulainen H.; RT "Identification of novel transcription factor-like gene from human RT intestinal cells."; RL Biochem. Biophys. Res. Commun. 276:660-666(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH POLR2J AND RB1, AND RP TISSUE SPECIFICITY. RC TISSUE=Skeletal muscle; RX PubMed=10783144; RA Fanciulli M., Bruno T., Di Padova M., De Angelis R., Iezzi S., RA Iacobini C., Floridi A., Passananti C.; RT "Identification of a novel partner of RNA polymerase II subunit 11, RT Che-1, which interacts with and affects the growth suppression RT function of Rb."; RL FASEB J. 14:904-912(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 361-560. RC TISSUE=Umbilical cord blood; RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.; RT "Human partial CDS from CD34+ stem cells."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, PHOSPHORYLATION AT THE G1/S TRANSITION, AND INTERACTION WITH RP RB1; RBL1 AND RBL2. RX PubMed=12450794; DOI=10.1016/S1535-6108(02)00182-4; RA Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M., RA Corbi N., Libri V., Benassi B., Mattei E., Chersi A., Soddu S., RA Floridi A., Passananti C., Fanciulli M.; RT "Che-1 affects cell growth by interfering with the recruitment of RT HDAC1 by Rb."; RL Cancer Cell 2:387-399(2002). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.E02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [10] RP FUNCTION, AND INTERACTION WITH SP1. RX PubMed=12847090; DOI=10.1074/jbc.M306694200; RA Di Padova M., Bruno T., De Nicola F., Iezzi S., D'Angelo C., Gallo R., RA Nicosia D., Corbi N., Biroccio A., Floridi A., Passananti C., RA Fanciulli M.; RT "Che-1 arrests human colon carcinoma cell proliferation by displacing RT HDAC1 from the p21WAF1/CIP1 promoter."; RL J. Biol. Chem. 278:36496-36504(2003). RN [11] RP INTERACTION WITH MAPT. RX PubMed=14697667; DOI=10.1016/j.mcn.2003.08.002; RA Barbato C., Corbi N., Canu N., Fanciulli M., Serafino A., Ciotti M., RA Libri V., Bruno T., Amadoro G., De Angelis R., Calissano P., RA Passananti C.; RT "Rb binding protein Che-1 interacts with Tau in cerebellar granule RT neurons. Modulation during neuronal apoptosis."; RL Mol. Cell. Neurosci. 24:1038-1050(2003). RN [12] RP FUNCTION, AND INTERACTION WITH PAWR. RX PubMed=14627703; DOI=10.1074/jbc.M309811200; RA Guo Q., Xie J.; RT "AATF inhibits aberrant production of amyloid beta peptide 1-42 by RT interacting directly with Par-4."; RL J. Biol. Chem. 279:4596-4603(2004). RN [13] RP FUNCTION. RX PubMed=15207272; DOI=10.1016/j.nbd.2004.02.003; RA Xie J., Guo Q.; RT "AATF protects neural cells against oxidative damage induced by RT amyloid beta-peptide."; RL Neurobiol. Dis. 16:150-157(2004). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND RP SER-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316; SER-320 AND RP SER-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-316; SER-320 RP AND SER-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-316; SER-320 RP AND SER-321, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). CC -!- FUNCTION: May function as a general inhibitor of the histone CC deacetylase HDAC1. Binding to the pocket region of RB1 may CC displace HDAC1 from RB1/E2F complexes, leading to activation of CC E2F target genes and cell cycle progression. Conversely, CC displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads CC to increased expression of this CDK inhibitor and blocks cell CC cycle progression. Also antagonizes PAWR mediated induction of CC aberrant amyloid peptide production in Alzheimer disease CC (presenile and senile dementia), although the molecular basis for CC this phenomenon has not been described to date. CC -!- SUBUNIT: Binds PAWR, POLR2J, RB1/RB, RBL1/P107, RBL2/P130, and CC SP1. May also bind MAPT. CC -!- INTERACTION: CC Q13315:ATM; NbExp=3; IntAct=EBI-372428, EBI-495465; CC O96017:CHEK2; NbExp=4; IntAct=EBI-372428, EBI-1180783; CC Q6ZWQ9:Myl12a (xeno); NbExp=3; IntAct=EBI-372428, EBI-8034418; CC Q04206:RELA; NbExp=3; IntAct=EBI-372428, EBI-73886; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at high CC levels in brain, heart, kidney, placenta and thymus. CC -!- PTM: Hyperphosphorylated during the G1/S phase transition. CC -!- SIMILARITY: Belongs to the AATF family. CC -!- SEQUENCE CAUTION: CC Sequence=AAD52016.1; Type=Frameshift; Positions=355, 365, 487, 498, 503; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/AATFID534ch17q11.html"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ249940; CAB57451.2; -; mRNA. DR EMBL; AF083208; AAD52016.1; ALT_FRAME; mRNA. DR EMBL; AK057229; BAG51888.1; -; mRNA. DR EMBL; AC003103; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471199; EAW57575.1; -; Genomic_DNA. DR EMBL; BC000591; AAH00591.1; -; mRNA. DR EMBL; AF161395; AAF28955.1; -; mRNA. DR CCDS; CCDS32632.1; -. DR RefSeq; NP_036270.1; NM_012138.3. DR UniGene; Hs.195740; -. DR ProteinModelPortal; Q9NY61; -. DR BioGrid; 117743; 33. DR IntAct; Q9NY61; 16. DR MINT; MINT-131397; -. DR STRING; 9606.ENSP00000225402; -. DR PhosphoSite; Q9NY61; -. DR DMDM; 71152211; -. DR SWISS-2DPAGE; Q9NY61; -. DR MaxQB; Q9NY61; -. DR PaxDb; Q9NY61; -. DR PRIDE; Q9NY61; -. DR DNASU; 26574; -. DR Ensembl; ENST00000225402; ENSP00000225402; ENSG00000108270. DR GeneID; 26574; -. DR KEGG; hsa:26574; -. DR UCSC; uc002hni.3; human. DR CTD; 26574; -. DR GeneCards; GC17P035306; -. DR HGNC; HGNC:19235; AATF. DR HPA; HPA004940; -. DR MIM; 608463; gene. DR neXtProt; NX_Q9NY61; -. DR PharmGKB; PA128395780; -. DR eggNOG; NOG270454; -. DR HOGENOM; HOG000007555; -. DR HOVERGEN; HBG080805; -. DR InParanoid; Q9NY61; -. DR KO; K14782; -. DR OMA; QLHPPDE; -. DR OrthoDB; EOG7VDXQ2; -. DR PhylomeDB; Q9NY61; -. DR TreeFam; TF324341; -. DR Reactome; REACT_111102; Signal Transduction. DR ChiTaRS; AATF; human. DR GeneWiki; Apoptosis-antagonizing_transcription_factor; -. DR GenomeRNAi; 26574; -. DR NextBio; 48910; -. DR PRO; PR:Q9NY61; -. DR ArrayExpress; Q9NY61; -. DR Bgee; Q9NY61; -. DR CleanEx; HS_AATF; -. DR Genevestigator; Q9NY61; -. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043522; F:leucine zipper domain binding; IPI:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:UniProtKB. DR GO; GO:0040016; P:embryonic cleavage; IEA:Ensembl. DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IEA:Ensembl. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IDA:UniProtKB. DR GO; GO:0032929; P:negative regulation of superoxide anion generation; IDA:UniProtKB. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl. DR GO; GO:0042254; P:ribosome biogenesis; IEA:Ensembl. DR InterPro; IPR025160; AATF. DR InterPro; IPR012617; AATF_C. DR Pfam; PF13339; AATF-Che1; 1. DR Pfam; PF08164; TRAUB; 1. PE 1: Evidence at protein level; KW Acetylation; Complete proteome; Nucleus; Phosphoprotein; KW Reference proteome. FT INIT_MET 1 1 Removed. FT CHAIN 2 560 Protein AATF. FT /FTId=PRO_0000056616. FT REGION 273 315 POLR2J binding. FT REGION 316 372 RB1 binding. FT REGION 373 472 RB1 and SP1 binding. FT COMPBIAS 96 195 Glu-rich. FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 203 203 Phosphoserine. FT MOD_RES 316 316 Phosphoserine. FT MOD_RES 320 320 Phosphoserine. FT MOD_RES 321 321 Phosphoserine. FT CONFLICT 2 3 AG -> GR (in Ref. 2; AAD52016). FT CONFLICT 4 5 Missing (in Ref. 2; AAD52016). FT CONFLICT 139 139 S -> T (in Ref. 2; AAD52016). FT CONFLICT 262 262 L -> V (in Ref. 2; AAD52016). FT CONFLICT 272 272 S -> A (in Ref. 2; AAD52016). FT CONFLICT 306 306 L -> V (in Ref. 2; AAD52016). FT CONFLICT 402 402 D -> C (in Ref. 2; AAD52016). SQ SEQUENCE 560 AA; 63133 MW; EC493EF3B4C3A199 CRC64; MAGPQPLALQ LEQLLNPRPS EADPEADPEE ATAARVIDRF DEGEDGEGDF LVVGSIRKLA SASLLDTDKR YCGKTTSRKA WNEDHWEQTL PGSSDEEISD EEGSGDEDSE GLGLEEYDED DLGAAEEQEC GDHRESKKSR SHSAKTPGFS VQSISDFEKF TKGMDDLGSS EEEEDEESGM EEGDDAEDSQ GESEEDRAGD RNSEDDGVVM TFSSVKVSEE VEKGRAVKNQ IALWDQLLEG RIKLQKALLT TNQLPQPDVF PLFKDKGGPE FSSALKNSHK ALKALLRSLV GLQEELLFQY PDTRYLVDGT KPNAGSEEIS SEDDELVEEK KQQRRRVPAK RKLEMEDYPS FMAKRFADFT VYRNRTLQKW HDKTKLASGK LGKGFGAFER SILTQIDHIL MDKERLLRRT QTKRSVYRVL GKPEPAAQPV PESLPGEPEI LPQAPANAHL KDLDEEIFDD DDFYHQLLRE LIERKTSSLD PNDQVAMGRQ WLAIQKLRSK IHKKVDRKAS KGRKLRFHVL SKLLSFMAPI DHTTMNDDAR TELYRSLFGQ LHPPDEGHGD // ID ABC3A_HUMAN Reviewed; 199 AA. AC P31941; A0AVM1; Q12807; Q5JZ93; Q9UH18; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 3. DT 09-JUL-2014, entry version 128. DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3A; DE Short=A3A; DE EC=3.5.4.-; DE AltName: Full=Phorbolin-1; GN Name=APOBEC3A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-27; 31-35; 53-60; RP 112-123; 129-137 AND 192-198, AND FUNCTION. RC TISSUE=Keratinocyte; RX PubMed=10469298; DOI=10.1046/j.1523-1747.1999.00682.x; RA Madsen P.P., Anant S., Rasmussen H.H., Gromov P., Vorum H., RA Dumanski J.P., Tommerup N., Collins J.E., Wright C.L., Dunham I., RA Macginnitie A.J., Davidson N.O., Celis J.E.; RT "Psoriasis upregulated phorbolin-1 shares structural but not RT functional similarity to the mRNA-editing protein apobec-1."; RL J. Invest. Dermatol. 113:162-169(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 53-60; 112-121 AND 129-137. RC TISSUE=Keratinocyte; RX PubMed=1286667; DOI=10.1002/elps.11501301199; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). RN [6] RP GENE FAMILY ORGANIZATION, AND TISSUE SPECIFICITY. RX PubMed=11863358; DOI=10.1006/geno.2002.6718; RA Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., RA Navaratnam N.; RT "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on RT chromosome 22."; RL Genomics 79:285-296(2002). RN [7] RP REVIEW ON APOBEC FAMILIES. RX PubMed=12683974; DOI=10.1016/S0168-9525(03)00054-4; RA Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.; RT "Messenger RNA editing in mammals: new members of the APOBEC family RT seeking roles in the family business."; RL Trends Genet. 19:207-216(2003). RN [8] RP FUNCTION IN HOST DEFENSE. RX PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4; RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., RA Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.; RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif."; RL Cell 114:21-31(2003). RN [9] RP FUNCTION IN HOST DEFENSE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, RP MUTAGENESIS OF HIS-70; GLU-72 AND CYS-106, AND TISSUE SPECIFICITY. RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031; RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., RA Landau N.R., Weitzman M.D.; RT "APOBEC3A is a potent inhibitor of adeno-associated virus and RT retrotransposons."; RL Curr. Biol. 16:480-485(2006). RN [10] RP REVIEW. RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350; RA Chiu Y.L., Greene W.C.; RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing RT exogenous retroviruses and endogenous retroelements."; RL Annu. Rev. Immunol. 26:317-353(2008). RN [11] RP FUNCTION IN AAV INHIBITION, AND SUBCELLULAR LOCATION. RX PubMed=19461882; DOI=10.1371/journal.ppat.1000439; RA Narvaiza I., Linfesty D.C., Greener B.N., Hakata Y., Pintel D.J., RA Logue E., Landau N.R., Weitzman M.D.; RT "Deaminase-independent inhibition of parvoviruses by the APOBEC3A RT cytidine deaminase."; RL PLoS Pathog. 5:E1000439-E1000439(2009). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND ALTERNATIVE SPLICING RP (ISOFORMS 1 AND 2). RX PubMed=20615867; DOI=10.1074/jbc.M110.102822; RA Thielen B.K., McNevin J.P., McElrath M.J., Hunt B.V., Klein K.C., RA Lingappa J.R.; RT "Innate immune signaling induces high levels of TC-specific deaminase RT activity in primary monocyte-derived cells through expression of RT APOBEC3A isoforms."; RL J. Biol. Chem. 285:27753-27766(2010). RN [13] RP FUNCTION IN FOREIGN DNA CLEARANCE, CATALYTIC ACTIVITY, TISSUE RP SPECIFICITY, AND INDUCTION. RX PubMed=20062055; DOI=10.1038/nsmb.1744; RA Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.; RT "APOBEC3 proteins mediate the clearance of foreign DNA from human RT cells."; RL Nat. Struct. Mol. Biol. 17:222-229(2010). RN [14] RP TISSUE SPECIFICITY. RX PubMed=20308164; DOI=10.1093/nar/gkq174; RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L., RA Harris R.S.; RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in RT lymphocytes and tissues: implications for HIV-1 restriction."; RL Nucleic Acids Res. 38:4274-4284(2010). RN [15] RP FUNCTION IN DNA DEMETHYLATION. RX PubMed=21496894; DOI=10.1016/j.cell.2011.03.022; RA Guo J.U., Su Y., Zhong C., Ming G.L., Song H.; RT "Hydroxylation of 5-methylcytosine by TET1 promotes active DNA RT demethylation in the adult brain."; RL Cell 145:423-434(2011). RN [16] RP FUNCTION. RX PubMed=21460793; DOI=10.1038/embor.2011.46; RA Landry S., Narvaiza I., Linfesty D.C., Weitzman M.D.; RT "APOBEC3A can activate the DNA damage response and cause cell-cycle RT arrest."; RL EMBO Rep. 12:444-450(2011). RN [17] RP FUNCTION IN HOST DEFENSE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, RP AND MUTAGENESIS OF ARG-28; HIS-29; LYS-30; ASN-57; LYS-60; ARG-69; RP GLU-72; TRP-98; ARG-128; TYR-130; ASP-131; ASP-133 AND TYR-136. RX PubMed=21123384; DOI=10.1128/JVI.01651-10; RA Bulliard Y., Narvaiza I., Bertero A., Peddi S., Roehrig U.F., RA Ortiz M., Zoete V., Castro-Diaz N., Turelli P., Telenti A., RA Michielin O., Weitzman M.D., Trono D.; RT "Structure-function analyses point to a polynucleotide-accommodating RT groove essential for APOBEC3A restriction activities."; RL J. Virol. 85:1765-1776(2011). RN [18] RP SUBCELLULAR LOCATION. RX PubMed=21835787; DOI=10.1128/JVI.05238-11; RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L., RA Brown W.L., Harris R.S.; RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H RT demonstrate a conserved capacity to restrict Vif-deficient HIV-1."; RL J. Virol. 85:11220-11234(2011). RN [19] RP FUNCTION. RX PubMed=21368204; DOI=10.1073/pnas.1009687108; RA Suspene R., Aynaud M.M., Guetard D., Henry M., Eckhoff G., Marchio A., RA Pineau P., Dejean A., Vartanian J.P., Wain-Hobson S.; RT "Somatic hypermutation of human mitochondrial and nuclear DNA by RT APOBEC3 cytidine deaminases, a pathway for DNA catabolism."; RL Proc. Natl. Acad. Sci. U.S.A. 108:4858-4863(2011). RN [20] RP REVIEW. RA Love R.; RT "Cytosine deaminases APOBEC3A, APOBEC3C, and APOBEC3H: Current RT understanding of their functional roles."; RL Student Perspec. Contemp. Virol. 0:0-0(2011). RN [21] RP REVIEW. RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275; RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.; RT "Retroelements versus APOBEC3 family members: No great escape from the RT magnificent seven."; RL Front. Microbiol. 3:275-275(2012). RN [22] RP FUNCTION. RX PubMed=22896697; DOI=10.1074/jbc.M112.385161; RA Carpenter M.A., Li M., Rathore A., Lackey L., Law E.K., Land A.M., RA Leonard B., Shandilya S.M., Bohn M.F., Schiffer C.A., Brown W.L., RA Harris R.S.; RT "Methylcytosine and normal cytosine deamination by the foreign DNA RT restriction enzyme APOBEC3A."; RL J. Biol. Chem. 287:34801-34808(2012). RN [23] RP INTERACTION WITH TRIB3, AND SUBCELLULAR LOCATION. RX PubMed=22977230; DOI=10.1074/jbc.M112.372722; RA Aynaud M.M., Suspene R., Vidalain P.O., Mussil B., Guetard D., RA Tangy F., Wain-Hobson S., Vartanian J.P.; RT "Human Tribbles 3 protects nuclear DNA from cytidine deamination by RT APOBEC3A."; RL J. Biol. Chem. 287:39182-39192(2012). RN [24] RP FUNCTION IN HTLV-1 RESTRICTION. RX PubMed=22457529; DOI=10.1128/JVI.06570-11; RA Ooms M., Krikoni A., Kress A.K., Simon V., Muenk C.; RT "APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T- RT lymphotropic virus type 1."; RL J. Virol. 86:6097-6108(2012). RN [25] RP INTERACTION WITH AGO2. RX PubMed=22915799; DOI=10.1128/JVI.00595-12; RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.; RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by RT P bodies."; RL J. Virol. 86:11712-11724(2012). RN [26] RP REVIEW. RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004; RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.; RT "Functions and regulation of the APOBEC family of proteins."; RL Semin. Cell Dev. Biol. 23:258-268(2012). CC -!- FUNCTION: DNA deaminase (cytidine deaminase) with restriction CC activity against viruses, foreign DNA and mobility of CC retrotransposons. Exhibits antiviral activity against adeno- CC associated virus (AAV) and human T-cell leukemia virus type 1 CC (HTLV-1) and may inhibit the mobility of LTR and non-LTR CC retrotransposons. Selectively targets single-stranded DNA and can CC deaminate both methylcytosine and cytosine in foreign DNA. Can CC induce somatic hypermutation in the nuclear and mitochondrial DNA. CC May also play a role in the epigenetic regulation of gene CC expression through the process of active DNA demethylation. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- COFACTOR: Zinc (By similarity). CC -!- SUBUNIT: Interacts with AGO2. Interacts with TRIB3 (via N- CC terminus). CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; Synonyms=Phorbolin-1; CC IsoId=P31941-1; Sequence=Displayed; CC Note=Enzymatically active; CC Name=2; CC IsoId=P31941-2; Sequence=VSP_041723; CC Note=Enzymatically active; CC -!- TISSUE SPECIFICITY: Expressed in peripheral leukocytes with higher CC expression in CD14-positive phagocytic cells. Highly expressed in CC keratinocytes and in periphery blood monocytes. Also detected in CC non-lymphoid tissues including lung and adipose tissues. Found at CC high levels in colorectal adenocarcinoma, Burkitt's lymphoma and CC chronic myelogenous leukemia. CC -!- INDUCTION: Up-regulated by interferon and CpG single-stranded DNA CC (at protein level). CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes CC found in a cluster, thought to result from gene duplication, on CC chromosome 22. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. CC -!- SIMILARITY: Contains 1 CMP/dCMP deaminase zinc-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U03891; AAA03706.2; -; mRNA. DR EMBL; CR456393; CAG30279.1; -; mRNA. DR EMBL; AL022318; CAI17897.1; -; Genomic_DNA. DR EMBL; BC126416; AAI26417.1; -; mRNA. DR CCDS; CCDS13981.1; -. [P31941-1] DR PIR; G01233; G01233. DR RefSeq; NP_001180218.1; NM_001193289.1. [P31941-1] DR RefSeq; NP_663745.1; NM_145699.3. [P31941-1] DR RefSeq; XP_005277016.1; XM_005276959.1. [P31941-1] DR RefSeq; XP_005277017.1; XM_005276960.1. [P31941-1] DR UniGene; Hs.226307; -. DR PDB; 2M65; NMR; -; A=1-199. DR PDBsum; 2M65; -. DR ProteinModelPortal; P31941; -. DR SMR; P31941; 1-199. DR BioGrid; 128318; 1. DR STRING; 9606.ENSP00000249116; -. DR BindingDB; P31941; -. DR ChEMBL; CHEMBL1741179; -. DR PhosphoSite; P31941; -. DR DMDM; 12644206; -. DR PaxDb; P31941; -. DR PRIDE; P31941; -. DR DNASU; 200315; -. DR Ensembl; ENST00000249116; ENSP00000249116; ENSG00000128383. [P31941-1] DR Ensembl; ENST00000402255; ENSP00000384359; ENSG00000128383. [P31941-1] DR Ensembl; ENST00000570508; ENSP00000461288; ENSG00000262156. [P31941-1] DR GeneID; 100913187; -. DR GeneID; 200315; -. DR KEGG; hsa:100913187; -. DR KEGG; hsa:200315; -. DR UCSC; uc003awn.2; human. [P31941-1] DR CTD; 100913187; -. DR CTD; 200315; -. DR GeneCards; GC22P039348; -. DR HGNC; HGNC:17343; APOBEC3A. DR HPA; HPA043237; -. DR MIM; 607109; gene. DR neXtProt; NX_P31941; -. DR PharmGKB; PA24891; -. DR eggNOG; NOG293254; -. DR HOGENOM; HOG000033754; -. DR HOVERGEN; HBG050434; -. DR InParanoid; P31941; -. DR KO; K01500; -. DR OMA; LHNQAKN; -. DR OrthoDB; EOG71CFNW; -. DR PhylomeDB; P31941; -. DR TreeFam; TF331356; -. DR NextBio; 89887; -. DR PRO; PR:P31941; -. DR Bgee; P31941; -. DR CleanEx; HS_APOBEC3A; -. DR Genevestigator; P31941; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0004126; F:cytidine deaminase activity; IDA:UniProtKB. DR GO; GO:0047844; F:deoxycytidine deaminase activity; IMP:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB. DR GO; GO:0044356; P:clearance of foreign intracellular DNA by conversion of DNA cytidine to uridine; IDA:UniProtKB. DR GO; GO:0009972; P:cytidine deamination; IDA:GOC. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB. DR GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB. DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB. DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR007904; APOBEC_C. DR InterPro; IPR016193; Cytidine_deaminase-like. DR Pfam; PF05240; APOBEC_C; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Antiviral defense; KW Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; KW Immunity; Innate immunity; Metal-binding; Nucleus; Polymorphism; KW Reference proteome; Zinc. FT CHAIN 1 199 DNA dC->dU-editing enzyme APOBEC-3A. FT /FTId=PRO_0000171752. FT DOMAIN 70 106 CMP/dCMP deaminase zinc-binding. FT ACT_SITE 72 72 Proton donor (By similarity). FT METAL 70 70 Zinc; catalytic (By similarity). FT METAL 101 101 Zinc; catalytic (By similarity). FT METAL 106 106 Zinc; catalytic (By similarity). FT VAR_SEQ 1 12 Missing (in isoform 2). FT /FTId=VSP_041723. FT VARIANT 19 19 T -> A (in dbSNP:rs17000556). FT /FTId=VAR_048721. FT MUTAGEN 28 28 R->E: No effect on deaminase activity FT despite an altered restriction activity FT towards genetic invaders. FT MUTAGEN 29 29 H->A: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 30 30 K->F: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 57 57 N->A: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 60 60 K->A: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 69 69 R->A: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 70 70 H->R: Altered deaminase activity. FT MUTAGEN 72 72 E->Q: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 98 98 W->L: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 106 106 C->S: Altered deaminase activity. FT MUTAGEN 128 128 R->A: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 130 130 Y->A: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 131 131 D->N: No effect on deaminase activity FT despite an altered restriction activity FT towards genetic invaders. FT MUTAGEN 133 133 D->N: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT MUTAGEN 136 136 Y->A: Altered deaminase activity and FT restriction activity towards genetic FT invaders. FT HELIX 15 21 FT STRAND 27 29 FT STRAND 32 41 FT STRAND 44 47 FT STRAND 53 56 FT TURN 62 65 FT HELIX 71 76 FT HELIX 79 82 FT STRAND 88 98 FT TURN 103 105 FT HELIX 106 117 FT STRAND 120 128 FT HELIX 136 144 FT STRAND 149 152 FT HELIX 155 165 FT HELIX 179 194 SQ SEQUENCE 199 AA; 23012 MW; 42E99E0D7DF7AA14 CRC64; MEASPASGPR HLMDPHIFTS NFNNGIGRHK TYLCYEVERL DNGTSVKMDQ HRGFLHNQAK NLLCGFYGRH AELRFLDLVP SLQLDPAQIY RVTWFISWSP CFSWGCAGEV RAFLQENTHV RLRIFAARIY DYDPLYKEAL QMLRDAGAQV SIMTYDEFKH CWDTFVDHQG CPFQPWDGLD EHSQALSGRL RAILQNQGN // ID ABC3B_HUMAN Reviewed; 382 AA. AC Q9UH17; B0QYD2; O95618; Q20WL1; Q5IFJ4; Q7Z2N3; Q7Z6D6; Q9UE74; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 09-JUL-2014, entry version 118. DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3B; DE Short=A3B; DE EC=3.5.4.-; DE AltName: Full=Phorbolin-1-related protein; DE AltName: Full=Phorbolin-2/3; GN Name=APOBEC3B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LYS-146, AND RP INDUCTION. RC TISSUE=Keratinocyte; RX PubMed=10469298; DOI=10.1046/j.1523-1747.1999.00682.x; RA Madsen P.P., Anant S., Rasmussen H.H., Gromov P., Vorum H., RA Dumanski J.P., Tommerup N., Collins J.E., Wright C.L., Dunham I., RA Macginnitie A.J., Davidson N.O., Celis J.E.; RT "Psoriasis upregulated phorbolin-1 shares structural but not RT functional similarity to the mRNA-editing protein apobec-1."; RL J. Invest. Dermatol. 113:162-169(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RX PubMed=16060832; DOI=10.1089/aid.2005.21.611; RA Rose K.M., Marin M., Kozak S.L., Kabat D.; RT "Regulated production and anti-HIV type 1 activities of cytidine RT deaminases APOBEC3B, 3F, and 3G."; RL AIDS Res. Hum. Retroviruses 21:611-619(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS RP GLU-62 AND LYS-146. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP LYS-146. RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, RNA-BINDING, RP ZINC-BINDING, AND INTERACTION WITH APOBEC3G. RX PubMed=11863358; DOI=10.1006/geno.2002.6718; RA Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., RA Navaratnam N.; RT "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on RT chromosome 22."; RL Genomics 79:285-296(2002). RN [7] RP REVIEW ON APOBEC FAMILIES. RX PubMed=12683974; DOI=10.1016/S0168-9525(03)00054-4; RA Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.; RT "Messenger RNA editing in mammals: new members of the APOBEC family RT seeking roles in the family business."; RL Trends Genet. 19:207-216(2003). RN [8] RP FUNCTION IN HIV-1 INFECTIVITY. RX PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4; RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., RA Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.; RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif."; RL Cell 114:21-31(2003). RN [9] RP FUNCTION IN SIV RESTRICTION. RX PubMed=15466872; DOI=10.1074/jbc.M408802200; RA Yu Q., Chen D., Koenig R., Mariani R., Unutmaz D., Landau N.R.; RT "APOBEC3B and APOBEC3C are potent inhibitors of simian RT immunodeficiency virus replication."; RL J. Biol. Chem. 279:53379-53386(2004). RN [10] RP FUNCTION IN RETROTRANSPOSITION. RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031; RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., RA Landau N.R., Weitzman M.D.; RT "APOBEC3A is a potent inhibitor of adeno-associated virus and RT retrotransposons."; RL Curr. Biol. 16:480-485(2006). RN [11] RP DOMAIN CMP/DCMP DEAMINASE ZINC-BINDING. RX PubMed=17020885; DOI=10.1074/jbc.M604980200; RA Hakata Y., Landau N.R.; RT "Reversed functional organization of mouse and human APOBEC3 cytidine RT deaminase domains."; RL J. Biol. Chem. 281:36624-36631(2006). RN [12] RP SUBCELLULAR LOCATION. RX PubMed=16699599; DOI=10.1371/journal.ppat.0020041; RA Wichroski M.J., Robb G.B., Rana T.M.; RT "Human retroviral host restriction factors APOBEC3G and APOBEC3F RT localize to mRNA processing bodies."; RL PLoS Pathog. 2:E41-E41(2006). RN [13] RP REVIEW. RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350; RA Chiu Y.L., Greene W.C.; RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing RT exogenous retroviruses and endogenous retroelements."; RL Annu. Rev. Immunol. 26:317-353(2008). RN [14] RP REVIEW ON FUNCTION IN HBV RESTRICTION. RX PubMed=18448976; DOI=10.1097/QCO.0b013e3282fe1bb2; RA Bonvin M., Greeve J.; RT "Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine RT deaminases as effectors in innate immunity against the hepatitis B RT virus."; RL Curr. Opin. Infect. Dis. 21:298-303(2008). RN [15] RP SUBCELLULAR LOCATION. RX PubMed=18667511; DOI=10.1128/JVI.02471-07; RA Stenglein M.D., Matsuo H., Harris R.S.; RT "Two regions within the amino-terminal half of APOBEC3G cooperate to RT determine cytoplasmic localization."; RL J. Virol. 82:9591-9599(2008). RN [16] RP TISSUE SPECIFICITY. RX PubMed=20308164; DOI=10.1093/nar/gkq174; RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L., RA Harris R.S.; RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in RT lymphocytes and tissues: implications for HIV-1 restriction."; RL Nucleic Acids Res. 38:4274-4284(2010). RN [17] RP FUNCTION IN RETROTRANSPOSITION. RX PubMed=20062055; DOI=10.1038/nsmb.1744; RA Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.; RT "APOBEC3 proteins mediate the clearance of foreign DNA from human RT cells."; RL Nat. Struct. Mol. Biol. 17:222-229(2010). RN [18] RP SUBCELLULAR LOCATION. RX PubMed=21835787; DOI=10.1128/JVI.05238-11; RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L., RA Brown W.L., Harris R.S.; RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H RT demonstrate a conserved capacity to restrict Vif-deficient HIV-1."; RL J. Virol. 85:11220-11234(2011). RN [19] RP REVIEW. RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275; RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.; RT "Retroelements versus APOBEC3 family members: No great escape from the RT magnificent seven."; RL Front. Microbiol. 3:275-275(2012). RN [20] RP FUNCTION IN HTLV-1 RESTRICTION. RX PubMed=22457529; DOI=10.1128/JVI.06570-11; RA Ooms M., Krikoni A., Kress A.K., Simon V., Muenk C.; RT "APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T- RT lymphotropic virus type 1."; RL J. Virol. 86:6097-6108(2012). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=22915799; DOI=10.1128/JVI.00595-12; RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.; RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by RT P bodies."; RL J. Virol. 86:11712-11724(2012). RN [22] RP REVIEW. RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004; RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.; RT "Functions and regulation of the APOBEC family of proteins."; RL Semin. Cell Dev. Biol. 23:258-268(2012). CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an CC inhibitor of retrovirus replication and retrotransposon mobility CC via deaminase-dependent and -independent mechanisms. After the CC penetration of retroviral nucleocapsids into target cells of CC infection and the initiation of reverse transcription, it can CC induce the conversion of cytosine to uracil in the minus-sense CC single-strand viral DNA, leading to G-to-A hypermutations in the CC subsequent plus-strand viral DNA. The resultant detrimental levels CC of mutations in the proviral genome, along with a deamination- CC independent mechanism that works prior to the proviral CC integration, together exert efficient antiretroviral effects in CC infected target cells. Selectively targets single-stranded DNA and CC does not deaminate double-stranded DNA or single-or double- CC stranded RNA. Exhibits antiviral activity against simian CC immunodeficiency virus (SIV), hepatitis B virus (HBV) and human T- CC cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility CC of LTR and non-LTR retrotransposons. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- COFACTOR: Zinc. CC -!- SUBUNIT: Homodimer. Interacts with APOBEC3G. Does not interact CC with APOBEC1. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9UH17-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UH17-2; Sequence=VSP_009802; CC Note=May be due to a competing donor splice site; CC Name=3; CC IsoId=Q9UH17-3; Sequence=VSP_044900; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed at high and moderate levels in CC peripheral blood leukocytes, spleen, testes, heart, thymus, CC prostate and ovary. Also expressed at low levels in several other CC tissues. CC -!- INDUCTION: Phorbol 12-myristate 13-acetate (PMA) induces CC overexpression in keratinocytes. Up-regulated by IFN-alpha. CC -!- DOMAIN: The CMP/dCMP deaminase zinc-binding 1 domain mediates RNA CC binding, RNA-dependent oligomerization and virion incorporation CC whereas the CMP/dCMP deaminase zinc-binding 2 domain confers CC deoxycytidine deaminase activity and substrate sequence CC specificity (PubMed:17020885). CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes CC found in a cluster, thought to result from gene duplication, on CC chromosome 22. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. CC -!- SIMILARITY: Contains 2 CMP/dCMP deaminase zinc-binding domains. CC -!- SEQUENCE CAUTION: CC Sequence=AAD00089.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAD00090.1; Type=Frameshift; Positions=59, 134; Note=Frameshifts result in two separate ORFs termed phorbolins 2 and 3; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U61083; AAD00089.1; ALT_INIT; mRNA. DR EMBL; U61084; AAD00090.1; ALT_FRAME; mRNA. DR EMBL; AY743217; AAW31743.1; -; mRNA. DR EMBL; CT841510; CAJ86440.1; -; mRNA. DR EMBL; AL022318; CAB45270.1; -; Genomic_DNA. DR EMBL; AL022318; CAQ09851.1; -; Genomic_DNA. DR EMBL; BC053859; AAH53859.1; -; mRNA. DR CCDS; CCDS13982.1; -. [Q9UH17-1] DR CCDS; CCDS58807.1; -. [Q9UH17-3] DR RefSeq; NP_001257340.1; NM_001270411.1. DR RefSeq; NP_004891.4; NM_004900.4. DR UniGene; Hs.226307; -. DR UniGene; Hs.658626; -. DR ProteinModelPortal; Q9UH17; -. DR SMR; Q9UH17; 4-382. DR BioGrid; 114950; 2. DR IntAct; Q9UH17; 3. DR MINT; MINT-4992727; -. DR STRING; 9606.ENSP00000327459; -. DR PhosphoSite; Q9UH17; -. DR DMDM; 12643884; -. DR MaxQB; Q9UH17; -. DR PaxDb; Q9UH17; -. DR PRIDE; Q9UH17; -. DR DNASU; 9582; -. DR Ensembl; ENST00000333467; ENSP00000327459; ENSG00000179750. [Q9UH17-1] DR Ensembl; ENST00000335760; ENSP00000338897; ENSG00000179750. [Q9UH17-2] DR Ensembl; ENST00000407298; ENSP00000385068; ENSG00000179750. [Q9UH17-3] DR GeneID; 9582; -. DR KEGG; hsa:9582; -. DR UCSC; uc003awo.2; human. [Q9UH17-1] DR UCSC; uc003awp.2; human. DR CTD; 9582; -. DR GeneCards; GC22P039378; -. DR HGNC; HGNC:17352; APOBEC3B. DR MIM; 607110; gene. DR neXtProt; NX_Q9UH17; -. DR PharmGKB; PA24892; -. DR eggNOG; NOG135704; -. DR HOGENOM; HOG000033755; -. DR HOVERGEN; HBG050434; -. DR KO; K01500; -. DR OrthoDB; EOG75QR3Z; -. DR PhylomeDB; Q9UH17; -. DR TreeFam; TF331356; -. DR GeneWiki; APOBEC3B; -. DR GenomeRNAi; 9582; -. DR NextBio; 35465727; -. DR PRO; PR:Q9UH17; -. DR ArrayExpress; Q9UH17; -. DR Bgee; Q9UH17; -. DR CleanEx; HS_APOBEC3B; -. DR Genevestigator; Q9UH17; -. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0047844; F:deoxycytidine deaminase activity; IMP:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0008152; P:metabolic process; IMP:GOC. DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR007904; APOBEC_C. DR InterPro; IPR013158; APOBEC_N. DR InterPro; IPR016193; Cytidine_deaminase-like. DR Pfam; PF05240; APOBEC_C; 1. DR Pfam; PF08210; APOBEC_N; 1. DR SUPFAM; SSF53927; SSF53927; 2. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 2. PE 1: Evidence at protein level; KW Alternative splicing; Antiviral defense; Complete proteome; Hydrolase; KW Immunity; Innate immunity; Metal-binding; Nucleus; Polymorphism; KW Reference proteome; Repeat; RNA-binding; Zinc. FT CHAIN 1 382 DNA dC->dU-editing enzyme APOBEC-3B. FT /FTId=PRO_0000171753. FT DOMAIN 66 100 CMP/dCMP deaminase zinc-binding 1. FT DOMAIN 253 289 CMP/dCMP deaminase zinc-binding 2. FT ACT_SITE 255 255 Proton donor (Potential). FT METAL 66 66 Zinc (By similarity). FT METAL 97 97 Zinc (By similarity). FT METAL 100 100 Zinc (By similarity). FT METAL 253 253 Zinc (By similarity). FT METAL 284 284 Zinc (By similarity). FT METAL 289 289 Zinc (By similarity). FT VAR_SEQ 191 382 YLMDPDTFTFNFNNDPLVLRRRQTYLCYEVERLDNGTWVLM FT DQHMGFLCNEAKNLLCGFYGRHAELRFLDLVPSLQLDPAQI FT YRVTWFISWSPCFSWGCAGEVRAFLQENTHVRLRIFAARIY FT DYDPLYKEALQMLRDAGAQVSIMTYDEFEYCWDTFVYRQGC FT PFQPWDGLEEHSQALSGRLRAILQNQGN -> LRIFSVAFT FT AAMRSCASWTWFLLCSWTRPRSTGSLGSSPGAPASPGAVPG FT KCVRSFRRTHT (in isoform 2). FT /FTId=VSP_009802. FT VAR_SEQ 242 266 Missing (in isoform 3). FT /FTId=VSP_044900. FT VARIANT 62 62 K -> E (in dbSNP:rs2076109). FT /FTId=VAR_018142. FT VARIANT 98 98 P -> L (in dbSNP:rs2076110). FT /FTId=VAR_018143. FT VARIANT 109 109 S -> A (in dbSNP:rs17000697). FT /FTId=VAR_033455. FT VARIANT 146 146 T -> K (in dbSNP:rs5995649). FT /FTId=VAR_018144. FT VARIANT 351 351 R -> H (in dbSNP:rs1053813). FT /FTId=VAR_048722. FT CONFLICT 103 104 KL -> NV (in Ref. 1; AAD00090). FT CONFLICT 227 228 TW -> WM (in Ref. 1; AAD00089). FT CONFLICT 255 256 EL -> DW (in Ref. 1; AAD00089). FT CONFLICT 306 306 R -> P (in Ref. 1; AAD00089). FT CONFLICT 356 356 F -> S (in Ref. 2; AAW31743). SQ SEQUENCE 382 AA; 45924 MW; DA6EDD23E8856240 CRC64; MNPQIRNPME RMYRDTFYDN FENEPILYGR SYTWLCYEVK IKRGRSNLLW DTGVFRGQVY FKPQYHAEMC FLSWFCGNQL PAYKCFQITW FVSWTPCPDC VAKLAEFLSE HPNVTLTISA ARLYYYWERD YRRALCRLSQ AGARVTIMDY EEFAYCWENF VYNEGQQFMP WYKFDENYAF LHRTLKEILR YLMDPDTFTF NFNNDPLVLR RRQTYLCYEV ERLDNGTWVL MDQHMGFLCN EAKNLLCGFY GRHAELRFLD LVPSLQLDPA QIYRVTWFIS WSPCFSWGCA GEVRAFLQEN THVRLRIFAA RIYDYDPLYK EALQMLRDAG AQVSIMTYDE FEYCWDTFVY RQGCPFQPWD GLEEHSQALS GRLRAILQNQ GN // ID ABC3C_HUMAN Reviewed; 190 AA. AC Q9NRW3; B2R884; Q5JZ92; Q7Z2N7; Q96F12; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2004, sequence version 2. DT 09-JUL-2014, entry version 111. DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3C; DE Short=A3C; DE EC=3.5.4.-; DE AltName: Full=APOBEC1-like; DE AltName: Full=Phorbolin I; GN Name=APOBEC3C; Synonyms=APOBEC1L, PBI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Hematopoietic stem cell; RA Gu J., Huang Q., Yu Y., Xu S., Wang Y., Han Z., Chen Z., Zhou J., RA Tu Y., Gu W., Fu G., Huang C.; RT "Novel genes expressed in hematopoietic stem/progenitor cells from RT myelodysplastic syndrome patients."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP GENE FAMILY ORGANIZATION, AND TISSUE SPECIFICITY. RX PubMed=11863358; DOI=10.1006/geno.2002.6718; RA Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., RA Navaratnam N.; RT "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on RT chromosome 22."; RL Genomics 79:285-296(2002). RN [8] RP FUNCTION IN HIV-1 INFECTIVITY. RX PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4; RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., RA Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.; RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif."; RL Cell 114:21-31(2003). RN [9] RP FUNCTION IN SIV RESTRICTION. RX PubMed=15466872; DOI=10.1074/jbc.M408802200; RA Yu Q., Chen D., Koenig R., Mariani R., Unutmaz D., Landau N.R.; RT "APOBEC3B and APOBEC3C are potent inhibitors of simian RT immunodeficiency virus replication."; RL J. Biol. Chem. 279:53379-53386(2004). RN [10] RP FUNCTION IN RETROTRANSPOSITION. RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031; RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., RA Landau N.R., Weitzman M.D.; RT "APOBEC3A is a potent inhibitor of adeno-associated virus and RT retrotransposons."; RL Curr. Biol. 16:480-485(2006). RN [11] RP REVIEW. RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350; RA Chiu Y.L., Greene W.C.; RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing RT exogenous retroviruses and endogenous retroelements."; RL Annu. Rev. Immunol. 26:317-353(2008). RN [12] RP REVIEW ON FUNCTION IN HBV RESTRICTION. RX PubMed=18448976; DOI=10.1097/QCO.0b013e3282fe1bb2; RA Bonvin M., Greeve J.; RT "Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine RT deaminases as effectors in innate immunity against the hepatitis B RT virus."; RL Curr. Opin. Infect. Dis. 21:298-303(2008). RN [13] RP INTERACTION WITH HUMAN FOAMY VIRUS PROTEIN BET. RX PubMed=19074429; DOI=10.1074/jbc.M808853200; RA Perkovic M., Schmidt S., Marino D., Russell R.A., Stauch B., RA Hofmann H., Kopietz F., Kloke B.-P., Zielonka J., Stroever H., RA Hermle J., Lindemann D., Pathak V.K., Schneider G., Loechelt M., RA Cichutek K., Muenk C.; RT "Species-specific inhibition of APOBEC3C by the prototype foamy virus RT protein bet."; RL J. Biol. Chem. 284:5819-5826(2009). RN [14] RP FUNCTION IN RETROTRANSPOSITION. RX PubMed=20062055; DOI=10.1038/nsmb.1744; RA Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.; RT "APOBEC3 proteins mediate the clearance of foreign DNA from human RT cells."; RL Nat. Struct. Mol. Biol. 17:222-229(2010). RN [15] RP TISSUE SPECIFICITY. RX PubMed=20308164; DOI=10.1093/nar/gkq174; RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L., RA Harris R.S.; RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in RT lymphocytes and tissues: implications for HIV-1 restriction."; RL Nucleic Acids Res. 38:4274-4284(2010). RN [16] RP FUNCTION IN DNA DEMETHYLATION. RX PubMed=21496894; DOI=10.1016/j.cell.2011.03.022; RA Guo J.U., Su Y., Zhong C., Ming G.L., Song H.; RT "Hydroxylation of 5-methylcytosine by TET1 promotes active DNA RT demethylation in the adult brain."; RL Cell 145:423-434(2011). RN [17] RP FUNCTION IN EBV AND HHV-1 INHIBITION. RX PubMed=21632763; DOI=10.1128/JVI.00290-11; RA Suspene R., Aynaud M.M., Koch S., Pasdeloup D., Labetoulle M., RA Gaertner B., Vartanian J.P., Meyerhans A., Wain-Hobson S.; RT "Genetic editing of herpes simplex virus 1 and Epstein-Barr RT herpesvirus genomes by human APOBEC3 cytidine deaminases in culture RT and in vivo."; RL J. Virol. 85:7594-7602(2011). RN [18] RP SUBCELLULAR LOCATION. RX PubMed=21835787; DOI=10.1128/JVI.05238-11; RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L., RA Brown W.L., Harris R.S.; RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H RT demonstrate a conserved capacity to restrict Vif-deficient HIV-1."; RL J. Virol. 85:11220-11234(2011). RN [19] RP REVIEW. RA Love R.; RT "Cytosine deaminases APOBEC3A, APOBEC3C, and APOBEC3H: Current RT understanding of their functional roles."; RL Student Perspec. Contemp. Virol. 0:0-0(2011). RN [20] RP REVIEW. RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275; RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.; RT "Retroelements versus APOBEC3 family members: No great escape from the RT magnificent seven."; RL Front. Microbiol. 3:275-275(2012). RN [21] RP INTERACTION WITH TRIB3, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=22977230; DOI=10.1074/jbc.M112.372722; RA Aynaud M.M., Suspene R., Vidalain P.O., Mussil B., Guetard D., RA Tangy F., Wain-Hobson S., Vartanian J.P.; RT "Human Tribbles 3 protects nuclear DNA from cytidine deamination by RT APOBEC3A."; RL J. Biol. Chem. 287:39182-39192(2012). RN [22] RP INTERACTION WITH AGO2. RX PubMed=22915799; DOI=10.1128/JVI.00595-12; RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.; RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by RT P bodies."; RL J. Virol. 86:11712-11724(2012). RN [23] RP REVIEW. RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004; RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.; RT "Functions and regulation of the APOBEC family of proteins."; RL Semin. Cell Dev. Biol. 23:258-268(2012). CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an CC inhibitor of retrovirus replication and retrotransposon mobility CC via deaminase-dependent and -independent mechanisms. After the CC penetration of retroviral nucleocapsids into target cells of CC infection and the initiation of reverse transcription, it can CC induce the conversion of cytosine to uracil in the minus-sense CC single-strand viral DNA, leading to G-to-A hypermutations in the CC subsequent plus-strand viral DNA. The resultant detrimental levels CC of mutations in the proviral genome, along with a deamination- CC independent mechanism that works prior to the proviral CC integration, together exert efficient antiretroviral effects in CC infected target cells. Selectively targets single-stranded DNA and CC does not deaminate double-stranded DNA or single-or double- CC stranded RNA. Exhibits antiviral activity against simian CC immunodeficiency virus (SIV), hepatitis B virus (HBV), herpes CC simplex virus 1 (HHV-1) and Epstein-Barr virus (EBV) and may CC inhibit the mobility of LTR and non-LTR retrotransposons. May also CC play a role in the epigenetic regulation of gene expression CC through the process of active DNA demethylation. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- COFACTOR: Zinc (By similarity). CC -!- SUBUNIT: Homodimer. Interacts with human foamy virus protein Bet; CC this interaction does not induce APOBEC3C degradation, but CC prevents dimerization and incorporation into virion of the latter. CC Interacts with TRIB3 and AGO2. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. CC -!- TISSUE SPECIFICITY: Expressed in spleen, testes, peripherical CC blood lymphocytes, heart, thymus, prostate and ovary. CC -!- INDUCTION: Up-regulated by IFN-alpha. CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes CC found in a cluster, thought to result from gene duplication, on CC chromosome 22. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. CC -!- SIMILARITY: Contains 1 CMP/dCMP deaminase zinc-binding domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAF86650.1; Type=Frameshift; Positions=172; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF165520; AAF86650.1; ALT_FRAME; mRNA. DR EMBL; CR456394; CAG30280.1; -; mRNA. DR EMBL; AK313272; BAG36081.1; -; mRNA. DR EMBL; AL022318; CAI17898.1; -; Genomic_DNA. DR EMBL; CH471095; EAW60284.1; -; Genomic_DNA. DR EMBL; BC011739; AAH11739.1; -; mRNA. DR EMBL; BC021080; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS13983.1; -. DR RefSeq; NP_055323.2; NM_014508.2. DR UniGene; Hs.441124; -. DR PDB; 3VM8; X-ray; 3.00 A; A/B=1-190. DR PDB; 3VOW; X-ray; 2.15 A; A/B=1-190. DR PDBsum; 3VM8; -. DR PDBsum; 3VOW; -. DR ProteinModelPortal; Q9NRW3; -. DR SMR; Q9NRW3; 5-190. DR BioGrid; 118162; 9. DR DIP; DIP-48919N; -. DR IntAct; Q9NRW3; 4. DR MINT; MINT-6631470; -. DR STRING; 9606.ENSP00000355340; -. DR PhosphoSite; Q9NRW3; -. DR DMDM; 48474983; -. DR MaxQB; Q9NRW3; -. DR PaxDb; Q9NRW3; -. DR PRIDE; Q9NRW3; -. DR DNASU; 27350; -. DR Ensembl; ENST00000361441; ENSP00000355340; ENSG00000244509. DR GeneID; 27350; -. DR KEGG; hsa:27350; -. DR UCSC; uc003awr.3; human. DR CTD; 27350; -. DR GeneCards; GC22P039410; -. DR HGNC; HGNC:17353; APOBEC3C. DR HPA; CAB033048; -. DR MIM; 607750; gene. DR neXtProt; NX_Q9NRW3; -. DR PharmGKB; PA24893; -. DR eggNOG; NOG289247; -. DR HOGENOM; HOG000033754; -. DR HOVERGEN; HBG050434; -. DR InParanoid; Q9NRW3; -. DR KO; K01500; -. DR OMA; SETHCHA; -. DR PhylomeDB; Q9NRW3; -. DR TreeFam; TF331356; -. DR ChiTaRS; APOBEC3C; human. DR GeneWiki; APOBEC3C; -. DR GenomeRNAi; 27350; -. DR NextBio; 50452; -. DR PRO; PR:Q9NRW3; -. DR ArrayExpress; Q9NRW3; -. DR Bgee; Q9NRW3; -. DR CleanEx; HS_APOBEC3C; -. DR Genevestigator; Q9NRW3; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:InterPro. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009972; P:cytidine deamination; IDA:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB. DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR007904; APOBEC_C. DR InterPro; IPR016193; Cytidine_deaminase-like. DR Pfam; PF05240; APOBEC_C; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1. PE 1: Evidence at protein level; KW 3D-structure; Antiviral defense; Complete proteome; Cytoplasm; KW Host-virus interaction; Hydrolase; Immunity; Innate immunity; KW Metal-binding; Nucleus; Reference proteome; Zinc. FT CHAIN 1 190 DNA dC->dU-editing enzyme APOBEC-3C. FT /FTId=PRO_0000171755. FT DOMAIN 66 100 CMP/dCMP deaminase zinc-binding. FT ACT_SITE 68 68 Proton donor (By similarity). FT METAL 66 66 Zinc; catalytic (By similarity). FT METAL 97 97 Zinc; catalytic (By similarity). FT METAL 100 100 Zinc; catalytic (By similarity). FT CONFLICT 31 31 N -> D (in Ref. 6; AAH11739). FT HELIX 14 20 FT TURN 27 29 FT STRAND 32 43 FT STRAND 46 58 FT HELIX 63 65 FT HELIX 67 75 FT STRAND 84 94 FT HELIX 98 110 FT STRAND 114 122 FT TURN 124 127 FT HELIX 129 141 FT STRAND 144 147 FT HELIX 150 160 FT HELIX 174 189 SQ SEQUENCE 190 AA; 22826 MW; BE49E80F95C71214 CRC64; MNPQIRNPMK AMYPGTFYFQ FKNLWEANDR NETWLCFTVE GIKRRSVVSW KTGVFRNQVD SETHCHAERC FLSWFCDDIL SPNTKYQVTW YTSWSPCPDC AGEVAEFLAR HSNVNLTIFT ARLYYFQYPC YQEGLRSLSQ EGVAVEIMDY EDFKYCWENF VYNDNEPFKP WKGLKTNFRL LKRRLRESLQ // ID ABC3F_HUMAN Reviewed; 373 AA. AC Q8IUX4; B0QYD4; Q45F03; Q6ICH3; Q7Z2N2; Q7Z2N5; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 3. DT 09-JUL-2014, entry version 110. DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3F; DE EC=3.5.4.-; DE AltName: Full=Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3F; DE Short=A3F; GN Name=APOBEC3F; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANTS THR-178; RP ILE-231 AND CYS-307. RG SeattleSNPs variation discovery resource; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND RP VARIANTS PRO-48 AND SER-108. RC TISSUE=Pancreas, Spleen, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP GENE FAMILY ORGANIZATION, AND TISSUE SPECIFICITY. RX PubMed=11863358; DOI=10.1006/geno.2002.6718; RA Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., RA Navaratnam N.; RT "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on RT chromosome 22."; RL Genomics 79:285-296(2002). RN [7] RP REVIEW ON APOBEC FAMILIES. RX PubMed=12683974; DOI=10.1016/S0168-9525(03)00054-4; RA Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.; RT "Messenger RNA editing in mammals: new members of the APOBEC family RT seeking roles in the family business."; RL Trends Genet. 19:207-216(2003). RN [8] RP FUNCTION IN HIV-1 INFECTIVITY, AND TISSUE SPECIFICITY. RX PubMed=15152192; DOI=10.1038/sj.emboj.7600246; RA Wiegand H.L., Doehle B.P., Bogerd H.P., Cullen B.R.; RT "A second human antiretroviral factor, APOBEC3F, is suppressed by the RT HIV-1 and HIV-2 Vif proteins."; RL EMBO J. 23:2451-2458(2004). RN [9] RP FUNCTION IN RETROTRANSPOSITION, AND SUBCELLULAR LOCATION. RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031; RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., RA Landau N.R., Weitzman M.D.; RT "APOBEC3A is a potent inhibitor of adeno-associated virus and RT retrotransposons."; RL Curr. Biol. 16:480-485(2006). RN [10] RP DOMAIN CMP/DCMP DEAMINASE ZINC-BINDING, AND MUTAGENESIS OF GLU-67 AND RP GLU-251. RX PubMed=17020885; DOI=10.1074/jbc.M604980200; RA Hakata Y., Landau N.R.; RT "Reversed functional organization of mouse and human APOBEC3 cytidine RT deaminase domains."; RL J. Biol. Chem. 281:36624-36631(2006). RN [11] RP FUNCTION IN SFV RESTRICTION. RX PubMed=16378963; DOI=10.1128/JVI.80.2.605-614.2006; RA Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A., RA Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.; RT "Restriction of foamy viruses by APOBEC cytidine deaminases."; RL J. Virol. 80:605-614(2006). RN [12] RP SUBCELLULAR LOCATION, AND INTERACTION WITH APOBEC3G. RX PubMed=16699599; DOI=10.1371/journal.ppat.0020041; RA Wichroski M.J., Robb G.B., Rana T.M.; RT "Human retroviral host restriction factors APOBEC3G and APOBEC3F RT localize to mRNA processing bodies."; RL PLoS Pathog. 2:E41-E41(2006). RN [13] RP REVIEW. RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350; RA Chiu Y.L., Greene W.C.; RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing RT exogenous retroviruses and endogenous retroelements."; RL Annu. Rev. Immunol. 26:317-353(2008). RN [14] RP REVIEW ON FUNCTION IN HBV RESTRICTION. RX PubMed=18448976; DOI=10.1097/QCO.0b013e3282fe1bb2; RA Bonvin M., Greeve J.; RT "Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine RT deaminases as effectors in innate immunity against the hepatitis B RT virus."; RL Curr. Opin. Infect. Dis. 21:298-303(2008). RN [15] RP FUNCTION IN EIAV RESTRICTION. RX PubMed=19458006; DOI=10.1128/JVI.00015-09; RA Zielonka J., Bravo I.G., Marino D., Conrad E., Perkovic M., RA Battenberg M., Cichutek K., Muenk C.; RT "Restriction of equine infectious anemia virus by equine APOBEC3 RT cytidine deaminases."; RL J. Virol. 83:7547-7559(2009). RN [16] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=20219927; DOI=10.1128/JVI.02358-09; RA Mbisa J.L., Bu W., Pathak V.K.; RT "APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different RT mechanisms."; RL J. Virol. 84:5250-5259(2010). RN [17] RP FUNCTION IN XMRV RESTRICTION. RX PubMed=20335265; DOI=10.1128/JVI.00134-10; RA Paprotka T., Venkatachari N.J., Chaipan C., Burdick R., RA Delviks-Frankenberry K.A., Hu W.S., Pathak V.K.; RT "Inhibition of xenotropic murine leukemia virus-related virus by RT APOBEC3 proteins and antiviral drugs."; RL J. Virol. 84:5719-5729(2010). RN [18] RP FUNCTION IN RETROTRANSPOSITION. RX PubMed=20062055; DOI=10.1038/nsmb.1744; RA Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.; RT "APOBEC3 proteins mediate the clearance of foreign DNA from human RT cells."; RL Nat. Struct. Mol. Biol. 17:222-229(2010). RN [19] RP TISSUE SPECIFICITY. RX PubMed=20308164; DOI=10.1093/nar/gkq174; RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L., RA Harris R.S.; RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in RT lymphocytes and tissues: implications for HIV-1 restriction."; RL Nucleic Acids Res. 38:4274-4284(2010). RN [20] RP FUNCTION IN DNA DEMETHYLATION. RX PubMed=21496894; DOI=10.1016/j.cell.2011.03.022; RA Guo J.U., Su Y., Zhong C., Ming G.L., Song H.; RT "Hydroxylation of 5-methylcytosine by TET1 promotes active DNA RT demethylation in the adult brain."; RL Cell 145:423-434(2011). RN [21] RP FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, AND ENZYME RP REGULATION. RX PubMed=21835787; DOI=10.1128/JVI.05238-11; RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L., RA Brown W.L., Harris R.S.; RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H RT demonstrate a conserved capacity to restrict Vif-deficient HIV-1."; RL J. Virol. 85:11220-11234(2011). RN [22] RP REVIEW. RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275; RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.; RT "Retroelements versus APOBEC3 family members: No great escape from the RT magnificent seven."; RL Front. Microbiol. 3:275-275(2012). RN [23] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AGO1; AGO2 AND RP AGO3. RX PubMed=22915799; DOI=10.1128/JVI.00595-12; RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.; RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by RT P bodies."; RL J. Virol. 86:11712-11724(2012). RN [24] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=22807680; DOI=10.1371/journal.ppat.1002800; RA Refsland E.W., Hultquist J.F., Harris R.S.; RT "Endogenous origins of HIV-1 G-to-A hypermutation and restriction in RT the nonpermissive T cell line CEM2n."; RL PLoS Pathog. 8:E1002800-E1002800(2012). RN [25] RP REVIEW. RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004; RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.; RT "Functions and regulation of the APOBEC family of proteins."; RL Semin. Cell Dev. Biol. 23:258-268(2012). RN [26] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=23097438; DOI=10.1128/JVI.00676-12; RA Chaipan C., Smith J.L., Hu W.S., Pathak V.K.; RT "APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and RT APOBEC3DE in human primary CD4+ t cells and macrophages."; RL J. Virol. 87:444-453(2013). RN [27] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=23152537; DOI=10.1128/JVI.02587-12; RA Gillick K., Pollpeter D., Phalora P., Kim E.Y., Wolinsky S.M., RA Malim M.H.; RT "The suppression of HIV-1 infection by APOBEC3 proteins in primary RT human CD4+ T cells is associated with the inhibition of processive RT reverse transcription as well as excessive cytidine deamination."; RL J. Virol. 87:1508-1517(2013). CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an CC inhibitor of retrovirus replication and retrotransposon mobility CC via deaminase-dependent and -independent mechanisms. Exhibits CC antiviral activity against vif-deficient HIV-1. After the CC penetration of retroviral nucleocapsids into target cells of CC infection and the initiation of reverse transcription, it can CC induce the conversion of cytosine to uracil in the minus-sense CC single-strand viral DNA, leading to G-to-A hypermutations in the CC subsequent plus-strand viral DNA. The resultant detrimental levels CC of mutations in the proviral genome, along with a deamination- CC independent mechanism that works prior to the proviral CC integration, together exert efficient antiretroviral effects in CC infected target cells. Selectively targets single-stranded DNA and CC does not deaminate double-stranded DNA or single- or double- CC stranded RNA. Exhibits antiviral activity also against hepatitis B CC virus (HBV), equine infectious anemia virus (EIAV), xenotropic CC MuLV-related virus (XMRV) and simian foamy virus (SFV) and may CC inhibit the mobility of LTR and non-LTR retrotransposons. May also CC play a role in the epigenetic regulation of gene expression CC through the process of active DNA demethylation. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- COFACTOR: Zinc (By similarity). CC -!- ENZYME REGULATION: Antiviral activity is neutralized by the HIV-1 CC virion infectivity factor (VIF), that prevents its incorporation CC into progeny virions by both inhibiting its translation and/or by CC inducing its ubiquitination and subsequent degradation by the 26S CC proteasome. CC -!- SUBUNIT: Binds HIV-1 Vif. In the absence of Vif protein, CC specifically packaged into HIV-1 virions. Interacts with APOBEC3G CC in an RNA-dependent manner. Interacts with AGO1, AGO2 and AGO3. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, P-body. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8IUX4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IUX4-2; Sequence=VSP_009803, VSP_009804; CC Note=May be due to a competing donor splice site. No CC experimental confirmation available; CC Name=3; CC IsoId=Q8IUX4-3; Sequence=VSP_042754, VSP_042755; CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in ovary. CC -!- INDUCTION: Up-regulated by IFN-alpha. CC -!- DOMAIN: The CMP/dCMP deaminase zinc-binding 1 domain mediates RNA CC binding, RNA-dependent oligomerization and virion incorporation CC whereas the CMP/dCMP deaminase zinc-binding 2 domain confers CC deoxycytidine deaminase activity and substrate sequence CC specificity (PubMed:17020885). CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes CC found in a cluster, thought to result from gene duplication, on CC chromosome 22. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. CC -!- SIMILARITY: Contains 2 CMP/dCMP deaminase zinc-binding domains. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/apobec3f/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR456395; CAG30281.1; -; mRNA. DR EMBL; DQ146365; AAZ38720.1; -; Genomic_DNA. DR EMBL; AL022318; CAQ09853.1; -; Genomic_DNA. DR EMBL; CH471095; EAW60288.1; -; Genomic_DNA. DR EMBL; CH471095; EAW60289.1; -; Genomic_DNA. DR EMBL; BC038808; AAH38808.1; -; mRNA. DR EMBL; BC061914; AAH61914.1; -; mRNA. DR CCDS; CCDS33648.1; -. [Q8IUX4-1] DR CCDS; CCDS33649.1; -. [Q8IUX4-3] DR RefSeq; NP_001006667.1; NM_001006666.1. [Q8IUX4-3] DR RefSeq; NP_660341.2; NM_145298.5. [Q8IUX4-1] DR UniGene; Hs.659809; -. DR UniGene; Hs.660143; -. DR PDB; 4IOU; X-ray; 2.75 A; A/B/C/D=185-373. DR PDB; 4J4J; X-ray; 3.10 A; A/B=218-373. DR PDBsum; 4IOU; -. DR PDBsum; 4J4J; -. DR ProteinModelPortal; Q8IUX4; -. DR SMR; Q8IUX4; 6-189, 194-373. DR BioGrid; 128319; 5. DR DIP; DIP-59966N; -. DR MINT; MINT-6631309; -. DR STRING; 9606.ENSP00000309749; -. DR ChEMBL; CHEMBL2007626; -. DR PhosphoSite; Q8IUX4; -. DR DMDM; 161784334; -. DR MaxQB; Q8IUX4; -. DR PaxDb; Q8IUX4; -. DR PRIDE; Q8IUX4; -. DR DNASU; 200316; -. DR Ensembl; ENST00000308521; ENSP00000309749; ENSG00000128394. [Q8IUX4-1] DR Ensembl; ENST00000381565; ENSP00000370977; ENSG00000128394. [Q8IUX4-3] DR GeneID; 200316; -. DR KEGG; hsa:200316; -. DR UCSC; uc003awv.3; human. [Q8IUX4-3] DR UCSC; uc003aww.3; human. [Q8IUX4-1] DR CTD; 200316; -. DR GeneCards; GC22P039436; -. DR H-InvDB; HIX0213264; -. DR HGNC; HGNC:17356; APOBEC3F. DR MIM; 608993; gene. DR neXtProt; NX_Q8IUX4; -. DR PharmGKB; PA24896; -. DR eggNOG; NOG135704; -. DR HOGENOM; HOG000142455; -. DR HOVERGEN; HBG050434; -. DR InParanoid; Q8IUX4; -. DR KO; K01500; -. DR OMA; SHARRCP; -. DR OrthoDB; EOG7GXPJ6; -. DR PhylomeDB; Q8IUX4; -. DR TreeFam; TF331356; -. DR BRENDA; 3.5.4.5; 2681. DR GeneWiki; APOBEC3F; -. DR GenomeRNAi; 200316; -. DR NextBio; 89891; -. DR PRO; PR:Q8IUX4; -. DR ArrayExpress; Q8IUX4; -. DR Bgee; Q8IUX4; -. DR CleanEx; HS_APOBEC3F; -. DR Genevestigator; Q8IUX4; -. DR GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; TAS:HGNC. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IDA:UniProtKB. DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0004126; F:cytidine deaminase activity; IDA:HGNC. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:HGNC. DR GO; GO:0008270; F:zinc ion binding; IDA:HGNC. DR GO; GO:0016553; P:base conversion or substitution editing; IDA:HGNC. DR GO; GO:0009972; P:cytidine deamination; IDA:GOC. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB. DR GO; GO:0080111; P:DNA demethylation; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IDA:HGNC. DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB. DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB. DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB. DR GO; GO:0048525; P:negative regulation of viral process; IDA:HGNC. DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:HGNC. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR013158; APOBEC_N. DR InterPro; IPR016193; Cytidine_deaminase-like. DR Pfam; PF08210; APOBEC_N; 2. DR SUPFAM; SSF53927; SSF53927; 2. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; KW Complete proteome; Cytoplasm; Hydrolase; Immunity; Innate immunity; KW Metal-binding; Polymorphism; Reference proteome; Repeat; Zinc. FT CHAIN 1 373 DNA dC->dU-editing enzyme APOBEC-3F. FT /FTId=PRO_0000171757. FT DOMAIN 65 99 CMP/dCMP deaminase zinc-binding 1. FT DOMAIN 249 283 CMP/dCMP deaminase zinc-binding 2. FT ACT_SITE 251 251 Proton donor (By similarity). FT METAL 65 65 Zinc (By similarity). FT METAL 96 96 Zinc (By similarity). FT METAL 99 99 Zinc (By similarity). FT VAR_SEQ 58 79 VYSQPEHHAEMCFLSWFCGNQL -> VPPGLQSLCRQELSQ FT LGKQTTH (in isoform 2). FT /FTId=VSP_009803. FT VAR_SEQ 59 113 YSQPEHHAEMCFLSWFCGNQLPAYKCFQITWFVSWTPCPDC FT VAKLAEFLAEHPNV -> PRSFIRAPFQVLSSPFGQCAPPH FT GTAQVQWPPQLTAGREQGRP (in isoform 3). FT /FTId=VSP_042754. FT VAR_SEQ 80 373 Missing (in isoform 2). FT /FTId=VSP_009804. FT VAR_SEQ 114 373 Missing (in isoform 3). FT /FTId=VSP_042755. FT VARIANT 48 48 R -> P (in dbSNP:rs35053197). FT /FTId=VAR_038355. FT VARIANT 61 61 Q -> L (in dbSNP:rs2076109). FT /FTId=VAR_018145. FT VARIANT 97 97 P -> L (in dbSNP:rs2076110). FT /FTId=VAR_018146. FT VARIANT 108 108 A -> S (in dbSNP:rs2020390). FT /FTId=VAR_018147. FT VARIANT 178 178 A -> T (in dbSNP:rs34182094). FT /FTId=VAR_025058. FT VARIANT 231 231 V -> I (in dbSNP:rs2076101). FT /FTId=VAR_018148. FT VARIANT 307 307 Y -> C (in dbSNP:rs12157816). FT /FTId=VAR_025059. FT MUTAGEN 67 67 E->A: Decrease in cytidine deaminase and FT antiviral activity; when associated with FT A-251. FT MUTAGEN 67 67 E->A: No effect on cytidine deaminase and FT antiviral activity. FT MUTAGEN 251 251 E->A: Decrease in cytidine deaminase and FT antiviral activity. FT MUTAGEN 251 251 E->A: Decrease in cytidine deaminase and FT antiviral activity; when associated with FT A-67. FT HELIX 197 203 FT STRAND 218 229 FT STRAND 232 238 FT STRAND 243 245 FT HELIX 250 261 FT STRAND 267 277 FT HELIX 281 293 FT STRAND 297 304 FT TURN 307 310 FT HELIX 312 323 FT STRAND 327 330 FT HELIX 333 342 FT HELIX 357 372 SQ SEQUENCE 373 AA; 45020 MW; AF1A0E13830695F4 CRC64; MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPRLD AKIFRGQVYS QPEHHAEMCF LSWFCGNQLP AYKCFQITWF VSWTPCPDCV AKLAEFLAEH PNVTLTISAA RLYYYWERDY RRALCRLSQA GARVKIMDDE EFAYCWENFV YSEGQPFMPW YKFDDNYAFL HRTLKEILRN PMEAMYPHIF YFHFKNLRKA YGRNESWLCF TMEVVKHHSP VSWKRGVFRN QVDPETHCHA ERCFLSWFCD DILSPNTNYE VTWYTSWSPC PECAGEVAEF LARHSNVNLT IFTARLYYFW DTDYQEGLRS LSQEGASVEI MGYKDFKYCW ENFVYNDDEP FKPWKGLKYN FLFLDSKLQE ILE // ID ABC3G_HUMAN Reviewed; 384 AA. AC Q9HC16; B2RDR9; Q45F02; Q5TF77; Q7Z2N1; Q7Z2N4; Q9H9H8; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 09-JUL-2014, entry version 130. DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3G; DE EC=3.5.4.-; DE AltName: Full=APOBEC-related cytidine deaminase; DE Short=APOBEC-related protein; DE Short=ARCD; DE AltName: Full=APOBEC-related protein 9; DE Short=ARP-9; DE AltName: Full=CEM-15; DE Short=CEM15; DE AltName: Full=Deoxycytidine deaminase; DE Short=A3G; GN Name=APOBEC3G; ORFNames=MDS019; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN HIV-1 RP INFECTION INHIBITION. RC TISSUE=Kidney; RX PubMed=14557625; DOI=10.1128/JVI.77.21.11398-11407.2003; RA Kao S., Khan M.A., Miyagi E., Plishka R., Buckler-White A., RA Strebel K.; RT "The human immunodeficiency virus type 1 Vif protein reduces RT intracellular expression and inhibits packaging of APOBEC3G (CEM15), a RT cellular inhibitor of virus infectivity."; RL J. Virol. 77:11398-11407(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Synovium, and Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hematopoietic stem cell; RA Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.; RT "Novel genes expressed in hematopoietic stem/progenitor cells from RT myelodysplastic syndrome patients."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-186 AND GLU-275. RG SeattleSNPs program for genomic applications; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Skin, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP GENE FAMILY ORGANIZATION, TISSUE SPECIFICITY, SUBUNIT, RNA-BINDING, RP AND ZINC-BINDING. RX PubMed=11863358; DOI=10.1006/geno.2002.6718; RA Jarmuz A., Chester A., Bayliss J., Gisbourne J., Dunham I., Scott J., RA Navaratnam N.; RT "An anthropoid-specific locus of orphan C to U RNA-editing enzymes on RT chromosome 22."; RL Genomics 79:285-296(2002). RN [10] RP TISSUE SPECIFICITY, AND FUNCTION IN HIV-1 INFECTION INHIBITION. RC TISSUE=T-cell lymphoma; RX PubMed=12167863; DOI=10.1038/nature00939; RA Sheehy A.M., Gaddis N.C., Choi J.D., Malim M.H.; RT "Isolation of a human gene that inhibits HIV-1 infection and is RT suppressed by the viral Vif protein."; RL Nature 418:646-650(2002). RN [11] RP SUBCELLULAR LOCATION, FUNCTION IN DNA C TO U EDITING, AND MUTAGENESIS RP OF GLU-67; HIS-81; GLU-85; CYS-97; CYS-100; CYS-221; HIS-257; GLU-259; RP CYS-288; CYS-291 AND GLU-323. RX PubMed=12808466; DOI=10.1038/nature01709; RA Mangeat B., Turelli P., Caron G., Friedli M., Perrin L., Trono D.; RT "Broad antiretroviral defence by human APOBEC3G through lethal editing RT of nascent reverse transcripts."; RL Nature 424:99-103(2003). RN [12] RP FUNCTION IN DNA C TO U EDITING, AND MLV INFECTION INHIBITION. RX PubMed=12809610; DOI=10.1016/S0092-8674(03)00423-9; RA Harris R.S., Bishop K.N., Sheehy A.M., Craig H.M., RA Petersen-Mahrt S.K., Watt I.N., Neuberger M.S., Malim M.H.; RT "DNA deamination mediates innate immunity to retroviral infection."; RL Cell 113:803-809(2003). RN [13] RP CATALYTIC ACTIVITY, FUNCTION IN DNA C TO U EDITING, AND MUTAGENESIS OF RP HIS-81; CYS-97; CYS-100; HIS-257; CYS-288 AND CYS-291. RX PubMed=12808465; DOI=10.1038/nature01707; RA Zhang H., Yang B., Pomerantz R.J., Zhang C., Arunachalam S.C., Gao L.; RT "The cytidine deaminase CEM15 induces hypermutation in newly RT synthesized HIV-1 DNA."; RL Nature 424:94-98(2003). RN [14] RP FUNCTION IN DNA C TO U EDITING, AND INTERACTION WITH VIF. RX PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4; RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., RA Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.; RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif."; RL Cell 114:21-31(2003). RN [15] RP FUNCTION IN DNA C TO U EDITING, INFECTION REGULATION OF HIV-1, AND RP MUTAGENESIS OF GLU-67; CYS-100; GLU-259 AND CYS-291. RC TISSUE=T-cell lymphoma; RX PubMed=12970355; DOI=10.1074/jbc.C300376200; RA Shindo K., Takaori-Kondo A., Kobayashi M., Abudu A., Fukunaga K., RA Uchiyama T.; RT "The enzymatic activity of CEM15/Apobec-3G is essential for the RT regulation of the infectivity of HIV-1 virion but not a sole RT determinant of its antiviral activity."; RL J. Biol. Chem. 278:44412-44416(2003). RN [16] RP INTERACTION WITH VIF, PROTEASOME MEDIATED DEGRADATION, AND TRANSLATION RP INHIBITION. RX PubMed=14527406; DOI=10.1016/S1097-2765(03)00353-8; RA Stopak K., de Noronha C., Yonemoto W., Greene W.C.; RT "HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both RT its translation and intracellular stability."; RL Mol. Cell 12:591-601(2003). RN [17] RP INTERACTION WITH VIF, AND UBIQUITINATION. RX PubMed=14528301; DOI=10.1038/nm946; RA Marin M., Rose K.M., Kozak S.L., Kabat D.; RT "HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its RT degradation."; RL Nat. Med. 9:1398-1403(2003). RN [18] RP FUNCTION IN DNA C TO U EDITING, AND UBIQUITINATION. RX PubMed=14528300; DOI=10.1038/nm945; RA Sheehy A.M., Gaddis N.C., Malim M.H.; RT "The antiretroviral enzyme APOBEC3G is degraded by the proteasome in RT response to HIV-1 Vif."; RL Nat. Med. 9:1404-1407(2003). RN [19] RP REVIEW ON APOBEC FAMILY. RX PubMed=12683974; DOI=10.1016/S0168-9525(03)00054-4; RA Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.; RT "Messenger RNA editing in mammals: new members of the APOBEC family RT seeking roles in the family business."; RL Trends Genet. 19:207-216(2003). RN [20] RP REVIEW. RX PubMed=14557052; DOI=10.1016/j.molmed.2003.08.008; RA Vartanian J.P., Sommer P., Wain-Hobson S.; RT "Death and the retrovirus."; RL Trends Mol. Med. 9:409-413(2003). RN [21] RP REVIEW. RX PubMed=14565218; DOI=10.1016/j.ymthe.2003.08.010; RA Cullen B.R.; RT "HIV-1 Vif: counteracting innate antiretroviral defenses."; RL Mol. Ther. 8:525-527(2003). RN [22] RP MUTAGENESIS OF ASP-128. RX PubMed=15054139; DOI=10.1073/pnas.0400830101; RA Xu H., Svarovskaia E.S., Barr R., Zhang Y., Khan M.A., Strebel K., RA Pathak V.K.; RT "A single amino acid substitution in human APOBEC3G antiretroviral RT enzyme confers resistance to HIV-1 virion infectivity factor-induced RT depletion."; RL Proc. Natl. Acad. Sci. U.S.A. 101:5652-5657(2004). RN [23] RP FUNCTION IN HBV INHIBITION. RX PubMed=15031497; DOI=10.1126/science.1092066; RA Turelli P., Mangeat B., Jost S., Vianin S., Trono D.; RT "Inhibition of hepatitis B virus replication by APOBEC3G."; RL Science 303:1829-1829(2004). RN [24] RP FUNCTION IN RETROTRANSPOSITION, AND SUBCELLULAR LOCATION. RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031; RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., RA Landau N.R., Weitzman M.D.; RT "APOBEC3A is a potent inhibitor of adeno-associated virus and RT retrotransposons."; RL Curr. Biol. 16:480-485(2006). RN [25] RP DOMAIN CMP/DCMP DEAMINASE ZINC-BINDING, SUBUNIT, AND MUTAGENESIS OF RP GLU-67 AND GLU-259. RX PubMed=17020885; DOI=10.1074/jbc.M604980200; RA Hakata Y., Landau N.R.; RT "Reversed functional organization of mouse and human APOBEC3 cytidine RT deaminase domains."; RL J. Biol. Chem. 281:36624-36631(2006). RN [26] RP FUNCTION IN SFV RESTRICTION. RX PubMed=16378963; DOI=10.1128/JVI.80.2.605-614.2006; RA Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A., RA Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.; RT "Restriction of foamy viruses by APOBEC cytidine deaminases."; RL J. Virol. 80:605-614(2006). RN [27] RP SUBCELLULAR LOCATION, AND INTERACTION WITH APOBEC3F; AGO2; EIF4E; RP EIF4ENIF1; DCP2 AND DDX6. RX PubMed=16699599; DOI=10.1371/journal.ppat.0020041; RA Wichroski M.J., Robb G.B., Rana T.M.; RT "Human retroviral host restriction factors APOBEC3G and APOBEC3F RT localize to mRNA processing bodies."; RL PLoS Pathog. 2:E41-E41(2006). RN [28] RP REVIEW. RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350; RA Chiu Y.L., Greene W.C.; RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing RT exogenous retroviruses and endogenous retroelements."; RL Annu. Rev. Immunol. 26:317-353(2008). RN [29] RP REVIEW ON FUNCTION IN HBV RESTRICTION. RX PubMed=18448976; DOI=10.1097/QCO.0b013e3282fe1bb2; RA Bonvin M., Greeve J.; RT "Hepatitis B: modern concepts in pathogenesis--APOBEC3 cytidine RT deaminases as effectors in innate immunity against the hepatitis B RT virus."; RL Curr. Opin. Infect. Dis. 21:298-303(2008). RN [30] RP SUBUNIT. RX PubMed=18842592; DOI=10.1074/jbc.M803726200; RA Bennett R.P., Salter J.D., Liu X., Wedekind J.E., Smith H.C.; RT "APOBEC3G subunits self-associate via the C-terminal deaminase RT domain."; RL J. Biol. Chem. 283:33329-33336(2008). RN [31] RP SUBCELLULAR LOCATION. RX PubMed=18667511; DOI=10.1128/JVI.02471-07; RA Stenglein M.D., Matsuo H., Harris R.S.; RT "Two regions within the amino-terminal half of APOBEC3G cooperate to RT determine cytoplasmic localization."; RL J. Virol. 82:9591-9599(2008). RN [32] RP PHOSPHORYLATION AT THR-32, AND INTERACTION WITH PRKACA. RX PubMed=18836454; DOI=10.1038/nsmb.1497; RA Shirakawa K., Takaori-Kondo A., Yokoyama M., Izumi T., Matsui M., RA Io K., Sato T., Sato H., Uchiyama T.; RT "Phosphorylation of APOBEC3G by protein kinase A regulates its RT interaction with HIV-1 Vif."; RL Nat. Struct. Mol. Biol. 15:1184-1191(2008). RN [33] RP FUNCTION IN EIAV RESTRICTION. RX PubMed=19458006; DOI=10.1128/JVI.00015-09; RA Zielonka J., Bravo I.G., Marino D., Conrad E., Perkovic M., RA Battenberg M., Cichutek K., Muenk C.; RT "Restriction of equine infectious anemia virus by equine APOBEC3 RT cytidine deaminases."; RL J. Virol. 83:7547-7559(2009). RN [34] RP REVIEW. RX PubMed=19008196; DOI=10.1098/rstb.2008.0193; RA Chiu Y.L., Greene W.C.; RT "APOBEC3G: an intracellular centurion."; RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 364:689-703(2009). RN [35] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=20219927; DOI=10.1128/JVI.02358-09; RA Mbisa J.L., Bu W., Pathak V.K.; RT "APOBEC3F and APOBEC3G inhibit HIV-1 DNA integration by different RT mechanisms."; RL J. Virol. 84:5250-5259(2010). RN [36] RP FUNCTION IN XMRV RESTRICTION. RX PubMed=20335265; DOI=10.1128/JVI.00134-10; RA Paprotka T., Venkatachari N.J., Chaipan C., Burdick R., RA Delviks-Frankenberry K.A., Hu W.S., Pathak V.K.; RT "Inhibition of xenotropic murine leukemia virus-related virus by RT APOBEC3 proteins and antiviral drugs."; RL J. Virol. 84:5719-5729(2010). RN [37] RP TISSUE SPECIFICITY. RX PubMed=20308164; DOI=10.1093/nar/gkq174; RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L., RA Harris R.S.; RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in RT lymphocytes and tissues: implications for HIV-1 restriction."; RL Nucleic Acids Res. 38:4274-4284(2010). RN [38] RP INTERACTION WITH HEPATITIS B VIRUS CAPSID PROTEIN. RX PubMed=20510315; DOI=10.1016/j.virusres.2010.05.009; RA Zhao D., Wang X., Lou G., Peng G., Li J., Zhu H., Chen F., Li S., RA Liu D., Chen Z., Yang Z.; RT "APOBEC3G directly binds Hepatitis B virus core protein in cell and RT cell free systems."; RL Virus Res. 151:213-219(2010). RN [39] RP PHOSPHORYLATION AT THR-32 AND THR-218, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF THR-218. RX PubMed=21659520; DOI=10.1074/jbc.M111.235721; RA Demorest Z.L., Li M., Harris R.S.; RT "Phosphorylation directly regulates the intrinsic DNA cytidine RT deaminase activity of activation-induced deaminase and APOBEC3G RT protein."; RL J. Biol. Chem. 286:26568-26575(2011). RN [40] RP FUNCTION IN HOST DEFENSE, AND MUTAGENESIS OF GLU-217 AND PRO-247. RX PubMed=21123384; DOI=10.1128/JVI.01651-10; RA Bulliard Y., Narvaiza I., Bertero A., Peddi S., Roehrig U.F., RA Ortiz M., Zoete V., Castro-Diaz N., Turelli P., Telenti A., RA Michielin O., Weitzman M.D., Trono D.; RT "Structure-function analyses point to a polynucleotide-accommodating RT groove essential for APOBEC3A restriction activities."; RL J. Virol. 85:1765-1776(2011). RN [41] RP FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, AND ENZYME RP REGULATION. RX PubMed=21835787; DOI=10.1128/JVI.05238-11; RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L., RA Brown W.L., Harris R.S.; RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H RT demonstrate a conserved capacity to restrict Vif-deficient HIV-1."; RL J. Virol. 85:11220-11234(2011). RN [42] RP REVIEW. RX PubMed=21239176; DOI=10.1016/j.tibs.2010.12.003; RA Smith H.C.; RT "APOBEC3G: a double agent in defense."; RL Trends Biochem. Sci. 36:239-244(2011). RN [43] RP DOMAIN CMP/DCMP DEAMINASE ZINC-BINDING. RX PubMed=21489586; DOI=10.1016/j.virol.2011.03.014; RA Li X., Ma J., Zhang Q., Zhou J., Yin X., Zhai C., You X., Yu L., RA Guo F., Zhao L., Li Z., Zeng Y., Cen S.; RT "Functional analysis of the two cytidine deaminase domains in RT APOBEC3G."; RL Virology 414:130-136(2011). RN [44] RP REVIEW. RX PubMed=22787460; DOI=10.3389/fmicb.2012.00250; RA Imahashi M., Nakashima M., Iwatani Y.; RT "Antiviral mechanism and biochemical basis of the human APOBEC3 RT family."; RL Front. Microbiol. 3:250-250(2012). RN [45] RP REVIEW. RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275; RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.; RT "Retroelements versus APOBEC3 family members: No great escape from the RT magnificent seven."; RL Front. Microbiol. 3:275-275(2012). RN [46] RP FUNCTION, AND INTERACTION WITH MOV10. RX PubMed=22791714; DOI=10.1074/jbc.M112.354001; RA Liu C., Zhang X., Huang F., Yang B., Li J., Liu B., Luo H., Zhang P., RA Zhang H.; RT "APOBEC3G inhibits microRNA-mediated repression of translation by RT interfering with the interaction between Argonaute-2 and MOV10."; RL J. Biol. Chem. 287:29373-29383(2012). RN [47] RP INTERACTION WITH HIV-1 REVERSE TRANSCRIPTASE/RIBONUCLEASE H. RX PubMed=22301159; DOI=10.1128/JVI.06594-11; RA Wang X., Ao Z., Chen L., Kobinger G., Peng J., Yao X.; RT "The cellular antiviral protein APOBEC3G interacts with HIV-1 reverse RT transcriptase and inhibits its function during viral replication."; RL J. Virol. 86:3777-3786(2012). RN [48] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AGO1; AGO2 AND RP AGO3. RX PubMed=22915799; DOI=10.1128/JVI.00595-12; RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.; RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by RT P bodies."; RL J. Virol. 86:11712-11724(2012). RN [49] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=22807680; DOI=10.1371/journal.ppat.1002800; RA Refsland E.W., Hultquist J.F., Harris R.S.; RT "Endogenous origins of HIV-1 G-to-A hypermutation and restriction in RT the nonpermissive T cell line CEM2n."; RL PLoS Pathog. 8:E1002800-E1002800(2012). RN [50] RP REVIEW. RX PubMed=22546055; DOI=10.1186/1742-4690-9-35; RA Monajemi M., Woodworth C.F., Benkaroun J., Grant M., Larijani M.; RT "Emerging complexities of APOBEC3G action on immunity and viral RT fitness during HIV infection and treatment."; RL Retrovirology 9:35-35(2012). RN [51] RP REVIEW. RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004; RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.; RT "Functions and regulation of the APOBEC family of proteins."; RL Semin. Cell Dev. Biol. 23:258-268(2012). RN [52] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=23097438; DOI=10.1128/JVI.00676-12; RA Chaipan C., Smith J.L., Hu W.S., Pathak V.K.; RT "APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and RT APOBEC3DE in human primary CD4+ t cells and macrophages."; RL J. Virol. 87:444-453(2013). RN [53] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=23152537; DOI=10.1128/JVI.02587-12; RA Gillick K., Pollpeter D., Phalora P., Kim E.Y., Wolinsky S.M., RA Malim M.H.; RT "The suppression of HIV-1 infection by APOBEC3 proteins in primary RT human CD4+ T cells is associated with the inhibition of processive RT reverse transcription as well as excessive cytidine deamination."; RL J. Virol. 87:1508-1517(2013). RN [54] RP STRUCTURE BY NMR OF 198-384 IN COMPLEX WITH ZINC, CATALYTIC ACTIVITY, RP FUNCTION, AND MUTAGENESIS OF ARG-213; ARG-215; GLU-259; TRP-285; RP ARG-313 AND ARG-320. RX PubMed=18288108; DOI=10.1038/nature06638; RA Chen K.M., Harjes E., Gross P.J., Fahmy A., Lu Y., Shindo K., RA Harris R.S., Matsuo H.; RT "Structure of the DNA deaminase domain of the HIV-1 restriction factor RT APOBEC3G."; RL Nature 452:116-119(2008). RN [55] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 197-380 IN COMPLEX WITH RP ZINC, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-213; ARG-215; RP ASN-244; TRP-285 AND TYR-315. RX PubMed=18849968; DOI=10.1038/nature07357; RA Holden L.G., Prochnow C., Chang Y.P., Bransteitter R., Chelico L., RA Sen U., Stevens R.C., Goodman M.F., Chen X.S.; RT "Crystal structure of the anti-viral APOBEC3G catalytic domain and RT functional implications."; RL Nature 456:121-124(2008). RN [56] RP STRUCTURE BY NMR OF 193-384 IN COMPLEX WITH ZINC, AND CATALYTIC RP ACTIVITY. RX PubMed=19153609; DOI=10.1038/emboj.2008.290; RA Furukawa A., Nagata T., Matsugami A., Habu Y., Sugiyama R., RA Hayashi F., Kobayashi N., Yokoyama S., Takaku H., Katahira M.; RT "Structure, interaction and real-time monitoring of the enzymatic RT reaction of wild-type APOBEC3G."; RL EMBO J. 28:440-451(2009). RN [57] RP X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 191-380. RX PubMed=22181350; DOI=10.1021/cb200440y; RA Li M., Shandilya S.M., Carpenter M.A., Rathore A., Brown W.L., RA Perkins A.L., Harki D.A., Solberg J., Hook D.J., Pandey K.K., RA Parniak M.A., Johnson J.R., Krogan N.J., Somasundaran M., Ali A., RA Schiffer C.A., Harris R.S.; RT "First-in-class small molecule inhibitors of the single-strand DNA RT cytosine deaminase APOBEC3G."; RL ACS Chem. Biol. 7:506-517(2012). CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an CC inhibitor of retrovirus replication and retrotransposon mobility CC via deaminase-dependent and -independent mechanisms. Exhibits CC potent antiviral activity against vif-deficient HIV-1. After the CC penetration of retroviral nucleocapsids into target cells of CC infection and the initiation of reverse transcription, it can CC induce the conversion of cytosine to uracil in the minus-sense CC single-strand viral DNA, leading to G-to-A hypermutations in the CC subsequent plus-strand viral DNA. The resultant detrimental levels CC of mutations in the proviral genome, along with a deamination- CC independent mechanism that works prior to the proviral CC integration, together exert efficient antiretroviral effects in CC infected target cells. Selectively targets single-stranded DNA and CC does not deaminate double-stranded DNA or single-or double- CC stranded RNA. Exhibits antiviral activity also against simian CC immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine CC infectious anemia virus (EIAV), xenotropic MuLV-related virus CC (XMRV) and simian foamy virus (SFV). May inhibit the mobility of CC LTR and non-LTR retrotransposons. CC -!- CATALYTIC ACTIVITY: Deoxycytidine + H(2)O = deoxyuridine + NH(3). CC -!- COFACTOR: Zinc. CC -!- ENZYME REGULATION: Assembly into ribonucleoprotein complexes of CC high-molecular-mass (HMM) inhibits its enzymatic activity. CC Antiviral activity is neutralized by the HIV-1 virion infectivity CC factor (VIF), that prevents its incorporation into progeny HIV-1 CC virions by both inhibiting its translation and/or by inducing its CC ubiquitination and subsequent degradation by the 26S proteasome. CC Can also be neutralized by simian immunodeficiency virus sooty CC mangabey monkey virus (SIV-sm) and chimpanzee immunodeficiency CC virus (SIV-cpz) VIF. CC -!- SUBUNIT: Homodimer. Homooligomer. Can bind RNA to form CC ribonucleoprotein complexes of high-molecular-mass (HMM) or low- CC molecular-mass (LMM). HMM is inactive and heterogeneous in protein CC composition because of binding nonselectively to cellular RNAs, CC which in turn are associated with variety of cellular proteins. CC The LMM form which is enzymatically active has few or no RNAs CC associated. Its ability to form homooligomer is distinct from its CC ability to assemble into HMM. Interacts with APOBEC3B, APOBEC3F, CC MOV10, AGO2, EIF4E, EIF4ENIF1, DCP2 and DDX6 in an RNA-dependent CC manner. Interacts with AGO1, AGO3 and PKA/PRKACA. Interacts with CC HIV-1 VIF and reverse transcriptase/ribonuclease H. Interacts with CC hepatitis B virus capsid protein. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, P-body. CC Note=Mainly cytoplasmic. Small amount are found in the nucleus. CC During HIV-1 infection, virion-encapsidated in absence of HIV-1 CC VIF. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9HC16-1; Sequence=Displayed; CC Name=3; CC IsoId=Q9HC16-3; Sequence=VSP_009588, VSP_009589; CC Note=May be due to a competing donor splice site; CC -!- TISSUE SPECIFICITY: Expressed in spleen, testes, ovary and CC peripheral blood leukocytes and CD4+ lymphocytes. Also expressed CC in non-permissive peripheral blood mononuclear cells, and several CC tumor cell lines; no expression detected in permissive lymphoid CC and non-lymphoid cell lines. Exists only in the LMM form in CC peripheral blood-derived resting CD4 T-cells and monocytes, both CC of which are refractory to HIV-1 infection. LMM is converted to a CC HMM complex when resting CD4 T-cells are activated or when CC monocytes are induced to differentiate into macrophages. This CC change correlates with increased susceptibility of these cells to CC HIV-1 infection. CC -!- INDUCTION: Up-regulated by IFN-alpha. CC -!- DOMAIN: The CMP/dCMP deaminase zinc-binding 1 domain mediates RNA CC binding, RNA-dependent oligomerization and virion incorporation CC whereas the CMP/dCMP deaminase zinc-binding 2 domain confers CC deoxycytidine deaminase activity and substrate sequence CC specificity (PubMed:17020885). CC -!- PTM: Ubiquitinated in the presence of HIV-1 VIF. Association with CC VIF targets the protein for proteolysis by the ubiquitin-dependent CC proteasome pathway. CC -!- PTM: Phosphorylation at Thr-32 reduces its binding to HIV-1 VIF CC and subsequent ubiquitination and degradation thus promoting its CC antiviral activity. CC -!- MISCELLANEOUS: Accumulation of APOBEC3G induced non-lethal CC hypermutation could contribute to the genetic variation of primate CC lentiviral populations. CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes CC found in a cluster, thought to result from gene duplication, on CC chromosome 22. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. CC -!- SIMILARITY: Contains 2 CMP/dCMP deaminase zinc-binding domains. CC -!- SEQUENCE CAUTION: CC Sequence=CAB45274.1; Type=Erroneous gene model prediction; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/apobec3g/"; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein wars - Issue 45 CC of April 2004; CC URL="http://web.expasy.org/spotlight/back_issues/045"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AK022802; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK315650; BAG38016.1; -; mRNA. DR EMBL; AF182420; AAG14956.1; -; mRNA. DR EMBL; CR456472; CAG30358.1; -; mRNA. DR EMBL; DQ147772; AAZ38722.1; -; Genomic_DNA. DR EMBL; AL022318; CAB45274.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL078641; CAI21556.1; -; Genomic_DNA. DR EMBL; AL022318; CAI21556.1; JOINED; Genomic_DNA. DR EMBL; AL022318; CAI17900.1; -; Genomic_DNA. DR EMBL; AL078641; CAI17900.1; JOINED; Genomic_DNA. DR EMBL; CH471095; EAW60292.1; -; Genomic_DNA. DR EMBL; BC024268; AAH24268.1; -; mRNA. DR EMBL; BC061914; AAH61914.1; -; mRNA. DR CCDS; CCDS13984.1; -. [Q9HC16-1] DR RefSeq; NP_068594.1; NM_021822.3. [Q9HC16-1] DR UniGene; Hs.660143; -. DR PDB; 2JYW; NMR; -; A=198-384. DR PDB; 2KBO; NMR; -; A=193-384. DR PDB; 2KEM; NMR; -; A=191-384. DR PDB; 3E1U; X-ray; 2.30 A; A=197-380. DR PDB; 3IQS; X-ray; 2.30 A; A=197-380. DR PDB; 3IR2; X-ray; 2.25 A; A/B=191-384. DR PDB; 3V4J; X-ray; 2.04 A; A/B=191-384. DR PDB; 3V4K; X-ray; 1.38 A; A/B=191-380. DR PDBsum; 2JYW; -. DR PDBsum; 2KBO; -. DR PDBsum; 2KEM; -. DR PDBsum; 3E1U; -. DR PDBsum; 3IQS; -. DR PDBsum; 3IR2; -. DR PDBsum; 3V4J; -. DR PDBsum; 3V4K; -. DR ProteinModelPortal; Q9HC16; -. DR SMR; Q9HC16; 16-193, 197-380. DR BioGrid; 121920; 11. DR BioGrid; 128319; 5. DR DIP; DIP-37519N; -. DR IntAct; Q9HC16; 2. DR MINT; MINT-1428867; -. DR STRING; 9606.ENSP00000385057; -. DR BindingDB; Q9HC16; -. DR ChEMBL; CHEMBL1741217; -. DR PhosphoSite; Q9HC16; -. DR DMDM; 44887683; -. DR MaxQB; Q9HC16; -. DR PaxDb; Q9HC16; -. DR PRIDE; Q9HC16; -. DR DNASU; 200316; -. DR DNASU; 60489; -. DR Ensembl; ENST00000407997; ENSP00000385057; ENSG00000239713. [Q9HC16-1] DR Ensembl; ENST00000452957; ENSP00000413376; ENSG00000239713. [Q9HC16-1] DR GeneID; 60489; -. DR KEGG; hsa:60489; -. DR UCSC; uc003awx.3; human. [Q9HC16-1] DR CTD; 60489; -. DR GeneCards; GC22P039437; -. DR HGNC; HGNC:17357; APOBEC3G. DR HPA; HPA001812; -. DR MIM; 607113; gene. DR neXtProt; NX_Q9HC16; -. DR PharmGKB; PA24897; -. DR eggNOG; NOG135704; -. DR HOVERGEN; HBG050434; -. DR InParanoid; Q9HC16; -. DR KO; K01500; -. DR OMA; WDPDYQE; -. DR OrthoDB; EOG75QR3Z; -. DR PhylomeDB; Q9HC16; -. DR TreeFam; TF331356; -. DR BRENDA; 3.5.4.5; 2681. DR Reactome; REACT_116125; Disease. DR ChiTaRS; APOBEC3G; human. DR EvolutionaryTrace; Q9HC16; -. DR GeneWiki; APOBEC3G; -. DR GenomeRNAi; 60489; -. DR NextBio; 65375; -. DR PRO; PR:Q9HC16; -. DR ArrayExpress; Q9HC16; -. DR Bgee; Q9HC16; -. DR CleanEx; HS_APOBEC3G; -. DR Genevestigator; Q9HC16; -. DR GO; GO:0030895; C:apolipoprotein B mRNA editing enzyme complex; TAS:HGNC. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0004126; F:cytidine deaminase activity; TAS:HGNC. DR GO; GO:0047844; F:deoxycytidine deaminase activity; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; NAS:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0016553; P:base conversion or substitution editing; TAS:HGNC. DR GO; GO:0009972; P:cytidine deamination; IDA:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IDA:HGNC. DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB. DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB. DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB. DR GO; GO:0048525; P:negative regulation of viral process; IDA:HGNC. DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:HGNC. DR GO; GO:0016032; P:viral process; TAS:Reactome. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR013158; APOBEC_N. DR InterPro; IPR016193; Cytidine_deaminase-like. DR Pfam; PF08210; APOBEC_N; 2. DR SUPFAM; SSF53927; SSF53927; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; KW Complete proteome; Cytoplasm; Host-virus interaction; Hydrolase; KW Immunity; Innate immunity; Metal-binding; Nucleus; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Ubl conjugation; Zinc. FT CHAIN 1 384 DNA dC->dU-editing enzyme APOBEC-3G. FT /FTId=PRO_0000171761. FT DOMAIN 65 100 CMP/dCMP deaminase zinc-binding 1. FT DOMAIN 257 291 CMP/dCMP deaminase zinc-binding 2. FT REGION 1 60 Essential for cytoplasmic localization. FT REGION 209 336 Necessary for homooligomerization. FT REGION 213 215 Interaction with DNA (Probable). FT REGION 313 320 Interaction with DNA (Probable). FT ACT_SITE 259 259 Proton donor (Probable). FT METAL 65 65 Zinc (By similarity). FT METAL 97 97 Zinc (By similarity). FT METAL 100 100 Zinc (By similarity). FT METAL 257 257 Zinc; catalytic. FT METAL 288 288 Zinc; catalytic. FT METAL 291 291 Zinc; catalytic. FT SITE 244 244 Interaction with DNA (Probable). FT MOD_RES 32 32 Phosphothreonine; by PKA. FT MOD_RES 218 218 Phosphothreonine; by PKA and CAMK2. FT VAR_SEQ 58 79 VYSELKYHPEMRFFHWFSKWRK -> VPPGLQSLCRQELSQ FT LGKQTTH (in isoform 3). FT /FTId=VSP_009588. FT VAR_SEQ 80 384 Missing (in isoform 3). FT /FTId=VSP_009589. FT VARIANT 186 186 H -> R (in dbSNP:rs8177832). FT /FTId=VAR_017837. FT VARIANT 256 256 R -> H (in dbSNP:rs17000736). FT /FTId=VAR_048723. FT VARIANT 275 275 Q -> E (in dbSNP:rs17496046). FT /FTId=VAR_025060. FT MUTAGEN 67 67 E->A: Loss of cytidine deaminase activity FT and significant decrease in antiviral FT activity; when associated with A-259. FT MUTAGEN 67 67 E->A: No effect on cytidine deaminase and FT antiviral activity. FT MUTAGEN 67 67 E->Q: Decreases cytidine deaminase FT activity. FT MUTAGEN 81 81 H->A: Decreases cytidine deaminase FT activity. FT MUTAGEN 85 85 E->Q: Does not decrease cytidine FT deaminase activity. FT MUTAGEN 97 97 C->A: Decreases cytidine deaminase FT activity. FT MUTAGEN 100 100 C->A,S: Decreases cytidine deaminase FT activity. FT MUTAGEN 128 128 D->K: Complete loss of VIF-induced FT degradation. FT MUTAGEN 213 213 R->A: Slightly reduces enzyme activity. FT MUTAGEN 213 213 R->E: Reduces enzyme activity. FT MUTAGEN 215 215 R->A,E: Abolishes enzyme activity. FT MUTAGEN 217 217 E->K: Modifies the spectrum of action FT against mobile genetic elements; when FT associated with K-247. FT MUTAGEN 218 218 T->A: Loss of phosphorylation. No effect FT on cytidine deaminase activity or HIV-1 FT restriction activity. FT MUTAGEN 218 218 T->E: Phosphomimetic mutant which shows FT loss of cytidine deaminase activity and FT HIV-1 restriction activity. FT MUTAGEN 221 221 C->S: Does not decrease cytidine FT deaminase activity. FT MUTAGEN 244 244 N->A: Abolishes enzyme activity. FT MUTAGEN 247 247 P->K: Modifies the spectrum of action FT against mobile genetic elements; when FT associated with K-217. FT MUTAGEN 256 256 R->E: Strongly reduces enzyme activity. FT MUTAGEN 257 257 H->A: Decreases cytidine deaminase FT activity. FT MUTAGEN 259 259 E->A: Loss of cytidine deaminase activity FT and significant decrease in antiviral FT activity. FT MUTAGEN 259 259 E->A: Loss of cytidine deaminase activity FT and significant decrease in antiviral FT activity; when associated with A-67. FT MUTAGEN 259 259 E->Q: Decreases cytidine deaminase FT activity and antiviral activity. FT MUTAGEN 285 285 W->A: Abolishes enzyme activity. FT MUTAGEN 288 288 C->A: Decreases cytidine deaminase FT activity. FT MUTAGEN 291 291 C->A,S: Decreases cytidine deaminase FT activity. FT MUTAGEN 313 313 R->A,E: Abolishes enzyme activity. FT MUTAGEN 315 315 Y->A: Abolishes enzyme activity. FT MUTAGEN 320 320 R->A: Slightly reduces enzyme activity. FT MUTAGEN 320 320 R->E: Reduces enzyme activity. FT MUTAGEN 323 323 E->Q: Does not decrease cytidine FT deaminase activity. FT CONFLICT 162 162 S -> N (in Ref. 1; no nucleotide entry). FT CONFLICT 370 370 D -> Y (in Ref. 1; no nucleotide entry). FT STRAND 195 197 FT HELIX 199 206 FT STRAND 213 217 FT STRAND 219 228 FT STRAND 231 234 FT HELIX 236 238 FT STRAND 240 243 FT STRAND 247 250 FT HELIX 258 265 FT HELIX 266 269 FT STRAND 273 275 FT STRAND 277 285 FT HELIX 289 301 FT STRAND 305 313 FT STRAND 318 320 FT HELIX 321 330 FT STRAND 334 337 FT HELIX 340 350 FT HELIX 364 379 SQ SEQUENCE 384 AA; 46408 MW; 60525DC3B7D903D6 CRC64; MKPHFRNTVE RMYRDTFSYN FYNRPILSRR NTVWLCYEVK TKGPSRPPLD AKIFRGQVYS ELKYHPEMRF FHWFSKWRKL HRDQEYEVTW YISWSPCTKC TRDMATFLAE DPKVTLTIFV ARLYYFWDPD YQEALRSLCQ KRDGPRATMK IMNYDEFQHC WSKFVYSQRE LFEPWNNLPK YYILLHIMLG EILRHSMDPP TFTFNFNNEP WVRGRHETYL CYEVERMHND TWVLLNQRRG FLCNQAPHKH GFLEGRHAEL CFLDVIPFWK LDLDQDYRVT CFTSWSPCFS CAQEMAKFIS KNKHVSLCIF TARIYDDQGR CQEGLRTLAE AGAKISIMTY SEFKHCWDTF VDHQGCPFQP WDGLDEHSQD LSGRLRAILQ NQEN // ID ABC3H_HUMAN Reviewed; 200 AA. AC Q6NTF7; B0QYP0; B0QYP1; B7TQM5; E9PF38; Q5JYL9; Q6IC87; DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 3. DT 09-JUL-2014, entry version 83. DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3H; DE EC=3.5.4.-; DE AltName: Full=APOBEC-related protein 10; DE Short=ARP-10; DE AltName: Full=Apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like 3H; DE Short=A3H; GN Name=APOBEC3H; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLU-140, AND RP ALTERNATIVE SPLICING. RX PubMed=18945781; DOI=10.1128/JVI.01665-08; RA Harari A., Ooms M., Mulder L.C., Simon V.; RT "Polymorphisms and splice variants influence the antiretroviral RT activity of human APOBEC3H."; RL J. Virol. 83:295-303(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS RP ASN-15 DEL; LEU-18; ARG-105; GLU-140 AND ASP-178. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT RP GLU-140. RC TISSUE=Astrocyte; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP REVIEW ON APOBEC FAMILY. RX PubMed=12683974; DOI=10.1016/S0168-9525(03)00054-4; RA Wedekind J.E., Dance G.S.C., Sowden M.P., Smith H.C.; RT "Messenger RNA editing in mammals: new members of the APOBEC family RT seeking roles in the family business."; RL Trends Genet. 19:207-216(2003). RN [6] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=16571802; DOI=10.1128/JVI.80.8.3853-3862.2006; RA OhAinle M., Kerns J.A., Malik H.S., Emerman M.; RT "Adaptive evolution and antiviral activity of the conserved mammalian RT cytidine deaminase APOBEC3H."; RL J. Virol. 80:3853-3862(2006). RN [7] RP FUNCTION. RX PubMed=16920826; DOI=10.1128/JVI.01123-06; RA Dang Y., Wang X., Esselman W.J., Zheng Y.-H.; RT "Identification of APOBEC3DE as another antiretroviral factor from the RT human APOBEC family."; RL J. Virol. 80:10522-10533(2006). RN [8] RP REVIEW. RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350; RA Chiu Y.L., Greene W.C.; RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing RT exogenous retroviruses and endogenous retroelements."; RL Annu. Rev. Immunol. 26:317-353(2008). RN [9] RP FUNCTION, AND CHARACTERIZATION OF VARIANTS ASN-15 DEL AND ARG-105. RX PubMed=18779051; DOI=10.1016/j.chom.2008.07.005; RA OhAinle M., Kerns J.A., Li M.M., Malik H.S., Emerman M.; RT "Antiretroelement activity of APOBEC3H was lost twice in recent human RT evolution."; RL Cell Host Microbe 4:249-259(2008). RN [10] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=18299330; DOI=10.1074/jbc.M707586200; RA Dang Y., Siew L.M., Wang X., Han Y., Lampen R., Zheng Y.H.; RT "Human cytidine deaminase APOBEC3H restricts HIV-1 replication."; RL J. Biol. Chem. 283:11606-11614(2008). RN [11] RP FUNCTION, CHARACTERIZATION OF ALLELE A3H-VAR, AND MUTAGENESIS OF RP GLU-56. RX PubMed=18827027; DOI=10.1096/fj.07-088781; RA Tan L., Sarkis P.T., Wang T., Tian C., Yu X.F.; RT "Sole copy of Z2-type human cytidine deaminase APOBEC3H has inhibitory RT activity against retrotransposons and HIV-1."; RL FASEB J. 23:279-287(2009). RN [12] RP TISSUE SPECIFICITY. RX PubMed=20308164; DOI=10.1093/nar/gkq174; RA Refsland E.W., Stenglein M.D., Shindo K., Albin J.S., Brown W.L., RA Harris R.S.; RT "Quantitative profiling of the full APOBEC3 mRNA repertoire in RT lymphocytes and tissues: implications for HIV-1 restriction."; RL Nucleic Acids Res. 38:4274-4284(2010). RN [13] RP FUNCTION IN RETROTRANSPOSITION. RX PubMed=20062055; DOI=10.1038/nsmb.1744; RA Stenglein M.D., Burns M.B., Li M., Lengyel J., Harris R.S.; RT "APOBEC3 proteins mediate the clearance of foreign DNA from human RT cells."; RL Nat. Struct. Mol. Biol. 17:222-229(2010). RN [14] RP CHARACTERIZATION OF ALLELE A3H-VAR, AND SUBCELLULAR LOCATION. RX PubMed=21653666; DOI=10.1128/JVI.00624-11; RA Li M.M., Emerman M.; RT "Polymorphism in human APOBEC3H affects a phenotype dominant for RT subcellular localization and antiviral activity."; RL J. Virol. 85:8197-8207(2011). RN [15] RP FUNCTION IN HIV-1 RESTRICTION, SUBCELLULAR LOCATION, AND ENZYME RP REGULATION. RX PubMed=21835787; DOI=10.1128/JVI.05238-11; RA Hultquist J.F., Lengyel J.A., Refsland E.W., LaRue R.S., Lackey L., RA Brown W.L., Harris R.S.; RT "Human and rhesus APOBEC3D, APOBEC3F, APOBEC3G, and APOBEC3H RT demonstrate a conserved capacity to restrict Vif-deficient HIV-1."; RL J. Virol. 85:11220-11234(2011). RN [16] RP REVIEW. RA Love R.; RT "Cytosine deaminases APOBEC3A, APOBEC3C, and APOBEC3H: Current RT understanding of their functional roles."; RL Student Perspec. Contemp. Virol. 0:0-0(2011). RN [17] RP REVIEW. RX PubMed=22912627; DOI=10.3389/fmicb.2012.00275; RA Arias J.F., Koyama T., Kinomoto M., Tokunaga K.; RT "Retroelements versus APOBEC3 family members: No great escape from the RT magnificent seven."; RL Front. Microbiol. 3:275-275(2012). RN [18] RP FUNCTION IN HTLV-1 RESTRICTION. RX PubMed=22457529; DOI=10.1128/JVI.06570-11; RA Ooms M., Krikoni A., Kress A.K., Simon V., Muenk C.; RT "APOBEC3A, APOBEC3B, and APOBEC3H haplotype 2 restrict human T- RT lymphotropic virus type 1."; RL J. Virol. 86:6097-6108(2012). RN [19] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AGO1; AGO2 AND RP AGO3. RX PubMed=22915799; DOI=10.1128/JVI.00595-12; RA Phalora P.K., Sherer N.M., Wolinsky S.M., Swanson C.M., Malim M.H.; RT "HIV-1 replication and APOBEC3 antiviral activity are not regulated by RT P bodies."; RL J. Virol. 86:11712-11724(2012). RN [20] RP REVIEW. RX PubMed=22001110; DOI=10.1016/j.semcdb.2011.10.004; RA Smith H.C., Bennett R.P., Kizilyer A., McDougall W.M., Prohaska K.M.; RT "Functions and regulation of the APOBEC family of proteins."; RL Semin. Cell Dev. Biol. 23:258-268(2012). RN [21] RP FUNCTION IN HIV-1 RESTRICTION. RX PubMed=23097438; DOI=10.1128/JVI.00676-12; RA Chaipan C., Smith J.L., Hu W.S., Pathak V.K.; RT "APOBEC3G restricts HIV-1 to a greater extent than APOBEC3F and RT APOBEC3DE in human primary CD4+ t cells and macrophages."; RL J. Virol. 87:444-453(2013). CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an CC inhibitor of retrovirus replication and retrotransposon mobility CC via deaminase-dependent and -independent mechanisms. The A3H- CC var/haplotype 2 exhibits antiviral activity against vif-deficient CC HIV-1. After the penetration of retroviral nucleocapsids into CC target cells of infection and the initiation of reverse CC transcription, it can induce the conversion of cytosine to uracil CC in the minus-sense single-strand viral DNA, leading to G-to-A CC hypermutations in the subsequent plus-strand viral DNA. The CC resultant detrimental levels of mutations in the proviral genome, CC along with a deamination-independent mechanism that works prior to CC the proviral integration, together exert efficient antiretroviral CC effects in infected target cells. Selectively targets single- CC stranded DNA and does not deaminate double-stranded DNA or single- CC or double-stranded RNA. Exhibits antiviral activity also against CC T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility CC of LTR and non-LTR retrotransposons. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- COFACTOR: Zinc (By similarity). CC -!- ENZYME REGULATION: Antiviral activity is neutralized by the HIV-1 CC virion infectivity factor (VIF), that prevents its incorporation CC into progeny virions by both inhibiting its translation and/or by CC inducing its ubiquitination and subsequent degradation by the 26S CC proteasome. CC -!- SUBUNIT: Interacts with AGO1, AGO2 and AGO3. CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, P-body. CC Note=Haplotype 1 is distributed in both the nucleus and cytoplasm, CC whereas haplotype 2 is predominantly cytoplasmic. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q6NTF7-1; Sequence=Displayed; CC Note=No experimental confirmation available; CC Name=2; CC IsoId=Q6NTF7-2; Sequence=VSP_035034; CC Name=3; CC IsoId=Q6NTF7-3; Sequence=VSP_039975; CC Name=4; CC IsoId=Q6NTF7-4; Sequence=VSP_047044; CC Note=Gene prediction based on EST data; CC -!- TISSUE SPECIFICITY: Expressed in lymphoid organs. Also detected in CC non-lymphoid tissues including lung, testis, ovary, fetal liver CC and skin. CC -!- POLYMORPHISM: There are at least 4 different haplotypes in the CC human population. The allele A3H-var/haplotype 2 encodes a more CC stable protein which is able to block HIV-1 replication. The CC displayed allele (haplotype 1) is unstable and inefficient to CC block HIV-1 replication. CC -!- MISCELLANEOUS: APOBEC3H from old world monkeys has retained its CC antiviral activity, while it is lost in other primates. CC -!- MISCELLANEOUS: It is one of seven related genes or pseudogenes CC found in a cluster, thought to result from gene duplication, on CC chromosome 22. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. CC -!- SIMILARITY: Contains 1 CMP/dCMP deaminase zinc-binding domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; FJ376613; ACK77774.1; -; mRNA. DR EMBL; CR456481; CAG30367.3; -; mRNA. DR EMBL; AL031846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC069023; AAH69023.1; -; mRNA. DR EMBL; BQ052182; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS13985.1; -. [Q6NTF7-3] DR CCDS; CCDS54530.1; -. [Q6NTF7-1] DR CCDS; CCDS54531.1; -. [Q6NTF7-2] DR CCDS; CCDS54532.1; -. [Q6NTF7-4] DR RefSeq; NP_001159474.1; NM_001166002.1. [Q6NTF7-2] DR RefSeq; NP_001159475.1; NM_001166003.1. [Q6NTF7-1] DR RefSeq; NP_861438.2; NM_181773.3. [Q6NTF7-3] DR UniGene; Hs.440515; -. DR ProteinModelPortal; Q6NTF7; -. DR SMR; Q6NTF7; 8-177. DR STRING; 9606.ENSP00000344182; -. DR PhosphoSite; Q6NTF7; -. DR DMDM; 205371798; -. DR PaxDb; Q6NTF7; -. DR PRIDE; Q6NTF7; -. DR DNASU; 164668; -. DR Ensembl; ENST00000348946; ENSP00000216123; ENSG00000100298. [Q6NTF7-2] DR Ensembl; ENST00000401756; ENSP00000385741; ENSG00000100298. [Q6NTF7-1] DR Ensembl; ENST00000421988; ENSP00000393520; ENSG00000100298. [Q6NTF7-4] DR Ensembl; ENST00000442487; ENSP00000411754; ENSG00000100298. [Q6NTF7-3] DR GeneID; 164668; -. DR KEGG; hsa:164668; -. DR UCSC; uc021wpt.1; human. [Q6NTF7-1] DR UCSC; uc021wpu.1; human. [Q6NTF7-3] DR UCSC; uc021wpv.1; human. [Q6NTF7-2] DR CTD; 164668; -. DR GeneCards; GC22P039493; -. DR HGNC; HGNC:24100; APOBEC3H. DR HPA; HPA021492; -. DR MIM; 610976; gene. DR neXtProt; NX_Q6NTF7; -. DR PharmGKB; PA162376694; -. DR eggNOG; NOG135704; -. DR HOGENOM; HOG000033754; -. DR HOVERGEN; HBG050434; -. DR InParanoid; Q6NTF7; -. DR OMA; DETQCYQ; -. DR OrthoDB; EOG7W154V; -. DR PhylomeDB; Q6NTF7; -. DR TreeFam; TF331356; -. DR GeneWiki; APOBEC3H; -. DR GenomeRNAi; 164668; -. DR NextBio; 33762998; -. DR PRO; PR:Q6NTF7; -. DR ArrayExpress; Q6NTF7; -. DR Bgee; Q6NTF7; -. DR CleanEx; HS_APOBEC3H; -. DR Genevestigator; Q6NTF7; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0004126; F:cytidine deaminase activity; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0009972; P:cytidine deamination; IDA:GOC. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0070383; P:DNA cytosine deamination; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB. DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB. DR GO; GO:0048525; P:negative regulation of viral process; IMP:UniProtKB. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR007904; APOBEC_C. DR InterPro; IPR002125; CMP_dCMP_Zn-bd. DR InterPro; IPR016193; Cytidine_deaminase-like. DR Pfam; PF05240; APOBEC_C; 1. DR Pfam; PF00383; dCMP_cyt_deam_1; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 1. PE 1: Evidence at protein level; KW Alternative splicing; Antiviral defense; Coiled coil; KW Complete proteome; Cytoplasm; Hydrolase; Immunity; Innate immunity; KW Metal-binding; Nucleus; Polymorphism; Reference proteome; Zinc. FT CHAIN 1 200 DNA dC->dU-editing enzyme APOBEC-3H. FT /FTId=PRO_0000291663. FT DOMAIN 54 88 CMP/dCMP deaminase zinc-binding. FT COILED 160 182 Potential. FT ACT_SITE 56 56 Proton donor (By similarity). FT METAL 54 54 Zinc (By similarity). FT METAL 85 85 Zinc (By similarity). FT METAL 88 88 Zinc (By similarity). FT VAR_SEQ 140 200 KFADCWENFVDHEKPLSFNPYKMLEELDKNSRAIKRRLERI FT KIPGVRAQGRYMDILCDAEV -> NSRGTCAGSLHGYIV FT (in isoform 4). FT /FTId=VSP_047044. FT VAR_SEQ 182 200 IPGVRAQGRYMDILCDAEV -> S (in isoform 2). FT /FTId=VSP_035034. FT VAR_SEQ 182 200 IPGVRAQGRYMDILCDAEV -> QS (in isoform 3). FT /FTId=VSP_039975. FT VARIANT 15 15 Missing (decreases protein stability). FT /FTId=VAR_065622. FT VARIANT 18 18 R -> L (in dbSNP:rs139293). FT /FTId=VAR_032835. FT VARIANT 105 105 G -> R (in allele A3H-Var; haplotype 2; FT allele presenting a higher expression and FT which is more effective in FT retrotransposons and HIV-1 restriction; FT increases protein stability and exhibits FT a cytoplasmic localization; FT dbSNP:rs139297). FT /FTId=VAR_032836. FT VARIANT 121 121 K -> E (in allele A3H-Var; haplotype 2; FT allele presenting a higher expression and FT more effective in retrotransposons and FT HIV-1 restriction; dbSNP:rs139298). FT /FTId=VAR_032837. FT VARIANT 121 121 K -> N (in dbSNP:rs139299). FT /FTId=VAR_032838. FT VARIANT 140 140 K -> E (in dbSNP:rs139300). FT /FTId=VAR_067444. FT VARIANT 178 178 E -> D (in allele A3H-Var; haplotype 2; FT allele presenting a higher expression and FT more effective in retrotransposons and FT HIV-1 restriction; dbSNP:rs139302). FT /FTId=VAR_032839. FT MUTAGEN 56 56 E->Q: Reduces the ability to inhibit the FT retrotransposition of LINE-1 elements. FT CONFLICT 121 121 K -> D (in Ref. 2; CAG30367). SQ SEQUENCE 200 AA; 23531 MW; 6F89E0138CC29386 CRC64; MALLTAETFR LQFNNKRRLR RPYYPRKALL CYQLTPQNGS TPTRGYFENK KKCHAEICFI NEIKSMGLDE TQCYQVTCYL TWSPCSSCAW ELVDFIKAHD HLNLGIFASR LYYHWCKPQQ KGLRLLCGSQ VPVEVMGFPK FADCWENFVD HEKPLSFNPY KMLEELDKNS RAIKRRLERI KIPGVRAQGR YMDILCDAEV // ID ABCA1_HUMAN Reviewed; 2261 AA. AC O95477; Q5VX33; Q96S56; Q96T85; Q9NQV4; Q9UN06; Q9UN07; Q9UN08; AC Q9UN09; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 09-JUL-2014, entry version 159. DE RecName: Full=ATP-binding cassette sub-family A member 1; DE AltName: Full=ATP-binding cassette transporter 1; DE Short=ABC-1; DE Short=ATP-binding cassette 1; DE AltName: Full=Cholesterol efflux regulatory protein; GN Name=ABCA1; Synonyms=ABC1, CERP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ARG-1587. RX PubMed=10884428; DOI=10.1073/pnas.97.14.7987; RA Santamarina-Fojo S., Peterson K.M., Knapper C.L., Qiu Y., RA Freeman L.A., Cheng J.-F., Osorio J., Remaley A.T., Yang X.-P., RA Haudenschild C.C., Prades C., Chimini G., Blackmon E.E., RA Francois T.L., Duverger N., Rubin E.M., Rosier M., Denefle P., RA Fredrickson D.S., Brewer H.B. Jr.; RT "Complete genomic sequence of the human ABCA1 gene: analysis of the RT human and mouse ATP-binding cassette A promoter."; RL Proc. Natl. Acad. Sci. U.S.A. 97:7987-7992(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-1587. RC TISSUE=Skin; RA Schwartz K., Lawn R.M., Wade D.P.; RT "ABCA1 gene expression and apoA-I-mediated cholesterol efflux are RT regulated by LXR."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-1587. RX PubMed=11352567; DOI=10.1006/geno.2000.6467; RA Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F.; RT "Human and mouse ABCA1 comparative sequencing and transgenesis studies RT revealing novel regulatory sequences."; RL Genomics 73:66-76(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Tanaka A.R., Abe-Dohmae S., Arakawa R., Sadanami K., Kidera A., RA Kioka N., Amachi T., Yokoyama S., Ueda K.; RT "A new topological model of functional human ABCA1-signal peptide RT cleavage and glycosylation of a large extracellular domain."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-2261, AND VARIANTS THR-1555; RP ARG-1587; PRO-1648 AND PRO-2168. RX PubMed=10092505; DOI=10.1006/bbrc.1999.0406; RA Langmann T., Klucken J., Reil M., Liebisch G., Luciani M.-F., RA Chimini G., Kaminski W.E., Schmitz G.; RT "Molecular cloning of the human ATP-binding cassette transporter 1 RT (hABC1): evidence for sterol-dependent regulation in macrophages."; RL Biochem. Biophys. Res. Commun. 257:29-33(1999). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 21-2261, AND VARIANTS RP THR-1555; ARG-1587; PRO-1648 AND PRO-2168. RX PubMed=10431238; DOI=10.1038/11921; RA Rust S., Rosier M., Funke H., Real J., Amoura Z., Piette J.-C., RA Deleuze J.-F., Brewer H.B. Jr., Duverger N., Denefle P., Assmann G.; RT "Tangier disease is caused by mutations in the gene encoding ATP- RT binding cassette transporter 1."; RL Nat. Genet. 22:352-355(1999). RN [8] RP PHOSPHORYLATION AT SER-1042 AND SER-2054. RX PubMed=12196520; DOI=10.1074/jbc.M204923200; RA See R.H., Caday-Malcolm R.A., Singaraja R.R., Zhou S., Silverston A., RA Huber M.T., Moran J., James E.R., Janoo R., Savill J.M., Rigot V., RA Zhang L.H., Wang M., Chimini G., Wellington C.L., Tafuri S.R., RA Hayden M.R.; RT "Protein kinase A site-specific phosphorylation regulates ATP-binding RT cassette A1 (ABCA1)-mediated phospholipid efflux."; RL J. Biol. Chem. 277:41835-41842(2002). RN [9] RP REPRESSION BY ZNF202. RX PubMed=11279031; DOI=10.1074/jbc.M100218200; RA Porsch-Oezcueruemez M., Langmann T., Heimerl S., Borsukova H., RA Kaminski W.E., Drobnik W., Honer C., Schumacher C., Schmitz G.; RT "The zinc finger protein 202 (ZNF202) is a transcriptional repressor RT of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene RT expression and a modulator of cellular lipid efflux."; RL J. Biol. Chem. 276:12427-12433(2001). RN [10] RP INDUCTION BY LPS. RX PubMed=12032171; RA Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.; RT "Bacterial lipopolysaccharide induces expression of ABCA1 but not RT ABCG1 via an LXR-independent pathway."; RL J. Lipid Res. 43:952-959(2002). RN [11] RP INTERACTION WITH MEGF10. RX PubMed=17205124; DOI=10.1371/journal.pone.0000120; RA Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V., RA Zhou Z., Chimini G.; RT "Cooperation between engulfment receptors: the case of ABCA1 and RT MEGF10."; RL PLoS ONE 1:E120-E120(2006). RN [12] RP REVIEW ON VARIANTS. RX PubMed=12763760; DOI=10.1161/01.ATV.0000078520.89539.77; RA Singaraja R.R., Brunham L.R., Visscher H., Kastelein J.J.P., RA Hayden M.R.; RT "Efflux and atherosclerosis: the clinical and biochemical impact of RT variations in the ABCA1 gene."; RL Arterioscler. Thromb. Vasc. Biol. 23:1322-1332(2003). RN [13] RP PALMITOYLATION AT CYS-3; CYS-23; CYS-1110 AND CYS-1111, AND RP SUBCELLULAR LOCATION. RX PubMed=19556522; DOI=10.1161/CIRCRESAHA.108.193011; RA Singaraja R.R., Kang M.H., Vaid K., Sanders S.S., Vilas G.L., RA Arstikaitis P., Coutinho J., Drisdel R.C., El-Husseini Ael D., RA Green W.N., Berthiaume L., Hayden M.R.; RT "Palmitoylation of ATP-binding cassette transporter A1 is essential RT for its trafficking and function."; RL Circ. Res. 105:138-147(2009). RN [14] RP DISULFIDE BONDS, AND SUBCELLULAR LOCATION. RX PubMed=19258317; DOI=10.1074/jbc.M900580200; RA Hozoji M., Kimura Y., Kioka N., Ueda K.; RT "Formation of two intramolecular disulfide bonds is necessary for RT ApoA-I-dependent cholesterol efflux mediated by ABCA1."; RL J. Biol. Chem. 284:11293-11300(2009). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98 AND ASN-244. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [16] RP VARIANTS HDLD2 THR-1091 AND 1893-GLU-ASP-1894 DEL. RX PubMed=10533863; DOI=10.1016/S0140-6736(99)07026-9; RA Marcil M., Brooks-Wilson A., Clee S.M., Roomp K., Zhang L.-H., Yu L., RA Collins J.A., van Dam M., Molhuizen H.O.F., Loubser O., RA Ouellette B.F.F., Sensen C.W., Fichter K., Mott S., Denis M., RA Boucher B., Pimstone S., Genest J. Jr., Kastelein J.J.P., Hayden M.R.; RT "Mutations in the ABC1 gene in familial HDL deficiency with defective RT cholesterol efflux."; RL Lancet 354:1341-1346(1999). RN [17] RP VARIANTS HDLD1 ARG-597 AND ARG-1477, AND VARIANT HDLD2 LEU-693 DEL. RX PubMed=10431236; DOI=10.1038/11905; RA Brooks-Wilson A., Marcil M., Clee S.M., Zhang L.-H., Roomp K., RA van Dam M., Yu L., Brewer C., Collins J.A., Molhuizen H.O.F., RA Loubser O., Ouelette B.F.F., Fichter K., Ashbourne-Excoffon K.J.D., RA Sensen C.W., Scherer S., Mott S., Denis M., Martindale D., RA Frohlich J., Morgan K., Koop B., Pimstone S., Kastelein J.J.P., RA Hayden M.R.; RT "Mutations in ABC1 in Tangier disease and familial high-density RT lipoprotein deficiency."; RL Nat. Genet. 22:336-345(1999). RN [18] RP VARIANTS HDLD1 SER-590; SER-935 AND VAL-937, AND VARIANTS ALA-399 AND RP MET-883. RX PubMed=10431237; DOI=10.1038/11914; RA Bodzioch M., Orso E., Klucken J., Langmann T., Boettcher A., RA Diederich W., Drobnik W., Barlage S., Buechler C., RA Porsch-Oezcueruemez M., Kaminski W.E., Hahmann H.W., Oette K., RA Rothe G., Aslanidis C., Lackner K.J., Schmitz G.; RT "The gene encoding ATP-binding cassette transporter 1 is mutated in RT Tangier disease."; RL Nat. Genet. 22:347-351(1999). RN [19] RP VARIANTS HDLD1 ARG-597; ILE-929 AND ARG-1477, AND VARIANTS HDLD2 RP LEU-693 DEL; THR-1091; 1893-GLU-ASP-1894 DEL AND LEU-2150. RX PubMed=11086027; DOI=10.1172/JCI10727; RA Clee S.M., Kastelein J.J.P., van Dam M., Marcil M., Roomp K., RA Zwarts K.Y., Collins J.A., Roelants R., Tamasawa N., Stulc T., RA Suda T., Ceska R., Boucher B., Rondeau C., DeSouich C., RA Brooks-Wilson A., Molhuizen H.O.F., Frohlich J., Genest J. Jr., RA Hayden M.R.; RT "Age and residual cholesterol efflux affect HDL cholesterol levels and RT coronary artery disease in ABCA1 heterozygotes."; RL J. Clin. Invest. 106:1263-1270(2000). RN [20] RP VARIANTS HDLD1 ASN-1289 AND HIS-1800. RX PubMed=10706591; RA Brousseau M.E., Schaefer E.J., Dupuis J., Eustace B., RA Van Eerdewegh P., Goldkamp A.L., Thurston L.M., FitzGerald M.G., RA Yasek-McKenna D., O'Neill G., Eberhart G.P., Weiffenbach B., RA Ordovas J.M., Freeman M.W., Brown R.H. Jr., Gu J.Z.; RT "Novel mutations in the gene encoding ATP-binding cassette 1 in four RT tangier disease kindreds."; RL J. Lipid Res. 41:433-441(2000). RN [21] RP VARIANT HDLD1 ASP-1046, VARIANT HDLD2 CYS-230, AND VARIANTS LYS-219; RP ILE-825; MET-883 AND ARG-1587. RX PubMed=10938021; DOI=10.1161/01.ATV.20.8.1983; RA Wang J., Burnett J.R., Near S., Young K., Zinman B., Hanley A.J.G., RA Connelly P.W., Harris S.B., Hegele R.A.; RT "Common and rare ABCA1 variants affecting plasma HDL cholesterol."; RL Arterioscler. Thromb. Vasc. Biol. 20:1983-1989(2000). RN [22] RP VARIANT HDLD1 TRP-587, AND VARIANT PRO-2168. RX PubMed=11257260; DOI=10.1016/S0021-9150(00)00587-6; RA Bertolini S., Pisciotta L., Seri M., Cusano R., Cantafora A., RA Calabresi L., Franceschini G., Ravazzolo R., Calandra S.; RT "A point mutation in ABC1 gene in a patient with severe premature RT coronary heart disease and mild clinical phenotype of Tangier RT disease."; RL Atherosclerosis 154:599-605(2001). RN [23] RP VARIANTS LYS-219; MET-883 AND ASP-1172. RX PubMed=11257261; DOI=10.1016/S0021-9150(00)00722-X; RA Brousseau M.E., Bodzioch M., Schaefer E.J., Goldkamp A.L., Kielar D., RA Probst M., Ordovas J.M., Aslanidis C., Lackner K.J., RA Bloomfield Rubins H., Collins D., Robins S.J., Wilson P.W.F., RA Schmitz G.; RT "Common variants in the gene encoding ATP-binding cassette transporter RT 1 in men with low HDL cholesterol levels and coronary heart disease."; RL Atherosclerosis 154:607-611(2001). RN [24] RP VARIANT HDLD1 LEU-1506. RX PubMed=11476961; DOI=10.1016/S0925-4439(01)00053-9; RA Lapicka-Bodzioch K., Bodzioch M., Kruell M., Kielar D., Probst M., RA Kiec B., Andrikovics H., Boettcher A., Hubacek J., Aslanidis C., RA Suttorp N., Schmitz G.; RT "Homogeneous assay based on 52 primer sets to scan for mutations of RT the ABCA1 gene and its application in genetic analysis of a new RT patient with familial high-density lipoprotein deficiency syndrome."; RL Biochim. Biophys. Acta 1537:42-48(2001). RN [25] RP VARIANTS HDLD1 ASN-1289 AND TRP-2081, AND VARIANT LYS-219. RX PubMed=11476965; DOI=10.1016/S0925-4439(01)00058-8; RA Huang W., Moriyama K., Koga T., Hua H., Ageta M., Kawabata S., RA Mawatari K., Imamura T., Eto T., Kawamura M., Teramoto T., Sasaki J.; RT "Novel mutations in ABCA1 gene in Japanese patients with Tangier RT disease and familial high density lipoprotein deficiency with coronary RT heart disease."; RL Biochim. Biophys. Acta 1537:71-78(2001). RN [26] RP VARIANTS LYS-219; ALA-399; MET-771; PRO-774; ASN-776; ILE-825; RP MET-883; ASP-1172; ARG-1587 AND CYS-1731. RX PubMed=11238261; DOI=10.1161/01.CIR.103.9.1198; RA Clee S.M., Zwinderman A.H., Engert J.C., Zwarts K.Y., RA Molhuizen H.O.F., Roomp K., Jukema J.W., van Wijland M., van Dam M., RA Hudson T.J., Brooks-Wilson A., Genest J. Jr., Kastelein J.J.P., RA Hayden M.R.; RT "Common genetic variation in ABCA1 is associated with altered RT lipoprotein levels and a modified risk for coronary artery disease."; RL Circulation 103:1198-1205(2001). RN [27] RP VARIANT HDLD2 LEU-85. RX PubMed=12204794; DOI=10.1016/S0021-9150(02)00106-5; RA Hong S.H., Rhyne J., Zeller K., Miller M.; RT "ABCA1(Alabama): a novel variant associated with HDL deficiency and RT premature coronary artery disease."; RL Atherosclerosis 164:245-250(2002). RN [28] RP VARIANTS HDLD2 TYR-1099 AND SER-2009. RX PubMed=12009425; DOI=10.1016/S0925-4439(02)00066-2; RA Hong S.H., Rhyne J., Zeller K., Miller M.; RT "Novel ABCA1 compound variant associated with HDL cholesterol RT deficiency."; RL Biochim. Biophys. Acta 1587:60-64(2002). RN [29] RP VARIANT HDLD1 THR-255, AND VARIANT ATHEROSCLEROSIS ASP-1611. RX PubMed=11785958; DOI=10.1006/bbrc.2001.6219; RA Nishida Y., Hirano K., Tsukamoto K., Nagano M., Ikegami C., Roomp K., RA Ishihara M., Sakane N., Zhang Z., Tsujii K., Matsuyama A., Ohama T., RA Matsuura F., Ishigami M., Sakai N., Hiraoka H., Hattori H., RA Wellington C., Yoshida Y., Misugi S., Hayden M.R., Egashira T., RA Yamashita S., Matsuzawa Y.; RT "Expression and functional analyses of novel mutations of ATP-binding RT cassette transporter-1 in Japanese patients with high-density RT lipoprotein deficiency."; RL Biochem. Biophys. Res. Commun. 290:713-721(2002). RN [30] RP VARIANT HDLD1 LEU-590. RX PubMed=12407001; RA Hong S.H., Riley W., Rhyne J., Friel G., Miller M.; RT "Lack of association between increased carotid intima-media thickening RT and decreased HDL-cholesterol in a family with a novel ABCA1 variant, RT G2265T."; RL Clin. Chem. 48:2066-2070(2002). RN [31] RP VARIANTS HDLD1 HIS-935 AND SER-935. RX PubMed=12111381; DOI=10.1007/s100380200044; RA Guo Z., Inazu A., Yu W., Suzumura T., Okamoto M., Nohara A., RA Higashikata T., Sano R., Wakasugi K., Hayakawa T., Yoshida K., RA Suehiro T., Schmitz G., Mabuchi H.; RT "Double deletions and missense mutations in the first nucleotide- RT binding fold of the ATP-binding cassette transporter A1 (ABCA1) gene RT in Japanese patients with Tangier disease."; RL J. Hum. Genet. 47:325-329(2002). RN [32] RP VARIANT HDLD1 TRP-1680. RX PubMed=12111371; DOI=10.1007/s100380200051; RA Ishii J., Nagano M., Kujiraoka T., Ishihara M., Egashira T., RA Takada D., Tsuji M., Hattori H., Emi M.; RT "Clinical variant of Tangier disease in Japan: mutation of the ABCA1 RT gene in hypoalphalipoproteinemia with corneal lipidosis."; RL J. Hum. Genet. 47:366-369(2002). RN [33] RP VARIANT HDLD1 GLN-1851. RX PubMed=14576201; DOI=10.1161/01.RES.0000102957.84247.8F; RA Hong S.H., Rhyne J., Miller M.; RT "Novel polypyrimidine variation (IVS46: del T -39._.-46) in ABCA1 RT causes exon skipping and contributes to HDL cholesterol deficiency in RT a family with premature coronary disease."; RL Circ. Res. 93:1006-1012(2003). RN [34] RP VARIANTS ILE-825 AND MET-883, AND ASSOCIATION OF VARIANTS ILE-825 AND RP MET-883 WITH HIGHER PLASMA HDL CHOLESTEROL. RX PubMed=12709788; DOI=10.1007/s00439-003-0943-3; RA Tan J.H., Low P.S., Tan Y.S., Tong M.C., Saha N., Yang H., Heng C.K.; RT "ABCA1 gene polymorphisms and their associations with coronary artery RT disease and plasma lipids in males from three ethnic populations in RT Singapore."; RL Hum. Genet. 113:106-117(2003). RN [35] RP VARIANTS LYS-219; MET-771; ILE-825; MET-883; ASP-1172; PHE-1181 AND RP ARG-1587. RX PubMed=12966036; DOI=10.1093/hmg/ddg314; RA Morabia A., Cayanis E., Costanza M.C., Ross B.M., Flaherty M.S., RA Alvin G.B., Das K., Gilliam T.C.; RT "Association of extreme blood lipid profile phenotypic variation with RT 11 reverse cholesterol transport genes and 10 non-genetic RT cardiovascular disease risk factors."; RL Hum. Mol. Genet. 12:2733-2743(2003). RN [36] RP VARIANT LYS-219. RX PubMed=12624133; DOI=10.1136/jmg.40.3.163; RA Cenarro A., Artieda M., Castillo S., Mozas P., Reyes G., Tejedor D., RA Alonso R., Mata P., Pocovi M., Civeira F.; RT "A common variant in the ABCA1 gene is associated with a lower risk RT for premature coronary heart disease in familial RT hypercholesterolaemia."; RL J. Med. Genet. 40:163-168(2003). RN [37] RP VARIANTS HDLD1 LEU-590; ARG-840 AND CYS-1068, AND VARIANTS MET-771; RP SER-2163 AND ILE-2244. RX PubMed=15262183; DOI=10.1016/j.atherosclerosis.2004.02.019; RA Probst M.C., Thumann H., Aslanidis C., Langmann T., Buechler C., RA Patsch W., Baralle F.E., Dallinga-Thie G.M., Geisel J., Keller C., RA Menys V.C., Schmitz G.; RT "Screening for functional sequence variations and mutations in RT ABCA1."; RL Atherosclerosis 175:269-279(2004). RN [38] RP VARIANTS HDLD1 LYS-284; CYS-482; HIS-1800; SER-1901 AND HIS-2196. RX PubMed=15019541; DOI=10.1016/j.atherosclerosis.2003.11.009; RA Pisciotta L., Hamilton-Craig I., Tarugi P., Bellocchio A., Fasano T., RA Alessandrini P., Bon G.B., Siepi D., Mannarino E., Cattin L., RA Averna M., Cefalu A.B., Cantafora A., Calandra S., Bertolini S.; RT "Familial HDL deficiency due to ABCA1 gene mutations with or without RT other genetic lipoprotein disorders."; RL Atherosclerosis 172:309-320(2004). RN [39] RP VARIANTS HDLD1 PHE-1379 AND ASP-1704, AND CHARACTERIZATION OF VARIANTS RP HDLD1 PHE-1379 AND ASP-1704. RX PubMed=15158913; DOI=10.1016/j.bbadis.2004.01.007; RA Albrecht C., Baynes K., Sardini A., Schepelmann S., Eden E.R., RA Davies S.W., Higgins C.F., Feher M.D., Owen J.S., Soutar A.K.; RT "Two novel missense mutations in ABCA1 result in altered trafficking RT and cause severe autosomal recessive HDL deficiency."; RL Biochim. Biophys. Acta 1689:47-57(2004). RN [40] RP VARIANT HDLD1 HIS-1800, AND VARIANTS LYS-219; CYS-364; MET-771; RP PRO-774; ASN-776; ILE-825; MET-883; SER-1065; ASP-1172; VAL-1216 AND RP ARG-1587. RX PubMed=15520867; DOI=10.1172/JCI20361; RA Frikke-Schmidt R., Nordestgaard B.G., Jensen G.B., Tybjaerg-Hansen A.; RT "Genetic variation in ABC transporter A1 contributes to HDL RT cholesterol in the general population."; RL J. Clin. Invest. 114:1343-1353(2004). RN [41] RP VARIANT HDLD1 HIS-1800, AND VARIANTS ALA-248; GLN-401; TRP-496; RP SER-590; GLN-638; SER-774; GLY-815; PHE-1181; THR-1341; GLY-1376; RP GLN-1615; THR-1670; GLN-1680 AND GLU-2243. RX PubMed=15297675; DOI=10.1126/science.1099870; RA Cohen J.C., Kiss R.S., Pertsemlidis A., Marcel Y.L., McPherson R., RA Hobbs H.H.; RT "Multiple rare alleles contribute to low plasma levels of HDL RT cholesterol."; RL Science 305:869-872(2004). RN [42] RP VARIANT SCOTT SYNDROME GLN-1925, AND CHARACTERIZATION OF VARIANT SCOTT RP SYNDROME GLN-1925. RX PubMed=15790791; DOI=10.1182/blood-2004-05-2056; RA Albrecht C., McVey J.H., Elliott J.I., Sardini A., Kasza I., RA Mumford A.D., Naoumova R.P., Tuddenham E.G., Szabo K., Higgins C.F.; RT "A novel missense mutation in ABCA1 results in altered protein RT trafficking and reduced phosphatidylserine translocation in a patient RT with Scott syndrome."; RL Blood 106:542-549(2005). RN [43] RP VARIANT ASN-776, AND ASSOCIATION OF VARIANT ASN-776 WITH INCREASED RP RISK OF ISCHEMIC HEART DISEASE. RX PubMed=16226177; DOI=10.1016/j.jacc.2005.06.066; RA Frikke-Schmidt R., Nordestgaard B.G., Schnohr P., Steffensen R., RA Tybjaerg-Hansen A.; RT "Mutation in ABCA1 predicted risk of ischemic heart disease in the RT Copenhagen City Heart Study Population."; RL J. Am. Coll. Cardiol. 46:1516-1520(2005). RN [44] RP VARIANT HDLD2 TRP-1897. RX PubMed=15722566; DOI=10.1194/jlr.D400038-JLR200; RA Fasano T., Bocchi L., Pisciotta L., Bertolini S., Calandra S.; RT "Denaturing high-performance liquid chromatography in the detection of RT ABCA1 gene mutations in familial HDL deficiency."; RL J. Lipid Res. 46:817-822(2005). RN [45] RP VARIANTS [LARGE SCALE ANALYSIS] ASP-210; TYR-917; THR-1407 AND RP THR-2109. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: cAMP-dependent and sulfonylurea-sensitive anion CC transporter. Key gatekeeper influencing intracellular cholesterol CC transport. CC -!- SUBUNIT: Interacts with MEGF10. CC -!- INTERACTION: CC P02647:APOA1; NbExp=4; IntAct=EBI-784112, EBI-701692; CC P60953:CDC42; NbExp=2; IntAct=EBI-784112, EBI-81752; CC Q13424:SNTA1; NbExp=2; IntAct=EBI-784112, EBI-717191; CC Q13884:SNTB1; NbExp=3; IntAct=EBI-784112, EBI-295843; CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Widely expressed, but most abundant in CC macrophages. CC -!- INDUCTION: By bacterial lipopolysaccharides (LPS). LPS regulates CC expression through a liver X receptor (LXR) -independent CC mechanism. Repressed by ZNF202. CC -!- DOMAIN: Multifunctional polypeptide with two homologous halves, CC each containing a hydrophobic membrane-anchoring domain and an ATP CC binding cassette (ABC) domain. CC -!- PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux. CC -!- PTM: Palmitoylation by DHHC8 is essential for membrane CC localization. CC -!- POLYMORPHISM: Genetic variations in ABCA1 define the high density CC lipoprotein cholesterol level quantitative trait locus 13 CC (HDLCQ13) [MIM:600046]. CC -!- DISEASE: High density lipoprotein deficiency 1 (HDLD1) CC [MIM:205400]: Recessive disorder characterized by absence of high CC density lipoprotein (HDL) cholesterol from plasma, accumulation of CC cholesteryl esters, premature coronary artery disease (CAD), CC hepatosplenomegaly, recurrent peripheral neuropathy and CC progressive muscle wasting and weakness. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- DISEASE: High density lipoprotein deficiency 2 (HDLD2) CC [MIM:604091]: Inherited as autosomal dominant trait. It is CC characterized by moderately low HDL cholesterol, predilection CC toward premature coronary artery disease (CAD) and a reduction in CC cellular cholesterol efflux. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA CC family. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC -!- SEQUENCE CAUTION: CC Sequence=AAD49849.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=CAA10005.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and CC polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=ABCA1"; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=O95477"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF275948; AAF86276.1; -; Genomic_DNA. DR EMBL; AL353685; CAH72444.1; -; Genomic_DNA. DR EMBL; AL359846; CAH72444.1; JOINED; Genomic_DNA. DR EMBL; AL359846; CAH73579.1; -; Genomic_DNA. DR EMBL; AL353685; CAH73579.1; JOINED; Genomic_DNA. DR EMBL; AF285167; AAF98175.1; -; mRNA. DR EMBL; AF287262; AAK43526.1; -; Genomic_DNA. DR EMBL; AB055982; BAB63210.1; -; mRNA. DR EMBL; AJ012376; CAA10005.1; ALT_INIT; mRNA. DR EMBL; AF165281; AAD49849.1; ALT_INIT; mRNA. DR EMBL; AF165286; AAD49851.1; -; Genomic_DNA. DR EMBL; AF165282; AAD49851.1; JOINED; Genomic_DNA. DR EMBL; AF165283; AAD49851.1; JOINED; Genomic_DNA. DR EMBL; AF165284; AAD49851.1; JOINED; Genomic_DNA. DR EMBL; AF165285; AAD49851.1; JOINED; Genomic_DNA. DR EMBL; AF165306; AAD49852.1; -; Genomic_DNA. DR EMBL; AF165287; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165288; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165289; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165290; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165291; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165292; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165293; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165294; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165295; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165296; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165297; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165298; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165299; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165300; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165301; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165302; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165303; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165304; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165305; AAD49852.1; JOINED; Genomic_DNA. DR EMBL; AF165309; AAD49854.1; -; Genomic_DNA. DR EMBL; AF165307; AAD49854.1; JOINED; Genomic_DNA. DR EMBL; AF165308; AAD49854.1; JOINED; Genomic_DNA. DR EMBL; AF165310; AAD49853.1; -; Genomic_DNA. DR CCDS; CCDS6762.1; -. DR RefSeq; NP_005493.2; NM_005502.3. DR UniGene; Hs.659274; -. DR ProteinModelPortal; O95477; -. DR BioGrid; 106537; 24. DR DIP; DIP-29211N; -. DR IntAct; O95477; 17. DR MINT; MINT-239561; -. DR ChEMBL; CHEMBL2362986; -. DR DrugBank; DB00171; Adenosine triphosphate. DR DrugBank; DB01016; Glibenclamide. DR TCDB; 3.A.1.211.14; the atp-binding cassette (abc) superfamily. DR PhosphoSite; O95477; -. DR MaxQB; O95477; -. DR PaxDb; O95477; -. DR PRIDE; O95477; -. DR Ensembl; ENST00000374736; ENSP00000363868; ENSG00000165029. DR GeneID; 19; -. DR KEGG; hsa:19; -. DR UCSC; uc004bcl.3; human. DR CTD; 19; -. DR GeneCards; GC09M107543; -. DR HGNC; HGNC:29; ABCA1. DR MIM; 205400; phenotype. DR MIM; 600046; gene+phenotype. DR MIM; 604091; phenotype. DR neXtProt; NX_O95477; -. DR Orphanet; 425; Apolipoprotein A-I deficiency. DR Orphanet; 31150; Tangier disease. DR PharmGKB; PA24373; -. DR eggNOG; COG1131; -. DR HOVERGEN; HBG050436; -. DR InParanoid; O95477; -. DR KO; K05641; -. DR OMA; FSMRSWS; -. DR OrthoDB; EOG78D7J6; -. DR PhylomeDB; O95477; -. DR TreeFam; TF105191; -. DR Reactome; REACT_111217; Metabolism. DR SignaLink; O95477; -. DR ChiTaRS; ABCA1; human. DR GeneWiki; ABCA1; -. DR GenomeRNAi; 19; -. DR NextBio; 51; -. DR PRO; PR:O95477; -. DR ArrayExpress; O95477; -. DR Bgee; O95477; -. DR Genevestigator; O95477; -. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0030139; C:endocytic vesicle; IDA:BHF-UCL. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL. DR GO; GO:0045121; C:membrane raft; IDA:BHF-UCL. DR GO; GO:0045335; C:phagocytic vesicle; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008509; F:anion transmembrane transporter activity; ISS:BHF-UCL. DR GO; GO:0034186; F:apolipoprotein A-I binding; IPI:BHF-UCL. DR GO; GO:0034188; F:apolipoprotein A-I receptor activity; IDA:BHF-UCL. DR GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL. DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0015485; F:cholesterol binding; IC:BHF-UCL. DR GO; GO:0017127; F:cholesterol transporter activity; IDA:BHF-UCL. DR GO; GO:0005543; F:phospholipid binding; IC:BHF-UCL. DR GO; GO:0005548; F:phospholipid transporter activity; IDA:BHF-UCL. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0031267; F:small GTPase binding; IPI:BHF-UCL. DR GO; GO:0019905; F:syntaxin binding; IPI:BHF-UCL. DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IDA:GOC. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0071397; P:cellular response to cholesterol; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl. DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL. DR GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL. DR GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL. DR GO; GO:0016197; P:endosomal transport; IDA:BHF-UCL. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0034380; P:high-density lipoprotein particle assembly; IMP:BHF-UCL. DR GO; GO:0050702; P:interleukin-1 beta secretion; IMP:BHF-UCL. DR GO; GO:0032367; P:intracellular cholesterol transport; IMP:BHF-UCL. DR GO; GO:0042157; P:lipoprotein metabolic process; TAS:Reactome. DR GO; GO:0007040; P:lysosome organization; IDA:BHF-UCL. DR GO; GO:0010887; P:negative regulation of cholesterol storage; TAS:BHF-UCL. DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; TAS:BHF-UCL. DR GO; GO:0002790; P:peptide secretion; IEA:Ensembl. DR GO; GO:0006911; P:phagocytosis, engulfment; IEA:Ensembl. DR GO; GO:0033700; P:phospholipid efflux; IDA:BHF-UCL. DR GO; GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL. DR GO; GO:0045332; P:phospholipid translocation; IEA:Ensembl. DR GO; GO:0060155; P:platelet dense granule organization; IMP:BHF-UCL. DR GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IMP:BHF-UCL. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl. DR GO; GO:0006497; P:protein lipidation; IEA:Ensembl. DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; IMP:BHF-UCL. DR GO; GO:0042493; P:response to drug; IEA:Ensembl. DR GO; GO:0034616; P:response to laminar fluid shear stress; IEP:BHF-UCL. DR GO; GO:0055098; P:response to low-density lipoprotein particle; IEP:BHF-UCL. DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl. DR GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR026082; ABC_A. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR19229; PTHR19229; 1. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW Atherosclerosis; ATP-binding; Cholesterol metabolism; KW Complete proteome; Disease mutation; Disulfide bond; Glycoprotein; KW Lipid metabolism; Lipoprotein; Membrane; Nucleotide-binding; KW Palmitate; Phosphoprotein; Polymorphism; Reference proteome; Repeat; KW Steroid metabolism; Sterol metabolism; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 2261 ATP-binding cassette sub-family A member FT 1. FT /FTId=PRO_0000093288. FT TRANSMEM 22 42 Helical; (Potential). FT TOPO_DOM 43 639 Extracellular. FT TRANSMEM 640 660 Helical; (Potential). FT TRANSMEM 683 703 Helical; (Potential). FT TRANSMEM 716 736 Helical; (Potential). FT TRANSMEM 745 765 Helical; (Potential). FT TRANSMEM 777 797 Helical; (Potential). FT TRANSMEM 827 847 Helical; (Potential). FT TRANSMEM 1041 1057 Helical; (Potential). FT TRANSMEM 1351 1371 Helical; (Potential). FT TOPO_DOM 1372 1656 Extracellular. FT TRANSMEM 1657 1677 Helical; (Potential). FT TRANSMEM 1703 1723 Helical; (Potential). FT TRANSMEM 1735 1755 Helical; (Potential). FT TRANSMEM 1768 1788 Helical; (Potential). FT TRANSMEM 1802 1822 Helical; (Potential). FT TRANSMEM 1852 1872 Helical; (Potential). FT DOMAIN 899 1131 ABC transporter 1. FT DOMAIN 1912 2144 ABC transporter 2. FT NP_BIND 933 940 ATP 1 (Potential). FT NP_BIND 1946 1953 ATP 2 (Potential). FT MOD_RES 1042 1042 Phosphoserine; by PKA. FT MOD_RES 1296 1296 Phosphoserine (By similarity). FT MOD_RES 2054 2054 Phosphoserine; by PKA. FT LIPID 3 3 S-palmitoyl cysteine. FT LIPID 23 23 S-palmitoyl cysteine. FT LIPID 1110 1110 S-palmitoyl cysteine. FT LIPID 1111 1111 S-palmitoyl cysteine. FT CARBOHYD 14 14 N-linked (GlcNAc...) (Potential). FT CARBOHYD 98 98 N-linked (GlcNAc...). FT CARBOHYD 151 151 N-linked (GlcNAc...) (Potential). FT CARBOHYD 161 161 N-linked (GlcNAc...) (Potential). FT CARBOHYD 196 196 N-linked (GlcNAc...) (Potential). FT CARBOHYD 244 244 N-linked (GlcNAc...). FT CARBOHYD 292 292 N-linked (GlcNAc...) (Potential). FT CARBOHYD 337 337 N-linked (GlcNAc...) (Potential). FT CARBOHYD 349 349 N-linked (GlcNAc...) (Potential). FT CARBOHYD 400 400 N-linked (GlcNAc...) (Potential). FT CARBOHYD 478 478 N-linked (GlcNAc...) (Potential). FT CARBOHYD 489 489 N-linked (GlcNAc...) (Potential). FT CARBOHYD 521 521 N-linked (GlcNAc...) (Potential). FT CARBOHYD 820 820 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1144 1144 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1294 1294 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1453 1453 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1504 1504 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1637 1637 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2044 2044 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2238 2238 N-linked (GlcNAc...) (Potential). FT DISULFID 75 309 FT DISULFID 1463 1477 FT VARIANT 85 85 P -> L (in HDLD2; Alabama; FT dbSNP:rs145183203). FT /FTId=VAR_017529. FT VARIANT 210 210 E -> D (in a colorectal cancer sample; FT somatic mutation). FT /FTId=VAR_035724. FT VARIANT 219 219 R -> K (common polymorphism; associated FT with a decreased severity of CAD; FT dbSNP:rs2230806). FT /FTId=VAR_012618. FT VARIANT 230 230 R -> C (in HDLD2; dbSNP:rs9282541). FT /FTId=VAR_012619. FT VARIANT 248 248 P -> A. FT /FTId=VAR_062481. FT VARIANT 255 255 A -> T (in HDLD1; deficient cellular FT cholesterol efflux). FT /FTId=VAR_012620. FT VARIANT 284 284 E -> K (in HDLD1). FT /FTId=VAR_062482. FT VARIANT 364 364 S -> C. FT /FTId=VAR_062483. FT VARIANT 399 399 V -> A (in dbSNP:rs9282543). FT /FTId=VAR_009145. FT VARIANT 401 401 K -> Q. FT /FTId=VAR_062484. FT VARIANT 482 482 Y -> C (in HDLD1). FT /FTId=VAR_062485. FT VARIANT 496 496 R -> W (associated with increased plasma FT HDL cholesterol; dbSNP:rs147675550). FT /FTId=VAR_062486. FT VARIANT 587 587 R -> W (in HDLD1; dbSNP:rs2853574). FT /FTId=VAR_009146. FT VARIANT 590 590 W -> L (in HDLD1). FT /FTId=VAR_062487. FT VARIANT 590 590 W -> S (in HDLD1). FT /FTId=VAR_009147. FT VARIANT 597 597 Q -> R (in HDLD1; dbSNP:rs2853578). FT /FTId=VAR_009148. FT VARIANT 638 638 R -> Q (associated with reduced plasma FT HDL cholesterol). FT /FTId=VAR_062488. FT VARIANT 693 693 Missing (in HDLD2). FT /FTId=VAR_009149. FT VARIANT 771 771 V -> M (associated with HDL cholesterol; FT dbSNP:rs2066718). FT /FTId=VAR_012621. FT VARIANT 774 774 T -> P (in dbSNP:rs35819696). FT /FTId=VAR_012622. FT VARIANT 774 774 T -> S. FT /FTId=VAR_062489. FT VARIANT 776 776 K -> N (may be associated with increased FT risk of ischemic heart disease; FT dbSNP:rs138880920). FT /FTId=VAR_012623. FT VARIANT 815 815 E -> G (associated with reduced plasma FT HDL cholesterol; dbSNP:rs145582736). FT /FTId=VAR_062490. FT VARIANT 825 825 V -> I (associated with higher plasma FT cholesterol; dbSNP:rs2066715). FT /FTId=VAR_012624. FT VARIANT 840 840 W -> R (in HDLD1). FT /FTId=VAR_062491. FT VARIANT 883 883 I -> M (associated with higher plasma FT cholesterol; dbSNP:rs2066714). FT /FTId=VAR_012625. FT VARIANT 917 917 D -> Y (in a colorectal cancer sample; FT somatic mutation). FT /FTId=VAR_035725. FT VARIANT 929 929 T -> I (in HDLD1). FT /FTId=VAR_012626. FT VARIANT 935 935 N -> H (in HDLD1; dbSNP:rs28937314). FT /FTId=VAR_037968. FT VARIANT 935 935 N -> S (in HDLD1; dbSNP:rs28937313). FT /FTId=VAR_009150. FT VARIANT 937 937 A -> V (in HDLD1). FT /FTId=VAR_009151. FT VARIANT 1046 1046 A -> D (in HDLD1). FT /FTId=VAR_012627. FT VARIANT 1054 1054 V -> I (in dbSNP:rs13306072). FT /FTId=VAR_037969. FT VARIANT 1065 1065 P -> S. FT /FTId=VAR_062492. FT VARIANT 1068 1068 R -> C (in HDLD1). FT /FTId=VAR_062493. FT VARIANT 1091 1091 M -> T (in HDLD2). FT /FTId=VAR_012628. FT VARIANT 1099 1099 D -> Y (in HDLD2; dbSNP:rs28933692). FT /FTId=VAR_017530. FT VARIANT 1172 1172 E -> D (associated with premature FT coronary heart disease; FT dbSNP:rs33918808). FT /FTId=VAR_012629. FT VARIANT 1181 1181 S -> F (associated with reduced plasma FT HDL cholesterol; dbSNP:rs76881554). FT /FTId=VAR_017016. FT VARIANT 1216 1216 G -> V. FT /FTId=VAR_062494. FT VARIANT 1289 1289 D -> N (in HDLD1). FT /FTId=VAR_009152. FT VARIANT 1341 1341 R -> T (associated with reduced plasma FT HDL cholesterol; dbSNP:rs147743782). FT /FTId=VAR_062495. FT VARIANT 1376 1376 S -> G. FT /FTId=VAR_062496. FT VARIANT 1379 1379 L -> F (in HDLD1; the mutant protein is FT retained in the endoplasmic reticulum FT while the wild-type protein is located at FT the plasma membrane). FT /FTId=VAR_062497. FT VARIANT 1407 1407 A -> T (in a colorectal cancer sample; FT somatic mutation). FT /FTId=VAR_035726. FT VARIANT 1477 1477 C -> R (in HDLD1). FT /FTId=VAR_009153. FT VARIANT 1506 1506 S -> L (in HDLD1). FT /FTId=VAR_012630. FT VARIANT 1517 1517 I -> R (in HDLD1). FT /FTId=VAR_009154. FT VARIANT 1555 1555 I -> T (in dbSNP:rs1997618). FT /FTId=VAR_012638. FT VARIANT 1587 1587 K -> R (associated with HDL cholesterol; FT dbSNP:rs2230808). FT /FTId=VAR_012631. FT VARIANT 1611 1611 N -> D (probable disease-associated FT mutation; associated with FT atherosclerosis; deficient cellular FT cholesterol efflux). FT /FTId=VAR_012632. FT VARIANT 1615 1615 R -> Q (associated with reduced plasma FT HDL cholesterol). FT /FTId=VAR_062498. FT VARIANT 1648 1648 L -> P (in dbSNP:rs1883024). FT /FTId=VAR_012639. FT VARIANT 1670 1670 A -> T (associated with reduced plasma FT HDL cholesterol). FT /FTId=VAR_062499. FT VARIANT 1680 1680 R -> Q (associated with increased plasma FT HDL cholesterol; dbSNP:rs150125857). FT /FTId=VAR_062500. FT VARIANT 1680 1680 R -> W (in HDLD1; dbSNP:rs137854498). FT /FTId=VAR_037970. FT VARIANT 1704 1704 V -> D (in HDLD1; the mutant protein is FT retained in the endoplasmic reticulum FT while the wild-type protein is located at FT the plasma membrane). FT /FTId=VAR_062501. FT VARIANT 1731 1731 S -> C. FT /FTId=VAR_012633. FT VARIANT 1800 1800 N -> H (in HDLD1). FT /FTId=VAR_009155. FT VARIANT 1851 1851 R -> Q (in HDLD1). FT /FTId=VAR_062502. FT VARIANT 1893 1894 Missing (in HDLD2). FT /FTId=VAR_012634. FT VARIANT 1897 1897 R -> W (in HDLD2; uncertain pathological FT significance). FT /FTId=VAR_062503. FT VARIANT 1901 1901 R -> S (in HDLD1). FT /FTId=VAR_062504. FT VARIANT 1925 1925 R -> Q (in Scott syndrome; shows impaired FT trafficking of the mutant protein to the FT plasma membrane; dbSNP:rs142688906). FT /FTId=VAR_062505. FT VARIANT 2009 2009 F -> S (in HDLD2). FT /FTId=VAR_037971. FT VARIANT 2081 2081 R -> W (in HDLD1). FT /FTId=VAR_012635. FT VARIANT 2109 2109 A -> T (in a colorectal cancer sample; FT somatic mutation). FT /FTId=VAR_035727. FT VARIANT 2150 2150 P -> L (in HDLD2). FT /FTId=VAR_012636. FT VARIANT 2163 2163 F -> S (could be associated with reduced FT plasma HDL cholesterol). FT /FTId=VAR_062506. FT VARIANT 2168 2168 L -> P (in dbSNP:rs2853577). FT /FTId=VAR_012637. FT VARIANT 2196 2196 Q -> H (in HDLD1). FT /FTId=VAR_062507. FT VARIANT 2243 2243 D -> E (in dbSNP:rs34879708). FT /FTId=VAR_062508. FT VARIANT 2244 2244 V -> I (could be associated with reduced FT plasma HDL cholesterol; FT dbSNP:rs144588452). FT /FTId=VAR_062509. FT CONFLICT 793 793 Y -> C (in Ref. 3; AAK43526). FT CONFLICT 831 831 D -> N (in Ref. 3; AAK43526). FT CONFLICT 1005 1005 E -> K (in Ref. 3; AAK43526). FT CONFLICT 1745 1746 Missing (in Ref. 7; AAD49852). SQ SEQUENCE 2261 AA; 254302 MW; 21A2CF8F3F518D6D CRC64; MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVARLFSDAR RLLLYSQKDT SMKDMRKVLR TLQQIKKSSS NLKLQDFLVD NETFSGFLYH NLSLPKSTVD KMLRADVILH KVFLQGYQLH LTSLCNGSKS EEMIQLGDQE VSELCGLPRE KLAAAERVLR SNMDILKPIL RTLNSTSPFP SKELAEATKT LLHSLGTLAQ ELFSMRSWSD MRQEVMFLTN VNSSSSSTQI YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNGTE EDAETFYDNS TTPYCNDLMK NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS PKIWTFMENS QEMDLVRMLL DSRDNDHFWE QQLDGLDWTA QDIVAFLAKH PEDVQSSNGS VYTWREAFNE TNQAIRTISR FMECVNLNKL EPIATEVWLI NKSMELLDER KFWAGIVFTG ITPGSIELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV EQAIIRVLTG TEKKTGVYMQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKGIV YEKEARLKET MRIMGLDNSI LWFSWFISSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV FLSVFAVVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFTLKIFAS LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTSVSMMLF DTFLYGVMTW YIEAVFPGQY GIPRPWYFPC TKSYWFGEES DEKSHPGSNQ KRISEICMEE EPTHLKLGVS IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL GKDIRSEMST IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG LPSSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ GRTIILSTHH MDEADVLGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS SCRNSSSTVS YLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE TSDGTLPARR NRRAFGDKQS CLRPFTEDDA ADPNDSDIDP ESRETDLLSG MDGKGSYQVK GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ PWMYNEQYTF VSNDAPEDTG TLELLNALTK DPGFGTRCME GNPIPDTPCQ AGEEEWTTAP VPQTIMDLFQ NGNWTMQNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QNTADILQDL TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NTQALPPSQE VNDAIKQMKK HLKLAKDSSA DRFLNSLGRF MTGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK GENPSHYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTDNKLNNIN DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG VVFFLITVLI QYRFFIRPRP VNAKLSPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI YRRKRKPAVD RICVGIPPGE CFGLLGVNGA GKSSTFKMLT GDTTVTRGDA FLNKNSILSN IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKVGEWAIR KLGLVKYGEK YAGNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSV VKEGRSVVLT SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQDFFG LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V // ID ABCA4_HUMAN Reviewed; 2273 AA. AC P78363; O15112; O60438; O60915; Q0QD48; Q4LE31; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 09-JUL-2014, entry version 152. DE RecName: Full=Retinal-specific ATP-binding cassette transporter; DE AltName: Full=ATP-binding cassette sub-family A member 4; DE AltName: Full=RIM ABC transporter; DE Short=RIM protein; DE Short=RmP; DE AltName: Full=Stargardt disease protein; GN Name=ABCA4; Synonyms=ABCR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS STGD1, AND VARIANTS HIS-846; RP GLN-943 AND ASP-1817. RX PubMed=9054934; DOI=10.1038/ng0397-236; RA Allikmets R., Singh N., Sun H., Shroyer N.F., Hutchinson A., RA Chidambaram A., Gerrard B., Baird L., Stauffer D., Peiffer A., RA Rattner A., Smallwood P.M., Li Y., Anderson K.L., Lewis R.A., RA Nathans J., Leppert M., Dean M., Lupski J.R.; RT "A photoreceptor cell-specific ATP-binding transporter gene (ABCR) is RT mutated in recessive Stargardt macular dystrophy."; RL Nat. Genet. 15:236-246(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9202155; DOI=10.1016/S0014-5793(97)00517-6; RA Azarian S.M., Travis G.H.; RT "The photoreceptor rim protein is an ABC transporter encoded by the RT gene for recessive Stargardt's disease (ABCR)."; RL FEBS Lett. 409:247-252(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS STGD1 TRP-18 AND CYS-212, RP AND VARIANT ASP-1817. RX PubMed=9503029; DOI=10.1006/geno.1997.5164; RA Gerber S., Rozet J.-M., van de Pol T.J.R., Hoyng C.B., Munnich A., RA Blankenagel A., Kaplan J., Cremers F.P.M.; RT "Complete exon-intron structure of the retina-specific ATP binding RT transporter gene (ABCR) allows the identification of novel mutations RT underlying Stargardt disease."; RL Genomics 48:139-142(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS STGD1. RX PubMed=9490294; DOI=10.1007/s004390050649; RA Nasonkin I., Illing M., Koehler M.R., Schmid M., Molday R.S., RA Weber B.H.F.; RT "Mapping of the rod photoreceptor ABC transporter (ABCR) to 1p21-p22.1 RT and identification of novel mutations in Stargardt's disease."; RL Hum. Genet. 102:21-26(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-943. RC TISSUE=Brain; RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., RA Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.; RT "Preparation of a set of expression-ready clones of mammalian long RT cDNAs encoding large proteins by the ORF trap cloning method."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-29. RC TISSUE=Retina; RX PubMed=17286855; DOI=10.1186/1471-2164-8-42; RA Roni V., Carpio R., Wissinger B.; RT "Mapping of transcription start sites of human retina expressed RT genes."; RL BMC Genomics 8:42-42(2007). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10075733; DOI=10.1074/jbc.274.12.8269; RA Sun H., Molday R.S., Nathans J.; RT "Retinal stimulates ATP hydrolysis by purified and reconstituted ABCR, RT the photoreceptor-specific ATP-binding cassette transporter RT responsible for Stargardt disease."; RL J. Biol. Chem. 274:8269-8281(1999). RN [9] RP DISEASE. RX PubMed=9466990; DOI=10.1093/hmg/7.3.355; RA Cremers F.P.M., van de Pol D.J.R., van Driel M.A., den Hollander A.I., RA van Haren F.J.J., Knoers N.V.A.M., Tijmes N., Bergen A.A.B., RA Rohrschneider K., Blankenagel A., Pinckers A.J.L.G., Deutman A.F., RA Hoyng C.B.; RT "Autosomal recessive retinitis pigmentosa and cone-rod dystrophy RT caused by splice site mutations in the Stargardt's disease gene RT ABCR."; RL Hum. Mol. Genet. 7:355-362(1998). RN [10] RP MEMBRANE TOPOLOGY, AND GLYCOSYLATION AT ASN-98; ASN-415; ASN-444; RP ASN-504; ASN-1469; ASN-1529; ASN-1588 AND ASN-1662. RX PubMed=11320094; DOI=10.1074/jbc.M101902200; RA Bungert S., Molday L.L., Molday R.S.; RT "Membrane topology of the ATP binding cassette transporter ABCR and RT its relationship to ABC1 and related ABCA transporters: identification RT of N-linked glycosylation sites."; RL J. Biol. Chem. 276:23539-23546(2001). RN [11] RP VARIANTS ARMD2, AND VARIANTS. RX PubMed=9295268; DOI=10.1126/science.277.5333.1805; RA Allikmets R., Shroyer N.F., Singh N., Seddon J.M., Lewis R.A., RA Bernstein P.S., Peiffer A., Zabriskie N.A., Li Y., Hutchinson A., RA Dean M., Lupski J.R., Leppert M.; RT "Mutation of the Stargardt disease gene (ABCR) in age-related macular RT degeneration."; RL Science 277:1805-1807(1997). RN [12] RP VARIANTS STGD1 TRP-18; CYS-212; HIS-636; MET-1019; VAL-1038; CYS-1108; RP TRP-1640; SER-1977 AND HIS-2107, AND VARIANTS FFM PRO-11; PRO-541; RP VAL-1038; GLU-1091; CYS-1508; PHE-1970 AND ARG-1971. RX PubMed=9781034; DOI=10.1038/sj.ejhg.5200221; RA Rozet J.-M., Gerber S., Souied E., Perrault I., Chatelin S., Ghazi I., RA Leowski C., Dufier J.-L., Munnich A., Kaplan J.; RT "Spectrum of ABCR gene mutations in autosomal recessive macular RT dystrophies."; RL Eur. J. Hum. Genet. 6:291-295(1998). RN [13] RP VARIANTS STGD1. RX PubMed=9973280; DOI=10.1086/302251; RA Lewis R.A., Shroyer N.F., Singh N., Allikmets R., Hutchinson A., RA Li Y., Lupski J.R., Leppert M., Dean M.; RT "Genotype/phenotype analysis of a photoreceptor-specific ATP-binding RT cassette transporter gene, ABCR, in Stargardt disease."; RL Am. J. Hum. Genet. 64:422-434(1999). RN [14] RP VARIANTS STGD1, AND VARIANTS. RX PubMed=10090887; DOI=10.1086/302323; RA Maugeri A., van Driel M.A., van de Pol D.J.R., Klevering B.J., RA van Haren F.J.J., Tijmes N., Bergen A.A.B., Rohrschneider K., RA Blankenagel A., Pinckers A.J.L.G., Dahl N., Brunner H.G., RA Deutman A.F., Hoyng C.B., Cremers F.P.M.; RT "The 2588G-->C mutation in the ABCR gene is a mild frequent founder RT mutation in the western European population and allows the RT classification of ABCR Mutations in patients with Stargardt disease."; RL Am. J. Hum. Genet. 64:1024-1035(1999). RN [15] RP VARIANT STGD1 TYR-54, AND VARIANT ALA-863. RX PubMed=10612508; DOI=10.1016/S0002-9394(99)00236-6; RA Zhang K., Garibaldi D.C., Kniazeva M., Albini T., Chiang M.F., RA Kerrigan M., Sunness J.S., Han M., Allikmets R.; RT "A novel mutation in the ABCR gene in four patients with autosomal RT recessive Stargardt disease."; RL Am. J. Ophthalmol. 128:720-724(1999). RN [16] RP VARIANTS STGD1 VAL-60; ARG-206; ASN-300; PRO-541; ALA-849; PRO-974; RP VAL-1038; CYS-1108; LEU-1408; ARG-1488; ASP-1652; PRO-1729; GLU-1961; RP TRP-2038; TRP-2077; HIS-2107; ARG-2128 AND TYR-2150. RX PubMed=10206579; DOI=10.1001/archopht.117.4.504; RA Fishman G.A., Stone E.M., Grover S., Derlacki D.J., Haines H.L., RA Hockey R.R.; RT "Variation of clinical expression in patients with Stargardt dystrophy RT and sequence variations in the ABCR gene."; RL Arch. Ophthalmol. 117:504-510(1999). RN [17] RP VARIANTS GLU-1961 AND ASN-2177. RX PubMed=10880298; DOI=10.1086/303018; RA Allikmets R., Tammur J., Hutchinson A., Lewis R.A., Shroyer N.F., RA Dalakishvili K., Lupski J.R., Steiner K., Pauleikhoff D., Holz F.G., RA Weber B.H.F., Dean M., Atkinson A., Gail M.H., Bernstein P.S., RA Singh N., Peiffer A., Zabriskie N.A., Leppert M., Seddon J.M., RA Zhang K., Sunness J.S., Udar N.S., Yelchits S., Silva-Garcia R., RA Small K.W., Simonelli F., Testa F., D'Urso M., Brancato R., RA Rinaldi E., Ingvast S., Taube A., Wadelius C., Souied E., Ducroq D., RA Kaplan J., Assink J.J.M., ten Brink J.B., de Jong P.T.V.M., RA Bergen A.A.B., Maugeri A., van Driel M.A., Hoyng C.B., Cremers F.P.M., RA Paloma E., Coco R., Balcells S., Gonzalez-Duarte R., Kermani S., RA Stanga P., Bhattacharya S.S., Bird A.C.; RT "Further evidence for an association of ABCR alleles with age-related RT macular degeneration."; RL Am. J. Hum. Genet. 67:487-491(2000). RN [18] RP VARIANTS STGD1 GLU-60; THR-60; GLU-65; LEU-68; ARG-72; CYS-212; RP SER-230; SER-247; VAL-328; LYS-471; PRO-541; GLN-572; ARG-607; RP LYS-635; CYS-653; TYR-764; ARG-765; ALA-901; ILE-959; LYS-1036; RP VAL-1038; PRO-1063; ASP-1087; CYS-1097; CYS-1108; LEU-1380; LYS-1399; RP PRO-1430; VAL-1440; HIS-1443; LEU-1486; TYR-1488; MET-1537; PRO-1689; RP LEU-1705; THR-1733; ARG-1748; PRO-1763; LYS-1885; HIS-1898; GLU-1961; RP ARG-1975; SER-1977; GLY-2077; TRP-2077 AND VAL-2241, AND VARIANTS RP GLN-152; HIS-212; ARG-423; ILE-552; ARG-914; GLN-943; THR-1562; RP ILE-1868; MET-1921; LEU-1948; PHE-1970; ALA-2059; ASN-2177 AND RP VAL-2216. RX PubMed=10958763; DOI=10.1086/303090; RA Rivera A., White K., Stoehr H., Steiner K., Hemmrich N., Grimm T., RA Jurklies B., Lorenz B., Scholl H.P.N., Apfelstedt-Sylla E., RA Weber B.H.F.; RT "A comprehensive survey of sequence variation in the ABCA4 (ABCR) gene RT in Stargardt disease and age-related macular degeneration."; RL Am. J. Hum. Genet. 67:800-813(2000). RN [19] RP VARIANTS CORD3 GLU-65; CYS-212; PRO-541; ALA-863; GLY-863 DEL; RP VAL-1038; LYS-1122; TYR-1490 AND ASP-1598. RX PubMed=10958761; DOI=10.1086/303079; RA Maugeri A., Klevering B.J., Rohrschneider K., Blankenagel A., RA Brunner H.G., Deutman A.F., Hoyng C.B., Cremers F.P.M.; RT "Mutations in the ABCA4 (ABCR) gene are the major cause of autosomal RT recessive cone-rod dystrophy."; RL Am. J. Hum. Genet. 67:960-966(2000). RN [20] RP VARIANTS STGD1 ASP-340; GLN-572; ALA-863; SER-965; VAL-1038; ALA-1780 RP AND HIS-1898, AND VARIANT GLN-943. RX PubMed=10746567; DOI=10.1007/s004390051034; RA Shroyer N.F., Lewis R.A., Lupski J.R.; RT "Complex inheritance of ABCR mutations in Stargardt disease: linkage RT disequilibrium, complex alleles, and pseudodominance."; RL Hum. Genet. 106:244-248(2000). RN [21] RP VARIANTS STGD1. RX PubMed=10634594; RA Papaioannou M., Ocaka L., Bessant D., Lois N., Bird A.C., Payne A., RA Bhattacharya S.S.; RT "An analysis of ABCR mutations in British patients with recessive RT retinal dystrophies."; RL Invest. Ophthalmol. Vis. Sci. 41:16-19(2000). RN [22] RP VARIANTS STGD1 CYS-212; ASP-767; ILE-897; VAL-1038; LYS-1087; RP LYS-1399; GLN-1640 AND GLU-1961, AND VARIANT HIS-212. RX PubMed=10711710; RA Simonelli F., Testa F., de Crecchio G., Rinaldi E., Hutchinson A., RA Atkinson A., Dean M., D'Urso M., Allikmets R.; RT "New ABCR mutations and clinical phenotype in Italian patients with RT Stargardt disease."; RL Invest. Ophthalmol. Vis. Sci. 41:892-897(2000). RN [23] RP CHARACTERIZATION OF VARIANTS, AND MUTAGENESIS OF GLY-966; LYS-969; RP GLY-1975 AND LYS-1978. RX PubMed=11017087; DOI=10.1038/79994; RA Sun H., Smallwood P.M., Nathans J.; RT "Biochemical defects in ABCR protein variants associated with human RT retinopathies."; RL Nat. Genet. 26:242-246(2000). RN [24] RP VARIANT STGD1 ASN-972, AND VARIANTS GLN-943; ILE-1868 AND LEU-1948. RX PubMed=11594993; DOI=10.1034/j.1600-0420.2001.790520.x; RA Eksandh L., Ekstroem U., Abrahamson M., Bauer B., Andreasson S.; RT "Different clinical expressions in two families with Stargardt's RT macular dystrophy (STGD1)."; RL Acta Ophthalmol. Scand. 79:524-530(2001). RN [25] RP VARIANTS RETINAL TOXICITY CYS-1129; ARG-1201 AND HIS-2107, AND RP VARIANTS HIS-212; ARG-423; ILE-1868 AND ILE-2255. RX PubMed=11384574; DOI=10.1016/S0002-9394(01)00838-8; RA Shroyer N.F., Lewis R.A., Lupski J.R.; RT "Analysis of the ABCR (ABCA4) gene in 4-aminoquinoline retinopathy: is RT retinal toxicity by chloroquine and hydroxychloroquine related to RT Stargardt disease?"; RL Am. J. Ophthalmol. 131:761-766(2001). RN [26] RP VARIANTS GLU-1961 AND ASN-2177. RX PubMed=11346402; DOI=10.1001/archopht.119.5.745; RA Guymer R.H., Heon E., Lotery A.J., Munier F.L., Schorderet D.F., RA Baird P.N., McNeil R.J., Haines H.L., Sheffield V.C., Stone E.M.; RT "Variation of codons 1961 and 2177 of the Stargardt disease gene is RT not associated with age-related macular degeneration."; RL Arch. Ophthalmol. 119:745-751(2001). RN [27] RP VARIANTS FFM GLY-339; ALA-863; TRP-943; ARG-991; VAL-1038; CYS-1108; RP ARG-1488; THR-1562; GLN-1640; PHE-2027; GLN-2030 AND CYS-2106, AND RP VARIANTS HIS-212; ARG-423; GLN-943; THR-1148; ILE-1868 AND ILE-2255. RX PubMed=11379881; DOI=10.1007/s004390100493; RA Yatsenko A.N., Shroyer N.F., Lewis R.A., Lupski J.R.; RT "Late-onset Stargardt disease is associated with missense mutations RT that map outside known functional regions of ABCR (ABCA4)."; RL Hum. Genet. 108:346-355(2001). RN [28] RP VARIANTS STGD1 SER-686; TRP-1055; ASP-1799; ASP-1805; PRO-1940 AND RP HIS-2107, VARIANTS FFM MET-1253 AND PRO-1940, VARIANTS CORD3 CYS-212 RP AND ARG-2060, AND VARIANTS GLN-943; LEU-1948 AND ILE-2255. RX PubMed=11385708; DOI=10.1002/humu.1133; RA Paloma E., Martinez-Mir A., Vilageliu L., Gonzalez-Duarte R., RA Balcells S.; RT "Spectrum of ABCA4 (ABCR) gene mutations in Spanish patients with RT autosomal recessive macular dystrophies."; RL Hum. Mutat. 17:504-510(2001). RN [29] RP VARIANTS STGD1, AND VARIANTS. RX PubMed=11328725; RA Webster A.R., Heon E., Lotery A.J., Vandenburgh K., Casavant T.L., RA Oh K.T., Beck G., Fishman G.A., Lam B.L., Levin A., Heckenlively J.R., RA Jacobson S.G., Weleber R.G., Sheffield V.C., Stone E.M.; RT "An analysis of allelic variation in the ABCA4 gene."; RL Invest. Ophthalmol. Vis. Sci. 42:1179-1189(2001). RN [30] RP VARIANTS STGD1 13-LYS--TRP-15 DEL; TYR-54; LYS-58; VAL-60; GLU-65; RP GLU-77; HIS-190; PRO-244; ARG-309; CYS-525; CYS-537; PRO-541; PRO-549; RP ARG-550; GLN-602; ARG-607; MET-643; ASP-767; PRO-797; ARG-821; RP THR-824; ALA-863; ALA-935; TRP-943; ALA-989; VAL-1038; CYS-1108; RP LEU-1108; LYS-1122; ARG-1201; GLN-1300; LEU-1380; PRO-1388; ARG-1408; RP LEU-1486; ARG-1488; TYR-1490; MET-1526; ASN-1532; THR-1562; TRP-1640; RP LEU-1776; THR-1846; GLU-1961; SER-1977; PHE-2027; GLN-2030; PRO-2035; RP LEU-2050; CYS-2107; HIS-2107; TRP-2139; ARG-2150 AND TYR-2150, RP VARIANTS CORD3 GLN-1640 AND ASP-2146, AND VARIANTS HIS-212; ARG-423; RP GLN-943; THR-1637; ILE-1868 AND LEU-1948. RX PubMed=11527935; RA Briggs C.E., Rucinski D., Rosenfeld P.J., Hirose T., Berson E.L., RA Dryja T.P.; RT "Mutations in ABCR (ABCA4) in patients with Stargardt macular RT degeneration or cone-rod degeneration."; RL Invest. Ophthalmol. Vis. Sci. 42:2229-2236(2001). RN [31] RP VARIANT ARG-423. RX PubMed=12111378; DOI=10.1007/s100380200041; RA Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K., RA Harigae S., Osawa S., Nakamura Y.; RT "Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes RT encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8, RT ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and RT ABCG8."; RL J. Hum. Genet. 47:285-310(2002). RN [32] RP VARIANT [LARGE SCALE ANALYSIS] MET-224. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [33] RP VARIANTS ARMD2 GLU-762; LEU-1129; CYS-1724; SER-1977; ASN-2047 AND RP TYR-2137, AND VARIANT ILE-552. RX PubMed=19028736; DOI=10.1136/bjo.2008.145193; RA Aguirre-Lamban J., Riveiro-Alvarez R., Maia-Lopes S., RA Cantalapiedra D., Vallespin E., Avila-Fernandez A., RA Villaverde-Montero C., Trujillo-Tiebas M.J., Ramos C., Ayuso C.; RT "Molecular analysis of the ABCA4 gene for reliable detection of RT allelic variations in Spanish patients: identification of 21 novel RT variants."; RL Br. J. Ophthalmol. 93:614-621(2009). RN [34] RP VARIANTS STGD1 VAL-156; CYS-212; LYS-380; ARG-550; PRO-572; TRP-602; RP ARG-607; CYS-653; ASP-767; ILE-897; ALA-901; MET-931; SER-965; RP MET-1019; HIS-1108; LEU-1129; LEU-1380; ILE-1433; LEU-1486; TYR-1490; RP GLN-1640; TRP-1640; ARG-1748; ASP-1799; PRO-1940; GLU-1961; SER-1977; RP PHE-2027; ARG-2060; HIS-2107; TYR-2150 AND VAL-2241. RX PubMed=18977788; DOI=10.1136/bjo.2008.148155; RA Riveiro-Alvarez R., Aguirre-Lamban J., Lopez-Martinez M.A., RA Trujillo-Tiebas M.J., Cantalapiedra D., Vallespin E., RA Avila-Fernandez A., Ramos C., Ayuso C.; RT "Frequency of ABCA4 mutations in 278 Spanish controls: an insight into RT the prevalence of autosomal recessive Stargardt disease."; RL Br. J. Ophthalmol. 93:1359-1364(2009). CC -!- FUNCTION: In the visual cycle, acts as an inward-directed retinoid CC flipase, retinoid substrates imported by ABCA4 from the CC extracellular or intradiscal (rod) membrane surfaces to the CC cytoplasmic membrane surface are all-trans-retinaldehyde (ATR) and CC N-retinyl-phosphatidyl-ethanolamine (NR-PE). Once transported to CC the cytoplasmic surface, ATR is reduced to vitamin A by trans- CC retinol dehydrogenase (tRDH) and then transferred to the retinal CC pigment epithelium (RPE) where it is converted to 11-cis-retinal. CC May play a role in photoresponse, removing ATR/NR-PE from the CC extracellular photoreceptor surfaces during bleach recovery. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC Note=Localized to outer segment disk edges of rods and cones, with CC around one million copies/photoreceptor. CC -!- TISSUE SPECIFICITY: Retinal-specific. Seems to be exclusively CC found in the rims of rod photoreceptor cells. CC -!- POLYMORPHISM: The variant Ala-863 is present in the general CC population at a frequency of approximately 3% and 1% in Northern CC Europe and United States, respectively. It is a mild alteration CC probably leading to STGD phenotype only in combination with a more CC severe allele. The variant Glu-1961 is found with high frequency CC in healthy individuals of Somali ancestry. CC -!- DISEASE: Stargardt disease 1 (STGD1) [MIM:248200]: A common CC hereditary macular degeneration. It is characterized by decreased CC central vision, atrophy of the macula and underlying retinal CC pigment epithelium, and frequent presence of prominent flecks in CC the posterior pole of the retina. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Fundus flavimaculatus (FFM) [MIM:248200]: Autosomal CC recessive retinal disorder very similar to Stargardt disease. In CC contrast to Stargardt disease, FFM is characterized by later onset CC and slowly progressive course. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Macular degeneration, age-related, 2 (ARMD2) CC [MIM:153800]: A form of age-related macular degeneration, a CC multifactorial eye disease and the most common cause of CC irreversible vision loss in the developed world. In most patients, CC the disease is manifest as ophthalmoscopically visible yellowish CC accumulations of protein and lipid that lie beneath the retinal CC pigment epithelium and within an elastin-containing structure CC known as Bruch membrane. Note=Disease susceptibility is associated CC with variations affecting the gene represented in this entry. CC -!- DISEASE: Cone-rod dystrophy 3 (CORD3) [MIM:604116]: An inherited CC retinal dystrophy characterized by retinal pigment deposits CC visible on fundus examination, predominantly in the macular CC region, and initial loss of cone photoreceptors followed by rod CC degeneration. This leads to decreased visual acuity and CC sensitivity in the central visual field, followed by loss of CC peripheral vision. Severe loss of vision occurs earlier than in CC retinitis pigmentosa. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- DISEASE: Retinitis pigmentosa 19 (RP19) [MIM:601718]: A retinal CC dystrophy belonging to the group of pigmentary retinopathies. CC Retinitis pigmentosa is characterized by retinal pigment deposits CC visible on fundus examination and primary loss of rod CC photoreceptor cells followed by secondary loss of cone CC photoreceptors. Patients typically have night vision blindness and CC loss of midperipheral visual field. As their condition progresses, CC they lose their far peripheral visual field and eventually central CC vision as well. RP19 is characterized by choroidal atrophy. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA CC family. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC -!- SEQUENCE CAUTION: CC Sequence=BAE06122.1; Type=Erroneous initiation; CC -!- WEB RESOURCE: Name=Mutations of the ABCA4 gene; Note=Retina CC International's Scientific Newsletter; CC URL="http://www.retina-international.org/files/sci-news/abcrmut.htm"; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P78363"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U88667; AAC51144.1; -; mRNA. DR EMBL; AF000148; AAC23915.1; -; mRNA. DR EMBL; Y15635; CAA75729.1; -; Genomic_DNA. DR EMBL; Y15636; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15637; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15638; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15639; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15640; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15641; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15642; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15643; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15644; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15645; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15646; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15647; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15648; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15649; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15650; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15651; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15652; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15653; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15654; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15655; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15656; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15657; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15658; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15659; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15660; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15661; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15662; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15663; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15664; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15665; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15666; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15667; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15668; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15669; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15670; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15671; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15672; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15673; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15674; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15675; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15676; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15677; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15678; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15679; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15680; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15681; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15682; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15683; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; Y15684; CAA75729.1; JOINED; Genomic_DNA. DR EMBL; AF001945; AAC05632.1; -; mRNA. DR EMBL; AB210040; BAE06122.1; ALT_INIT; mRNA. DR EMBL; AC093579; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105278; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DQ426859; ABD90529.1; -; mRNA. DR CCDS; CCDS747.1; -. DR RefSeq; NP_000341.2; NM_000350.2. DR UniGene; Hs.416707; -. DR ProteinModelPortal; P78363; -. DR BioGrid; 106542; 1. DR STRING; 9606.ENSP00000359245; -. DR TCDB; 3.A.1.211.2; the atp-binding cassette (abc) superfamily. DR PhosphoSite; P78363; -. DR DMDM; 6707663; -. DR PaxDb; P78363; -. DR PRIDE; P78363; -. DR DNASU; 24; -. DR Ensembl; ENST00000370225; ENSP00000359245; ENSG00000198691. DR GeneID; 24; -. DR KEGG; hsa:24; -. DR UCSC; uc001dqh.3; human. DR CTD; 24; -. DR GeneCards; GC01M094458; -. DR GeneReviews; ABCA4; -. DR H-InvDB; HIX0028510; -. DR HGNC; HGNC:34; ABCA4. DR MIM; 153800; phenotype. DR MIM; 248200; phenotype. DR MIM; 601691; gene. DR MIM; 601718; phenotype. DR MIM; 604116; phenotype. DR neXtProt; NX_P78363; -. DR Orphanet; 279; Age-related macular degeneration. DR Orphanet; 1872; Cone rod dystrophy. DR Orphanet; 791; Retinitis pigmentosa. DR Orphanet; 827; Stargardt disease. DR PharmGKB; PA24379; -. DR eggNOG; COG1131; -. DR HOGENOM; HOG000231547; -. DR HOVERGEN; HBG050436; -. DR InParanoid; P78363; -. DR KO; K05644; -. DR OMA; IMVKGAF; -. DR OrthoDB; EOG78D7J6; -. DR PhylomeDB; P78363; -. DR TreeFam; TF105191; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR ChiTaRS; ABCA4; human. DR GeneWiki; ABCA4; -. DR GenomeRNAi; 24; -. DR NextBio; 75; -. DR PRO; PR:P78363; -. DR ArrayExpress; P78363; -. DR Bgee; P78363; -. DR CleanEx; HS_ABCA4; -. DR Genevestigator; P78363; -. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; TAS:ProtInc. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; TAS:ProtInc. DR GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:Ensembl. DR GO; GO:0005215; F:transporter activity; TAS:ProtInc. DR GO; GO:0006649; P:phospholipid transfer to membrane; IEA:Ensembl. DR GO; GO:0045494; P:photoreceptor cell maintenance; IEA:Ensembl. DR GO; GO:0007603; P:phototransduction, visible light; TAS:Reactome. DR GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0006810; P:transport; TAS:ProtInc. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR026082; ABC_A. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005951; Rim_ABC_transpt. DR PANTHER; PTHR19229; PTHR19229; 1. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR01257; rim_protein; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW Age-related macular degeneration; ATP-binding; Complete proteome; KW Cone-rod dystrophy; Disease mutation; Disulfide bond; Glycoprotein; KW Membrane; Nucleotide-binding; Polymorphism; Reference proteome; KW Repeat; Retinitis pigmentosa; Sensory transduction; Stargardt disease; KW Transmembrane; Transmembrane helix; Transport; Vision. FT CHAIN 1 2273 Retinal-specific ATP-binding cassette FT transporter. FT /FTId=PRO_0000093301. FT TOPO_DOM 1 21 Cytoplasmic. FT TRANSMEM 22 42 Helical; (Potential). FT TOPO_DOM 43 646 Extracellular. FT TRANSMEM 647 667 Helical; (Potential). FT TRANSMEM 700 720 Helical; (Potential). FT TRANSMEM 731 751 Helical; (Potential). FT TRANSMEM 760 780 Helical; (Potential). FT TRANSMEM 836 856 Helical; (Potential). FT TOPO_DOM 857 1376 Cytoplasmic. FT TRANSMEM 1377 1397 Helical; (Potential). FT TOPO_DOM 1398 1727 Extracellular. FT TRANSMEM 1728 1748 Helical; (Potential). FT TRANSMEM 1760 1780 Helical; (Potential). FT TRANSMEM 1793 1813 Helical; (Potential). FT TRANSMEM 1832 1852 Helical; (Potential). FT TRANSMEM 1874 1894 Helical; (Potential). FT TOPO_DOM 1895 2273 Cytoplasmic. FT DOMAIN 929 1160 ABC transporter 1. FT DOMAIN 1938 2170 ABC transporter 2. FT NP_BIND 963 970 ATP 1 (Potential). FT NP_BIND 1972 1979 ATP 2 (Potential). FT CARBOHYD 98 98 N-linked (GlcNAc...). FT CARBOHYD 415 415 N-linked (GlcNAc...). FT CARBOHYD 444 444 N-linked (GlcNAc...). FT CARBOHYD 504 504 N-linked (GlcNAc...). FT CARBOHYD 1469 1469 N-linked (GlcNAc...). FT CARBOHYD 1529 1529 N-linked (GlcNAc...). FT CARBOHYD 1588 1588 N-linked (GlcNAc...). FT CARBOHYD 1662 1662 N-linked (GlcNAc...). FT DISULFID 75 324 By similarity. FT DISULFID 1488 1502 By similarity. FT VARIANT 11 11 L -> P (in FFM). FT /FTId=VAR_012493. FT VARIANT 13 15 Missing (in STGD1). FT /FTId=VAR_012494. FT VARIANT 18 18 R -> W (in STGD1; dbSNP:rs121909205). FT /FTId=VAR_008398. FT VARIANT 24 24 R -> H (in STGD1). FT /FTId=VAR_008399. FT VARIANT 54 54 C -> Y (in STGD1). FT /FTId=VAR_008400. FT VARIANT 58 58 N -> K (in STGD1). FT /FTId=VAR_012495. FT VARIANT 60 60 A -> E (in STGD1). FT /FTId=VAR_012496. FT VARIANT 60 60 A -> T (in STGD1). FT /FTId=VAR_012497. FT VARIANT 60 60 A -> V (in STGD1). FT /FTId=VAR_008492. FT VARIANT 65 65 G -> E (in STGD1 and CORD3). FT /FTId=VAR_008401. FT VARIANT 68 68 P -> L (in STGD1). FT /FTId=VAR_012498. FT VARIANT 68 68 P -> R (in STGD1). FT /FTId=VAR_012499. FT VARIANT 72 72 G -> R (in STGD1). FT /FTId=VAR_012500. FT VARIANT 75 75 C -> G (in STGD1). FT /FTId=VAR_008402. FT VARIANT 77 77 V -> E (in STGD1). FT /FTId=VAR_012501. FT VARIANT 96 96 N -> D (in STGD1). FT /FTId=VAR_008403. FT VARIANT 96 96 N -> H (in STGD1). FT /FTId=VAR_008404. FT VARIANT 100 100 S -> P (in STGD1). FT /FTId=VAR_012502. FT VARIANT 152 152 R -> Q (in dbSNP:rs62646862). FT /FTId=VAR_012503. FT VARIANT 156 156 I -> V (in STGD1; dbSNP:rs62646863). FT /FTId=VAR_012504. FT VARIANT 190 190 Q -> H (in STGD1). FT /FTId=VAR_012505. FT VARIANT 192 192 A -> T (in STGD1). FT /FTId=VAR_008405. FT VARIANT 206 206 S -> R (in STGD1; reduced basal and FT retinal-stimulated ATP-hydrolysis; FT dbSNP:rs61748536). FT /FTId=VAR_012506. FT VARIANT 212 212 R -> C (in STGD1 and CORD3; common FT mutation in southern Europe; reduced ATP- FT binding capacity). FT /FTId=VAR_008406. FT VARIANT 212 212 R -> H (in dbSNP:rs6657239). FT /FTId=VAR_012507. FT VARIANT 220 220 R -> C (in STGD1). FT /FTId=VAR_012508. FT VARIANT 224 224 T -> M (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035736. FT VARIANT 230 230 C -> S (in STGD1). FT /FTId=VAR_012509. FT VARIANT 244 244 L -> P (in STGD1). FT /FTId=VAR_012510. FT VARIANT 247 247 N -> S (in STGD1). FT /FTId=VAR_012511. FT VARIANT 249 249 D -> G (in STGD1). FT /FTId=VAR_008407. FT VARIANT 300 300 T -> N (in STGD1). FT /FTId=VAR_008408. FT VARIANT 309 309 P -> R (in STGD1). FT /FTId=VAR_012512. FT VARIANT 328 328 E -> V (in STGD1). FT /FTId=VAR_012513. FT VARIANT 333 333 R -> W (in STGD1). FT /FTId=VAR_012514. FT VARIANT 336 336 S -> C (in STGD1). FT /FTId=VAR_008409. FT VARIANT 339 339 W -> G (in FFM). FT /FTId=VAR_012515. FT VARIANT 340 340 Y -> D (in STGD1). FT /FTId=VAR_008410. FT VARIANT 380 380 N -> K (in STGD1). FT /FTId=VAR_012516. FT VARIANT 407 407 A -> V (in STGD1 and CORD3). FT /FTId=VAR_008411. FT VARIANT 423 423 H -> R (in dbSNP:rs3112831). FT /FTId=VAR_012517. FT VARIANT 445 445 S -> R (in STGD1). FT /FTId=VAR_008412. FT VARIANT 471 471 E -> K (in ARMD2 and STGD1; ATP-binding FT capacity and retinal stimulation as in FT wild-type; dbSNP:rs1800548). FT /FTId=VAR_008413. FT VARIANT 523 523 D -> E (in STGD1). FT /FTId=VAR_008414. FT VARIANT 525 525 F -> C (in STGD1). FT /FTId=VAR_012518. FT VARIANT 537 537 R -> C (in STGD1). FT /FTId=VAR_012519. FT VARIANT 541 541 L -> P (in STGD1, FFM and CORD3; reduced FT ATP-binding capacity; abolishes retinal- FT stimulated ATP hydrolysis). FT /FTId=VAR_008415. FT VARIANT 549 549 A -> P (in STGD1). FT /FTId=VAR_012520. FT VARIANT 550 550 G -> R (in STGD1). FT /FTId=VAR_012521. FT VARIANT 552 552 V -> I. FT /FTId=VAR_012522. FT VARIANT 572 572 R -> P (in STGD1). FT /FTId=VAR_008416. FT VARIANT 572 572 R -> Q (in STGD1). FT /FTId=VAR_008417. FT VARIANT 602 602 R -> Q (in STGD1). FT /FTId=VAR_012523. FT VARIANT 602 602 R -> W (in STGD1). FT /FTId=VAR_008418. FT VARIANT 607 607 G -> R (in STGD1). FT /FTId=VAR_012524. FT VARIANT 607 607 G -> W (in STGD1). FT /FTId=VAR_012525. FT VARIANT 608 608 F -> I (in STGD1). FT /FTId=VAR_008419. FT VARIANT 635 635 Q -> K (in STGD1). FT /FTId=VAR_012526. FT VARIANT 636 636 Q -> H (in STGD1). FT /FTId=VAR_012527. FT VARIANT 643 643 V -> G (in dbSNP:rs114572202). FT /FTId=VAR_008420. FT VARIANT 643 643 V -> M (in STGD1; dbSNP:rs143548435). FT /FTId=VAR_012528. FT VARIANT 645 645 D -> N (in STGD1). FT /FTId=VAR_008421. FT VARIANT 653 653 R -> C (in STGD1). FT /FTId=VAR_012529. FT VARIANT 686 686 L -> S (in STGD1). FT /FTId=VAR_012530. FT VARIANT 716 716 T -> M (in STGD1). FT /FTId=VAR_012531. FT VARIANT 752 752 S -> I (in dbSNP:rs1801369). FT /FTId=VAR_014703. FT VARIANT 762 762 A -> E (in ARMD2). FT /FTId=VAR_067427. FT VARIANT 764 764 C -> Y (in STGD1). FT /FTId=VAR_012532. FT VARIANT 765 765 S -> N (in STGD1). FT /FTId=VAR_012534. FT VARIANT 765 765 S -> R (in STGD1). FT /FTId=VAR_012533. FT VARIANT 767 767 V -> D (in STGD1). FT /FTId=VAR_012535. FT VARIANT 797 797 L -> P (in STGD1). FT /FTId=VAR_012536. FT VARIANT 818 818 G -> E (in ARMD2 and STGD1; reduced ATP- FT binding capacity). FT /FTId=VAR_008422. FT VARIANT 821 821 W -> R (in STGD1). FT /FTId=VAR_008423. FT VARIANT 824 824 I -> T (in STGD1). FT /FTId=VAR_012537. FT VARIANT 846 846 D -> H. FT /FTId=VAR_008493. FT VARIANT 849 849 V -> A (in STGD1; dbSNP:rs61749435). FT /FTId=VAR_012538. FT VARIANT 851 851 G -> D (in STGD1; highly reduced ATP- FT binding capacity). FT /FTId=VAR_008424. FT VARIANT 854 854 A -> T (in STGD1). FT /FTId=VAR_012539. FT VARIANT 863 863 G -> A (in STGD1, FFM and CORD3; frequent FT mutation in northern Europe in linkage FT disequilibrium with the polymorphic FT variant Q-943; reduced ATP-binding FT capacity and retinal-stimulated ATP FT hydrolysis; dbSNP:rs76157638). FT /FTId=VAR_008425. FT VARIANT 863 863 Missing (in STGD1 and CORD3; reduced ATP- FT binding capacity and retinal-stimulated FT ATP hydrolysis). FT /FTId=VAR_012540. FT VARIANT 873 873 F -> L (in STGD1). FT /FTId=VAR_012541. FT VARIANT 897 897 T -> I (in STGD1; dbSNP:rs61749440). FT /FTId=VAR_012542. FT VARIANT 901 901 T -> A (in dbSNP:rs61754030). FT /FTId=VAR_008426. FT VARIANT 914 914 H -> R. FT /FTId=VAR_012543. FT VARIANT 931 931 V -> M (in STGD1; dbSNP:rs58331765). FT /FTId=VAR_008427. FT VARIANT 935 935 V -> A (in STGD1). FT /FTId=VAR_012544. FT VARIANT 943 943 R -> Q (in linkage disequilibrium with A- FT 863 in the European population; FT dbSNP:rs1801581). FT /FTId=VAR_008428. FT VARIANT 943 943 R -> W (in STGD1 and FFM; FT dbSNP:rs61749446). FT /FTId=VAR_012545. FT VARIANT 957 957 Q -> R (in STGD1). FT /FTId=VAR_008429. FT VARIANT 959 959 T -> I (in STGD1). FT /FTId=VAR_012546. FT VARIANT 965 965 N -> S (in STGD1; reduced retinal- FT stimulated ATP hydrolysis). FT /FTId=VAR_008430. FT VARIANT 971 971 T -> N (in STGD1; highly reduced ATP- FT binding capacity; abolishes retinal- FT stimulated ATP hydrolysis). FT /FTId=VAR_012547. FT VARIANT 972 972 T -> N (in STGD1; unknown pathological FT significance). FT /FTId=VAR_012548. FT VARIANT 974 974 S -> P (in STGD1). FT /FTId=VAR_012549. FT VARIANT 978 978 G -> C (in STGD1). FT /FTId=VAR_008431. FT VARIANT 989 989 V -> A (in STGD1; dbSNP:rs139296587). FT /FTId=VAR_012550. FT VARIANT 991 991 G -> R (in FFM; dbSNP:rs147484266). FT /FTId=VAR_012551. FT VARIANT 1014 1014 L -> R (in STGD1). FT /FTId=VAR_012552. FT VARIANT 1019 1019 T -> A (in STGD1). FT /FTId=VAR_012553. FT VARIANT 1019 1019 T -> M (in STGD1). FT /FTId=VAR_012554. FT VARIANT 1022 1022 E -> K (in STGD1). FT /FTId=VAR_012555. FT VARIANT 1031 1031 K -> E (in STGD1). FT /FTId=VAR_012556. FT VARIANT 1036 1036 E -> K (in STGD1). FT /FTId=VAR_008432. FT VARIANT 1038 1038 A -> V (in STGD1, FFM and CORD3; frequent FT mutation; reduced ATP-binding and FT retinal-stimulated ATP hydrolysis; FT dbSNP:rs61751374). FT /FTId=VAR_008433. FT VARIANT 1055 1055 R -> W (in STGD1). FT /FTId=VAR_012557. FT VARIANT 1063 1063 S -> P (in STGD1). FT /FTId=VAR_012558. FT VARIANT 1071 1071 S -> L (in STGD1; reduced ATP-binding FT capacity). FT /FTId=VAR_008434. FT VARIANT 1072 1072 V -> A (in STGD1). FT /FTId=VAR_008435. FT VARIANT 1087 1087 E -> D (in STGD1). FT /FTId=VAR_012559. FT VARIANT 1087 1087 E -> K (in STGD1). FT /FTId=VAR_008436. FT VARIANT 1091 1091 G -> E (in FFM). FT /FTId=VAR_012560. FT VARIANT 1097 1097 R -> C (in STGD1). FT /FTId=VAR_012561. FT VARIANT 1108 1108 R -> C (in STGD1 and FFM; reduced ATP- FT binding capacity; dbSNP:rs61750120). FT /FTId=VAR_012562. FT VARIANT 1108 1108 R -> H (in STGD1). FT /FTId=VAR_012563. FT VARIANT 1108 1108 R -> L (in STGD1). FT /FTId=VAR_012564. FT VARIANT 1112 1112 T -> N (in STGD1). FT /FTId=VAR_008437. FT VARIANT 1122 1122 E -> K (in STGD1 and CORD3). FT /FTId=VAR_008438. FT VARIANT 1129 1129 R -> C (in STGD1; may predispose to FT develop retinal toxicity after treatment FT with chloroquine and hydroxychloroquine). FT /FTId=VAR_012565. FT VARIANT 1129 1129 R -> L (in ARMD2 and STGD1; also found in FT patients with fundus flavimaculatus; FT reduced ATP-binding capacity; FT dbSNP:rs1801269). FT /FTId=VAR_008439. FT VARIANT 1148 1148 K -> T. FT /FTId=VAR_012566. FT VARIANT 1201 1201 L -> R (in STGD1; may predispose to FT develop retinal toxicity after treatment FT with chloroquine and hydroxychloroquine; FT dbSNP:rs61750126). FT /FTId=VAR_008440. FT VARIANT 1204 1204 D -> N (in STGD1). FT /FTId=VAR_008441. FT VARIANT 1250 1250 L -> P (in STGD1). FT /FTId=VAR_012567. FT VARIANT 1253 1253 T -> M (in FFM; unknown pathological FT significance). FT /FTId=VAR_012568. FT VARIANT 1300 1300 R -> Q (in STGD1; dbSNP:rs61750129). FT /FTId=VAR_012569. FT VARIANT 1314 1314 P -> T. FT /FTId=VAR_008442. FT VARIANT 1380 1380 P -> L (in STGD1; reduced ATP-binding FT capacity). FT /FTId=VAR_008443. FT VARIANT 1388 1388 L -> P (in STGD1). FT /FTId=VAR_012570. FT VARIANT 1399 1399 E -> K (in STGD1). FT /FTId=VAR_012571. FT VARIANT 1406 1406 H -> Y (in STGD1). FT /FTId=VAR_008444. FT VARIANT 1408 1408 W -> L (in STGD1). FT /FTId=VAR_008445. FT VARIANT 1408 1408 W -> R (in STGD1; reduced retinal- FT stimulated ATP hydrolysis). FT /FTId=VAR_008446. FT VARIANT 1428 1428 T -> M (in ARMD2; dbSNP:rs1800549). FT /FTId=VAR_008447. FT VARIANT 1429 1429 V -> A (in STGD1). FT /FTId=VAR_008448. FT VARIANT 1430 1430 L -> P (in STGD1). FT /FTId=VAR_012572. FT VARIANT 1433 1433 V -> I (in STGD1; dbSNP:rs56357060). FT /FTId=VAR_008449. FT VARIANT 1439 1439 G -> D (in STGD1). FT /FTId=VAR_008450. FT VARIANT 1440 1440 F -> S (in STGD1). FT /FTId=VAR_008451. FT VARIANT 1440 1440 F -> V (in STGD1). FT /FTId=VAR_012573. FT VARIANT 1443 1443 R -> H (in STGD1). FT /FTId=VAR_012574. FT VARIANT 1486 1486 P -> L (in STGD1). FT /FTId=VAR_008452. FT VARIANT 1488 1488 C -> F (in STGD1). FT /FTId=VAR_012575. FT VARIANT 1488 1488 C -> R (in STGD1 and FFM; reduced FT retinal-stimulated ATP hydrolysis). FT /FTId=VAR_008453. FT VARIANT 1488 1488 C -> Y (in STGD1). FT /FTId=VAR_012576. FT VARIANT 1490 1490 C -> Y (in STGD1 and CORD3; reduced FT retinal-stimulated ATP hydrolysis). FT /FTId=VAR_008454. FT VARIANT 1508 1508 G -> C (in FFM). FT /FTId=VAR_012577. FT VARIANT 1513 1513 Q -> R (in STGD1). FT /FTId=VAR_012578. FT VARIANT 1517 1517 R -> S (in ARMD2; dbSNP:rs1800550). FT /FTId=VAR_008455. FT VARIANT 1525 1525 L -> P (in STGD1). FT /FTId=VAR_012579. FT VARIANT 1526 1526 T -> M (in STGD1; reduced retinal- FT stimulated ATP hydrolysis). FT /FTId=VAR_008456. FT VARIANT 1532 1532 D -> N (in STGD1). FT /FTId=VAR_008457. FT VARIANT 1537 1537 T -> M (in STGD1). FT /FTId=VAR_012580. FT VARIANT 1562 1562 I -> T (in STGD1, FFM, ARMD2 and CORD3; FT dbSNP:rs1762111). FT /FTId=VAR_008458. FT VARIANT 1578 1578 G -> R (in ARMD2; dbSNP:rs1800551). FT /FTId=VAR_008459. FT VARIANT 1598 1598 A -> D (in CORD3). FT /FTId=VAR_012581. FT VARIANT 1631 1631 L -> P (in STGD1). FT /FTId=VAR_008460. FT VARIANT 1637 1637 A -> T (rare polymorphism). FT /FTId=VAR_012582. FT VARIANT 1640 1640 R -> Q (in STGD1, FFM and CORD3). FT /FTId=VAR_012583. FT VARIANT 1640 1640 R -> W (in STGD1 and CORD3). FT /FTId=VAR_008461. FT VARIANT 1652 1652 Y -> D (in STGD1). FT /FTId=VAR_008462. FT VARIANT 1681 1685 Missing (in STGD1; highly reduced ATP- FT binding capacity). FT /FTId=VAR_012584. FT VARIANT 1689 1689 S -> P (in STGD1). FT /FTId=VAR_012585. FT VARIANT 1693 1693 V -> I (in STGD1; dbSNP:rs61750563). FT /FTId=VAR_012586. FT VARIANT 1696 1696 S -> N (in STGD1). FT /FTId=VAR_008463. FT VARIANT 1703 1703 Q -> K (in STGD1). FT /FTId=VAR_008464. FT VARIANT 1705 1705 R -> L (in STGD1). FT /FTId=VAR_012587. FT VARIANT 1724 1724 W -> C (in ARMD2). FT /FTId=VAR_067428. FT VARIANT 1729 1729 L -> P (in STGD1). FT /FTId=VAR_008465. FT VARIANT 1733 1733 M -> T (in STGD1). FT /FTId=VAR_012588. FT VARIANT 1736 1736 S -> P (in STGD1). FT /FTId=VAR_012589. FT VARIANT 1748 1748 G -> R (in STGD1). FT /FTId=VAR_012590. FT VARIANT 1761 1763 Missing (in STGD1; highly reduced ATP- FT binding capacity). FT /FTId=VAR_012591. FT VARIANT 1763 1763 L -> P (in STGD1). FT /FTId=VAR_012592. FT VARIANT 1776 1776 P -> L (in STGD1). FT /FTId=VAR_012593. FT VARIANT 1780 1780 P -> A (in STGD1). FT /FTId=VAR_012594. FT VARIANT 1794 1794 A -> D (in STGD1). FT /FTId=VAR_008466. FT VARIANT 1799 1799 N -> D (in STGD1). FT /FTId=VAR_012595. FT VARIANT 1805 1805 N -> D (in STGD1). FT /FTId=VAR_012596. FT VARIANT 1817 1817 E -> D. FT /FTId=VAR_012597. FT VARIANT 1820 1820 R -> P (in STGD1). FT /FTId=VAR_008467. FT VARIANT 1838 1838 H -> Y (in STGD1). FT /FTId=VAR_008468. FT VARIANT 1843 1843 R -> W (in STGD1). FT /FTId=VAR_008469. FT VARIANT 1846 1846 I -> T. FT /FTId=VAR_008494. FT VARIANT 1868 1868 N -> I (slightly reduced retinal- FT stimulated ATP hydrolysis; FT dbSNP:rs1801466). FT /FTId=VAR_008470. FT VARIANT 1884 1884 V -> E (in STGD1). FT /FTId=VAR_012598. FT VARIANT 1885 1885 E -> K (in STGD1). FT /FTId=VAR_012599. FT VARIANT 1886 1886 G -> E (in STGD1; highly reduced ATP- FT binding capacity). FT /FTId=VAR_008471. FT VARIANT 1890 1890 Missing (in STGD1). FT /FTId=VAR_008472. FT VARIANT 1896 1896 V -> D (in STGD1). FT /FTId=VAR_012600. FT VARIANT 1898 1898 R -> H (in STGD1 and ARMD2; FT dbSNP:rs1800552). FT /FTId=VAR_008473. FT VARIANT 1921 1921 V -> M (in dbSNP:rs61753032). FT /FTId=VAR_012601. FT VARIANT 1940 1940 L -> P (in STGD1 and FFM). FT /FTId=VAR_012602. FT VARIANT 1948 1948 P -> L (in dbSNP:rs56142141). FT /FTId=VAR_008474. FT VARIANT 1961 1961 G -> E (in STGD1 and FFM; frequent FT mutation; may be associated with ARMD2; FT inhibition of ATP hydrolysis by retinal; FT dbSNP:rs1800553). FT /FTId=VAR_008475. FT VARIANT 1970 1970 L -> F (in ARMD2 and FFM; FT dbSNP:rs1800554). FT /FTId=VAR_008476. FT VARIANT 1971 1971 L -> R (in FFM; highly reduced ATP- FT binding capacity; abolishes basal and FT retinal-stimulated ATP hydrolysis). FT /FTId=VAR_012603. FT VARIANT 1975 1975 G -> R (in STGD1). FT /FTId=VAR_012604. FT VARIANT 1977 1977 G -> S (in STGD1 and ARMD2; highly FT reduced ATP-binding capacity; inhibition FT of ATP hydrolysis by retinal). FT /FTId=VAR_008477. FT VARIANT 2027 2027 L -> F (in STGD1 and FFM; highly reduced FT ATP-binding capacity; dbSNP:rs61751408). FT /FTId=VAR_008478. FT VARIANT 2030 2030 R -> Q (in STGD1 and FFM; FT dbSNP:rs61750641). FT /FTId=VAR_008480. FT VARIANT 2035 2035 L -> P (in STGD1). FT /FTId=VAR_012605. FT VARIANT 2038 2038 R -> W (in STGD1; highly reduced ATP- FT binding capacity). FT /FTId=VAR_008495. FT VARIANT 2047 2047 I -> N (in ARMD2). FT /FTId=VAR_067429. FT VARIANT 2050 2050 V -> L (in STGD1; dbSNP:rs41292677). FT /FTId=VAR_008481. FT VARIANT 2059 2059 G -> A. FT /FTId=VAR_012606. FT VARIANT 2060 2060 L -> R (in CORD3). FT /FTId=VAR_012607. FT VARIANT 2071 2071 Y -> F (in STGD1). FT /FTId=VAR_012608. FT VARIANT 2077 2077 R -> G (in STGD1). FT /FTId=VAR_012609. FT VARIANT 2077 2077 R -> W (in STGD1; highly reduced ATP- FT binding capacity). FT /FTId=VAR_008482. FT VARIANT 2096 2096 E -> K (in STGD1; inhibition of ATP FT hydrolysis by retinal). FT /FTId=VAR_008483. FT VARIANT 2106 2106 R -> C (in STGD1 and FFM; reduced ATP- FT binding capacity). FT /FTId=VAR_008484. FT VARIANT 2107 2107 R -> C (in STGD1; dbSNP:rs2297669). FT /FTId=VAR_012610. FT VARIANT 2107 2107 R -> H (in STGD1; may predispose to FT develop retinal toxicity after treatment FT with chloroquine and hydroxychloroquine; FT dbSNP:rs62642564). FT /FTId=VAR_008485. FT VARIANT 2128 2128 H -> R (in STGD1). FT /FTId=VAR_008486. FT VARIANT 2131 2131 E -> K (in STGD1). FT /FTId=VAR_008487. FT VARIANT 2137 2137 C -> Y (in ARMD2). FT /FTId=VAR_067430. FT VARIANT 2139 2139 R -> W (in STGD1). FT /FTId=VAR_008488. FT VARIANT 2146 2146 G -> D (in CORD3). FT /FTId=VAR_012611. FT VARIANT 2149 2149 R -> L (in STGD1). FT /FTId=VAR_012612. FT VARIANT 2150 2150 C -> R (in STGD1). FT /FTId=VAR_012613. FT VARIANT 2150 2150 C -> Y (in STGD1 and CORD3). FT /FTId=VAR_008489. FT VARIANT 2160 2160 K -> R (in STGD1). FT /FTId=VAR_008490. FT VARIANT 2177 2177 D -> N (may be associated with ARMD2; FT increased retinal-stimulated ATP FT hydrolysis; dbSNP:rs1800555). FT /FTId=VAR_008491. FT VARIANT 2216 2216 A -> V. FT /FTId=VAR_012614. FT VARIANT 2229 2229 L -> P (in STGD1). FT /FTId=VAR_012615. FT VARIANT 2241 2241 L -> V (in STGD1; dbSNP:rs61748521). FT /FTId=VAR_012616. FT VARIANT 2255 2255 S -> I (in dbSNP:rs6666652). FT /FTId=VAR_009157. FT VARIANT 2263 2263 R -> L (in STGD1). FT /FTId=VAR_012617. FT MUTAGEN 966 966 G->D: Abolishes basal and retinal- FT stimulated ATP hydrolysis. FT MUTAGEN 969 969 K->M: Abolishes basal and retinal- FT stimulated ATP hydrolysis. FT MUTAGEN 1975 1975 G->D: Inhibition of retinal-stimulated FT ATP hydrolysis. FT MUTAGEN 1978 1978 K->M: Inhibition of retinal-stimulated FT ATP hydrolysis. FT CONFLICT 722 722 G -> V (in Ref. 2; AAC23915). FT CONFLICT 849 849 V -> C (in Ref. 1; AAC51144). FT CONFLICT 882 882 G -> S (in Ref. 1; AAC51144 and 3; FT CAA75729). FT CONFLICT 941 941 C -> S (in Ref. 2; AAC23915). FT CONFLICT 1116 1116 S -> P (in Ref. 1; AAC51144). FT CONFLICT 1125 1126 LL -> HQ (in Ref. 1; AAC51144). FT CONFLICT 1395 1395 P -> L (in Ref. 1; AAC51144 and 3; FT CAA75729). FT CONFLICT 1465 1465 S -> C (in Ref. 4; AAC05632). FT CONFLICT 1518 1518 S -> T (in Ref. 4; AAC05632). FT CONFLICT 1733 1733 M -> V (in Ref. 2; AAC23915). FT CONFLICT 1989 1989 T -> N (in Ref. 2; AAC23915). FT CONFLICT 2119 2119 E -> K (in Ref. 1; AAC51144). SQ SEQUENCE 2273 AA; 255944 MW; 6E7012D3041CD043 CRC64; MGFVRQIQLL LWKNWTLRKR QKIRFVVELV WPLSLFLVLI WLRNANPLYS HHECHFPNKA MPSAGMLPWL QGIFCNVNNP CFQSPTPGES PGIVSNYNNS ILARVYRDFQ ELLMNAPESQ HLGRIWTELH ILSQFMDTLR THPERIAGRG IRIRDILKDE ETLTLFLIKN IGLSDSVVYL LINSQVRPEQ FAHGVPDLAL KDIACSEALL ERFIIFSQRR GAKTVRYALC SLSQGTLQWI EDTLYANVDF FKLFRVLPTL LDSRSQGINL RSWGGILSDM SPRIQEFIHR PSMQDLLWVT RPLMQNGGPE TFTKLMGILS DLLCGYPEGG GSRVLSFNWY EDNNYKAFLG IDSTRKDPIY SYDRRTTSFC NALIQSLESN PLTKIAWRAA KPLLMGKILY TPDSPAARRI LKNANSTFEE LEHVRKLVKA WEEVGPQIWY FFDNSTQMNM IRDTLGNPTV KDFLNRQLGE EGITAEAILN FLYKGPRESQ ADDMANFDWR DIFNITDRTL RLVNQYLECL VLDKFESYND ETQLTQRALS LLEENMFWAG VVFPDMYPWT SSLPPHVKYK IRMDIDVVEK TNKIKDRYWD SGPRADPVED FRYIWGGFAY LQDMVEQGIT RSQVQAEAPV GIYLQQMPYP CFVDDSFMII LNRCFPIFMV LAWIYSVSMT VKSIVLEKEL RLKETLKNQG VSNAVIWCTW FLDSFSIMSM SIFLLTIFIM HGRILHYSDP FILFLFLLAF STATIMLCFL LSTFFSKASL AAACSGVIYF TLYLPHILCF AWQDRMTAEL KKAVSLLSPV AFGFGTEYLV RFEEQGLGLQ WSNIGNSPTE GDEFSFLLSM QMMLLDAAVY GLLAWYLDQV FPGDYGTPLP WYFLLQESYW LGGEGCSTRE ERALEKTEPL TEETEDPEHP EGIHDSFFER EHPGWVPGVC VKNLVKIFEP CGRPAVDRLN ITFYENQITA FLGHNGAGKT TTLSILTGLL PPTSGTVLVG GRDIETSLDA VRQSLGMCPQ HNILFHHLTV AEHMLFYAQL KGKSQEEAQL EMEAMLEDTG LHHKRNEEAQ DLSGGMQRKL SVAIAFVGDA KVVILDEPTS GVDPYSRRSI WDLLLKYRSG RTIIMSTHHM DEADLLGDRI AIIAQGRLYC SGTPLFLKNC FGTGLYLTLV RKMKNIQSQR KGSEGTCSCS SKGFSTTCPA HVDDLTPEQV LDGDVNELMD VVLHHVPEAK LVECIGQELI FLLPNKNFKH RAYASLFREL EETLADLGLS SFGISDTPLE EIFLKVTEDS DSGPLFAGGA QQKRENVNPR HPCLGPREKA GQTPQDSNVC SPGAPAAHPE GQPPPEPECP GPQLNTGTQL VLQHVQALLV KRFQHTIRSH KDFLAQIVLP ATFVFLALML SIVIPPFGEY PALTLHPWIY GQQYTFFSMD EPGSEQFTVL ADVLLNKPGF GNRCLKEGWL PEYPCGNSTP WKTPSVSPNI TQLFQKQKWT QVNPSPSCRC STREKLTMLP ECPEGAGGLP PPQRTQRSTE ILQDLTDRNI SDFLVKTYPA LIRSSLKSKF WVNEQRYGGI SIGGKLPVVP ITGEALVGFL SDLGRIMNVS GGPITREASK EIPDFLKHLE TEDNIKVWFN NKGWHALVSF LNVAHNAILR ASLPKDRSPE EYGITVISQP LNLTKEQLSE ITVLTTSVDA VVAICVIFSM SFVPASFVLY LIQERVNKSK HLQFISGVSP TTYWVTNFLW DIMNYSVSAG LVVGIFIGFQ KKAYTSPENL PALVALLLLY GWAVIPMMYP ASFLFDVPST AYVALSCANL FIGINSSAIT FILELFENNR TLLRFNAVLR KLLIVFPHFC LGRGLIDLAL SQAVTDVYAR FGEEHSANPF HWDLIGKNLF AMVVEGVVYF LLTLLVQRHF FLSQWIAEPT KEPIVDEDDD VAEERQRIIT GGNKTDILRL HELTKIYPGT SSPAVDRLCV GVRPGECFGL LGVNGAGKTT TFKMLTGDTT VTSGDATVAG KSILTNISEV HQNMGYCPQF DAIDELLTGR EHLYLYARLR GVPAEEIEKV ANWSIKSLGL TVYADCLAGT YSGGNKRKLS TAIALIGCPP LVLLDEPTTG MDPQARRMLW NVIVSIIREG RAVVLTSHSM EECEALCTRL AIMVKGAFRC MGTIQHLKSK FGDGYIVTMK IKSPKDDLLP DLNPVEQFFQ GNFPGSVQRE RHYNMLQFQV SSSSLARIFQ LLLSHKDSLL IEEYSVTQTT LDQVFVNFAK QQTESHDLPL HPRAAGASRQ AQD // ID ABCAC_HUMAN Reviewed; 2595 AA. AC Q86UK0; Q53QE2; Q53S55; Q8IZW6; Q96JT3; Q9Y4M5; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 3. DT 09-JUL-2014, entry version 114. DE RecName: Full=ATP-binding cassette sub-family A member 12; DE AltName: Full=ATP-binding cassette transporter 12; DE Short=ATP-binding cassette 12; GN Name=ABCA12; Synonyms=ABC12; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP VARIANT THR-777. RC TISSUE=Placenta; RX PubMed=12697999; DOI=10.1159/000069811; RA Annilo T., Shulemin S., Chen Z.Q., Arnould I., Prades C., Lemoine C., RA Maintoux-Larois C., Devaud C., Dean M., Denefle P., Rosier M.; RT "Identification and characterization of a novel ABCA subfamily member, RT ABCA12, located in the lamellar ichthyosis region on 2q34."; RL Cytogenet. Genome Res. 98:169-176(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT THR-777. RC TISSUE=Retina; RA Bonner T.I., Moses T., Detera-Wadleigh S.; RT "A retinal cDNA for the ATP-binding cassette transporter ABCA12."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 221-2595, AND VARIANT THR-777. RA Schaap F.G., van Wijland M., Groen A.K.; RT "Cloning of a novel ABC transporter (ABCA12) tentatively involved in RT lipid homeostatis."; RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2400-2595. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP REVIEW ON VARIANTS, AND INVOLVEMENT IN ARCI. RX PubMed=20672373; DOI=10.1002/humu.21326; RA Akiyama M.; RT "ABCA12 mutations and autosomal recessive congenital ichthyosis: a RT review of genotype/phenotype correlations and of pathogenetic RT concepts."; RL Hum. Mutat. 31:1090-1096(2010). RN [7] RP VARIANTS ARCI4A SER-1380; GLU-1381; HIS-1514; LYS-1539 AND SER-1651. RX PubMed=12915478; DOI=10.1093/hmg/ddg235; RA Lefevre C., Audebert S., Jobard F., Bouadjar B., Lakhdar H., RA Boughdene-Stambouli O., Blanchet-Bardon C., Heilig R., Foglio M., RA Weissenbach J., Lathrop M., Prud'homme J.F., Fischer J.; RT "Mutations in the transporter ABCA12 are associated with lamellar RT ichthyosis type 2."; RL Hum. Mol. Genet. 12:2369-2378(2003). RN [8] RP VARIANT ARCI4B ASN-2365. RX PubMed=15756637; DOI=10.1086/429844; RA Kelsell D.P., Norgett E.E., Unsworth H., Teh M.-T., Cullup T., RA Mein C.A., Dopping-Hepenstal P.J., Dale B.A., Tadini G., Fleckman P., RA Stephens K.G., Sybert V.P., Mallory S.B., North B.V., Witt D.R., RA Sprecher E., Taylor A.E.M., Ilchyshyn A., Kennedy C.T., Goodyear H., RA Moss C., Paige D., Harper J.I., Young B.D., Leigh I.M., Eady R.A.J., RA O'Toole E.A.; RT "Mutations in ABCA12 underlie the severe congenital skin disease RT harlequin ichthyosis."; RL Am. J. Hum. Genet. 76:794-803(2005). RN [9] RP VARIANT ARCI4B ASN-387. RX PubMed=16675967; DOI=10.1038/sj.jid.5700295; RA Akiyama M., Sakai K., Sugiyama-Nakagiri Y., Yamanaka Y., RA McMillan J.R., Sawamura D., Niizeki H., Miyagawa S., Shimizu H.; RT "Compound heterozygous mutations including a de novo missense mutation RT in ABCA12 led to a case of harlequin ichthyosis with moderate clinical RT severity."; RL J. Invest. Dermatol. 126:1518-1523(2006). RN [10] RP VARIANT ARCI4B ARG-1179. RX PubMed=16902423; DOI=10.1038/sj.jid.5700455; RA Thomas A.C., Cullup T., Norgett E.E., Hill T., Barton S., Dale B.A., RA Sprecher E., Sheridan E., Taylor A.E., Wilroy R.S., DeLozier C., RA Burrows N., Goodyear H., Fleckman P., Stephens K.G., Mehta L., RA Watson R.M., Graham R., Wolf R., Slavotinek A., Martin M., Bourn D., RA Mein C.A., O'Toole E.A., Kelsell D.P.; RT "ABCA12 is the major harlequin ichthyosis gene."; RL J. Invest. Dermatol. 126:2408-2413(2006). RN [11] RP VARIANTS ARCI4A PRO-345 AND THR-1494. RX PubMed=17508018; DOI=10.1038/sj.jid.5700885; RA Natsuga K., Akiyama M., Kato N., Sakai K., Sugiyama-Nakagiri Y., RA Nishimura M., Hata H., Abe M., Arita K., Tsuji-Abe Y., Onozuka T., RA Aoyagi S., Kodama K., Ujiie H., Tomita Y., Shimizu H.; RT "Novel ABCA12 mutations identified in two cases of non-bullous RT congenital ichthyosiform erythroderma associated with multiple skin RT malignant neoplasia."; RL J. Invest. Dermatol. 127:2669-2673(2007). RN [12] RP VARIANT ARCI4A ASP-1136. RX PubMed=18284401; DOI=10.1111/j.1365-2133.2008.08439.x; RA Akiyama M., Sakai K., Hatamochi A., Yamazaki S., McMillan J.R., RA Shimizu H.; RT "Novel compound heterozygous nonsense and missense ABCA12 mutations RT lead to nonbullous congenital ichthyosiform erythroderma."; RL Br. J. Dermatol. 158:864-867(2008). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] VAL-476. RX PubMed=18772397; DOI=10.1126/science.1164368; RA Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P., RA Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., RA Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., RA Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D., RA Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C., RA Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N., RA Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.; RT "Core signaling pathways in human pancreatic cancers revealed by RT global genomic analyses."; RL Science 321:1801-1806(2008). RN [14] RP VARIANTS ARCI4A SER-1235; HIS-1514; LEU-1798 AND LYS-1980. RX PubMed=19262603; DOI=10.1038/jid.2009.23; RA Sakai K., Akiyama M., Yanagi T., McMillan J.R., Suzuki T., RA Tsukamoto K., Sugiyama H., Hatano Y., Hayashitani M., Takamori K., RA Nakashima K., Shimizu H.; RT "ABCA12 is a major causative gene for non-bullous congenital RT ichthyosiform erythroderma."; RL J. Invest. Dermatol. 129:2306-2309(2009). RN [15] RP VARIANT ARCI4A VAL-1559. RX PubMed=22257947; DOI=10.1684/ejd.2011.1638; RA Nawaz S., Tariq M., Ahmad I., Malik N.A., Baig S.M., Dahl N., Klar J.; RT "Non-bullous congenital ichthyosiform erythroderma associated with RT homozygosity for a novel missense mutation in an ATP binding domain of RT ABCA12."; RL Eur. J. Dermatol. 22:178-181(2012). CC -!- FUNCTION: Probable transporter involved in lipid homeostasis. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=Additional isoforms seem to exist; CC Name=1; CC IsoId=Q86UK0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86UK0-2; Sequence=VSP_011283, VSP_011284; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Mainly expressed in the stomach, placenta, CC testis and fetal brain. CC -!- DOMAIN: Multifunctional polypeptide with two homologous halves, CC each containing a hydrophobic membrane-anchoring domain and an ATP CC binding cassette (ABC) domain (By similarity). CC -!- DISEASE: Ichthyosis, congenital, autosomal recessive 4A (ARCI4A) CC [MIM:601277]: A form of autosomal recessive congenital ichthyosis, CC a disorder of keratinization with abnormal differentiation and CC desquamation of the epidermis, resulting in abnormal skin scaling CC over the whole body. The main skin phenotypes are lamellar CC ichthyosis (LI) and non-bullous congenital ichthyosiform CC erythroderma (NCIE), although phenotypic overlap within the same CC patient or among patients from the same family can occur. Lamellar CC ichthyosis is a condition often associated with an embedment in a CC collodion-like membrane at birth; skin scales later develop, CC covering the entire body surface. Non-bullous congenital CC ichthyosiform erythroderma characterized by fine whitish scaling CC on an erythrodermal background; larger brownish scales are present CC on the buttocks, neck and legs. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Ichthyosis, congenital, autosomal recessive 4B (ARCI4B) CC [MIM:242500]: A rare, very severe form of congenital ichthyosis, CC in which the neonate is born with a thick covering of armor-like CC scales. The skin dries out to form hard diamond-shaped plaques CC separated by fissures, resembling 'armor plating'. The normal CC facial features are severely affected, with distortion of the lips CC (eclabion), eyelids (ectropion), ears, and nostrils. Affected CC babies are often born prematurely and rarely survive the perinatal CC period. Babies who survive into infancy and beyond develop skin CC changes resembling severe non-bullous congenital ichthyosiform CC erythroderma. Note=The disease is caused by mutations affecting CC the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA CC family. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC -!- SEQUENCE CAUTION: CC Sequence=AAN40735.1; Type=Erroneous initiation; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q86UK0"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY219711; AAP21093.1; -; mRNA. DR EMBL; AY033486; AAK54355.1; -; mRNA. DR EMBL; AC072062; AAY24276.1; -; Genomic_DNA. DR EMBL; AC114780; AAY24230.1; -; Genomic_DNA. DR EMBL; AF418105; AAN40735.1; ALT_INIT; mRNA. DR EMBL; AL080207; CAB45776.1; -; mRNA. DR CCDS; CCDS33372.1; -. [Q86UK0-1] DR CCDS; CCDS33373.1; -. [Q86UK0-2] DR PIR; T12512; T12512. DR RefSeq; NP_056472.2; NM_015657.3. [Q86UK0-2] DR RefSeq; NP_775099.2; NM_173076.2. [Q86UK0-1] DR UniGene; Hs.134585; -. DR ProteinModelPortal; Q86UK0; -. DR BioGrid; 117585; 1. DR STRING; 9606.ENSP00000272895; -. DR TCDB; 3.A.1.211.13; the atp-binding cassette (abc) superfamily. DR PhosphoSite; Q86UK0; -. DR DMDM; 269849713; -. DR MaxQB; Q86UK0; -. DR PaxDb; Q86UK0; -. DR PRIDE; Q86UK0; -. DR Ensembl; ENST00000272895; ENSP00000272895; ENSG00000144452. [Q86UK0-1] DR Ensembl; ENST00000389661; ENSP00000374312; ENSG00000144452. [Q86UK0-2] DR GeneID; 26154; -. DR KEGG; hsa:26154; -. DR UCSC; uc002vev.3; human. [Q86UK0-2] DR UCSC; uc002vew.3; human. [Q86UK0-1] DR CTD; 26154; -. DR GeneCards; GC02M215796; -. DR GeneReviews; ABCA12; -. DR HGNC; HGNC:14637; ABCA12. DR HPA; HPA043194; -. DR MIM; 242500; phenotype. DR MIM; 601277; phenotype. DR MIM; 607800; gene. DR neXtProt; NX_Q86UK0; -. DR Orphanet; 79394; Congenital non-bullous ichthyosiform erythroderma. DR Orphanet; 457; Harlequin ichthyosis. DR Orphanet; 313; Lamellar ichthyosis. DR PharmGKB; PA29604; -. DR eggNOG; COG1131; -. DR HOGENOM; HOG000168538; -. DR HOVERGEN; HBG080807; -. DR InParanoid; Q86UK0; -. DR KO; K05646; -. DR OMA; GMAAPWY; -. DR OrthoDB; EOG78D7J6; -. DR PhylomeDB; Q86UK0; -. DR TreeFam; TF105191; -. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR GeneWiki; ABCA12; -. DR GenomeRNAi; 26154; -. DR NextBio; 48241; -. DR PRO; PR:Q86UK0; -. DR ArrayExpress; Q86UK0; -. DR Bgee; Q86UK0; -. DR CleanEx; HS_ABCA12; -. DR Genevestigator; Q86UK0; -. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0019725; P:cellular homeostasis; NAS:UniProtKB. DR GO; GO:0035627; P:ceramide transport; IEA:Ensembl. DR GO; GO:0061436; P:establishment of skin barrier; IEA:Ensembl. DR GO; GO:0031424; P:keratinization; IEA:Ensembl. DR GO; GO:0055088; P:lipid homeostasis; IEA:Ensembl. DR GO; GO:0006869; P:lipid transport; NAS:UniProtKB. DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl. DR GO; GO:0043129; P:surfactant homeostasis; IEA:Ensembl. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR026082; ABC_A. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR19229; PTHR19229; 1. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Complete proteome; KW Disease mutation; Glycoprotein; Ichthyosis; Membrane; KW Nucleotide-binding; Polymorphism; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 2595 ATP-binding cassette sub-family A member FT 12. FT /FTId=PRO_0000093300. FT TRANSMEM 23 43 Helical; (Potential). FT TRANSMEM 1065 1085 Helical; (Potential). FT TRANSMEM 1112 1132 Helical; (Potential). FT TRANSMEM 1145 1165 Helical; (Potential). FT TRANSMEM 1174 1194 Helical; (Potential). FT TRANSMEM 1200 1220 Helical; (Potential). FT TRANSMEM 1250 1270 Helical; (Potential). FT TRANSMEM 1747 1767 Helical; (Potential). FT TRANSMEM 1979 1999 Helical; (Potential). FT TRANSMEM 2035 2055 Helical; (Potential). FT TRANSMEM 2072 2092 Helical; (Potential). FT TRANSMEM 2103 2123 Helical; (Potential). FT TRANSMEM 2187 2207 Helical; (Potential). FT TRANSMEM 2270 2290 Helical; (Potential). FT DOMAIN 1346 1577 ABC transporter 1. FT DOMAIN 2254 2489 ABC transporter 2. FT NP_BIND 1378 1385 ATP 1 (Potential). FT NP_BIND 2290 2297 ATP 2 (Potential). FT CARBOHYD 156 156 N-linked (GlcNAc...) (Potential). FT CARBOHYD 174 174 N-linked (GlcNAc...) (Potential). FT CARBOHYD 214 214 N-linked (GlcNAc...) (Potential). FT CARBOHYD 275 275 N-linked (GlcNAc...) (Potential). FT CARBOHYD 333 333 N-linked (GlcNAc...) (Potential). FT CARBOHYD 367 367 N-linked (GlcNAc...) (Potential). FT CARBOHYD 383 383 N-linked (GlcNAc...) (Potential). FT CARBOHYD 412 412 N-linked (GlcNAc...) (Potential). FT CARBOHYD 435 435 N-linked (GlcNAc...) (Potential). FT CARBOHYD 528 528 N-linked (GlcNAc...) (Potential). FT CARBOHYD 543 543 N-linked (GlcNAc...) (Potential). FT CARBOHYD 577 577 N-linked (GlcNAc...) (Potential). FT CARBOHYD 608 608 N-linked (GlcNAc...) (Potential). FT CARBOHYD 623 623 N-linked (GlcNAc...) (Potential). FT CARBOHYD 648 648 N-linked (GlcNAc...) (Potential). FT CARBOHYD 752 752 N-linked (GlcNAc...) (Potential). FT CARBOHYD 826 826 N-linked (GlcNAc...) (Potential). FT CARBOHYD 920 920 N-linked (GlcNAc...) (Potential). FT CARBOHYD 963 963 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1170 1170 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1524 1524 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1663 1663 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1704 1704 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1769 1769 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1819 1819 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1835 1835 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1876 1876 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1921 1921 N-linked (GlcNAc...) (Potential). FT CARBOHYD 1952 1952 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2178 2178 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2208 2208 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2223 2223 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2318 2318 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2542 2542 N-linked (GlcNAc...) (Potential). FT CARBOHYD 2547 2547 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 1 318 Missing (in isoform 2). FT /FTId=VSP_011283. FT VAR_SEQ 319 328 LLYTLDSPAQ -> MFTYIKIITS (in isoform 2). FT /FTId=VSP_011284. FT VARIANT 199 199 W -> C (in dbSNP:rs16853238). FT /FTId=VAR_055473. FT VARIANT 237 237 N -> H (in dbSNP:rs11890512). FT /FTId=VAR_055474. FT VARIANT 274 274 Q -> R (in dbSNP:rs11890468). FT /FTId=VAR_055475. FT VARIANT 287 287 R -> G (in dbSNP:rs11891778). FT /FTId=VAR_055476. FT VARIANT 345 345 T -> P (in ARCI4A; skin phenotype FT consistent with non-bullous congenital FT ichthyosiform erythroderma). FT /FTId=VAR_067075. FT VARIANT 387 387 S -> N (in ARCI4B). FT /FTId=VAR_067076. FT VARIANT 459 459 S -> T (in dbSNP:rs7560008). FT /FTId=VAR_019597. FT VARIANT 476 476 A -> V (in a pancreatic ductal FT adenocarcinoma sample; somatic mutation). FT /FTId=VAR_062663. FT VARIANT 550 550 E -> G (in dbSNP:rs16853149). FT /FTId=VAR_027444. FT VARIANT 777 777 S -> T (in dbSNP:rs7560008). FT /FTId=VAR_027445. FT VARIANT 1136 1136 G -> D (in ARCI4A; skin phenotype FT consistent with non-bullous congenital FT ichthyosiform erythroderma). FT /FTId=VAR_067077. FT VARIANT 1179 1179 G -> R (in ARCI4B). FT /FTId=VAR_067078. FT VARIANT 1235 1235 W -> S (in ARCI4A; skin phenotype FT consistent with non-bullous congenital FT ichthyosiform erythroderma). FT /FTId=VAR_067079. FT VARIANT 1251 1251 G -> D (in dbSNP:rs13414448). FT /FTId=VAR_027446. FT VARIANT 1380 1380 N -> S (in ARCI4A; dbSNP:rs28940269). FT /FTId=VAR_019598. FT VARIANT 1381 1381 G -> E (in ARCI4A; dbSNP:rs28940268). FT /FTId=VAR_019599. FT VARIANT 1494 1494 I -> T (in ARCI4A; skin phenotype FT consistent with non-bullous congenital FT ichthyosiform erythroderma). FT /FTId=VAR_067080. FT VARIANT 1514 1514 R -> H (in ARCI4A; dbSNP:rs28940270). FT /FTId=VAR_019600. FT VARIANT 1539 1539 E -> K (in ARCI4A; dbSNP:rs28940271). FT /FTId=VAR_019601. FT VARIANT 1546 1546 R -> C (in dbSNP:rs13401480). FT /FTId=VAR_027447. FT VARIANT 1559 1559 G -> V (in ARCI4A; skin phenotype FT consistent with non-bullous congenital FT ichthyosiform erythroderma). FT /FTId=VAR_067081. FT VARIANT 1651 1651 G -> S (in ARCI4A; dbSNP:rs28940568). FT /FTId=VAR_019602. FT VARIANT 1798 1798 P -> L (in ARCI4A; skin phenotype FT consistent with non-bullous congenital FT ichthyosiform erythroderma). FT /FTId=VAR_067082. FT VARIANT 1980 1980 T -> K (in ARCI4A; skin phenotype FT consistent with non-bullous congenital FT ichthyosiform erythroderma). FT /FTId=VAR_067083. FT VARIANT 2064 2064 E -> K (in dbSNP:rs1213011). FT /FTId=VAR_027448. FT VARIANT 2365 2365 D -> N (in ARCI4B; dbSNP:rs726070). FT /FTId=VAR_027449. FT CONFLICT 651 651 Y -> D (in Ref. 1; AAP21093). FT CONFLICT 811 811 Y -> H (in Ref. 1; AAP21093). FT CONFLICT 826 826 N -> D (in Ref. 2; AAK54355). FT CONFLICT 2079 2079 Y -> H (in Ref. 1; AAP21093). SQ SEQUENCE 2595 AA; 293237 MW; 5B71359B642BBAE6 CRC64; MASLFHQLQI LVWKNWLGVK RQPLWTLVLI LWPVIIFIIL AITRTKFPPT AKPTCYLAPR NLPSTGFFPF LQTLLCDTDS KCKDTPYGPQ DLLRRKGIDD ALFKDSEILR KSSNLDKDSS LSFQSTQVPE RRHASLATVF PSPSSDLEIP GTYTFNGSQV LARILGLEKL LKQNSTSEDI RRELCDSYSG YIVDDAFSWT FLGRNVFNKF CLSNMTLLES SLQELNKQFS QLSSDPNNQK IVFQEIVRML SFFSQVQEQK AVWQLLSSFP NVFQNDTSLS NLFDVLRKAN SVLLVVQKVY PRFATNEGFR TLQKSVKHLL YTLDSPAQGD SDNITHVWNE DDGQTLSPSS LAAQLLILEN FEDALLNISA NSPYIPYLAC VRNVTDSLAR GSPENLRLLQ STIRFKKSFL RNGSYEDYFP PVPEVLKSKL SQLRNLTELL CESETFSLIE KSCQLSDMSF GSLCEESEFD LQLLEAAELG TEIAASLLYH DNVISKKVRD LLTGDPSKIN LNMDQFLEQA LQMNYLENIT QLIPIIEAML HVNNSADASE KPGQLLEMFK NVEELKEDLR RTTGMSNRTI DKLLAIPIPD NRAEIISQVF WLHSCDTNIT TPKLEDAMKE FCNLSLSERS RQSYLIGLTL LHYLNIYNFT YKVFFPRKDQ KPVEKMMELF IRLKEILNQM ASGTHPLLDK MRSLKQMHLP RSVPLTQAMY RSNRMNTPQG SFSTISQALC SQGITTEYLT AMLPSSQRPK GNHTKDFLTY KLTKEQIASK YGIPINSTPF CFSLYKDIIN MPAGPVIWAF LKPMLLGRIL YAPYNPVTKA IMEKSNVTLR QLAELREKSQ EWMDKSPLFM NSFHLLNQAI PMLQNTLRNP FVQVFVKFSV GLDAVELLKQ IDELDILRLK LENNIDIIDQ LNTLSSLTVN ISSCVLYDRI QAAKTIDEME REAKRLYKSN ELFGSVIFKL PSNRSWHRGY DSGNVFLPPV IKYTIRMSLK TAQTTRSLRT KIWAPGPHNS PSHNQIYGRA FIYLQDSIER AIIELQTGRN SQEIAVQVQA IPYPCFMKDN FLTSVSYSLP IVLMVAWVVF IAAFVKKLVY EKDLRLHEYM KMMGVNSCSH FFAWLIESVG FLLVTIVILI IILKFGNILP KTNGFILFLY FSDYSFSVIA MSYLISVFFN NTNIAALIGS LIYIIAFFPF IVLVTVENEL SYVLKVFMSL LSPTAFSYAS QYIARYEEQG IGLQWENMYT SPVQDDTTSF GWLCCLILAD SFIYFLIAWY VRNVFPGTYG MAAPWYFPIL PSYWKERFGC AEVKPEKSNG LMFTNIMMQN TNPSASPEYM FSSNIEPEPK DLTVGVALHG VTKIYGSKVA VDNLNLNFYE GHITSLLGPN GAGKTTTISM LTGLFGASAG TIFVYGKDIK TDLHTVRKNM GVCMQHDVLF SYLTTKEHLL LYGSIKVPHW TKKQLHEEVK RTLKDTGLYS HRHKRVGTLS GGMKRKLSIS IALIGGSRVV ILDEPSTGVD PCSRRSIWDV ISKNKTARTI ILSTHHLDEA EVLSDRIAFL EQGGLRCCGS PFYLKEAFGD GYHLTLTKKK SPNLNANAVC DTMAVTAMIQ SHLPEAYLKE DIGGELVYVL PPFSTKVSGA YLSLLRALDN GMGDLNIGCY GISDTTVEEV FLNLTKESQK NSAMSLEHLT QKKIGNSNAN GISTPDDLSV SSSNFTDRDD KILTRGERLD GFGLLLKKIM AILIKRFHHT RRNWKGLIAQ VILPIVFVTT AMGLGTLRNS SNSYPEIQIS PSLYGTSEQT AFYANYHPST EALVSAMWDF PGIDNMCLNT SDLQCLNKDS LEKWNTSGEP ITNFGVCSCS ENVQECPKFN YSPPHRRTYS SQVIYNLTGQ RVENYLISTA NEFVQKRYGG WSFGLPLTKD LRFDITGVPA NRTLAKVWYD PEGYHSLPAY LNSLNNFLLR VNMSKYDAAR HGIIMYSHPY PGVQDQEQAT ISSLIDILVA LSILMGYSVT TASFVTYVVR EHQTKAKQLQ HISGIGVTCY WVTNFIYDMV FYLVPVAFSI GIIAIFKLPA FYSENNLGAV SLLLLLFGYA TFSWMYLLAG LFHETGMAFI TYVCVNLFFG INSIVSLSVV YFLSKEKPND PTLELISETL KRIFLIFPQF CFGYGLIELS QQQSVLDFLK AYGVEYPNET FEMNKLGAMF VALVSQGTMF FSLRLLINES LIKKLRLFFR KFNSSHVRET IDEDEDVRAE RLRVESGAAE FDLVQLYCLT KTYQLIHKKI IAVNNISIGI PAGECFGLLG VNGAGKTTIF KMLTGDIIPS SGNILIRNKT GSLGHVDSHS SLVGYCPQED ALDDLVTVEE HLYFYARVHG IPEKDIKETV HKLLRRLHLM PFKDRATSMC SYGTKRKLST ALALIGKPSI LLLDEPSSGM DPKSKRHLWK IISEEVQNKC SVILTSHSME ECEALCTRLA IMVNGKFQCI GSLQHIKSRF GRGFTVKVHL KNNKVTMETL TKFMQLHFPK TYLKDQHLSM LEYHVPVTAG GVANIFDLLE TNKTALNITN FLVSQTTLEE VFINFAKDQK SYETADTSSQ GSTISVDSQD DQMES // ID ABCB5_HUMAN Reviewed; 812 AA. AC Q2M3G0; A4D131; A7BKA4; B5MD19; B7WPL1; F8QQP8; J3KQ04; Q2M3I5; AC Q5I5Q7; Q5I5Q8; Q6KG50; Q6XFQ5; Q8IXA1; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 09-JUL-2014, entry version 87. DE RecName: Full=ATP-binding cassette sub-family B member 5; DE AltName: Full=ABCB5 P-gp; DE AltName: Full=P-glycoprotein ABCB5; GN Name=ABCB5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND VARIANT LYS-525. RC TISSUE=Melanocyte, and Melanoma; RX PubMed=12960149; DOI=10.1074/jbc.M308700200; RA Frank N.Y., Pendse S.S., Lapchak P.H., Margaryan A., Shlain D., RA Doeing C., Sayegh M.H., Frank M.H.; RT "Regulation of progenitor cell fusion by ABCB5 P-glycoprotein, a novel RT human ATP-binding cassette transporter."; RL J. Biol. Chem. 278:47156-47165(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS GLU-115 AND RP LYS-525, AND TISSUE SPECIFICITY. RC TISSUE=Melanoma; RX PubMed=15760339; DOI=10.1111/j.1600-0749.2005.00214.x; RA Chen K.G., Szakacs G., Annereau J.-P., Rouzaud F., Liang X.-J., RA Valencia J.C., Nagineni C.N., Hooks J.J., Hearing V.J., RA Gottesman M.M.; RT "Principal expression of two mRNA isoforms (ABCB 5alpha and ABCB RT 5beta) of the ATP-binding cassette transporter gene ABCB 5 in melanoma RT cells and melanocytes."; RL Pigment Cell Res. 18:102-112(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Colon adenocarcinoma; RX PubMed=21652540; DOI=10.1158/0008-5472.CAN-11-0221; RA Wilson B.J., Schatton T., Zhan Q., Gasser M., Ma J., Saab K.R., RA Schanche R., Waaga-Gasser A.M., Gold J.S., Huang Q., Murphy G.F., RA Frank M.H., Frank N.Y.; RT "ABCB5 identifies a therapy-refractory tumor cell population in RT colorectal cancer patients."; RL Cancer Res. 71:5307-5316(2011). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, AND VARIANT LYS-525. RC TISSUE=Prostate, and Testis; RX PubMed=22306008; DOI=10.1016/j.bbrc.2012.01.090; RA Kawanobe T., Kogure S., Nakamura S., Sato M., Katayama K., RA Mitsuhashi J., Noguchi K., Sugimoto Y.; RT "Expression of human ABCB5 confers resistance to taxanes and RT anthracyclines."; RL Biochem. Biophys. Res. Commun. 418:736-741(2012). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT LYS-525. RA Meij I.C., van Aubel R., Tammur J., Dean M., Russel F.G., RA Allikmets R., Cremers F.P.M.; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., RA Mural R.J., Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-525. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Melanoma; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP FUNCTION. RX PubMed=15205344; DOI=10.1158/0008-5472.CAN-03-3884; RA Huang Y., Anderle P., Bussey K.J., Barbacioru C., Shankavaram U., RA Dai Z., Reinhold W.C., Papp A., Weinstein J.N., Sadee W.; RT "Membrane transporters and channels: role of the transportome in RT cancer chemosensitivity and chemoresistance."; RL Cancer Res. 64:4294-4301(2004). RN [11] RP FUNCTION. RX PubMed=15899824; DOI=10.1158/0008-5472.CAN-04-3327; RA Frank N.Y., Margaryan A., Huang Y., Schatton T., Waaga-Gasser A.M., RA Gasser M., Sayegh M.H., Sadee W., Frank M.H.; RT "ABCB5-mediated doxorubicin transport and chemoresistance in human RT malignant melanoma."; RL Cancer Res. 65:4320-4333(2005). RN [12] RP VARIANT [LARGE SCALE ANALYSIS] VAL-230. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] THR-435. RX PubMed=18772397; DOI=10.1126/science.1164368; RA Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P., RA Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., RA Lin M.T., Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., RA Nikolsky Y., Hartigan J., Smith D.R., Hidalgo M., Leach S.D., RA Klein A.P., Jaffee E.M., Goggins M., Maitra A., Iacobuzio-Donahue C., RA Eshleman J.R., Kern S.E., Hruban R.H., Karchin R., Papadopoulos N., RA Parmigiani G., Vogelstein B., Velculescu V.E., Kinzler K.W.; RT "Core signaling pathways in human pancreatic cancers revealed by RT global genomic analyses."; RL Science 321:1801-1806(2008). CC -!- FUNCTION: Plasma membrane transporter able to mediate efflux from CC cells of the rhodamine dye and of the therapeutic drug CC doxorubicin. Responsible for the resistance to doxorubicin of a CC subset of malignant melanomas. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=ABCB5beta; CC IsoId=Q2M3G0-1; Sequence=Displayed; CC Name=2; Synonyms=ABCB5alpha; CC IsoId=Q2M3G0-2; Sequence=VSP_021075, VSP_021076; CC Name=3; CC IsoId=Q2M3G0-3; Sequence=VSP_045489, VSP_045490; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q2M3G0-4; Sequence=VSP_046857; CC Note=Contains 1 extra ABC transmembrane type-1 domain; CC -!- TISSUE SPECIFICITY: Expressed by CD133-expressing progenitor cells CC among epidermal melanocytes (at protein level). Widely expressed CC with specific expression in pigment cells. Also expressed in CC several malignant tissues. CC -!- MISCELLANEOUS: Depletion of ABCB5 by RNAi increases the CC sensitivity to several drugs of a subset of melanoma cells. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB CC family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC -!- CAUTION: Was named ABCB1 by some authors. CC -!- SEQUENCE CAUTION: CC Sequence=AAN76500.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAQ03033.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/ABCB5ID44305ch7p15.html"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF319622; AAN76500.1; ALT_INIT; mRNA. DR EMBL; AF399931; AAQ03033.1; ALT_INIT; mRNA. DR EMBL; AY090613; AAM09027.1; -; mRNA. DR EMBL; AY234788; AAO73470.1; -; mRNA. DR EMBL; AY851364; AAW31629.1; -; mRNA. DR EMBL; AY851365; AAW31630.1; -; mRNA. DR EMBL; GU437216; ADV32636.1; -; mRNA. DR EMBL; AB353947; BAF75364.1; -; mRNA. DR EMBL; AY230001; AAP55848.1; -; mRNA. DR EMBL; AC002486; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005060; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236948; EAL24273.1; -; Genomic_DNA. DR EMBL; CH471073; EAW93726.1; -; Genomic_DNA. DR EMBL; BC104894; AAI04895.2; -; mRNA. DR EMBL; BC104920; AAI04921.1; -; mRNA. DR EMBL; BC110370; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS5371.1; -. [Q2M3G0-1] DR CCDS; CCDS55090.1; -. [Q2M3G0-4] DR CCDS; CCDS55091.1; -. [Q2M3G0-2] DR CCDS; CCDS55092.1; -. [Q2M3G0-3] DR RefSeq; NP_001157413.1; NM_001163941.1. [Q2M3G0-4] DR RefSeq; NP_001157414.1; NM_001163942.1. [Q2M3G0-2] DR RefSeq; NP_001157465.1; NM_001163993.2. [Q2M3G0-3] DR RefSeq; NP_848654.3; NM_178559.5. [Q2M3G0-1] DR UniGene; Hs.404102; -. DR ProteinModelPortal; Q2M3G0; -. DR SMR; Q2M3G0; 16-197, 203-811. DR IntAct; Q2M3G0; 1. DR ChEMBL; CHEMBL1772928; -. DR TCDB; 3.A.1.201.13; the atp-binding cassette (abc) superfamily. DR PhosphoSite; Q2M3G0; -. DR DMDM; 308153645; -. DR PaxDb; Q2M3G0; -. DR PRIDE; Q2M3G0; -. DR DNASU; 340273; -. DR Ensembl; ENST00000258738; ENSP00000258738; ENSG00000004846. [Q2M3G0-1] DR Ensembl; ENST00000404938; ENSP00000384881; ENSG00000004846. [Q2M3G0-4] DR Ensembl; ENST00000406935; ENSP00000383899; ENSG00000004846. [Q2M3G0-3] DR Ensembl; ENST00000443026; ENSP00000406730; ENSG00000004846. [Q2M3G0-2] DR GeneID; 340273; -. DR KEGG; hsa:340273; -. DR UCSC; uc003suv.4; human. [Q2M3G0-2] DR UCSC; uc003suw.4; human. [Q2M3G0-1] DR CTD; 340273; -. DR GeneCards; GC07P020653; -. DR H-InvDB; HIX0025281; -. DR HGNC; HGNC:46; ABCB5. DR HPA; HPA026975; -. DR MIM; 611785; gene. DR neXtProt; NX_Q2M3G0; -. DR PharmGKB; PA24387; -. DR eggNOG; COG1132; -. DR HOVERGEN; HBG080809; -. DR InParanoid; Q2M3G0; -. DR KO; K05660; -. DR OMA; YCIGAAV; -. DR OrthoDB; EOG7Z3F4H; -. DR PhylomeDB; Q2M3G0; -. DR TreeFam; TF105193; -. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR GeneWiki; ABCB5; -. DR GenomeRNAi; 340273; -. DR NextBio; 35535241; -. DR PRO; PR:Q2M3G0; -. DR ArrayExpress; Q2M3G0; -. DR Bgee; Q2M3G0; -. DR CleanEx; HS_ABCB5; -. DR Genevestigator; Q2M3G0; -. DR GO; GO:0016324; C:apical plasma membrane; IBA:RefGenome. DR GO; GO:0000139; C:Golgi membrane; IBA:RefGenome. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB. DR GO; GO:0046581; C:intercellular canaliculus; IBA:RefGenome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:RefGenome. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0042391; P:regulation of membrane potential; IDA:UniProtKB. DR GO; GO:0055085; P:transmembrane transport; IDA:UniProtKB. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR001140; ABC_transptr_TM_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell membrane; Complete proteome; KW Membrane; Nucleotide-binding; Polymorphism; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 812 ATP-binding cassette sub-family B member FT 5. FT /FTId=PRO_0000253575. FT TOPO_DOM 1 247 Extracellular (Potential). FT TRANSMEM 248 268 Helical; (Potential). FT TOPO_DOM 269 291 Cytoplasmic (Potential). FT TRANSMEM 292 312 Helical; (Potential). FT TOPO_DOM 313 381 Extracellular (Potential). FT TRANSMEM 382 402 Helical; (Potential). FT TOPO_DOM 403 471 Cytoplasmic (Potential). FT TRANSMEM 472 492 Helical; (Potential). FT TOPO_DOM 493 508 Extracellular (Potential). FT TRANSMEM 509 529 Helical; (Potential). FT TOPO_DOM 530 812 Cytoplasmic (Potential). FT DOMAIN 2 177 ABC transporter 1. FT DOMAIN 247 535 ABC transmembrane type-1. FT DOMAIN 570 808 ABC transporter 2. FT NP_BIND 605 612 ATP (Potential). FT VAR_SEQ 1 1 M -> MENSERAEEMQENYQRNGTAEEQPKLRKEAVGSIEI FT FRFADGLDITLMILGILASLVNGACLPLMPLVLGEMSDNLI FT SGCLVQTNTTNYQNCTQSQEKLNEDMTLLTLYYVGIGVAAL FT IFGYIQISLWIITAARQTKRIRKQFFHSVLAQDIGWFDSCD FT IGELNTRMTDDIDKISDGIGDKIALLFQNMSTFSIGLAVGL FT VKGWKLTLVTLSTSPLIMASAAACSRMVISLTSKELSAYSK FT AGAVAEEVLSSIRTVIAFRAQEKELQRYTQNLKDAKDFGIK FT RTIASKVSLGAVYFFMNGTYGLAFWYGTSLILNGEPGYTIG FT TVLAVFFSVIHSSYCIGAAVPHFETFAIARGAAFHIFQVID FT KKPSIDNFSTAGYKPESIEGTVEFKNVSFNYPSRPSIKILK FT GLNLRIKSGETVALVGLNGSGKSTVVQLLQRLYDPDDGFIM FT (in isoform 4). FT /FTId=VSP_046857. FT VAR_SEQ 125 131 ASKGRTT -> DTPRYSF (in isoform 2). FT /FTId=VSP_021075. FT VAR_SEQ 125 126 AS -> KK (in isoform 3). FT /FTId=VSP_045489. FT VAR_SEQ 127 812 Missing (in isoform 3). FT /FTId=VSP_045490. FT VAR_SEQ 132 812 Missing (in isoform 2). FT /FTId=VSP_021076. FT VARIANT 115 115 K -> E (in dbSNP:rs2301641). FT /FTId=VAR_028387. FT VARIANT 224 224 K -> R (in dbSNP:rs13222448). FT /FTId=VAR_028388. FT VARIANT 230 230 E -> V (in a colorectal cancer sample; FT somatic mutation). FT /FTId=VAR_035731. FT VARIANT 435 435 A -> T (in a pancreatic ductal FT adenocarcinoma sample; somatic mutation). FT /FTId=VAR_062662. FT VARIANT 460 460 Q -> H (in dbSNP:rs35885925). FT /FTId=VAR_033456. FT VARIANT 470 470 A -> T (in dbSNP:rs17143304). FT /FTId=VAR_028389. FT VARIANT 525 525 E -> K (in dbSNP:rs6461515). FT /FTId=VAR_028390. FT CONFLICT 132 132 I -> M (in Ref. 1; AAN76500). FT CONFLICT 696 696 L -> P (in Ref. 2; AAW31630). SQ SEQUENCE 812 AA; 89832 MW; 588E5F90AE305BE5 CRC64; MVDENDIRAL NVRHYRDHIG VVSQEPVLFG TTISNNIKYG RDDVTDEEME RAAREANAYD FIMEFPNKFN TLVGEKGAQM SGGQKQRIAI ARALVRNPKI LILDEATSAL DSESKSAVQA ALEKASKGRT TIVVAHRLST IRSADLIVTL KDGMLAEKGA HAELMAKRGL YYSLVMSQDI KKADEQMESM TYSTERKTNS LPLHSVKSIK SDFIDKAEES TQSKEISLPE VSLLKILKLN KPEWPFVVLG TLASVLNGTV HPVFSIIFAK IITMFGNNDK TTLKHDAEIY SMIFVILGVI CFVSYFMQGL FYGRAGEILT MRLRHLAFKA MLYQDIAWFD EKENSTGGLT TILAIDIAQI QGATGSRIGV LTQNATNMGL SVIISFIYGW EMTFLILSIA PVLAVTGMIE TAAMTGFANK DKQELKHAGK IATEALENIR TIVSLTREKA FEQMYEEMLQ TQHRNTSKKA QIIGSCYAFS HAFIYFAYAA GFRFGAYLIQ AGRMTPEGMF IVFTAIAYGA MAIGETLVLA PEYSKAKSGA AHLFALLEKK PNIDSRSQEG KKPDTCEGNL EFREVSFFYP CRPDVFILRG LSLSIERGKT VAFVGSSGCG KSTSVQLLQR LYDPVQGQVL FDGVDAKELN VQWLRSQIAI VPQEPVLFNC SIAENIAYGD NSRVVPLDEI KEAANAANIH SFIEGLPEKY NTQVGLKGAQ LSGGQKQRLA IARALLQKPK ILLLDEATSA LDNDSEKVVQ HALDKARTGR TCLVVTHRLS AIQNADLIVV LHNGKIKEQG THQELLRNRD IYFKLVNAQS VQ // ID ABCB6_HUMAN Reviewed; 842 AA. AC Q9NP58; O75542; Q49A66; Q59GQ5; Q6ZME6; Q96ME8; Q9HAQ6; Q9HAQ7; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-JUL-2014, entry version 142. DE RecName: Full=ATP-binding cassette sub-family B member 6, mitochondrial; DE AltName: Full=Mitochondrial ABC transporter 3; DE Short=Mt-ABC transporter 3; DE AltName: Full=P-glycoprotein-related protein; DE AltName: Full=Ubiquitously-expressed mammalian ABC half transporter; GN Name=ABCB6; Synonyms=MTABC3, PRP, UMAT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=10837493; DOI=10.1074/jbc.275.23.17536; RA Mitsuhashi N., Miki T., Senbongi H., Yokoi N., Yano H., Miyazaki M., RA Nakajima N., Iwanaga T., Yokoyama Y., Shibata T., Seino S.; RT "MTABC3, a novel mitochondrial ATP-binding cassette protein involved RT in iron homeostasis."; RL J. Biol. Chem. 275:17536-17540(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 1-229. RC TISSUE=Colon, and Liver; RX PubMed=11955620; DOI=10.1016/S0167-4781(01)00340-2; RA Emadi-Konjin H.-P., Zhang H., Anandan V., Sun D., Schuetz J.D., RA Furuya K.N.; RT "Isolation of a genomic clone containing the promoter region of the RT human ATP binding cassette (ABC) transporter, ABCB6."; RL Biochim. Biophys. Acta 1574:117-130(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Hirsch-Ernst K.I., Schaefer A., Ernst B.-P., Schmitz-Salue C., RA Awuah D., Kahl G.F.; RT "Subcellular localization of the ABC transporter umat."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 112-842 (ISOFORM 1). RC TISSUE=Hepatoma, and Neuroepithelium; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 332-842 (ISOFORM 1). RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY CELLULAR PORPHYRINS, RP SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION WITH HEMIN. RX PubMed=17006453; DOI=10.1038/nature05125; RA Krishnamurthy P.C., Du G., Fukuda Y., Sun D., Sampath J., Mercer K.E., RA Wang J., Sosa-Pineda B., Murti K.G., Schuetz J.D.; RT "Identification of a mammalian mitochondrial porphyrin transporter."; RL Nature 443:586-589(2006). RN [9] RP SUBCELLULAR LOCATION. RX PubMed=17661442; DOI=10.1021/bi700015m; RA Paterson J.K., Shukla S., Black C.M., Tachiwada T., Garfield S., RA Wincovitch S., Ernst D.N., Agadir A., Li X., Ambudkar S.V., RA Szakacs G., Akiyama S., Gottesman M.M.; RT "Human ABCB6 localizes to both the outer mitochondrial membrane and RT the plasma membrane."; RL Biochemistry 46:9443-9452(2007). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=18279659; DOI=10.1016/j.bbrc.2008.02.027; RA Tsuchida M., Emi Y., Kida Y., Sakaguchi M.; RT "Human ABC transporter isoform B6 (ABCB6) localizes primarily in the RT Golgi apparatus."; RL Biochem. Biophys. Res. Commun. 369:369-375(2008). RN [11] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS MCOPCB7 THR-57 AND RP VAL-811, AND CHARACTERIZATION OF VARIANTS MCOPCB7 THR-57 AND VAL-811. RX PubMed=22226084; DOI=10.1016/j.ajhg.2011.11.026; RA Wang L., He F., Bu J., Liu X., Du W., Dong J., Cooney J.D., RA Dubey S.K., Shi Y., Gong B., Li J., McBride P.F., Jia Y., Lu F., RA Soltis K.A., Lin Y., Namburi P., Liang C., Sundaresan P., Paw B.H., RA Li D.Y., Phillips J.D., Yang Z.; RT "ABCB6 mutations cause ocular coloboma."; RL Am. J. Hum. Genet. 90:40-48(2012). RN [12] RP INVOLVEMENT IN LANGEREIS BLOOD GROUP SYSTEM. RX PubMed=22246506; DOI=10.1038/ng.1069; RA Helias V., Saison C., Ballif B.A., Peyrard T., Takahashi J., RA Takahashi H., Tanaka M., Deybach J.C., Puy H., Le Gall M., Sureau C., RA Pham B.N., Le Pennec P.Y., Tani Y., Cartron J.P., Arnaud L.; RT "ABCB6 is dispensable for erythropoiesis and specifies the new blood RT group system Langereis."; RL Nat. Genet. 44:170-173(2012). RN [13] RP STRUCTURE BY NMR OF 558-842 IN COMPLEX WITH ADP. RX PubMed=16791740; DOI=10.1007/s10858-006-9000-6; RA Kurashima-Ito K., Ikeya T., Senbongi H., Tochio H., Mikawa T., RA Shibata T., Ito Y.; RT "Heteronuclear multidimensional NMR and homology modelling studies of RT the C-terminal nucleotide-binding domain of the human mitochondrial RT ABC transporter ABCB6."; RL J. Biomol. NMR 35:53-71(2006). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 558-842 IN COMPLEXES WITH RP ADP; ATP AND PHOSPHATE. RX PubMed=20823549; DOI=10.1107/S0907444910028593; RA Haffke M., Menzel A., Carius Y., Jahn D., Heinz D.W.; RT "Structures of the nucleotide-binding domain of the human ABCB6 RT transporter and its complexes with nucleotides."; RL Acta Crystallogr. D 66:979-987(2010). RN [15] RP VARIANT [LARGE SCALE ANALYSIS] GLY-69. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [16] RP VARIANTS DUH3 GLY-170; PRO-356 AND GLU-579, AND CHARACTERIZATION OF RP VARIANTS DUH3 GLY-170; PRO-356 AND GLU-579. RX PubMed=23519333; DOI=10.1038/jid.2013.145; RA Zhang C., Li D., Zhang J., Chen X., Huang M., Archacki S., Tian Y., RA Ren W., Mei A., Zhang Q., Fang M., Su Z., Yin Y., Liu D., Chen Y., RA Cui X., Li C., Yang H., Wang Q., Wang J., Liu M., Deng Y.; RT "Mutations in ABCB6 cause dyschromatosis universalis hereditaria."; RL J. Invest. Dermatol. 133:2221-2228(2013). CC -!- FUNCTION: Binds heme and porphyrins and functions in their ATP- CC dependent uptake into the mitochondria. Plays a crucial role in CC heme synthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cell membrane. Mitochondrion outer membrane; CC Multi-pass membrane protein. Endoplasmic reticulum. Golgi CC apparatus. Endosome (By similarity). Note=localized to the CC endosome-like compartement and dendrite tips. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NP58-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NP58-4; Sequence=VSP_021973; CC Note=Ref.4 (BAB71347) sequence differs from that shown due to CC splicing through aberrant splice sites; CC -!- TISSUE SPECIFICITY: Widely expressed. High expression is detected CC in the retinal epithelium. CC -!- DEVELOPMENTAL STAGE: Highly expressed in fetal liver. CC -!- INDUCTION: Up-regulated by cellular porphyrins (at protein level). CC -!- POLYMORPHISM: Genetic variations in ABCB6 define the Langereis CC blood group system (LAN) [MIM:111600]. Individuals with Lan(-) CC blood group lack the Lan antigen on their red blood cells. These CC individuals may have anti-Lan antibodies in their serum, which can CC cause transfusion reactions or hemolytic disease of the fetus or CC newborn. The Lan(-) blood group is only clinically significant in CC transfusion settings or during pregnancy; otherwise Lan(-) CC individuals have no clinical features. CC -!- DISEASE: Microphthalmia, isolated, with coloboma, 7 (MCOPCB7) CC [MIM:614497]: A disorder of eye formation, ranging from small size CC of a single eye to complete bilateral absence of ocular tissues. CC Ocular abnormalities like opacities of the cornea and lens, CC scaring of the retina and choroid, and other abnormalities may CC also be present. Ocular colobomas are a set of malformations CC resulting from abnormal morphogenesis of the optic cup and stalk, CC and the fusion of the fetal fissure (optic fissure). Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Dyschromatosis universalis hereditaria 3 (DUH3) CC [MIM:615402]: An autosomal dominant pigmentary genodermatosis CC characterized by a mixture of hyperpigmented and hypopigmented CC macules distributed randomly over the body, that appear in infancy CC or early childhood. The trunk and extremities are the dominant CC sites of abnormal pigmentation. Facial lesions can be seen in 50% CC of affected individuals, but involvement of palms and soles is CC unusual. Abnormalities of hair and nails have also been reported. CC Dyschromatosis universalis hereditaria may be associated with CC abnormalities of dermal connective tissue, nerve tissue, or other CC systemic complications. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Depletion of Abcb6 by RNAi abrogates heme CC biosynthesis. Overexpression enhances porphyrin biosynthesis. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB CC family. Heavy Metal importer (TC 3.A.1.210) subfamily. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAG33617.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=AAG33618.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=AAH43423.1; Type=Miscellaneous discrepancy; Note=Intron retention; CC Sequence=BAD18782.1; Type=Erroneous termination; Positions=168; Note=Translated as Trp; CC Sequence=BAD92291.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q9NP58"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB039371; BAA96733.1; -; Genomic_DNA. DR EMBL; AF076775; AAF75107.1; -; mRNA. DR EMBL; AF308472; AAG33617.1; ALT_INIT; mRNA. DR EMBL; AF308473; AAG33618.1; ALT_INIT; Genomic_DNA. DR EMBL; AJ289233; CAB95766.2; -; mRNA. DR EMBL; AK057026; BAB71347.1; ALT_SEQ; mRNA. DR EMBL; AK172812; BAD18782.1; ALT_SEQ; mRNA. DR EMBL; AB209054; BAD92291.1; ALT_SEQ; mRNA. DR EMBL; BC000559; AAH00559.1; -; mRNA. DR EMBL; BC043423; AAH43423.1; ALT_SEQ; mRNA. DR EMBL; AF070598; AAC28653.1; -; mRNA. DR CCDS; CCDS2436.1; -. [Q9NP58-1] DR RefSeq; NP_005680.1; NM_005689.2. [Q9NP58-1] DR UniGene; Hs.107911; -. DR PDB; 3NH6; X-ray; 2.00 A; A=558-842. DR PDB; 3NH9; X-ray; 2.10 A; A=558-842. DR PDB; 3NHA; X-ray; 2.10 A; A=558-842. DR PDB; 3NHB; X-ray; 2.15 A; A=558-842. DR PDBsum; 3NH6; -. DR PDBsum; 3NH9; -. DR PDBsum; 3NHA; -. DR PDBsum; 3NHB; -. DR ProteinModelPortal; Q9NP58; -. DR SMR; Q9NP58; 234-833. DR BioGrid; 115369; 6. DR IntAct; Q9NP58; 3. DR MINT; MINT-3071268; -. DR STRING; 9606.ENSP00000265316; -. DR BindingDB; Q9NP58; -. DR ChEMBL; CHEMBL2007630; -. DR TCDB; 3.A.1.210.6; the atp-binding cassette (abc) superfamily. DR PhosphoSite; Q9NP58; -. DR DMDM; 13123949; -. DR MaxQB; Q9NP58; -. DR PaxDb; Q9NP58; -. DR PRIDE; Q9NP58; -. DR DNASU; 10058; -. DR Ensembl; ENST00000265316; ENSP00000265316; ENSG00000115657. [Q9NP58-1] DR Ensembl; ENST00000439002; ENSP00000394333; ENSG00000115657. [Q9NP58-4] DR GeneID; 10058; -. DR KEGG; hsa:10058; -. DR UCSC; uc002vkc.2; human. [Q9NP58-1] DR UCSC; uc010fwe.2; human. [Q9NP58-4] DR CTD; 10058; -. DR GeneCards; GC02M220038; -. DR HGNC; HGNC:47; ABCB6. DR HPA; HPA046723; -. DR MIM; 111600; phenotype. DR MIM; 605452; gene. DR MIM; 614497; phenotype. DR MIM; 615402; phenotype. DR neXtProt; NX_Q9NP58; -. DR Orphanet; 98938; Colobomatous microphthalmia. DR Orphanet; 241; Dyschromatosis universalis. DR Orphanet; 194; Ocular coloboma. DR PharmGKB; PA24388; -. DR eggNOG; COG5265; -. DR HOVERGEN; HBG080810; -. DR InParanoid; Q9NP58; -. DR KO; K05661; -. DR OMA; KPQTMER; -. DR OrthoDB; EOG7Z69BT; -. DR PhylomeDB; Q9NP58; -. DR TreeFam; TF105194; -. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR ChiTaRS; ABCB6; human. DR EvolutionaryTrace; Q9NP58; -. DR GeneWiki; ABCB6; -. DR GenomeRNAi; 10058; -. DR NextBio; 38003; -. DR PRO; PR:Q9NP58; -. DR Bgee; Q9NP58; -. DR CleanEx; HS_ABCB6; -. DR Genevestigator; Q9NP58; -. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; NAS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005768; C:endosome; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005740; C:mitochondrial envelope; IDA:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005774; C:vacuolar membrane; IBA:RefGenome. DR GO; GO:0005524; F:ATP binding; IDA:MGI. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0020037; F:heme binding; IDA:UniProtKB. DR GO; GO:0015232; F:heme transporter activity; TAS:Reactome. DR GO; GO:0015439; F:heme-transporting ATPase activity; IMP:UniProtKB. DR GO; GO:0007420; P:brain development; IMP:UniProtKB. DR GO; GO:0070574; P:cadmium ion transmembrane transport; IBA:RefGenome. DR GO; GO:0006879; P:cellular iron ion homeostasis; NAS:UniProtKB. DR GO; GO:0071585; P:detoxification of cadmium ion; IBA:RefGenome. DR GO; GO:0015886; P:heme transport; IDA:UniProtKB. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IDA:UniProtKB. DR GO; GO:0043588; P:skin development; IMP:UniProtKB. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0006810; P:transport; IDA:MGI. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR001140; ABC_transptr_TM_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Complete proteome; Disease mutation; Dyskeratosis congenita; KW Endoplasmic reticulum; Endosome; Golgi apparatus; Membrane; KW Microphthalmia; Mitochondrion; Mitochondrion outer membrane; KW Nucleotide-binding; Polymorphism; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 842 ATP-binding cassette sub-family B member FT 6, mitochondrial. FT /FTId=PRO_0000000248. FT TRANSMEM 27 47 Helical; (Potential). FT TRANSMEM 73 93 Helical; (Potential). FT TRANSMEM 107 127 Helical; (Potential). FT TRANSMEM 148 168 Helical; (Potential). FT TRANSMEM 186 206 Helical; (Potential). FT TRANSMEM 265 285 Helical; (Potential). FT TRANSMEM 376 396 Helical; (Potential). FT TRANSMEM 409 431 Helical; (Potential). FT TRANSMEM 502 522 Helical; (Potential). FT TRANSMEM 530 550 Helical; (Potential). FT DOMAIN 265 556 ABC transmembrane type-1. FT DOMAIN 590 824 ABC transporter. FT NP_BIND 623 634 ATP. FT BINDING 599 599 ATP. FT VAR_SEQ 183 228 Missing (in isoform 2). FT /FTId=VSP_021973. FT VARIANT 57 57 A -> T (in MCOPCB7; hypomorphic FT mutation). FT /FTId=VAR_067394. FT VARIANT 69 69 R -> G (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035732. FT VARIANT 170 170 S -> G (in DUH3; the protein is retained FT in the Golgi apparatus). FT /FTId=VAR_070602. FT VARIANT 293 293 L -> V (in dbSNP:rs13018440). FT /FTId=VAR_047552. FT VARIANT 343 343 R -> Q (in dbSNP:rs60322991). FT /FTId=VAR_060986. FT VARIANT 356 356 L -> P (in DUH3; the protein is retained FT in the Golgi apparatus). FT /FTId=VAR_070603. FT VARIANT 579 579 G -> E (in DUH3; the protein is retained FT in the Golgi apparatus). FT /FTId=VAR_070604. FT VARIANT 648 648 R -> Q (in dbSNP:rs13402964). FT /FTId=VAR_029749. FT VARIANT 811 811 L -> V (in MCOPCB7; hypomorphic FT mutation). FT /FTId=VAR_067395. FT CONFLICT 170 170 S -> N (in Ref. 2; AAG33618). FT CONFLICT 320 320 T -> S (in Ref. 4; BAD18782). FT CONFLICT 413 413 F -> S (in Ref. 4; BAD18782). FT CONFLICT 616 616 G -> E (in Ref. 4; BAD18782). FT CONFLICT 638 638 R -> L (in Ref. 4; BAD18782). FT HELIX 561 572 FT STRAND 590 600 FT STRAND 604 613 FT STRAND 618 625 FT HELIX 628 636 FT STRAND 643 649 FT HELIX 654 656 FT HELIX 659 664 FT STRAND 666 669 FT STRAND 677 679 FT HELIX 680 685 FT HELIX 693 702 FT HELIX 706 711 FT HELIX 715 717 FT STRAND 719 721 FT HELIX 729 743 FT STRAND 746 751 FT HELIX 759 773 FT STRAND 776 781 FT HELIX 785 789 FT STRAND 792 798 FT STRAND 801 806 FT HELIX 808 814 FT HELIX 817 826 SQ SEQUENCE 842 AA; 93886 MW; E63A7D59DCE5B9ED CRC64; MVTVGNYCEA EGPVGPAWMQ DGLSPCFFFT LVPSTRMALG TLALVLALPC RRRERPAGAD SLSWGAGPRI SPYVLQLLLA TLQAALPLAG LAGRVGTARG APLPSYLLLA SVLESLAGAC GLWLLVVERS QARQRLAMGI WIKFRHSPGL LLLWTVAFAA ENLALVSWNS PQWWWARADL GQQVQFSLWV LRYVVSGGLF VLGLWAPGLR PQSYTLQVHE EDQDVERSQV RSAAQQSTWR DFGRKLRLLS GYLWPRGSPA LQLVVLICLG LMGLERALNV LVPIFYRNIV NLLTEKAPWN SLAWTVTSYV FLKFLQGGGT GSTGFVSNLR TFLWIRVQQF TSRRVELLIF SHLHELSLRW HLGRRTGEVL RIADRGTSSV TGLLSYLVFN VIPTLADIII GIIYFSMFFN AWFGLIVFLC MSLYLTLTIV VTEWRTKFRR AMNTQENATR ARAVDSLLNF ETVKYYNAES YEVERYREAI IKYQGLEWKS SASLVLLNQT QNLVIGLGLL AGSLLCAYFV TEQKLQVGDY VLFGTYIIQL YMPLNWFGTY YRMIQTNFID MENMFDLLKE ETEVKDLPGA GPLRFQKGRI EFENVHFSYA DGRETLQDVS FTVMPGQTLA LVGPSGAGKS TILRLLFRFY DISSGCIRID GQDISQVTQA SLRSHIGVVP QDTVLFNDTI ADNIRYGRVT AGNDEVEAAA QAAGIHDAIM AFPEGYRTQV GERGLKLSGG EKQRVAIART ILKAPGIILL DEATSALDTS NERAIQASLA KVCANRTTIV VAHRLSTVVN ADQILVIKDG CIVERGRHEA LLSRGGVYAD MWQLQQGQEE TSEDTKPQTM ER // ID ABCB7_HUMAN Reviewed; 752 AA. AC O75027; G3XAC4; O75345; Q5VWY7; Q5VWY8; Q9BRE1; Q9UND1; Q9UP01; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 09-JUL-2014, entry version 141. DE RecName: Full=ATP-binding cassette sub-family B member 7, mitochondrial; DE AltName: Full=ATP-binding cassette transporter 7; DE Short=ABC transporter 7 protein; DE Flags: Precursor; GN Name=ABCB7; Synonyms=ABC7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLY-315 AND RP ILE-346. RC TISSUE=Placenta; RX PubMed=9621516; DOI=10.1007/s100380050051; RA Shimada Y., Okuno S., Kawai A., Shinomiya H., Saito A., Suzuki M., RA Omori Y., Nishino N., Kanemoto N., Fujiwara T., Horie M., RA Takahashi E.; RT "Cloning and chromosomal mapping of a novel ABC transporter gene RT (hABC7), a candidate for X-linked sideroblastic anemia with RT spinocerebellar ataxia."; RL J. Hum. Genet. 43:115-122(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASAT MET-400. RX PubMed=10196363; DOI=10.1093/hmg/8.5.743; RA Allikmets R., Raskind W.H., Hutchinson A., Schueck N.D., Dean M., RA Koeller D.M.; RT "Mutation of a putative mitochondrial iron transporter gene (ABC7) in RT X-linked sideroblastic anemia and ataxia (XLSA/A)."; RL Hum. Mol. Genet. 8:743-749(1999). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASAT LYS-433. RX PubMed=11050011; RA Bekri S., Kispal G., Lange H., Fitzsimons E., Tolmie J., Lill R., RA Bishop D.F.; RT "Human ABC7 transporter: gene structure and mutation causing X-linked RT sideroblastic anemia with ataxia with disruption of cytosolic iron- RT sulfur protein maturation."; RL Blood 96:3256-3264(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175; RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., RA Wang Y.-X., Chen S.-J., Chen Z.; RT "Identification of genes expressed in human CD34(+) hematopoietic RT stem/progenitor cells by expressed sequence tags and efficient full- RT length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-752 (ISOFORM 1). RX PubMed=9883897; DOI=10.1016/S0014-5793(98)01560-9; RA Csere P., Lill R., Kispal G.; RT "Identification of a human mitochondrial ABC transporter, the RT functional orthologue of yeast Atm1p."; RL FEBS Lett. 441:266-270(1998). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-216 AND LYS-251, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP VARIANT ASAT LEU-411, AND VARIANTS GLY-315 AND ILE-346. RX PubMed=11843825; DOI=10.1046/j.1365-2141.2001.03015.x; RA Maguire A., Hellier K., Hammans S., May A.; RT "X-linked cerebellar ataxia and sideroblastic anaemia associated with RT a missense mutation in the ABC7 gene predicting V411L."; RL Br. J. Haematol. 115:910-917(2001). RN [13] RP VARIANT ASAT ASP-208. RX PubMed=22398176; DOI=10.1016/j.ejpn.2012.02.003; RA D'Hooghe M., Selleslag D., Mortier G., Van Coster R., Vermeersch P., RA Billiet J., Bekri S.; RT "X-linked sideroblastic anemia and ataxia: A new family with RT identification of a fourth ABCB7 gene mutation."; RL Eur. J. Paediatr. Neurol. 16:730-735(2012). CC -!- FUNCTION: Could be involved in the transport of heme from the CC mitochondria to the cytosol. Plays a central role in the CC maturation of cytosolic iron-sulfur (Fe/S) cluster-containing CC proteins. CC -!- SUBUNIT: Homodimer or heterodimer (Potential). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O75027-1; Sequence=Displayed; CC Name=2; CC IsoId=O75027-2; Sequence=VSP_014635; CC Name=3; CC IsoId=O75027-3; Sequence=VSP_054700; CC Note=No experimental confirmation available. Gene prediction CC based on EST data; CC -!- DISEASE: Anemia, sideroblastic, spinocerebellar ataxia (ASAT) CC [MIM:301310]: A X-linked recessive disorder characterized by an CC infantile to early childhood onset of non-progressive cerebellar CC ataxia and mild anemia, with hypochromia and microcytosis. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB CC family. Heavy Metal importer (TC 3.A.1.210) subfamily. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=O75027"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB005289; BAA28861.1; -; mRNA. DR EMBL; AF133659; AAD33045.1; -; mRNA. DR EMBL; AF241887; AAK20173.1; -; Genomic_DNA. DR EMBL; AF241872; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241873; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241874; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241875; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241876; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241877; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241878; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241879; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241880; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241881; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241882; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241883; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241884; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241885; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF241886; AAK20173.1; JOINED; Genomic_DNA. DR EMBL; AF038950; AAC39865.1; -; mRNA. DR EMBL; BT009918; AAP88920.1; -; mRNA. DR EMBL; AL360179; CAH70564.1; -; Genomic_DNA. DR EMBL; AL359545; CAH70564.1; JOINED; Genomic_DNA. DR EMBL; AL360179; CAH70565.1; -; Genomic_DNA. DR EMBL; AL359545; CAH70565.1; JOINED; Genomic_DNA. DR EMBL; AL359545; CAI41573.1; -; Genomic_DNA. DR EMBL; AL360179; CAI41573.1; JOINED; Genomic_DNA. DR EMBL; AL359545; CAI41574.1; -; Genomic_DNA. DR EMBL; AL360179; CAI41574.1; JOINED; Genomic_DNA. DR EMBL; CH471104; EAW98635.1; -; Genomic_DNA. DR EMBL; BC006323; AAH06323.1; -; mRNA. DR EMBL; AF078777; AAD47141.1; -; mRNA. DR CCDS; CCDS14428.1; -. [O75027-2] DR CCDS; CCDS65291.1; -. [O75027-1] DR RefSeq; NP_001258625.1; NM_001271696.1. [O75027-1] DR RefSeq; NP_001258626.1; NM_001271697.1. [O75027-3] DR RefSeq; NP_001258627.1; NM_001271698.1. DR RefSeq; NP_004290.2; NM_004299.4. [O75027-2] DR UniGene; Hs.370480; -. DR ProteinModelPortal; O75027; -. DR SMR; O75027; 127-738. DR BioGrid; 106540; 11. DR IntAct; O75027; 2. DR STRING; 9606.ENSP00000253577; -. DR TCDB; 3.A.1.210.4; the atp-binding cassette (abc) superfamily. DR PhosphoSite; O75027; -. DR MaxQB; O75027; -. DR PaxDb; O75027; -. DR PRIDE; O75027; -. DR DNASU; 22; -. DR Ensembl; ENST00000253577; ENSP00000253577; ENSG00000131269. [O75027-2] DR Ensembl; ENST00000339447; ENSP00000343849; ENSG00000131269. DR Ensembl; ENST00000373394; ENSP00000362492; ENSG00000131269. [O75027-1] DR GeneID; 22; -. DR KEGG; hsa:22; -. DR UCSC; uc004ebz.4; human. [O75027-2] DR UCSC; uc004eca.4; human. [O75027-1] DR CTD; 22; -. DR GeneCards; GC0XM074189; -. DR GeneReviews; ABCB7; -. DR H-InvDB; HIX0028475; -. DR HGNC; HGNC:48; ABCB7. DR HPA; HPA034982; -. DR MIM; 300135; gene. DR MIM; 301310; phenotype. DR neXtProt; NX_O75027; -. DR Orphanet; 2802; X-linked sideroblastic anemia - ataxia. DR PharmGKB; PA24389; -. DR eggNOG; COG5265; -. DR HOVERGEN; HBG080194; -. DR KO; K05662; -. DR OMA; MHQLSLR; -. DR OrthoDB; EOG7Z69BT; -. DR PhylomeDB; O75027; -. DR TreeFam; TF105195; -. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR GeneWiki; ABCB7; -. DR GenomeRNAi; 22; -. DR NextBio; 35517837; -. DR PRO; PR:O75027; -. DR ArrayExpress; O75027; -. DR Bgee; O75027; -. DR CleanEx; HS_ABCB7; -. DR Genevestigator; O75027; -. DR GO; GO:0016021; C:integral component of membrane; IBA:RefGenome. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005524; F:ATP binding; TAS:ProtInc. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:RefGenome. DR GO; GO:0015232; F:heme transporter activity; TAS:ProtInc. DR GO; GO:0006879; P:cellular iron ion homeostasis; IBA:RefGenome. DR GO; GO:0015886; P:heme transport; TAS:GOC. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0055085; P:transmembrane transport; IBA:RefGenome. DR GO; GO:0006810; P:transport; TAS:ProtInc. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR001140; ABC_transptr_TM_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Complete proteome; KW Disease mutation; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; KW Polymorphism; Reference proteome; Transit peptide; Transmembrane; KW Transmembrane helix; Transport. FT TRANSIT 1 ? Mitochondrion (Potential). FT CHAIN ? 752 ATP-binding cassette sub-family B member FT 7, mitochondrial. FT /FTId=PRO_0000000249. FT TRANSMEM 141 161 Helical; (Potential). FT TRANSMEM 186 206 Helical; (Potential). FT TRANSMEM 260 280 Helical; (Potential). FT TRANSMEM 291 311 Helical; (Potential). FT TRANSMEM 383 403 Helical; (Potential). FT TRANSMEM 410 430 Helical; (Potential). FT DOMAIN 140 436 ABC transmembrane type-1. FT DOMAIN 472 706 ABC transporter. FT NP_BIND 505 516 ATP (By similarity). FT BINDING 481 481 ATP (By similarity). FT MOD_RES 216 216 N6-acetyllysine. FT MOD_RES 251 251 N6-acetyllysine. FT MOD_RES 336 336 Phosphoserine (By similarity). FT MOD_RES 340 340 Phosphotyrosine (By similarity). FT MOD_RES 342 342 Phosphothreonine (By similarity). FT VAR_SEQ 56 56 Q -> QQ (in isoform 2). FT /FTId=VSP_014635. FT VAR_SEQ 112 151 Missing (in isoform 3). FT /FTId=VSP_054700. FT VARIANT 208 208 E -> D (in ASAT). FT /FTId=VAR_067354. FT VARIANT 315 315 R -> G. FT /FTId=VAR_022872. FT VARIANT 346 346 F -> I. FT /FTId=VAR_022873. FT VARIANT 400 400 I -> M (in ASAT). FT /FTId=VAR_009156. FT VARIANT 411 411 V -> L (in ASAT). FT /FTId=VAR_022874. FT VARIANT 433 433 E -> K (in ASAT; impaired maturation of FT cytosolic Fe/S proteins). FT /FTId=VAR_012640. FT VARIANT 580 580 A -> V (in dbSNP:rs1340989). FT /FTId=VAR_055471. FT VARIANT 581 581 V -> A (in dbSNP:rs1340989). FT /FTId=VAR_037972. FT CONFLICT 141 141 A -> P (in Ref. 4; AAC39865). FT CONFLICT 258 258 R -> K (in Ref. 1; BAA28861). FT CONFLICT 271 276 LLPIMF -> PLPNHV (in Ref. 4; AAC39865). FT CONFLICT 280 280 L -> LL (in Ref. 4; AAC39865). FT CONFLICT 290 290 G -> C (in Ref. 4; AAC39865). FT CONFLICT 293 297 FALVT -> LLGN (in Ref. 4; AAC39865). FT CONFLICT 320 324 IEMNK -> LEIDQ (in Ref. 4; AAC39865). FT CONFLICT 542 542 E -> V (in Ref. 9; AAD47141). SQ SEQUENCE 752 AA; 82641 MW; B1FFA57ABD24FB90 CRC64; MALLAMHSWR WAAAAAAFEK RRHSAILIRP LVSVSGSGPQ WRPHQLGALG TARAYQIPES LKSITWQRLG KGNSGQFLDA AKALQVWPLI EKRTCWHGHA GGGLHTDPKE GLKDVDTRKI IKAMLSYVWP KDRPDLRARV AISLGFLGGA KAMNIVVPFM FKYAVDSLNQ MSGNMLNLSD APNTVATMAT AVLIGYGVSR AGAAFFNEVR NAVFGKVAQN SIRRIAKNVF LHLHNLDLGF HLSRQTGALS KAIDRGTRGI SFVLSALVFN LLPIMFEVML VSGVLYYKCG AQFALVTLGT LGTYTAFTVA VTRWRTRFRI EMNKADNDAG NAAIDSLLNY ETVKYFNNER YEAQRYDGFL KTYETASLKS TSTLAMLNFG QSAIFSVGLT AIMVLASQGI VAGTLTVGDL VMVNGLLFQL SLPLNFLGTV YRETRQALID MNTLFTLLKV DTQIKDKVMA SPLQITPQTA TVAFDNVHFE YIEGQKVLSG ISFEVPAGKK VAIVGGSGSG KSTIVRLLFR FYEPQKGSIY LAGQNIQDVS LESLRRAVGV VPQDAVLFHN TIYYNLLYGN ISASPEEVYA VAKLAGLHDA ILRMPHGYDT QVGERGLKLS GGEKQRVAIA RAILKDPPVI LYDEATSSLD SITEETILGA MKDVVKHRTS IFIAHRLSTV VDADEIIVLD QGKVAERGTH HGLLANPHSI YSEMWHTQSS RVQNHDNPKW EAKKENISKE EERKKLQEEI VNSVKGCGNC SC // ID ABCB9_HUMAN Reviewed; 766 AA. AC Q9NP78; B4E2J0; Q5W9G7; Q769F3; Q769F4; Q96AB1; Q9P208; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-JUL-2014, entry version 139. DE RecName: Full=ATP-binding cassette sub-family B member 9; DE AltName: Full=ATP-binding cassette transporter 9; DE Short=ABC transporter 9 protein; DE Short=hABCB9; DE AltName: Full=TAP-like protein; DE Short=TAPL; GN Name=ABCB9; Synonyms=KIAA1520; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION. RC TISSUE=Embryonic kidney; RX PubMed=11011155; DOI=10.1093/oxfordjournals.jbchem.a022805; RA Kobayashi A., Kasano M., Maeda T., Hori S., Motojima K., Suzuki M., RA Fujiwara T., Takahashi E., Yabe T., Tanaka K., Kasahara M., RA Yamaguchi Y., Maeda M.; RT "A half-type ABC transporter TAPL is highly conserved between rodent RT and man, and the human gene is not responsive to interferon-gamma in RT contrast to TAP1 and TAP2."; RL J. Biochem. 128:711-718(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, RP AND TISSUE SPECIFICITY. RC TISSUE=Lymphoblast; RX PubMed=10748049; DOI=10.1074/jbc.M001819200; RA Zhang F., Zhang W., Liu L., Fisher C.L., Hui D., Childs S., RA Dorovini-Zis K., Ling V.; RT "Characterization of ABCB9, an ATP binding cassette protein associated RT with lysosomes."; RL J. Biol. Chem. 275:23287-23294(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5). RC TISSUE=Cervix carcinoma, and Embryonic kidney; RX PubMed=13679046; DOI=10.1016/j.bbrc.2003.08.081; RA Kobayashi A., Hori S., Suita N., Maeda M.; RT "Gene organization of human transporter associated with antigen RT processing-like (TAPL, ABCB9): analysis of alternative splicing RT variants and promoter activity."; RL Biochem. Biophys. Res. Commun. 309:815-822(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028; RA Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.; RT "Alternative splice variants encoding unstable protein domains exist RT in the human brain."; RL J. Mol. Biol. 343:1207-1220(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10819331; DOI=10.1093/dnares/7.2.143; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 7:143-150(2000). RN [6] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R.; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=15577206; DOI=10.1248/bpb.27.1916; RA Kobayashi A., Maeda T., Maeda M.; RT "Membrane localization of transporter associated with antigen RT processing (TAP)-like (ABCB9) visualized in vivo with a fluorescence RT protein-fusion technique."; RL Biol. Pharm. Bull. 27:1916-1922(2004). RN [11] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=15863492; DOI=10.1074/jbc.M503231200; RA Wolters J.C., Abele R., Tampe R.; RT "Selective and ATP-dependent translocation of peptides by the RT homodimeric ATP binding cassette transporter TAP-like (ABCB9)."; RL J. Biol. Chem. 280:23631-23636(2005). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=17977821; DOI=10.1074/jbc.M708139200; RA Demirel O., Waibler Z., Kalinke U., Grunebach F., Appel S., RA Brossart P., Hasilik A., Tampe R., Abele R.; RT "Identification of a lysosomal peptide transport system induced during RT dendritic cell development."; RL J. Biol. Chem. 282:37836-37843(2007). RN [13] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Placenta; RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x; RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., RA Schaefer H., Elsaesser H.-P., Mann M., Hasilik A.; RT "Integral and associated lysosomal membrane proteins."; RL Traffic 8:1676-1686(2007). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=18952056; DOI=10.1016/j.bbrc.2008.10.078; RA Kamakura A., Fujimoto Y., Motohashi Y., Ohashi K., RA Ohashi-Kobayashi A., Maeda M.; RT "Functional dissection of transmembrane domains of human TAP-like RT (ABCB9)."; RL Biochem. Biophys. Res. Commun. 377:847-851(2008). RN [15] RP SUBCELLULAR LOCATION, AND DOMAIN. RX PubMed=18175933; DOI=10.1248/bpb.31.1; RA Ohara T., Ohashi-Kobayashi A., Maeda M.; RT "Biochemical characterization of transporter associated with antigen RT processing (TAP)-like (ABCB9) expressed in insect cells."; RL Biol. Pharm. Bull. 31:1-5(2008). RN [16] RP FUNCTION. RX PubMed=18434309; DOI=10.1074/jbc.M801794200; RA Zhao C., Haase W., Tampe R., Abele R.; RT "Peptide specificity and lipid activation of the lysosomal transport RT complex ABCB9 (TAPL)."; RL J. Biol. Chem. 283:17083-17091(2008). RN [17] RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 136-LYS-LYS-137. RX PubMed=20377823; DOI=10.1111/j.1600-0854.2009.01021.x; RA Demirel O., Bangert I., Tampe R., Abele R.; RT "Tuning the cellular trafficking of the lysosomal peptide transporter RT TAPL by its N-terminal domain."; RL Traffic 11:383-393(2010). RN [18] RP SUBCELLULAR LOCATION. RX PubMed=21212514; DOI=10.1248/bpb.34.36; RA Fujimoto Y., Kamakura A., Motohashi Y., Ohashi-Kobayashi A., Maeda M.; RT "Transporter associated with antigen processing-like (ABCB9) stably RT expressed in Chinese hamster ovary-K1 cells is sorted to the RT microdomains of lysosomal membranes."; RL Biol. Pharm. Bull. 34:36-40(2011). RN [19] RP VARIANT MET-121. RX PubMed=11829140; DOI=10.1007/s10038-002-8653-6; RA Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., RA Higuchi S., Nakamura Y.; RT "Three hundred twenty-six genetic variations in genes encoding nine RT members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the RT Japanese population."; RL J. Hum. Genet. 47:38-50(2002). CC -!- FUNCTION: ATP-dependent low-affinity peptide transporter which CC translocates a broad spectrum of peptides from the cytosol to the CC lysosomal lumen. Displays a broad peptide length specificity from CC 6-mer up to at least 59-mer peptides with an optimum of 23-mers. CC Favors positively charged, aromatic or hydrophobic residues in the CC N- and C-terminal positions whereas negatively charged residues as CC well as asparagine and methionine are not favored. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=6.8 uM for peptide RRYQNSTCL; CC pH dependence: CC Optimum pH is 7.0; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane CC protein. Note=May be located in membrane rafts. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=12A, c1-l; CC IsoId=Q9NP78-1; Sequence=Displayed; CC Name=2; Synonyms=c1-s; CC IsoId=Q9NP78-2; Sequence=VSP_000027; CC Name=3; CC IsoId=Q9NP78-3; Sequence=VSP_000029, VSP_000030; CC Note=No experimental confirmation available; CC Name=4; Synonyms=12B; CC IsoId=Q9NP78-5; Sequence=VSP_041884, VSP_041886; CC Name=5; Synonyms=12C; CC IsoId=Q9NP78-6; Sequence=VSP_041885; CC Name=6; CC IsoId=Q9NP78-7; Sequence=VSP_044884; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in testis, and at moderate CC levels in brain, spinal cord, and thyroid. Not expressed in CC monocytes but strongly expressed during differentiation of CC monocytes to dendritic cells and macrophages. CC -!- INDUCTION: Not induced by interferon-gamma. CC -!- DOMAIN: The N-terminal region comprising the first four CC transmembrane domains is required for lysosomal localization but CC not for homodimerization or peptide transport. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB CC family. MHC peptide exporter (TC 3.A.1.209) subfamily. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC -!- CAUTION: Has also been detected in the endoplasmic reticulum CC (PubMed:11011155) but appears to be a lysosomal protein in vivo. CC -!- SEQUENCE CAUTION: CC Sequence=BAA96044.2; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC Sequence=BAD66830.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q9NP78"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB045381; BAA97989.2; -; mRNA. DR EMBL; AF216494; AAF89993.1; -; mRNA. DR EMBL; AB112582; BAC98409.1; -; mRNA. DR EMBL; AB112583; BAC98410.1; -; mRNA. DR EMBL; AB177852; BAD66830.1; ALT_INIT; mRNA. DR EMBL; AB040953; BAA96044.2; ALT_INIT; mRNA. DR EMBL; AK304295; BAG65152.1; -; mRNA. DR EMBL; AC026362; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC027290; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC017348; AAH17348.1; -; mRNA. DR CCDS; CCDS58286.1; -. [Q9NP78-7] DR CCDS; CCDS58287.1; -. [Q9NP78-6] DR CCDS; CCDS58288.1; -. [Q9NP78-5] DR CCDS; CCDS9241.1; -. [Q9NP78-1] DR RefSeq; NP_001229942.1; NM_001243013.1. [Q9NP78-7] DR RefSeq; NP_001229943.1; NM_001243014.1. [Q9NP78-6] DR RefSeq; NP_062570.1; NM_019624.3. [Q9NP78-2] DR RefSeq; NP_062571.1; NM_019625.3. [Q9NP78-1] DR RefSeq; NP_982269.2; NM_203444.3. [Q9NP78-5] DR UniGene; Hs.511951; -. DR ProteinModelPortal; Q9NP78; -. DR SMR; Q9NP78; 175-739. DR BioGrid; 117021; 1. DR STRING; 9606.ENSP00000280560; -. DR ChEMBL; CHEMBL1293189; -. DR TCDB; 3.A.1.209.2; the atp-binding cassette (abc) superfamily. DR PhosphoSite; Q9NP78; -. DR DMDM; 22095458; -. DR PaxDb; Q9NP78; -. DR PRIDE; Q9NP78; -. DR Ensembl; ENST00000280560; ENSP00000280560; ENSG00000150967. [Q9NP78-1] DR Ensembl; ENST00000344275; ENSP00000456813; ENSG00000150967. [Q9NP78-6] DR Ensembl; ENST00000346530; ENSP00000280559; ENSG00000150967. [Q9NP78-2] DR Ensembl; ENST00000392439; ENSP00000376234; ENSG00000150967. [Q9NP78-1] DR Ensembl; ENST00000442833; ENSP00000456375; ENSG00000150967. [Q9NP78-5] DR Ensembl; ENST00000540285; ENSP00000441734; ENSG00000150967. [Q9NP78-7] DR Ensembl; ENST00000542678; ENSP00000440288; ENSG00000150967. [Q9NP78-1] DR GeneID; 23457; -. DR KEGG; hsa:23457; -. DR UCSC; uc001udm.4; human. [Q9NP78-1] DR UCSC; uc001udo.4; human. [Q9NP78-2] DR UCSC; uc001udr.3; human. [Q9NP78-3] DR UCSC; uc010taj.2; human. DR UCSC; uc021rfp.1; human. [Q9NP78-5] DR CTD; 23457; -. DR GeneCards; GC12M123413; -. DR HGNC; HGNC:50; ABCB9. DR HPA; HPA035114; -. DR MIM; 605453; gene. DR neXtProt; NX_Q9NP78; -. DR PharmGKB; PA24391; -. DR eggNOG; COG1132; -. DR HOVERGEN; HBG008358; -. DR InParanoid; Q9NP78; -. DR KO; K05656; -. DR OrthoDB; EOG7Z3F4H; -. DR PhylomeDB; Q9NP78; -. DR TreeFam; TF105197; -. DR BRENDA; 3.6.3.43; 2681. DR GeneWiki; ABCB9; -. DR GenomeRNAi; 23457; -. DR NextBio; 45751; -. DR PRO; PR:Q9NP78; -. DR ArrayExpress; Q9NP78; -. DR Bgee; Q9NP78; -. DR CleanEx; HS_ABCB9; -. DR Genevestigator; Q9NP78; -. DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0005764; C:lysosome; IDA:UniProt. DR GO; GO:0005886; C:plasma membrane; IBA:RefGenome. DR GO; GO:0042825; C:TAP complex; IBA:RefGenome. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0042288; F:MHC class I protein binding; IBA:RefGenome. DR GO; GO:0015421; F:oligopeptide-transporting ATPase activity; IBA:RefGenome. DR GO; GO:0042605; F:peptide antigen binding; IBA:RefGenome. DR GO; GO:0015440; F:peptide-transporting ATPase activity; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProt. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0046978; F:TAP1 binding; IBA:RefGenome. DR GO; GO:0046979; F:TAP2 binding; IBA:RefGenome. DR GO; GO:0046980; F:tapasin binding; IBA:RefGenome. DR GO; GO:0035672; P:oligopeptide transmembrane transport; IBA:GOC. DR GO; GO:0015833; P:peptide transport; IDA:UniProtKB. DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IBA:RefGenome. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:RefGenome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR001140; ABC_transptr_TM_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Complete proteome; Lysosome; KW Membrane; Nucleotide-binding; Peptide transport; Polymorphism; KW Protein transport; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 766 ATP-binding cassette sub-family B member FT 9. FT /FTId=PRO_0000000252. FT TRANSMEM 7 27 Helical; (Potential). FT TRANSMEM 47 67 Helical; (Potential). FT TRANSMEM 84 104 Helical; (Potential). FT TRANSMEM 116 136 Helical; (Potential). FT TRANSMEM 185 205 Helical; (Potential). FT TRANSMEM 225 245 Helical; (Potential). FT TRANSMEM 319 339 Helical; (Potential). FT TRANSMEM 416 436 Helical; (Potential). FT DOMAIN 188 471 ABC transmembrane type-1. FT DOMAIN 504 740 ABC transporter. FT NP_BIND 539 546 ATP (Potential). FT COMPBIAS 384 389 Poly-Glu. FT VAR_SEQ 418 460 Missing (in isoform 2). FT /FTId=VSP_000027. FT VAR_SEQ 461 523 Missing (in isoform 6). FT /FTId=VSP_044884. FT VAR_SEQ 582 596 ISLVSQEPVLFARSI -> VCARAWATLLRPFCI (in FT isoform 3). FT /FTId=VSP_000029. FT VAR_SEQ 597 766 Missing (in isoform 3). FT /FTId=VSP_000030. FT VAR_SEQ 681 683 IQQ -> CAG (in isoform 4). FT /FTId=VSP_041884. FT VAR_SEQ 682 766 Missing (in isoform 5). FT /FTId=VSP_041885. FT VAR_SEQ 684 766 Missing (in isoform 4). FT /FTId=VSP_041886. FT VARIANT 121 121 V -> M (in dbSNP:rs3803002). FT /FTId=VAR_013701. FT MUTAGEN 136 137 LL->AA: No effect on lysosomal FT localization. SQ SEQUENCE 766 AA; 84475 MW; C83FA62C929EC792 CRC64; MRLWKAVVVT LAFMSVDICV TTAIYVFSHL DRSLLEDIRH FNIFDSVLDL WAACLYRSCL LLGATIGVAK NSALGPRRLR ASWLVITLVC LFVGIYAMVK LLLFSEVRRP IRDPWFWALF VWTYISLGAS FLLWWLLSTV RPGTQALEPG AATEAEGFPG SGRPPPEQAS GATLQKLLSY TKPDVAFLVA ASFFLIVAAL GETFLPYYTG RAIDGIVIQK SMDQFSTAVV IVCLLAIGSS FAAGIRGGIF TLIFARLNIR LRNCLFRSLV SQETSFFDEN RTGDLISRLT SDTTMVSDLV SQNINVFLRN TVKVTGVVVF MFSLSWQLSL VTFMGFPIIM MVSNIYGKYY KRLSKEVQNA LARASNTAEE TISAMKTVRS FANEEEEAEV YLRKLQQVYK LNRKEAAAYM YYVWGSGLTL LVVQVSILYY GGHLVISGQM TSGNLIAFII YEFVLGDCME SVGSVYSGLM QGVGAAEKVF EFIDRQPTMV HDGSLAPDHL EGRVDFENVT FTYRTRPHTQ VLQNVSFSLS PGKVTALVGP SGSGKSSCVN ILENFYPLEG GRVLLDGKPI SAYDHKYLHR VISLVSQEPV LFARSITDNI SYGLPTVPFE MVVEAAQKAN AHGFIMELQD GYSTETGEKG AQLSGGQKQR VAMARALVRN PPVLILDEAT SALDAESEYL IQQAIHGNLQ KHTVLIIAHR LSTVEHAHLI VVLDKGRVVQ QGTHQQLLAQ GGLYAKLVQR QMLGLQPAAD FTAGHNEPVA NGSHKA // ID ABCBB_HUMAN Reviewed; 1321 AA. AC O95342; Q53TL2; Q9UNB2; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 03-NOV-2009, sequence version 2. DT 09-JUL-2014, entry version 137. DE RecName: Full=Bile salt export pump; DE AltName: Full=ATP-binding cassette sub-family B member 11; GN Name=ABCB11; Synonyms=BSEP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PFIC2 GLY-297; GLU-461; RP GLY-482; ARG-982; CYS-1153 AND GLN-1268. RX PubMed=9806540; DOI=10.1038/3034; RA Strautnieks S.S., Bull L.N., Knisely A.S., Kocoshis S.A., Dahl N., RA Arnell H., Sokal E.M., Dahan K., Childs S., Ling V., Tanner M.S., RA Kagalwalla A.F., Nemeth A., Pawlowska J., Baker A., Mieli-Vergani G., RA Freimer N.B., Gardiner R.M., Thompson R.J.; RT "A gene encoding a liver-specific ABC transporter is mutated in RT progressive familial intrahepatic cholestasis."; RL Nat. Genet. 20:233-238(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-444. RA Mol O., Hooiveld G.J.E.J., Jansen P.L.M., Muller M.; RT "Cellular localization and functional characterization of the human RT bile salt export pump (BSEP)."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [4] RP GLYCOSYLATION AT ASN-109; ASN-116; ASN-122 AND ASN-125. RX PubMed=17082223; DOI=10.1152/ajpgi.00415.2006; RA Mochizuki K., Kagawa T., Numari A., Harris M.J., Itoh J., Watanabe N., RA Mine T., Arias I.M.; RT "Two N-linked glycans are required to maintain the transport activity RT of the bile salt export pump (ABCB11) in MDCK II cells."; RL Am. J. Physiol. 292:G818-G828(2007). RN [5] RP VARIANTS PFIC2 VAL-238 AND SER-336. RX PubMed=10579978; DOI=10.1016/S0016-5085(99)70287-8; RA Jansen P.L.M., Strautnieks S.S., Jacquemin E., Hadchouel M., RA Sokal E.M., Hooiveld G.J.E.J., Koning J.H., De Jager-Krikken A., RA Kuipers F., Stellaard F., Bijleveld C.M., Gouw A., Van Goor H., RA Thompson R.J., Muller M.; RT "Hepatocanalicular bile salt export pump deficiency in patients with RT progressive familial intrahepatic cholestasis."; RL Gastroenterology 117:1370-1379(1999). RN [6] RP VARIANT ALA-444. RX PubMed=11829140; DOI=10.1007/s10038-002-8653-6; RA Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., RA Higuchi S., Nakamura Y.; RT "Three hundred twenty-six genetic variations in genes encoding nine RT members of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the RT Japanese population."; RL J. Hum. Genet. 47:38-50(2002). RN [7] RP VARIANTS PFIC2 LEU-284 AND ASP-1004. RX PubMed=11815775; DOI=10.1067/mpd.2002.119993; RA Chen H.-L., Chang P.-S., Hsu H.-C., Ni Y.-H., Hsu H.-Y., Lee J.-H., RA Jeng Y.-M., Shau W.-Y., Chang M.-H.; RT "FIC1 and BSEP defects in Taiwanese patients with chronic intrahepatic RT cholestasis with low gamma-glutamyltranspeptidase levels."; RL J. Pediatr. 140:119-124(2002). RN [8] RP VARIANTS BRIC2 GLY-186; GLY-297; THR-570; PRO-923; PRO-926; CYS-1050 RP AND HIS-1128. RX PubMed=15300568; DOI=10.1053/j.gastro.2004.04.065; RA van Mil S.W.C., van der Woerd W.L., van der Brugge G., Sturm E., RA Jansen P.L.M., Bull L.N., van den Berg I.E.T., Berger R., RA Houwen R.H.J., Klomp L.W.J.; RT "Benign recurrent intrahepatic cholestasis type 2 is caused by RT mutations in ABCB11."; RL Gastroenterology 127:379-384(2004). RN [9] RP VARIANTS GLN-415; ALA-444; SER-591 AND VAL-677. RX PubMed=15077010; DOI=10.1097/00008571-200402000-00003; RA Pauli-Magnus C., Lang T., Meier Y., Zodan-Marin T., Jung D., RA Breymann C., Zimmermann R., Kenngott S., Beuers U., Reichel C., RA Kerb R., Penger A., Meier P.J., Kullak-Ublick G.A.; RT "Sequence analysis of bile salt export pump (ABCB11) and multidrug RT resistance p-glycoprotein 3 (ABCB4, MDR3) in patients with RT intrahepatic cholestasis of pregnancy."; RL Pharmacogenetics 14:91-102(2004). RN [10] RP VARIANTS BRIC2 GLY-297 AND THR-432, AND CHARACTERIZATION OF VARIANTS RP BRIC2 GLY-297 AND THR-432. RX PubMed=16039748; DOI=10.1016/j.jhep.2005.05.020; RA Noe J., Kullak-Ublick G.A., Jochum W., Stieger B., Kerb R., Haberl M., RA Muellhaupt B., Meier P.J., Pauli-Magnus C.; RT "Impaired expression and function of the bile salt export pump due to RT three novel ABCB11 mutations in intrahepatic cholestasis."; RL J. Hepatol. 43:536-543(2005). RN [11] RP VARIANTS VAL-206; ALA-284; LYS-299; ALA-444; GLY-616; ALA-619; RP VAL-677; HIS-698; VAL-865 AND GLN-958. RX PubMed=16763017; DOI=10.1124/dmd.105.008854; RA Lang T., Haberl M., Jung D., Drescher A., Schlagenhaufer R., Keil A., RA Mornhinweg E., Stieger B., Kullak-Ublick G.A., Kerb R.; RT "Genetic variability, haplotype structures, and ethnic diversity of RT hepatic transporters MDR3 (ABCB4) and bile salt export pump RT (ABCB11)."; RL Drug Metab. Dispos. 34:1582-1599(2006). RN [12] RP VARIANTS ALA-444 AND VAL-677. RX PubMed=16799996; DOI=10.1002/hep.21214; RA Meier Y., Pauli-Magnus C., Zanger U.M., Klein K., Schaeffeler E., RA Nussler A.K., Nussler N., Eichelbaum M., Meier P.J., Stieger B.; RT "Interindividual variability of canalicular ATP-binding-cassette RT (ABC)-transporter expression in human liver."; RL Hepatology 44:62-74(2006). RN [13] RP VARIANTS ALA-284; ALA-444; TYR-676; VAL-677; HIS-698 AND ARG-855, RP BIOPHYSICOCHEMICAL PROPERTIES, AND CHARACTERIZATION OF VARIANTS RP ALA-444; TYR-676; VAL-677 AND ARG-855. RX PubMed=17264802; DOI=10.1097/01.fpc.0000230418.28091.76; RA Lang C., Meier Y., Stieger B., Beuers U., Lang T., Kerb R., RA Kullak-Ublick G.A., Meier P.J., Pauli-Magnus C.; RT "Mutations and polymorphisms in the bile salt export pump and the RT multidrug resistance protein 3 associated with drug-induced liver RT injury."; RL Pharmacogenet. Genomics 17:47-60(2007). CC -!- FUNCTION: Involved in the ATP-dependent secretion of bile salts CC into the canaliculus of hepatocytes. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=30.4 uM for taurocholate; CC Vmax=232 pmol/min/mg enzyme for taurocholate transport; CC -!- SUBUNIT: Interacts with HAX1 (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed predominantly, if not exclusively in CC the liver, where it was further localized to the canalicular CC microvilli and to subcanalicular vesicles of the hepatocytes by in CC situ. CC -!- DOMAIN: Multifunctional polypeptide with two homologous halves, CC each containing a hydrophobic membrane-anchoring domain and an ATP CC binding cassette (ABC) domain. CC -!- DISEASE: Cholestasis, progressive familial intrahepatic, 2 (PFIC2) CC [MIM:601847]: A disorder characterized by early onset of CC cholestasis that progresses to hepatic fibrosis, cirrhosis, and CC end-stage liver disease before adulthood. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- DISEASE: Cholestasis, benign recurrent intrahepatic, 2 (BRIC2) CC [MIM:605479]: A disorder characterized by intermittent episodes of CC cholestasis without progression to liver failure. There is initial CC elevation of serum bile acids, followed by cholestatic jaundice CC which generally spontaneously resolves after periods of weeks to CC months. The cholestatic attacks vary in severity and duration. CC Patients are asymptomatic between episodes, both clinically and CC biochemically. Note=The disease is caused by mutations affecting CC the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB CC family. Multidrug resistance exporter (TC 3.A.1.201) subfamily. CC -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=O95342"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF091582; AAC77455.1; -; mRNA. DR EMBL; AF136523; AAD28285.1; -; mRNA. DR EMBL; AC008177; AAY24305.1; -; Genomic_DNA. DR EMBL; AC093723; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC069137; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS46444.1; -. DR RefSeq; NP_003733.2; NM_003742.2. DR UniGene; Hs.658439; -. DR ProteinModelPortal; O95342; -. DR SMR; O95342; 18-1316. DR BioGrid; 114199; 6. DR IntAct; O95342; 2. DR MINT; MINT-5003953; -. DR STRING; 9606.ENSP00000263817; -. DR BindingDB; O95342; -. DR ChEMBL; CHEMBL6020; -. DR DrugBank; DB00171; Adenosine triphosphate. DR DrugBank; DB00559; Bosentan. DR DrugBank; DB01016; Glibenclamide. DR TCDB; 3.A.1.201.2; the atp-binding cassette (abc) superfamily. DR PhosphoSite; O95342; -. DR MaxQB; O95342; -. DR PaxDb; O95342; -. DR PRIDE; O95342; -. DR Ensembl; ENST00000263817; ENSP00000263817; ENSG00000073734. DR Ensembl; ENST00000576612; ENSP00000459250; ENSG00000263298. DR GeneID; 8647; -. DR KEGG; hsa:8647; -. DR UCSC; uc002ueo.1; human. DR CTD; 8647; -. DR GeneCards; GC02M169743; -. DR GeneReviews; ABCB11; -. DR H-InvDB; HIX0029772; -. DR HGNC; HGNC:42; ABCB11. DR HPA; HPA019035; -. DR MIM; 601847; phenotype. DR MIM; 603201; gene. DR MIM; 605479; phenotype. DR neXtProt; NX_O95342; -. DR Orphanet; 99961; Benign recurrent intrahepatic cholestasis type 2. DR Orphanet; 69665; Intrahepatic cholestasis of pregnancy. DR Orphanet; 79304; Progressive familial intrahepatic cholestasis type 2. DR PharmGKB; PA374; -. DR eggNOG; COG1132; -. DR HOVERGEN; HBG080809; -. DR InParanoid; O95342; -. DR KO; K05664; -. DR OMA; TIVWTNS; -. DR PhylomeDB; O95342; -. DR TreeFam; TF105193; -. DR Reactome; REACT_111217; Metabolism. DR ChiTaRS; ABCB11; human. DR GeneWiki; ABCB11; -. DR GenomeRNAi; 8647; -. DR NextBio; 32419; -. DR PRO; PR:O95342; -. DR ArrayExpress; O95342; -. DR Bgee; O95342; -. DR CleanEx; HS_ABCB11; -. DR Genevestigator; O95342; -. DR GO; GO:0016324; C:apical plasma membrane; IBA:RefGenome. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0000139; C:Golgi membrane; IBA:RefGenome. DR GO; GO:0016021; C:integral component of membrane; IBA:RefGenome. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0046581; C:intercellular canaliculus; IBA:RefGenome. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; TAS:ProtInc. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IBA:RefGenome. DR GO; GO:0015432; F:bile acid-exporting ATPase activity; TAS:ProtInc. DR GO; GO:0015126; F:canalicular bile acid transmembrane transporter activity; IBA:RefGenome. DR GO; GO:0008554; F:sodium-exporting ATPase activity, phosphorylative mechanism; TAS:ProtInc. DR GO; GO:0005215; F:transporter activity; TAS:ProtInc. DR GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome. DR GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome. DR GO; GO:0008206; P:bile acid metabolic process; TAS:Reactome. DR GO; GO:0015722; P:canalicular bile acid transport; IBA:RefGenome. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0035725; P:sodium ion transmembrane transport; TAS:GOC. DR GO; GO:0055085; P:transmembrane transport; IBA:RefGenome. DR GO; GO:0006810; P:transport; TAS:ProtInc. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR001140; ABC_transptr_TM_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF90123; SSF90123; 3. DR PROSITE; PS50929; ABC_TM1F; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Disease mutation; Glycoprotein; KW Intrahepatic cholestasis; Membrane; Nucleotide-binding; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 1321 Bile salt export pump. FT /FTId=PRO_0000093296. FT TOPO_DOM 1 62 Cytoplasmic (Potential). FT TRANSMEM 63 83 Helical; (Potential). FT TOPO_DOM 84 147 Extracellular (Potential). FT TRANSMEM 148 168 Helical; (Potential). FT TOPO_DOM 169 215 Cytoplasmic (Potential). FT TRANSMEM 216 236 Helical; (Potential). FT TOPO_DOM 237 240 Extracellular (Potential). FT TRANSMEM 241 261 Helical; (Potential). FT TOPO_DOM 262 319 Cytoplasmic (Potential). FT TRANSMEM 320 340 Helical; (Potential). FT TOPO_DOM 341 353 Extracellular (Potential). FT TRANSMEM 354 374 Helical; (Potential). FT TOPO_DOM 375 755 Cytoplasmic (Potential). FT TRANSMEM 756 776 Helical; (Potential). FT TOPO_DOM 777 794 Extracellular (Potential). FT TRANSMEM 795 815 Helical; (Potential). FT TOPO_DOM 816 869 Cytoplasmic (Potential). FT TRANSMEM 870 890 Helical; (Potential). FT TRANSMEM 891 911 Helical; (Potential). FT TOPO_DOM 912 979 Cytoplasmic (Potential). FT TRANSMEM 980 1000 Helical; (Potential). FT TOPO_DOM 1001 1011 Extracellular (Potential). FT TRANSMEM 1012 1032 Helical; (Potential). FT TOPO_DOM 1033 1321 Cytoplasmic (Potential). FT DOMAIN 62 385 ABC transmembrane type-1 1. FT DOMAIN 420 656 ABC transporter 1. FT DOMAIN 755 1043 ABC transmembrane type-1 2. FT DOMAIN 1078 1316 ABC transporter 2. FT NP_BIND 455 462 ATP 1 (Potential). FT NP_BIND 1113 1120 ATP 2 (Potential). FT REGION 651 672 Interaction with HAX1 (By similarity). FT MOD_RES 690 690 Phosphoserine (By similarity). FT CARBOHYD 109 109 N-linked (GlcNAc...). FT CARBOHYD 116 116 N-linked (GlcNAc...). FT CARBOHYD 122 122 N-linked (GlcNAc...). FT CARBOHYD 125 125 N-linked (GlcNAc...). FT VARIANT 56 56 S -> L (in dbSNP:rs11568361). FT /FTId=VAR_055472. FT VARIANT 186 186 E -> G (in BRIC2). FT /FTId=VAR_030386. FT VARIANT 206 206 I -> V (in dbSNP:rs11568357). FT /FTId=VAR_030387. FT VARIANT 238 238 G -> V (in PFIC2). FT /FTId=VAR_030388. FT VARIANT 284 284 V -> A. FT /FTId=VAR_035349. FT VARIANT 284 284 V -> L (in PFIC2). FT /FTId=VAR_013332. FT VARIANT 297 297 E -> G (in PFIC2 and BRIC2; reduced FT transport capacity for taurocholate). FT /FTId=VAR_010271. FT VARIANT 299 299 R -> K (in dbSNP:rs2287617). FT /FTId=VAR_030389. FT VARIANT 336 336 C -> S (in PFIC2). FT /FTId=VAR_030390. FT VARIANT 415 415 R -> Q. FT /FTId=VAR_043074. FT VARIANT 432 432 R -> T (in BRIC2; reduced transport FT capacity for taurocholate). FT /FTId=VAR_030391. FT VARIANT 444 444 V -> A (more frequent in patients with FT drug-induced cholestasis than healthy FT controls; associated with lower hepatic FT expression; does not affect transport FT capacity for taurocholate; FT dbSNP:rs2287622). FT /FTId=VAR_013333. FT VARIANT 444 444 V -> D (in dbSNP:rs2287622). FT /FTId=VAR_059106. FT VARIANT 444 444 V -> G (in dbSNP:rs2287622). FT /FTId=VAR_059107. FT VARIANT 461 461 K -> E (in PFIC2). FT /FTId=VAR_013334. FT VARIANT 482 482 D -> G (in PFIC2). FT /FTId=VAR_013335. FT VARIANT 570 570 A -> T (in BRIC2). FT /FTId=VAR_030392. FT VARIANT 591 591 N -> S (in a patient with intrahepatic FT cholestasis of pregnancy; FT dbSNP:rs11568367). FT /FTId=VAR_043075. FT VARIANT 616 616 R -> G. FT /FTId=VAR_035350. FT VARIANT 619 619 T -> A. FT /FTId=VAR_035351. FT VARIANT 676 676 D -> Y (in fluvastatin-induced FT cholestasis; does not affect transport FT capacity for taurocholate). FT /FTId=VAR_043076. FT VARIANT 677 677 M -> V (does not affect transport FT capacity for taurocholate; FT dbSNP:rs11568364). FT /FTId=VAR_030393. FT VARIANT 698 698 R -> H (in dbSNP:rs138642043). FT /FTId=VAR_035352. FT VARIANT 855 855 G -> R (in ethinylestradiol/gestodene- FT induced cholestasis; loss of transport FT capacity for taurocholate). FT /FTId=VAR_043077. FT VARIANT 865 865 A -> V (in dbSNP:rs118109635). FT /FTId=VAR_035353. FT VARIANT 923 923 T -> P (in BRIC2). FT /FTId=VAR_030394. FT VARIANT 926 926 A -> P (in BRIC2). FT /FTId=VAR_030395. FT VARIANT 958 958 R -> Q. FT /FTId=VAR_035354. FT VARIANT 982 982 G -> R (in PFIC2). FT /FTId=VAR_013336. FT VARIANT 1004 1004 G -> D (in PFIC2). FT /FTId=VAR_013337. FT VARIANT 1050 1050 R -> C (in BRIC2). FT /FTId=VAR_030396. FT VARIANT 1128 1128 R -> H (in BRIC2). FT /FTId=VAR_030397. FT VARIANT 1153 1153 R -> C (in PFIC2). FT /FTId=VAR_013338. FT VARIANT 1186 1186 E -> K (in dbSNP:rs1521808). FT /FTId=VAR_030398. FT VARIANT 1268 1268 R -> Q (in PFIC2). FT /FTId=VAR_013339. FT CONFLICT 339 339 L -> V (in Ref. 1; AAC77455). SQ SEQUENCE 1321 AA; 146407 MW; 61EE2173E2351D80 CRC64; MSDSVILRSI KKFGEENDGF ESDKSYNNDK KSRLQDEKKG DGVRVGFFQL FRFSSSTDIW LMFVGSLCAF LHGIAQPGVL LIFGTMTDVF IDYDVELQEL QIPGKACVNN TIVWTNSSLN QNMTNGTRCG LLNIESEMIK FASYYAGIAV AVLITGYIQI CFWVIAAARQ IQKMRKFYFR RIMRMEIGWF DCNSVGELNT RFSDDINKIN DAIADQMALF IQRMTSTICG FLLGFFRGWK LTLVIISVSP LIGIGAATIG LSVSKFTDYE LKAYAKAGVV ADEVISSMRT VAAFGGEKRE VERYEKNLVF AQRWGIRKGI VMGFFTGFVW CLIFLCYALA FWYGSTLVLD EGEYTPGTLV QIFLSVIVGA LNLGNASPCL EAFATGRAAA TSIFETIDRK PIIDCMSEDG YKLDRIKGEI EFHNVTFHYP SRPEVKILND LNMVIKPGEM TALVGPSGAG KSTALQLIQR FYDPCEGMVT VDGHDIRSLN IQWLRDQIGI VEQEPVLFST TIAENIRYGR EDATMEDIVQ AAKEANAYNF IMDLPQQFDT LVGEGGGQMS GGQKQRVAIA RALIRNPKIL LLDMATSALD NESEAMVQEV LSKIQHGHTI ISVAHRLSTV RAADTIIGFE HGTAVERGTH EELLERKGVY FTLVTLQSQG NQALNEEDIK DATEDDMLAR TFSRGSYQDS LRASIRQRSK SQLSYLVHEP PLAVVDHKST YEEDRKDKDI PVQEEVEPAP VRRILKFSAP EWPYMLVGSV GAAVNGTVTP LYAFLFSQIL GTFSIPDKEE QRSQINGVCL LFVAMGCVSL FTQFLQGYAF AKSGELLTKR LRKFGFRAML GQDIAWFDDL RNSPGALTTR LATDASQVQG AAGSQIGMIV NSFTNVTVAM IIAFSFSWKL SLVILCFFPF LALSGATQTR MLTGFASRDK QALEMVGQIT NEALSNIRTV AGIGKERRFI EALETELEKP FKTAIQKANI YGFCFAFAQC IMFIANSASY RYGGYLISNE GLHFSYVFRV ISAVVLSATA LGRAFSYTPS YAKAKISAAR FFQLLDRQPP ISVYNTAGEK WDNFQGKIDF VDCKFTYPSR PDSQVLNGLS VSISPGQTLA FVGSSGCGKS TSIQLLERFY DPDQGKVMID GHDSKKVNVQ FLRSNIGIVS QEPVLFACSI MDNIKYGDNT KEIPMERVIA AAKQAQLHDF VMSLPEKYET NVGSQGSQLS RGEKQRIAIA RAIVRDPKIL LLDEATSALD TESEKTVQVA LDKAREGRTC IVIAHRLSTI QNADIIAVMA QGVVIEKGTH EELMAQKGAY YKLVTTGSPI S // ID ABCC8_HUMAN Reviewed; 1581 AA. AC Q09428; A6NMX8; E3UYX6; O75948; Q16583; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 6. DT 09-JUL-2014, entry version 153. DE RecName: Full=ATP-binding cassette sub-family C member 8; DE AltName: Full=Sulfonylurea receptor 1; GN Name=ABCC8; Synonyms=HRINS, SUR, SUR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Heart; RX PubMed=21671119; DOI=10.1007/s00018-011-0739-x; RA Schmid D., Stolzlechner M., Sorgner A., Bentele C., Assinger A., RA Chiba P., Moeslinger T.; RT "An abundant, truncated human sulfonylurea receptor 1 splice variant RT has prodiabetic properties and impairs sulfonylurea action."; RL Cell. Mol. Life Sci. 69:129-148(2012). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND RP VARIANT SER-1369. RC TISSUE=Pancreatic islet; RA Gonzalez G., Aguilar-Bryan L., Bryan J.; RT "Human beta cell sulfonylurea receptor, SUR1, expression."; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT RP SER-1369. RC TISSUE=Brain, and Foreskin; RA Thomas P.T., Wohllk N., Huang E., Gagel R.F., Cote G.J.; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-1369. RC TISSUE=Pancreas; RA Nishimura M., Miki T., Aizawa T., Seino S.; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1187-1581, AND VARIANT SER-1369. RC TISSUE=Pancreatic islet; RX PubMed=7716548; DOI=10.1126/science.7716548; RA Thomas P.M., Cote G.J., Wohllk N., Haddad B., Mathew P.M., Rabl W., RA Aguilar-Bryan L., Gagel R.F., Bryan J.; RT "Mutations in the sulfonylurea receptor gene in familial persistent RT hyperinsulinemic hypoglycemia of infancy."; RL Science 268:426-429(1995). RN [7] RP TOPOLOGY. RX PubMed=10506167; DOI=10.1074/jbc.274.41.29122; RA Raab-Graham K.F., Cirilo L.J., Boettcher A.A., Radeke C.M., RA Vandenberg C.A.; RT "Membrane topology of the amino-terminal region of the sulfonylurea RT receptor."; RL J. Biol. Chem. 274:29122-29129(1999). RN [8] RP REVIEW. RX PubMed=10204114; DOI=10.1210/er.20.2.101; RA Aguilar-Bryan L., Bryan J.; RT "Molecular biology of adenosine triphosphate-sensitive potassium RT channels."; RL Endocr. Rev. 20:101-135(1999). RN [9] RP REVIEW ON VARIANTS. RX PubMed=10338089; RX DOI=10.1002/(SICI)1098-1004(1999)13:5<351::AID-HUMU3>3.0.CO;2-R; RA Meissner T., Beinbrech B., Mayatepek E.; RT "Congenital hyperinsulinism: molecular basis of a heterogeneous RT disease."; RL Hum. Mutat. 13:351-361(1999). RN [10] RP VARIANT HHF1 VAL-716. RX PubMed=8751851; RA Thomas P.M., Wohllk N., Huang E., Kuhnle U., Rabl W., Gagel R.F., RA Cote G.J.; RT "Inactivation of the first nucleotide-binding fold of the sulfonylurea RT receptor, and familial persistent hyperinsulinemic hypoglycemia of RT infancy."; RL Am. J. Hum. Genet. 59:510-518(1996). RN [11] RP VARIANT SER-1369. RX PubMed=8635661; DOI=10.2337/diab.45.6.825; RA Inoue H., Ferrer J., Welling C.M., Elbein S.C., Hoffman M., RA Mayorga R., Warren-Perry M., Zhang Y., Millns H., Turner R., RA Province M., Bryan J., Permutt M.A., Aguilar-Bryan L.; RT "Sequence variants in the sulfonylurea receptor (SUR) gene are RT associated with NIDDM in Caucasians."; RL Diabetes 45:825-831(1996). RN [12] RP VARIANT HHF1 PHE-1387 DEL, AND VARIANTS GLY-1360; SER-1369 AND RP ILE-1572. RX PubMed=8923011; DOI=10.1093/hmg/5.11.1813; RA Nestorowicz A., Wilson B.A., Schoor K.P., Inoue H., Glaser B., RA Landau H., Stanley C.A., Thornton P.S., Clement J.P. IV, Bryan J., RA Aguilar-Bryan L., Permutt M.A.; RT "Mutations in the sulfonylurea receptor gene are associated with RT familial hyperinsulinism in Ashkenazi Jews."; RL Hum. Mol. Genet. 5:1813-1822(1996). RN [13] RP CHARACTERIZATION OF VARIANT HHF1 ARG-1478. RX PubMed=8650576; DOI=10.1126/science.272.5269.1785; RA Nichols C.G., Shyng S.-L., Nestorowicz A., Glaser B., Clement J.P. IV, RA Gonzalez G., Aguilar-Bryan L., Permutt M.A., Bryan J.; RT "Adenosine diphosphate as an intracellular regulator of insulin RT secretion."; RL Science 272:1785-1787(1996). RN [14] RP VARIANTS GLN-275; MET-560; ASN-810; CYS-834 AND SER-1369. RX PubMed=9519757; DOI=10.2337/diabetes.47.3.476; RA Ohta Y., Tanizawa Y., Inoue H., Hosaka T., Ueda K., Matsutani A., RA Repunte V.P., Yamada M., Kurachi Y., Bryan J., Aguilar-Bryan L., RA Permutt M.A., Oka Y.; RT "Identification and functional analysis of sulfonylurea receptor 1 RT variants in Japanese patients with NIDDM."; RL Diabetes 47:476-481(1998). RN [15] RP VARIANTS ASN-673 AND SER-1369. RX PubMed=9568693; DOI=10.2337/diabetes.47.4.598; RA Hansen T., Echwald S.M., Hansen L., Moeller A.M., Almind K., RA Clausen J.O., Urhammer S.A., Inoue H., Ferrer J., Bryan J., RA Aguilar-Bryan L., Permutt M.A., Pedersen O.; RT "Decreased tolbutamide-stimulated insulin secretion in healthy RT subjects with sequence variants in the high-affinity sulfonylurea RT receptor gene."; RL Diabetes 47:598-605(1998). RN [16] RP CHARACTERIZATION OF VARIANTS HHF1 GLN-125; SER-188; LEU-591; MET-1138; RP GLN-1214; SER-1381; PHE-1387 DEL AND HIS-1393. RX PubMed=9648840; DOI=10.2337/diabetes.47.7.1145; RA Shyng S.-L., Ferrigni T., Shepard J.B., Nestorowicz A., Glaser B., RA Permutt M.A., Nichols C.G.; RT "Functional analyses of novel mutations in the sulfonylurea receptor 1 RT associated with persistent hyperinsulinemic hypoglycemia of infancy."; RL Diabetes 47:1145-1151(1998). RN [17] RP VARIANTS HHF1 GLN-74; GLN-125; SER-188; ASP-406; LEU-591; MET-1138; RP GLN-1214; ARG-1378; SER-1381; PHE-1387 DEL AND HIS-1393. RX PubMed=9618169; DOI=10.1093/hmg/7.7.1119; RA Nestorowicz A., Glaser B., Wilson B.A., Shyng S.-L., Nichols C.G., RA Stanley C.A., Thornton P.S., Permutt M.A.; RT "Genetic heterogeneity in familial hyperinsulinism."; RL Hum. Mol. Genet. 7:1119-1128(1998). RN [18] RP VARIANTS HHF1 PRO-1352; CYS-1420 AND TRP-1493. RX PubMed=9769320; DOI=10.1172/JCI4495; RA Verkarre V., Fournet J.-C., de Lonlay P., Gross-Morand M.-S., RA Devillers M., Rahier J., Brunelle F., Robert J.-J., Nihoul-Fekete C., RA Saudubray J.-M., Junien C.; RT "Paternal mutation of the sulfonylurea receptor (SUR1) gene and RT maternal loss of 11p15 imprinted genes lead to persistent RT hyperinsulinism in focal adenomatous hyperplasia."; RL J. Clin. Invest. 102:1286-1291(1998). RN [19] RP VARIANT HHF1 ASP-187. RX PubMed=10334322; DOI=10.2337/diabetes.48.2.408; RA Otonkoski T., Aemmaelae C., Huopio H., Cote G.J., Chapman J., RA Cosgrove K., Ashfield R., Huang E., Komulainen J., Ashcroft F.M., RA Dunne M.J., Kere J., Thomas P.M.; RT "A point mutation inactivating the sulfonylurea receptor causes the RT severe form of persistent hyperinsulinemic hypoglycemia of infancy in RT Finland."; RL Diabetes 48:408-415(1999). RN [20] RP VARIANTS SER-1369 AND ILE-1572. RX PubMed=10447255; RX DOI=10.1002/(SICI)1098-1004(1999)14:1<23::AID-HUMU3>3.0.CO;2-#; RA Glaser B., Furth J., Stanley C.A., Baker L., Thornton P.S., Landau H., RA Permutt M.A.; RT "Intragenic single nucleotide polymorphism haplotype analysis of SUR1 RT mutations in familial hyperinsulinism."; RL Hum. Mutat. 14:23-29(1999). RN [21] RP VARIANTS HHF1 GLY-841; CYS-1420 AND TRP-1493. RX PubMed=10202168; DOI=10.1056/NEJM199904153401505; RA de Lonlay-Debeney P., Poggi-Travert F., Fournet J.-C., Sempoux C., RA Vici C.D., Brunelle F., Touati G., Rahier J., Junien C., RA Nihoul-Fekete C., Robert J.-J., Saudubray J.-M.; RT "Clinical features of 52 neonates with hyperinsulinism."; RL N. Engl. J. Med. 340:1169-1175(1999). RN [22] RP CHARACTERIZATION OF VARIANTS HHF1 CYS-1420 AND GLN-1436, AND VARIANT RP SER-1369. RX PubMed=10615958; DOI=10.2337/diabetes.49.1.114; RA Tanizawa Y., Matsuda K., Matsuo M., Ohta Y., Ochi N., Adachi M., RA Koga M., Mizuno S., Kajita M., Tanaka Y., Tachibana K., Inoue H., RA Furukawa S., Amachi T., Ueda K., Oka Y.; RT "Genetic analysis of Japanese patients with persistent RT hyperinsulinemic hypoglycemia of infancy: nucleotide-binding fold-2 RT mutation impairs cooperative binding of adenine nucleotides to RT sulfonylurea receptor 1."; RL Diabetes 49:114-120(2000). RN [23] RP CHARACTERIZATION OF VARIANT HHF1 LYS-1506. RX PubMed=11018078; DOI=10.1172/JCI9804; RA Huopio H., Reimann F., Ashfield R., Komulainen J., Lenko H.-L., RA Rahier J., Vauhkonen I., Kere J., Laakso M., Ashcroft F., RA Otonkoski T.; RT "Dominantly inherited hyperinsulinism caused by a mutation in the RT sulfonylurea receptor type 1."; RL J. Clin. Invest. 106:897-906(2000). RN [24] RP CHARACTERIZATION OF VARIANT HHF1 PHE-1387 DEL. RX PubMed=11226335; DOI=10.1073/pnas.051499698; RA Cartier E.A., Conti L.R., Vandenberg C.A., Shyng S.-L.; RT "Defective trafficking and function of KATP channels caused by a RT sulfonylurea receptor 1 mutation associated with persistent RT hyperinsulinemic hypoglycemia of infancy."; RL Proc. Natl. Acad. Sci. U.S.A. 98:2882-2887(2001). RN [25] RP CHARACTERIZATION OF VARIANT HHF1 PRO-1543. RX PubMed=11867634; DOI=10.1074/jbc.M200363200; RA Taschenberger G., Mougey A., Shen S., Lester L.B., LaFranchi S., RA Shyng S.-L.; RT "Identification of a familial hyperinsulinism-causing mutation in the RT sulfonylurea receptor 1 that prevents normal trafficking and function RT of KATP channels."; RL J. Biol. Chem. 277:17139-17146(2002). RN [26] RP VARIANTS HHF1 ASP-187; THR-1457; LYS-1506; ASP-1550 AND VAL-1551. RX PubMed=12364426; DOI=10.1210/jc.2002-020378; RA Huopio H., Jaeaeskelaeinen J., Komulainen J., Miettinen R., RA Kaerkkaeinen P., Laakso M., Tapanainen P., Voutilainen R., RA Otonkoski T.; RT "Acute insulin response tests for the differential diagnosis of RT congenital hyperinsulinism."; RL J. Clin. Endocrinol. Metab. 87:4502-4507(2002). RN [27] RP VARIANT HHF1 SER-1385 DEL, AND CHARACTERIZATION OF VARIANT HHF1 RP SER-1385 DEL. RX PubMed=12941782; DOI=10.2337/diabetes.52.9.2403; RA Thornton P.S., MacMullen C., Ganguly A., Ruchelli E., Steinkrauss L., RA Crane A., Aguilar-Bryan L., Stanley C.A.; RT "Clinical and molecular characterization of a dominant form of RT congenital hyperinsulinism caused by a mutation in the high-affinity RT sulfonylurea receptor."; RL Diabetes 52:2403-2410(2003). RN [28] RP VARIANT LIH HIS-1352, AND CHARACTERIZATION OF VARIANT LIH HIS-1352. RX PubMed=15356046; DOI=10.1210/jc.2004-0441; RA Magge S.N., Shyng S.-L., MacMullen C., Steinkrauss L., Ganguly A., RA Katz L.E.L., Stanley C.A.; RT "Familial leucine-sensitive hypoglycemia of infancy due to a dominant RT mutation of the beta-cell sulfonylurea receptor."; RL J. Clin. Endocrinol. Metab. 89:4450-4456(2004). RN [29] RP VARIANTS HHF1 GLU-70; ARG-111; GLU-1342; HIS-1418 AND TRP-1493, AND RP CHARACTERIZATION OF VARIANTS HHF1 GLU-70; ARG-111; GLU-1342; HIS-1418 RP AND TRP-1493. RX PubMed=15579781; DOI=10.1210/jc.2004-1233; RA Tornovsky S., Crane A., Cosgrove K.E., Hussain K., Lavie J., RA Heyman M., Nesher Y., Kuchinski N., Ben-Shushan E., Shatz O., RA Nahari E., Potikha T., Zangen D., Tenenbaum-Rakover Y., de Vries L., RA Argente J., Gracia R., Landau H., Eliakim A., Lindley K., Dunne M.J., RA Aguilar-Bryan L., Glaser B.; RT "Hyperinsulinism of infancy: novel ABCC8 and KCNJ11 mutations and RT evidence for additional locus heterogeneity."; RL J. Clin. Endocrinol. Metab. 89:6224-6234(2004). RN [30] RP VARIANTS HHF1 GLN-1384 AND LYS-1486, AND VARIANT SER-1369. RX PubMed=15807877; DOI=10.1111/j.1365-2265.2005.02242.x; RA Ohkubo K., Nagashima M., Naito Y., Taguchi T., Suita S., Okamoto N., RA Fujinaga H., Tsumura K., Kikuchi K., Ono J.; RT "Genotypes of the pancreatic beta-cell K-ATP channel and clinical RT phenotypes of Japanese patients with persistent hyperinsulinaemic RT hypoglycaemia of infancy."; RL Clin. Endocrinol. (Oxf.) 62:458-465(2005). RN [31] RP VARIANTS HHF1 SER-27; TRP-74; SER-188; GLN-495; LYS-501; SER-686; RP TRP-1214; GLN-1214; ASN-1336; PHE-1387 DEL; HIS-1471 AND ASN-1471. RX PubMed=15562009; DOI=10.1210/jc.2004-1604; RA Henwood M.J., Kelly A., MacMullen C., Bhatia P., Ganguly A., RA Thornton P.S., Stanley C.A.; RT "Genotype-phenotype correlations in children with congenital RT hyperinsulinism due to recessive mutations of the adenosine RT triphosphate-sensitive potassium channel genes."; RL J. Clin. Endocrinol. Metab. 90:789-794(2005). RN [32] RP VARIANT PNDM LEU-132, AND CHARACTERIZATION OF VARIANT PNDM LEU-132. RX PubMed=16613899; DOI=10.1093/hmg/ddl101; RA Proks P., Arnold A.L., Bruining J., Girard C., Flanagan S.E., RA Larkin B., Colclough K., Hattersley A.T., Ashcroft F.M., Ellard S.; RT "A heterozygous activating mutation in the sulphonylurea receptor SUR1 RT (ABCC8) causes neonatal diabetes."; RL Hum. Mol. Genet. 15:1793-1800(2006). RN [33] RP VARIANTS HHF1 TRP-74; ARG-111; SER-188; ARG-233; ASN-310; ARG-551; RP THR-719; PRO-1130; ARG-1147; LYS-1295 AND PRO-1450, AND VARIANTS RP SER-1369 AND ILE-1572. RX PubMed=16429405; DOI=10.1002/humu.9401; RA Fernandez-Marmiesse A., Salas A., Vega A., Fernandez-Lorenzo J.R., RA Barreiro J., Carracedo A.; RT "Mutation spectra of ABCC8 gene in Spanish patients with RT Hyperinsulinism of Infancy (HI)."; RL Hum. Mutat. 27:214-214(2006). RN [34] RP VARIANTS HHF1 ARG-7; ASP-21; SER-27; TRP-74; LYS-501; PRO-503; RP SER-686; TRP-1214; TRP-1214; GLN-1349; ARG-1378; PHE-1387 DEL; RP ARG-1400 AND GLN-1493. RX PubMed=16357843; DOI=10.1038/modpathol.3800497; RA Suchi M., MacMullen C.M., Thornton P.S., Adzick N.S., Ganguly A., RA Ruchelli E.D., Stanley C.A.; RT "Molecular and immunohistochemical analyses of the focal form of RT congenital hyperinsulinism."; RL Mod. Pathol. 19:122-129(2006). RN [35] RP VARIANTS PNDM ARG-213 AND VAL-1424, VARIANTS TNDM2 ARG-435; VAL-582; RP TYR-1023; GLN-1182 AND CYS-1379, CHARACTERIZATION OF VARIANT PNDM RP VAL-1424, AND CHARACTERIZATION OF VARIANT TNDM2 TYR-1023. RX PubMed=16885549; DOI=10.1056/NEJMoa055068; RA Babenko A.P., Polak M., Cave H., Busiah K., Czernichow P., RA Scharfmann R., Bryan J., Aguilar-Bryan L., Vaxillaire M., Froguel P.; RT "Activating mutations in the ABCC8 gene in neonatal diabetes RT mellitus."; RL N. Engl. J. Med. 355:456-466(2006). RN [36] RP VARIANT PNDM ALA-86. RX PubMed=17213273; DOI=10.1210/jc.2006-2490; RA Stanik J., Gasperikova D., Paskova M., Barak L., Javorkova J., RA Jancova E., Ciljakova M., Hlava P., Michalek J., Flanagan S.E., RA Pearson E., Hattersley A.T., Ellard S., Klimes I.; RT "Prevalence of permanent neonatal diabetes in Slovakia and successful RT replacement of insulin with sulfonylurea therapy in KCNJ11 and ABCC8 RT mutation carriers."; RL J. Clin. Endocrinol. Metab. 92:1276-1282(2007). CC -!- FUNCTION: Putative subunit of the beta-cell ATP-sensitive CC potassium channel (KATP). Regulator of ATP-sensitive K(+) channels CC and insulin release. CC -!- SUBUNIT: Interacts with KCNJ11. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q09428-1; Sequence=Displayed; CC Name=2; CC IsoId=Q09428-2; Sequence=VSP_000055; CC Name=3; Synonyms=SUR1Delta2; CC IsoId=Q09428-3; Sequence=VSP_044090; CC Note=Abundant isoform with prodiabetic properties, predominant CC in heart; CC -!- DISEASE: Leucine-induced hypoglycemia (LIH) [MIM:240800]: Rare CC cause of hypoglycemia and is described as a condition in which CC symptomatic hypoglycemia is provoked by high protein feedings. CC Hypoglycemia is also elicited by administration of oral or CC intravenous infusions of a single amino acid, leucine. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- DISEASE: Familial hyperinsulinemic hypoglycemia 1 (HHF1) CC [MIM:256450]: Most common cause of persistent hypoglycemia in CC infancy. Unless early and aggressive intervention is undertaken, CC brain damage from recurrent episodes of hypoglycemia may occur. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Diabetes mellitus, permanent neonatal (PNDM) CC [MIM:606176]: A rare form of diabetes distinct from childhood- CC onset autoimmune diabetes mellitus type 1. It is characterized by CC insulin-requiring hyperglycemia that is diagnosed within the first CC months of life. Permanent neonatal diabetes requires lifelong CC therapy. Note=The disease is caused by mutations affecting the CC gene represented in this entry. CC -!- DISEASE: Transient neonatal diabetes mellitus 2 (TNDM2) CC [MIM:610374]: Neonatal diabetes is a form of diabetes mellitus CC defined by the onset of mild-to-severe hyperglycemia within the CC first months of life. Transient neonatal diabetes remits early, CC with a possible relapse during adolescence. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC CC family. Conjugate transporter (TC 3.A.1.208) subfamily. CC -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q09428"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; HM635782; ADM67556.1; -; mRNA. DR EMBL; L78207; AAB02278.1; -; mRNA. DR EMBL; L78243; AAB02417.1; -; Genomic_DNA. DR EMBL; L78208; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78209; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78210; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78211; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78212; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78255; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78213; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78214; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78215; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78216; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78217; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78218; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78219; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78220; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78221; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78222; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78223; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78225; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78254; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78226; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78227; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78228; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78229; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78230; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78231; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78232; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78233; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78234; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78235; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78236; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78237; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78238; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78239; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78240; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78241; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78242; AAB02417.1; JOINED; Genomic_DNA. DR EMBL; L78243; AAB02418.1; -; Genomic_DNA. DR EMBL; L78208; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78209; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78210; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78211; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78212; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78255; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78213; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78214; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78215; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78216; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78217; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78218; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78219; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78220; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78221; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78222; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78224; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78225; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78254; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78226; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78227; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78228; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78229; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78230; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78231; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78232; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78233; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78234; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78235; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78236; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78237; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78238; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78239; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78240; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78241; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; L78242; AAB02418.1; JOINED; Genomic_DNA. DR EMBL; U63421; AAB36699.1; -; mRNA. DR EMBL; U63455; AAB36700.1; -; Genomic_DNA. DR EMBL; U63422; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63423; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63424; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63425; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63426; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63427; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63428; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63429; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63430; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63431; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63432; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63433; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63434; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63435; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63436; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63437; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63438; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63439; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63441; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63442; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63443; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63444; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63445; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63446; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63447; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63448; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63449; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63450; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63451; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63452; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63453; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; U63454; AAB36700.1; JOINED; Genomic_DNA. DR EMBL; AF087138; AAC36724.1; -; mRNA. DR EMBL; AC124798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L40625; AAA99227.1; -; mRNA. DR CCDS; CCDS31437.1; -. [Q09428-1] DR RefSeq; NP_000343.2; NM_000352.4. [Q09428-1] DR RefSeq; NP_001274103.1; NM_001287174.1. [Q09428-2] DR UniGene; Hs.54470; -. DR ProteinModelPortal; Q09428; -. DR BioGrid; 112700; 2. DR DIP; DIP-58642N; -. DR STRING; 9606.ENSP00000374467; -. DR BindingDB; Q09428; -. DR ChEMBL; CHEMBL2096972; -. DR DrugBank; DB00171; Adenosine triphosphate. DR DrugBank; DB01016; Glibenclamide. DR DrugBank; DB01120; Gliclazide. DR DrugBank; DB01252; Mitiglinide. DR DrugBank; DB00731; Nateglinide. DR DrugBank; DB00912; Repaglinide. DR TCDB; 3.A.1.208.4; the atp-binding cassette (abc) superfamily. DR PhosphoSite; Q09428; -. DR DMDM; 311033501; -. DR PaxDb; Q09428; -. DR PRIDE; Q09428; -. DR DNASU; 6833; -. DR Ensembl; ENST00000302539; ENSP00000303960; ENSG00000006071. [Q09428-2] DR Ensembl; ENST00000389817; ENSP00000374467; ENSG00000006071. [Q09428-1] DR GeneID; 6833; -. DR KEGG; hsa:6833; -. DR UCSC; uc001mnc.3; human. [Q09428-1] DR CTD; 6833; -. DR GeneCards; GC11M017414; -. DR GeneReviews; ABCC8; -. DR H-InvDB; HIX0035864; -. DR HGNC; HGNC:59; ABCC8. DR HPA; CAB011451; -. DR HPA; HPA042318; -. DR MIM; 240800; phenotype. DR MIM; 256450; phenotype. DR MIM; 600509; gene. DR MIM; 602485; phenotype. DR MIM; 606176; phenotype. DR MIM; 610374; phenotype. DR neXtProt; NX_Q09428; -. DR Orphanet; 276575; Autosomal dominant hyperinsulinism due to SUR1 deficiency. DR Orphanet; 79643; Autosomal recessive hyperinsulinism due to SUR1 deficiency. DR Orphanet; 276598; Diazoxide-resistant focal hyperinsulinism due to SUR1 deficiency. DR Orphanet; 552; MODY syndrome. DR Orphanet; 99885; Permanent neonatal diabetes mellitus. DR Orphanet; 99886; Transient neonatal diabetes mellitus. DR PharmGKB; PA24395; -. DR eggNOG; COG1132; -. DR HOVERGEN; HBG101342; -. DR KO; K05032; -. DR OMA; RKDSVFA; -. DR OrthoDB; EOG7MWGW0; -. DR PhylomeDB; Q09428; -. DR TreeFam; TF105201; -. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_13685; Neuronal System. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR SignaLink; Q09428; -. DR GeneWiki; ABCC8; -. DR GenomeRNAi; 6833; -. DR NextBio; 26675; -. DR PRO; PR:Q09428; -. DR ArrayExpress; Q09428; -. DR Bgee; Q09428; -. DR CleanEx; HS_ABCC8; -. DR Genevestigator; Q09428; -. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL. DR GO; GO:0005524; F:ATP binding; TAS:ProtInc. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL. DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; TAS:ProtInc. DR GO; GO:0008281; F:sulfonylurea receptor activity; TAS:ProtInc. DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc. DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome. DR GO; GO:0071805; P:potassium ion transmembrane transport; TAS:GOC. DR GO; GO:0006813; P:potassium ion transport; TAS:ProtInc. DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; TAS:GOC. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR001140; ABC_transptr_TM_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000388; Sulphorea_rcpt. DR InterPro; IPR000844; Surea_rcpt-1. DR Pfam; PF00664; ABC_membrane; 2. DR Pfam; PF00005; ABC_tran; 2. DR PRINTS; PR01093; SULFNYLUR1. DR PRINTS; PR01092; SULFNYLUREAR. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF90123; SSF90123; 2. DR PROSITE; PS50929; ABC_TM1F; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Complete proteome; KW Diabetes mellitus; Disease mutation; Glycoprotein; Membrane; KW Nucleotide-binding; Polymorphism; Receptor; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 1581 ATP-binding cassette sub-family C member FT 8. FT /FTId=PRO_0000093400. FT TOPO_DOM 1 34 Extracellular (By similarity). FT TRANSMEM 35 55 Helical; Name=1; (By similarity). FT TOPO_DOM 56 75 Cytoplasmic (By similarity). FT TRANSMEM 76 96 Helical; Name=2; (By similarity). FT TOPO_DOM 97 101 Extracellular (By similarity). FT TRANSMEM 102 122 Helical; Name=3; (By similarity). FT TOPO_DOM 123 134 Cytoplasmic (By similarity). FT TRANSMEM 135 154 Helical; Name=4; (By similarity). FT TOPO_DOM 155 167 Extracellular (By similarity). FT TRANSMEM 168 194 Helical; Name=5; (By similarity). FT TOPO_DOM 195 311 Cytoplasmic (By similarity). FT TRANSMEM 312 331 Helical; Name=6; (By similarity). FT TOPO_DOM 332 355 Extracellular (By similarity). FT TRANSMEM 356 376 Helical; Name=7; (By similarity). FT TOPO_DOM 377 434 Cytoplasmic (By similarity). FT TRANSMEM 435 455 Helical; Name=8; (By similarity). FT TOPO_DOM 456 458 Extracellular (By similarity). FT TRANSMEM 459 479 Helical; Name=9; (By similarity). FT TOPO_DOM 480 541 Cytoplasmic (By similarity). FT TRANSMEM 542 562 Helical; Name=10; (By similarity). FT TOPO_DOM 563 584 Extracellular (By similarity). FT TRANSMEM 585 605 Helical; Name=11; (By similarity). FT TOPO_DOM 606 1004 Cytoplasmic (By similarity). FT TRANSMEM 1005 1025 Helical; Name=12; (By similarity). FT TOPO_DOM 1026 1072 Extracellular (By similarity). FT TRANSMEM 1073 1093 Helical; Name=13; (By similarity). FT TOPO_DOM 1094 1137 Cytoplasmic (By similarity). FT TRANSMEM 1138 1158 Helical; Name=14; (By similarity). FT TOPO_DOM 1159 1159 Extracellular (By similarity). FT TRANSMEM 1160 1180 Helical; Name=15; (By similarity). FT TOPO_DOM 1181 1251 Cytoplasmic (By similarity). FT TRANSMEM 1252 1272 Helical; Name=16; (By similarity). FT TOPO_DOM 1273 1276 Extracellular (By similarity). FT TRANSMEM 1277 1297 Helical; Name=17; (By similarity). FT TOPO_DOM 1298 1581 Cytoplasmic (By similarity). FT DOMAIN 299 602 ABC transmembrane type-1 1. FT DOMAIN 679 929 ABC transporter 1. FT DOMAIN 1012 1306 ABC transmembrane type-1 2. FT DOMAIN 1344 1578 ABC transporter 2. FT NP_BIND 713 720 ATP 1 (Potential). FT NP_BIND 1378 1385 ATP 2 (Potential). FT CARBOHYD 10 10 N-linked (GlcNAc...) (By similarity). FT CARBOHYD 1049 1049 N-linked (GlcNAc...) (By similarity). FT VAR_SEQ 51 1581 Missing (in isoform 3). FT /FTId=VSP_044090. FT VAR_SEQ 740 740 S -> SS (in isoform 2). FT /FTId=VSP_000055. FT VARIANT 7 7 G -> R (in HHF1). FT /FTId=VAR_031349. FT VARIANT 21 21 V -> D (in HHF1). FT /FTId=VAR_031350. FT VARIANT 27 27 F -> S (in HHF1). FT /FTId=VAR_031351. FT VARIANT 70 70 G -> E (in HHF1; altered intracellular FT trafficking). FT /FTId=VAR_031352. FT VARIANT 74 74 R -> Q (in HHF1). FT /FTId=VAR_008639. FT VARIANT 74 74 R -> W (in HHF1; dbSNP:rs201682634). FT /FTId=VAR_031353. FT VARIANT 86 86 V -> A (in PNDM). FT /FTId=VAR_031354. FT VARIANT 104 104 L -> V (in dbSNP:rs10400391). FT /FTId=VAR_029777. FT VARIANT 111 111 G -> R (in HHF1; altered intracellular FT trafficking). FT /FTId=VAR_031355. FT VARIANT 116 116 A -> P (in HHF1). FT /FTId=VAR_031356. FT VARIANT 125 125 H -> Q (in HHF1; mild; dbSNP:rs60637558). FT /FTId=VAR_008640. FT VARIANT 132 132 F -> L (in PNDM; with neurologic FT features; reduces the sensitivity of the FT K(ATP) channel to inhibition by MgATP; FT increases whole-cell K(ATP) current). FT /FTId=VAR_029778. FT VARIANT 187 187 V -> D (in HHF1; severe; high prevalence FT in Finland; loss of channel activity). FT /FTId=VAR_008641. FT VARIANT 188 188 N -> S (in HHF1; severe). FT /FTId=VAR_008642. FT VARIANT 213 213 L -> R (in PNDM). FT /FTId=VAR_029779. FT VARIANT 233 233 M -> R (in HHF1). FT /FTId=VAR_031357. FT VARIANT 275 275 R -> Q. FT /FTId=VAR_008643. FT VARIANT 310 310 D -> N (in HHF1). FT /FTId=VAR_031358. FT VARIANT 406 406 N -> D (in HHF1). FT /FTId=VAR_008644. FT VARIANT 418 418 C -> R (in HHF1; dbSNP:rs67254669). FT /FTId=VAR_031359. FT VARIANT 435 435 C -> R (in TNDM2). FT /FTId=VAR_029780. FT VARIANT 495 495 R -> Q (in HHF1). FT /FTId=VAR_031360. FT VARIANT 501 501 E -> K (in HHF1). FT /FTId=VAR_031361. FT VARIANT 503 503 L -> P (in HHF1). FT /FTId=VAR_031362. FT VARIANT 508 508 L -> P (in HHF1). FT /FTId=VAR_031363. FT VARIANT 551 551 P -> R (in HHF1). FT /FTId=VAR_031364. FT VARIANT 560 560 V -> M (in dbSNP:rs4148619). FT /FTId=VAR_008645. FT VARIANT 582 582 L -> V (in TNDM2). FT /FTId=VAR_029781. FT VARIANT 591 591 F -> L (in HHF1). FT /FTId=VAR_008646. FT VARIANT 620 620 R -> C (in HHF1; dbSNP:rs58241708). FT /FTId=VAR_031365. FT VARIANT 673 673 D -> N. FT /FTId=VAR_015006. FT VARIANT 686 686 F -> S (in HHF1). FT /FTId=VAR_031366. FT VARIANT 716 716 G -> V (in HHF1). FT /FTId=VAR_000100. FT VARIANT 719 719 K -> T (in HHF1). FT /FTId=VAR_031367. FT VARIANT 810 810 D -> N. FT /FTId=VAR_008647. FT VARIANT 834 834 R -> C. FT /FTId=VAR_008648. FT VARIANT 841 841 R -> G (in HHF1). FT /FTId=VAR_031368. FT VARIANT 889 889 K -> T (in HHF1). FT /FTId=VAR_031369. FT VARIANT 956 956 S -> F (in HHF1). FT /FTId=VAR_031370. FT VARIANT 1023 1023 H -> Y (in TNDM2; overactive channel). FT /FTId=VAR_029782. FT VARIANT 1130 1130 T -> P (in HHF1). FT /FTId=VAR_031371. FT VARIANT 1138 1138 T -> M (in HHF1). FT /FTId=VAR_008649. FT VARIANT 1147 1147 L -> R (in HHF1). FT /FTId=VAR_031372. FT VARIANT 1182 1182 R -> Q (in TNDM2). FT /FTId=VAR_029783. FT VARIANT 1214 1214 R -> Q (in HHF1; severe). FT /FTId=VAR_008650. FT VARIANT 1214 1214 R -> W (in HHF1). FT /FTId=VAR_031373. FT VARIANT 1295 1295 N -> K (in HHF1). FT /FTId=VAR_031374. FT VARIANT 1336 1336 K -> N (in HHF1). FT /FTId=VAR_031375. FT VARIANT 1342 1342 G -> E (in HHF1; altered intracellular FT trafficking). FT /FTId=VAR_031376. FT VARIANT 1349 1349 L -> Q (in HHF1). FT /FTId=VAR_031377. FT VARIANT 1352 1352 R -> H (in LIH; partially impairs ATP- FT dependent potassium channel function). FT /FTId=VAR_029784. FT VARIANT 1352 1352 R -> P (in HHF1; dbSNP:rs28936370). FT /FTId=VAR_008537. FT VARIANT 1360 1360 V -> G. FT /FTId=VAR_008651. FT VARIANT 1360 1360 V -> M (in HHF1). FT /FTId=VAR_015007. FT VARIANT 1369 1369 A -> S (in dbSNP:rs757110). FT /FTId=VAR_008652. FT VARIANT 1378 1378 G -> R (in HHF1). FT /FTId=VAR_008653. FT VARIANT 1379 1379 R -> C (in TNDM2). FT /FTId=VAR_029785. FT VARIANT 1381 1381 G -> S (in HHF1). FT /FTId=VAR_008654. FT VARIANT 1384 1384 K -> Q (in HHF1). FT /FTId=VAR_031378. FT VARIANT 1385 1385 Missing (in HHF1; does not alter surface FT expression but channels are not FT functional). FT /FTId=VAR_029786. FT VARIANT 1386 1386 S -> F (in HHF1). FT /FTId=VAR_031379. FT VARIANT 1387 1387 Missing (in HHF1; severe; high frequency FT in Ashkenazi Jewish patients; defective FT trafficking and lack of surface FT expression). FT /FTId=VAR_008538. FT VARIANT 1393 1393 R -> H (in HHF1; severe; loss of channel FT activity). FT /FTId=VAR_008655. FT VARIANT 1400 1400 G -> R (in HHF1). FT /FTId=VAR_031380. FT VARIANT 1418 1418 R -> H (in HHF1; altered intracellular FT trafficking). FT /FTId=VAR_031381. FT VARIANT 1420 1420 R -> C (in HHF1; modest impairment of FT channel function; dbSNP:rs28938469). FT /FTId=VAR_008539. FT VARIANT 1424 1424 I -> V (in PNDM; overactive channel). FT /FTId=VAR_029787. FT VARIANT 1436 1436 R -> Q (in HHF1; cannot form a functional FT channel, due to protein instability or FT defective transport to the membrane). FT /FTId=VAR_015008. FT VARIANT 1450 1450 L -> P (in HHF1). FT /FTId=VAR_031382. FT VARIANT 1457 1457 A -> T (in HHF1). FT /FTId=VAR_031383. FT VARIANT 1471 1471 D -> H (in HHF1). FT /FTId=VAR_031384. FT VARIANT 1471 1471 D -> N (in HHF1). FT /FTId=VAR_031385. FT VARIANT 1478 1478 G -> R (in HHF1; channels insensitive to FT metabolic inhibition and to activation by FT ADP). FT /FTId=VAR_008656. FT VARIANT 1486 1486 R -> K (in HHF1). FT /FTId=VAR_031386. FT VARIANT 1493 1493 R -> Q (in HHF1). FT /FTId=VAR_031387. FT VARIANT 1493 1493 R -> W (in HHF1; altered intracellular FT trafficking; dbSNP:rs28936371). FT /FTId=VAR_008540. FT VARIANT 1506 1506 E -> K (in HHF1; mild; dominantly FT inherited; channels insensitive to FT metabolic inhibition and to activation by FT ADP). FT /FTId=VAR_015009. FT VARIANT 1507 1507 A -> AAS (in HHF1). FT /FTId=VAR_008657. FT VARIANT 1543 1543 L -> P (in HHF1; reduced channels surface FT expression and response to ADP). FT /FTId=VAR_015010. FT VARIANT 1550 1550 V -> D (in HHF1). FT /FTId=VAR_031388. FT VARIANT 1551 1551 L -> V (in HHF1). FT /FTId=VAR_031389. FT VARIANT 1572 1572 V -> I (in dbSNP:rs8192690). FT /FTId=VAR_008658. FT CONFLICT 30 30 A -> V (in Ref. 2; AAB02278/AAB02417/ FT AAB02418). FT CONFLICT 157 157 F -> L (in Ref. 3; AAB36699/AAB36700). FT CONFLICT 163 163 G -> A (in Ref. 2; AAB02278/AAB02417/ FT AAB02418). FT CONFLICT 167 167 L -> V (in Ref. 2; AAB02278/AAB02417/ FT AAB02418). FT CONFLICT 225 225 L -> P (in Ref. 3; AAB36699/AAB36700). FT CONFLICT 256 256 A -> V (in Ref. 3; AAB36699/AAB36700). FT CONFLICT 487 487 S -> T (in Ref. 2; AAB02278/AAB02417/ FT AAB02418). FT CONFLICT 1069 1070 VL -> AV (in Ref. 2; AAB02278/AAB02417/ FT AAB02418). FT CONFLICT 1172 1172 I -> V (in Ref. 3; AAB36699/AAB36700). FT CONFLICT 1410 1410 A -> R (in Ref. 3; AAB36699/AAB36700). FT CONFLICT 1418 1418 R -> P (in Ref. 3; AAB36699/AAB36700). SQ SEQUENCE 1581 AA; 176992 MW; 09CF2EC97899D1CE CRC64; MPLAFCGSEN HSAAYRVDQG VLNNGCFVDA LNVVPHVFLL FITFPILFIG WGSQSSKVHI HHSTWLHFPG HNLRWILTFM LLFVLVCEIA EGILSDGVTE SHHLHLYMPA GMAFMAAVTS VVYYHNIETS NFPKLLIALL VYWTLAFITK TIKFVKFLDH AIGFSQLRFC LTGLLVILYG MLLLVEVNVI RVRRYIFFKT PREVKPPEDL QDLGVRFLQP FVNLLSKGTY WWMNAFIKTA HKKPIDLRAI GKLPIAMRAL TNYQRLCEAF DAQVRKDIQG TQGARAIWQA LSHAFGRRLV LSSTFRILAD LLGFAGPLCI FGIVDHLGKE NDVFQPKTQF LGVYFVSSQE FLANAYVLAV LLFLALLLQR TFLQASYYVA IETGINLRGA IQTKIYNKIM HLSTSNLSMG EMTAGQICNL VAIDTNQLMW FFFLCPNLWA MPVQIIVGVI LLYYILGVSA LIGAAVIILL APVQYFVATK LSQAQRSTLE YSNERLKQTN EMLRGIKLLK LYAWENIFRT RVETTRRKEM TSLRAFAIYT SISIFMNTAI PIAAVLITFV GHVSFFKEAD FSPSVAFASL SLFHILVTPL FLLSSVVRST VKALVSVQKL SEFLSSAEIR EEQCAPHEPT PQGPASKYQA VPLRVVNRKR PAREDCRGLT GPLQSLVPSA DGDADNCCVQ IMGGYFTWTP DGIPTLSNIT IRIPRGQLTM IVGQVGCGKS SLLLAALGEM QKVSGAVFWS SLPDSEIGED PSPERETATD LDIRKRGPVA YASQKPWLLN ATVEENIIFE SPFNKQRYKM VIEACSLQPD IDILPHGDQT QIGERGINLS GGQRQRISVA RALYQHANVV FLDDPFSALD IHLSDHLMQA GILELLRDDK RTVVLVTHKL QYLPHADWII AMKDGTIQRE GTLKDFQRSE CQLFEHWKTL MNRQDQELEK ETVTERKATE PPQGLSRAMS SRDGLLQDEE EEEEEAAESE EDDNLSSMLH QRAEIPWRAC AKYLSSAGIL LLSLLVFSQL LKHMVLVAID YWLAKWTDSA LTLTPAARNC SLSQECTLDQ TVYAMVFTVL CSLGIVLCLV TSVTVEWTGL KVAKRLHRSL LNRIILAPMR FFETTPLGSI LNRFSSDCNT IDQHIPSTLE CLSRSTLLCV SALAVISYVT PVFLVALLPL AIVCYFIQKY FRVASRDLQQ LDDTTQLPLL SHFAETVEGL TTIRAFRYEA RFQQKLLEYT DSNNIASLFL TAANRWLEVR MEYIGACVVL IAAVTSISNS LHRELSAGLV GLGLTYALMV SNYLNWMVRN LADMELQLGA VKRIHGLLKT EAESYEGLLA PSLIPKNWPD QGKIQIQNLS VRYDSSLKPV LKHVNALIAP GQKIGICGRT GSGKSSFSLA FFRMVDTFEG HIIIDGIDIA KLPLHTLRSR LSIILQDPVL FSGTIRFNLD PERKCSDSTL WEALEIAQLK LVVKALPGGL DAIITEGGEN FSQGQRQLFC LARAFVRKTS IFIMDEATAS IDMATENILQ KVVMTAFADR TVVTIAHRVH TILSADLVIV LKRGAILEFD KPEKLLSRKD SVFASFVRAD K // ID ABCD1_HUMAN Reviewed; 745 AA. AC P33897; Q6GTZ2; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 09-JUL-2014, entry version 167. DE RecName: Full=ATP-binding cassette sub-family D member 1; DE AltName: Full=Adrenoleukodystrophy protein; DE Short=ALDP; GN Name=ABCD1; Synonyms=ALD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=8441467; DOI=10.1038/361726a0; RA Mosser J., Douar A.-M., Sarde C.-O., Kioschis P., Feil R., Moser H., RA Poustka A.-M., Mandel J.-L., Aubourg P.; RT "Putative X-linked adrenoleukodystrophy gene shares unexpected RT homology with ABC transporters."; RL Nature 361:726-730(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUBUNIT, AND CHARACTERIZATION OF VARIANTS ALD HIS-389; GLN-401; RP ARG-484 AND GLN-591. RX PubMed=10551832; DOI=10.1074/jbc.274.46.32738; RA Liu L.X., Janvier K., Berteaux-Lecellier V., Cartier N., Benarous R., RA Aubourg P.; RT "Homo- and heterodimerization of peroxisomal ATP-binding cassette RT half-transporters."; RL J. Biol. Chem. 274:32738-32743(1999). RN [5] RP FUNCTION, AND CHARACTERIZATION OF VARIANTS ALD SER-512 AND LEU-606. RX PubMed=11248239; DOI=10.1016/S0014-5793(01)02235-9; RA Roerig P., Mayerhofer P., Holzinger A., Gaertner J.; RT "Characterization and functional analysis of the nucleotide binding RT fold in human peroxisomal ATP binding cassette transporters."; RL FEBS Lett. 492:66-72(2001). RN [6] RP REVIEW. RX PubMed=8507690; DOI=10.1016/0300-9084(93)90089-B; RA Aubourg P., Mosser J., Douar A.-M., Sarde C.-O., Lopez J., RA Mandel J.-L.; RT "Adrenoleukodystrophy gene: unexpected homology to a protein involved RT in peroxisome biogenesis."; RL Biochimie 75:293-302(1993). RN [7] RP INTERACTION WITH PEX19. RC TISSUE=Brain; RX PubMed=10777694; DOI=10.1006/bbrc.2000.2572; RA Gloeckner C.J., Mayerhofer P.U., Landgraf P., Muntau A.C., RA Holzinger A., Gerber J.-K., Kammerer S., Adamski J., Roscher A.A.; RT "Human adrenoleukodystrophy protein and related peroxisomal ABC RT transporters interact with the peroxisomal assembly protein PEX19p."; RL Biochem. Biophys. Res. Commun. 271:144-150(2000). RN [8] RP INTERACTION WITH PEX19. RX PubMed=10704444; DOI=10.1083/jcb.148.5.931; RA Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.; RT "PEX19 binds multiple peroxisomal membrane proteins, is predominantly RT cytoplasmic, and is required for peroxisome membrane synthesis."; RL J. Cell Biol. 148:931-944(2000). RN [9] RP REVIEW ON VARIANTS. RX PubMed=9195223; RX DOI=10.1002/(SICI)1098-1004(1997)9:6<500::AID-HUMU2>3.0.CO;2-5; RA Dodd A., Rowland S.A., Hawkes S.L.J., Kennedy M.A., Love D.R.; RT "Mutations in the adrenoleukodystrophy gene."; RL Hum. Mutat. 9:500-511(1997). RN [10] RP REVIEW ON VARIANTS. RX PubMed=11748843; DOI=10.1002/humu.1227; RA Kemp S., Pujol A., Waterham H.R., van Geel B.M., Boehm C.D., RA Raymond G.V., Cutting G.R., Wanders R.J.A., Moser H.W.; RT "ABCD1 mutations and the X-linked adrenoleukodystrophy mutation RT database: role in diagnosis and clinical correlations."; RL Hum. Mutat. 18:499-515(2001). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP VARIANT ALD LYS-291. RX PubMed=7904210; DOI=10.1093/hmg/2.11.1949; RA Cartier N., Sarde C.-O., Douar A.-M., Mosser J., Mandel J.-L., RA Aubourg P.; RT "Abnormal messenger RNA expression and a missense mutation in patients RT with X-linked adrenoleukodystrophy."; RL Hum. Mol. Genet. 2:1949-1951(1993). RN [15] RP VARIANTS ALD SER-148; ASP-174; ARG-266; GLN-401; TRP-418 AND PHE-515. RX PubMed=7849723; DOI=10.1093/hmg/3.10.1903; RA Fuchs S., Sarde C.-O., Wedemann H., Schwinger E., Mandel J.-L., RA Gal A.; RT "Missense mutations are frequent in the gene for X-chromosomal RT adrenoleukodystrophy (ALD)."; RL Hum. Mol. Genet. 3:1903-1905(1994). RN [16] RP VARIANTS ALD TRP-518; LEU-606; CYS-617 AND HIS-617. RX PubMed=8040304; DOI=10.1172/JCI117363; RA Fanen P., Guidoux S., Sarde C.-O., Mandel J.-L., Goossens M., RA Aubourg P.; RT "Identification of mutations in the putative ATP-binding domain of the RT adrenoleukodystrophy gene."; RL J. Clin. Invest. 94:516-520(1994). RN [17] RP VARIANTS ALD. RX PubMed=7825602; RA Ligtenberg M.J.L., Kemp S., Sarde C.-O., van Geel B.M., Kleijer W.J., RA Barth P.G., Mandel J.-L., van Oost B.A., Bolhuis P.A.; RT "Spectrum of mutations in the gene encoding the adrenoleukodystrophy RT protein."; RL Am. J. Hum. Genet. 56:44-50(1995). RN [18] RP VARIANTS ALD HIS-104; GLU-178; GLY-528 DEL AND LEU-560. RX PubMed=7717396; RA Braun A., Ambach H., Kammerer S., Rolinski B., Stoeckler S., Rabl W., RA Gaertner J., Zierz S., Roscher A.A.; RT "Mutations in the gene for X-linked adrenoleukodystrophy in patients RT with different clinical phenotypes."; RL Am. J. Hum. Genet. 56:854-861(1995). RN [19] RP VARIANTS ALD. RX PubMed=7581394; DOI=10.1002/humu.1380060203; RA Kok F., Neumann S., Sarde C.-O., Zheng S., Wu K.-H., Wei H.-M., RA Bergin J., Watkins P.A., Gould S., Sack G., Moser H., Mandel J.-L., RA Smith K.D.; RT "Mutational analysis of patients with X-linked adrenoleukodystrophy."; RL Hum. Mutat. 6:104-115(1995). RN [20] RP VARIANTS ALD. RX PubMed=8651290; RA Feigenbaum V., Lombard-Platet G., Guidoux S., Sarde C.-O., RA Mandel J.-L., Aubourg P.; RT "Mutational and protein analysis of patients and heterozygous women RT with X-linked adrenoleukodystrophy."; RL Am. J. Hum. Genet. 58:1135-1144(1996). RN [21] RP VARIANTS ALD PRO-107; ASP-174; MET-254; GLY-389; GLN-401; TRP-418; RP LYS-609; CYS-617 AND GLY-617. RX PubMed=8566952; DOI=10.1007/BF02265264; RA Krasemann E.W., Meier V., Korenke G.C., Hunneman D.H., Hanefeld F.; RT "Identification of mutations in the ALD-gene of 20 families with RT adrenoleukodystrophy/adrenomyeloneuropathy."; RL Hum. Genet. 97:194-197(1996). RN [22] RP VARIANT ALD ARG-679. RX PubMed=9452087; RA Korenke G.C., Krasemann E., Meier V., Beuche W., Hunneman D.H., RA Hanefeld F.; RT "First missense mutation (W679R) in exon 10 of the RT adrenoleukodystrophy gene in siblings with adrenomyeloneuropathy."; RL Hum. Mutat. Suppl. 1:S204-S206(1998). RN [23] RP VARIANTS ALD PRO-105; SER-143; SER-148; PRO-190; ASP-298; SER-529 AND RP TYR-638. RX PubMed=10480364; DOI=10.1007/s004399900090; RA Wichers M., Kohler W., Brennemann W., Boese V., Sokolowski P., RA Bidlingmaier F., Ludwig M.; RT "X-linked adrenomyeloneuropathy associated with 14 novel ALD-gene RT mutations: no correlation between type of mutation and age of onset."; RL Hum. Genet. 105:116-119(1999). RN [24] RP VARIANTS ALD LEU-108 AND SER-143. RX PubMed=10369742; DOI=10.1006/mcpr.1999.0232; RA Perusi C., Gomez-Lira M., Mottes M., Pignatti P.F., Bertini E., RA Cappa M., Vigliani M.C., Schiffer D., Rizzuto N., Salviati A.; RT "Two novel missense mutations causing adrenoleukodystrophy in Italian RT patients."; RL Mol. Cell. Probes 13:179-182(1999). RN [25] RP VARIANTS ALD ARG-103; ARG-116; SER-152; CYS-174; TRP-189; THR-218; RP PRO-229; ASP-298; GLN-401; TRP-401; TRP-418; LEU-543; HIS-554; RP VAL-616; ARG-633 AND PRO-646. RX PubMed=10737980; RX DOI=10.1002/(SICI)1098-1004(200004)15:4<348::AID-HUMU7>3.0.CO;2-N; RA Lachtermacher M.B., Seuanez H.N., Moser A.B., Moser H.W., Smith K.D.; RT "Determination of 30 X-linked adrenoleukodystrophy mutations, RT including 15 not previously described."; RL Hum. Mutat. 15:348-353(2000). RN [26] RP VARIANTS ALD GLN-401; TRP-418; LEU-543 AND ARG-556. RX PubMed=10980539; RX DOI=10.1002/1098-1004(200009)16:3<271::AID-HUMU15>3.0.CO;2-D; RA Lira M.G., Mottes M., Pignatti P.F., Medica I., Uziel G., Cappa M., RA Bertini E., Rizzuto N., Salviati A.; RT "Detection of mutations in the ALD gene (ABCD1) in seven Italian RT families: description of four novel mutations."; RL Hum. Mutat. 16:271-271(2000). RN [27] RP VARIANTS ALD LEU-98; ASP-99; GLU-217; GLN-518; ASP-608; ILE-633 AND RP PRO-660, AND VARIANT THR-13. RX PubMed=11438993; DOI=10.1002/humu.1149; RA Dvorakova L., Storkanova G., Unterrainer G., Hujova J., Kmoch S., RA Zeman J., Hrebicek M., Berger J.; RT "Eight novel ABCD1 gene mutations and three polymorphisms in patients RT with X-linked adrenoleukodystrophy: the first polymorphism causing an RT amino acid exchange."; RL Hum. Mutat. 18:52-60(2001). RN [28] RP VARIANT ALD VAL-GLY-GLN-300 INS. RX PubMed=11810273; DOI=10.1007/s00439-001-0632-z; RA Guimaraes C.P., Lemos M., Menezes I., Coelho T., Sa-Miranda C., RA Azevedo J.E.; RT "Characterisation of two mutations in the ABCD1 gene leading to low RT levels of normal ALDP."; RL Hum. Genet. 109:616-622(2001). RN [29] RP INVOLVEMENT IN CONTIGUOUS ABCD1/DXS1375E DELETION SYNDROME. RX PubMed=11992258; DOI=10.1086/340849; RA Corzo D., Gibson W., Johnson K., Mitchell G., LePage G., Cox G.F., RA Casey R., Zeiss C., Tyson H., Cutting G.R., Raymond G.V., Smith K.D., RA Watkins P.A., Moser A.B., Moser H.W., Steinberg S.J.; RT "Contiguous deletion of the X-linked adrenoleukodystrophy gene (ABCD1) RT and DXS1357E: a novel neonatal phenotype similar to peroxisomal RT biogenesis disorders."; RL Am. J. Hum. Genet. 70:1520-1531(2002). RN [30] RP VARIANTS ALD TRP-88; CYS-152; CYS-181; SER-343; PRO-503; ARG-514 AND RP HIS-554. RX PubMed=15643618; DOI=10.1002/humu.9303; RA Montagna G., Di Biase A., Cappa M., Melone M.A.B., Piantadosi C., RA Colabianchi D., Patrono C., Attori L., Cannelli N., Cotrufo R., RA Salvati S., Santorelli F.M.; RT "Identification of seven novel mutations in ABCD1 by a DHPLC-based RT assay in Italian patients with X-linked adrenoleukodystrophy."; RL Hum. Mutat. 25:222-222(2005). RN [31] RP VARIANTS ALD GLN-401; PRO-516; LEU-560; PRO-606 AND GLN-660. RX PubMed=21889498; DOI=10.1016/j.cca.2011.08.026; RA Shukla P., Gupta N., Gulati S., Ghosh M., Vasisht S., Sharma R., RA Gupta A.K., Kalra V., Kabra M.; RT "Molecular analysis of ABCD1 gene in Indian patients with X-linked RT adrenoleukodystrophy."; RL Clin. Chim. Acta 412:2289-2295(2011). RN [32] RP VARIANTS ALD LEU-139 DEL; ARG-198; ARG-266; GLU-266; TRP-401; GLN-518; RP PHE-523; CYS-540; LEU-560; PRO-606; HIS-617; THR-626; PRO-632; RP ARG-633; LYS-640 AND ASP-677. RX PubMed=21700483; DOI=10.1016/j.ymgme.2011.05.016; RA Wang Y., Busin R., Reeves C., Bezman L., Raymond G., Toomer C.J., RA Watkins P.A., Snowden A., Moser A., Naidu S., Bibat G., Hewson S., RA Tam K., Clarke J.T., Charnas L., Stetten G., Karczeski B., Cutting G., RA Steinberg S.; RT "X-linked adrenoleukodystrophy: ABCD1 de novo mutations and RT mosaicism."; RL Mol. Genet. Metab. 104:160-166(2011). CC -!- FUNCTION: Probable transporter. The nucleotide-binding fold acts CC as an ATP-binding subunit with ATPase activity. CC -!- SUBUNIT: Can form homodimers and heterodimers with ABCD2/ALDR and CC ABCD3/PMP70. Dimerization is necessary to form an active CC transporter. Interacts with PEX19. CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-81045, EBI-81045; CC P48410:Abcd1 (xeno); NbExp=2; IntAct=EBI-81045, EBI-81118; CC P28288:ABCD3; NbExp=2; IntAct=EBI-81045, EBI-80992; CC P40855:PEX19; NbExp=3; IntAct=EBI-81045, EBI-594747; CC -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane CC protein. CC -!- DISEASE: Adrenoleukodystrophy (ALD) [MIM:300100]: A peroxisomal CC metabolic disorder characterized by progressive multifocal CC demyelination of the central nervous system and by peripheral CC adrenal insufficiency (Addison disease). It results in mental CC deterioration, corticospinal tract dysfunction, and cortical CC blindness. Different clinical manifestations exist like: cerebral CC childhood ALD (CALD), adult cerebral ALD (ACALD), CC adrenomyeloneuropathy (AMN) and 'Addison disease only' (ADO) CC phenotype. Note=The disease is caused by mutations affecting the CC gene represented in this entry. CC -!- DISEASE: Note=The promoter region of ABCD1 is deleted in the CC chromosome Xq28 deletion syndrome which involves ABCD1 and the CC neighboring gene BCAP31. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD CC family. Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) CC subfamily. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC -!- WEB RESOURCE: Name=X-ALD gene mutation database; CC URL="http://www.x-ald.nl/"; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P33897"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z21876; CAA79922.1; -; mRNA. DR EMBL; Z31348; CAA83230.1; -; Genomic_DNA. DR EMBL; Z31006; CAA83230.1; JOINED; Genomic_DNA. DR EMBL; Z31007; CAA83230.1; JOINED; Genomic_DNA. DR EMBL; Z31008; CAA83230.1; JOINED; Genomic_DNA. DR EMBL; Z31009; CAA83230.1; JOINED; Genomic_DNA. DR EMBL; Z31010; CAA83230.1; JOINED; Genomic_DNA. DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC015541; AAH15541.1; -; mRNA. DR EMBL; BC025358; AAH25358.1; -; mRNA. DR CCDS; CCDS14728.1; -. DR PIR; G02500; G02500. DR RefSeq; NP_000024.2; NM_000033.3. DR UniGene; Hs.159546; -. DR ProteinModelPortal; P33897; -. DR SMR; P33897; 466-675. DR BioGrid; 106717; 17. DR IntAct; P33897; 6. DR STRING; 9606.ENSP00000218104; -. DR TCDB; 3.A.1.203.3; the atp-binding cassette (abc) superfamily. DR PhosphoSite; P33897; -. DR DMDM; 67476960; -. DR MaxQB; P33897; -. DR PaxDb; P33897; -. DR PeptideAtlas; P33897; -. DR PRIDE; P33897; -. DR DNASU; 215; -. DR Ensembl; ENST00000218104; ENSP00000218104; ENSG00000101986. DR Ensembl; ENST00000601366; ENSP00000473207; ENSG00000268757. DR GeneID; 215; -. DR KEGG; hsa:215; -. DR UCSC; uc004fif.2; human. DR CTD; 215; -. DR GeneCards; GC0XP152990; -. DR GeneReviews; ABCD1; -. DR HGNC; HGNC:61; ABCD1. DR HPA; HPA035214; -. DR MIM; 300100; phenotype. DR MIM; 300371; gene. DR neXtProt; NX_P33897; -. DR Orphanet; 139399; Adrenomyeloneuropathy. DR Orphanet; 369942; CADDS. DR Orphanet; 139396; X-linked cerebral adrenoleukodystrophy. DR PharmGKB; PA24396; -. DR eggNOG; COG4178; -. DR HOGENOM; HOG000206081; -. DR HOVERGEN; HBG050438; -. DR InParanoid; P33897; -. DR KO; K05675; -. DR OMA; IPKMQRR; -. DR PhylomeDB; P33897; -. DR TreeFam; TF105205; -. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR GeneWiki; ABCD1; -. DR GenomeRNAi; 215; -. DR NextBio; 870; -. DR PRO; PR:P33897; -. DR ArrayExpress; P33897; -. DR Bgee; P33897; -. DR CleanEx; HS_ABCD1; -. DR Genevestigator; P33897; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATPase activity; IDA:UniProtKB. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; NAS:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0005325; F:peroxisomal fatty-acyl-CoA transporter activity; IGI:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0005215; F:transporter activity; NAS:UniProtKB. DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome. DR GO; GO:0006200; P:ATP catabolic process; IDA:GOC. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB. DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; TAS:Reactome. DR GO; GO:0043651; P:linoleic acid metabolic process; TAS:Reactome. DR GO; GO:0042758; P:long-chain fatty acid catabolic process; IGI:UniProtKB. DR GO; GO:0015910; P:peroxisomal long-chain fatty acid import; IGI:UniProtKB. DR GO; GO:0015919; P:peroxisomal membrane transport; NAS:UniProtKB. DR GO; GO:0007031; P:peroxisome organization; IDA:UniProtKB. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0033559; P:unsaturated fatty acid metabolic process; TAS:Reactome. DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IDA:UniProtKB. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR010509; ABC_Peroxi_TM. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR005283; FA_transporter. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF06472; ABC_membrane_2; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR TIGRFAMs; TIGR00954; 3a01203; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Disease mutation; Glycoprotein; KW Membrane; Nucleotide-binding; Peroxisome; Phosphoprotein; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 745 ATP-binding cassette sub-family D member FT 1. FT /FTId=PRO_0000093304. FT TRANSMEM 92 112 Helical; (Potential). FT TRANSMEM 131 151 Helical; (Potential). FT TRANSMEM 238 258 Helical; (Potential). FT TRANSMEM 333 353 Helical; (Potential). FT TRANSMEM 473 493 Helical; (Potential). FT DOMAIN 94 386 ABC transmembrane type-1. FT DOMAIN 474 700 ABC transporter. FT NP_BIND 507 514 ATP (By similarity). FT REGION 67 186 Interaction with PEX19. FT MOD_RES 733 733 Phosphoserine. FT CARBOHYD 214 214 N-linked (GlcNAc...) (Potential). FT VARIANT 13 13 N -> T (very rare polymorphism; does not FT affect ALDP function; dbSNP:rs183021839). FT /FTId=VAR_013340. FT VARIANT 88 88 C -> W (in ALD). FT /FTId=VAR_023004. FT VARIANT 90 90 E -> K (in ALD). FT /FTId=VAR_009349. FT VARIANT 98 98 S -> L (in ALD; CALD type). FT /FTId=VAR_000024. FT VARIANT 99 99 A -> D (in ALD; AMN-type). FT /FTId=VAR_013341. FT VARIANT 103 103 S -> R (in ALD). FT /FTId=VAR_009350. FT VARIANT 104 104 R -> C (in ALD). FT /FTId=VAR_000025. FT VARIANT 104 104 R -> H (in ALD; ADO-type). FT /FTId=VAR_000026. FT VARIANT 105 105 T -> I (in ALD; ADO-type). FT /FTId=VAR_000027. FT VARIANT 105 105 T -> P (in ALD). FT /FTId=VAR_009351. FT VARIANT 107 107 L -> P (in ALD; ALD/AMN/ADO-types and FT asymptomatic). FT /FTId=VAR_000028. FT VARIANT 108 108 S -> L (in ALD). FT /FTId=VAR_009352. FT VARIANT 108 108 S -> W (in ALD; CALD and AMN-types). FT /FTId=VAR_000029. FT VARIANT 113 113 R -> C (in ALD). FT /FTId=VAR_009353. FT VARIANT 113 113 R -> P (in ALD). FT /FTId=VAR_013342. FT VARIANT 116 116 G -> R (in ALD; CALD-type). FT /FTId=VAR_000030. FT VARIANT 138 141 Missing (in ALD; ALD-type). FT /FTId=VAR_000032. FT VARIANT 139 139 Missing (in ALD). FT /FTId=VAR_067239. FT VARIANT 141 141 A -> T (in ALD). FT /FTId=VAR_000033. FT VARIANT 143 143 P -> S (in ALD). FT /FTId=VAR_009354. FT VARIANT 148 148 N -> S (in ALD; ADO-type). FT /FTId=VAR_000034. FT VARIANT 149 149 S -> N (in ALD). FT /FTId=VAR_000035. FT VARIANT 152 152 R -> C (in ALD; ADO-type). FT /FTId=VAR_000036. FT VARIANT 152 152 R -> L (in ALD). FT /FTId=VAR_009355. FT VARIANT 152 152 R -> P (in ALD). FT /FTId=VAR_000037. FT VARIANT 152 152 R -> S (in ALD). FT /FTId=VAR_009356. FT VARIANT 161 161 S -> P (in ALD). FT /FTId=VAR_009357. FT VARIANT 163 163 R -> H (in ALD). FT /FTId=VAR_000038. FT VARIANT 163 163 R -> P (in ALD). FT /FTId=VAR_009358. FT VARIANT 174 174 Y -> C (in ALD). FT /FTId=VAR_009359. FT VARIANT 174 174 Y -> D (in ALD; ALD-type). FT /FTId=VAR_000039. FT VARIANT 174 174 Y -> S (in ALD; CALD-type). FT /FTId=VAR_000040. FT VARIANT 178 178 Q -> E (in ALD; AMN-type). FT /FTId=VAR_000041. FT VARIANT 181 181 Y -> C (in ALD; ALMD-type). FT /FTId=VAR_000042. FT VARIANT 182 182 R -> P (in ALD). FT /FTId=VAR_000043. FT VARIANT 189 189 R -> W (in ALD). FT /FTId=VAR_009360. FT VARIANT 190 190 L -> P (in ALD). FT /FTId=VAR_009361. FT VARIANT 194 194 D -> H (in ALD). FT /FTId=VAR_000044. FT VARIANT 198 198 T -> K (in ALD). FT /FTId=VAR_009362. FT VARIANT 198 198 T -> R (in ALD). FT /FTId=VAR_067240. FT VARIANT 200 200 D -> N (in ALD). FT /FTId=VAR_009363. FT VARIANT 200 200 D -> V (in ALD; CALD-type). FT /FTId=VAR_000045. FT VARIANT 207 207 S -> SAAS (in ALD). FT /FTId=VAR_013343. FT VARIANT 211 211 L -> P (in ALD). FT /FTId=VAR_000046. FT VARIANT 213 213 S -> C (in ALD). FT /FTId=VAR_009364. FT VARIANT 214 214 N -> D (in ALD). FT /FTId=VAR_009365. FT VARIANT 217 217 K -> E (in ALD). FT /FTId=VAR_013344. FT VARIANT 218 218 P -> T (in ALD). FT /FTId=VAR_009366. FT VARIANT 220 220 L -> P (in ALD). FT /FTId=VAR_000047. FT VARIANT 221 221 D -> G (in ALD; CALD and AMN-types). FT /FTId=VAR_000048. FT VARIANT 224 224 V -> E (in ALD). FT /FTId=VAR_013345. FT VARIANT 229 229 L -> P (in ALD). FT /FTId=VAR_009367. FT VARIANT 254 254 T -> M (in ALD; AMN-type). FT /FTId=VAR_000049. FT VARIANT 254 254 T -> P (in ALD; AMN-type). FT /FTId=VAR_000050. FT VARIANT 263 263 P -> L (in ALD; CALD, AMN and AD-types). FT /FTId=VAR_000051. FT VARIANT 266 266 G -> E (in ALD). FT /FTId=VAR_067241. FT VARIANT 266 266 G -> R (in ALD). FT /FTId=VAR_000052. FT VARIANT 271 271 E -> K (in ALD). FT /FTId=VAR_009368. FT VARIANT 274 274 R -> W (in ALD). FT /FTId=VAR_013346. FT VARIANT 276 276 K -> E (in ALD; CALD-type). FT /FTId=VAR_000053. FT VARIANT 277 277 G -> GN (in ALD; ADO-type). FT /FTId=VAR_000055. FT VARIANT 277 277 G -> R (in ALD; AMN-type). FT /FTId=VAR_000054. FT VARIANT 277 277 G -> W (in ALD). FT /FTId=VAR_000056. FT VARIANT 280 280 R -> C (in ALD). FT /FTId=VAR_013347. FT VARIANT 285 285 R -> P (in ALD). FT /FTId=VAR_009369. FT VARIANT 291 291 E -> D (in ALD; ACALD and CALD-types). FT /FTId=VAR_000057. FT VARIANT 291 291 E -> K (in ALD). FT /FTId=VAR_000058. FT VARIANT 291 291 Missing (in ALD; ALD-type). FT /FTId=VAR_000059. FT VARIANT 294 294 A -> T (in ALD; AMN-type). FT /FTId=VAR_000060. FT VARIANT 296 296 Y -> C (in ALD). FT /FTId=VAR_009370. FT VARIANT 298 298 G -> D (in ALD). FT /FTId=VAR_009371. FT VARIANT 300 300 E -> EVGQ (in ALD). FT /FTId=VAR_013348. FT VARIANT 302 302 E -> K (in ALD). FT /FTId=VAR_009372. FT VARIANT 322 322 L -> P (in ALD). FT /FTId=VAR_009373. FT VARIANT 336 336 K -> M (in ALD). FT /FTId=VAR_009374. FT VARIANT 339 339 W -> R (in ALD). FT /FTId=VAR_013349. FT VARIANT 342 342 S -> P (in ALD; AMN-type). FT /FTId=VAR_000061. FT VARIANT 343 343 G -> D (in ALD). FT /FTId=VAR_013350. FT VARIANT 343 343 G -> S (in ALD). FT /FTId=VAR_023005. FT VARIANT 389 389 R -> G (in ALD; AMN-type). FT /FTId=VAR_000062. FT VARIANT 389 389 R -> H (in ALD; does not affect protein FT stability, homo- and heterodimerization FT with ALDR and PMP70). FT /FTId=VAR_000063. FT VARIANT 401 401 R -> Q (in ALD; ALD and AMN-types; does FT not affect protein stability, homo- and FT heterodimerization with ALDR and PMP70). FT /FTId=VAR_000064. FT VARIANT 401 401 R -> W (in ALD). FT /FTId=VAR_009375. FT VARIANT 418 418 R -> W (in ALD; AMN-type). FT /FTId=VAR_000065. FT VARIANT 427 427 Missing (in ALD). FT /FTId=VAR_013351. FT VARIANT 484 484 P -> R (in ALD; CALD, AMN and ADO-types; FT significantly decreases homodimerization FT and abolishes heterodimerization with FT ALDR and PMP70). FT /FTId=VAR_000066. FT VARIANT 503 503 L -> P (in ALD). FT /FTId=VAR_023006. FT VARIANT 507 507 G -> V (in ALD; CALD-types). FT /FTId=VAR_000067. FT VARIANT 512 512 G -> S (in ALD; CALD and AS-types; FT reduced ATPase activity). FT /FTId=VAR_000068. FT VARIANT 514 514 S -> R (in ALD). FT /FTId=VAR_023007. FT VARIANT 515 515 S -> F (in ALD). FT /FTId=VAR_000069. FT VARIANT 516 516 L -> P (in ALD). FT /FTId=VAR_067328. FT VARIANT 518 518 R -> Q (in ALD; CALD-type). FT /FTId=VAR_000070. FT VARIANT 518 518 R -> W (in ALD; CALD-type). FT /FTId=VAR_000071. FT VARIANT 522 522 G -> W (in ALD; AD-type). FT /FTId=VAR_000072. FT VARIANT 523 523 L -> F (in ALD). FT /FTId=VAR_067242. FT VARIANT 528 528 Missing (in ALD; CALD-type). FT /FTId=VAR_000073. FT VARIANT 529 529 G -> S (in ALD). FT /FTId=VAR_009376. FT VARIANT 534 534 P -> L (in ALD; CALD-type). FT /FTId=VAR_000074. FT VARIANT 540 540 F -> C (in ALD). FT /FTId=VAR_067243. FT VARIANT 540 540 F -> S (in ALD). FT /FTId=VAR_009377. FT VARIANT 543 543 P -> L (in ALD). FT /FTId=VAR_009378. FT VARIANT 544 544 Q -> R (in ALD). FT /FTId=VAR_009379. FT VARIANT 552 552 S -> P (in ALD). FT /FTId=VAR_009380. FT VARIANT 554 554 R -> H (in ALD). FT /FTId=VAR_009381. FT VARIANT 556 556 Q -> R (in ALD; ACALD type). FT /FTId=VAR_013352. FT VARIANT 560 560 P -> L (in ALD; CALD-type). FT /FTId=VAR_000075. FT VARIANT 560 560 P -> R (in ALD; AMN and ALMD-types). FT /FTId=VAR_000076. FT VARIANT 560 560 P -> S (in ALD). FT /FTId=VAR_013353. FT VARIANT 566 566 M -> K (in ALD). FT /FTId=VAR_000077. FT VARIANT 591 591 R -> P (in ALD). FT /FTId=VAR_013354. FT VARIANT 591 591 R -> Q (in ALD; AMN-type; significantly FT decreases homodimerization and abolishes FT heterodimerization with ALDR and PMP70). FT /FTId=VAR_000078. FT VARIANT 591 591 R -> W (in ALD). FT /FTId=VAR_009382. FT VARIANT 606 606 S -> L (in ALD; decreased ATP-binding FT affinity). FT /FTId=VAR_000079. FT VARIANT 606 606 S -> P (in ALD; CALD, AMN and ALMD- FT types). FT /FTId=VAR_000080. FT VARIANT 608 608 G -> D (in ALD; CALD-type). FT /FTId=VAR_013355. FT VARIANT 609 609 E -> G (in ALD). FT /FTId=VAR_000081. FT VARIANT 609 609 E -> K (in ALD; AMN-type). FT /FTId=VAR_000082. FT VARIANT 616 616 A -> V (in ALD). FT /FTId=VAR_009383. FT VARIANT 617 617 R -> C (in ALD; ALD-type and FT asymptomatic). FT /FTId=VAR_000083. FT VARIANT 617 617 R -> G (in ALD; ADO and AMN-types with FT cerebral involvement). FT /FTId=VAR_000084. FT VARIANT 617 617 R -> H (in ALD). FT /FTId=VAR_000085. FT VARIANT 626 626 A -> D (in ALD). FT /FTId=VAR_013356. FT VARIANT 626 626 A -> T (in ALD; CALD and AMN-types). FT /FTId=VAR_000086. FT VARIANT 629 629 D -> H (in ALD). FT /FTId=VAR_000087. FT VARIANT 630 630 E -> G (in ALD). FT /FTId=VAR_009384. FT VARIANT 631 631 C -> Y (in ALD). FT /FTId=VAR_009385. FT VARIANT 632 632 T -> I (in ALD). FT /FTId=VAR_013357. FT VARIANT 632 632 T -> P (in ALD). FT /FTId=VAR_067244. FT VARIANT 633 633 S -> I (in ALD; asymptomatic). FT /FTId=VAR_013358. FT VARIANT 633 633 S -> R (in ALD). FT /FTId=VAR_009386. FT VARIANT 635 635 V -> M (in ALD). FT /FTId=VAR_013359. FT VARIANT 636 636 S -> I (in ALD). FT /FTId=VAR_009387. FT VARIANT 638 638 D -> Y (in ALD). FT /FTId=VAR_009388. FT VARIANT 640 640 E -> K (in ALD). FT /FTId=VAR_067245. FT VARIANT 646 646 A -> P (in ALD). FT /FTId=VAR_009389. FT VARIANT 654 654 L -> P (in ALD). FT /FTId=VAR_009390. FT VARIANT 657 657 Missing (in ALD; CALD-type). FT /FTId=VAR_000088. FT VARIANT 660 660 R -> P (in ALD; CALD-type). FT /FTId=VAR_013360. FT VARIANT 660 660 R -> Q (in ALD). FT /FTId=VAR_067329. FT VARIANT 660 660 R -> W (in ALD; CALD, ALMD and AS-types). FT /FTId=VAR_000089. FT VARIANT 667 667 H -> D (in ALD). FT /FTId=VAR_009391. FT VARIANT 668 668 T -> I (in ALD). FT /FTId=VAR_009392. FT VARIANT 677 677 G -> D (in ALD). FT /FTId=VAR_067246. FT VARIANT 679 679 W -> R (in ALD; AMN-type). FT /FTId=VAR_000090. FT VARIANT 693 693 T -> M (in ALD). FT /FTId=VAR_009393. FT CONFLICT 123 123 V -> A (in Ref. 1; CAA79922/CAA83230). SQ SEQUENCE 745 AA; 82937 MW; 82F90905F71FFDC8 CRC64; MPVLSRPRPW RGNTLKRTAV LLALAAYGAH KVYPLVRQCL APARGLQAPA GEPTQEASGV AAAKAGMNRV FLQRLLWLLR LLFPRVLCRE TGLLALHSAA LVSRTFLSVY VARLDGRLAR CIVRKDPRAF GWQLLQWLLI ALPATFVNSA IRYLEGQLAL SFRSRLVAHA YRLYFSQQTY YRVSNMDGRL RNPDQSLTED VVAFAASVAH LYSNLTKPLL DVAVTSYTLL RAARSRGAGT AWPSAIAGLV VFLTANVLRA FSPKFGELVA EEARRKGELR YMHSRVVANS EEIAFYGGHE VELALLQRSY QDLASQINLI LLERLWYVML EQFLMKYVWS ASGLLMVAVP IITATGYSES DAEAVKKAAL EKKEEELVSE RTEAFTIARN LLTAAADAIE RIMSSYKEVT ELAGYTARVH EMFQVFEDVQ RCHFKRPREL EDAQAGSGTI GRSGVRVEGP LKIRGQVVDV EQGIICENIP IVTPSGEVVV ASLNIRVEEG MHLLITGPNG CGKSSLFRIL GGLWPTYGGV LYKPPPQRMF YIPQRPYMSV GSLRDQVIYP DSVEDMQRKG YSEQDLEAIL DVVHLHHILQ REGGWEAMCD WKDVLSGGEK QRIGMARMFY HRPKYALLDE CTSAVSIDVE GKIFQAAKDA GIALLSITHR PSLWKYHTHL LQFDGEGGWK FEKLDSAARL SLTEEKQRLE QQLAGIPKMQ RRLQELCQIL GEAVAPAHVP APSPQGPGGL QGAST // ID ABCF1_HUMAN Reviewed; 845 AA. AC Q8NE71; A2BF75; O14897; Q69YP6; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 2. DT 09-JUL-2014, entry version 119. DE RecName: Full=ATP-binding cassette sub-family F member 1; DE AltName: Full=ATP-binding cassette 50; DE AltName: Full=TNF-alpha-stimulated ABC protein; GN Name=ABCF1; Synonyms=ABC50; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=9790762; DOI=10.1006/geno.1998.5480; RA Richard M., Drouin R., Beaulieu A.D.; RT "ABC50, a novel human ATP-binding cassette protein found in tumor RT necrosis factor-alpha-stimulated synoviocytes."; RL Genomics 53:137-145(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Inoko H.; RT "Genome diversity in HLA: a new strategy for detection of genetic RT polymorphisms in expressed genes within the HLA class III and class I RT regions."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Embryonic stem cell, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-845 (ISOFORM 1). RC TISSUE=Melanoma; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; THR-108; SER-109; RP SER-140 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-573 AND LYS-582. RC TISSUE=Mammary cancer; RX PubMed=17370265; DOI=10.1002/pmic.200600410; RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; RT "Tryptic digestion of ubiquitin standards reveals an improved strategy RT for identifying ubiquitinated proteins by mass spectrometry."; RL Proteomics 7:868-874(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [11] RP INTERACTION WITH EIF2S1, ASSOCIATION WITH RIBOSOMES, PHOSPHORYLATION RP AT SER-109 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY, AND RP MUTAGENESIS OF SER-109 AND SER-140. RX PubMed=17894550; DOI=10.1042/BJ20070811; RA Paytubi S., Morrice N.A., Boudeau J., Proud C.G.; RT "The N-terminal region of ABC50 interacts with eukaryotic initiation RT factor eIF2 and is a target for regulatory phosphorylation by CK2."; RL Biochem. J. 409:223-231(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-228, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by RT enrichment and fractionation of phosphopeptides with strong anion RT exchange chromatography."; RL Proteomics 8:1346-1361(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP FUNCTION, ATP-BINDING, ASSOCIATION WITH RIBOSOMES, MUTAGENESIS OF RP LYS-342; GLN-367; GLY-454; GLU-477; HIS-506; LYS-664; GLN-695; RP GLY-745; GLU-768 AND HIS-797, AND SUBCELLULAR LOCATION. RX PubMed=19570978; DOI=10.1074/jbc.M109.031625; RA Paytubi S., Wang X., Lam Y.W., Izquierdo L., Hunter M.J., Jan E., RA Hundal H.S., Proud C.G.; RT "ABC50 promotes translation initiation in mammalian cells."; RL J. Biol. Chem. 284:24061-24073(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140 RP AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-105; THR-108; RP SER-109; SER-140 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-109; SER-140; RP SER-166 AND SER-228, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). CC -!- FUNCTION: Isoform 2 is required for efficient Cap- and IRES- CC mediated mRNA translation initiation. Isoform 2 is not involved in CC the ribosome biogenesis. CC -!- SUBUNIT: Isoform 2 interacts (via N-terminus) with EIF2S1; the CC interaction is independent of its phosphorylated status. Isoform 2 CC associates (via both ABC transporter domains) with the ribosomes. CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus, nucleoplasm. CC Nucleus envelope. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8NE71-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8NE71-2; Sequence=VSP_012078; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- INDUCTION: By TNF in cultured synoviocytes. CC -!- PTM: Isoform 2 is phosphorylated at phosphoserine and CC phosphothreonine. Isoform 2 phosphorylation on Ser-109 and Ser-140 CC by CK2; inhibits association of EIF2 with ribosomes. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF CC family. EF3 subfamily. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q8NE71"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF027302; AAC70891.1; -; mRNA. DR EMBL; BA000025; BAB63325.1; -; Genomic_DNA. DR EMBL; AB088096; BAC54928.1; -; Genomic_DNA. DR EMBL; AL662800; CAI18158.1; -; Genomic_DNA. DR EMBL; AL662800; CAI18159.1; -; Genomic_DNA. DR EMBL; AL662825; CAI17836.1; -; Genomic_DNA. DR EMBL; AL662825; CAI17837.1; -; Genomic_DNA. DR EMBL; BX000357; CAI18562.1; -; Genomic_DNA. DR EMBL; BX000357; CAI18563.1; -; Genomic_DNA. DR EMBL; BX119957; CAM25907.1; -; Genomic_DNA. DR EMBL; BX248518; CAM25907.1; JOINED; Genomic_DNA. DR EMBL; BX248518; CAM26017.1; -; Genomic_DNA. DR EMBL; BX119957; CAM26017.1; JOINED; Genomic_DNA. DR EMBL; CR753328; CAQ07804.1; -; Genomic_DNA. DR EMBL; CR388372; CAQ07804.1; JOINED; Genomic_DNA. DR EMBL; CR388372; CAQ07873.1; -; Genomic_DNA. DR EMBL; CR753328; CAQ07873.1; JOINED; Genomic_DNA. DR EMBL; BX927220; CAQ09058.1; -; Genomic_DNA. DR EMBL; CR759778; CAQ09401.1; -; Genomic_DNA. DR EMBL; CR847863; CAQ09401.1; JOINED; Genomic_DNA. DR EMBL; CR847863; CAQ10059.1; -; Genomic_DNA. DR EMBL; CR759778; CAQ10059.1; JOINED; Genomic_DNA. DR EMBL; BC034488; AAH34488.1; -; mRNA. DR EMBL; BC112923; AAI12924.1; -; mRNA. DR EMBL; AL832430; CAH10648.1; -; mRNA. DR CCDS; CCDS34380.1; -. [Q8NE71-1] DR CCDS; CCDS34381.1; -. [Q8NE71-2] DR RefSeq; NP_001020262.1; NM_001025091.1. [Q8NE71-1] DR RefSeq; NP_001081.1; NM_001090.2. [Q8NE71-2] DR UniGene; Hs.655285; -. DR ProteinModelPortal; Q8NE71; -. DR SMR; Q8NE71; 301-834. DR BioGrid; 106541; 48. DR IntAct; Q8NE71; 6. DR MINT; MINT-1392646; -. DR STRING; 9606.ENSP00000412553; -. DR PhosphoSite; Q8NE71; -. DR DMDM; 56417894; -. DR MaxQB; Q8NE71; -. DR PaxDb; Q8NE71; -. DR PRIDE; Q8NE71; -. DR DNASU; 23; -. DR Ensembl; ENST00000326195; ENSP00000313603; ENSG00000204574. [Q8NE71-1] DR Ensembl; ENST00000376545; ENSP00000365728; ENSG00000204574. [Q8NE71-2] DR Ensembl; ENST00000383587; ENSP00000373081; ENSG00000206490. [Q8NE71-2] DR Ensembl; ENST00000383588; ENSP00000373082; ENSG00000206490. [Q8NE71-1] DR Ensembl; ENST00000412443; ENSP00000404726; ENSG00000236342. [Q8NE71-2] DR Ensembl; ENST00000419893; ENSP00000389065; ENSG00000232169. [Q8NE71-1] DR Ensembl; ENST00000420257; ENSP00000391102; ENSG00000225989. [Q8NE71-2] DR Ensembl; ENST00000421042; ENSP00000393143; ENSG00000231129. [Q8NE71-2] DR Ensembl; ENST00000423247; ENSP00000411327; ENSG00000225989. [Q8NE71-1] DR Ensembl; ENST00000426219; ENSP00000414373; ENSG00000231129. [Q8NE71-1] DR Ensembl; ENST00000448939; ENSP00000403526; ENSG00000232169. [Q8NE71-2] DR Ensembl; ENST00000452530; ENSP00000389472; ENSG00000236149. [Q8NE71-2] DR Ensembl; ENST00000457078; ENSP00000412553; ENSG00000236342. [Q8NE71-1] DR Ensembl; ENST00000457111; ENSP00000413319; ENSG00000236149. [Q8NE71-1] DR GeneID; 23; -. DR KEGG; hsa:23; -. DR UCSC; uc003nqk.2; human. [Q8NE71-1] DR CTD; 23; -. DR GeneCards; GC06P030539; -. DR GeneCards; GC06Pj30529; -. DR GeneCards; GC06Pk30529; -. DR GeneCards; GC06Pl30583; -. DR GeneCards; GC06Pm30617; -. DR GeneCards; GC06Pn30528; -. DR GeneCards; GC06Po30530; -. DR HGNC; HGNC:70; ABCF1. DR HPA; HPA017578; -. DR MIM; 603429; gene. DR neXtProt; NX_Q8NE71; -. DR PharmGKB; PA24405; -. DR eggNOG; COG0488; -. DR HOGENOM; HOG000271637; -. DR HOVERGEN; HBG050440; -. DR InParanoid; Q8NE71; -. DR KO; K06184; -. DR OMA; FNELVIP; -. DR PhylomeDB; Q8NE71; -. DR TreeFam; TF105207; -. DR ChiTaRS; ABCF1; human. DR GeneWiki; ABCF1; -. DR GenomeRNAi; 23; -. DR NextBio; 69; -. DR PRO; PR:Q8NE71; -. DR ArrayExpress; Q8NE71; -. DR Bgee; Q8NE71; -. DR CleanEx; HS_ABCF1; -. DR Genevestigator; Q8NE71; -. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB. DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB. DR GO; GO:0005840; C:ribosome; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB. DR GO; GO:0008135; F:translation factor activity, nucleic acid binding; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB. DR GO; GO:0006412; P:translation; TAS:ProtInc. DR GO; GO:0006413; P:translational initiation; IMP:UniProtKB. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 3. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 1: Evidence at protein level; KW Activator; Alternative splicing; ATP-binding; Complete proteome; KW Cytoplasm; Isopeptide bond; Nucleotide-binding; Nucleus; KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; KW Ubl conjugation. FT CHAIN 1 845 ATP-binding cassette sub-family F member FT 1. FT /FTId=PRO_0000093318. FT DOMAIN 304 548 ABC transporter 1. FT DOMAIN 625 840 ABC transporter 2. FT NP_BIND 336 343 ATP 1 (By similarity). FT NP_BIND 658 665 ATP 2 (By similarity). FT COMPBIAS 141 243 Glu-rich. FT MOD_RES 22 22 Phosphoserine. FT MOD_RES 24 24 Phosphoserine. FT MOD_RES 105 105 Phosphoserine. FT MOD_RES 108 108 Phosphothreonine. FT MOD_RES 109 109 Phosphoserine; by CK2. FT MOD_RES 140 140 Phosphoserine; by CK2. FT MOD_RES 166 166 Phosphoserine. FT MOD_RES 228 228 Phosphoserine. FT MOD_RES 595 595 Phosphoserine. FT CROSSLNK 573 573 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 582 582 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT VAR_SEQ 226 263 Missing (in isoform 2). FT /FTId=VSP_012078. FT VARIANT 198 198 N -> D (in dbSNP:rs6902544). FT /FTId=VAR_048136. FT MUTAGEN 109 109 S->A: Reduces phosphorylation. Inhibits FT strongly phosphorylation by CK2; when FT associated with S-140. Does not inhibit FT interaction with EIF2; when associated FT with S-140. Does not inhibit association FT with ribosomes; when associated with S- FT 140. Reduces EIF2 interaction with FT ribosomes; when associated with S-140. FT Does not inhibit protein synthesis; when FT associated with A-140. FT MUTAGEN 140 140 S->A: Reduces phosphorylation. Inhibits FT strongly phosphorylation by CK2; when FT associated with S-109. Does not inhibits FT interaction with EIF2; when associated FT with S-109. Does not inhibit association FT with ribosomes; when associated with S- FT 109. Reduces EIF2 interaction with FT ribosomes; when associated with S-109. FT Does not inhibit protein synthesis; when FT associated with A-109. FT MUTAGEN 342 342 K->M: Does not inhibit ribosome binding. FT Reduces ATP-binding. Inhibits ATP-binding FT and reduces protein synthesis; when FT associated with M-664. Shows an enhanced FT association with polyribosomes; when FT associated with M-664. Does not inhibit FT IRES-mediated protein synthesis; when FT associated with M-664. FT MUTAGEN 367 367 Q->E: Does not inhibit ribosome binding. FT MUTAGEN 454 454 G->D: Does not inhibit ribosome binding. FT MUTAGEN 477 477 E->Q: Does not inhibit ribosome binding. FT Reduces protein synthesis; when FT associated with Q-768. FT MUTAGEN 506 506 H->L: Does not inhibit ribosome binding. FT MUTAGEN 664 664 K->M: Does not inhibit ribosome binding. FT Reduces ATP-binding. Inhibits ATP-binding FT and reduces protein synthesis; when FT associated with M-342. Shows a reduced FT association with polyribosomes; when FT associated with M-664. Does not inhibit FT IRES-mediated protein synthesis; when FT associated with M-664. FT MUTAGEN 695 695 Q->E: Does not inhibit ribosome binding. FT MUTAGEN 745 745 G->D: Does not inhibit ribosome binding. FT MUTAGEN 768 768 E->Q: Does not inhibit ribosome binding. FT Reduces protein synthesis; when FT associated with Q-477. FT MUTAGEN 797 797 H->L: Does not inhibit ribosome binding. FT CONFLICT 166 166 S -> P (in Ref. 5; AAH34488). SQ SEQUENCE 845 AA; 95926 MW; 5C5AA662DF4C99E4 CRC64; MPKAPKQQPP EPEWIGDGES TSPSDKVVKK GKKDKKIKKT FFEELAVEDK QAGEEEKVLK EKEQQQQQQQ QQQKKKRDTR KGRRKKDVDD DGEEKELMER LKKLSVPTSD EEDEVPAPKP RGGKKTKGGN VFAALIQDQS EEEEEEEKHP PKPAKPEKNR INKAVSEEQQ PALKGKKGKE EKSKGKAKPQ NKFAALDNEE EDKEEEIIKE KEPPKQGKEK AKKAEQGSEE EGEGEEEEEE GGESKADDPY AHLSKKEKKK LKKQMEYERQ VASLKAANAA ENDFSVSQAE MSSRQAMLEN ASDIKLEKFS ISAHGKELFV NADLYIVAGR RYGLVGPNGK GKTTLLKHIA NRALSIPPNI DVLLCEQEVV ADETPAVQAV LRADTKRLKL LEEERRLQGQ LEQGDDTAAE RLEKVYEELR ATGAAAAEAK ARRILAGLGF DPEMQNRPTQ KFSGGWRMRV SLARALFMEP TLLMLDEPTN HLDLNAVIWL NNYLQGWRKT LLIVSHDQGF LDDVCTDIIH LDAQRLHYYR GNYMTFKKMY QQKQKELLKQ YEKQEKKLKE LKAGGKSTKQ AEKQTKEALT RKQQKCRRKN QDEESQEAPE LLKRPKEYTV RFTFPDPPPL SPPVLGLHGV TFGYQGQKPL FKNLDFGIDM DSRICIVGPN GVGKSTLLLL LTGKLTPTHG EMRKNHRLKI GFFNQQYAEQ LRMEETPTEY LQRGFNLPYQ DARKCLGRFG LESHAHTIQI CKLSGGQKAR VVFAELACRE PDVLILDEPT NNLDIESIDA LGEAINEYKG AVIVVSHDAR LITETNCQLW VVEEQSVSQI DGDFEDYKRE VLEALGEVMV SRPRE // ID ABCD3_HUMAN Reviewed; 659 AA. AC P28288; D3DT46; Q15271; Q6NUN5; Q96DA3; Q9H529; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 09-JUL-2014, entry version 151. DE RecName: Full=ATP-binding cassette sub-family D member 3; DE AltName: Full=70 kDa peroxisomal membrane protein; DE Short=PMP70; GN Name=ABCD3; Synonyms=PMP70, PXMP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-17. RC TISSUE=Liver; RX PubMed=1301993; DOI=10.1038/ng0492-16; RA Gaertner J., Moser H., Valle D.; RT "Mutations in the 70K peroxisomal membrane protein gene in Zellweger RT syndrome."; RL Nat. Genet. 1:16-23(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=1536884; DOI=10.1016/0167-4781(92)90510-7; RA Kamijo K., Kamijo T., Ueno I., Osumi T., Hashimoto T.; RT "Nucleotide sequence of the human 70 kDa peroxisomal membrane protein: RT a member of ATP-binding cassette transporters."; RL Biochim. Biophys. Acta 1129:323-327(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9521874; DOI=10.1006/geno.1997.5177; RA Gaertner J., Jimenez-Sanchez G., Roerig P., Valle D.; RT "Genomic organization of the 70-kDa peroxisomal membrane protein gene RT (PXMP1)."; RL Genomics 48:203-208(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Brain, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP SUBUNIT. RX PubMed=10551832; DOI=10.1074/jbc.274.46.32738; RA Liu L.X., Janvier K., Berteaux-Lecellier V., Cartier N., Benarous R., RA Aubourg P.; RT "Homo- and heterodimerization of peroxisomal ATP-binding cassette RT half-transporters."; RL J. Biol. Chem. 274:32738-32743(1999). RN [9] RP INTERACTION WITH PEX19. RC TISSUE=Brain; RX PubMed=10777694; DOI=10.1006/bbrc.2000.2572; RA Gloeckner C.J., Mayerhofer P.U., Landgraf P., Muntau A.C., RA Holzinger A., Gerber J.-K., Kammerer S., Adamski J., Roscher A.A.; RT "Human adrenoleukodystrophy protein and related peroxisomal ABC RT transporters interact with the peroxisomal assembly protein PEX19p."; RL Biochem. Biophys. Res. Commun. 271:144-150(2000). RN [10] RP SUBCELLULAR LOCATION, AND INTERACTION WITH PEX19. RX PubMed=10704444; DOI=10.1083/jcb.148.5.931; RA Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.; RT "PEX19 binds multiple peroxisomal membrane proteins, is predominantly RT cytoplasmic, and is required for peroxisome membrane synthesis."; RL J. Cell Biol. 148:931-944(2000). RN [11] RP FUNCTION, AND MUTAGENESIS OF GLY-478 AND SER-572. RX PubMed=11248239; DOI=10.1016/S0014-5793(01)02235-9; RA Roerig P., Mayerhofer P., Holzinger A., Gaertner J.; RT "Characterization and functional analysis of the nucleotide binding RT fold in human peroxisomal ATP binding cassette transporters."; RL FEBS Lett. 492:66-72(2001). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-260 AND LYS-399, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Probable transporter. The nucleotide-binding fold acts CC as an ATP-binding subunit with ATPase activity. CC -!- SUBUNIT: Can form heterodimers with ABCD1/ALD and ABCD2/ALDR. CC Dimerization is necessary to form an active transporter. Interacts CC with PEX19. CC -!- INTERACTION: CC P33897:ABCD1; NbExp=2; IntAct=EBI-80992, EBI-81045; CC P40855:PEX19; NbExp=4; IntAct=EBI-80992, EBI-594747; CC -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P28288-1; Sequence=Displayed; CC Name=2; CC IsoId=P28288-2; Sequence=VSP_031189; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=P28288-3; Sequence=VSP_031187, VSP_031188; CC -!- MISCELLANEOUS: Mutation in ABCD3 have been found in two CC individuals affected by Zellweger syndrome. However, the role of CC ABCD3 in the causation of Zellweger syndrome remains uncertain. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD CC family. Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) CC subfamily. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P28288"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M81182; AAA60128.1; -; mRNA. DR EMBL; X58528; CAA41416.1; -; mRNA. DR EMBL; X83467; CAA58470.1; -; Genomic_DNA. DR EMBL; X83468; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83469; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83470; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83471; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83472; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83473; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83474; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83475; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83476; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83477; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83478; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83479; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83480; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83481; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83482; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83483; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83484; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83485; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83486; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83487; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83488; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; X83489; CAA58470.1; JOINED; Genomic_DNA. DR EMBL; BT006644; AAP35290.1; -; mRNA. DR EMBL; AL138758; CAC15960.2; -; Genomic_DNA. DR EMBL; AC093117; CAC15960.2; JOINED; Genomic_DNA. DR EMBL; AC118469; CAC15960.2; JOINED; Genomic_DNA. DR EMBL; CH471097; EAW73049.1; -; Genomic_DNA. DR EMBL; CH471097; EAW73050.1; -; Genomic_DNA. DR EMBL; CH471097; EAW73047.1; -; Genomic_DNA. DR EMBL; CH471097; EAW73048.1; -; Genomic_DNA. DR EMBL; BC009712; AAH09712.1; -; mRNA. DR EMBL; BC068509; AAH68509.1; -; mRNA. DR CCDS; CCDS44175.1; -. [P28288-3] DR CCDS; CCDS749.1; -. [P28288-1] DR PIR; S20313; S20313. DR RefSeq; NP_001116146.1; NM_001122674.1. [P28288-3] DR RefSeq; NP_002849.1; NM_002858.3. [P28288-1] DR UniGene; Hs.700576; -. DR ProteinModelPortal; P28288; -. DR SMR; P28288; 427-640. DR BioGrid; 111783; 41. DR IntAct; P28288; 12. DR MINT; MINT-3010926; -. DR STRING; 9606.ENSP00000359233; -. DR TCDB; 3.A.1.203.1; the atp-binding cassette (abc) superfamily. DR PhosphoSite; P28288; -. DR DMDM; 130358; -. DR MaxQB; P28288; -. DR PaxDb; P28288; -. DR PeptideAtlas; P28288; -. DR PRIDE; P28288; -. DR DNASU; 5825; -. DR Ensembl; ENST00000315713; ENSP00000326880; ENSG00000117528. [P28288-3] DR Ensembl; ENST00000370214; ENSP00000359233; ENSG00000117528. [P28288-1] DR Ensembl; ENST00000394233; ENSP00000377780; ENSG00000117528. [P28288-2] DR GeneID; 5825; -. DR KEGG; hsa:5825; -. DR UCSC; uc001dqm.4; human. [P28288-3] DR UCSC; uc001dqn.4; human. [P28288-1] DR UCSC; uc009wdr.3; human. [P28288-2] DR CTD; 5825; -. DR GeneCards; GC01P094883; -. DR HGNC; HGNC:67; ABCD3. DR HPA; HPA032026; -. DR HPA; HPA032027; -. DR MIM; 170995; gene. DR neXtProt; NX_P28288; -. DR PharmGKB; PA24402; -. DR eggNOG; COG4178; -. DR HOGENOM; HOG000206081; -. DR HOVERGEN; HBG050438; -. DR InParanoid; P28288; -. DR KO; K05677; -. DR OrthoDB; EOG70ZZMP; -. DR PhylomeDB; P28288; -. DR TreeFam; TF105205; -. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR ChiTaRS; ABCD3; human. DR GeneWiki; ABCD3; -. DR GenomeRNAi; 5825; -. DR NextBio; 22689; -. DR PRO; PR:P28288; -. DR ArrayExpress; P28288; -. DR Bgee; P28288; -. DR CleanEx; HS_ABCD3; -. DR Genevestigator; P28288; -. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl. DR GO; GO:0005782; C:peroxisomal matrix; IDA:UniProtKB. DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0016887; F:ATPase activity; IDA:UniProtKB. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0006200; P:ATP catabolic process; IDA:GOC. DR GO; GO:0006635; P:fatty acid beta-oxidation; IGI:UniProtKB. DR GO; GO:0007031; P:peroxisome organization; IDA:UniProtKB. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IGI:UniProtKB. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR010509; ABC_Peroxi_TM. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR005283; FA_transporter. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF06472; ABC_membrane_2; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR TIGRFAMs; TIGR00954; 3a01203; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Complete proteome; KW Glycoprotein; Membrane; Nucleotide-binding; Peroxisome; KW Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 659 ATP-binding cassette sub-family D member FT 3. FT /FTId=PRO_0000093309. FT TRANSMEM 84 104 Helical; (Potential). FT TRANSMEM 126 146 Helical; (Potential). FT TRANSMEM 224 244 Helical; (Potential). FT TRANSMEM 313 333 Helical; (Potential). FT DOMAIN 85 372 ABC transmembrane type-1. FT DOMAIN 440 659 ABC transporter. FT NP_BIND 473 480 ATP (Potential). FT REGION 2 199 Interaction with PEX19. FT REGION 2 124 Targeting to peroxisomes. FT MOD_RES 61 61 N6-acetyllysine (By similarity). FT MOD_RES 260 260 N6-acetyllysine. FT MOD_RES 399 399 N6-acetyllysine. FT MOD_RES 533 533 N6-acetyllysine (By similarity). FT MOD_RES 659 659 Phosphoserine (By similarity). FT CARBOHYD 12 12 N-linked (GlcNAc...) (Potential). FT CARBOHYD 106 106 N-linked (GlcNAc...) (Potential). FT CARBOHYD 206 206 N-linked (GlcNAc...) (Potential). FT VAR_SEQ 229 236 GPASMMAY -> VLGKILWH (in isoform 3). FT /FTId=VSP_031187. FT VAR_SEQ 237 659 Missing (in isoform 3). FT /FTId=VSP_031188. FT VAR_SEQ 277 386 Missing (in isoform 2). FT /FTId=VSP_031189. FT VARIANT 17 17 G -> D (in a patient with Zellweger FT syndrome). FT /FTId=VAR_000091. FT MUTAGEN 478 478 G->R: Decreased ATP-binding affinity. FT MUTAGEN 572 572 S->I: Decreased ATPase activity. FT CONFLICT 175 175 M -> K (in Ref. 2; CAA41416). FT CONFLICT 191 192 QD -> LV (in Ref. 3; CAA58470). FT CONFLICT 336 336 P -> L (in Ref. 3; CAA58470). FT CONFLICT 503 503 G -> R (in Ref. 2; CAA41416). FT CONFLICT 542 542 L -> Q (in Ref. 2; CAA41416). FT CONFLICT 616 634 VGITLFTVSHRKSLWKHHE -> GWHHSLHLCLIGNLFGNI FT MR (in Ref. 3; CAA58470). SQ SEQUENCE 659 AA; 75476 MW; 2CA976FEB6EB6217 CRC64; MAAFSKYLTA RNSSLAGAAF LLLCLLHKRR RALGLHGKKS GKPPLQNNEK EGKKERAVVD KVFFSRLIQI LKIMVPRTFC KETGYLVLIA VMLVSRTYCD VWMIQNGTLI ESGIIGRSRK DFKRYLLNFI AAMPLISLVN NFLKYGLNEL KLCFRVRLTK YLYEEYLQAF TYYKMGNLDN RIANPDQLLT QDVEKFCNSV VDLYSNLSKP FLDIVLYIFK LTSAIGAQGP ASMMAYLVVS GLFLTRLRRP IGKMTITEQK YEGEYRYVNS RLITNSEEIA FYNGNKREKQ TVHSVFRKLV EHLHNFILFR FSMGFIDSII AKYLATVVGY LVVSRPFLDL SHPRHLKSTH SELLEDYYQS GRMLLRMSQA LGRIVLAGRE MTRLAGFTAR ITELMQVLKD LNHGKYERTM VSQQEKGIEG VQVIPLIPGA GEIIIADNII KFDHVPLATP NGDVLIRDLN FEVRSGANVL ICGPNGCGKS SLFRVLGELW PLFGGRLTKP ERGKLFYVPQ RPYMTLGTLR DQVIYPDGRE DQKRKGISDL VLKEYLDNVQ LGHILEREGG WDSVQDWMDV LSGGEKQRMA MARLFYHKPQ FAILDECTSA VSVDVEGYIY SHCRKVGITL FTVSHRKSLW KHHEYYLHMD GRGNYEFKQI TEDTVEFGS // ID ABCG1_HUMAN Reviewed; 678 AA. AC P45844; Q86SU8; Q96L76; Q9BXK6; Q9BXK7; Q9BXK8; Q9BXK9; Q9BXL0; AC Q9BXL1; Q9BXL2; Q9BXL3; Q9BXL4; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 3. DT 09-JUL-2014, entry version 154. DE RecName: Full=ATP-binding cassette sub-family G member 1; DE AltName: Full=ATP-binding cassette transporter 8; DE AltName: Full=White protein homolog; GN Name=ABCG1; Synonyms=ABC8, WHT1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-678 (ISOFORMS 1 AND 4). RC TISSUE=Retina; RX PubMed=8659545; RA Chen H.M., Rossier C., Lalioti M.D., Lynn A., Chakravarti A., RA Perrin G., Antonarakis S.E.; RT "Cloning of the cDNA for a human homologue of the Drosophila white RT gene and mapping to chromosome 21q22.3."; RL Am. J. Hum. Genet. 59:66-75(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=10950923; DOI=10.1006/geno.2000.6253; RA Berry A., Scott H.S., Kudoh J., Talior I., Korostishevsky M., RA Wattenhofer M., Guipponi M., Barras C., Rossier C., Shibuya K., RA Wang J., Kawasaki K., Asakawa S., Minoshima S., Shimizu N., RA Antonarakis S.E., Bonne-Tamir B.; RT "Refined localization of autosomal recessive nonsyndromic deafness RT DFNB10 locus using 34 novel microsatellite markers, genomic structure, RT and exclusion of six known genes in the region."; RL Genomics 68:22-29(2000). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND REPRESSION BY RP ZNF202. RX PubMed=11279031; DOI=10.1074/jbc.M100218200; RA Porsch-Oezcueruemez M., Langmann T., Heimerl S., Borsukova H., RA Kaminski W.E., Drobnik W., Honer C., Schumacher C., Schmitz G.; RT "The zinc finger protein 202 (ZNF202) is a transcriptional repressor RT of ATP binding cassette transporter A1 (ABCA1) and ABCG1 gene RT expression and a modulator of cellular lipid efflux."; RL J. Biol. Chem. 276:12427-12433(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2; 3; 4; 5; 6 AND RP 7). RX PubMed=11162488; DOI=10.1006/bbrc.2000.4089; RA Lorkowski S., Rust S., Engel T., Jung E., Tegelkamp K., Galinski E.A., RA Assmann G., Cullen P.; RT "Genomic sequence and structure of the human ABCG1 (ABC8) gene."; RL Biochem. Biophys. Res. Commun. 280:121-131(2001). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), AND VARIANT LEU-668. RX PubMed=11500512; DOI=10.1074/jbc.M105863200; RA Kennedy M.A., Venkateswaran A., Tarr P.T., Xenarios I., Kudoh J., RA Shimizu N., Edwards P.A.; RT "Characterization of the human ABCG1 gene: liver X receptor activates RT an internal promoter that produces a novel transcript encoding an RT alternative form of the protein."; RL J. Biol. Chem. 276:39438-39447(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1). RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., RA Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-678. RC TISSUE=Fetal brain; RX PubMed=9034316; DOI=10.1016/S0378-1119(96)00633-6; RA Croop J.M., Tiller G.E., Fletcher J.A., Lux M.L., Raab E., RA Goldenson D., Son D., Arciniegas S., Wu R.; RT "Isolation and characterization of a mammalian homolog of the RT Drosophila white gene."; RL Gene 185:77-85(1997). RN [9] RP INDUCTION, AND PROBABLE FUNCTION. RX PubMed=10799558; DOI=10.1074/jbc.275.19.14700; RA Venkateswaran A., Repa J.J., Lobaccaro J.-M.A., Bronson A., RA Mangelsdorf D.J., Edwards P.A.; RT "Human white/murine ABC8 mRNA levels are highly induced in lipid- RT loaded macrophages. A transcriptional role for specific oxysterols."; RL J. Biol. Chem. 275:14700-14707(2000). RN [10] RP INDUCTION, AND PROBABLE FUNCTION. RX PubMed=10639163; DOI=10.1073/pnas.97.2.817; RA Klucken J., Buechler C., Orso E., Kaminski W.E., RA Porsch-Oezcueruemez M., Liebisch G., Kapinsky M., Diederich W., RA Drobnik W., Dean M., Allikmets R., Schmitz G.; RT "ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a RT regulator of macrophage cholesterol and phospholipid transport."; RL Proc. Natl. Acad. Sci. U.S.A. 97:817-822(2000). RN [11] RP INDUCTION. RX PubMed=12032171; RA Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.; RT "Bacterial lipopolysaccharide induces expression of ABCA1 but not RT ABCG1 via an LXR-independent pathway."; RL J. Lipid Res. 43:952-959(2002). RN [12] RP REVIEW. RX PubMed=11590207; RA Schmitz G., Langmann T., Heimerl S.; RT "Role of ABCG1 and other ABCG family members in lipid metabolism."; RL J. Lipid Res. 42:1513-1520(2001). RN [13] RP TISSUE SPECIFICITY. RX PubMed=11350058; DOI=10.1006/bbrc.2001.4863; RA Lorkowski S., Kratz M., Wenner C., Schmidt R., Weitkamp B., Fobker M., RA Reinhardt J., Rauterberg J., Galinski E.A., Cullen P.; RT "Expression of the ATP-binding cassette transporter gene ABCG1 (ABC8) RT in Tangier disease."; RL Biochem. Biophys. Res. Commun. 283:821-830(2001). RN [14] RP SUBCELLULAR LOCATION, AND MISCELLANEOUS. RX PubMed=22042635; DOI=10.1074/mcp.M111.013458; RA Uhlen M., Oksvold P., Algenas C., Hamsten C., Fagerberg L., RA Klevebring D., Lundberg E., Odeberg J., Ponten F., Kondo T., RA Sivertsson A.; RT "Antibody-based protein profiling of the human chromosome 21."; RL Mol. Cell. Proteomics 11:0-0(2012). RN [15] RP PALMITOYLATION AT CYS-30; CYS-154; CYS-315; CYS-394 AND CYS-406, AND RP MUTAGENESIS OF CYS-30; CYS-154; CYS-315; CYS-394 AND CYS-406. RX PubMed=23388354; DOI=10.1016/j.bbalip.2013.01.019; RA Gu H.M., Li G., Gao X., Berthiaume L.G., Zhang D.W.; RT "Characterization of palmitoylation of ATP binding cassette RT transporter G1: Effect on protein trafficking and function."; RL Biochim. Biophys. Acta 1831:1067-1078(2013). CC -!- FUNCTION: Transporter involved in macrophage lipid homeostasis. Is CC an active component of the macrophage lipid export complex. Could CC also be involved in intracellular lipid transport processes. The CC role in cellular lipid homeostasis may not be limited to CC macrophages. CC -!- SUBUNIT: May form heterodimers with several heterologous partners CC of the ABCG subfamily. CC -!- INTERACTION: CC Q9H172:ABCG4; NbExp=2; IntAct=EBI-8584087, EBI-8584118; CC -!- SUBCELLULAR LOCATION: Mitochondrion. Endoplasmic reticulum CC membrane; Multi-pass membrane protein. Golgi apparatus membrane; CC Multi-pass membrane protein. Note=Predominantly localized in the CC intracellular compartments mainly associated with the endoplasmic CC reticulum (ER) and Golgi membranes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Comment=Additional isoforms seem to exist; CC Name=1; CC IsoId=P45844-1; Sequence=Displayed; CC Name=2; Synonyms=J; CC IsoId=P45844-2; Sequence=VSP_000047, VSP_000051; CC Name=3; Synonyms=ABDE; CC IsoId=P45844-3; Sequence=VSP_000048, VSP_000051; CC Name=4; Synonyms=G; CC IsoId=P45844-4; Sequence=VSP_000051; CC Name=5; Synonyms=F; CC IsoId=P45844-5; Sequence=VSP_000049, VSP_000051; CC Name=6; Synonyms=HI; CC IsoId=P45844-6; Sequence=VSP_000046, VSP_000051; CC Name=7; Synonyms=C; CC IsoId=P45844-7; Sequence=VSP_000050, VSP_000051; CC Name=8; CC IsoId=P45844-8; Sequence=VSP_010718; CC -!- TISSUE SPECIFICITY: Expressed in several tissues. Expressed in CC macrophages; expression is increased in macrophages from patients CC with Tangier disease. CC -!- INDUCTION: Strongly induced in monocyte-derived macrophages during CC cholesterol influx. Conversely, mRNA and protein expression are CC suppressed by lipid efflux. Induction is mediated by the liver X CC receptor/retinoid X receptor (LXR/RXR) pathway. Not induced by CC bacterial lipopolysaccharides (LPS). Repressed by ZNF202. CC -!- PTM: Palmitoylation at Cys-315 seems important for trafficking CC from the endoplasmic reticulum. CC -!- MISCELLANEOUS: A protein of the expected size has been detected by CC antibody binding and Western blot in at least one of the analyzed CC tissues or cells (PubMed:22042635). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG CC family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-2 domain. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAC51098.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=AAK28841.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAA95530.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=BAB13728.2; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=CAA62631.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC Sequence=CAC00730.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=P45844"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X91249; CAA62631.1; ALT_INIT; mRNA. DR EMBL; AB038161; BAB13728.2; ALT_INIT; Genomic_DNA. DR EMBL; AJ289137; CAC00730.1; ALT_INIT; Genomic_DNA. DR EMBL; AJ289138; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289139; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289140; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289141; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289142; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289143; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289144; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289145; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289146; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289147; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289148; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289149; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289150; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AJ289151; CAC00730.1; JOINED; Genomic_DNA. DR EMBL; AF323658; AAK28836.1; -; Genomic_DNA. DR EMBL; AF323644; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323645; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28836.1; JOINED; Genomic_DNA. DR EMBL; AF323664; AAK28842.1; -; mRNA. DR EMBL; AF323658; AAK28833.1; -; Genomic_DNA. DR EMBL; AF323640; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323645; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28833.1; JOINED; Genomic_DNA. DR EMBL; AF323660; AAK28838.1; -; mRNA. DR EMBL; AF323663; AAK28841.1; ALT_INIT; mRNA. DR EMBL; AF323658; AAK28835.1; -; Genomic_DNA. DR EMBL; AF323642; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323645; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28835.1; JOINED; Genomic_DNA. DR EMBL; AF323662; AAK28840.1; -; mRNA. DR EMBL; AF323658; AAK28837.1; -; Genomic_DNA. DR EMBL; AF323643; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323645; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28837.1; JOINED; Genomic_DNA. DR EMBL; AF323658; AAK28834.1; -; Genomic_DNA. DR EMBL; AF323645; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323646; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323647; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323648; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323649; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323650; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323651; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323652; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323653; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323654; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323655; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323656; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323657; AAK28834.1; JOINED; Genomic_DNA. DR EMBL; AF323661; AAK28839.1; -; mRNA. DR EMBL; AY048757; AAL06598.1; -; mRNA. DR EMBL; AP001746; BAA95530.1; ALT_INIT; Genomic_DNA. DR EMBL; BC029158; AAH29158.2; -; mRNA. DR EMBL; U34919; AAC51098.1; ALT_INIT; mRNA. DR CCDS; CCDS13681.1; -. [P45844-5] DR CCDS; CCDS13682.1; -. [P45844-1] DR CCDS; CCDS13683.1; -. [P45844-2] DR CCDS; CCDS42937.1; -. [P45844-3] DR CCDS; CCDS42938.1; -. [P45844-4] DR RefSeq; NP_004906.3; NM_004915.3. [P45844-1] DR RefSeq; NP_058198.2; NM_016818.2. [P45844-4] DR RefSeq; NP_997057.1; NM_207174.1. [P45844-2] DR RefSeq; NP_997510.1; NM_207627.1. [P45844-3] DR RefSeq; NP_997511.1; NM_207628.1. [P45844-7] DR RefSeq; NP_997512.1; NM_207629.1. [P45844-5] DR UniGene; Hs.124649; -. DR UniGene; Hs.418279; -. DR ProteinModelPortal; P45844; -. DR SMR; P45844; 9-323. DR BioGrid; 114980; 2. DR IntAct; P45844; 2. DR DrugBank; DB00171; Adenosine triphosphate. DR TCDB; 3.A.1.204.12; the atp-binding cassette (abc) superfamily. DR PhosphoSite; P45844; -. DR DMDM; 17433715; -. DR MaxQB; P45844; -. DR PaxDb; P45844; -. DR PRIDE; P45844; -. DR DNASU; 9619; -. DR Ensembl; ENST00000343687; ENSP00000339744; ENSG00000160179. [P45844-2] DR Ensembl; ENST00000347800; ENSP00000291524; ENSG00000160179. [P45844-5] DR Ensembl; ENST00000361802; ENSP00000354995; ENSG00000160179. [P45844-1] DR Ensembl; ENST00000398449; ENSP00000381467; ENSG00000160179. [P45844-4] DR Ensembl; ENST00000398457; ENSP00000381475; ENSG00000160179. [P45844-3] DR GeneID; 9619; -. DR KEGG; hsa:9619; -. DR UCSC; uc002zam.3; human. [P45844-7] DR UCSC; uc002zan.3; human. [P45844-3] DR UCSC; uc002zao.3; human. [P45844-5] DR UCSC; uc002zap.3; human. [P45844-4] DR UCSC; uc002zaq.3; human. [P45844-1] DR UCSC; uc002zar.3; human. [P45844-2] DR CTD; 9619; -. DR GeneCards; GC21P043619; -. DR HGNC; HGNC:73; ABCG1. DR HPA; HPA031470; -. DR HPA; HPA031471; -. DR MIM; 603076; gene. DR neXtProt; NX_P45844; -. DR PharmGKB; PA24408; -. DR eggNOG; COG1131; -. DR HOVERGEN; HBG103052; -. DR KO; K05679; -. DR OMA; RERICDT; -. DR OrthoDB; EOG7KWSGT; -. DR PhylomeDB; P45844; -. DR TreeFam; TF105210; -. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR ChiTaRS; ABCG1; human. DR GeneWiki; ABCG1; -. DR GenomeRNAi; 9619; -. DR NextBio; 36087; -. DR PRO; PR:P45844; -. DR ArrayExpress; P45844; -. DR Bgee; P45844; -. DR Genevestigator; P45844; -. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005768; C:endosome; ISS:BHF-UCL. DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0055037; C:recycling endosome; ISS:BHF-UCL. DR GO; GO:0043531; F:ADP binding; IDA:BHF-UCL. DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL. DR GO; GO:0015485; F:cholesterol binding; IC:BHF-UCL. DR GO; GO:0017127; F:cholesterol transporter activity; IDA:BHF-UCL. DR GO; GO:0034437; F:glycoprotein transporter activity; IDA:BHF-UCL. DR GO; GO:0005543; F:phospholipid binding; IC:BHF-UCL. DR GO; GO:0005548; F:phospholipid transporter activity; IDA:BHF-UCL. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0046983; F:protein dimerization activity; NAS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0034041; F:sterol-transporting ATPase activity; IDA:BHF-UCL. DR GO; GO:0019534; F:toxin transporter activity; IDA:BHF-UCL. DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IDA:BHF-UCL. DR GO; GO:0033344; P:cholesterol efflux; IDA:BHF-UCL. DR GO; GO:0042632; P:cholesterol homeostasis; IDA:BHF-UCL. DR GO; GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL. DR GO; GO:0009720; P:detection of hormone stimulus; NAS:UniProtKB. DR GO; GO:0034436; P:glycoprotein transport; IDA:BHF-UCL. DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; ISS:BHF-UCL. DR GO; GO:0032367; P:intracellular cholesterol transport; IMP:BHF-UCL. DR GO; GO:0042157; P:lipoprotein metabolic process; TAS:Reactome. DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISS:BHF-UCL. DR GO; GO:0010887; P:negative regulation of cholesterol storage; TAS:BHF-UCL. DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; TAS:BHF-UCL. DR GO; GO:0033700; P:phospholipid efflux; IMP:BHF-UCL. DR GO; GO:0055091; P:phospholipid homeostasis; IMP:BHF-UCL. DR GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; ISS:BHF-UCL. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl. DR GO; GO:0010872; P:regulation of cholesterol esterification; ISS:BHF-UCL. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:BHF-UCL. DR GO; GO:0055099; P:response to high density lipoprotein particle; IEA:Ensembl. DR GO; GO:0033993; P:response to lipid; IDA:BHF-UCL. DR GO; GO:0010033; P:response to organic substance; IDA:UniProtKB. DR GO; GO:0043691; P:reverse cholesterol transport; ISS:BHF-UCL. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:1901998; P:toxin transport; IDA:GOC. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013525; ABC_2_trans. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR020064; ABCG1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005284; Pigment_permease. DR PANTHER; PTHR19241:SF177; PTHR19241:SF177; 1. DR Pfam; PF01061; ABC2_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00955; 3a01204; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Complete proteome; KW Endoplasmic reticulum; Golgi apparatus; Lipid transport; Lipoprotein; KW Membrane; Mitochondrion; Nucleotide-binding; Palmitate; Polymorphism; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 678 ATP-binding cassette sub-family G member FT 1. FT /FTId=PRO_0000093384. FT TOPO_DOM 1 426 Cytoplasmic (Potential). FT TRANSMEM 427 445 Helical; (Potential). FT TOPO_DOM 446 456 Extracellular (Potential). FT TRANSMEM 457 477 Helical; (Potential). FT TOPO_DOM 478 506 Cytoplasmic (Potential). FT TRANSMEM 507 525 Helical; (Potential). FT TOPO_DOM 526 533 Extracellular (Potential). FT TRANSMEM 534 555 Helical; (Potential). FT TOPO_DOM 556 567 Cytoplasmic (Potential). FT TRANSMEM 568 586 Helical; (Potential). FT TOPO_DOM 587 649 Extracellular (Potential). FT TRANSMEM 650 669 Helical; (Potential). FT TOPO_DOM 670 678 Cytoplasmic (Potential). FT DOMAIN 77 317 ABC transporter. FT DOMAIN 415 673 ABC transmembrane type-2. FT NP_BIND 118 125 ATP (Potential). FT LIPID 30 30 S-palmitoyl cysteine. FT LIPID 154 154 S-palmitoyl cysteine. FT LIPID 315 315 S-palmitoyl cysteine. FT LIPID 394 394 S-palmitoyl cysteine. FT LIPID 406 406 S-palmitoyl cysteine. FT VAR_SEQ 1 95 MACLMAAFSVGTAMNASSYSAEMTEPKSVCVSVDEVVSSNM FT EATETDLLNGHLKKVDNNLTEAQRFSSLPRRAAVNIEFRDL FT SYSVPEGPWWRKK -> MVRRGWSVCTAILLARLWCLVPTH FT TFLSEYPEAAEYPHPGWVYWLQMAVAPGHLRAWVMRNNVTT FT NIPSAFSGTLTHEEKAVLTVFTGTATAVHVQVAALASAKLE FT SSVFVTDCVSCKIENVCDSALQGKRVPMSGLQGSSIVIMPP FT SNRPLASAASCTWSVQVQGGPHHLGVVAISGKVLSAAHGAG FT RAYGWGFPGDPMEE (in isoform 8). FT /FTId=VSP_010718. FT VAR_SEQ 1 22 Missing (in isoform 7). FT /FTId=VSP_000050. FT VAR_SEQ 1 14 MACLMAAFSVGTAM -> MRISLPRAPERDGGVSASSLLDT FT VT (in isoform 2). FT /FTId=VSP_000047. FT VAR_SEQ 1 14 MACLMAAFSVGTAM -> MLGTQGWTKQRKPCPQ (in FT isoform 3). FT /FTId=VSP_000048. FT VAR_SEQ 1 14 MACLMAAFSVGTAM -> MIMRLPQPHGT (in isoform FT 5). FT /FTId=VSP_000049. FT VAR_SEQ 1 4 Missing (in isoform 6). FT /FTId=VSP_000046. FT VAR_SEQ 375 386 Missing (in isoform 2, isoform 3, isoform FT 4, isoform 5, isoform 6 and isoform 7). FT /FTId=VSP_000051. FT VARIANT 668 668 F -> L. FT /FTId=VAR_012279. FT MUTAGEN 30 30 C->A: No significant effect. FT MUTAGEN 154 154 C->A: No significant effect. FT MUTAGEN 315 315 C->A,S: Significantly decreases ABCG1- FT mediated cholesterol efflux. FT MUTAGEN 394 394 C->A: No significant effect. FT MUTAGEN 406 406 C->A: No significant effect. FT CONFLICT 38 38 S -> T (in Ref. 4; AAK28839/AAK28841). FT CONFLICT 448 448 A -> T (in Ref. 1; CAA62631, 4; AAK28838/ FT AAK28839/AAK28840/AAK28841/AAK28842 and FT 5; AAL06598). FT CONFLICT 533 533 R -> A (in Ref. 8; AAC51098). SQ SEQUENCE 678 AA; 75592 MW; B901CABDA6C19E09 CRC64; MACLMAAFSV GTAMNASSYS AEMTEPKSVC VSVDEVVSSN MEATETDLLN GHLKKVDNNL TEAQRFSSLP RRAAVNIEFR DLSYSVPEGP WWRKKGYKTL LKGISGKFNS GELVAIMGPS GAGKSTLMNI LAGYRETGMK GAVLINGLPR DLRCFRKVSC YIMQDDMLLP HLTVQEAMMV SAHLKLQEKD EGRREMVKEI LTALGLLSCA NTRTGSLSGG QRKRLAIALE LVNNPPVMFF DEPTSGLDSA SCFQVVSLMK GLAQGGRSII CTIHQPSAKL FELFDQLYVL SQGQCVYRGK VCNLVPYLRD LGLNCPTYHN PADFVMEVAS GEYGDQNSRL VRAVREGMCD SDHKRDLGGD AEVNPFLWHR PSEEVKQTKR LKGLRKDSSS MEGCHSFSAS CLTQFCILFK RTFLSIMRDS VLTHLRITSH IGIGLLIGLL YLGIGNEAKK VLSNSGFLFF SMLFLMFAAL MPTVLTFPLE MGVFLREHLN YWYSLKAYYL AKTMADVPFQ IMFPVAYCSI VYWMTSQPSD AVRFVLFAAL GTMTSLVAQS LGLLIGAAST SLQVATFVGP VTAIPVLLFS GFFVSFDTIP TYLQWMSYIS YVRYGFEGVI LSIYGLDRED LHCDIDETCH FQKSEAILRE LDVENAKLYL DFIVLGIFFI SLRLIAYFVL RYKIRAER // ID ABCG2_HUMAN Reviewed; 655 AA. AC Q9UNQ0; A0A1W3; A8K1T5; O95374; Q4W5I3; Q53ZQ1; Q569L4; Q5YLG4; AC Q86V64; Q8IX16; Q96LD6; Q96TA8; Q9BY73; Q9NUS0; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 3. DT 09-JUL-2014, entry version 148. DE RecName: Full=ATP-binding cassette sub-family G member 2; DE AltName: Full=Breast cancer resistance protein; DE AltName: Full=CDw338; DE AltName: Full=Mitoxantrone resistance-associated protein; DE AltName: Full=Placenta-specific ATP-binding cassette transporter; DE AltName: Full=Urate exporter; DE AltName: CD_antigen=CD338; GN Name=ABCG2; Synonyms=ABCP, BCRP, BCRP1, MXR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLU-166 AND SER-208, RP AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=9850061; RA Allikmets R., Schriml L.M., Hutchinson A., Romano-Spica V., Dean M.; RT "A human placenta-specific ATP-binding cassette gene (ABCP) on RT chromosome 4q22 that is involved in multidrug resistance."; RL Cancer Res. 58:5337-5339(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Mammary cancer; RX PubMed=9861027; DOI=10.1073/pnas.95.26.15665; RA Doyle L.A., Yang W., Abruzzo L.V., Krogmann T., Gao Y., Rishi A.K., RA Ross D.D.; RT "A multidrug resistance transporter from human MCF-7 breast cancer RT cells."; RL Proc. Natl. Acad. Sci. U.S.A. 95:15665-15670(1998). RN [3] RP ERRATUM. RA Doyle L.A., Yang W., Abruzzo L.V., Krogmann T., Gao Y., Rishi A.K., RA Ross D.D.; RL Proc. Natl. Acad. Sci. U.S.A. 96:2569-2569(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Kage K., Tsukahara S., Sugiyama T., Asada S., Ishikawa E., Tsuruo T., RA Sugimoto Y.; RT "Breast cancer resistance protein constitutes a 140-kDa complex as a RT homodimer."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11306452; RA Komatani H., Kotani H., Hara Y., Nakagawa R., Matsumoto M., RA Arakawa H., Nishimura S.; RT "Identification of breast cancer resistant protein/mitoxantrone RT resistance/placenta-specific, ATP-binding cassette transporter as a RT transporter of NB-506 and J-107088, topoisomerase I inhibitors with an RT indolocarbazole structure."; RL Cancer Res. 61:2827-2832(2001). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=11533706; DOI=10.1038/nm0901-1028; RA Zhou S., Schuetz J.D., Bunting K.D., Colapietro A.M., Sampath J., RA Morris J.J., Lagutina I., Grosveld G.C., Osawa M., Nakauchi H., RA Sorrentino B.P.; RT "The ABC transporter Bcrp1/ABCG2 is expressed in a wide variety of RT stem cells and is a molecular determinant of the side-population RT phenotype."; RL Nat. Med. 7:1028-1034(2001). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANTS GLU-166 RP AND SER-208. RC TISSUE=Brain endothelium; RX PubMed=12958161; DOI=10.1096/fj.02-1131fje; RA Zhang W., Mojsilovic-Petrovic J., Andrade M.F., Zhang H., Ball M., RA Stanimirovic D.B.; RT "The expression and functional characterization of ABCG2 in brain RT endothelial cells and vessels."; RL FASEB J. 17:2085-2087(2003). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-141. RA Yoshikawa M., Yabuuchi H., Ikegami Y., Ishikawa T.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-316. RA Sudarikov A., Makarik T., Andreeff M.; RT "Cell line K562 resistant to Hoechst 33342."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hippocampus, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-12; LYS-141; RP HIS-296 AND THR-528. RG SeattleSNPs variation discovery resource; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP LYS-141. RC TISSUE=Pancreas, and PNS; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 294-655 (ISOFORM 1). RX PubMed=9892175; RA Miyake K., Mickley L., Litman T., Zhan Z., Robey R.W., Cristensen B., RA Brangi M., Greenberger L., Dean M., Fojo T., Bates S.E.; RT "Molecular cloning of cDNAs which are highly overexpressed in RT mitoxantrone-resistant cells: demonstration of homology to ABC RT transport genes."; RL Cancer Res. 59:8-13(1999). RN [15] RP REVIEW. RX PubMed=11590207; RA Schmitz G., Langmann T., Heimerl S.; RT "Role of ABCG1 and other ABCG family members in lipid metabolism."; RL J. Lipid Res. 42:1513-1520(2001). RN [16] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=15001581; DOI=10.1074/jbc.M310785200; RA Xu J., Liu Y., Yang Y., Bates S., Zhang J.T.; RT "Characterization of oligomeric human half-ABC transporter ATP-binding RT cassette G2."; RL J. Biol. Chem. 279:19781-19789(2004). RN [17] RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-596, AND MUTAGENESIS OF RP ASN-418; ASN-557 AND ASN-596. RX PubMed=15807535; DOI=10.1021/bi0479858; RA Diop N.K., Hrycyna C.A.; RT "N-linked glycosylation of the human ABC transporter ABCG2 on RT asparagine 596 is not essential for expression, transport activity, or RT trafficking to the plasma membrane."; RL Biochemistry 44:5420-5429(2005). RN [18] RP MUTAGENESIS OF ARG-482. RX PubMed=15670731; DOI=10.1016/j.bbamem.2004.11.005; RA Oezvegy-Laczka C., Koebloes G., Sarkadi B., Varadi A.; RT "Single amino acid (482) variants of the ABCG2 multidrug transporter: RT major differences in transport capacity and substrate recognition."; RL Biochim. Biophys. Acta 1668:53-63(2005). RN [19] RP MUTAGENESIS OF LYS-86, SUBCELLULAR LOCATION, AND HOMODIMERIZATION. RX PubMed=15769853; DOI=10.1242/jcs.01729; RA Henriksen U., Gether U., Litman T.; RT "Effect of Walker A mutation (K86M) on oligomerization and surface RT targeting of the multidrug resistance transporter ABCG2."; RL J. Cell Sci. 118:1417-1426(2005). RN [20] RP SUBUNIT, AND DISULFIDE BONDS. RX PubMed=17686774; DOI=10.1074/jbc.C700133200; RA Wakabayashi K., Nakagawa H., Tamura A., Koshiba S., Hoshijima K., RA Komada M., Ishikawa T.; RT "Intramolecular disulfide bond is a critical check point determining RT degradative fates of ATP-binding cassette (ABC) transporter ABCG2 RT protein."; RL J. Biol. Chem. 282:27841-27846(2007). RN [21] RP INVOLVEMENT IN UAQTL1 AND GOUT. RX PubMed=18834626; DOI=10.1016/S0140-6736(08)61343-4; RA Dehghan A., Kottgen A., Yang Q., Hwang S.J., Kao W.L., Rivadeneira F., RA Boerwinkle E., Levy D., Hofman A., Astor B.C., Benjamin E.J., RA van Duijn C.M., Witteman J.C., Coresh J., Fox C.S.; RT "Association of three genetic loci with uric acid concentration and RT risk of gout: a genome-wide association study."; RL Lancet 372:1953-1961(2008). RN [22] RP INVOLVEMENT IN UAQTL1, ASSOCIATION OF VARIANT LYS-141 WITH GOUT, AND RP CHARACTERIZATION OF VARIANT LYS-141. RX PubMed=19506252; DOI=10.1073/pnas.0901249106; RA Woodward O.M., Kottgen A., Coresh J., Boerwinkle E., Guggino W.B., RA Kottgen M.; RT "Identification of a urate transporter, ABCG2, with a common RT functional polymorphism causing gout."; RL Proc. Natl. Acad. Sci. U.S.A. 106:10338-10342(2009). RN [23] RP INVOLVEMENT IN UAQTL1, AND ASSOCIATION OF VARIANT LYS-141 WITH GOUT. RX PubMed=20368174; DOI=10.1126/scitranslmed.3000237; RA Matsuo H., Takada T., Ichida K., Nakamura T., Nakayama A., RA Ikebuchi Y., Ito K., Kusanagi Y., Chiba T., Tadokoro S., Takada Y., RA Oikawa Y., Inoue H., Suzuki K., Okada R., Nishiyama J., Domoto H., RA Watanabe S., Fujita M., Morimoto Y., Naito M., Nishio K., Hishida A., RA Wakai K., Asai Y., Niwa K., Kamakura K., Nonoyama S., Sakurai Y., RA Hosoya T., Kanai Y., Suzuki H., Hamajima N., Shinomiya N.; RT "Common defects of ABCG2, a high-capacity urate exporter, cause gout: RT a function-based genetic analysis in a Japanese population."; RL Sci. Transl. Med. 1:5ra11-5ra11(2009). RN [24] RP FUNCTION, DOMAIN, AND MUTAGENESIS OF HIS-583; CYS-603 AND TYR-605. RX PubMed=20705604; DOI=10.1074/jbc.M110.139170; RA Desuzinges-Mandon E., Arnaud O., Martinez L., Huche F., Di Pietro A., RA Falson P.; RT "ABCG2 transports and transfers heme to albumin through its large RT extracellular loop."; RL J. Biol. Chem. 285:33123-33133(2010). RN [25] RP FUNCTION. RX PubMed=22132962; DOI=10.1080/15257770.2011.633953; RA Nakayama A., Matsuo H., Takada T., Ichida K., Nakamura T., RA Ikebuchi Y., Ito K., Hosoya T., Kanai Y., Suzuki H., Shinomiya N.; RT "ABCG2 is a high-capacity urate transporter and its genetic impairment RT increases serum uric acid levels in humans."; RL Nucleosides Nucleotides Nucleic Acids 30:1091-1097(2011). RN [26] RP REVIEW. RX PubMed=22509477; RA Mo W., Zhang J.T.; RT "Human ABCG2: structure, function, and its role in multidrug RT resistance."; RL Int. J. Biochem. Mol. Biol. 3:1-27(2012). RN [27] RP INVOLVEMENT IN JR, AND VARIANT MET-12. RX PubMed=22246507; DOI=10.1038/ng.1075; RA Zelinski T., Coghlan G., Liu X.Q., Reid M.E.; RT "ABCG2 null alleles define the Jr(a-) blood group phenotype."; RL Nat. Genet. 44:131-132(2012). RN [28] RP INVOLVEMENT IN JR. RX PubMed=22246505; DOI=10.1038/ng.1070; RA Saison C., Helias V., Ballif B.A., Peyrard T., Puy H., Miyazaki T., RA Perrot S., Vayssier-Taussat M., Waldner M., Le Pennec P.Y., RA Cartron J.P., Arnaud L.; RT "Null alleles of ABCG2 encoding the breast cancer resistance protein RT define the new blood group system Junior."; RL Nat. Genet. 44:174-177(2012). RN [29] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=23189181; DOI=10.1371/journal.pone.0050082; RA Kobuchi H., Moriya K., Ogino T., Fujita H., Inoue K., Shuin T., RA Yasuda T., Utsumi K., Utsumi T.; RT "Mitochondrial localization of ABC transporter ABCG2 and its function RT in 5-aminolevulinic acid-mediated protoporphyrin IX accumulation."; RL PLoS ONE 7:E50082-E50082(2012). RN [30] RP VARIANTS MET-12 AND LYS-141. RX PubMed=12111378; DOI=10.1007/s100380200041; RA Iida A., Saito S., Sekine A., Mishima C., Kitamura Y., Kondo K., RA Harigae S., Osawa S., Nakamura Y.; RT "Catalog of 605 single-nucleotide polymorphisms (SNPs) among 13 genes RT encoding human ATP-binding cassette transporters: ABCA4, ABCA7, ABCA8, RT ABCD1, ABCD3, ABCD4, ABCE1, ABCF1, ABCG1, ABCG2, ABCG4, ABCG5, and RT ABCG8."; RL J. Hum. Genet. 47:285-310(2002). RN [31] RP VARIANTS LEU-431 AND LEU-489. RX PubMed=15618737; DOI=10.2133/dmpk.18.212; RA Itoda M., Saito Y., Shirao K., Minami H., Ohtsu A., Yoshida T., RA Saijo N., Suzuki H., Sugiyama Y., Ozawa S., Sawada J.; RT "Eight novel single nucleotide polymorphisms in ABCG2/BCRP in Japanese RT cancer patients administered irinotacan."; RL Drug Metab. Pharmacokinet. 18:212-217(2003). RN [32] RP VARIANTS MET-12; LYS-141; LEU-206 AND TYR-590. RX PubMed=12544509; DOI=10.1097/00008571-200301000-00004; RA Zamber C.P., Lamba J.K., Yasuda K., Farnum J., Thummel K., RA Schuetz J.D., Schuetz E.G.; RT "Natural allelic variants of breast cancer resistance protein (BCRP) RT and their relationship to BCRP expression in human intestine."; RL Pharmacogenetics 13:19-28(2003). RN [33] RP CHARACTERIZATION OF VARIANTS MET-12; LYS-141 AND ASN-620. RX PubMed=15838659; DOI=10.1007/s00280-004-0931-x; RA Morisaki K., Robey R.W., Oezvegy-Laczka C., Honjo Y., Polgar O., RA Steadman K., Sarkadi B., Bates S.E.; RT "Single nucleotide polymorphisms modify the transporter activity of RT ABCG2."; RL Cancer Chemother. Pharmacol. 56:161-172(2005). RN [34] RP VARIANTS MET-12; LEU-13; LYS-141; GLN-160; ARG-354; LEU-431; ASN-441 RP AND LEU-489. RX PubMed=16702730; DOI=10.2133/dmpk.21.109; RA Maekawa K., Itoda M., Sai K., Saito Y., Kaniwa N., Shirao K., RA Hamaguchi T., Kunitoh H., Yamamoto N., Tamura T., Minami H., RA Kubota K., Ohtsu A., Yoshida T., Saijo N., Kamatani N., Ozawa S., RA Sawada J.; RT "Genetic variation and haplotype structure of the ABC transporter gene RT ABCG2 in a Japanese population."; RL Drug Metab. Pharmacokinet. 21:109-121(2006). CC -!- FUNCTION: High-capacity urate exporter functioning in both renal CC and extrarenal urate excretion. Plays a role in porphyrin CC homeostasis as it is able to mediates the export of protoporhyrin CC IX (PPIX) both from mitochondria to cytosol and from cytosol to CC extracellular space, and cellular export of hemin, and heme. CC Xenobiotic transporter that may play an important role in the CC exclusion of xenobiotics from the brain. Appears to play a major CC role in the multidrug resistance phenotype of several cancer cell CC lines. Implicated in the efflux of numerous drugs and xenobiotics: CC mitoxantrone, the photosensitizer pheophorbide, camptothecin, CC methotrexate, azidothymidine (AZT), and the anthracyclines CC daunorubicin and doxorubicin. CC -!- SUBUNIT: Monomer under reducing conditions, the minimal functional CC units is a homodimer; disulfide-linked, but the major oligomeric CC form in plasma membranes is a homotetramer with possibility of CC higher order oligomerization up to homododecamers. CC -!- INTERACTION: CC P11309-1:PIM1; NbExp=9; IntAct=EBI-1569435, EBI-1018629; CC P0CG48:UBC; NbExp=2; IntAct=EBI-1569435, EBI-3390054; CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC Mitochondrion membrane; Multi-pass membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UNQ0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UNQ0-2; Sequence=VSP_014232, VSP_014233; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in placenta. Low expression CC in small intestine, liver and colon. CC -!- INDUCTION: Up-regulated in brain tumors. CC -!- DOMAIN: The extracellular loop 3 (ECL3) is involved in binding CC porphyrins and transfer them to other carriers, probably albumin. CC -!- PTM: Glycosylation-deficient ABCG2 is normally expressed and CC functional. CC -!- POLYMORPHISM: Genetic variations in ABCG2 define the blood group CC Junior system (JR) [MIM:614490]. Individuals with Jr(a-) blood CC group lack the Jr(a) antigen on their red blood cells. These CC individuals may have anti-Jr(a) antibodies in their serum, which CC can cause transfusion reactions or hemolytic disease of the fetus CC or newborn. Although the clinical significance of the Jr(a-) blood CC group has been controversial, severe fatal hemolytic disease of CC the newborn has been reported. The Jr(a-) phenotype has a higher CC frequency in individuals of Asian descent, compared to those of CC European descent. The Jr(a-) phenotype is inherited as an CC autosomal recessive trait. CC -!- POLYMORPHISM: Genetic variations in ABCG2 influence the variance CC in serum uric acid concentrations and define the serum uric acid CC concentration quantitative trait locus 1 (UAQTL1) [MIM:138900]. CC Excess serum accumulation of uric acid can lead to the development CC of gout, a common disorder characterized by tissue deposition of CC monosodium urate crystals as a consequence of hyperuricemia. CC -!- MISCELLANEOUS: When overexpressed, the transfected cells become CC resistant to mitoxantrone, daunorubicin and doxorubicin. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG CC family. Eye pigment precursor importer (TC 3.A.1.204) subfamily. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-2 domain. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC -!- SEQUENCE CAUTION: CC Sequence=AF093771; Type=Frameshift; Positions=486, 586; CC Sequence=AF093772; Type=Frameshift; Positions=386, 502, 586; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/abcg2/"; CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC CC proteins; CC URL="http://abcmutations.hegelab.org/proteinDetails?uniprot_id=Q9UNQ0"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF103796; AAD09188.1; -; mRNA. DR EMBL; AF098951; AAC97367.1; -; mRNA. DR EMBL; AB056867; BAB39212.1; -; mRNA. DR EMBL; AB051855; BAB46933.1; -; mRNA. DR EMBL; AY017168; AAG52982.1; -; mRNA. DR EMBL; AY289766; AAP44087.1; -; mRNA. DR EMBL; AY288307; AAP31310.1; -; mRNA. DR EMBL; AF463519; AAO14617.1; -; mRNA. DR EMBL; AY333755; AAQ92941.1; -; mRNA. DR EMBL; AY333756; AAQ92942.1; -; mRNA. DR EMBL; AK002040; BAA92050.1; -; mRNA. DR EMBL; AK290000; BAF82689.1; -; mRNA. DR EMBL; DQ996467; ABI97388.1; -; Genomic_DNA. DR EMBL; AC084732; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC097484; AAY40902.1; -; Genomic_DNA. DR EMBL; BC021281; AAH21281.1; -; mRNA. DR EMBL; BC092408; AAH92408.1; -; mRNA. DR EMBL; AF093771; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AF093772; -; NOT_ANNOTATED_CDS; mRNA. DR CCDS; CCDS3628.1; -. [Q9UNQ0-1] DR CCDS; CCDS58910.1; -. [Q9UNQ0-2] DR RefSeq; NP_001244315.1; NM_001257386.1. [Q9UNQ0-2] DR RefSeq; NP_004818.2; NM_004827.2. [Q9UNQ0-1] DR RefSeq; XP_005263411.1; XM_005263354.1. [Q9UNQ0-1] DR RefSeq; XP_005263412.1; XM_005263355.1. [Q9UNQ0-1] DR UniGene; Hs.480218; -. DR ProteinModelPortal; Q9UNQ0; -. DR SMR; Q9UNQ0; 37-337. DR BioGrid; 114821; 3. DR DIP; DIP-29162N; -. DR IntAct; Q9UNQ0; 3. DR MINT; MINT-2840423; -. DR BindingDB; Q9UNQ0; -. DR ChEMBL; CHEMBL5393; -. DR DrugBank; DB00619; Imatinib. DR DrugBank; DB01204; Mitoxantrone. DR DrugBank; DB00622; Nicardipine. DR DrugBank; DB01054; Nitrendipine. DR DrugBank; DB01098; Rosuvastatin. DR DrugBank; DB01232; Saquinavir. DR DrugBank; DB01030; Topotecan. DR TCDB; 3.A.1.204.2; the atp-binding cassette (abc) superfamily. DR PhosphoSite; Q9UNQ0; -. DR DMDM; 67462103; -. DR MaxQB; Q9UNQ0; -. DR PaxDb; Q9UNQ0; -. DR PRIDE; Q9UNQ0; -. DR DNASU; 9429; -. DR Ensembl; ENST00000237612; ENSP00000237612; ENSG00000118777. [Q9UNQ0-1] DR Ensembl; ENST00000515655; ENSP00000426917; ENSG00000118777. [Q9UNQ0-2] DR GeneID; 9429; -. DR KEGG; hsa:9429; -. DR UCSC; uc003hrf.3; human. [Q9UNQ0-1] DR UCSC; uc003hrh.3; human. [Q9UNQ0-2] DR CTD; 9429; -. DR GeneCards; GC04M089011; -. DR HGNC; HGNC:74; ABCG2. DR HPA; CAB037299; -. DR HPA; HPA054719; -. DR MIM; 138900; phenotype. DR MIM; 603756; gene. DR MIM; 614490; phenotype. DR neXtProt; NX_Q9UNQ0; -. DR PharmGKB; PA390; -. DR eggNOG; COG1131; -. DR HOVERGEN; HBG050441; -. DR InParanoid; Q9UNQ0; -. DR KO; K05681; -. DR OMA; FYKETKA; -. DR OrthoDB; EOG7HXCR2; -. DR PhylomeDB; Q9UNQ0; -. DR TreeFam; TF105211; -. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_15518; Transmembrane transport of small molecules. DR ChiTaRS; ABCG2; human. DR GeneWiki; ABCG2; -. DR GenomeRNAi; 9429; -. DR NextBio; 35322; -. DR PRO; PR:Q9UNQ0; -. DR ArrayExpress; Q9UNQ0; -. DR Bgee; Q9UNQ0; -. DR Genevestigator; Q9UNQ0; -. DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc. DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; TAS:ProtInc. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; TAS:ProtInc. DR GO; GO:0015232; F:heme transporter activity; TAS:Reactome. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0005215; F:transporter activity; TAS:ProtInc. DR GO; GO:0008559; F:xenobiotic-transporting ATPase activity; TAS:ProtInc. DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome. DR GO; GO:0006855; P:drug transmembrane transport; TAS:Reactome. DR GO; GO:0015886; P:heme transport; TAS:GOC. DR GO; GO:0042493; P:response to drug; TAS:ProtInc. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome. DR GO; GO:0006810; P:transport; TAS:ProtInc. DR GO; GO:0046415; P:urate metabolic process; IMP:UniProtKB. DR GO; GO:0042908; P:xenobiotic transport; TAS:GOC. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013525; ABC_2_trans. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01061; ABC2_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell membrane; Complete proteome; KW Disulfide bond; Glycoprotein; Membrane; Mitochondrion; KW Nucleotide-binding; Polymorphism; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 655 ATP-binding cassette sub-family G member FT 2. FT /FTId=PRO_0000093386. FT TOPO_DOM 1 395 Cytoplasmic (Potential). FT TRANSMEM 396 416 Helical; (Potential). FT TOPO_DOM 417 428 Extracellular (Potential). FT TRANSMEM 429 449 Helical; (Potential). FT TOPO_DOM 450 477 Cytoplasmic (Potential). FT TRANSMEM 478 498 Helical; (Potential). FT TOPO_DOM 499 506 Extracellular (Potential). FT TRANSMEM 507 527 Helical; (Potential). FT TOPO_DOM 528 535 Cytoplasmic (Potential). FT TRANSMEM 536 556 Helical; (Potential). FT TOPO_DOM 557 630 Extracellular (Potential). FT TRANSMEM 631 651 Helical; (Potential). FT TOPO_DOM 652 655 Cytoplasmic (Potential). FT DOMAIN 37 286 ABC transporter. FT DOMAIN 389 651 ABC transmembrane type-2. FT NP_BIND 80 87 ATP (Potential). FT SITE 418 418 Not glycosylated. FT SITE 557 557 Not glycosylated. FT CARBOHYD 596 596 N-linked (GlcNAc...). FT DISULFID 592 608 FT DISULFID 603 603 Interchain. FT VAR_SEQ 550 611 IFSGLLVNLTTIASWLSWLQYFSIPRYGFTALQHNEFLGQN FT FCPGLNATGNNPCNYATCTGE -> VCWSISQPLHLGCHGF FT STSAFHDMDLRLCSIMNFWDKTSAQDSMQQETILVTMQHVL FT AKNIW (in isoform 2). FT /FTId=VSP_014232. FT VAR_SEQ 612 655 Missing (in isoform 2). FT /FTId=VSP_014233. FT VARIANT 12 12 V -> M (found in Jr(a-) blood group FT phenotype; dbSNP:rs2231137). FT /FTId=VAR_020779. FT VARIANT 13 13 S -> L. FT /FTId=VAR_067363. FT VARIANT 141 141 Q -> K (polymorphism associated with high FT serum levels of uric acid and increased FT risk of gout; results in lower urate FT transport rates compared to wild-type; FT dbSNP:rs2231142). FT /FTId=VAR_020780. FT VARIANT 160 160 R -> Q. FT /FTId=VAR_067364. FT VARIANT 166 166 Q -> E (in dbSNP:rs1061017). FT /FTId=VAR_022704. FT VARIANT 206 206 I -> L. FT /FTId=VAR_022705. FT VARIANT 208 208 F -> S (in dbSNP:rs1061018). FT /FTId=VAR_022706. FT VARIANT 248 248 S -> P (in dbSNP:rs3116448). FT /FTId=VAR_022707. FT VARIANT 296 296 D -> H (in dbSNP:rs41282401). FT /FTId=VAR_030357. FT VARIANT 316 316 T -> P. FT /FTId=VAR_022443. FT VARIANT 354 354 G -> R (in dbSNP:rs138606116). FT /FTId=VAR_067365. FT VARIANT 431 431 F -> L. FT /FTId=VAR_018349. FT VARIANT 441 441 S -> N. FT /FTId=VAR_067366. FT VARIANT 489 489 F -> L (in dbSNP:rs192169063). FT /FTId=VAR_018350. FT VARIANT 528 528 A -> T (in dbSNP:rs45605536). FT /FTId=VAR_030358. FT VARIANT 571 571 F -> I (in dbSNP:rs9282571). FT /FTId=VAR_022708. FT VARIANT 590 590 N -> Y (in dbSNP:rs34264773). FT /FTId=VAR_035355. FT VARIANT 620 620 D -> N (in dbSNP:rs34783571). FT /FTId=VAR_022709. FT MUTAGEN 86 86 K->M: Inactive and altered subcellular FT location. FT MUTAGEN 418 418 N->Q: No effect. FT MUTAGEN 482 482 R->D: Decreases ATPase activity. FT MUTAGEN 482 482 R->G,N,S,T: Increases ATPase activity. FT MUTAGEN 482 482 R->K,I,M,Y: No change in ATPase activity. FT MUTAGEN 482 482 R->T,Y: Decreases transport activity. FT MUTAGEN 557 557 N->Q: No effect. FT MUTAGEN 583 583 H->A: Strongly reduced binding to hemin FT but not to PPIX. FT MUTAGEN 596 596 N->Q: Loss of glycosylation. FT MUTAGEN 603 603 C->A: Strongly reduced binding to hemin FT but not to PPIX. FT MUTAGEN 605 605 Y->A: No effect on hemin binding. FT CONFLICT 24 24 A -> V (in Ref. 1; AAD09188 and 7; FT AAP44087). FT CONFLICT 315 316 Missing (in Ref. 10; BAA92050). FT CONFLICT 390 390 G -> V (in Ref. 13; AAH92408). FT CONFLICT 482 482 R -> G (in Ref. 14; AF093771/AF093772). FT CONFLICT 482 482 R -> T (in Ref. 2; AAC97367). FT CONFLICT 484 485 LP -> FT (in Ref. 14; AF093772). FT CONFLICT 501 501 P -> A (in Ref. 6; AAG52982). SQ SEQUENCE 655 AA; 72314 MW; A8AF66B96034C5A8 CRC64; MSSSNVEVFI PVSQGNTNGF PATASNDLKA FTEGAVLSFH NICYRVKLKS GFLPCRKPVE KEILSNINGI MKPGLNAILG PTGGGKSSLL DVLAARKDPS GLSGDVLING APRPANFKCN SGYVVQDDVV MGTLTVRENL QFSAALRLAT TMTNHEKNER INRVIQELGL DKVADSKVGT QFIRGVSGGE RKRTSIGMEL ITDPSILFLD EPTTGLDSST ANAVLLLLKR MSKQGRTIIF SIHQPRYSIF KLFDSLTLLA SGRLMFHGPA QEALGYFESA GYHCEAYNNP ADFFLDIING DSTAVALNRE EDFKATEIIE PSKQDKPLIE KLAEIYVNSS FYKETKAELH QLSGGEKKKK ITVFKEISYT TSFCHQLRWV SKRSFKNLLG NPQASIAQII VTVVLGLVIG AIYFGLKNDS TGIQNRAGVL FFLTTNQCFS SVSAVELFVV EKKLFIHEYI SGYYRVSSYF LGKLLSDLLP MRMLPSIIFT CIVYFMLGLK PKADAFFVMM FTLMMVAYSA SSMALAIAAG QSVVSVATLL MTICFVFMMI FSGLLVNLTT IASWLSWLQY FSIPRYGFTA LQHNEFLGQN FCPGLNATGN NPCNYATCTG EEYLVKQGID LSPWGLWKNH VALACMIVIF LTIAYLKLLF LKKYS // ID ABI1_HUMAN Reviewed; 508 AA. AC Q8IZP0; A9Z1Y6; B3KX62; B4DQ58; H7BXI6; O15147; O76049; O95060; AC Q5T2R3; Q5T2R4; Q5T2R6; Q5T2R7; Q5T2R9; Q5W070; Q5W072; Q8TB63; AC Q96S81; Q9NXZ9; Q9NYB8; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 09-JUL-2014, entry version 128. DE RecName: Full=Abl interactor 1; DE AltName: Full=Abelson interactor 1; DE Short=Abi-1; DE AltName: Full=Abl-binding protein 4; DE Short=AblBP4; DE AltName: Full=Eps8 SH3 domain-binding protein; DE Short=Eps8-binding protein; DE AltName: Full=Nap1-binding protein; DE Short=Nap1BP; DE AltName: Full=Spectrin SH3 domain-binding protein 1; DE AltName: Full=e3B1; GN Name=ABI1; Synonyms=SSH3BP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), PHOSPHORYLATION, SUBCELLULAR RP LOCATION, AND INTERACTION WITH EPS8 AND ABL1. RX PubMed=9010225; DOI=10.1038/sj.onc.1200822; RA Biesova Z., Piccoli C., Wong W.T.; RT "Isolation and characterization of e3B1, an eps8 binding protein that RT regulates cell growth."; RL Oncogene 14:233-241(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS RP 3; 7; 8 AND 9), AND INTERACTION WITH SPTA1. RX PubMed=9593709; DOI=10.1074/jbc.273.22.13681; RA Ziemnicka-Kotula D., Xu J., Gu H., Potempska A., Kim K.S., RA Jenkins E.C., Trenkner E., Kotula L.; RT "Identification of a candidate human spectrin Src homology 3 domain- RT binding protein suggests a general mechanism of association of RT tyrosine kinases with the spectrin-based membrane skeleton."; RL J. Biol. Chem. 273:13681-13692(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND RP INTERACTION WITH ABL1; NAP1 AND NCK1. RX PubMed=11418237; DOI=10.1016/S0378-1119(01)00521-2; RA Yamamoto A., Suzuki T., Sakaki Y.; RT "Isolation of hNap1BP which interacts with human Nap 1 (NCKAP1) whose RT expression is down-regulated in Alzheimer's disease."; RL Gene 271:159-169(2001). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND INTERACTION WITH NCF1. RC TISSUE=Umbilical vein endothelial cell; RX PubMed=12681507; DOI=10.1016/S0014-5793(03)00262-X; RA Gu Y., Souza R.F., Wu R.F., Xu Y.C., Terada L.S.; RT "Induction of colonic epithelial cell apoptosis by p47-dependent RT oxidants(1)."; RL FEBS Lett. 540:195-200(2003). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=T-cell; RA Wilson L.A., Fields D., Cruz L., Friesen J., Siminovitch K.A.; RT "A new member of the Abl interactor protein family, AblBP4."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Chikri M.M., Boutin M.P., Vaxillaire M.M., Froguel M.P.; RT "In silico cloning of the human SSH3BP1/e3B1 gene."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Quackenbush R.C., Pendergast A.M.; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 11 AND 12). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP PROTEIN SEQUENCE OF 2-17. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [13] RP PROTEIN SEQUENCE OF 2-17; 139-154; 229-237 AND 451-477, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Hepatoma; RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.; RL Submitted (JUL-2007) to UniProtKB. RN [14] RP FUNCTION, AND INTERACTION WITH SOS1; SOS2 AND GRB2. RX PubMed=11003655; DOI=10.1128/MCB.20.20.7591-7601.2000; RA Fan P.-D., Goff S.P.; RT "Abl interactor 1 binds to sos and inhibits epidermal growth factor- RT and v-Abl-induced activation of extracellular signal-regulated RT kinases."; RL Mol. Cell. Biol. 20:7591-7601(2000). RN [15] RP ALTERNATIVE SPLICING (ISOFORMS 2 AND 10), AND CHROMOSOMAL RP TRANSLOCATION WITH KMT2A. RX PubMed=9694699; RA Taki T., Shibuya N., Taniwaki M., Hanada R., Morishita K., Bessho F., RA Yanagisawa M., Hayashi Y.; RT "ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene RT in acute myeloid leukemia with t(10;11)(p11.2;q23)."; RL Blood 92:1125-1130(1998). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [17] RP FUNCTION, AND PHOSPHORYLATION AT TYR-213. RX PubMed=18328268; DOI=10.1016/j.bbamcr.2008.01.028; RA Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X., RA Debnath A.K., Cowburn D., Kotula L.; RT "Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase RT by phosphopeptides derived from Abi1/Hssh3bp1."; RL Biochim. Biophys. Acta 1783:737-747(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-216, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND THR-507, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-225 AND RP SER-323, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [25] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: May act in negative regulation of cell growth and CC transformation by interacting with nonreceptor tyrosine kinases CC ABL1 and/or ABL2. May play a role in regulation of EGF-induced Erk CC pathway activation. Involved in cytoskeletal reorganization and CC EGFR signaling. Together with EPS8 participates in transduction of CC signals from Ras to Rac. In vitro, a trimeric complex of ABI1, CC EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange CC factor (GEF) activity and ABI1 seems to act as an adapter in the CC complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH. CC Recruits WASF1 to lamellipodia and there seems to regulate WASF1 CC protein level. In brain, seems to regulate the dendritic outgrowth CC and branching as well as to determine the shape and number of CC synaptic contacts of developing neurons. CC -!- SUBUNIT: Interacts with ABL1, ENAH, STX1A, SNAP25, VAMP2, EPS8, CC and through its N-terminus with WASF1. Part of a complex CC consisting of ABI1, STX1A and SNAP25. Part of a complex consisting CC of ABI1, EPS8 and SOS1 (By similarity). Interacts with SOS1, SOS2, CC GRB2, SPTA1 and the first SH3 domain of NCK1. Isoform 6 does not CC interact with NCK1. Component of the WAVE2 complex composed of CC ABI1, CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Interacts (via SH3 CC domain) with SHANK2 and SHANK3, but not SHANK1; the interaction is CC direct. Interacts with the heterodimer MYC:MAX; the interaction CC may enhance MYC:MAX transcriptional activity. CC -!- INTERACTION: CC P00519:ABL1; NbExp=11; IntAct=EBI-375446, EBI-375543; CC P00520-4:Abl1 (xeno); NbExp=5; IntAct=EBI-8593095, EBI-8593082; CC P42684:ABL2; NbExp=2; IntAct=EBI-375446, EBI-1102694; CC O00555:CACNA1A; NbExp=2; IntAct=EBI-375446, EBI-766279; CC P22681:CBL; NbExp=3; IntAct=EBI-7358775, EBI-518228; CC Q08509:Eps8 (xeno); NbExp=2; IntAct=EBI-375446, EBI-375596; CC P14598:NCF1; NbExp=5; IntAct=EBI-375446, EBI-395044; CC Q9Y2A7:NCKAP1; NbExp=2; IntAct=EBI-375446, EBI-389845; CC P27986:PIK3R1; NbExp=8; IntAct=EBI-375446, EBI-79464; CC P26450:Pik3r1 (xeno); NbExp=3; IntAct=EBI-375446, EBI-641764; CC Q92569:PIK3R3; NbExp=2; IntAct=EBI-375446, EBI-79893; CC P20936:RASA1; NbExp=2; IntAct=EBI-375446, EBI-1026476; CC O14512:SOCS7; NbExp=2; IntAct=EBI-375446, EBI-1539606; CC P02549:SPTA1; NbExp=2; IntAct=EBI-375446, EBI-375617; CC P15498:VAV1; NbExp=2; IntAct=EBI-375446, EBI-625518; CC P52735:VAV2; NbExp=2; IntAct=EBI-375446, EBI-297549; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). Cell projection, lamellipodium (By similarity). Cell CC projection, filopodium (By similarity). Cell projection, growth CC cone (By similarity). Cell junction, synapse, postsynaptic cell CC membrane, postsynaptic density (By similarity). Cytoplasm, CC cytoskeleton (By similarity). Note=Localized to protruding CC lamellipodia and filopodia tips. Also localized to neuronal growth CC cones and synaptosomes. May shuttle from the postsynaptic CC densities to the nucleus (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=12; CC Comment=Additional isoforms seem to exist; CC Name=1; CC IsoId=Q8IZP0-1; Sequence=Displayed; CC Name=2; Synonyms=long, B48; CC IsoId=Q8IZP0-2; Sequence=VSP_010749, VSP_010750, VSP_010751, CC VSP_010752; CC Name=3; CC IsoId=Q8IZP0-3; Sequence=VSP_010750, VSP_010752; CC Name=4; CC IsoId=Q8IZP0-4; Sequence=VSP_010750, VSP_010751, VSP_010752; CC Name=5; CC IsoId=Q8IZP0-5; Sequence=VSP_010749, VSP_010750; CC Name=6; CC IsoId=Q8IZP0-6; Sequence=VSP_010750, VSP_010751; CC Name=7; Synonyms=4; CC IsoId=Q8IZP0-7; Sequence=VSP_010750, VSP_010751, VSP_010754, CC VSP_010755; CC Name=8; Synonyms=5; CC IsoId=Q8IZP0-8; Sequence=VSP_010750, VSP_010751, VSP_010754, CC VSP_010752; CC Name=9; Synonyms=2; CC IsoId=Q8IZP0-9; Sequence=VSP_010750; CC Name=10; Synonyms=B30; CC IsoId=Q8IZP0-10; Sequence=VSP_010749, VSP_010750, VSP_010751, CC VSP_010754, VSP_010752, VSP_010753; CC Name=11; CC IsoId=Q8IZP0-11; Sequence=VSP_043403, VSP_010750, VSP_010751, CC VSP_010754, VSP_010752, VSP_010753; CC Note=No experimental confirmation available; CC Name=12; CC IsoId=Q8IZP0-12; Sequence=VSP_044604, VSP_010752; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in CC brain. CC -!- DOMAIN: The t-SNARE coiled-coil homology domain is necessary and CC sufficient for interaction with STX1A (By similarity). CC -!- PTM: Phosphorylated on tyrosine residues after serum stimulation CC or induction by v-Abl. Seems to be phosphorylated at Tyr-53 by CC ABL1, required for nuclear but not for synaptic localization. CC -!- DISEASE: Note=A chromosomal aberration involving ABI1 is a cause CC of acute leukemias. Translocation t(10;11)(p11.2;q23) with CC KMT2A/MLL1. ABI1 isoform 2 was found to be present in acute CC leukemia KMT2A/MLL1-ABI1 fusion transcript. CC -!- SIMILARITY: Belongs to the ABI family. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/ABI1ID233.html"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF006516; AAB62569.1; -; mRNA. DR EMBL; U87166; AAC39757.1; -; mRNA. DR EMBL; AB040151; BAB55675.1; -; mRNA. DR EMBL; AF540955; AAN28379.1; -; mRNA. DR EMBL; AF001628; AAD00897.1; -; mRNA. DR EMBL; AJ277065; CAB88006.1; -; Genomic_DNA. DR EMBL; AJ277066; CAB88006.1; JOINED; Genomic_DNA. DR EMBL; AJ277067; CAB88006.1; JOINED; Genomic_DNA. DR EMBL; AJ277068; CAB88006.1; JOINED; Genomic_DNA. DR EMBL; AJ277069; CAB88006.1; JOINED; Genomic_DNA. DR EMBL; AJ277070; CAB88006.1; JOINED; Genomic_DNA. DR EMBL; AJ277071; CAB88006.1; JOINED; Genomic_DNA. DR EMBL; AJ277072; CAB88006.1; JOINED; Genomic_DNA. DR EMBL; AJ277073; CAB88006.1; JOINED; Genomic_DNA. DR EMBL; AJ277074; CAB88006.1; JOINED; Genomic_DNA. DR EMBL; AF260262; AAF70309.1; -; mRNA. DR EMBL; AK126803; BAG54374.1; -; mRNA. DR EMBL; AK298646; BAG60820.1; -; mRNA. DR EMBL; AK291823; BAF84512.1; -; mRNA. DR EMBL; AL139404; CAH73112.1; -; Genomic_DNA. DR EMBL; AL390961; CAH73112.1; JOINED; Genomic_DNA. DR EMBL; AL139404; CAH73113.1; -; Genomic_DNA. DR EMBL; AL390961; CAH73113.1; JOINED; Genomic_DNA. DR EMBL; AL139404; CAH73114.1; -; Genomic_DNA. DR EMBL; AL390961; CAH73114.1; JOINED; Genomic_DNA. DR EMBL; AL139404; CAH73115.1; -; Genomic_DNA. DR EMBL; AL390961; CAH73115.1; JOINED; Genomic_DNA. DR EMBL; AL139404; CAH73116.1; -; Genomic_DNA. DR EMBL; AL390961; CAH73116.1; JOINED; Genomic_DNA. DR EMBL; AL139404; CAH73117.1; -; Genomic_DNA. DR EMBL; AL390961; CAH73117.1; JOINED; Genomic_DNA. DR EMBL; AL139404; CAH73118.1; -; Genomic_DNA. DR EMBL; AL390961; CAH73118.1; JOINED; Genomic_DNA. DR EMBL; AL139404; CAH73119.1; -; Genomic_DNA. DR EMBL; AL390961; CAH73119.1; JOINED; Genomic_DNA. DR EMBL; AL390961; CAI17272.1; -; Genomic_DNA. DR EMBL; AL139404; CAI17272.1; JOINED; Genomic_DNA. DR EMBL; AL390961; CAI17273.1; -; Genomic_DNA. DR EMBL; AL139404; CAI17273.1; JOINED; Genomic_DNA. DR EMBL; AL390961; CAI17274.1; -; Genomic_DNA. DR EMBL; AL139404; CAI17274.1; JOINED; Genomic_DNA. DR EMBL; AL390961; CAI17275.1; -; Genomic_DNA. DR EMBL; AL139404; CAI17275.1; JOINED; Genomic_DNA. DR EMBL; AL390961; CAI17276.1; -; Genomic_DNA. DR EMBL; AL139404; CAI17276.1; JOINED; Genomic_DNA. DR EMBL; AL390961; CAI17277.1; -; Genomic_DNA. DR EMBL; AL139404; CAI17277.1; JOINED; Genomic_DNA. DR EMBL; AL390961; CAI17278.1; -; Genomic_DNA. DR EMBL; AL139404; CAI17278.1; JOINED; Genomic_DNA. DR EMBL; AL390961; CAI17279.1; -; Genomic_DNA. DR EMBL; AL139404; CAI17279.1; JOINED; Genomic_DNA. DR EMBL; CH471072; EAW86079.1; -; Genomic_DNA. DR EMBL; CH471072; EAW86080.1; -; Genomic_DNA. DR EMBL; BC024254; AAH24254.1; -; mRNA. DR CCDS; CCDS31169.1; -. [Q8IZP0-5] DR CCDS; CCDS31170.1; -. [Q8IZP0-3] DR CCDS; CCDS31171.1; -. [Q8IZP0-9] DR CCDS; CCDS53497.1; -. [Q8IZP0-11] DR CCDS; CCDS53498.1; -. [Q8IZP0-2] DR CCDS; CCDS53499.1; -. [Q8IZP0-4] DR CCDS; CCDS53500.1; -. [Q8IZP0-6] DR CCDS; CCDS53501.1; -. [Q8IZP0-12] DR CCDS; CCDS7150.1; -. [Q8IZP0-1] DR RefSeq; NP_001012768.1; NM_001012750.2. [Q8IZP0-9] DR RefSeq; NP_001012769.1; NM_001012751.2. [Q8IZP0-3] DR RefSeq; NP_001012770.1; NM_001012752.2. [Q8IZP0-5] DR RefSeq; NP_001171587.1; NM_001178116.1. [Q8IZP0-12] DR RefSeq; NP_001171590.1; NM_001178119.1. [Q8IZP0-6] DR RefSeq; NP_001171591.1; NM_001178120.1. [Q8IZP0-4] DR RefSeq; NP_001171592.1; NM_001178121.1. [Q8IZP0-2] DR RefSeq; NP_001171593.1; NM_001178122.1. [Q8IZP0-7] DR RefSeq; NP_001171594.1; NM_001178123.1. DR RefSeq; NP_001171595.1; NM_001178124.1. [Q8IZP0-10] DR RefSeq; NP_001171596.1; NM_001178125.1. [Q8IZP0-11] DR RefSeq; NP_005461.2; NM_005470.3. [Q8IZP0-1] DR UniGene; Hs.508148; -. DR ProteinModelPortal; Q8IZP0; -. DR SMR; Q8IZP0; 1-154, 436-503. DR BioGrid; 115324; 24. DR DIP; DIP-31118N; -. DR IntAct; Q8IZP0; 61. DR MINT; MINT-106609; -. DR PhosphoSite; Q8IZP0; -. DR DMDM; 50400546; -. DR MaxQB; Q8IZP0; -. DR PaxDb; Q8IZP0; -. DR PRIDE; Q8IZP0; -. DR Ensembl; ENST00000346832; ENSP00000279599; ENSG00000136754. [Q8IZP0-12] DR Ensembl; ENST00000359188; ENSP00000352114; ENSG00000136754. [Q8IZP0-6] DR Ensembl; ENST00000376138; ENSP00000365308; ENSG00000136754. [Q8IZP0-3] DR Ensembl; ENST00000376139; ENSP00000365309; ENSG00000136754. [Q8IZP0-5] DR Ensembl; ENST00000376140; ENSP00000365310; ENSG00000136754. [Q8IZP0-9] DR Ensembl; ENST00000376142; ENSP00000365312; ENSG00000136754. [Q8IZP0-1] DR Ensembl; ENST00000376166; ENSP00000365336; ENSG00000136754. [Q8IZP0-2] DR Ensembl; ENST00000376170; ENSP00000365340; ENSG00000136754. [Q8IZP0-4] DR Ensembl; ENST00000490841; ENSP00000440101; ENSG00000136754. [Q8IZP0-11] DR GeneID; 10006; -. DR KEGG; hsa:10006; -. DR UCSC; uc001isx.3; human. [Q8IZP0-1] DR UCSC; uc001isy.3; human. [Q8IZP0-9] DR UCSC; uc001isz.3; human. [Q8IZP0-5] DR UCSC; uc001ita.3; human. [Q8IZP0-3] DR UCSC; uc001itc.3; human. [Q8IZP0-6] DR UCSC; uc001itd.3; human. [Q8IZP0-4] DR UCSC; uc001ite.3; human. [Q8IZP0-2] DR UCSC; uc010qdh.2; human. [Q8IZP0-10] DR UCSC; uc010qdi.2; human. [Q8IZP0-11] DR CTD; 10006; -. DR GeneCards; GC10M027075; -. DR HGNC; HGNC:11320; ABI1. DR HPA; CAB008375; -. DR HPA; HPA029973; -. DR MIM; 603050; gene. DR neXtProt; NX_Q8IZP0; -. DR PharmGKB; PA36144; -. DR eggNOG; NOG262939; -. DR HOVERGEN; HBG050446; -. DR OrthoDB; EOG7J17ZT; -. DR PhylomeDB; Q8IZP0; -. DR TreeFam; TF314303; -. DR Reactome; REACT_6900; Immune System. DR SignaLink; Q8IZP0; -. DR ChiTaRS; ABI1; human. DR GeneWiki; ABI1; -. DR GenomeRNAi; 10006; -. DR NextBio; 37795; -. DR PRO; PR:Q8IZP0; -. DR ArrayExpress; Q8IZP0; -. DR Bgee; Q8IZP0; -. DR Genevestigator; Q8IZP0; -. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0030175; C:filopodium; IDA:UniProtKB. DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW. DR GO; GO:0031209; C:SCAR complex; IDA:UniProt. DR GO; GO:0008092; F:cytoskeletal protein binding; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0032403; F:protein complex binding; IDA:UniProt. DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IEA:Ensembl. DR GO; GO:0008154; P:actin polymerization or depolymerization; NAS:UniProtKB. DR GO; GO:0006928; P:cellular component movement; IDA:UniProtKB. DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0072673; P:lamellipodium morphogenesis; IEA:Ensembl. DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI. DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc. DR InterPro; IPR028457; ABI. DR InterPro; IPR028456; ABI1. DR InterPro; IPR012849; Abl-interactor_HHR_dom. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR000727; T_SNARE_dom. DR PANTHER; PTHR10460; PTHR10460; 1. DR PANTHER; PTHR10460:SF2; PTHR10460:SF2; 1. DR Pfam; PF07815; Abi_HHR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SSF50044; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS50192; T_SNARE; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell junction; Cell membrane; KW Cell projection; Chromosomal rearrangement; Coiled coil; KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW Membrane; Nucleus; Phosphoprotein; Polymorphism; KW Postsynaptic cell membrane; Reference proteome; SH3 domain; Synapse. FT INIT_MET 1 1 Removed. FT CHAIN 2 508 Abl interactor 1. FT /FTId=PRO_0000191787. FT DOMAIN 45 107 t-SNARE coiled-coil homology. FT DOMAIN 446 505 SH3. FT REGION 18 79 Required for binding to WASF1 (By FT similarity). FT COMPBIAS 260 418 Pro-rich. FT SITE 95 96 Breakpoint for translocation to form FT KMT2A/MLL1-ABI1. FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 53 53 Phosphotyrosine (By similarity). FT MOD_RES 183 183 Phosphoserine. FT MOD_RES 213 213 Phosphotyrosine; by ABL1. FT MOD_RES 216 216 Phosphoserine. FT MOD_RES 222 222 Phosphoserine. FT MOD_RES 225 225 Phosphoserine. FT MOD_RES 323 323 Phosphoserine. FT MOD_RES 455 455 Phosphotyrosine (By similarity). FT MOD_RES 507 507 Phosphothreonine. FT VAR_SEQ 38 38 I -> IQRHGFAVLLCLLSNSWP (in isoform 12). FT /FTId=VSP_044604. FT VAR_SEQ 96 159 Missing (in isoform 11). FT /FTId=VSP_043403. FT VAR_SEQ 154 158 Missing (in isoform 2, isoform 5 and FT isoform 10). FT /FTId=VSP_010749. FT VAR_SEQ 274 300 Missing (in isoform 2, isoform 3, isoform FT 4, isoform 5, isoform 6, isoform 7, FT isoform 8, isoform 9, isoform 10 and FT isoform 11). FT /FTId=VSP_010750. FT VAR_SEQ 301 301 Missing (in isoform 2, isoform 4, isoform FT 6, isoform 7, isoform 8, isoform 10 and FT isoform 11). FT /FTId=VSP_010751. FT VAR_SEQ 302 359 Missing (in isoform 7, isoform 8, isoform FT 10 and isoform 11). FT /FTId=VSP_010754. FT VAR_SEQ 360 388 Missing (in isoform 2, isoform 3, isoform FT 4, isoform 8, isoform 10, isoform 11 and FT isoform 12). FT /FTId=VSP_010752. FT VAR_SEQ 360 360 I -> V (in isoform 7). FT /FTId=VSP_010755. FT VAR_SEQ 389 389 I -> V (in isoform 10 and isoform 11). FT /FTId=VSP_010753. FT VARIANT 331 331 G -> A (in dbSNP:rs2306236). FT /FTId=VAR_048159. FT CONFLICT 177 177 P -> L (in Ref. 2; AAC39757). FT CONFLICT 410 410 S -> F (in Ref. 2; AAC39757 and 4; FT AAN28379). FT CONFLICT 437 437 D -> G (in Ref. 8; BAG54374). SQ SEQUENCE 508 AA; 55081 MW; 2D76F305934127CB CRC64; MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK PPSPPMSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT IGPENISVPP PSGAPPAPPL APLLPVSTVI AAPGSAPGSQ YGTMTRQISR HNSTTSSTSS GGYRRTPSVT AQFSAQPHVN GGPLYSQNSI SIAPPPPPMP QLTPQIPLTG FVARVQENIA DSPTPPPPPP PDDIPMFDDS PPPPPPPPVD YEDEEAAVVQ YNDPYADGDP AWAPKNYIEK VVAIYDYTKD KDDELSFMEG AIIYVIKKND DGWYEGVCNR VTGLFPGNYV ESIMHYTD // ID ABI2_HUMAN Reviewed; 513 AA. AC Q9NYB9; B4DSN1; Q13147; Q13249; Q13801; Q9BV70; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 09-JUL-2014, entry version 122. DE RecName: Full=Abl interactor 2; DE AltName: Full=Abelson interactor 2; DE Short=Abi-2; DE AltName: Full=Abl-binding protein 3; DE Short=AblBP3; DE AltName: Full=Arg-binding protein 1; DE Short=ArgBP1; GN Name=ABI2; Synonyms=ARGBPIA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABL1. RX PubMed=7590236; DOI=10.1101/gad.9.21.2569; RA Dai Z., Pendergast A.M.; RT "Abi-2, a novel SH3-containing protein interacts with the c-Abl RT tyrosine kinase and modulates c-Abl transforming activity."; RL Genes Dev. 9:2569-2582(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Ren R.; RT "Cloning of a binding substrate of the Abl protein tyrosine kinase."; RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH RP ABL2. RC TISSUE=Brain; RX PubMed=8649853; RA Wang B., Mysliwiec T., Krainc D., Jensen R.A., Sonoda G., Testa J.R., RA Golemis E.A., Kruh G.D.; RT "Identification of ArgBP1, an Arg protein tyrosine kinase binding RT protein that is the human homologue of a CNS-specific Xenopus gene."; RL Oncogene 12:1921-1929(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION. RX PubMed=10498863; DOI=10.1038/sj.onc.1202911; RA Juang J.L., Hoffmann F.M.; RT "Drosophila abelson interacting protein (dAbi) is a positive regulator RT of abelson tyrosine kinase activity."; RL Oncogene 18:5138-5147(1999). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=11516653; DOI=10.1016/S0960-9822(01)00239-1; RA Stradal T.E.B., Courtney K.D., Rottner K., Hahne P., Small J.V., RA Pendergast A.M.; RT "The Abl interactor proteins localize to sites of actin polymerization RT at the tips of lamellipodia and filopodia."; RL Curr. Biol. 11:891-895(2001). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227 AND SER-368, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP STRUCTURE BY NMR OF 444-508. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of Abl interactor 2 (Abelson RT interactor 2)."; RL Submitted (FEB-2008) to the PDB data bank. RN [14] RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-164, AND SUBUNIT. RX PubMed=21107423; DOI=10.1038/nature09623; RA Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M., RA Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.; RT "Structure and control of the actin regulatory WAVE complex."; RL Nature 468:533-538(2010). CC -!- FUNCTION: May act in regulation of cell growth and transformation CC by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. CC Part of the WAVE complex that regulates lamellipodia formation. CC The WAVE complex regulates actin filament reorganization via its CC interaction with the Arp2/3 complex. Regulates ABL1/c-Abl-mediated CC phosphorylation of MENA. CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 CC or CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a CC heterdimer containing NCKAP1 and CYFIP1 interacts with a CC heterotrimer formed by WAVE1, ABI2 and BRK1. CYFIP2 binds to CC activated RAC1 which causes the complex to dissociate, releasing CC activated WASF1. The complex can also be activated by NCK1 (By CC similarity). Interacts with ABL1 and ABL2. CC -!- INTERACTION: CC P00519:ABL1; NbExp=2; IntAct=EBI-743598, EBI-375543; CC Q8VHK2:Caskin1 (xeno); NbExp=3; IntAct=EBI-743598, EBI-7049475; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform 1: Cell projection, lamellipodium CC (By similarity). Cell projection, filopodium (By similarity). CC Cytoplasm, cytoskeleton (By similarity). Note=Isoform 1 but not CC isoform 3 is localized to protruding lamellipodia and filopodia CC tips (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Abi-2b; CC IsoId=Q9NYB9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NYB9-2; Sequence=VSP_010761, VSP_010762, VSP_010763; CC Name=3; Synonyms=Abi-2a; CC IsoId=Q9NYB9-3; Sequence=VSP_010759, VSP_010760, VSP_010761, CC VSP_010762; CC Name=4; CC IsoId=Q9NYB9-4; Sequence=VSP_010761; CC -!- PTM: Is a substrate for ABL1. CC -!- SIMILARITY: Belongs to the ABI family. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U23435; AAA92289.1; -; mRNA. DR EMBL; U31089; AAA75446.1; -; mRNA. DR EMBL; AF260261; AAF70308.1; -; mRNA. DR EMBL; X95632; CAA64885.1; -; mRNA. DR EMBL; BT009920; AAP88922.1; -; mRNA. DR EMBL; AK299824; BAG61693.1; -; mRNA. DR EMBL; BC001439; AAH01439.1; -; mRNA. DR CCDS; CCDS2358.1; -. [Q9NYB9-2] DR CCDS; CCDS63093.1; -. [Q9NYB9-1] DR CCDS; CCDS63094.1; -. [Q9NYB9-4] DR CCDS; CCDS63096.1; -. [Q9NYB9-3] DR PIR; G01936; G01936. DR RefSeq; NP_001269854.1; NM_001282925.1. DR RefSeq; NP_001269855.1; NM_001282926.1. DR RefSeq; NP_001269856.1; NM_001282927.1. [Q9NYB9-3] DR RefSeq; NP_005750.4; NM_005759.5. [Q9NYB9-2] DR RefSeq; XP_006712248.1; XM_006712185.1. [Q9NYB9-3] DR UniGene; Hs.471156; -. DR PDB; 2ED0; NMR; -; A=444-508. DR PDB; 3P8C; X-ray; 2.29 A; F=1-164. DR PDB; 4N78; X-ray; 2.43 A; F=1-513. DR PDBsum; 2ED0; -. DR PDBsum; 3P8C; -. DR PDBsum; 4N78; -. DR ProteinModelPortal; Q9NYB9; -. DR SMR; Q9NYB9; 1-154, 444-508. DR BioGrid; 115454; 21. DR DIP; DIP-37566N; -. DR IntAct; Q9NYB9; 23. DR MINT; MINT-252647; -. DR STRING; 9606.ENSP00000261017; -. DR PhosphoSite; Q9NYB9; -. DR DMDM; 50400673; -. DR MaxQB; Q9NYB9; -. DR PaxDb; Q9NYB9; -. DR PRIDE; Q9NYB9; -. DR DNASU; 10152; -. DR Ensembl; ENST00000261016; ENSP00000261016; ENSG00000138443. [Q9NYB9-3] DR Ensembl; ENST00000261017; ENSP00000261017; ENSG00000138443. [Q9NYB9-2] DR Ensembl; ENST00000424558; ENSP00000391433; ENSG00000138443. DR GeneID; 10152; -. DR KEGG; hsa:10152; -. DR UCSC; uc002uzz.3; human. [Q9NYB9-2] DR UCSC; uc002vab.3; human. [Q9NYB9-3] DR CTD; 10152; -. DR GeneCards; GC02P204192; -. DR H-InvDB; HIX0002759; -. DR HGNC; HGNC:24011; ABI2. DR MIM; 606442; gene. DR neXtProt; NX_Q9NYB9; -. DR PharmGKB; PA134977642; -. DR eggNOG; NOG262939; -. DR HOGENOM; HOG000293213; -. DR HOVERGEN; HBG050446; -. DR InParanoid; Q9NYB9; -. DR KO; K05751; -. DR PhylomeDB; Q9NYB9; -. DR TreeFam; TF314303; -. DR Reactome; REACT_6900; Immune System. DR ChiTaRS; ABI2; human. DR EvolutionaryTrace; Q9NYB9; -. DR GeneWiki; ABI2; -. DR GenomeRNAi; 10152; -. DR NextBio; 38426; -. DR PRO; PR:Q9NYB9; -. DR ArrayExpress; Q9NYB9; -. DR Bgee; Q9NYB9; -. DR CleanEx; HS_ABI2; -. DR Genevestigator; Q9NYB9; -. DR GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0030175; C:filopodium; IDA:UniProtKB. DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB. DR GO; GO:0031209; C:SCAR complex; IDA:UniProt. DR GO; GO:0008093; F:cytoskeletal adaptor activity; TAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0019900; F:kinase binding; NAS:UniProtKB. DR GO; GO:0070064; F:proline-rich region binding; IPI:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0032403; F:protein complex binding; IDA:UniProt. DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL. DR GO; GO:0008154; P:actin polymerization or depolymerization; NAS:UniProtKB. DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl. DR GO; GO:0016477; P:cell migration; TAS:UniProtKB. DR GO; GO:0006928; P:cellular component movement; IDA:UniProtKB. DR GO; GO:0007010; P:cytoskeleton organization; TAS:UniProtKB. DR GO; GO:0016358; P:dendrite development; IEA:Ensembl. DR GO; GO:0007611; P:learning or memory; IEA:Ensembl. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI. DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:UniProt. DR GO; GO:0016601; P:Rac protein signal transduction; IDA:UniProt. DR InterPro; IPR028457; ABI. DR InterPro; IPR028454; Abi2. DR InterPro; IPR012849; Abl-interactor_HHR_dom. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR000727; T_SNARE_dom. DR PANTHER; PTHR10460; PTHR10460; 1. DR PANTHER; PTHR10460:SF3; PTHR10460:SF3; 1. DR Pfam; PF07815; Abi_HHR; 1. DR Pfam; PF14604; SH3_9; 1. DR PRINTS; PR00452; SH3DOMAIN. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SSF50044; 1. DR PROSITE; PS50002; SH3; 1. DR PROSITE; PS50192; T_SNARE; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Coiled coil; KW Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; KW Reference proteome; SH3 domain. FT CHAIN 1 513 Abl interactor 2. FT /FTId=PRO_0000191790. FT DOMAIN 45 107 t-SNARE coiled-coil homology. FT DOMAIN 451 510 SH3. FT COMPBIAS 172 423 Pro-rich. FT MOD_RES 227 227 Phosphoserine. FT MOD_RES 368 368 Phosphoserine. FT VAR_SEQ 1 45 Missing (in isoform 3). FT /FTId=VSP_010759. FT VAR_SEQ 46 95 ALEETKAYTTQSLASVAYLINTLANNVLQMLDIQASQLRRM FT ESSINHISQ -> MSCRCWISRHPSYEGWNLQSIIFHKQIR FT GVDLESTFVTKFGNNCSLRLNE (in isoform 3). FT /FTId=VSP_010760. FT VAR_SEQ 154 159 Missing (in isoform 2, isoform 3 and FT isoform 4). FT /FTId=VSP_010761. FT VAR_SEQ 284 344 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_010762. FT VAR_SEQ 399 399 S -> SLAPPPPSILQVTPQLPLMGFVARVQENIS (in FT isoform 2). FT /FTId=VSP_010763. FT CONFLICT 22 22 S -> R (in Ref. 3; CAA64885). FT CONFLICT 69 69 A -> D (in Ref. 3; CAA64885). FT CONFLICT 243 243 S -> T (in Ref. 2; AAA75446). FT CONFLICT 249 249 G -> P (in Ref. 1; AAA92289). FT CONFLICT 317 317 N -> D (in Ref. 5; BAG61693). FT CONFLICT 324 325 PN -> QT (in Ref. 5; BAG61693). FT CONFLICT 432 432 A -> V (in Ref. 2; AAA75446). FT CONFLICT 500 500 F -> S (in Ref. 2; AAA75446). FT HELIX 1 9 FT HELIX 11 39 FT HELIX 43 110 FT STRAND 123 125 FT TURN 143 151 FT STRAND 453 458 FT STRAND 477 483 FT STRAND 485 493 FT STRAND 496 501 FT STRAND 504 507 SQ SEQUENCE 513 AA; 55663 MW; 822983A69E5EA512 CRC64; MAELQMLLEE EIPGGRRALF DSYTNLERVA DYCENNYIQS ADKQRALEET KAYTTQSLAS VAYLINTLAN NVLQMLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR THKIIAPANL ERPVRYIRKP IDYTILDDIG HGVKWLLRFK VSTQNMKMGG LPRTTPPTQK PPSPPMSGKG TLGRHSPYRT LEPVRPPVVP NDYVPSPTRN MAPSQQSPVR TASVNQRNRT YSSSGSSGGS HPSSRSSSRE NSGSGSVGVP IAVPTPSPPS VFPAPAGSAG TPPLPATSAS APAPLVPATV PSSTAPNAAA GGAPNLADGF TSPTPPVVSS TPPTGHPVQF YSMNRPASRH TPPTIGGSLP YRRPPSITSQ TSLQNQMNGG PFYSQNPVSD TPPPPPPVEE PVFDESPPPP PPPEDYEEEE AAVVEYSDPY AEEDPPWAPR SYLEKVVAIY DYTKDKEDEL SFQEGAIIYV IKKNDDGWYE GVMNGVTGLF PGNYVESIMH YSE // ID ABL1_HUMAN Reviewed; 1130 AA. AC P00519; A3KFJ3; Q13869; Q13870; Q16133; Q17R61; Q45F09; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 4. DT 09-JUL-2014, entry version 204. DE RecName: Full=Tyrosine-protein kinase ABL1; DE EC=2.7.10.2; DE AltName: Full=Abelson murine leukemia viral oncogene homolog 1; DE AltName: Full=Abelson tyrosine-protein kinase 1; DE AltName: Full=Proto-oncogene c-Abl; DE AltName: Full=p150; GN Name=ABL1; Synonyms=ABL, JTK7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA), ALTERNATIVE SPLICING, AND RP VARIANT PRO-140. RX PubMed=3021337; DOI=10.1016/0092-8674(86)90450-2; RA Shtivelman E., Lifshitz B., Gale R.P., Roe B.A., Canaani E.; RT "Alternative splicing of RNAs transcribed from the human abl gene and RT from the bcr-abl fused gene."; RL Cell 47:277-284(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IA). RC TISSUE=Fibroblast; RX PubMed=2687768; RA Fainstein E., Einat M., Gokkel E., Marcelle C., Croce C.M., Gale R.P., RA Canaani E.; RT "Nucleotide sequence analysis of human abl and bcr-abl cDNAs."; RL Oncogene 4:1477-1481(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS IA AND IB). RC TISSUE=Lung; RX PubMed=7665185; DOI=10.1006/geno.1995.1008; RA Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D., RA Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y., RA McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G., RA Heisterkamp N., Groffen J., Roe B.A.; RT "Sequence and analysis of the human ABL gene, the BCR gene, and RT regions involved in the Philadelphia chromosomal translocation."; RL Genomics 27:67-82(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-706; PRO-852; RP SER-900 AND LEU-972. RG NIEHS SNPs program; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IB). RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-40, AND SUBCELLULAR COMPONENT. RX PubMed=2825022; DOI=10.1038/330386a0; RA Fainstein E., Marcelle C., Rosner A., Canaani E., Gale R.P., RA Dreazen O., Smith S.D., Croce C.M.; RT "A new fused transcript in Philadelphia chromosome positive acute RT lymphocytic leukaemia."; RL Nature 330:386-388(1987). RN [9] RP NUCLEOTIDE SEQUENCE OF 360-426. RX PubMed=6191223; DOI=10.1038/304167a0; RA Groffen J., Heisterkamp N., Reynolds F.H. Jr., Stephenson J.R.; RT "Homology between phosphotyrosine acceptor site of human c-abl and RT viral oncogene products."; RL Nature 304:167-169(1983). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 825-845. RX PubMed=7545908; RA Inokuchi K., Futaki M., Dan K., Nomura T.; RT "Sequence analysis of the mutation at codon 834 and the sequence RT variation of codon 837 of c-abl gene."; RL Leukemia 8:343-344(1994). RN [11] RP MYRISTOYLATION (ISOFORM IB). RX PubMed=2542016; RA Jackson P., Baltimore D.; RT "N-terminal mutations activate the leukemogenic potential of the RT myristoylated form of c-abl."; RL EMBO J. 8:449-456(1989). RN [12] RP DOMAIN, AND DNA-BINDING. RX PubMed=2183353; DOI=10.1126/science.2183353; RA Kipreos E.T., Wang J.Y.; RT "Differential phosphorylation of c-Abl in cell cycle determined by RT cdc2 kinase and phosphatase activity."; RL Science 248:217-220(1990). RN [13] RP FUNCTION. RX PubMed=9037071; DOI=10.1073/pnas.94.4.1437; RA Yuan Z.M., Huang Y., Ishiko T., Kharbanda S., Weichselbaum R., RA Kufe D.; RT "Regulation of DNA damage-induced apoptosis by the c-Abl tyrosine RT kinase."; RL Proc. Natl. Acad. Sci. U.S.A. 94:1437-1440(1997). RN [14] RP INTERACTION WITH RIN1, AND FUNCTION. RX PubMed=9144171; DOI=10.1073/pnas.94.10.4954; RA Han L., Wong D., Dhaka A., Afar D.E.H., White M., Xie W., RA Herschman H., Witte O., Colicelli J.; RT "Protein binding and signaling properties of RIN1 suggest a unique RT effector function."; RL Proc. Natl. Acad. Sci. U.S.A. 94:4954-4959(1997). RN [15] RP FUNCTION, AND INTERACTION WITH RAD51. RX PubMed=9461559; DOI=10.1074/jbc.273.7.3799; RA Yuan Z.M., Huang Y., Ishiko T., Nakada S., Utsugisawa T., RA Kharbanda S., Wang R., Sung P., Shinohara A., Weichselbaum R., RA Kufe D.; RT "Regulation of Rad51 function by c-Abl in response to DNA damage."; RL J. Biol. Chem. 273:3799-3802(1998). RN [16] RP INTERACTION WITH INPPL1. RX PubMed=10194451; RA Wisniewski D., Strife A., Swendeman S., Erdjument-Bromage H., RA Geromanos S., Kavanaugh W.M., Tempst P., Clarkson B.; RT "A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5- RT phosphatase (SHIP2) is constitutively tyrosine phosphorylated and RT associated with src homologous and collagen gene (SHC) in chronic RT myelogenous leukemia progenitor cells."; RL Blood 93:2707-2720(1999). RN [17] RP FUNCTION, ENZYME REGULATION, AND INTERACTION WITH TP73. RX PubMed=10391250; DOI=10.1038/21697; RA Agami R., Blandino G., Oren M., Shaul Y.; RT "Interaction of c-Abl and p73alpha and their collaboration to induce RT apoptosis."; RL Nature 399:809-813(1999). RN [18] RP DNA-BINDING. RX PubMed=10325413; DOI=10.1093/nar/27.11.2265; RA David-Cordonnier M.H., Payet D., D'Halluin J.C., Waring M.J., RA Travers A.A., Bailly C.; RT "The DNA-binding domain of human c-Abl tyrosine kinase promotes the RT interaction of a HMG chromosomal protein with DNA."; RL Nucleic Acids Res. 27:2265-2270(1999). RN [19] RP REVIEW ON FUNCTION. RX PubMed=11114745; DOI=10.1038/sj.onc.1203878; RA Wang J.Y.; RT "Regulation of cell death by the Abl tyrosine kinase."; RL Oncogene 19:5643-5650(2000). RN [20] RP INTERACTION WITH SORBS1. RX PubMed=11374898; DOI=10.1006/geno.2001.6541; RA Lin W.-H., Huang C.-J., Liu M.-W., Chang H.-M., Chen Y.-J., Tai T.-Y., RA Chuang L.-M.; RT "Cloning, mapping, and characterization of the human sorbin and SH3 RT domain containing 1 (SORBS1) gene: a protein associated with c-Abl RT during insulin signaling in the hepatoma cell line Hep3B."; RL Genomics 74:12-20(2001). RN [21] RP FUNCTION, AND INTERACTION WITH RAD52. RX PubMed=12379650; DOI=10.1074/jbc.M208151200; RA Kitao H., Yuan Z.M.; RT "Regulation of ionizing radiation-induced Rad52 nuclear foci formation RT by c-Abl-mediated phosphorylation."; RL J. Biol. Chem. 277:48944-48948(2002). RN [22] RP FUNCTION, AND INTERACTION WITH RAD9A. RX PubMed=11971963; DOI=10.1128/MCB.22.10.3292-3300.2002; RA Yoshida K., Komatsu K., Wang H.-G., Kufe D.; RT "c-Abl tyrosine kinase regulates the human Rad9 checkpoint protein in RT response to DNA damage."; RL Mol. Cell. Biol. 22:3292-3300(2002). RN [23] RP UBIQUITINATION. RX PubMed=12475393; DOI=10.1042/BJ20021539; RA Soubeyran P., Barac A., Szymkiewicz I., Dikic I.; RT "Cbl-ArgBP2 complex mediates ubiquitination and degradation of c- RT Abl."; RL Biochem. J. 370:29-34(2003). RN [24] RP FUNCTION. RX PubMed=12531427; DOI=10.1016/S0898-6568(02)00090-6; RA Sanguinetti A.R., Mastick C.C.; RT "c-Abl is required for oxidative stress-induced phosphorylation of RT caveolin-1 on tyrosine 14."; RL Cell. Signal. 15:289-298(2003). RN [25] RP FUNCTION. RX PubMed=12672821; DOI=10.1074/jbc.M301447200; RA Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H., RA Shishido T.; RT "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian RT enabled (Mena) by c-Abl kinase."; RL J. Biol. Chem. 278:21685-21692(2003). RN [26] RP REVIEW ON FUNCTION. RX PubMed=12775773; DOI=10.1242/jcs.00622; RA Woodring P.J., Hunter T., Wang J.Y.; RT "Regulation of F-actin-dependent processes by the Abl family of RT tyrosine kinases."; RL J. Cell Sci. 116:2613-2626(2003). RN [27] RP INTERACTION WITH BCR. RX PubMed=15302586; DOI=10.1016/j.yexcr.2004.05.010; RA Laurent C.E., Smithgall T.E.; RT "The c-Fes tyrosine kinase cooperates with the breakpoint cluster RT region protein (Bcr) to induce neurite extension in a Rac- and Cdc42- RT dependent manner."; RL Exp. Cell Res. 299:188-198(2004). RN [28] RP FUNCTION. RX PubMed=15556646; DOI=10.1016/j.febslet.2004.10.054; RA Grossmann A.H., Kolibaba K.S., Willis S.G., Corbin A.S., Langdon W.S., RA Deininger M.W., Druker B.J.; RT "Catalytic domains of tyrosine kinases determine the phosphorylation RT sites within c-Cbl."; RL FEBS Lett. 577:555-562(2004). RN [29] RP FUNCTION. RX PubMed=15031292; DOI=10.1074/jbc.M311479200; RA Perkinton M.S., Standen C.L., Lau K.F., Kesavapany S., Byers H.L., RA Ward M., McLoughlin D.M., Miller C.C.; RT "The c-Abl tyrosine kinase phosphorylates the Fe65 adaptor protein to RT stimulate Fe65/amyloid precursor protein nuclear signaling."; RL J. Biol. Chem. 279:22084-22091(2004). RN [30] RP REVIEW ON FUNCTION. RX PubMed=15686624; DOI=10.1038/sj.cr.7290261; RA Shaul Y., Ben-Yehoyada M.; RT "Role of c-Abl in the DNA damage stress response."; RL Cell Res. 15:33-35(2005). RN [31] RP FUNCTION. RX PubMed=15886098; DOI=10.1016/j.cub.2005.03.049; RA Hu H., Bliss J.M., Wang Y., Colicelli J.; RT "RIN1 is an ABL tyrosine kinase activator and a regulator of RT epithelial-cell adhesion and migration."; RL Curr. Biol. 15:815-823(2005). RN [32] RP FUNCTION, AND INTERACTION WITH CASP9. RX PubMed=15657060; DOI=10.1074/jbc.M413787200; RA Raina D., Pandey P., Ahmad R., Bharti A., Ren J., Kharbanda S., RA Weichselbaum R., Kufe D.; RT "c-Abl tyrosine kinase regulates caspase-9 autocleavage in the RT apoptotic response to DNA damage."; RL J. Biol. Chem. 280:11147-11151(2005). RN [33] RP INTERACTION WITH YWHAB; YWHAE; YWHAG; YWHAH; SFN AND YWHAZ, RP PHOSPHORYLATION AT THR-735, IDENTIFICATION BY MASS SPECTROMETRY, RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-735. RX PubMed=15696159; DOI=10.1038/ncb1228; RA Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.; RT "JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of RT c-Abl in the apoptotic response to DNA damage."; RL Nat. Cell Biol. 7:278-285(2005). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [35] RP ACETYLATION AT LYS-711, AND SUBCELLULAR LOCATION. RX PubMed=16648821; DOI=10.1038/sj.embor.7400700; RA di Bari M.G., Ciuffini L., Mingardi M., Testi R., Soddu S., Barila D.; RT "c-Abl acetylation by histone acetyltransferases regulates its RT nuclear-cytoplasmic localization."; RL EMBO Rep. 7:727-733(2006). RN [36] RP PHOSPHORYLATION AT TYR-70; TYR-115; TYR-128; TYR-139; TYR-172; TYR-185 RP TYR-215; TYR-226 AND TYR-393, INTERACTION WITH HCK; LYN AND FYN, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16912036; DOI=10.1074/jbc.M605902200; RA Meyn M.A. III, Wilson M.B., Abdi F.A., Fahey N., Schiavone A.P., RA Wu J., Hochrein J.M., Engen J.R., Smithgall T.E.; RT "Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and RT modulate Bcr-Abl transforming activity."; RL J. Biol. Chem. 281:30907-30916(2006). RN [37] RP FUNCTION. RX PubMed=16943190; DOI=10.1074/jbc.M603126200; RA Tanos B., Pendergast A.M.; RT "Abl tyrosine kinase regulates endocytosis of the epidermal growth RT factor receptor."; RL J. Biol. Chem. 281:32714-32723(2006). RN [38] RP FUNCTION, AND INTERACTION WITH PSMA7. RX PubMed=16678104; DOI=10.1016/j.molcel.2006.04.007; RA Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., RA Cao C.; RT "Interaction between c-Abl and Arg tyrosine kinases and proteasome RT subunit PSMA7 regulates proteasome degradation."; RL Mol. Cell 22:317-327(2006). RN [39] RP FUNCTION. RX PubMed=17306540; DOI=10.1016/j.cub.2007.01.057; RA Boyle S.N., Michaud G.A., Schweitzer B., Predki P.F., Koleske A.J.; RT "A critical role for cortactin phosphorylation by Abl-family kinases RT in PDGF-induced dorsal-wave formation."; RL Curr. Biol. 17:445-451(2007). RN [40] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WASF3. RX PubMed=17623672; DOI=10.1074/jbc.M701484200; RA Sossey-Alaoui K., Li X., Cowell J.K.; RT "c-Abl-mediated phosphorylation of WAVE3 is required for lamellipodia RT formation and cell migration."; RL J. Biol. Chem. 282:26257-26265(2007). RN [41] RP PHOSPHORYLATION AT SER-618 AND SER-619, AND INTERACTION WITH ABI2 AND RP CRK. RX PubMed=18161990; DOI=10.1021/bi701533j; RA Jung J.H., Pendergast A.M., Zipfel P.A., Traugh J.A.; RT "Phosphorylation of c-Abl by protein kinase Pak2 regulates RT differential binding of ABI2 and CRK."; RL Biochemistry 47:1094-1104(2008). RN [42] RP FUNCTION, AND ENZYME REGULATION. RX PubMed=18328268; DOI=10.1016/j.bbamcr.2008.01.028; RA Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X., RA Debnath A.K., Cowburn D., Kotula L.; RT "Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinase RT by phosphopeptides derived from Abi1/Hssh3bp1."; RL Biochim. Biophys. Acta 1783:737-747(2008). RN [43] RP FUNCTION. RX PubMed=18945674; DOI=10.1074/jbc.M804543200; RA Yogalingam G., Pendergast A.M.; RT "Abl kinases regulate autophagy by promoting the trafficking and RT function of lysosomal components."; RL J. Biol. Chem. 283:35941-35953(2008). RN [44] RP PHOSPHORYLATION AT TYR-70, AND INTERACTION WITH ABI1. RX PubMed=18775435; DOI=10.1016/j.jmb.2008.08.040; RA Chen S., O'Reilly L.P., Smithgall T.E., Engen J.R.; RT "Tyrosine phosphorylation in the SH3 domain disrupts negative RT regulatory interactions within the c-Abl kinase core."; RL J. Mol. Biol. 383:414-423(2008). RN [45] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-569; SER-659; RP THR-814; THR-844 AND SER-977, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [46] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569; THR-852 AND RP SER-917, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [47] RP REVIEW ON FUNCTION. RX PubMed=18182299; DOI=10.1016/j.tibs.2007.10.006; RA Backert S., Feller S.M., Wessler S.; RT "Emerging roles of Abl family tyrosine kinases in microbial RT pathogenesis."; RL Trends Biochem. Sci. 33:80-90(2008). RN [48] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [49] RP FUNCTION. RX PubMed=19891780; DOI=10.1186/1471-2121-10-80; RA Fernow I., Tomasovic A., Siehoff-Icking A., Tikkanen R.; RT "Cbl-associated protein is tyrosine phosphorylated by c-Abl and c-Src RT kinases."; RL BMC Cell Biol. 10:80-80(2009). RN [50] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [51] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-569, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [52] RP FUNCTION. RX PubMed=20417104; DOI=10.1016/j.cub.2010.03.048; RA Michael M., Vehlow A., Navarro C., Krause M.; RT "c-Abl, Lamellipodin, and Ena/VASP proteins cooperate in dorsal RT ruffling of fibroblasts and axonal morphogenesis."; RL Curr. Biol. 20:783-791(2010). RN [53] RP INTERACTION WITH MYLK AND CTTN. RX PubMed=20861316; DOI=10.1091/mbc.E09-10-0876; RA Dudek S.M., Chiang E.T., Camp S.M., Guo Y., Zhao J., Brown M.E., RA Singleton P.A., Wang L., Desai A., Arce F.T., Lal R., Van Eyk J.E., RA Imam S.Z., Garcia J.G.N.; RT "Abl tyrosine kinase phosphorylates nonmuscle Myosin light chain RT kinase to regulate endothelial barrier function."; RL Mol. Biol. Cell 21:4042-4056(2010). RN [54] RP REVIEW ON FUNCTION, AND DOMAIN. RX PubMed=20841568; DOI=10.1126/scisignal.3139re6; RA Colicelli J.; RT "ABL tyrosine kinases: evolution of function, regulation, and RT specificity."; RL Sci. Signal. 3:RE6-RE6(2010). RN [55] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [56] RP INTERACTION WITH STX17. RX PubMed=23006999; DOI=10.1016/j.bbamcr.2012.09.003; RA Muppirala M., Gupta V., Swarup G.; RT "Tyrosine phosphorylation of a SNARE protein, Syntaxin 17: RT Implications for membrane trafficking in the early secretory RT pathway."; RL Biochim. Biophys. Acta 1823:2109-2119(2012). RN [57] RP STRUCTURE BY NMR OF SH2 DOMAIN. RX PubMed=1505033; DOI=10.1016/0092-8674(92)90437-H; RA Overduin M., Rios C.B., Mayer B.J., Baltimore D., Cowburn D.; RT "Three-dimensional solution structure of the src homology 2 domain of RT c-abl."; RL Cell 70:697-704(1992). RN [58] RP STRUCTURE BY NMR OF SH2 DOMAIN. RX PubMed=1281542; DOI=10.1073/pnas.89.24.11673; RA Overduin M., Mayer B.J., Rios C.B., Baltimore D., Cowburn D.; RT "Secondary structure of Src homology 2 domain of c-Abl by RT heteronuclear NMR spectroscopy in solution."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11673-11677(1992). RN [59] RP 3D-STRUCTURE MODELING OF SH3 DOMAIN. RX PubMed=7892170; DOI=10.1002/prot.340200302; RA Pisabarro M.T., Ortiz A.R., Serrano L., Wade R.C.; RT "Homology modeling of the Abl-SH3 domain."; RL Proteins 20:203-215(1994). RN [60] RP STRUCTURE BY NMR OF SH3 DOMAIN. RX PubMed=8590002; DOI=10.1016/S0969-2126(01)00243-X; RA Gosser Y.Q., Zheng J., Overduin M., Mayer B.J., Cowburn D.; RT "The solution structure of Abl SH3, and its relationship to SH2 in the RT SH(32) construct."; RL Structure 3:1075-1086(1995). RN [61] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 64-121. RX PubMed=9698566; DOI=10.1006/jmbi.1998.1932; RA Pisabarro M.T., Serrano L., Wilmanns M.; RT "Crystal structure of the abl-SH3 domain complexed with a designed RT high-affinity peptide ligand: implications for SH3-ligand RT interactions."; RL J. Mol. Biol. 281:513-521(1998). RN [62] RP STRUCTURE BY NMR OF 62-122 IN COMPLEX WITH CRK. RX PubMed=12384576; DOI=10.1073/pnas.212518799; RA Donaldson L.W., Gish G., Pawson T., Kay L.E., Forman-Kay J.D.; RT "Structure of a regulatory complex involving the Abl SH3 domain, the RT Crk SH2 domain, and a Crk-derived phosphopeptide."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14053-14058(2002). RN [63] RP X-RAY CRYSTALLOGRAPHY (3.42 ANGSTROMS) OF 27-512, MYRISTOYLATION RP (ISOFORM IB), ENZYME REGULATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=12654251; DOI=10.1016/S0092-8674(03)00194-6; RA Nagar B., Hantschel O., Young M.A., Scheffzek K., Veach D., RA Bornmann W., Clarkson B., Superti-Furga G., Kuriyan J.; RT "Structural basis for the autoinhibition of c-Abl tyrosine kinase."; RL Cell 112:859-871(2003). RN [64] RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 229-513 OF MUTANT PRO-396 IN RP COMPLEX WITH INHIBITOR VX-680, FUNCTION, AND ENZYME REGULATION. RX PubMed=16424036; DOI=10.1158/0008-5472.CAN-05-2788; RA Young M.A., Shah N.P., Chao L.H., Seeliger M., Milanov Z.V., RA Biggs W.H. III, Treiber D.K., Patel H.K., Zarrinkar P.P., RA Lockhart D.J., Sawyers C.L., Kuriyan J.; RT "Structure of the kinase domain of an imatinib-resistant Abl mutant in RT complex with the Aurora kinase inhibitor VX-680."; RL Cancer Res. 66:1007-1014(2006). RN [65] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 38-512, IDENTIFICATION BY RP MASS SPECTROMETRY, MYRISTOYLATION OF N-TERMINUS (ISOFORM IB), RP PHOSPHORYLATION AT SER-50, AUTOINHIBITORY MECHANISM, AND ENZYME RP REGULATION. RX PubMed=16543148; DOI=10.1016/j.molcel.2006.01.035; RA Nagar B., Hantschel O., Seeliger M., Davies J.M., Weis W.I., RA Superti-Furga G., Kuriyan J.; RT "Organization of the SH3-SH2 unit in active and inactive forms of the RT c-Abl tyrosine kinase."; RL Mol. Cell 21:787-798(2006). RN [66] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 229-512 IN COMPLEXES WITH RP ATP-PEPTIDE CONJUGATE, AND CONFORMATION CHANGES DURING ACTIVATION. RX PubMed=16640460; DOI=10.1371/journal.pbio.0040144; RA Levinson N.M., Kuchment O., Shen K., Young M.A., Koldobskiy M., RA Karplus M., Cole P.A., Kuriyan J.; RT "A Src-like inactive conformation in the abl tyrosine kinase domain."; RL PLoS Biol. 4:E144-E144(2006). RN [67] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 229-500 IN COMPLEXES WITH RP IMATINIB AND WITH THE INHIBITORS NVP-AEG082; NVP-AFN941; NVP-AFG210 RP AND PD180970. RX PubMed=17164530; DOI=10.1107/S0907444906047287; RA Cowan-Jacob S.W., Fendrich G., Floersheimer A., Furet P., RA Liebetanz J., Rummel G., Rheinberger P., Centeleghe M., Fabbro D., RA Manley P.W.; RT "Structural biology contributions to the discovery of drugs to treat RT chronic myelogenous leukaemia."; RL Acta Crystallogr. D 63:80-93(2007). RN [68] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 64-121 OF MUTANT ALA-114 IN RP COMPLEX WITH PROLINE-RICH PEPTIDE. RX PubMed=17452790; DOI=10.1107/S0907444907011109; RA Camara-Artigas A., Palencia A., Martinez J.C., Luque I., Gavira J.A., RA Garcia-Ruiz J.M.; RT "Crystallization by capillary counter-diffusion and structure RT determination of the N114A mutant of the SH3 domain of Abl tyrosine RT kinase complexed with a high-affinity peptide ligand."; RL Acta Crystallogr. D 63:646-652(2007). RN [69] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 60-121 IN COMPLEX WITH RP PROLINE-RICH PEPTIDE P41. RX PubMed=19906645; DOI=10.1074/jbc.M109.048033; RA Palencia A., Camara-Artigas A., Pisabarro M.T., Martinez J.C., RA Luque I.; RT "Role of interfacial water molecules in proline-rich ligand RT recognition by the Src homology 3 domain of Abl."; RL J. Biol. Chem. 285:2823-2833(2010). RN [70] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 121-232 IN COMPLEX WITH RP ANTIBODY MIMIC HA4, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20357770; DOI=10.1038/nsmb.1793; RA Wojcik J., Hantschel O., Grebien F., Kaupe I., Bennett K.L., RA Barkinge J., Jones R.B., Koide A., Superti-Furga G., Koide S.; RT "A potent and highly specific FN3 monobody inhibitor of the Abl SH2 RT domain."; RL Nat. Struct. Mol. Biol. 17:519-527(2010). RN [71] RP VARIANTS GLY-47; LYS-166; VAL-706; LEU-810 AND LEU-972. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays a role CC in many key processes linked to cell growth and survival such as CC cytoskeleton remodeling in response to extracellular stimuli, cell CC motility and adhesion, receptor endocytosis, autophagy, DNA damage CC response and apoptosis. Coordinates actin remodeling through CC tyrosine phosphorylation of proteins controlling cytoskeleton CC dynamics like WASF3 (involved in branch formation); ANXA1 CC (involved in membrane anchoring); DBN1, DBNL, CTTN, RAPH1 and ENAH CC (involved in signaling); or MAPT and PXN (microtubule-binding CC proteins). Phosphorylation of WASF3 is critical for the CC stimulation of lamellipodia formation and cell migration. Involved CC in the regulation of cell adhesion and motility through CC phosphorylation of key regulators of these processes such as CC BCAR1, CRK, CRKL, DOK1, EFS or NEDD9. Phosphorylates multiple CC receptor tyrosine kinases and more particularly promotes CC endocytosis of EGFR, facilitates the formation of neuromuscular CC synapses through MUSK, inhibits PDGFRB-mediated chemotaxis and CC modulates the endocytosis of activated B-cell receptor complexes. CC Other substrates which are involved in endocytosis regulation are CC the caveolin (CAV1) and RIN1. Moreover, ABL1 regulates the CBL CC family of ubiquitin ligases that drive receptor down-regulation CC and actin remodeling. Phosphorylation of CBL leads to increased CC EGFR stability. Involved in late-stage autophagy by regulating CC positively the trafficking and function of lysosomal components. CC ABL1 targets to mitochondria in response to oxidative stress and CC thereby mediates mitochondrial dysfunction and cell death. ABL1 is CC also translocated in the nucleus where it has DNA-binding activity CC and is involved in DNA-damage response and apoptosis. Many CC substrates are known mediators of DNA repair: DDB1, DDB2, ERCC3, CC ERCC6, RAD9A, RAD51, RAD52 or WRN. Activates the proapoptotic CC pathway when the DNA damage is too severe to be repaired. CC Phosphorylates TP73, a primary regulator for this type of damage- CC induced apoptosis. Phosphorylates the caspase CASP9 on 'Tyr-153' CC and regulates its processing in the apoptotic response to DNA CC damage. Phosphorylates PSMA7 that leads to an inhibition of CC proteasomal activity and cell cycle transition blocks. ABL1 acts CC also as a regulator of multiple pathological signaling cascades CC during infection. Several known tyrosine-phosphorylated microbial CC proteins have been identified as ABL1 substrates. This is the case CC of A36R of Vaccinia virus, Tir (translocated intimin receptor) of CC pathogenic E.coli and possibly Citrobacter, CagA (cytotoxin- CC associated gene A) of H.pylori, or AnkA (ankyrin repeat-containing CC protein A) of A.phagocytophilum. Pathogens can highjack ABL1 CC kinase signaling to reorganize the host actin cytoskeleton for CC multiple purposes, like facilitating intracellular movement and CC host cell exit. Finally, functions as its own regulator through CC autocatalytic activity as well as through phosphorylation of its CC inhibitor, ABI1. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. CC -!- COFACTOR: Magnesium or manganese. CC -!- ENZYME REGULATION: Stabilized in the inactive form by an CC association between the SH3 domain and the SH2-TK linker region, CC interactions of the N-terminal cap, and contributions from an N- CC terminal myristoyl group and phospholipids. Activated by CC autophosphorylation as well as by SRC-family kinase-mediated CC phosphorylation. Activated by RIN1 binding to the SH2 and SH3 CC domains. Also stimulated by cell death inducers and DNA-damage. CC Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant CC phosphoinositide known to regulate cytoskeletal and membrane CC proteins, inhibits also the tyrosine kinase activity (By CC similarity). Inhibited by ABI1, whose activity is controlled by CC ABL1 itself through tyrosine phosphorylation. Also inhibited by CC imatinib mesylate (Gleevec) which is used for the treatment of CC chronic myeloid leukemia (CML), and by VX-680, an inhibitor that CC acts also on imatinib-resistant mutants. CC -!- SUBUNIT: Interacts with SORBS1 following insulin stimulation. CC Found in a trimolecular complex containing CDK5 and CABLES1. CC Interacts with CABLES1 and PSTPIP1. Interacts with ZDHHC16, ITGB1 CC and HCK (By similarity). Interacts with STX17; probably CC phosphorylates STX17. Interacts with INPPL1/SHIP2. Interacts with CC the 14-3-3 proteins, YWHAB, YWHAE, YWHAG, YWHAH, SFN AND YWHAZ; CC the interaction with 14-3-3 proteins requires phosphorylation on CC Thr-735 and, sequesters ABL1 into the cytoplasm. Interacts with CC ABI1, ABI2, BCR, CRK, FGR, FYN, HCK, LYN, PSMA7 RAD9A, RAD51, CC RAD52, TP73 and WASF3. A complex made of ABL1, CTTN and MYLK CC regulates cortical actin-based cytoskeletal rearrangement critical CC to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) CC barrier enhancement. Interacts (via SH3 domain) with CASP9; the CC interaction is direct and increases in the response of cells to CC genotoxic stress and ABL1/c-Abl activation. CC -!- INTERACTION: CC Q8IZP0:ABI1; NbExp=11; IntAct=EBI-375543, EBI-375446; CC Q9NYB9:ABI2; NbExp=2; IntAct=EBI-375543, EBI-743598; CC P10275:AR; NbExp=2; IntAct=EBI-375543, EBI-608057; CC Q4KMG0:CDON; NbExp=2; IntAct=EBI-375543, EBI-7016840; CC O35158:Cdon (xeno); NbExp=4; IntAct=EBI-375543, EBI-7016767; CC P46108:CRK; NbExp=2; IntAct=EBI-375543, EBI-886; CC P46109:CRKL; NbExp=2; IntAct=EBI-375543, EBI-910; CC P35222:CTNNB1; NbExp=2; IntAct=EBI-375543, EBI-491549; CC P04626:ERBB2; NbExp=2; IntAct=EBI-375543, EBI-641062; CC Q14315:FLNC; NbExp=2; IntAct=EBI-375543, EBI-489954; CC P05107:ITGB2; NbExp=4; IntAct=EBI-375543, EBI-300173; CC P10721:KIT; NbExp=2; IntAct=EBI-375543, EBI-1379503; CC Q92918:MAP4K1; NbExp=3; IntAct=EBI-375543, EBI-881; CC Q7Z434:MAVS; NbExp=6; IntAct=EBI-375543, EBI-995373; CC O43196:MSH5; NbExp=10; IntAct=EBI-375543, EBI-6092730; CC P15941:MUC1; NbExp=8; IntAct=EBI-375543, EBI-2804728; CC P16333:NCK1; NbExp=2; IntAct=EBI-375543, EBI-389883; CC O43900:PRICKLE3; NbExp=2; IntAct=EBI-375543, EBI-1751761; CC Q13905:RAPGEF1; NbExp=4; IntAct=EBI-375543, EBI-976876; CC Q86UR5:RIMS1; NbExp=2; IntAct=EBI-375543, EBI-1043236; CC Q13671:RIN1; NbExp=4; IntAct=EBI-375543, EBI-366017; CC P31947:SFN; NbExp=2; IntAct=EBI-375543, EBI-476295; CC Q15464:SHB; NbExp=5; IntAct=EBI-375543, EBI-4402156; CC O75751:SLC22A3; NbExp=2; IntAct=EBI-375543, EBI-1752674; CC Q9BX66:SORBS1; NbExp=2; IntAct=EBI-375543, EBI-433642; CC O60504-2:SORBS3; NbExp=5; IntAct=EBI-375543, EBI-1222956; CC Q07890:SOS2; NbExp=2; IntAct=EBI-375543, EBI-298181; CC P12931:SRC; NbExp=2; IntAct=EBI-375543, EBI-621482; CC Q9Y4G6:TLN2; NbExp=3; IntAct=EBI-375543, EBI-1220811; CC P11387:TOP1; NbExp=7; IntAct=EBI-375543, EBI-876302; CC P15498:VAV1; NbExp=5; IntAct=EBI-375543, EBI-625518; CC P63104:YWHAZ; NbExp=2; IntAct=EBI-375543, EBI-347088; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. CC Mitochondrion (By similarity). Note=Shuttles between the nucleus CC and cytoplasm depending on environmental signals. Sequestered into CC the cytoplasm through interaction with 14-3-3 proteins. Localizes CC to mitochondria in response to oxidative stress (By similarity). CC -!- SUBCELLULAR LOCATION: Isoform IB: Nucleus membrane; Lipid-anchor. CC Note=The myristoylated c-ABL protein is reported to be nuclear. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=IA; CC IsoId=P00519-1; Sequence=Displayed; CC Name=IB; CC IsoId=P00519-2; Sequence=VSP_004957; CC Note=Contains a N-myristoyl glycine at position 2; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- PTM: Acetylated at Lys-711 by EP300 which promotes the cytoplasmic CC translocation. CC -!- PTM: Phosphorylation at Tyr-70 by members of the SRC family of CC kinases disrupts SH3 domain-based autoinhibitory interactions and CC intermolecular associations, such as that with ABI1, and also CC enhances kinase activity. Phosphorylation at Tyr-226 and Tyr-393 CC correlate with increased activity. DNA damage-induced activation CC of ABL1 requires the function of ATM and Ser-446 phosphorylation CC (By similarity). Phosphorylation at Ser-569 has been attributed to CC a CDC2-associated kinase and is coupled to cell division (By CC similarity). Phosphorylation at Ser-618 and Ser-619 by PAK2 CC increases binding to CRK and reduces binding to ABI1. CC Phosphorylation on Thr-735 is required for binding 14-3-3 proteins CC for cytoplasmic translocation. Phosphorylated by PRKDC (By CC similarity). CC -!- PTM: Polyubiquitinated. Polyubiquitination of ABL1 leads to CC degradation. CC -!- PTM: Isoform IB is myristoylated on Gly-2. CC -!- DISEASE: Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal CC myeloproliferative disorder of a pluripotent stem cell with a CC specific cytogenetic abnormality, the Philadelphia chromosome CC (Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid, CC and sometimes T-lymphoid cells, but not marrow fibroblasts. CC Note=The gene represented in this entry is involved in disease CC pathogenesis. CC -!- DISEASE: Note=A chromosomal aberration involving ABL1 has been CC found in patients with chronic myeloid leukemia. Translocation CC t(9;22)(q34;q11) with BCR. The translocation produces a BCR-ABL CC found also in acute myeloid leukemia (AML) and acute lymphoblastic CC leukemia (ALL). CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. ABL subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SIMILARITY: Contains 1 SH2 domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/ABL.html"; CC -!- WEB RESOURCE: Name=CGP resequencing studies; CC URL="http://www.sanger.ac.uk/perl/genetics/CGP/cgp_viewer?action=gene&ln=ABL1"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/abl1/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Abl entry; CC URL="http://en.wikipedia.org/wiki/Abl_gene"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M14752; AAA51561.1; -; mRNA. DR EMBL; X16416; CAA34438.1; -; mRNA. DR EMBL; U07563; AAB60394.1; -; Genomic_DNA. DR EMBL; U07563; AAB60393.1; -; Genomic_DNA. DR EMBL; U07561; AAB60393.1; JOINED; Genomic_DNA. DR EMBL; DQ145721; AAZ38718.1; -; Genomic_DNA. DR EMBL; AL359092; CAM45752.1; -; Genomic_DNA. DR EMBL; AL161733; CAM45752.1; JOINED; Genomic_DNA. DR EMBL; AL161733; CAM45754.1; -; Genomic_DNA. DR EMBL; AL161733; CAM45756.1; -; Genomic_DNA. DR EMBL; AL359092; CAM45756.1; JOINED; Genomic_DNA. DR EMBL; CH471090; EAW87948.1; -; Genomic_DNA. DR EMBL; BC117451; AAI17452.1; -; mRNA. DR EMBL; S69223; AAD14034.1; -; Genomic_DNA. DR CCDS; CCDS35165.1; -. [P00519-2] DR CCDS; CCDS35166.1; -. [P00519-1] DR PIR; S08519; TVHUA. DR RefSeq; NP_005148.2; NM_005157.4. [P00519-1] DR RefSeq; NP_009297.2; NM_007313.2. [P00519-2] DR UniGene; Hs.431048; -. DR PDB; 1AB2; NMR; -; A=120-220. DR PDB; 1ABL; Model; -; A=65-121. DR PDB; 1AWO; NMR; -; A=65-119. DR PDB; 1BBZ; X-ray; 1.65 A; A/C/E/G=64-121. DR PDB; 1JU5; NMR; -; C=62-122. DR PDB; 1OPL; X-ray; 3.42 A; A/B=27-512. DR PDB; 1ZZP; NMR; -; A=1007-1130. DR PDB; 2ABL; X-ray; 2.50 A; A=57-218. DR PDB; 2E2B; X-ray; 2.20 A; A/B=229-515. DR PDB; 2F4J; X-ray; 1.91 A; A=229-513. DR PDB; 2FO0; X-ray; 2.27 A; A=38-512. DR PDB; 2G1T; X-ray; 1.80 A; A/B/C/D=229-512. DR PDB; 2G2F; X-ray; 2.70 A; A/B=229-512. DR PDB; 2G2H; X-ray; 2.00 A; A/B=229-512. DR PDB; 2G2I; X-ray; 3.12 A; A/B=229-512. DR PDB; 2GQG; X-ray; 2.40 A; A/B=229-500. DR PDB; 2HIW; X-ray; 2.20 A; A/B=230-512. DR PDB; 2HYY; X-ray; 2.40 A; A/B/C/D=228-500. DR PDB; 2HZ0; X-ray; 2.10 A; A/B=228-497. DR PDB; 2HZ4; X-ray; 2.80 A; A/B/C=228-500. DR PDB; 2HZI; X-ray; 1.70 A; A/B=229-500. DR PDB; 2O88; X-ray; 1.75 A; A/B=64-121. DR PDB; 2V7A; X-ray; 2.50 A; A/B=229-512. DR PDB; 3CS9; X-ray; 2.21 A; A/B/C/D=229-500. DR PDB; 3EG0; X-ray; 2.30 A; A=60-121. DR PDB; 3EG1; X-ray; 1.85 A; A/B=60-121. DR PDB; 3EG2; X-ray; 1.80 A; A=60-121. DR PDB; 3EG3; X-ray; 1.40 A; A=60-121. DR PDB; 3EGU; X-ray; 2.25 A; A=60-121. DR PDB; 3K2M; X-ray; 1.75 A; A/B=121-232. DR PDB; 3PYY; X-ray; 1.85 A; A/B=229-512. DR PDB; 3QRI; X-ray; 2.10 A; A/B=229-499. DR PDB; 3QRJ; X-ray; 1.82 A; A/B=229-499. DR PDB; 3QRK; X-ray; 2.30 A; A=229-499. DR PDB; 3T04; X-ray; 2.10 A; A=112-232. DR PDB; 3UE4; X-ray; 2.42 A; A/B=229-512. DR PDB; 3UYO; X-ray; 1.83 A; A=112-232. DR PDB; 4J9B; X-ray; 1.70 A; A=60-121. DR PDB; 4J9C; X-ray; 1.05 A; A=60-121. DR PDB; 4J9D; X-ray; 1.50 A; A/C/E=60-121. DR PDB; 4J9E; X-ray; 1.40 A; A/C/E=60-121. DR PDB; 4J9F; X-ray; 1.09 A; A/C/E=60-121. DR PDB; 4J9G; X-ray; 1.80 A; A/C/E=60-121. DR PDB; 4J9H; X-ray; 1.70 A; A/B/C/D/E/F=60-121. DR PDB; 4J9I; X-ray; 2.20 A; A/C/E=60-121. DR PDB; 4JJB; X-ray; 1.65 A; A=60-121. DR PDB; 4JJC; X-ray; 1.60 A; A=60-121. DR PDB; 4JJD; X-ray; 1.60 A; A=60-121. DR PDBsum; 1AB2; -. DR PDBsum; 1ABL; -. DR PDBsum; 1AWO; -. DR PDBsum; 1BBZ; -. DR PDBsum; 1JU5; -. DR PDBsum; 1OPL; -. DR PDBsum; 1ZZP; -. DR PDBsum; 2ABL; -. DR PDBsum; 2E2B; -. DR PDBsum; 2F4J; -. DR PDBsum; 2FO0; -. DR PDBsum; 2G1T; -. DR PDBsum; 2G2F; -. DR PDBsum; 2G2H; -. DR PDBsum; 2G2I; -. DR PDBsum; 2GQG; -. DR PDBsum; 2HIW; -. DR PDBsum; 2HYY; -. DR PDBsum; 2HZ0; -. DR PDBsum; 2HZ4; -. DR PDBsum; 2HZI; -. DR PDBsum; 2O88; -. DR PDBsum; 2V7A; -. DR PDBsum; 3CS9; -. DR PDBsum; 3EG0; -. DR PDBsum; 3EG1; -. DR PDBsum; 3EG2; -. DR PDBsum; 3EG3; -. DR PDBsum; 3EGU; -. DR PDBsum; 3K2M; -. DR PDBsum; 3PYY; -. DR PDBsum; 3QRI; -. DR PDBsum; 3QRJ; -. DR PDBsum; 3QRK; -. DR PDBsum; 3T04; -. DR PDBsum; 3UE4; -. DR PDBsum; 3UYO; -. DR PDBsum; 4J9B; -. DR PDBsum; 4J9C; -. DR PDBsum; 4J9D; -. DR PDBsum; 4J9E; -. DR PDBsum; 4J9F; -. DR PDBsum; 4J9G; -. DR PDBsum; 4J9H; -. DR PDBsum; 4J9I; -. DR PDBsum; 4JJB; -. DR PDBsum; 4JJC; -. DR PDBsum; 4JJD; -. DR ProteinModelPortal; P00519; -. DR SMR; P00519; 46-528, 1024-1130. DR BioGrid; 106543; 138. DR DIP; DIP-1042N; -. DR IntAct; P00519; 198. DR MINT; MINT-7236141; -. DR STRING; 9606.ENSP00000361423; -. DR BindingDB; P00519; -. DR ChEMBL; CHEMBL1862; -. DR DrugBank; DB00171; Adenosine triphosphate. DR DrugBank; DB01254; Dasatinib. DR DrugBank; DB00619; Imatinib. DR GuidetoPHARMACOLOGY; 1923; -. DR PhosphoSite; P00519; -. DR DMDM; 85681908; -. DR MaxQB; P00519; -. DR PaxDb; P00519; -. DR PRIDE; P00519; -. DR DNASU; 25; -. DR Ensembl; ENST00000318560; ENSP00000323315; ENSG00000097007. [P00519-1] DR Ensembl; ENST00000372348; ENSP00000361423; ENSG00000097007. [P00519-2] DR GeneID; 25; -. DR KEGG; hsa:25; -. DR UCSC; uc004bzv.3; human. [P00519-2] DR UCSC; uc004bzw.3; human. [P00519-1] DR CTD; 25; -. DR GeneCards; GC09P133589; -. DR HGNC; HGNC:76; ABL1. DR HPA; CAB002686; -. DR HPA; HPA027251; -. DR HPA; HPA027280; -. DR HPA; HPA028409; -. DR MIM; 189980; gene. DR MIM; 608232; phenotype. DR neXtProt; NX_P00519; -. DR Orphanet; 521; Chronic myeloid leukemia. DR Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia. DR Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia. DR PharmGKB; PA24413; -. DR eggNOG; COG0515; -. DR HOVERGEN; HBG004162; -. DR KO; K06619; -. DR OMA; GAFRESG; -. DR OrthoDB; EOG7GTT2V; -. DR PhylomeDB; P00519; -. DR TreeFam; TF105081; -. DR BRENDA; 2.7.10.2; 2681. DR Reactome; REACT_111045; Developmental Biology. DR Reactome; REACT_604; Hemostasis. DR Reactome; REACT_6900; Immune System. DR SignaLink; P00519; -. DR ChiTaRS; ABL1; human. DR EvolutionaryTrace; P00519; -. DR GeneWiki; ABL_(gene); -. DR GenomeRNAi; 25; -. DR NextBio; 79; -. DR PMAP-CutDB; P00519; -. DR PRO; PR:P00519; -. DR ArrayExpress; P00519; -. DR Bgee; P00519; -. DR CleanEx; HS_ABL1; -. DR Genevestigator; P00519; -. DR GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB. DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0003785; F:actin monomer binding; TAS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:BHF-UCL. DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; TAS:UniProtKB. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0070064; F:proline-rich region binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB. DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB. DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0006464; P:cellular protein modification process; NAS:UniProtKB. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB. DR GO; GO:0006975; P:DNA damage induced protein phosphorylation; IDA:UniProtKB. DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; TAS:UniProtKB. DR GO; GO:0006298; P:mismatch repair; TAS:ProtInc. DR GO; GO:0042692; P:muscle cell differentiation; TAS:Reactome. DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IDA:BHF-UCL. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome. DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IDA:BHF-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; TAS:UniProtKB. DR GO; GO:0010506; P:regulation of autophagy; TAS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl. DR GO; GO:2000145; P:regulation of cell motility; TAS:UniProtKB. DR GO; GO:0030100; P:regulation of endocytosis; TAS:UniProtKB. DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc. DR GO; GO:0042770; P:signal transduction in response to DNA damage; IDA:UniProtKB. DR Gene3D; 3.30.505.10; -; 1. DR InterPro; IPR015015; F-actin_binding. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR Pfam; PF08919; F_actin_bind; 1. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00808; FABD; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF50044; SSF50044; 1. DR SUPFAM; SSF55550; SSF55550; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; KW ATP-binding; Autophagy; Cell adhesion; Chromosomal rearrangement; KW Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair; KW DNA-binding; Endocytosis; Kinase; Lipoprotein; Magnesium; Manganese; KW Membrane; Metal-binding; Mitochondrion; Myristate; Nucleotide-binding; KW Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; KW Reference proteome; SH2 domain; SH3 domain; Transferase; KW Tyrosine-protein kinase; Ubl conjugation. FT CHAIN 1 1130 Tyrosine-protein kinase ABL1. FT /FTId=PRO_0000088050. FT DOMAIN 61 121 SH3. FT DOMAIN 127 217 SH2. FT DOMAIN 242 493 Protein kinase. FT NP_BIND 248 256 ATP. FT NP_BIND 316 322 ATP. FT REGION 1 60 CAP. FT REGION 869 968 DNA-binding (By similarity). FT REGION 953 1130 F-actin-binding. FT MOTIF 381 405 Kinase activation loop. FT MOTIF 605 609 Nuclear localization signal 1 FT (Potential). FT MOTIF 709 715 Nuclear localization signal 2 FT (Potential). FT MOTIF 762 769 Nuclear localization signal 3 FT (Potential). FT MOTIF 1090 1100 Nuclear export signal (By similarity). FT COMPBIAS 18 22 Poly-Ser. FT COMPBIAS 605 609 Poly-Lys. FT COMPBIAS 782 1019 Pro-rich. FT COMPBIAS 897 903 Poly-Pro. FT ACT_SITE 363 363 Proton acceptor (By similarity). FT BINDING 271 271 ATP. FT SITE 26 27 Breakpoint for translocation to form BCR- FT ABL oncogene. FT MOD_RES 50 50 Phosphoserine. FT MOD_RES 70 70 Phosphotyrosine; by autocatalysis. FT MOD_RES 115 115 Phosphotyrosine. FT MOD_RES 128 128 Phosphotyrosine. FT MOD_RES 139 139 Phosphotyrosine. FT MOD_RES 172 172 Phosphotyrosine. FT MOD_RES 185 185 Phosphotyrosine. FT MOD_RES 215 215 Phosphotyrosine. FT MOD_RES 226 226 Phosphotyrosine; by autocatalysis. FT MOD_RES 253 253 Phosphotyrosine. FT MOD_RES 257 257 Phosphotyrosine. FT MOD_RES 264 264 Phosphotyrosine. FT MOD_RES 392 392 Phosphothreonine. FT MOD_RES 393 393 Phosphotyrosine; by autocatalysis and FT SRC-type Tyr-kinases. FT MOD_RES 394 394 Phosphothreonine. FT MOD_RES 446 446 Phosphoserine (By similarity). FT MOD_RES 469 469 Phosphotyrosine. FT MOD_RES 569 569 Phosphoserine. FT MOD_RES 613 613 Phosphothreonine. FT MOD_RES 618 618 Phosphoserine; by PAK2. FT MOD_RES 619 619 Phosphoserine; by PAK2. FT MOD_RES 620 620 Phosphoserine. FT MOD_RES 659 659 Phosphoserine. FT MOD_RES 683 683 Phosphoserine. FT MOD_RES 711 711 N6-acetyllysine; by EP300. FT MOD_RES 718 718 Phosphoserine. FT MOD_RES 735 735 Phosphothreonine. FT MOD_RES 781 781 Phosphothreonine. FT MOD_RES 805 805 Phosphoserine. FT MOD_RES 809 809 Phosphoserine. FT MOD_RES 814 814 Phosphothreonine. FT MOD_RES 844 844 Phosphothreonine. FT MOD_RES 852 852 Phosphothreonine. FT MOD_RES 855 855 Phosphoserine. FT MOD_RES 917 917 Phosphoserine. FT MOD_RES 919 919 Phosphoserine. FT MOD_RES 936 936 Phosphoserine. FT MOD_RES 949 949 Phosphoserine. FT MOD_RES 977 977 Phosphoserine. FT VAR_SEQ 1 26 MLEICLKLVGCKSKKGLSSSSSCYLE -> MGQQPGKVLGD FT QRRPSLPALHFIKGAGKKESSRHGGPHCNVFVEH (in FT isoform IB). FT /FTId=VSP_004957. FT VARIANT 47 47 R -> G (in a lung large cell carcinoma FT sample; somatic mutation). FT /FTId=VAR_032676. FT VARIANT 140 140 L -> P (in dbSNP:rs1064152). FT /FTId=VAR_051692. FT VARIANT 166 166 R -> K (in a melanoma sample; somatic FT mutation). FT /FTId=VAR_032677. FT VARIANT 247 247 K -> R (in dbSNP:rs34549764). FT /FTId=VAR_051693. FT VARIANT 706 706 G -> V (in dbSNP:rs34634745). FT /FTId=VAR_025043. FT VARIANT 810 810 P -> L (in dbSNP:rs2229071). FT /FTId=VAR_032678. FT VARIANT 852 852 T -> P. FT /FTId=VAR_025044. FT VARIANT 900 900 P -> S (in dbSNP:rs35266696). FT /FTId=VAR_025045. FT VARIANT 968 968 S -> P (in dbSNP:rs1064165). FT /FTId=VAR_051694. FT VARIANT 972 972 S -> L (in dbSNP:rs2229067). FT /FTId=VAR_025046. FT MUTAGEN 735 735 T->A: Abolishes phosphorylation. Loss of FT binding YWHAS and YWHAZ. Localizes to the FT nucleus. No effect on kinase activity. FT CONFLICT 159 159 G -> S (in Ref. 1; AAA51561). FT CONFLICT 424 425 AF -> GK (in Ref. 9). FT CONFLICT 445 445 L -> R (in Ref. 1; AAA51561). FT CONFLICT 459 459 E -> K (in Ref. 1; AAA51561). FT CONFLICT 520 520 S -> T (in Ref. 1; AAA51561). FT CONFLICT 719 719 A -> V (in Ref. 1; AAA51561). FT CONFLICT 837 837 G -> E (in Ref. 2; CAA34438). FT CONFLICT 837 837 G -> W (in Ref. 1; AAA51561). FT CONFLICT 863 863 G -> R (in Ref. 1; AAA51561). FT CONFLICT 894 894 R -> K (in Ref. 1; AAA51561). FT CONFLICT 917 919 SPS -> RPG (in Ref. 1; AAA51561). FT CONFLICT 952 952 G -> A (in Ref. 1; AAA51561). FT CONFLICT 967 968 QS -> HP (in Ref. 1; AAA51561). FT CONFLICT 982 982 P -> PL (in Ref. 1; AAA51561). FT CONFLICT 1022 1022 Missing (in Ref. 1; AAA51561). FT CONFLICT 1045 1045 R -> G (in Ref. 1; AAA51561). FT CONFLICT 1103 1103 T -> S (in Ref. 1; AAA51561). FT HELIX 49 53 FT HELIX 58 60 FT STRAND 65 70 FT STRAND 76 79 FT STRAND 87 93 FT STRAND 97 104 FT STRAND 107 112 FT HELIX 113 115 FT STRAND 116 118 FT HELIX 122 124 FT STRAND 128 131 FT HELIX 134 140 FT TURN 141 143 FT STRAND 148 153 FT STRAND 155 157 FT STRAND 161 167 FT STRAND 170 178 FT STRAND 180 182 FT STRAND 184 187 FT STRAND 192 194 FT HELIX 195 204 FT STRAND 209 211 FT STRAND 226 228 FT STRAND 229 231 FT TURN 233 235 FT HELIX 239 241 FT STRAND 242 248 FT HELIX 249 251 FT STRAND 254 261 FT HELIX 262 264 FT STRAND 266 272 FT STRAND 275 278 FT HELIX 280 290 FT STRAND 301 305 FT STRAND 307 310 FT STRAND 312 316 FT STRAND 319 322 FT HELIX 323 329 FT TURN 332 334 FT HELIX 337 356 FT STRAND 359 361 FT HELIX 366 368 FT STRAND 369 371 FT HELIX 373 375 FT STRAND 377 379 FT HELIX 381 383 FT HELIX 384 387 FT HELIX 390 392 FT STRAND 395 401 FT HELIX 403 405 FT HELIX 408 413 FT HELIX 418 433 FT HELIX 445 447 FT HELIX 448 453 FT HELIX 466 475 FT HELIX 480 482 FT HELIX 486 499 FT TURN 510 512 FT HELIX 1029 1045 FT TURN 1046 1048 FT HELIX 1053 1070 FT HELIX 1071 1073 FT HELIX 1080 1097 FT STRAND 1101 1104 FT STRAND 1106 1108 FT HELIX 1115 1128 SQ SEQUENCE 1130 AA; 122873 MW; 85FE6C1C0E483EA2 CRC64; MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC EAQTKNGQGW VPSNYITPVN SLEKHSWYHG PVSRNAAEYL LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR NKPTVYGVSP NYDKWEMERT DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVNAVVL LYMATQISSA MEYLEKKNFI HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER PEGCPEKVYE LMRACWQWNP SDRPSFAEIH QAFETMFQES SISDEVEKEL GKQGVRGAVS TLLQAPELPT KTRTSRRAAE HRDTTDVPEM PHSKGQGESD PLDHEPAVSP LLPRKERGPP EGGLNEDERL LPKDKKTNLF SALIKKKKKT APTPPKRSSS FREMDGQPER RGAGEEEGRD ISNGALAFTP LDTADPAKSP KPSNGAGVPN GALRESGGSG FRSPHLWKKS STLTSSRLAT GEEEGGGSSS KRFLRSCSAS CVPHGAKDTE WRSVTLPRDL QSTGRQFDSS TFGGHKSEKP ALPRKRAGEN RSDQVTRGTV TPPPRLVKKN EEAADEVFKD IMESSPGSSP PNLTPKPLRR QVTVAPASGL PHKEEAGKGS ALGTPAAAEP VTPTSKAGSG APGGTSKGPA EESRVRRHKH SSESPGRDKG KLSRLKPAPP PPPAASAGKA GGKPSQSPSQ EAAGEAVLGA KTKATSLVDA VNSDAAKPSQ PGEGLKKPVL PATPKPQSAK PSGTPISPAP VPSTLPSASS ALAGDQPSST AFIPLISTRV SLRKTRQPPE RIASGAITKG VVLDSTEALC LAISRNSEQM ASHSAVLEAG KNLYTFCVSY VDSIQQMRNK FAFREAINKL ENNLRELQIC PATAGSGPAA TQDFSKLLSS VKEISDIVQR // ID ABL2_HUMAN Reviewed; 1182 AA. AC P42684; A0M8X0; B7UEF2; B7UEF3; B7UEF4; B7UEF5; Q5T0X6; Q5W0C5; AC Q6NZY6; Q7Z301; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 09-JUL-2014, entry version 168. DE RecName: Full=Abelson tyrosine-protein kinase 2; DE EC=2.7.10.2; DE AltName: Full=Abelson murine leukemia viral oncogene homolog 2; DE AltName: Full=Abelson-related gene protein; DE AltName: Full=Tyrosine-protein kinase ARG; GN Name=ABL2; Synonyms=ABLL, ARG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING RP (ISOFORM 2). RX PubMed=2198571; DOI=10.1073/pnas.87.15.5802; RA Kruh G.D., Perego R., Miki T., Aaronson S.A.; RT "The complete coding sequence of arg defines the Abelson subfamily of RT cytoplasmic tyrosine kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 87:5802-5806(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 7), ALTERNATIVE RP SPLICING (ISOFORM 10), AND VARIANT THR-12 (ISOFORM 4). RX PubMed=18810762; DOI=10.1002/jcb.21922; RA Bianchi C., Torsello B., Angeloni V., Bombelli S., Soldi M., RA Invernizzi L., Brambilla P., Perego R.A.; RT "Eight full-length abelson related gene (Arg) isoforms are RT constitutively expressed in caki-1 cell line and cell distribution of RT two isoforms has been analyzed after transfection."; RL J. Cell. Biochem. 105:1219-1227(2008). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Uterine endothelium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-930; MET-946; RP ARG-996; ASN-1085 AND ALA-1101. RG NIEHS SNPs program; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 343-469. RX PubMed=3787260; DOI=10.1126/science.3787260; RA Kruh G.D., King C.R., Kraus M.H., Popescu N.C., Amsbaugh S.C., RA McBride W.O., Aaronson S.A.; RT "A novel human gene closely related to the abl proto-oncogene."; RL Science 234:1545-1548(1986). RN [10] RP AUTOPHOSPHORYLATION AT TYR-272; TYR-439; TYR-568 AND TYR-683, AND RP ENZYME REGULATION. RX PubMed=12748290; DOI=10.1128/MCB.23.11.3884-3896.2003; RA Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.; RT "Two distinct phosphorylation pathways have additive effects on Abl RT family kinase activation."; RL Mol. Cell. Biol. 23:3884-3896(2003). RN [11] RP INTERACTION WITH RIN1, FUNCTION, AND ENZYME REGULATION. RX PubMed=15886098; DOI=10.1016/j.cub.2005.03.049; RA Hu H., Bliss J.M., Wang Y., Colicelli J.; RT "RIN1 is an ABL tyrosine kinase activator and a regulator of RT epithelial-cell adhesion and migration."; RL Curr. Biol. 15:815-823(2005). RN [12] RP FUNCTION, PHOSPHORYLATION AT TYR-261, AND UBIQUITINATION. RX PubMed=15735735; DOI=10.1038/sj.onc.1208454; RA Cao C., Li Y., Leng Y., Li P., Ma Q., Kufe D.; RT "Ubiquitination and degradation of the Arg tyrosine kinase is RT regulated by oxidative stress."; RL Oncogene 24:2433-2440(2005). RN [13] RP FUNCTION, AND INTERACTION WITH PSMA7. RX PubMed=16678104; DOI=10.1016/j.molcel.2006.04.007; RA Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., RA Cao C.; RT "Interaction between c-Abl and Arg tyrosine kinases and proteasome RT subunit PSMA7 regulates proteasome degradation."; RL Mol. Cell 22:317-327(2006). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [15] RP FUNCTION. RX PubMed=17306540; DOI=10.1016/j.cub.2007.01.057; RA Boyle S.N., Michaud G.A., Schweitzer B., Predki P.F., Koleske A.J.; RT "A critical role for cortactin phosphorylation by Abl-family kinases RT in PDGF-induced dorsal-wave formation."; RL Curr. Biol. 17:445-451(2007). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-817, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [17] RP FUNCTION. RX PubMed=18945674; DOI=10.1074/jbc.M804543200; RA Yogalingam G., Pendergast A.M.; RT "Abl kinases regulate autophagy by promoting the trafficking and RT function of lysosomal components."; RL J. Biol. Chem. 283:35941-35953(2008). RN [18] RP REVIEW ON FUNCTION. RX PubMed=12775773; DOI=10.1242/jcs.00622; RA Woodring P.J., Hunter T., Wang J.Y.; RT "Regulation of F-actin-dependent processes by the Abl family of RT tyrosine kinases."; RL J. Cell Sci. 116:2613-2626(2003). RN [19] RP REVIEW ON FUNCTION. RX PubMed=14729179; DOI=10.1016/j.tcb.2003.11.003; RA Hernandez S.E., Krishnaswami M., Miller A.L., Koleske A.J.; RT "How do Abl family kinases regulate cell shape and movement?"; RL Trends Cell Biol. 14:36-44(2004). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-915, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-631; SER-633; RP SER-655; SER-817; SER-820 AND SER-936, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [22] RP REVIEW ON FUNCTION. RX PubMed=18182299; DOI=10.1016/j.tibs.2007.10.006; RA Backert S., Feller S.M., Wessler S.; RT "Emerging roles of Abl family tyrosine kinases in microbial RT pathogenesis."; RL Trends Biochem. Sci. 33:80-90(2008). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-718, PHOSPHORYLATION RP [LARGE SCALE ANALYSIS] AT TYR-668 (ISOFORM 10), PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT TYR-647 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT TYR-683 (ISOFORM 5), PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT TYR-662 (ISOFORM 7), AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-936, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-936, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [27] RP REVIEW ON FUNCTION, AND DOMAIN. RX PubMed=20841568; DOI=10.1126/scisignal.3139re6; RA Colicelli J.; RT "ABL tyrosine kinases: evolution of function, regulation, and RT specificity."; RL Sci. Signal. 3:RE6-RE6(2010). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [29] RP STRUCTURE BY NMR OF 163-268. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the human ABL2 SH2 domain."; RL Submitted (FEB-2008) to the PDB data bank. RN [30] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 279-546 IN COMPLEXES WITH RP INHIBITORS. RX PubMed=21417343; DOI=10.1021/jm101506n; RA Salah E., Ugochukwu E., Barr A.J., von Delft F., Knapp S., RA Elkins J.M.; RT "Crystal structures of ABL-related gene (ABL2) in complex with RT imatinib, tozasertib (VX-680), and a type I inhibitor of the triazole RT carbothioamide class."; RL J. Med. Chem. 54:2359-2367(2011). RN [31] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 563-579 IN COMPLEX WITH RP CTTN, AND INTERACTION WITH CTTN. RX PubMed=22297987; DOI=10.1107/S1744309111056132; RA Liu W., MacGrath S.M., Koleske A.J., Boggon T.J.; RT "Lysozyme contamination facilitates crystallization of a RT heterotrimeric cortactin-Arg-lysozyme complex."; RL Acta Crystallogr. F 68:154-158(2012). RN [32] RP VARIANTS [LARGE SCALE ANALYSIS] HIS-78; GLN-99; ILE-519; SER-769; RP ARG-930 AND ARG-996, AND VARIANT [LARGE SCALE ANALYSIS] THR-12 RP (ISOFORM 4). RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an ABL1- CC overlapping role in key processes linked to cell growth and CC survival such as cytoskeleton remodeling in response to CC extracellular stimuli, cell motility and adhesion and receptor CC endocytosis. Coordinates actin remodeling through tyrosine CC phosphorylation of proteins controlling cytoskeleton dynamics like CC MYH10 (involved in movement); CTTN (involved in signaling); or CC TUBA1 and TUBB (microtubule subunits). Binds directly F-actin and CC regulates actin cytoskeletal structure through its F-actin- CC bundling activity. Involved in the regulation of cell adhesion and CC motility through phosphorylation of key regulators of these CC processes such as CRK, CRKL, DOK1 or ARHGAP35. Adhesion-dependent CC phosphorylation of ARHGAP35 promotes its association with RASA1, CC resulting in recruitment of ARHGAP35 to the cell periphery where CC it inhibits RHO. Phosphorylates multiple receptor tyrosine kinases CC like PDGFRB and other substrates which are involved in endocytosis CC regulation such as RIN1. In brain, may regulate neurotransmission CC by phosphorylating proteins at the synapse. ABL2 acts also as a CC regulator of multiple pathological signaling cascades during CC infection. Pathogens can highjack ABL2 kinase signaling to CC reorganize the host actin cytoskeleton for multiple purposes, like CC facilitating intracellular movement and host cell exit. Finally, CC functions as its own regulator through autocatalytic activity as CC well as through phosphorylation of its inhibitor, ABI1. CC -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a CC [protein]-L-tyrosine phosphate. CC -!- COFACTOR: Magnesium or manganese. CC -!- ENZYME REGULATION: Stabilized in the inactive form by an CC association between the SH3 domain and the SH2-TK linker region, CC interactions of the N-terminal cap, and contributions from an N- CC terminal myristoyl group and phospholipids. Activated by CC autophosphorylation as well as by SRC-family kinase-mediated CC phosphorylation. Activated by RIN1 binding to the SH2 and SH3 CC domains. Inhibited by imatinib mesylate (Gleevec) which is used CC for the treatment of chronic myeloid leukemia (CML). CC Phosphatidylinositol 4,5-bisphosphate (PIP2), a highly abundant CC phosphoinositide known to regulate cytoskeletal and membrane CC proteins, inhibits the tyrosine kinase activity (By similarity). CC -!- SUBUNIT: Interacts with PSMA7. Interacts with CTTN. CC -!- INTERACTION: CC Q8IZP0:ABI1; NbExp=2; IntAct=EBI-1102694, EBI-375446; CC P46108:CRK; NbExp=5; IntAct=EBI-1102694, EBI-886; CC P00533:EGFR; NbExp=7; IntAct=EBI-1102694, EBI-297353; CC P04626:ERBB2; NbExp=6; IntAct=EBI-1102694, EBI-641062; CC P21860:ERBB3; NbExp=10; IntAct=EBI-1102694, EBI-720706; CC Q15303:ERBB4; NbExp=4; IntAct=EBI-1102694, EBI-80371; CC P06241:FYN; NbExp=2; IntAct=EBI-1102694, EBI-515315; CC P62993:GRB2; NbExp=2; IntAct=EBI-1102694, EBI-401755; CC P10721:KIT; NbExp=2; IntAct=EBI-1102694, EBI-1379503; CC P16333:NCK1; NbExp=3; IntAct=EBI-1102694, EBI-389883; CC P27986:PIK3R1; NbExp=2; IntAct=EBI-1102694, EBI-79464; CC P19174:PLCG1; NbExp=4; IntAct=EBI-1102694, EBI-79387; CC Q13671:RIN1; NbExp=4; IntAct=EBI-1102694, EBI-366017; CC P12931:SRC; NbExp=2; IntAct=EBI-1102694, EBI-621482; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; Synonyms=IB, 1BLCTL; CC IsoId=P42684-1; Sequence=Displayed; CC Name=2; Synonyms=IA, 1ASCTL; CC IsoId=P42684-2; Sequence=VSP_004961; CC Name=3; Synonyms=IC, 1ALCTL; CC IsoId=P42684-3; Sequence=VSP_017112; CC Name=4; Synonyms=1ASCTS; CC IsoId=P42684-4; Sequence=VSP_004961, VSP_021308; CC Note=Variant in position: 12:N->T (in dbSNP:rs1318056). Contains CC a phosphotyrosine at position 647; CC Name=5; Synonyms=1BLCTS; CC IsoId=P42684-5; Sequence=VSP_021308; CC Note=Contains a phosphotyrosine at position 683; CC Name=6; Synonyms=1BSCTL; CC IsoId=P42684-6; Sequence=VSP_041772; CC Name=7; Synonyms=1BSCTS; CC IsoId=P42684-7; Sequence=VSP_041772, VSP_021308; CC Note=Contains a phosphotyrosine at position 662; CC Name=10; Synonyms=1ALCTS; CC IsoId=P42684-10; Sequence=VSP_017112, VSP_021308; CC Note=Contains a phosphotyrosine at position 668; CC Name=8; CC IsoId=P42684-8; Sequence=VSP_041772, VSP_041773, VSP_041774; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- DOMAIN: Contains two distinct classes of F-actin-binding domains. CC Although both can bind F-actin, the 2 are required to bundle actin CC filaments (By similarity). CC -!- PTM: Phosphorylated at Tyr-261 by ABL1 in response to oxidative CC stress. Phosphorylated by PDGFRB (By similarity). CC -!- PTM: Polyubiquitinated. Polyubiquitination of ABL2 leads to CC degradation. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. ABL subfamily. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC -!- SIMILARITY: Contains 1 SH2 domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- SEQUENCE CAUTION: CC Sequence=CAD98092.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/ABL2ID226.html"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/abl2/"; CC -!- WEB RESOURCE: Name=CGP resequencing studies; CC URL="http://www.sanger.ac.uk/perl/genetics/CGP/cgp_viewer?action=gene&ln=ABL2"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M35296; AAA35553.1; -; mRNA. DR EMBL; FJ542283; ACK76601.1; -; mRNA. DR EMBL; FJ542284; ACK76602.1; -; mRNA. DR EMBL; FJ542285; ACK76603.1; -; mRNA. DR EMBL; FJ542286; ACK76604.1; -; mRNA. DR EMBL; AK311045; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BX538317; CAD98092.1; ALT_INIT; mRNA. DR EMBL; DQ009672; AAY16984.1; -; Genomic_DNA. DR EMBL; AL139132; CAH70921.1; -; Genomic_DNA. DR EMBL; AL359179; CAH70921.1; JOINED; Genomic_DNA. DR EMBL; AL512326; CAH70921.1; JOINED; Genomic_DNA. DR EMBL; AL139132; CAH70925.1; -; Genomic_DNA. DR EMBL; AL359179; CAH70925.1; JOINED; Genomic_DNA. DR EMBL; AL512326; CAH70925.1; JOINED; Genomic_DNA. DR EMBL; AL359179; CAI15584.1; -; Genomic_DNA. DR EMBL; AL139132; CAI15584.1; JOINED; Genomic_DNA. DR EMBL; AL512326; CAI15584.1; JOINED; Genomic_DNA. DR EMBL; AL359179; CAI15585.1; -; Genomic_DNA. DR EMBL; AL139132; CAI15585.1; JOINED; Genomic_DNA. DR EMBL; AL512326; CAI15585.1; JOINED; Genomic_DNA. DR EMBL; AL512326; CAI13566.1; -; Genomic_DNA. DR EMBL; AL359179; CAI13566.1; JOINED; Genomic_DNA. DR EMBL; AL139132; CAI13566.1; JOINED; Genomic_DNA. DR EMBL; AL512326; CAI13570.1; -; Genomic_DNA. DR EMBL; AL359179; CAI13570.1; JOINED; Genomic_DNA. DR EMBL; AL139132; CAI13570.1; JOINED; Genomic_DNA. DR EMBL; CH471067; EAW91040.1; -; Genomic_DNA. DR EMBL; BC065912; AAH65912.1; -; mRNA. DR CCDS; CCDS30947.1; -. [P42684-1] DR CCDS; CCDS41441.2; -. [P42684-3] DR CCDS; CCDS44282.1; -. [P42684-10] DR CCDS; CCDS44283.1; -. [P42684-8] DR CCDS; CCDS53435.1; -. [P42684-4] DR CCDS; CCDS53436.1; -. [P42684-6] DR CCDS; CCDS53437.1; -. [P42684-7] DR CCDS; CCDS53438.1; -. [P42684-5] DR PIR; A35962; A35962. DR PIR; B35962; B35962. DR RefSeq; NP_001129472.1; NM_001136000.2. DR RefSeq; NP_001129473.1; NM_001136001.1. [P42684-8] DR RefSeq; NP_001161708.1; NM_001168236.1. [P42684-6] DR RefSeq; NP_001161709.1; NM_001168237.1. [P42684-5] DR RefSeq; NP_001161710.1; NM_001168238.1. [P42684-7] DR RefSeq; NP_001161711.1; NM_001168239.1. DR RefSeq; NP_005149.4; NM_005158.4. DR RefSeq; NP_009298.1; NM_007314.3. [P42684-1] DR UniGene; Hs.159472; -. DR PDB; 2ECD; NMR; -; A=163-268. DR PDB; 2KK1; NMR; -; A=1058-1182. DR PDB; 2XYN; X-ray; 2.81 A; A/B/C=279-546. DR PDB; 3GVU; X-ray; 2.05 A; A=279-546. DR PDB; 3HMI; X-ray; 1.65 A; A=279-546. DR PDB; 3ULR; X-ray; 1.65 A; C=563-579. DR PDB; 4EIH; X-ray; 1.20 A; A=165-273. DR PDBsum; 2ECD; -. DR PDBsum; 2KK1; -. DR PDBsum; 2XYN; -. DR PDBsum; 3GVU; -. DR PDBsum; 3HMI; -. DR PDBsum; 3ULR; -. DR PDBsum; 4EIH; -. DR ProteinModelPortal; P42684; -. DR SMR; P42684; 108-558, 1058-1182. DR BioGrid; 106545; 25. DR DIP; DIP-91N; -. DR IntAct; P42684; 34. DR MINT; MINT-1347081; -. DR STRING; 9606.ENSP00000356595; -. DR BindingDB; P42684; -. DR ChEMBL; CHEMBL4014; -. DR DrugBank; DB00171; Adenosine triphosphate. DR DrugBank; DB01254; Dasatinib. DR GuidetoPHARMACOLOGY; 1924; -. DR PhosphoSite; P42684; -. DR DMDM; 1168268; -. DR MaxQB; P42684; -. DR PaxDb; P42684; -. DR PRIDE; P42684; -. DR DNASU; 27; -. DR Ensembl; ENST00000344730; ENSP00000339209; ENSG00000143322. [P42684-10] DR Ensembl; ENST00000367623; ENSP00000356595; ENSG00000143322. [P42684-6] DR Ensembl; ENST00000392043; ENSP00000375897; ENSG00000143322. [P42684-8] DR Ensembl; ENST00000408940; ENSP00000386152; ENSG00000143322. [P42684-2] DR Ensembl; ENST00000502732; ENSP00000427562; ENSG00000143322. [P42684-1] DR Ensembl; ENST00000504405; ENSP00000426831; ENSG00000143322. [P42684-4] DR Ensembl; ENST00000507173; ENSP00000423413; ENSG00000143322. [P42684-7] DR Ensembl; ENST00000511413; ENSP00000424697; ENSG00000143322. [P42684-5] DR Ensembl; ENST00000512653; ENSP00000423578; ENSG00000143322. [P42684-3] DR GeneID; 27; -. DR KEGG; hsa:27; -. DR UCSC; uc001gmg.4; human. [P42684-10] DR UCSC; uc001gmi.4; human. [P42684-3] DR UCSC; uc001gmj.4; human. [P42684-1] DR UCSC; uc001gmk.3; human. [P42684-8] DR UCSC; uc010pne.2; human. [P42684-4] DR UCSC; uc010pnf.2; human. [P42684-5] DR UCSC; uc010png.2; human. [P42684-7] DR UCSC; uc010pnh.2; human. [P42684-6] DR CTD; 27; -. DR GeneCards; GC01M179068; -. DR HGNC; HGNC:77; ABL2. DR HPA; CAB017106; -. DR HPA; HPA001866; -. DR MIM; 164690; gene. DR neXtProt; NX_P42684; -. DR PharmGKB; PA24414; -. DR eggNOG; COG0515; -. DR HOVERGEN; HBG004162; -. DR InParanoid; P42684; -. DR KO; K08887; -. DR OMA; PPKCYGG; -. DR OrthoDB; EOG7GTT2V; -. DR PhylomeDB; P42684; -. DR TreeFam; TF105081; -. DR BRENDA; 2.7.10.2; 2681. DR Reactome; REACT_111045; Developmental Biology. DR SignaLink; P42684; -. DR ChiTaRS; ABL2; human. DR EvolutionaryTrace; P42684; -. DR GeneWiki; ABL2; -. DR GenomeRNAi; 27; -. DR NextBio; 89; -. DR PRO; PR:P42684; -. DR Bgee; P42684; -. DR CleanEx; HS_ABL2; -. DR Genevestigator; P42684; -. DR GO; GO:0015629; C:actin cytoskeleton; TAS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0051015; F:actin filament binding; TAS:UniProtKB. DR GO; GO:0003785; F:actin monomer binding; TAS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; TAS:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc. DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB. DR GO; GO:0051017; P:actin filament bundle assembly; IEA:Ensembl. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc. DR GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL. DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IDA:BHF-UCL. DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; TAS:UniProtKB. DR GO; GO:0010506; P:regulation of autophagy; TAS:UniProtKB. DR GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB. DR GO; GO:2000145; P:regulation of cell motility; TAS:UniProtKB. DR GO; GO:0030100; P:regulation of endocytosis; TAS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR Gene3D; 3.30.505.10; -; 1. DR InterPro; IPR015015; F-actin_binding. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR000980; SH2. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR Pfam; PF08919; F_actin_bind; 1. DR Pfam; PF07714; Pkinase_Tyr; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00808; FABD; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF50044; SSF50044; 1. DR SUPFAM; SSF55550; SSF55550; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell adhesion; KW Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Lipoprotein; KW Magnesium; Manganese; Metal-binding; Myristate; Nucleotide-binding; KW Phosphoprotein; Polymorphism; Reference proteome; SH2 domain; KW SH3 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 1182 Abelson tyrosine-protein kinase 2. FT /FTId=PRO_0000088052. FT DOMAIN 107 167 SH3. FT DOMAIN 173 263 SH2. FT DOMAIN 288 539 Protein kinase. FT NP_BIND 294 302 ATP (By similarity). FT NP_BIND 362 368 ATP (By similarity). FT REGION 2 106 CAP. FT REGION 694 930 F-actin-binding (By similarity). FT REGION 1020 1182 F-actin-binding (By similarity). FT MOTIF 427 451 Kinase activation loop (By similarity). FT MOTIF 658 660 Nuclear localization signal (Potential). FT COMPBIAS 561 564 Poly-Ser. FT COMPBIAS 732 739 Poly-Gly. FT COMPBIAS 843 1055 Pro-rich. FT COMPBIAS 984 988 Poly-Pro. FT ACT_SITE 409 409 Proton acceptor (By similarity). FT BINDING 317 317 ATP (By similarity). FT MOD_RES 261 261 Phosphotyrosine; by ABL1 and FT autocatalysis. FT MOD_RES 272 272 Phosphotyrosine; by autocatalysis. FT MOD_RES 275 275 Phosphoserine. FT MOD_RES 439 439 Phosphotyrosine; by autocatalysis and FT SRC-type Tyr-kinases. FT MOD_RES 568 568 Phosphotyrosine; by autocatalysis. FT MOD_RES 620 620 Phosphoserine. FT MOD_RES 631 631 Phosphoserine. FT MOD_RES 633 633 Phosphoserine. FT MOD_RES 655 655 Phosphoserine. FT MOD_RES 683 683 Phosphotyrosine; by autocatalysis. FT MOD_RES 718 718 Phosphotyrosine. FT MOD_RES 817 817 Phosphoserine. FT MOD_RES 820 820 Phosphoserine. FT MOD_RES 915 915 Phosphoserine. FT MOD_RES 936 936 Phosphoserine. FT LIPID 2 2 N-myristoyl glycine (By similarity). FT VAR_SEQ 2 73 GQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTT FT ETGFNIFTQHDHFASCVEDGFEGDKTGGSSP -> MVLGTV FT LLPPNSYGRDQDTSLCCLCTEASESALPDLT (in FT isoform 2 and isoform 4). FT /FTId=VSP_004961. FT VAR_SEQ 2 52 GQQVGRVGEAPGLQQPQPRGIRGSSAARPSGRRRDPAGRTT FT ETGFNIFTQH -> MVLGTVLLPPNSYGRDQDTSLCCLCTE FT ASESALPDLT (in isoform 3 and isoform 10). FT /FTId=VSP_017112. FT VAR_SEQ 53 73 Missing (in isoform 6, isoform 7 and FT isoform 8). FT /FTId=VSP_041772. FT VAR_SEQ 550 564 EEVAEELGRAASSSS -> EVLLHCANQTCITL (in FT isoform 8). FT /FTId=VSP_041773. FT VAR_SEQ 565 1182 Missing (in isoform 8). FT /FTId=VSP_041774. FT VAR_SEQ 688 790 Missing (in isoform 4, isoform 5, isoform FT 7 and isoform 10). FT /FTId=VSP_021308. FT VARIANT 78 78 R -> H (in dbSNP:rs55655202). FT /FTId=VAR_055411. FT VARIANT 99 99 E -> Q (somatic mutation in a breast FT cancer sample). FT /FTId=VAR_055412. FT VARIANT 519 519 R -> I (somatic mutation in a lung FT squamous cell carcinoma). FT /FTId=VAR_055413. FT VARIANT 769 769 T -> S (in dbSNP:rs55892721). FT /FTId=VAR_055414. FT VARIANT 930 930 K -> R (in dbSNP:rs17277288). FT /FTId=VAR_029232. FT VARIANT 946 946 V -> M (in dbSNP:rs28913889). FT /FTId=VAR_029233. FT VARIANT 996 996 P -> R (in dbSNP:rs28913890). FT /FTId=VAR_029234. FT VARIANT 1085 1085 S -> N (in dbSNP:rs28913891). FT /FTId=VAR_029235. FT VARIANT 1101 1101 T -> A (in dbSNP:rs28913892). FT /FTId=VAR_029236. FT CONFLICT 343 344 NL -> TI (in Ref. 9; no nucleotide FT entry). FT CONFLICT 435 435 T -> I (in Ref. 3; AK311045). FT CONFLICT 981 981 K -> R (in Ref. 4; CAD98092). FT HELIX 168 170 FT STRAND 174 177 FT HELIX 180 187 FT STRAND 194 199 FT STRAND 207 213 FT STRAND 216 221 FT STRAND 226 228 FT STRAND 230 233 FT STRAND 236 240 FT HELIX 241 248 FT STRAND 255 257 FT STRAND 280 282 FT HELIX 285 287 FT STRAND 288 293 FT HELIX 294 297 FT STRAND 300 307 FT HELIX 308 310 FT STRAND 312 318 FT HELIX 326 337 FT STRAND 347 351 FT STRAND 353 356 FT STRAND 358 362 FT HELIX 369 375 FT TURN 378 380 FT HELIX 383 402 FT HELIX 412 414 FT STRAND 415 417 FT HELIX 419 421 FT STRAND 423 425 FT STRAND 435 437 FT STRAND 438 440 FT HELIX 449 451 FT HELIX 454 459 FT HELIX 464 479 FT HELIX 491 493 FT HELIX 494 499 FT HELIX 512 521 FT HELIX 526 528 FT HELIX 532 545 FT HELIX 1069 1071 FT TURN 1076 1078 FT HELIX 1080 1083 FT HELIX 1086 1099 FT HELIX 1106 1123 FT HELIX 1124 1126 FT HELIX 1130 1152 FT STRAND 1155 1158 FT HELIX 1165 1181 SQ SEQUENCE 1182 AA; 128343 MW; ED93869BC2B14FAA CRC64; MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TTETGFNIFT QHDHFASCVE DGFEGDKTGG SSPEALHRPY GCDVEPQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTADGKV YVTAESRFST LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG EVYVGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV TEYMPYGNLL DYLRECNREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE TMFHDSSISE EVAEELGRAA SSSSVVPYLP RLPILPSKTR TLKKQVENKE NIEGAQDATE NSASSLAPGF IRGAQASSGS PALPRKQRDK SPSSLLEDAK ETCFTRDRKG GFFSSFMKKR NAPTPPKRSS SFREMENQPH KKYELTGNFS SVASLQHADG FSFTPAQQEA NLVPPKCYGG SFAQRNLCND DGGGGGGSGT AGGGWSGITG FFTPRLIKKT LGLRAGKPTA SDDTSKPFPR SNSTSSMSSG LPEQDRMAMT LPRNCQRSKL QLERTVSTSS QPEENVDRAN DMLPKKSEES AAPSRERPKA KLLPRGATAL PLRTPSGDLA ITEKDPPGVG VAGVAAAPKG KEKNGGARLG MAGVPEDGEQ PGWPSPAKAA PVLPTTHNHK VPVLISPTLK HTPADVQLIG TDSQGNKFKL LSEHQVTSSG DKDRPRRVKP KCAPPPPPVM RLLQHPSICS DPTEEPTALT AGQSTSETQE GGKKAALGAV PISGKAGRPV MPPPQVPLPT SSISPAKMAN GTAGTKVALR KTKQAAEKIS ADKISKEALL ECADLLSSAL TEPVPNSQLV DTGHQLLDYC SGYVDCIPQT RNKFAFREAV SKLELSLQEL QVSSAAAGVP GTNPVLNNLL SCVQEISDVV QR // ID ABLM1_HUMAN Reviewed; 778 AA. AC O14639; A6NI16; A6NJ06; A8MXA9; Q15039; Q5JVV1; Q5JVV2; Q5T6N3; AC Q5T6N5; Q68CQ9; Q9BUP1; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 3. DT 09-JUL-2014, entry version 136. DE RecName: Full=Actin-binding LIM protein 1; DE Short=abLIM-1; DE AltName: Full=Actin-binding LIM protein family member 1; DE AltName: Full=Actin-binding double zinc finger protein; DE AltName: Full=LIMAB1; DE AltName: Full=Limatin; GN Name=ABLIM1; Synonyms=ABLIM, KIAA0059, LIMAB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE RP SPLICING, AND TISSUE SPECIFICITY. RC TISSUE=Retina; RX PubMed=9245787; DOI=10.1083/jcb.138.3.575; RA Roof D.J., Hayes A., Adamian M., Chishti A.H., Li T.; RT "Molecular characterization of abLIM, a novel actin-binding and double RT zinc finger protein."; RL J. Cell Biol. 138:575-588(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites RT from human T cells using immobilized metal affinity chromatography and RT tandem mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-396, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [10] RP INTERACTION WITH ABRA. RX PubMed=17194709; DOI=10.1074/jbc.M607549200; RA Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T., RA Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N.; RT "Two novel members of the ABLIM protein family, ABLIM-2 and -3, RT associate with STARS and directly bind F-actin."; RL J. Biol. Chem. 282:8393-8403(2007). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-435; SER-455; RP SER-458; SER-587; SER-640 AND SER-655, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; TYR-373; SER-426; RP SER-431; THR-433 AND SER-435, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-640, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). CC -!- FUNCTION: May act as scaffold protein (By similarity). May play a CC role in the development of the retina. Has been suggested to play CC a role in axon guidance. CC -!- SUBUNIT: Binds F-actin. Interacts with ABRA. CC -!- INTERACTION: CC O95751:LDOC1; NbExp=2; IntAct=EBI-487024, EBI-740738; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm, CC cytoskeleton (By similarity). Note=Associated with the CC cytoskeleton (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=O14639-1; Sequence=Displayed; CC Name=2; CC IsoId=O14639-2; Sequence=VSP_012100; CC Name=3; CC IsoId=O14639-3; Sequence=VSP_012099, VSP_012102; CC Name=4; CC IsoId=O14639-4; Sequence=VSP_012099, VSP_012101, VSP_012102; CC Name=5; CC IsoId=O14639-5; Sequence=VSP_012099, VSP_041185, VSP_012102; CC -!- TISSUE SPECIFICITY: Detected in liver, heart, skeletal muscle, CC brain and retina, where it is concentrated in the inner segment CC and in the outer plexiform layers. CC -!- SIMILARITY: Contains 1 HP (headpiece) domain. CC -!- SIMILARITY: Contains 4 LIM zinc-binding domains. CC -!- SEQUENCE CAUTION: CC Sequence=BAA06681.2; Type=Erroneous initiation; Note=Translation N-terminally shortened; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF005654; AAC51676.1; -; mRNA. DR EMBL; D31883; BAA06681.2; ALT_INIT; mRNA. DR EMBL; AK098277; BAG53605.1; -; mRNA. DR EMBL; CR749819; CAH18679.1; -; mRNA. DR EMBL; AL133384; CAI40135.1; -; Genomic_DNA. DR EMBL; AL133384; CAI40136.1; -; Genomic_DNA. DR EMBL; AL133384; CAI40140.1; -; Genomic_DNA. DR EMBL; AL354873; CAI40140.1; JOINED; Genomic_DNA. DR EMBL; AL133384; CAI40141.1; -; Genomic_DNA. DR EMBL; AL354873; CAI40141.1; JOINED; Genomic_DNA. DR EMBL; AL354873; CAI10908.1; -; Genomic_DNA. DR EMBL; AL133384; CAI10908.1; JOINED; Genomic_DNA. DR EMBL; AL354873; CAI10910.1; -; Genomic_DNA. DR EMBL; AL133384; CAI10910.1; JOINED; Genomic_DNA. DR EMBL; AL590109; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002448; AAH02448.1; -; mRNA. DR CCDS; CCDS31288.1; -. [O14639-2] DR CCDS; CCDS31289.1; -. [O14639-5] DR CCDS; CCDS7590.1; -. [O14639-1] DR RefSeq; NP_001003407.1; NM_001003407.1. [O14639-2] DR RefSeq; NP_001003408.1; NM_001003408.1. DR RefSeq; NP_002304.3; NM_002313.5. [O14639-1] DR RefSeq; NP_006711.3; NM_006720.3. [O14639-5] DR RefSeq; XP_005269885.1; XM_005269828.2. [O14639-3] DR UniGene; Hs.438236; -. DR UniGene; Hs.538331; -. DR UniGene; Hs.593868; -. DR ProteinModelPortal; O14639; -. DR SMR; O14639; 89-344, 714-778. DR BioGrid; 110171; 21. DR IntAct; O14639; 17. DR MINT; MINT-1447354; -. DR STRING; 9606.ENSP00000338190; -. DR PhosphoSite; O14639; -. DR MaxQB; O14639; -. DR PaxDb; O14639; -. DR PRIDE; O14639; -. DR Ensembl; ENST00000277895; ENSP00000277895; ENSG00000099204. [O14639-1] DR Ensembl; ENST00000369252; ENSP00000358256; ENSG00000099204. [O14639-2] DR Ensembl; ENST00000369253; ENSP00000358257; ENSG00000099204. [O14639-4] DR Ensembl; ENST00000392952; ENSP00000376679; ENSG00000099204. [O14639-5] DR GeneID; 3983; -. DR KEGG; hsa:3983; -. DR UCSC; uc021pyu.1; human. [O14639-5] DR UCSC; uc021pyw.1; human. [O14639-1] DR UCSC; uc021pyz.1; human. [O14639-2] DR UCSC; uc021pzc.1; human. [O14639-4] DR CTD; 3983; -. DR GeneCards; GC10M116190; -. DR HGNC; HGNC:78; ABLIM1. DR HPA; HPA038951; -. DR HPA; HPA038952; -. DR MIM; 602330; gene. DR neXtProt; NX_O14639; -. DR PharmGKB; PA35023; -. DR eggNOG; NOG302299; -. DR HOVERGEN; HBG031499; -. DR KO; K07520; -. DR OMA; HHPSEKP; -. DR PhylomeDB; O14639; -. DR TreeFam; TF318042; -. DR Reactome; REACT_111045; Developmental Biology. DR ChiTaRS; ABLIM1; human. DR GeneWiki; ABLIM1; -. DR GenomeRNAi; 3983; -. DR NextBio; 15616; -. DR PRO; PR:O14639; -. DR ArrayExpress; O14639; -. DR Bgee; O14639; -. DR CleanEx; HS_ABLIM1; -. DR Genevestigator; O14639; -. DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro. DR GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; TAS:ProtInc. DR Gene3D; 1.10.950.10; -; 1. DR Gene3D; 2.10.110.10; -; 4. DR InterPro; IPR028448; ABLIM1. DR InterPro; IPR003128; Villin_headpiece. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR24213:SF18; PTHR24213:SF18; 1. DR Pfam; PF00412; LIM; 4. DR Pfam; PF02209; VHP; 1. DR SMART; SM00132; LIM; 4. DR SMART; SM00153; VHP; 1. DR SUPFAM; SSF47050; SSF47050; 1. DR PROSITE; PS51089; HP; 1. DR PROSITE; PS00478; LIM_DOMAIN_1; 4. DR PROSITE; PS50023; LIM_DOMAIN_2; 4. PE 1: Evidence at protein level; KW Actin-binding; Alternative splicing; Coiled coil; Complete proteome; KW Cytoplasm; Cytoskeleton; LIM domain; Metal-binding; Phosphoprotein; KW Polymorphism; Reference proteome; Repeat; Zinc. FT CHAIN 1 778 Actin-binding LIM protein 1. FT /FTId=PRO_0000075697. FT DOMAIN 97 156 LIM zinc-binding 1. FT DOMAIN 156 216 LIM zinc-binding 2. FT DOMAIN 224 283 LIM zinc-binding 3. FT DOMAIN 283 343 LIM zinc-binding 4. FT DOMAIN 710 778 HP. FT COILED 590 614 Potential. FT MOD_RES 367 367 Phosphoserine. FT MOD_RES 373 373 Phosphotyrosine. FT MOD_RES 396 396 Phosphotyrosine. FT MOD_RES 426 426 Phosphoserine. FT MOD_RES 431 431 Phosphoserine. FT MOD_RES 433 433 Phosphothreonine. FT MOD_RES 435 435 Phosphoserine. FT MOD_RES 439 439 Phosphotyrosine. FT MOD_RES 455 455 Phosphoserine. FT MOD_RES 458 458 Phosphoserine. FT MOD_RES 587 587 Phosphoserine. FT MOD_RES 640 640 Phosphoserine. FT MOD_RES 655 655 Phosphoserine. FT VAR_SEQ 1 316 Missing (in isoform 3, isoform 4 and FT isoform 5). FT /FTId=VSP_012099. FT VAR_SEQ 1 81 MPAFLGLKCLGKLCSSEKSKVTSSERTSARGSNRKRLIVED FT RRVSGTSFTAHRRATITHLLYLCPKDYCPRGRVCNSVDPF FT -> MLMTLEMTELTDPHHTMGDYK (in isoform 2). FT /FTId=VSP_012100. FT VAR_SEQ 347 347 R -> RLPNIRRSSSDFFYSKSLIRRTGRSPSLQ (in FT isoform 5). FT /FTId=VSP_041185. FT VAR_SEQ 348 373 Missing (in isoform 4). FT /FTId=VSP_012101. FT VAR_SEQ 480 514 Missing (in isoform 3, isoform 4 and FT isoform 5). FT /FTId=VSP_012102. FT VARIANT 434 434 P -> T (in dbSNP:rs11593544). FT /FTId=VAR_050141. FT VARIANT 637 637 R -> G (in dbSNP:rs7091419). FT /FTId=VAR_050142. FT CONFLICT 499 499 R -> L (in Ref. 1; AAC51676). FT CONFLICT 532 532 A -> R (in Ref. 1; AAC51676). FT CONFLICT 563 563 K -> E (in Ref. 2; BAA06681). FT CONFLICT 578 578 V -> I (in Ref. 2; BAA06681). SQ SEQUENCE 778 AA; 87688 MW; EBC2F14BE558752B CRC64; MPAFLGLKCL GKLCSSEKSK VTSSERTSAR GSNRKRLIVE DRRVSGTSFT AHRRATITHL LYLCPKDYCP RGRVCNSVDP FVAHPQDPHH PSEKPVIHCH KCGEPCKGEV LRVQTKHFHI KCFTCKVCGC DLAQGGFFIK NGEYLCTLDY QRMYGTRCHG CGEFVEGEVV TALGKTYHPN CFACTICKRP FPPGDRVTFN GRDCLCQLCA QPMSSSPKET TFSSNCAGCG RDIKNGQALL ALDKQWHLGC FKCKSCGKVL TGEYISKDGA PYCEKDYQGL FGVKCEACHQ FITGKVLEAG DKHYHPSCAR CSRCNQMFTE GEEMYLQGST VWHPDCKQST KTEEKLRPTR TSSESIYSRP GSSIPGSPGH TIYAKVDNEI LDYKDLAAIP KVKAIYDIER PDLITYEPFY TSGYDDKQER QSLGESPRTL SPTPSAEGYQ DVRDRMIHRS TSQGSINSPV YSRHSYTPTT SRSPQHFHRP GNEPSSGRNS PLPYRPDSRP LTPTYAQAPK HFHVPDQGIN IYRKPPIYKQ HAALAAQSKS SEDIIKFSKF PAAQAPDPSE TPKIETDHWP GPPSFAVVGP DMKRRSSGRE EDDEELLRRR QLQEEQLMKL NSGLGQLILK EEMEKESRER SSLLASRYDS PINSASHIPS SKTASLPGYG RNGLHRPVST DFAQYNSYGD VSGGVRDYQT LPDGHMPAMR MDRGVSMPNM LEPKIFPYEM LMVTNRGRNK ILREVDRTRL ERHLAPEVFR EIFGMSIQEF DRLPLWRRND MKKKAKLF // ID ACACA_HUMAN Reviewed; 2346 AA. AC Q13085; B2RP68; Q6KEV6; Q6XDA8; Q7Z2G8; Q7Z561; Q7Z563; Q7Z564; AC Q86WB2; Q86WB3; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 2. DT 09-JUL-2014, entry version 146. DE RecName: Full=Acetyl-CoA carboxylase 1; DE Short=ACC1; DE EC=6.4.1.2; DE AltName: Full=ACC-alpha; DE Includes: DE RecName: Full=Biotin carboxylase; DE EC=6.3.4.14; GN Name=ACACA; Synonyms=ACAC, ACC1, ACCA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=7732023; DOI=10.1073/pnas.92.9.4011; RA Abu-Elheiga L., Jayakumar A., Baldini A., Chirala S.S., Wakil S.J.; RT "Human acetyl-CoA carboxylase: characterization, molecular cloning, RT and evidence for two isoforms."; RL Proc. Natl. Acad. Sci. U.S.A. 92:4011-4015(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF RP 1-366 (ISOFORMS 2 AND 3), AND NUCLEOTIDE SEQUENCE [MRNA] OF 1-120 RP (ISOFORM 4). RC TISSUE=Adipocyte; RX PubMed=12810950; DOI=10.1073/pnas.1332670100; RA Mao J., Chirala S.S., Wakil S.J.; RT "Human acetyl-CoA carboxylase 1 gene: presence of three promoters and RT heterogeneity at the 5'-untranslated mRNA region."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7515-7520(2003). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-2271. RX PubMed=15333468; DOI=10.1093/carcin/bgh273; RA Sinilnikova O.M., Ginolhac S.M., Magnard C., Leone M., Anczukow O., RA Hughes D., Moreau K., Thompson D., Coutanson C., Hall J., RA Romestaing P., Gerard J.-P., Bonadona V., Lasset C., Goldgar D.E., RA Joulin V., Venezia N.D., Lenoir G.M.; RT "Acetyl-CoA carboxylase alpha gene and breast cancer susceptibility."; RL Carcinogenesis 25:2417-2424(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-113 (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [MRNA] OF 1-93 (ISOFORM 3). RC TISSUE=Mammary gland, and Testis; RX PubMed=14643797; DOI=10.1016/j.bbalip.2003.09.005; RA Travers M.T., Vallance A.J., Clegg R.A., Thomson R., Price N.T., RA Barber M.C.; RT "Characterisation of an N-terminal variant of acetyl-CoA carboxylase- RT alpha: expression in human tissues and evolutionary aspects."; RL Biochim. Biophys. Acta 1634:97-106(2003). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=15607423; DOI=10.1016/j.ygeno.2004.10.001; RA Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C., RA Joulin V.; RT "Asymmetric expression of transcripts derived from the shared promoter RT between the divergently oriented ACACA and TADA2L genes."; RL Genomics 85:71-84(2005). RN [7] RP PROTEIN SEQUENCE OF 1-18; 39-45; 77-86; 99-111; 121-132; 153-170; RP 218-224; 267-276; 278-288; 323-335; 568-579; 589-615; 646-657; RP 748-755; 818-838; 985-992; 997-1008; 1083-1096; 1147-1169; 1192-1199; RP 1233-1247; 1283-1294; 1317-1325; 1327-1334; 1372-1385; 1401-1420; RP 1508-1514; 1553-1564; 1668-1687; 1714-1731; 1750-1759; 1782-1798; RP 1824-1833; 1838-1856; 1905-1916; 1922-1929; 1978-2009; 2063-2072; RP 2104-2111; 2115-2127; 2139-2161; 2200-2209; 2213-2218; 2221-2229 AND RP 2261-2293, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-80, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Hepatoma; RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.; RL Submitted (JUL-2007) to UniProtKB. RN [8] RP INTERACTION WITH BRCA1. RX PubMed=12360400; DOI=10.1038/sj.onc.1205915; RA Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S., RA Lenoir G.M., Venezia N.D.; RT "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of RT BRCT domains."; RL Oncogene 21:6729-6739(2002). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-53, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [10] RP INTERACTION WITH BRCA1. RX PubMed=16326698; DOI=10.1074/jbc.M504652200; RA Moreau K., Dizin E., Ray H., Luquain C., Lefai E., Foufelle F., RA Billaud M., Lenoir G.M., Venezia N.D.; RT "BRCA1 affects lipid synthesis through its interaction with acetyl-CoA RT carboxylase."; RL J. Biol. Chem. 281:3172-3181(2006). RN [11] RP PHOSPHORYLATION AT SER-1263, AND MUTAGENESIS OF SER-78; SER-344; RP SER-432; SER-1201; SER-1263; SER-1585; SER-1952 AND SER-2211. RX PubMed=16698035; DOI=10.1016/j.jmb.2006.04.010; RA Ray H., Moreau K., Dizin E., Callebaut I., Venezia N.D.; RT "ACCA phosphopeptide recognition by the BRCT repeats of BRCA1."; RL J. Mol. Biol. 359:973-982(2006). RN [12] RP INVOLVEMENT IN ACACAD. RX PubMed=6114432; RA Blom W., de Muinck Keizer S.M.P.F., Scholte H.R.; RT "Acetyl-CoA carboxylase deficiency: an inborn error of de novo fatty RT acid synthesis."; RL N. Engl. J. Med. 305:465-466(1981). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; SER-29 AND RP SER-80, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-5 AND SER-29, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-29, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1334, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [20] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, AND RP INTERACTION WITH MID1IP1. RX PubMed=20952656; DOI=10.1073/pnas.1012736107; RA Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M., RA McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.; RT "Crystal structure of Spot 14, a modulator of fatty acid synthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-5; SER-23; SER-29 AND SER-80, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-80, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [24] RP VARIANT [LARGE SCALE ANALYSIS] GLN-1687. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis CC of long-chain fatty acids. Carries out three functions: biotin CC carboxyl carrier protein, biotin carboxylase and CC carboxyltransferase. CC -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate CC + malonyl-CoA. CC -!- CATALYTIC ACTIVITY: ATP + biotin-[carboxyl-carrier-protein] + CC CO(2) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier- CC protein]. CC -!- COFACTOR: Biotin. CC -!- COFACTOR: Binds 2 manganese ions per subunit. CC -!- ENZYME REGULATION: By phosphorylation (By similarity). Activity is CC increased by oligomerization. Citrate and MID1IP1 promote CC oligomerization. CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA CC from acetyl-CoA: step 1/1. CC -!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form CC filamentous polymers. Interacts in its inactive phosphorylated CC form with the BRCT domains of BRCA1 which prevents ACACA CC dephosphorylation and inhibits lipid synthesis. Interacts with CC MID1IP1; interaction with MID1IP1 promotes oligomerization and CC increases its activity. CC -!- INTERACTION: CC O60218:AKR1B10; NbExp=4; IntAct=EBI-717681, EBI-1572139; CC P38398:BRCA1; NbExp=2; IntAct=EBI-717681, EBI-349905; CC Q96EB6:SIRT1; NbExp=3; IntAct=EBI-717681, EBI-1802965; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=4; CC Name=1; CC IsoId=Q13085-1; Sequence=Displayed; CC Name=2; Synonyms=E5A; CC IsoId=Q13085-2; Sequence=VSP_026099; CC Name=3; Synonyms=E5B; CC IsoId=Q13085-3; Sequence=VSP_026098; CC Name=4; CC IsoId=Q13085-4; Sequence=VSP_026100; CC -!- TISSUE SPECIFICITY: Expressed in brain, placental, skeletal CC muscle, renal, pancreatic and adipose tissues; expressed at low CC level in pulmonary tissue; not detected in the liver. CC -!- PTM: Phosphorylation on Ser-1263 is required for interaction with CC BRCA1. CC -!- DISEASE: Acetyl-CoA carboxylase 1 deficiency (ACACAD) CC [MIM:613933]: An inborn error of de novo fatty acid synthesis CC associated with severe brain damage, persistent myopathy and poor CC growth. Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. CC -!- SIMILARITY: Contains 1 biotin carboxylation domain. CC -!- SIMILARITY: Contains 1 biotinyl-binding domain. CC -!- SIMILARITY: Contains 1 carboxyltransferase domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAP94120.1; Type=Erroneous initiation; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Acetyl-CoA carboxylase entry; CC URL="http://en.wikipedia.org/wiki/Acetyl-CoA_carboxylase"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U19822; AAC50139.1; -; mRNA. DR EMBL; AY315619; AAP94114.1; -; mRNA. DR EMBL; AY315620; AAP94115.1; -; mRNA. DR EMBL; AY315621; AAP94116.1; -; mRNA. DR EMBL; AY315623; AAP94118.1; -; mRNA. DR EMBL; AY315625; AAP94120.1; ALT_INIT; mRNA. DR EMBL; AY315627; AAP94122.1; -; mRNA. DR EMBL; AY237919; AAP69841.1; -; mRNA. DR EMBL; BC137287; AAI37288.1; -; mRNA. DR EMBL; AJ534888; CAD59556.1; -; mRNA. DR EMBL; AJ534889; CAD59557.1; -; mRNA. DR EMBL; AJ564444; CAD92089.1; -; mRNA. DR CCDS; CCDS11317.1; -. [Q13085-1] DR CCDS; CCDS11318.1; -. [Q13085-2] DR CCDS; CCDS42302.1; -. [Q13085-4] DR CCDS; CCDS42303.1; -. [Q13085-3] DR PIR; I38928; I38928. DR RefSeq; NP_942131.1; NM_198834.2. [Q13085-4] DR RefSeq; NP_942133.1; NM_198836.2. [Q13085-1] DR RefSeq; NP_942134.1; NM_198837.1. [Q13085-2] DR RefSeq; NP_942135.1; NM_198838.1. [Q13085-3] DR RefSeq; NP_942136.1; NM_198839.2. [Q13085-1] DR RefSeq; XP_005257323.1; XM_005257266.2. [Q13085-3] DR RefSeq; XP_005257324.1; XM_005257267.2. [Q13085-3] DR RefSeq; XP_006725384.1; XM_006725321.1. [Q13085-3] DR UniGene; Hs.160556; -. DR PDB; 2YL2; X-ray; 2.30 A; A/B=78-617. DR PDB; 3COJ; X-ray; 3.21 A; H/I/J/K/L/M/N/O=1258-1270. DR PDB; 4ASI; X-ray; 2.80 A; A/B/C/D/E/F=1571-2338. DR PDBsum; 2YL2; -. DR PDBsum; 3COJ; -. DR PDBsum; 4ASI; -. DR ProteinModelPortal; Q13085; -. DR SMR; Q13085; 102-817, 1581-2338. DR BioGrid; 106549; 65. DR DIP; DIP-36122N; -. DR IntAct; Q13085; 26. DR MINT; MINT-1415014; -. DR BindingDB; Q13085; -. DR ChEMBL; CHEMBL3351; -. DR DrugBank; DB00121; Biotin. DR GuidetoPHARMACOLOGY; 1263; -. DR PhosphoSite; Q13085; -. DR DMDM; 118601083; -. DR MaxQB; Q13085; -. DR PaxDb; Q13085; -. DR PRIDE; Q13085; -. DR Ensembl; ENST00000335166; ENSP00000335323; ENSG00000132142. [Q13085-3] DR Ensembl; ENST00000353139; ENSP00000344789; ENSG00000132142. [Q13085-4] DR Ensembl; ENST00000360679; ENSP00000353898; ENSG00000132142. [Q13085-2] DR Ensembl; ENST00000394406; ENSP00000377928; ENSG00000132142. [Q13085-1] DR Ensembl; ENST00000451642; ENSP00000397282; ENSG00000132142. DR GeneID; 31; -. DR KEGG; hsa:31; -. DR UCSC; uc002hnk.3; human. [Q13085-1] DR UCSC; uc002hnl.3; human. [Q13085-2] DR UCSC; uc002hno.3; human. [Q13085-4] DR CTD; 31; -. DR GeneCards; GC17M035441; -. DR HGNC; HGNC:84; ACACA. DR HPA; CAB013715; -. DR MIM; 200350; gene. DR MIM; 613933; phenotype. DR neXtProt; NX_Q13085; -. DR PharmGKB; PA24421; -. DR eggNOG; COG0511; -. DR HOVERGEN; HBG005371; -. DR InParanoid; Q13085; -. DR KO; K11262; -. DR OMA; HVFSGQC; -. DR OrthoDB; EOG7HXCPW; -. DR PhylomeDB; Q13085; -. DR TreeFam; TF300061; -. DR BRENDA; 6.4.1.2; 2681. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_116125; Disease. DR SABIO-RK; Q13085; -. DR UniPathway; UPA00655; UER00711. DR ChiTaRS; ACACA; human. DR EvolutionaryTrace; Q13085; -. DR GeneWiki; ACACA; -. DR GenomeRNAi; 31; -. DR NextBio; 111; -. DR PRO; PR:Q13085; -. DR ArrayExpress; Q13085; -. DR Bgee; Q13085; -. DR Genevestigator; Q13085; -. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0006084; P:acetyl-CoA metabolic process; ISS:UniProtKB. DR GO; GO:0006768; P:biotin metabolic process; TAS:Reactome. DR GO; GO:0006853; P:carnitine shuttle; TAS:Reactome. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome. DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB. DR GO; GO:0055088; P:lipid homeostasis; IEA:Ensembl. DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome. DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0044268; P:multicellular organismal protein metabolic process; IEA:Ensembl. DR GO; GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl. DR GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome. DR GO; GO:0006766; P:vitamin metabolic process; TAS:Reactome. DR GO; GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.90.226.10; -; 3. DR InterPro; IPR013537; AcCoA_COase_cen. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR001882; Biotin_BS. DR InterPro; IPR011764; Biotin_carboxylation_dom. DR InterPro; IPR005482; Biotin_COase_C. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR005481; CarbamoylP_synth_lsu_N. DR InterPro; IPR000022; Carboxyl_trans. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR011763; COA_CT_C. DR InterPro; IPR011762; COA_CT_N. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR011054; Rudment_hybrid_motif. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF08326; ACC_central; 1. DR Pfam; PF02785; Biotin_carb_C; 1. DR Pfam; PF00364; Biotin_lipoyl; 1. DR Pfam; PF01039; Carboxyl_trans; 1. DR Pfam; PF00289; CPSase_L_chain; 1. DR Pfam; PF02786; CPSase_L_D2; 1. DR SMART; SM00878; Biotin_carb_C; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52096; SSF52096; 2. DR SUPFAM; SSF52440; SSF52440; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS50979; BC; 1. DR PROSITE; PS00188; BIOTIN; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS50989; COA_CT_CTER; 1. DR PROSITE; PS50980; COA_CT_NTER; 1. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Allosteric enzyme; KW Alternative promoter usage; ATP-binding; Biotin; Complete proteome; KW Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis; KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism; KW Manganese; Metal-binding; Multifunctional enzyme; Nucleotide-binding; KW Phosphoprotein; Polymorphism; Reference proteome. FT CHAIN 1 2346 Acetyl-CoA carboxylase 1. FT /FTId=PRO_0000146764. FT DOMAIN 117 618 Biotin carboxylation. FT DOMAIN 275 466 ATP-grasp. FT DOMAIN 752 818 Biotinyl-binding. FT DOMAIN 1698 2194 Carboxyltransferase. FT NP_BIND 315 320 ATP (Potential). FT ACT_SITE 441 441 By similarity. FT METAL 424 424 Manganese 1 (By similarity). FT METAL 437 437 Manganese 1 (By similarity). FT METAL 437 437 Manganese 2 (By similarity). FT METAL 439 439 Manganese 2 (By similarity). FT BINDING 1823 1823 Coenzyme A (By similarity). FT BINDING 2127 2127 Coenzyme A (By similarity). FT BINDING 2129 2129 Coenzyme A (By similarity). FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 5 5 Phosphoserine. FT MOD_RES 23 23 Phosphoserine. FT MOD_RES 25 25 Phosphoserine. FT MOD_RES 29 29 Phosphoserine. FT MOD_RES 53 53 Phosphoserine. FT MOD_RES 78 78 Phosphoserine (By similarity). FT MOD_RES 80 80 Phosphoserine. FT MOD_RES 488 488 Phosphoserine. FT MOD_RES 786 786 N6-biotinyllysine (By similarity). FT MOD_RES 1201 1201 Phosphoserine (By similarity). FT MOD_RES 1216 1216 Phosphoserine (By similarity). FT MOD_RES 1263 1263 Phosphoserine. FT MOD_RES 1334 1334 N6-acetyllysine. FT VAR_SEQ 1 78 Missing (in isoform 3). FT /FTId=VSP_026098. FT VAR_SEQ 1 75 MDEPSPLAQPLELNQHSRFIIGSVSEDNSEDEISNLVKLDL FT LEEKEGSLSPASVGSDTLSDLGISSLQDGLALHI -> MEG FT SPEENKEMRYYMLQ (in isoform 2). FT /FTId=VSP_026099. FT VAR_SEQ 1 1 M -> MWWSTLMSILRARSFWKWISTQTVRIIRAVRAHFGG FT IM (in isoform 4). FT /FTId=VSP_026100. FT VARIANT 838 838 R -> W (in dbSNP:rs2287351). FT /FTId=VAR_042941. FT VARIANT 1687 1687 R -> Q (in a colorectal cancer sample; FT somatic mutation). FT /FTId=VAR_036514. FT VARIANT 2271 2271 A -> V (rare polymorphism; frequency FT <0.004; may play a role in breast cancer FT susceptibility). FT /FTId=VAR_028929. FT MUTAGEN 78 78 S->A: No effect on interaction with FT BRCA1. FT MUTAGEN 344 344 S->A: No effect on interaction with FT BRCA1. FT MUTAGEN 432 432 S->A: No effect on interaction with FT BRCA1. FT MUTAGEN 1201 1201 S->A: No effect on interaction with FT BRCA1. FT MUTAGEN 1263 1263 S->A: Abolishes interaction with BRCA1. FT MUTAGEN 1585 1585 S->A: No effect on interaction with FT BRCA1. FT MUTAGEN 1952 1952 S->A: No effect on interaction with FT BRCA1. FT MUTAGEN 2211 2211 S->A: No effect on interaction with FT BRCA1. FT CONFLICT 66 66 S -> A (in Ref. 1; AAC50139). FT CONFLICT 79 79 M -> W (in Ref. 1; AAC50139). FT CONFLICT 89 89 R -> G (in Ref. 1; AAC50139). FT CONFLICT 182 182 P -> A (in Ref. 1; AAC50139). FT CONFLICT 234 234 S -> N (in Ref. 1; AAC50139). FT CONFLICT 299 299 Q -> K (in Ref. 1; AAC50139). FT CONFLICT 303 303 E -> K (in Ref. 1; AAC50139). FT CONFLICT 364 364 A -> V (in Ref. 2; AAP94122). FT CONFLICT 446 446 H -> Q (in Ref. 1; AAC50139). FT CONFLICT 494 494 D -> N (in Ref. 1; AAC50139). FT CONFLICT 554 554 D -> G (in Ref. 1; AAC50139). FT CONFLICT 622 622 Q -> R (in Ref. 1; AAC50139). FT CONFLICT 640 640 A -> G (in Ref. 1; AAC50139). FT CONFLICT 814 814 V -> I (in Ref. 2; AAP94122). FT CONFLICT 1061 1061 N -> S (in Ref. 1; AAC50139). FT CONFLICT 1094 1095 EL -> DV (in Ref. 1; AAC50139). FT CONFLICT 1225 1225 S -> A (in Ref. 1; AAC50139). FT CONFLICT 1257 1257 S -> C (in Ref. 1; AAC50139). FT CONFLICT 1297 1297 C -> G (in Ref. 1; AAC50139). FT CONFLICT 1320 1320 V -> A (in Ref. 1; AAC50139). FT CONFLICT 1444 1444 N -> S (in Ref. 1; AAC50139). FT CONFLICT 1474 1474 F -> L (in Ref. 1; AAC50139). FT CONFLICT 1665 1666 TF -> SL (in Ref. 1; AAC50139). FT CONFLICT 1677 1677 I -> V (in Ref. 1; AAC50139). FT CONFLICT 1741 1741 P -> S (in Ref. 1; AAC50139). FT CONFLICT 1762 1762 S -> G (in Ref. 1; AAC50139). FT CONFLICT 1822 1822 C -> S (in Ref. 1; AAC50139). FT CONFLICT 1875 1875 M -> T (in Ref. 1; AAC50139). FT CONFLICT 1888 1888 D -> G (in Ref. 1; AAC50139). FT CONFLICT 1997 1997 I -> V (in Ref. 1; AAC50139). FT CONFLICT 2013 2013 Q -> H (in Ref. 1; AAC50139). FT CONFLICT 2058 2058 D -> H (in Ref. 1; AAC50139). FT CONFLICT 2075 2075 C -> S (in Ref. 1; AAC50139). FT CONFLICT 2098 2099 SS -> PT (in Ref. 1; AAC50139). FT CONFLICT 2158 2159 TA -> PT (in Ref. 1; AAC50139). FT CONFLICT 2166 2166 N -> S (in Ref. 1; AAC50139). FT CONFLICT 2234 2234 N -> S (in Ref. 1; AAC50139). FT CONFLICT 2321 2321 H -> R (in Ref. 2; AAP94122). FT HELIX 105 111 FT STRAND 120 123 FT HELIX 127 145 FT STRAND 150 157 FT HELIX 159 163 FT HELIX 168 171 FT STRAND 172 177 FT HELIX 183 185 FT TURN 186 188 FT HELIX 190 199 FT STRAND 203 206 FT TURN 211 214 FT HELIX 217 224 FT STRAND 228 231 FT HELIX 234 241 FT HELIX 243 252 FT TURN 261 264 FT HELIX 283 289 FT HELIX 294 304 FT STRAND 306 312 FT STRAND 320 324 FT TURN 327 329 FT HELIX 330 340 FT STRAND 346 350 FT STRAND 356 364 FT STRAND 370 382 FT STRAND 385 392 FT HELIX 398 415 FT STRAND 419 427 FT STRAND 433 439 FT TURN 444 446 FT HELIX 447 453 FT HELIX 457 465 FT HELIX 470 472 FT HELIX 474 479 FT TURN 492 495 FT STRAND 496 498 FT STRAND 503 510 FT STRAND 526 530 FT STRAND 537 542 FT STRAND 557 566 FT HELIX 567 582 FT HELIX 589 599 FT HELIX 601 604 FT HELIX 612 616 FT HELIX 1582 1592 FT HELIX 1598 1600 FT HELIX 1601 1619 FT HELIX 1628 1631 FT STRAND 1632 1639 FT STRAND 1645 1648 FT STRAND 1656 1666 FT STRAND 1675 1682 FT HELIX 1687 1689 FT HELIX 1693 1709 FT STRAND 1713 1717 FT HELIX 1728 1731 FT STRAND 1735 1739 FT HELIX 1744 1746 FT STRAND 1748 1753 FT HELIX 1755 1761 FT HELIX 1762 1764 FT STRAND 1767 1774 FT STRAND 1777 1785 FT HELIX 1795 1813 FT STRAND 1816 1820 FT STRAND 1822 1825 FT HELIX 1827 1834 FT STRAND 1837 1841 FT STRAND 1845 1849 FT HELIX 1851 1858 FT HELIX 1866 1870 FT HELIX 1872 1875 FT TURN 1876 1879 FT STRAND 1882 1887 FT HELIX 1888 1899 FT STRAND 1914 1917 FT HELIX 1934 1939 FT STRAND 1944 1946 FT STRAND 1961 1964 FT STRAND 1971 1978 FT STRAND 1981 1988 FT STRAND 1993 1996 FT STRAND 2010 2013 FT HELIX 2020 2036 FT STRAND 2040 2043 FT HELIX 2053 2057 FT HELIX 2060 2072 FT STRAND 2078 2082 FT STRAND 2087 2089 FT HELIX 2090 2094 FT HELIX 2098 2100 FT TURN 2102 2104 FT STRAND 2105 2110 FT STRAND 2114 2118 FT HELIX 2120 2127 FT HELIX 2130 2140 FT HELIX 2142 2150 FT HELIX 2158 2188 FT HELIX 2193 2198 FT STRAND 2201 2206 FT HELIX 2208 2210 FT HELIX 2211 2235 FT HELIX 2241 2256 FT HELIX 2258 2265 FT HELIX 2267 2278 FT HELIX 2289 2310 FT HELIX 2312 2314 FT HELIX 2315 2322 FT HELIX 2323 2325 FT HELIX 2328 2337 SQ SEQUENCE 2346 AA; 265554 MW; F1F0A518F8824FFC CRC64; MDEPSPLAQP LELNQHSRFI IGSVSEDNSE DEISNLVKLD LLEEKEGSLS PASVGSDTLS DLGISSLQDG LALHIRSSMS GLHLVKQGRD RKKIDSQRDF TVASPAEFVT RFGGNKVIEK VLIANNGIAA VKCMRSIRRW SYEMFRNERA IRFVVMVTPE DLKANAEYIK MADHYVPVPG GPNNNNYANV ELILDIAKRI PVQAVWAGWG HASENPKLPE LLLKNGIAFM GPPSQAMWAL GDKIASSIVA QTAGIPTLPW SGSGLRVDWQ ENDFSKRILN VPQELYEKGY VKDVDDGLQA AEEVGYPVMI KASEGGGGKG IRKVNNADDF PNLFRQVQAE VPGSPIFVMR LAKQSRHLEV QILADQYGNA ISLFGRDCSV QRRHQKIIEE APATIATPAV FEHMEQCAVK LAKMVGYVSA GTVEYLYSQD GSFYFLELNP RLQVEHPCTE MVADVNLPAA QLQIAMGIPL YRIKDIRMMY GVSPWGDSPI DFEDSAHVPC PRGHVIAARI TSENPDEGFK PSSGTVQELN FRSNKNVWGY FSVAAAGGLH EFADSQFGHC FSWGENREEA ISNMVVALKE LSIRGDFRTT VEYLIKLLET ESFQMNRIDT GWLDRLIAEK VQAERPDTML GVVCGALHVA DVSLRNSVSN FLHSLERGQV LPAHTLLNTV DVELIYEGVK YVLKVTRQSP NSYVVIMNGS CVEVDVHRLS DGGLLLSYDG SSYTTYMKEE VDRYRITIGN KTCVFEKEND PSVMRSPSAG KLIQYIVEDG GHVFAGQCYA EIEVMKMVMT LTAVESGCIH YVKRPGAALD PGCVLAKMQL DNPSKVQQAE LHTGSLPRIQ STALRGEKLH RVFHYVLDNL VNVMNGYCLP DPFFSSKVKD WVERLMKTLR DPSLPLLELQ DIMTSVSGRI PPNVEKSIKK EMAQYASNIT SVLCQFPSQQ IANILDSHAA TLNRKSEREV FFMNTQSIVQ LVQRYRSGIR GHMKAVVMDL LRQYLRVETQ FQNGHYDKCV FALREENKSD MNTVLNYIFS HAQVTKKNLL VTMLIDQLCG RDPTLTDELL NILTELTQLS KTTNAKVALR ARQVLIASHL PSYELRHNQV ESIFLSAIDM YGHQFCIENL QKLILSETSI FDVLPNFFYH SNQVVRMAAL EVYVRRAYIA YELNSVQHRQ LKDNTCVVEF QFMLPTSHPN RGNIPTLNRM SFSSNLNHYG MTHVASVSDV LLDNSFTPPC QRMGGMVSFR TFEDFVRIFD EVMGCFSDSP PQSPTFPEAG HTSLYDEDKV PRDEPIHILN VAIKTDCDIE DDRLAAMFRE FTQQNKATLV DHGIRRLTFL VAQKDFRKQV NYEVDRRFHR EFPKFFTFRA RDKFEEDRIY RHLEPALAFQ LELNRMRNFD LTAIPCANHK MHLYLGAAKV EVGTEVTDYR FFVRAIIRHS DLVTKEASFE YLQNEGERLL LEAMDELEVA FNNTNVRTDC NHIFLNFVPT VIMDPSKIEE SVRSMVMRYG SRLWKLRVLQ AELKINIRLT PTGKAIPIRL FLTNESGYYL DISLYKEVTD SRTAQIMFQA YGDKQGPLHG MLINTPYVTK DLLQSKRFQA QSLGTTYIYD IPEMFRQSLI KLWESMSTQA FLPSPPLPSD MLTYTELVLD DQGQLVHMNR LPGGNEIGMV AWKMTFKSPE YPEGRDIIVI GNDITYRIGS FGPQEDLLFL RASELARAEG IPRIYVSANS GARIGLAEEI RHMFHVAWVD PEDPYKGYRY LYLTPQDYKR VSALNSVHCE HVEDEGESRY KITDIIGKEE GIGPENLRGS GMIAGESSLA YNEIITISLV TCRAIGIGAY LVRLGQRTIQ VENSHLILTG AGALNKVLGR EVYTSNNQLG GIQIMHNNGV THCTVCDDFE GVFTVLHWLS YMPKSVHSSV PLLNSKDPID RIIEFVPTKT PYDPRWMLAG RPHPTQKGQW LSGFFDYGSF SEIMQPWAQT VVVGRARLGG IPVGVVAVET RTVELSIPAD PANLDSEAKI IQQAGQVWFP DSAFKTYQAI KDFNREGLPL MVFANWRGFS GGMKDMYDQV LKFGAYIVDG LRECCQPVLV YIPPQAELRG GSWVVIDSSI NPRHMEMYAD RESRGSVLEP EGTVEIKFRR KDLVKTMRRV DPVYIHLAER LGTPELSTAE RKELENKLKE REEFLIPIYH QVAVQFADLH DTPGRMQEKG VISDILDWKT SRTFFYWRLR RLLLEDLVKK KIHNANPELT DGQIQAMLRR WFVEVEGTVK AYVWDNNKDL AEWLEKQLTE EDGVHSVIEE NIKCISRDYV LKQIRSLVQA NPEVAMDSII HMTQHISPTQ RAEVIRILST MDSPST // ID ACADM_HUMAN Reviewed; 421 AA. AC P11310; Q5T4U4; Q9NYF1; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 09-JUL-2014, entry version 174. DE RecName: Full=Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; DE Short=MCAD; DE EC=1.3.8.7; DE Flags: Precursor; GN Name=ACADM; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3035565; DOI=10.1073/pnas.84.12.4068; RA Kelly D.P., Kim J.-J.P., Billadello J.J., Hainline B.E., Chu T.W., RA Strauss A.W.; RT "Nucleotide sequence of medium-chain acyl-CoA dehydrogenase mRNA and RT its expression in enzyme-deficient human tissue."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4068-4072(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=1731887; DOI=10.1021/bi00116a013; RA Zhang Z.F., Kelly D.P., Kim J.-J.P., Zhou Y.Q., Ogden M.L., RA Whelan A.J., Strauss A.W.; RT "Structural organization and regulatory regions of the human medium- RT chain acyl-CoA dehydrogenase gene."; RL Biochemistry 31:81-89(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Colon; RA Sun F., Wang Y., Block G.D.; RT "Medium-chain acyl-CoA dehydrogenase."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Heart; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 218-235, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Vishwanath V.; RL Submitted (MAR-2007) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-342, AND VARIANT ACADMD RP GLU-329. RX PubMed=2393404; DOI=10.1016/0006-291X(90)91421-N; RA Matsubara Y., Narisawa K., Miyabayashi S., Tada K., Coates P.M., RA Bachmann C., Elsas L.J. II, Pollitt R.J., Rhead W.J., Roe C.R.; RT "Identification of a common mutation in patients with medium-chain RT acyl-CoA dehydrogenase deficiency."; RL Biochem. Biophys. Res. Commun. 171:498-505(1990). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279 AND LYS-301, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP DEACETYLATION BY SIRT3. RX PubMed=24121500; DOI=10.1074/jbc.M113.510354; RA Bharathi S.S., Zhang Y., Mohsen A.W., Uppala R., Balasubramani M., RA Schreiber E., Uechi G., Beck M.E., Rardin M.J., Vockley J., Verdin E., RA Gibson B.W., Hirschey M.D., Goetzman E.S.; RT "SIRT3 regulates long-chain acyl-coA dehydrogenase by deacetylating RT conserved lysines near the active site."; RL J. Biol. Chem. 288:33837-33847(2013). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH FAD AND RP OCTANOYL-COENZYME A, AND SUBUNIT. RX PubMed=8823176; DOI=10.1021/bi9607867; RA Lee H.J., Wang M., Paschke R., Nandy A., Ghisla S., Kim J.-J.P.; RT "Crystal structures of the wild type and the Glu376Gly/Thr255Glu RT mutant of human medium-chain acyl-CoA dehydrogenase: influence of the RT location of the catalytic base on substrate specificity."; RL Biochemistry 35:12412-12420(1996). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 26-421 IN COMPLEXES WITH FAD RP AND THE ETFA-ETFB HETERODIMER, MUTAGENESIS OF LEU-86; LEU-98; LEU-100; RP ILE-108; GLU-237 AND GLU-384, AND SUBUNIT. RX PubMed=15159392; DOI=10.1074/jbc.M404884200; RA Toogood H.S., van Thiel A., Basran J., Sutcliffe M.J., Scrutton N.S., RA Leys D.; RT "Extensive domain motion and electron transfer in the human electron RT transferring flavoprotein-medium chain acyl-CoA dehydrogenase RT complex."; RL J. Biol. Chem. 279:32904-32912(2004). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEXES WITH FAD AND THE RP ETFA-ETFB HETERODIMER, MUTAGENESIS OF TRP-191; GLU-237 AND GLU-384, RP AND SUBUNIT. RX PubMed=15975918; DOI=10.1074/jbc.M505562200; RA Toogood H.S., van Thiel A., Scrutton N.S., Leys D.; RT "Stabilization of non-productive conformations underpins rapid RT electron transfer to electron-transferring flavoprotein."; RL J. Biol. Chem. 280:30361-30366(2005). RN [16] RP REVIEW ON VARIANTS ACADMD. RX PubMed=1363805; DOI=10.1002/humu.1380010402; RA Tanaka K., Yokota I., Coates P.M., Strauss A.W., Kelly D.P., RA Zhang Z.F., Gregersen N., Andresen B.S., Matsubara Y., Curtis D., RA Chen Y.-T.; RT "Mutations in the medium chain acyl-CoA dehydrogenase (MCAD) gene."; RL Hum. Mutat. 1:271-279(1992). RN [17] RP VARIANT ACADMD GLU-329. RX PubMed=2394825; DOI=10.1172/JCI114761; RA Yokota I., Indo Y., Coates P.M., Tanaka K.; RT "Molecular basis of medium chain acyl-coenzyme A dehydrogenase RT deficiency. An A to G transition at position 985 that causes a lysine- RT 304 to glutamate substitution in the mature protein is the single RT prevalent mutation."; RL J. Clin. Invest. 86:1000-1003(1990). RN [18] RP VARIANT ACADMD GLU-329. RX PubMed=2251268; DOI=10.1073/pnas.87.23.9236; RA Kelly D.P., Whelan A.J., Ogden M.L., Alpers R., Zhang Z.F., Bellus G., RA Gregersen N., Dorland L., Strauss A.W.; RT "Molecular characterization of inherited medium-chain acyl-CoA RT dehydrogenase deficiency."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9236-9240(1990). RN [19] RP VARIANTS ACADMD ILE-149; ARG-244; ARG-267 AND THR-375. RX PubMed=1684086; RA Yokota I., Coates P.M., Hale D.E., Rinaldo P., Tanaka K.; RT "Molecular survey of a prevalent mutation, 985A-to-G transition, and RT identification of five infrequent mutations in the medium-chain Acyl- RT CoA dehydrogenase (MCAD) gene in 55 patients with MCAD deficiency."; RL Am. J. Hum. Genet. 49:1280-1291(1991). RN [20] RP VARIANT ACADMD GLU-329. RX PubMed=1902818; DOI=10.1007/BF00201539; RA Gregersen N., Andresen B.S., Bross P., Winter V., Ruediger N., RA Engst S., Christensen E., Kelly D., Strauss A.W., Koelvraa S., RA Bolund L., Ghisla S.; RT "Molecular characterization of medium-chain acyl-CoA dehydrogenase RT (MCAD) deficiency: identification of a lys329 to glu mutation in the RT MCAD gene, and expression of inactive mutant enzyme protein in E. RT coli."; RL Hum. Genet. 86:545-551(1991). RN [21] RP VARIANT ACADMD GLU-329 FREQUENCY. RX PubMed=1671131; DOI=10.1016/0140-6736(91)90907-7; RA Blakemore A.I., Singleton H., Pollitt R.J., Engel P.C., Kolvraa S., RA Gregersen N., Curtis D.; RT "Frequency of the G985 MCAD mutation in the general population."; RL Lancet 337:298-299(1991). RN [22] RP VARIANTS ACADMD THR-326 AND ARG-336. RX PubMed=8198141; RA Andresen B.S., Jensen T.G., Bross P., Knudsen I., Winter V., RA Koelvraa S., Bolund L., Ding J.-H., Chen Y.-T., van Hove J.L.K., RA Curtis D., Yokota I., Tanaka K., Kim J.-J.P., Gregersen N.; RT "Disease-causing mutations in exon 11 of the medium-chain acyl-CoA RT dehydrogenase gene."; RL Am. J. Hum. Genet. 54:975-988(1994). RN [23] RP VARIANT ACADMD 115-GLY-CYS-116 DEL. RX PubMed=7603790; DOI=10.1203/00006450-199505000-00021; RA Ziadeh R., Hoffman E.P., Finegold D.N., Hoop R.C., Brackett J.C., RA Strauss A.W., Naylor E.W.; RT "Medium chain acyl-CoA dehydrogenase deficiency in Pennsylvania: RT neonatal screening shows high incidence and unexpected mutation RT frequencies."; RL Pediatr. Res. 37:675-678(1995). RN [24] RP VARIANT ACADMD ARG-195. RX PubMed=7929823; DOI=10.1172/JCI117486; RA Brackett J.C., Sims H.F., Steiner R.D., Nunge M., Zimmerman E.M., RA Demartinville B., Rinaldo P., Slaugh R., Strauss A.W.; RT "A novel mutation in medium chain acyl-CoA dehydrogenase causes sudden RT neonatal death."; RL J. Clin. Invest. 94:1477-1483(1994). RN [25] RP VARIANTS ACADMD TYR-116; ALA-193 AND CYS-352. RX PubMed=9158144; DOI=10.1093/hmg/6.5.695; RA Andresen B.S., Bross P., Udvari S., Kirk J., Gray G., Kmoch S., RA Chamoles N., Knudsen I., Winter V., Wilcken B., Yokota I., Hart K., RA Packman S., Harpey J.P., Saudubray J.-M., Hale D.E., Bolund L., RA Koelvraa S., Gregersen N.; RT "The molecular basis of medium-chain acyl-CoA dehydrogenase (MCAD) RT deficiency in compound heterozygous patients: is there correlation RT between genotype and phenotype?"; RL Hum. Mol. Genet. 6:695-707(1997). RN [26] RP CHARACTERIZATION OF VARIANT ACADMD ALA-193. RX PubMed=9882619; DOI=10.1042/0264-6021:3370225; RA Kuchler B., Abdel-Ghany A.G., Bross P., Nandy A., Rasched I., RA Ghisla S.; RT "Biochemical characterization of a variant human medium-chain acyl-CoA RT dehydrogenase with a disease-associated mutation localized in the RT active site."; RL Biochem. J. 337:225-230(1999). RN [27] RP VARIANTS ACADMD LEU-206 AND GLU-329. RX PubMed=10767181; DOI=10.1006/mgme.2000.2978; RA Yang B.-Z., Ding J.-H., Zhou C., Dimachkie M.M., Sweetman L., RA Dasouki M.J., Wilkinson J., Roe C.R.; RT "Identification of a novel mutation in patients with medium-chain RT acyl-CoA dehydrogenase deficiency."; RL Mol. Genet. Metab. 69:259-262(2000). RN [28] RP VARIANTS ACADMD HIS-67; THR-78; ILE-121 AND ARG-310. RX PubMed=11349232; DOI=10.1086/320602; RA Andresen B.S., Dobrowolski S.F., O'Reilly L., Muenzer J., RA McCandless S.E., Frazier D.M., Udvari S., Bross P., Knudsen I., RA Banas R., Chace D.H., Engel P.C., Naylor E.W., Gregersen N.; RT "Medium-chain acyl-CoA dehydrogenase (MCAD) mutations identified by RT MS/MS-based prospective screening of newborns differ from those RT observed in patients with clinical symptoms: identification and RT characterization of a new, prevalent mutation that results in mild RT MCAD deficiency."; RL Am. J. Hum. Genet. 68:1408-1418(2001). RN [29] RP VARIANT ACADMD LEU-245. RX PubMed=11409868; DOI=10.1007/s004390100501; RA Zschocke J., Schulze A., Lindner M., Fiesel S., Olgemoller K., RA Hoffmann G.F., Penzien J., Ruiter J.P.N., Wanders R.J.A., RA Mayatepek E.; RT "Molecular and functional characterization of mild MCAD deficiency."; RL Hum. Genet. 108:404-408(2001). RN [30] RP VARIANTS ACADMD THR-281 AND GLU-329. RX PubMed=11486912; DOI=10.1023/A:1010533408635; RA Albers S., Levy H.L., Irons M., Strauss A.W., Marsden D.; RT "Compound heterozygosity in four asymptomatic siblings with medium- RT chain acyl-CoA dehydrogenase deficiency."; RL J. Inherit. Metab. Dis. 24:417-418(2001). RN [31] RP VARIANT [LARGE SCALE ANALYSIS] ARG-132. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: This enzyme is specific for acyl chain lengths of 4 to CC 16. CC -!- CATALYTIC ACTIVITY: A medium-chain acyl-CoA + electron-transfer CC flavoprotein = a medium-chain trans-2,3-dehydroacyl-CoA + reduced CC electron-transfer flavoprotein. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta- CC oxidation. CC -!- SUBUNIT: Homotetramer. Interacts with the heterodimeric electron CC transfer flavoprotein ETF. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P11310-1; Sequence=Displayed; CC Name=2; CC IsoId=P11310-2; Sequence=VSP_038420; CC -!- PTM: Acetylation at Lys-307 and Lys-311 in proximity of the CC cofactor-binding sites reduces catalytic activity (By similarity). CC These sites are deacetylated by SIRT3. CC -!- DISEASE: Acyl-CoA dehydrogenase medium-chain deficiency (ACADMD) CC [MIM:201450]: An inborn error of mitochondrial fatty acid beta- CC oxidation which causes fasting hypoglycemia, hepatic dysfunction CC and encephalopathy, often resulting in death in infancy. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases CC of different substrate specificities are present in mammalian CC tissues. CC -!- MISCELLANEOUS: Utilizes the electron transfer flavoprotein (ETF) CC as electron acceptor that transfers the electrons to the main CC mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase CC (ETF dehydrogenase). CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M16827; AAA51566.1; -; mRNA. DR EMBL; M91432; AAA59567.1; -; Genomic_DNA. DR EMBL; M91421; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; M91422; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; M91423; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; M91425; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; M91426; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; M91427; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; M91428; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; M91429; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; M91430; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; M91431; AAA59567.1; JOINED; Genomic_DNA. DR EMBL; AF251043; AAF63626.1; -; mRNA. DR EMBL; AK312629; BAG35514.1; -; mRNA. DR EMBL; AL357314; CAI22390.1; -; Genomic_DNA. DR EMBL; CH471059; EAX06401.1; -; Genomic_DNA. DR EMBL; BC005377; AAH05377.1; -; mRNA. DR EMBL; M60505; AAB59625.1; -; Genomic_DNA. DR CCDS; CCDS44165.1; -. [P11310-2] DR CCDS; CCDS668.1; -. [P11310-1] DR PIR; A29031; DEHUCM. DR RefSeq; NP_000007.1; NM_000016.5. [P11310-1] DR RefSeq; NP_001120800.1; NM_001127328.2. [P11310-2] DR UniGene; Hs.445040; -. DR PDB; 1EGC; X-ray; 2.60 A; A/B/C/D=26-421. DR PDB; 1EGD; X-ray; 2.40 A; A/B/C/D=26-421. DR PDB; 1EGE; X-ray; 2.75 A; A/B/C/D=26-421. DR PDB; 1T9G; X-ray; 2.90 A; A/B/C/D=26-421. DR PDB; 2A1T; X-ray; 2.80 A; A/B/C/D=1-421. DR PDBsum; 1EGC; -. DR PDBsum; 1EGD; -. DR PDBsum; 1EGE; -. DR PDBsum; 1T9G; -. DR PDBsum; 2A1T; -. DR ProteinModelPortal; P11310; -. DR SMR; P11310; 35-421. DR BioGrid; 106552; 10. DR DIP; DIP-34281N; -. DR IntAct; P11310; 6. DR MINT; MINT-3007693; -. DR STRING; 9606.ENSP00000409612; -. DR PhosphoSite; P11310; -. DR DMDM; 113017; -. DR REPRODUCTION-2DPAGE; IPI00005040; -. DR UCD-2DPAGE; P11310; -. DR MaxQB; P11310; -. DR PaxDb; P11310; -. DR PRIDE; P11310; -. DR DNASU; 34; -. DR Ensembl; ENST00000370841; ENSP00000359878; ENSG00000117054. [P11310-1] DR Ensembl; ENST00000420607; ENSP00000409612; ENSG00000117054. [P11310-2] DR GeneID; 34; -. DR KEGG; hsa:34; -. DR UCSC; uc001dgw.4; human. [P11310-1] DR UCSC; uc009wbp.3; human. [P11310-2] DR CTD; 34; -. DR GeneCards; GC01P076190; -. DR GeneReviews; ACADM; -. DR HGNC; HGNC:89; ACADM. DR HPA; HPA006198; -. DR HPA; HPA026542; -. DR MIM; 201450; phenotype. DR MIM; 607008; gene. DR neXtProt; NX_P11310; -. DR Orphanet; 42; Medium chain acyl-CoA dehydrogenase deficiency. DR PharmGKB; PA24425; -. DR eggNOG; COG1960; -. DR HOGENOM; HOG000131659; -. DR HOVERGEN; HBG000224; -. DR KO; K00249; -. DR OrthoDB; EOG74FF0S; -. DR PhylomeDB; P11310; -. DR TreeFam; TF105020; -. DR BioCyc; MetaCyc:HS04089-MONOMER; -. DR Reactome; REACT_111217; Metabolism. DR SABIO-RK; P11310; -. DR UniPathway; UPA00660; -. DR EvolutionaryTrace; P11310; -. DR GenomeRNAi; 34; -. DR NextBio; 131; -. DR PRO; PR:P11310; -. DR ArrayExpress; P11310; -. DR Bgee; P11310; -. DR CleanEx; HS_ACADM; -. DR Genevestigator; P11310; -. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb. DR GO; GO:0005634; C:nucleus; IDA:UniProt. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IMP:UniProtKB. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL. DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IDA:BHF-UCL. DR GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl. DR GO; GO:0045329; P:carnitine biosynthetic process; IMP:BHF-UCL. DR GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IMP:BHF-UCL. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:UniProtKB. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:BHF-UCL. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:Ensembl. DR GO; GO:0001889; P:liver development; IEA:Ensembl. DR GO; GO:0051793; P:medium-chain fatty acid catabolic process; IDA:BHF-UCL. DR GO; GO:0051791; P:medium-chain fatty acid metabolic process; IDA:BHF-UCL. DR GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0006111; P:regulation of gluconeogenesis; IEA:Ensembl. DR GO; GO:0009409; P:response to cold; IEA:Ensembl. DR GO; GO:0042594; P:response to starvation; IEA:Ensembl. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disease mutation; FAD; KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Mitochondrion; KW Oxidoreductase; Polymorphism; Reference proteome; Transit peptide. FT TRANSIT 1 25 Mitochondrion. FT CHAIN 26 421 Medium-chain specific acyl-CoA FT dehydrogenase, mitochondrial. FT /FTId=PRO_0000000502. FT NP_BIND 158 167 FAD. FT NP_BIND 191 193 FAD. FT NP_BIND 306 308 FAD. FT NP_BIND 316 317 FAD. FT NP_BIND 374 378 FAD. FT NP_BIND 403 405 FAD. FT REGION 278 281 Substrate binding. FT ACT_SITE 401 401 Proton acceptor. FT BINDING 167 167 Substrate; via carbonyl oxygen. FT BINDING 216 216 Substrate. FT BINDING 402 402 Substrate; via amide nitrogen. FT BINDING 413 413 Substrate. FT MOD_RES 69 69 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 69 69 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 179 179 N6-succinyllysine (By similarity). FT MOD_RES 212 212 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 212 212 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 217 217 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 217 217 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 259 259 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 259 259 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 271 271 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 271 271 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 279 279 N6-acetyllysine. FT MOD_RES 301 301 N6-acetyllysine. FT VAR_SEQ 10 10 R -> RCSLQ (in isoform 2). FT /FTId=VSP_038420. FT VARIANT 53 53 R -> C (in ACADMD). FT /FTId=VAR_000317. FT VARIANT 67 67 Y -> H (in ACADMD; mild). FT /FTId=VAR_013698. FT VARIANT 78 78 I -> T (in ACADMD). FT /FTId=VAR_015954. FT VARIANT 115 116 Missing (in ACADMD). FT /FTId=VAR_000318. FT VARIANT 116 116 C -> Y (in ACADMD). FT /FTId=VAR_015955. FT VARIANT 121 121 T -> I (in ACADMD). FT /FTId=VAR_015956. FT VARIANT 132 132 P -> R (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_035716. FT VARIANT 149 149 M -> I (in ACADMD). FT /FTId=VAR_000319. FT VARIANT 193 193 T -> A (in ACADMD; the thermostability is FT markedly decreased). FT /FTId=VAR_000320. FT VARIANT 195 195 G -> R (in ACADMD). FT /FTId=VAR_000321. FT VARIANT 206 206 R -> L (in ACADMD). FT /FTId=VAR_015957. FT VARIANT 244 244 C -> R (in ACADMD). FT /FTId=VAR_000322. FT VARIANT 245 245 S -> L (in ACADMD). FT /FTId=VAR_013699. FT VARIANT 267 267 G -> R (in ACADMD). FT /FTId=VAR_000323. FT VARIANT 281 281 R -> T (in ACADMD; mild or benign FT clinical phenotype). FT /FTId=VAR_013700. FT VARIANT 310 310 G -> R (in ACADMD). FT /FTId=VAR_015958. FT VARIANT 326 326 M -> T (in ACADMD). FT /FTId=VAR_000324. FT VARIANT 329 329 K -> E (in ACADMD; most common variant; FT dbSNP:rs77931234). FT /FTId=VAR_000325. FT VARIANT 336 336 S -> R (in ACADMD). FT /FTId=VAR_000326. FT VARIANT 352 352 Y -> C (in ACADMD). FT /FTId=VAR_015959. FT VARIANT 375 375 I -> T (in ACADMD). FT /FTId=VAR_000327. FT MUTAGEN 86 86 L->M: Strongly reduced rate of electron FT transfer to ETF. FT MUTAGEN 98 98 L->W: Strongly reduced rate of electron FT transfer to ETF. FT MUTAGEN 100 100 L->Y: Strongly reduced rate of electron FT transfer to ETF. FT MUTAGEN 108 108 I->M: Strongly reduced rate of electron FT transfer to ETF. FT MUTAGEN 191 191 W->A: Loss of electron transfer to ETF. FT MUTAGEN 191 191 W->F: Reduces rate of electron transfer FT to ETF about six-fold. FT MUTAGEN 237 237 E->A: Strongly reduced rate of electron FT transfer to ETF. FT MUTAGEN 384 384 E->A: Reduces rate of electron transfer FT to ETF three-fold. FT MUTAGEN 384 384 E->Q: Reduces rate of electron transfer FT to ETF two-fold. FT CONFLICT 356 356 I -> T (in Ref. 3; AAF63626). FT STRAND 36 38 FT HELIX 43 59 FT HELIX 61 70 FT HELIX 75 84 FT HELIX 93 95 FT HELIX 102 115 FT HELIX 117 129 FT HELIX 131 136 FT HELIX 139 151 FT STRAND 156 159 FT STRAND 165 168 FT HELIX 169 171 FT STRAND 175 178 FT STRAND 180 193 FT TURN 194 197 FT STRAND 199 206 FT HELIX 215 217 FT STRAND 219 225 FT STRAND 231 233 FT STRAND 239 241 FT STRAND 247 258 FT HELIX 259 261 FT STRAND 262 265 FT TURN 266 268 FT HELIX 269 303 FT STRAND 309 312 FT HELIX 313 315 FT HELIX 317 345 FT HELIX 351 376 FT HELIX 377 379 FT HELIX 387 394 FT HELIX 395 398 FT TURN 399 401 FT HELIX 404 417 SQ SEQUENCE 421 AA; 46588 MW; 7CD0B5832410581B CRC64; MAAGFGRCCR VLRSISRFHW RSQHTKANRQ REPGLGFSFE FTEQQKEFQA TARKFAREEI IPVAAEYDKT GEYPVPLIRR AWELGLMNTH IPENCGGLGL GTFDACLISE ELAYGCTGVQ TAIEGNSLGQ MPIIIAGNDQ QKKKYLGRMT EEPLMCAYCV TEPGAGSDVA GIKTKAEKKG DEYIINGQKM WITNGGKANW YFLLARSDPD PKAPANKAFT GFIVEADTPG IQIGRKELNM GQRCSDTRGI VFEDVKVPKE NVLIGDGAGF KVAMGAFDKT RPVVAAGAVG LAQRALDEAT KYALERKTFG KLLVEHQAIS FMLAEMAMKV ELARMSYQRA AWEVDSGRRN TYYASIAKAF AGDIANQLAT DAVQILGGNG FNTEYPVEKL MRDAKIYQIY EGTSQIQRLI VAREHIDKYK N // ID ACADV_HUMAN Reviewed; 655 AA. AC P49748; B4DEB6; F5H2A9; O76056; Q8WUL0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 09-JUL-2014, entry version 151. DE RecName: Full=Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; DE Short=VLCAD; DE EC=1.3.8.9; DE Flags: Precursor; GN Name=ACADVL; Synonyms=VLCAD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=7668252; RA Aoyama T., Souri M., Ueno I., Kamijo T., Yamaguchi S., Rhead W.J., RA Tanaka K., Hashimoto T.; RT "Cloning of human very-long-chain acyl-coenzyme A dehydrogenase and RT molecular characterization of its deficiency in two patients."; RL Am. J. Hum. Genet. 57:273-283(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP VARIANTS. RC TISSUE=Placenta; RX PubMed=8845838; DOI=10.1093/hmg/5.4.461; RA Andresen B.S., Bross P., Vianey-Saban C., Divry P., Zabot M.-T., RA Roe C.R., Nada M.A., Byskov A., Kruse T.A., Neve S., Kristiansen K., RA Knudsen I., Corydon M.J., Gregersen N.; RT "Cloning and characterization of human very-long-chain acyl-CoA RT dehydrogenase cDNA, chromosomal assignment of the gene and RT identification in four patients of nine different mutations within the RT VLCAD gene."; RL Hum. Mol. Genet. 5:461-472(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RC TISSUE=Peripheral blood; RX PubMed=8554625; DOI=10.1006/bbrc.1995.2867; RA Orii K.O., Aoyama T., Souri M., Orii K.E., Kondo N., Orii T., RA Hashimoto T.; RT "Genomic DNA organization of human mitochondrial very-long-chain acyl- RT CoA dehydrogenase and mutation analysis."; RL Biochem. Biophys. Res. Commun. 217:987-992(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Liver, Lung, and Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP CHARACTERIZATION. RX PubMed=7769092; DOI=10.1172/JCI117947; RA Aoyama T., Souri M., Ushikubo S., Kamijo T., Yamaguchi S., RA Kelley R.I., Rhead W.J., Uetake K., Tanaka K., Hashimoto T.; RT "Purification of human very-long-chain acyl-coenzyme A dehydrogenase RT and characterization of its deficiency in seven patients."; RL J. Clin. Invest. 95:2465-2473(1995). RN [8] RP REVIEW ON VARIANTS. RX PubMed=9973285; DOI=10.1086/302261; RA Andresen B.S., Olpin S., Poorthuis B.J.H.M., Scholte H.R., RA Vianey-Saban C., Wanders R., Ijlst L., Morris A., Pourfarzam M., RA Bartlett K., Baumgartner E.R., de Klerk J.B.C., Schroeder L.D., RA Corydon T.J., Lund H., Winter V., Bross P., Bolund L., Gregersen N.; RT "Clear correlation of genotype with disease phenotype in very-long- RT chain acyl-CoA dehydrogenase deficiency."; RL Am. J. Hum. Genet. 64:479-494(1999). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239 AND LYS-331, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 69-655 IN COMPLEX WITH RP MYRISTOYL-COA, FUNCTION, SUBUNIT, COFACTOR, AND ACTIVE SITE. RX PubMed=18227065; DOI=10.1074/jbc.M709135200; RA McAndrew R.P., Wang Y., Mohsen A.W., He M., Vockley J., Kim J.J.; RT "Structural basis for substrate fatty acyl chain specificity: crystal RT structure of human very-long-chain acyl-CoA dehydrogenase."; RL J. Biol. Chem. 283:9435-9443(2008). RN [12] RP VARIANTS ACADVLD GLU-130 DEL; LYS-299 DEL; GLN-382 AND TRP-613. RX PubMed=8554073; RA Souri M., Aoyama T., Orii K., Yamaguchi S., Hashimoto T.; RT "Mutation analysis of very-long-chain acyl-coenzyme A dehydrogenase RT (VLCAD) deficiency: identification and characterization of mutant RT VLCAD cDNAs from four patients."; RL Am. J. Hum. Genet. 58:97-106(1996). RN [13] RP VARIANT ACADVLD HIS-450. RX PubMed=9546340; DOI=10.1002/ana.410430422; RA Smelt A.H., Poorthuis B.J.H.M., Onkenhout W., Scholte H.R., RA Andresen B.S., van Duinen S.G., Gregersen N., Wintzen A.R.; RT "Very long chain acyl-coenzyme A dehydrogenase deficiency with adult RT onset."; RL Ann. Neurol. 43:540-544(1998). RN [14] RP VARIANTS ACADVLD. RX PubMed=10077518; DOI=10.1161/01.CIR.99.10.1337; RA Mathur A., Sims H.F., Gopalakrishnan D., Gibson B., Rinaldo P., RA Vockley J., Hug G., Strauss A.W.; RT "Molecular heterogeneity in very-long-chain acyl-CoA dehydrogenase RT deficiency causing pediatric cardiomyopathy and sudden death."; RL Circulation 99:1337-1343(1999). CC -!- FUNCTION: Active toward esters of long-chain and very long chain CC fatty acids such as palmitoyl-CoA, mysritoyl-CoA and stearoyl-CoA. CC Can accommodate substrate acyl chain lengths as long as 24 CC carbons, but shows little activity for substrates of less than 12 CC carbons. CC -!- CATALYTIC ACTIVITY: A very-long-chain acyl-CoA + electron-transfer CC flavoprotein = a very-long-chain trans-2,3-dehydroacyl-CoA + CC reduced electron-transfer flavoprotein. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta- CC oxidation. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P49748-1; Sequence=Displayed; CC Name=2; CC IsoId=P49748-2; Sequence=VSP_007734; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=P49748-3; Sequence=VSP_046031; CC Note=No experimental confirmation available; CC -!- PTM: S-nitrosylation at Cys-237 in liver improves catalytic CC efficiency (By similarity). CC -!- DISEASE: Acyl-CoA dehydrogenase very long-chain deficiency CC (ACADVLD) [MIM:201475]: An inborn error of mitochondrial fatty CC acid beta-oxidation which leads to impaired long-chain fatty acid CC beta-oxidation. It is clinically heterogeneous, with three major CC phenotypes: a severe childhood form characterized by early onset, CC high mortality and high incidence of cardiomyopathy; a milder CC childhood form with later onset, characterized by hypoketotic CC hypoglycemia, low mortality and rare cardiomyopathy; an adult CC form, with isolated skeletal muscle involvement, rhabdomyolysis CC and myoglobinuria, usually triggered by exercise or fasting. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases CC of different substrate specificities are present in mammalian CC tissues. CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; D43682; BAA07781.1; -; mRNA. DR EMBL; L46590; AAA79002.1; -; Genomic_DNA. DR EMBL; X86556; CAA60253.1; -; mRNA. DR EMBL; D78298; BAA29057.1; -; Genomic_DNA. DR EMBL; AK293549; BAG57027.1; -; mRNA. DR EMBL; AC120057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000399; AAH00399.1; -; mRNA. DR EMBL; BC012912; AAH12912.1; -; mRNA. DR EMBL; BC020218; AAH20218.1; -; mRNA. DR CCDS; CCDS11090.1; -. [P49748-1] DR CCDS; CCDS42249.1; -. [P49748-2] DR CCDS; CCDS58509.1; -. [P49748-3] DR PIR; S54183; S54183. DR RefSeq; NP_000009.1; NM_000018.3. [P49748-1] DR RefSeq; NP_001029031.1; NM_001033859.2. [P49748-2] DR RefSeq; NP_001257376.1; NM_001270447.1. [P49748-3] DR UniGene; Hs.437178; -. DR PDB; 2UXW; X-ray; 1.45 A; A=72-655. DR PDB; 3B96; X-ray; 1.91 A; A=69-655. DR PDBsum; 2UXW; -. DR PDBsum; 3B96; -. DR ProteinModelPortal; P49748; -. DR SMR; P49748; 69-655. DR BioGrid; 106555; 11. DR IntAct; P49748; 12. DR MINT; MINT-4824254; -. DR STRING; 9606.ENSP00000325395; -. DR PhosphoSite; P49748; -. DR DMDM; 1703068; -. DR MaxQB; P49748; -. DR PaxDb; P49748; -. DR PRIDE; P49748; -. DR Ensembl; ENST00000350303; ENSP00000344152; ENSG00000072778. [P49748-2] DR Ensembl; ENST00000356839; ENSP00000349297; ENSG00000072778. [P49748-1] DR Ensembl; ENST00000543245; ENSP00000438689; ENSG00000072778. [P49748-3] DR GeneID; 37; -. DR KEGG; hsa:37; -. DR UCSC; uc002gev.4; human. [P49748-1] DR UCSC; uc002gew.4; human. [P49748-2] DR CTD; 37; -. DR GeneCards; GC17P007120; -. DR GeneReviews; ACADVL; -. DR HGNC; HGNC:92; ACADVL. DR HPA; HPA019006; -. DR HPA; HPA020595; -. DR MIM; 201475; phenotype. DR MIM; 609575; gene. DR neXtProt; NX_P49748; -. DR Orphanet; 26793; Very long chain acyl-CoA dehydrogenase deficiency. DR PharmGKB; PA24428; -. DR eggNOG; COG1960; -. DR HOVERGEN; HBG050448; -. DR InParanoid; P49748; -. DR KO; K09479; -. DR OMA; ATNRTQF; -. DR OrthoDB; EOG712TVX; -. DR PhylomeDB; P49748; -. DR TreeFam; TF105053; -. DR BioCyc; MetaCyc:ENSG00000072778-MONOMER; -. DR Reactome; REACT_111217; Metabolism. DR Reactome; REACT_17015; Metabolism of proteins. DR UniPathway; UPA00660; -. DR ChiTaRS; ACADVL; human. DR EvolutionaryTrace; P49748; -. DR GenomeRNAi; 37; -. DR NextBio; 143; -. DR PRO; PR:P49748; -. DR ArrayExpress; P49748; -. DR Bgee; P49748; -. DR CleanEx; HS_ACADVL; -. DR Genevestigator; P49748; -. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL. DR GO; GO:0005739; C:mitochondrion; ISS:BHF-UCL. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; TAS:Reactome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; TAS:ProtInc. DR GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome. DR GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:Reactome. DR GO; GO:0015980; P:energy derivation by oxidation of organic compounds; TAS:ProtInc. DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProt. DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:Reactome. DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; ISS:BHF-UCL. DR GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; ISS:BHF-UCL. DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISS:BHF-UCL. DR GO; GO:0090181; P:regulation of cholesterol metabolic process; ISS:BHF-UCL. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0001659; P:temperature homeostasis; ISS:BHF-UCL. DR Gene3D; 1.10.540.10; -; 1. DR Gene3D; 2.40.110.10; -; 1. DR InterPro; IPR006089; Acyl-CoA_DH_CS. DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom. DR InterPro; IPR009075; AcylCo_DH/oxidase_C. DR InterPro; IPR013786; AcylCoA_DH/ox_N. DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom. DR Pfam; PF00441; Acyl-CoA_dh_1; 1. DR Pfam; PF02770; Acyl-CoA_dh_M; 1. DR Pfam; PF02771; Acyl-CoA_dh_N; 1. DR SUPFAM; SSF47203; SSF47203; 1. DR SUPFAM; SSF56645; SSF56645; 1. DR PROSITE; PS00072; ACYL_COA_DH_1; 1. DR PROSITE; PS00073; ACYL_COA_DH_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cardiomyopathy; KW Complete proteome; Disease mutation; FAD; Fatty acid metabolism; KW Flavoprotein; Isopeptide bond; Lipid metabolism; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Polymorphism; Reference proteome; S-nitrosylation; Transit peptide; KW Ubl conjugation. FT TRANSIT 1 40 Mitochondrion (By similarity). FT CHAIN 41 655 Very long-chain specific acyl-CoA FT dehydrogenase, mitochondrial. FT /FTId=PRO_0000000515. FT NP_BIND 214 223 FAD. FT NP_BIND 249 251 FAD. FT NP_BIND 435 439 FAD (By similarity). FT NP_BIND 464 466 FAD. FT REGION 41 482 Catalytic. FT REGION 338 341 Substrate binding (By similarity). FT REGION 462 463 Substrate binding. FT REGION 483 516 Membrane-anchoring (Probable). FT ACT_SITE 462 462 Proton acceptor. FT BINDING 223 223 Substrate; via carbonyl oxygen (By FT similarity). FT BINDING 366 366 FAD (By similarity). FT BINDING 463 463 Substrate; via amide nitrogen (By FT similarity). FT MOD_RES 51 51 N6-acetyllysine (By similarity). FT MOD_RES 71 71 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 71 71 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 195 195 N6-succinyllysine (By similarity). FT MOD_RES 237 237 S-nitrosocysteine (By similarity). FT MOD_RES 239 239 N6-acetyllysine; alternate. FT MOD_RES 239 239 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 276 276 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 276 276 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 278 278 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 278 278 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 298 298 N6-acetyllysine (By similarity). FT MOD_RES 331 331 N6-acetyllysine; alternate. FT MOD_RES 331 331 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 372 372 N6-succinyllysine (By similarity). FT MOD_RES 482 482 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 482 482 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 550 550 N6-acetyllysine (By similarity). FT MOD_RES 556 556 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 556 556 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 639 639 N6-succinyllysine (By similarity). FT CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin); FT alternate (By similarity). FT VAR_SEQ 1 20 MQAARMAASLGRQLLRLGGG -> MLGGLAAAAGTRIMGKE FT IEAEAQRPLRQTWRPGQPPAMTAKTM (in isoform FT 3). FT /FTId=VSP_046031. FT VAR_SEQ 47 68 Missing (in isoform 2). FT /FTId=VSP_007734. FT VARIANT 17 17 L -> F (in dbSNP:rs2230179). FT /FTId=VAR_029286. FT VARIANT 43 43 G -> D (in dbSNP:rs2230178). FT /FTId=VAR_000330. FT VARIANT 65 65 P -> L (in dbSNP:rs28934585). FT /FTId=VAR_048176. FT VARIANT 130 130 Missing (in ACADVLD). FT /FTId=VAR_000331. FT VARIANT 158 158 T -> N (in ACADVLD). FT /FTId=VAR_000332. FT VARIANT 159 159 Q -> R (in ACADVLD). FT /FTId=VAR_000333. FT VARIANT 174 174 V -> M (in ACADVLD). FT /FTId=VAR_000334. FT VARIANT 185 185 G -> S (in ACADVLD). FT /FTId=VAR_000335. FT VARIANT 213 213 A -> P (in ACADVLD; dbSNP:rs140629318). FT /FTId=VAR_010101. FT VARIANT 218 218 E -> K (in ACADVLD). FT /FTId=VAR_000336. FT VARIANT 243 243 L -> R (in ACADVLD). FT /FTId=VAR_000337. FT VARIANT 247 247 K -> E (in ACADVLD). FT /FTId=VAR_010102. FT VARIANT 247 247 K -> T (in ACADVLD). FT /FTId=VAR_000338. FT VARIANT 260 260 T -> M (in ACADVLD; dbSNP:rs113994168). FT /FTId=VAR_000339. FT VARIANT 278 278 Missing (in ACADVLD). FT /FTId=VAR_000340. FT VARIANT 281 281 A -> D (in ACADVLD). FT /FTId=VAR_000341. FT VARIANT 283 283 V -> A (in ACADVLD; dbSNP:rs113994167). FT /FTId=VAR_000342. FT VARIANT 290 290 G -> D (in ACADVLD). FT /FTId=VAR_000343. FT VARIANT 294 294 G -> E (in ACADVLD; dbSNP:rs200573371). FT /FTId=VAR_000344. FT VARIANT 299 299 K -> N (in ACADVLD). FT /FTId=VAR_000345. FT VARIANT 299 299 Missing (in ACADVLD). FT /FTId=VAR_000346. FT VARIANT 317 317 V -> A (in ACADVLD). FT /FTId=VAR_000347. FT VARIANT 352 352 M -> V (in ACADVLD). FT /FTId=VAR_000348. FT VARIANT 359 359 A -> S (in dbSNP:rs1051701). FT /FTId=VAR_011990. FT VARIANT 366 366 R -> C (in ACADVLD). FT /FTId=VAR_000349. FT VARIANT 366 366 R -> H (in ACADVLD; dbSNP:rs112406105). FT /FTId=VAR_000350. FT VARIANT 381 381 Missing (in ACADVLD). FT /FTId=VAR_000351. FT VARIANT 382 382 K -> Q (in ACADVLD; dbSNP:rs118204015). FT /FTId=VAR_000352. FT VARIANT 405 405 D -> H (in ACADVLD). FT /FTId=VAR_000353. FT VARIANT 441 441 G -> D (in ACADVLD; dbSNP:rs2309689). FT /FTId=VAR_000354. FT VARIANT 450 450 R -> H (in ACADVLD; dbSNP:rs118204016). FT /FTId=VAR_000355. FT VARIANT 453 453 R -> Q (in ACADVLD; dbSNP:rs138058572). FT /FTId=VAR_000356. FT VARIANT 454 454 D -> N (in ACADVLD). FT /FTId=VAR_000357. FT VARIANT 456 456 R -> H (in ACADVLD). FT /FTId=VAR_000358. FT VARIANT 458 458 F -> L (in ACADVLD; dbSNP:rs118204017). FT /FTId=VAR_010103. FT VARIANT 459 459 R -> W (in ACADVLD). FT /FTId=VAR_000359. FT VARIANT 463 463 G -> E (in ACADVLD; dbSNP:rs200366828). FT /FTId=VAR_000360. FT VARIANT 469 469 R -> Q (in ACADVLD). FT /FTId=VAR_000361. FT VARIANT 469 469 R -> W (in ACADVLD; dbSNP:rs113994170). FT /FTId=VAR_000362. FT VARIANT 490 490 A -> P (in ACADVLD). FT /FTId=VAR_010104. FT VARIANT 502 502 L -> P (in ACADVLD). FT /FTId=VAR_000363. FT VARIANT 534 534 E -> K (in ACADVLD; dbSNP:rs2230180). FT /FTId=VAR_010105. FT VARIANT 602 602 L -> I (in ACADVLD). FT /FTId=VAR_000364. FT VARIANT 613 613 R -> W (in ACADVLD; dbSNP:rs118204014). FT /FTId=VAR_000365. FT VARIANT 615 615 R -> Q (in ACADVLD; dbSNP:rs148584617). FT /FTId=VAR_010106. FT VARIANT 623 623 S -> F (in dbSNP:rs13383). FT /FTId=VAR_011991. FT CONFLICT 193 193 G -> C (in Ref. 3; BAA29057). FT CONFLICT 200 200 K -> E (in Ref. 4; BAG57027). FT CONFLICT 541 541 E -> K (in Ref. 4; BAG57027). FT HELIX 73 77 FT TURN 78 80 FT TURN 85 87 FT HELIX 96 115 FT HELIX 119 125 FT HELIX 130 138 FT TURN 139 142 FT HELIX 148 150 FT HELIX 157 170 FT HELIX 172 182 FT TURN 183 186 FT HELIX 187 192 FT HELIX 195 206 FT STRAND 212 215 FT STRAND 221 223 FT HELIX 225 227 FT STRAND 231 234 FT STRAND 238 251 FT TURN 252 255 FT STRAND 257 268 FT TURN 270 272 FT STRAND 275 285 FT HELIX 286 288 FT STRAND 289 293 FT STRAND 307 318 FT HELIX 319 321 FT STRAND 322 325 FT HELIX 329 365 FT HELIX 373 375 FT HELIX 377 405 FT HELIX 412 437 FT HELIX 439 442 FT HELIX 448 455 FT HELIX 456 459 FT STRAND 461 463 FT HELIX 465 485 FT HELIX 486 488 FT TURN 522 524 FT HELIX 527 529 FT HELIX 530 554 FT HELIX 555 560 FT HELIX 562 591 FT HELIX 596 622 FT HELIX 627 644 SQ SEQUENCE 655 AA; 70390 MW; A5594D1EA7911D19 CRC64; MQAARMAASL GRQLLRLGGG SSRLTALLGQ PRPGPARRPY AGGAAQLALD KSDSHPSDAL TRKKPAKAES KSFAVGMFKG QLTTDQVFPY PSVLNEEQTQ FLKELVEPVS RFFEEVNDPA KNDALEMVEE TTWQGLKELG AFGLQVPSEL GGVGLCNTQY ARLVEIVGMH DLGVGITLGA HQSIGFKGIL LFGTKAQKEK YLPKLASGET VAAFCLTEPS SGSDAASIRT SAVPSPCGKY YTLNGSKLWI SNGGLADIFT VFAKTPVTDP ATGAVKEKIT AFVVERGFGG ITHGPPEKKM GIKASNTAEV FFDGVRVPSE NVLGEVGSGF KVAMHILNNG RFGMAAALAG TMRGIIAKAV DHATNRTQFG EKIHNFGLIQ EKLARMVMLQ YVTESMAYMV SANMDQGATD FQIEAAISKI FGSEAAWKVT DECIQIMGGM GFMKEPGVER VLRDLRIFRI FEGTNDILRL FVALQGCMDK GKELSGLGSA LKNPFGNAGL LLGEAGKQLR RRAGLGSGLS LSGLVHPELS RSGELAVRAL EQFATVVEAK LIKHKKGIVN EQFLLQRLAD GAIDLYAMVV VLSRASRSLS EGHPTAQHEK MLCDTWCIEA AARIREGMAA LQSDPWQQEL YRNFKSISKA LVERGGVVTS NPLGF // ID ACAP2_HUMAN Reviewed; 778 AA. AC Q15057; A8K2V4; Q8N5Z8; Q9UQR3; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 3. DT 09-JUL-2014, entry version 144. DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2; DE AltName: Full=Centaurin-beta-2; DE Short=Cnt-b2; GN Name=ACAP2; Synonyms=CENTB2, KIAA0041; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF ARG-442. RC TISSUE=Leukocyte; RX PubMed=11062263; DOI=10.1083/jcb.151.3.627; RA Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J., RA Hsu V.W., Donaldson J.G., Randazzo P.A.; RT "ACAPs are arf6 GTPase-activating proteins that function in the cell RT periphery."; RL J. Cell Biol. 151:627-638(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [3] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R., Nomura N.; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Tongue; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-742, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation CC factor 6 (ARF6). CC -!- ENZYME REGULATION: GAP activity stimulated by phosphatidylinositol CC 4,5-bisphosphate (PIP2) and phosphatidic acid. CC -!- SUBUNIT: Interacts with RAB35 (GTP-bound form); the interaction is CC direct and probably recruits ACAP2 to membranes. Interacts with CC MICALL1; the interaction is indirect through RAB35 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane CC protein (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed. Highest level in lung. CC -!- SIMILARITY: Contains 3 ANK repeats. CC -!- SIMILARITY: Contains 1 Arf-GAP domain. CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 PH domain. CC -!- SEQUENCE CAUTION: CC Sequence=BAA05064.2; Type=Erroneous initiation; CC Sequence=CAB41450.1; Type=Frameshift; Positions=98, 106, 111; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ238248; CAB41450.1; ALT_FRAME; mRNA. DR EMBL; D26069; BAA05064.2; ALT_INIT; mRNA. DR EMBL; AK290369; BAF83058.1; -; mRNA. DR EMBL; CH471052; EAW78027.1; -; Genomic_DNA. DR EMBL; BC031005; AAH31005.1; -; mRNA. DR EMBL; BC060767; AAH60767.1; -; mRNA. DR CCDS; CCDS33924.1; -. DR RefSeq; NP_036419.3; NM_012287.5. DR UniGene; Hs.593373; -. DR ProteinModelPortal; Q15057; -. DR SMR; Q15057; 7-360, 378-758. DR BioGrid; 117073; 3. DR IntAct; Q15057; 1. DR STRING; 9606.ENSP00000324287; -. DR PhosphoSite; Q15057; -. DR DMDM; 39932727; -. DR MaxQB; Q15057; -. DR PaxDb; Q15057; -. DR PeptideAtlas; Q15057; -. DR PRIDE; Q15057; -. DR Ensembl; ENST00000326793; ENSP00000324287; ENSG00000114331. DR GeneID; 23527; -. DR KEGG; hsa:23527; -. DR UCSC; uc003fun.4; human. DR CTD; 23527; -. DR GeneCards; GC03M194995; -. DR HGNC; HGNC:16469; ACAP2. DR HPA; HPA034807; -. DR HPA; HPA034808; -. DR MIM; 607766; gene. DR neXtProt; NX_Q15057; -. DR PharmGKB; PA26407; -. DR eggNOG; COG5347; -. DR HOGENOM; HOG000220815; -. DR HOVERGEN; HBG050889; -. DR InParanoid; Q15057; -. DR KO; K12489; -. DR OMA; QHATDED; -. DR OrthoDB; EOG7PVWNT; -. DR PhylomeDB; Q15057; -. DR TreeFam; TF318315; -. DR ChiTaRS; ACAP2; human. DR GeneWiki; CENTB2; -. DR GenomeRNAi; 23527; -. DR NextBio; 45992; -. DR PRO; PR:Q15057; -. DR ArrayExpress; Q15057; -. DR Bgee; Q15057; -. DR CleanEx; HS_ACAP2; -. DR Genevestigator; Q15057; -. DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB. DR GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB. DR GO; GO:0036010; P:protein localization to endosome; ISS:UniProtKB. DR GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro. DR Gene3D; 1.20.1270.60; -; 1. DR Gene3D; 1.25.40.20; -; 1. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR027267; AH/BAR-dom. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR001164; ArfGAP. DR InterPro; IPR011993; PH_like_dom. DR InterPro; IPR001849; Pleckstrin_homology. DR Pfam; PF00023; Ank; 2. DR Pfam; PF01412; ArfGap; 1. DR Pfam; PF00169; PH; 1. DR PRINTS; PR00405; REVINTRACTNG. DR SMART; SM00248; ANK; 3. DR SMART; SM00105; ArfGap; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF48403; SSF48403; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; 2. DR PROSITE; PS50115; ARFGAP; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW ANK repeat; Coiled coil; Complete proteome; Endosome; KW GTPase activation; Membrane; Metal-binding; Phosphoprotein; KW Reference proteome; Repeat; Zinc; Zinc-finger. FT CHAIN 1 778 Arf-GAP with coiled-coil, ANK repeat and FT PH domain-containing protein 2. FT /FTId=PRO_0000074210. FT DOMAIN 1 226 BAR. FT DOMAIN 266 361 PH. FT DOMAIN 399 520 Arf-GAP. FT REPEAT 640 669 ANK 1. FT REPEAT 673 702 ANK 2. FT REPEAT 706 735 ANK 3. FT ZN_FING 414 437 C4-type. FT MOD_RES 384 384 Phosphoserine. FT MOD_RES 521 521 Phosphoserine. FT MOD_RES 742 742 Phosphotyrosine. FT MUTAGEN 442 442 R->Q: Loss of GAP activity. FT CONFLICT 5 5 V -> G (in Ref. 1; CAB41450). FT CONFLICT 42 42 C -> G (in Ref. 1; CAB41450). FT CONFLICT 229 229 V -> G (in Ref. 1; CAB41450). FT CONFLICT 252 252 S -> R (in Ref. 1; CAB41450). FT CONFLICT 258 258 E -> K (in Ref. 1; CAB41450). FT CONFLICT 296 296 L -> V (in Ref. 1; CAB41450). FT CONFLICT 564 564 G -> E (in Ref. 6; AAH60767). SQ SEQUENCE 778 AA; 88029 MW; 64B620957FEE6195 CRC64; MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEATNILT ATRKCFRHIA LDYVLQINVL QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NASCCDCGLA DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE ANVEKMGIKK PQPGQRQEKE AYIRAKYVER KFVDKYSISL SPPEQQKKFV SKSSEEKRLS ISKFGPGDQV RASAQSSVRS NDSGIQQSSD DGRESLPSTV SANSLYEPEG ERQDSSMFLD SKHLNPGLQL YRASYEKNLP KMAEALAHGA DVNWANSEEN KATPLIQAVL GGSLVTCEFL LQNGANVNQR DVQGRGPLHH ATVLGHTGQV CLFLKRGANQ HATDEEGKDP LSIAVEAANA DIVTLLRLAR MNEEMRESEG LYGQPGDETY QDIFRDFSQM ASNNPEKLNR FQQDSQKF // ID ACBP_HUMAN Reviewed; 87 AA. AC P07108; B8ZWD2; B8ZWD6; B8ZWD7; P08869; Q4VWZ6; Q53SQ7; Q6IB48; AC Q9UCI8; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-JUL-2014, entry version 152. DE RecName: Full=Acyl-CoA-binding protein; DE Short=ACBP; DE AltName: Full=Diazepam-binding inhibitor; DE Short=DBI; DE AltName: Full=Endozepine; DE Short=EP; GN Name=DBI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=3020548; DOI=10.1073/pnas.83.19.7547; RA Gray P.W., Glaister D., Seeburg P.H., Guidotti A., Costa E.; RT "Cloning and expression of cDNA for human diazepam binding inhibitor, RT a natural ligand of an allosteric regulatory site of the gamma- RT aminobutyric acid type A receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 83:7547-7551(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2881742; DOI=10.1089/dna.1987.6.71; RA Webb N.R., Rose T.M., Malik N., Marquardt H., Shoyab M., Todaro G.J., RA Lee D.C.; RT "Bovine and human cDNA sequences encoding a putative benzodiazepine RT receptor ligand."; RL DNA 6:71-79(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY. RX PubMed=16055366; DOI=10.1016/j.biocel.2005.06.008; RA Nitz I., Doering F., Schrezenmeir J., Burwinkel B.; RT "Identification of new acyl-CoA binding protein transcripts in human RT and mouse."; RL Int. J. Biochem. Cell Biol. 37:2395-2405(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=21698759; DOI=10.1002/iub.471; RA Ludewig A.H., Nitz I., Klapper M., Doring F.; RT "Identification of a novel human Acyl-CoA binding protein isoform with RT a unique C-terminal domain."; RL IUBMB Life 63:547-552(2011). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), ALTERNATIVE RP SPLICING, AND ALTERNATIVE PROMOTER USAGE. RX PubMed=20345851; DOI=10.1111/j.1582-4934.2010.01055.x; RA Nitz I., Kruse M.L., Klapper M., Doring F.; RT "Specific regulation of low-abundance transcript variants encoding RT human Acyl-CoA binding protein (ACBP) isoforms."; RL J. Cell. Mol. Med. 15:909-927(2011). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP PROTEIN SEQUENCE OF 2-87 (ISOFORM 1), AND ACETYLATION AT SER-2. RC TISSUE=Brain; RX PubMed=3525533; RA Marquardt H., Todaro G.J., Shoyab M.; RT "Complete amino acid sequences of bovine and human endozepines. RT Homology with rat diazepam binding inhibitor."; RL J. Biol. Chem. 261:9727-9731(1986). RN [11] RP PROTEIN SEQUENCE OF 2-14 (ISOFORM 1). RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [12] RP PROTEIN SEQUENCE OF 26-30 AND 72-87. RX PubMed=1292782; RA Apfel R., Lottspeich F., Hoppe J., Behl C., Duerr G., Bogdahn U.; RT "Purification and analysis of growth regulating proteins secreted by a RT human melanoma cell line."; RL Melanoma Res. 2:327-336(1992). RN [13] RP ALTERNATIVE SPLICING. RX PubMed=7534063; RA Kolmer M., Rovio A., Alho H.; RT "The characterization of two diazepam binding inhibitor (DBI) RT transcripts in humans."; RL Biochem. J. 306:327-330(1995). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=17953517; DOI=10.1042/BJ20070559; RA Hansen J.S., Faergeman N.J., Kragelund B.B., Knudsen J.; RT "Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic RT reticulum and Golgi in a ligand-dependent manner in mammalian cells."; RL Biochem. J. 410:463-472(2008). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-8; LYS-19; LYS-55 AND RP LYS-77, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP MALONYLATION AT LYS-55. RX PubMed=21908771; DOI=10.1074/mcp.M111.012658; RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., RA He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., RA Dai J., Verdin E., Ye Y., Zhao Y.; RT "The first identification of lysine malonylation substrates and its RT regulatory enzyme."; RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ACYL-COENZYME A. RX PubMed=17044054; DOI=10.1002/prot.21124; RA Taskinen J.P., van Aalten D.M., Knudsen J., Wierenga R.K.; RT "High resolution crystal structures of unliganded and liganded human RT liver ACBP reveal a new mode of binding for the acyl-CoA ligand."; RL Proteins 66:229-238(2007). CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very CC high affinity and may function as an intracellular carrier of CC acyl-CoA esters. It is also able to displace diazepam from the CC benzodiazepine (BZD) recognition site located on the GABA type A CC receptor. It is therefore possible that this protein also acts as CC a neuropeptide to modulate the action of the GABA receptor. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Golgi apparatus. CC Note=Golgi localization is dependent on ligand binding. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=ACBP-1a, Short; CC IsoId=P07108-1; Sequence=Displayed; CC Name=2; Synonyms=ACBP-1b, Long; CC IsoId=P07108-2; Sequence=VSP_000068; CC Name=3; Synonyms=ACBP-1c; CC IsoId=P07108-3; Sequence=VSP_038680; CC Name=4; Synonyms=ACBP-1a1-g; CC IsoId=P07108-4; Sequence=VSP_043437; CC Name=5; Synonyms=ACBP-1g; CC IsoId=P07108-5; Sequence=VSP_043438; CC Name=6; Synonyms=ACBP-1e; CC IsoId=P07108-6; Sequence=VSP_044114; CC Note=Predominantly expressed in adipose tissue and hippocampus; CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitous, with a moderate CC expression level. Isoform 2 is ubiquitous with high level in liver CC and adipose tissue. Isoform 3 is ubiquitous with strong expression CC in adipose tissue and heart. CC -!- SIMILARITY: Belongs to the ACBP family. CC -!- SIMILARITY: Contains 1 ACB (acyl-CoA-binding) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M14200; AAA52171.1; -; mRNA. DR EMBL; M15887; AAA35788.1; -; mRNA. DR EMBL; FM213123; CAR82405.1; -; mRNA. DR EMBL; FM213124; CAR82406.1; -; mRNA. DR EMBL; FM213125; CAR82407.1; -; mRNA. DR EMBL; FM213126; CAR82408.1; -; mRNA. DR EMBL; FM213127; CAR82409.1; -; mRNA. DR EMBL; FM213128; CAR82410.1; -; mRNA. DR EMBL; FM213131; CAR82414.1; -; mRNA. DR EMBL; CR456956; CAG33237.1; -; mRNA. DR EMBL; AC016736; AAY14873.1; -; Genomic_DNA. DR EMBL; CH471103; EAW95214.1; -; Genomic_DNA. DR EMBL; BC006466; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC062996; AAH62996.1; -; mRNA. DR EMBL; AM000001; CAJ00736.1; -; mRNA. DR CCDS; CCDS2126.1; -. [P07108-2] DR CCDS; CCDS42740.1; -. [P07108-1] DR CCDS; CCDS42741.1; -. [P07108-3] DR CCDS; CCDS54390.1; -. [P07108-4] DR CCDS; CCDS54391.1; -. [P07108-5] DR PIR; B26448; NZHU. DR RefSeq; NP_001073331.1; NM_001079862.2. [P07108-1] DR RefSeq; NP_001073332.1; NM_001079863.1. [P07108-3] DR RefSeq; NP_001171488.1; NM_001178017.1. [P07108-5] DR RefSeq; NP_001171512.1; NM_001178041.2. [P07108-4] DR RefSeq; NP_001171513.1; NM_001178042.2. [P07108-2] DR RefSeq; NP_001269562.1; NM_001282633.1. [P07108-2] DR RefSeq; NP_001269563.1; NM_001282634.1. [P07108-2] DR RefSeq; NP_001269564.1; NM_001282635.1. [P07108-2] DR RefSeq; NP_065438.1; NM_020548.7. [P07108-2] DR UniGene; Hs.78888; -. DR PDB; 2CB8; X-ray; 1.40 A; A/B=2-87. DR PDB; 2FJ9; X-ray; 1.60 A; A=2-87. DR PDBsum; 2CB8; -. DR PDBsum; 2FJ9; -. DR ProteinModelPortal; P07108; -. DR SMR; P07108; 2-87. DR BioGrid; 107990; 10. DR IntAct; P07108; 9. DR MINT; MINT-1394907; -. DR STRING; 9606.ENSP00000311117; -. DR PhosphoSite; P07108; -. DR MaxQB; P07108; -. DR PaxDb; P07108; -. DR PRIDE; P07108; -. DR DNASU; 1622; -. DR Ensembl; ENST00000311521; ENSP00000311117; ENSG00000155368. [P07108-2] DR Ensembl; ENST00000355857; ENSP00000348116; ENSG00000155368. [P07108-1] DR Ensembl; ENST00000393103; ENSP00000376815; ENSG00000155368. [P07108-3] DR Ensembl; ENST00000409094; ENSP00000386486; ENSG00000155368. [P07108-2] DR Ensembl; ENST00000535617; ENSP00000442917; ENSG00000155368. [P07108-4] DR Ensembl; ENST00000535757; ENSP00000439012; ENSG00000155368. [P07108-2] DR Ensembl; ENST00000542275; ENSP00000440698; ENSG00000155368. [P07108-5] DR GeneID; 1622; -. DR KEGG; hsa:1622; -. DR UCSC; uc002tlv.3; human. [P07108-1] DR UCSC; uc002tlw.3; human. [P07108-2] DR UCSC; uc002tlx.3; human. [P07108-3] DR UCSC; uc010yyk.2; human. [P07108-4] DR UCSC; uc021vnj.1; human. [P07108-5] DR CTD; 1622; -. DR GeneCards; GC02P120124; -. DR HGNC; HGNC:2690; DBI. DR HPA; CAB008595; -. DR MIM; 125950; gene. DR neXtProt; NX_P07108; -. DR PharmGKB; PA27158; -. DR eggNOG; COG4281; -. DR HOVERGEN; HBG000398; -. DR KO; K08762; -. DR OMA; LTKRPSD; -. DR OrthoDB; EOG7SN8G8; -. DR PhylomeDB; P07108; -. DR TreeFam; TF335802; -. DR ChiTaRS; DBI; human. DR EvolutionaryTrace; P07108; -. DR GeneWiki; Diazepam_binding_inhibitor; -. DR GenomeRNAi; 1622; -. DR NextBio; 6658; -. DR PRO; PR:P07108; -. DR ArrayExpress; P07108; -. DR Bgee; P07108; -. DR CleanEx; HS_DBI; -. DR Genevestigator; P07108; -. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProt. DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl. DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProt. DR GO; GO:0030156; F:benzodiazepine receptor binding; TAS:ProtInc. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IDA:UniProt. DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProt. DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl. DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProt. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl. DR Gene3D; 1.20.80.10; -; 1. DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS. DR InterPro; IPR000582; Acyl-CoA-binding_protein. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx. DR Pfam; PF00887; ACBP; 1. DR PRINTS; PR00689; ACOABINDINGP. DR SUPFAM; SSF47027; SSF47027; 1. DR PROSITE; PS00880; ACB_1; 1. DR PROSITE; PS51228; ACB_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative promoter usage; KW Alternative splicing; Complete proteome; Direct protein sequencing; KW Endoplasmic reticulum; Golgi apparatus; Lipid-binding; Phosphoprotein; KW Polymorphism; Reference proteome; Transport. FT INIT_MET 1 1 Removed. FT CHAIN 2 87 Acyl-CoA-binding protein. FT /FTId=PRO_0000214004. FT DOMAIN 2 87 ACB. FT REGION 29 33 Acyl-CoA binding. FT BINDING 14 14 Acyl-CoA. FT BINDING 55 55 Acyl-CoA. FT BINDING 74 74 Acyl-CoA. FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 8 8 N6-acetyllysine; alternate. FT MOD_RES 8 8 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 17 17 N6-succinyllysine (By similarity). FT MOD_RES 19 19 N6-acetyllysine. FT MOD_RES 29 29 Phosphotyrosine. FT MOD_RES 55 55 N6-acetyllysine; alternate. FT MOD_RES 55 55 N6-malonyllysine; alternate. FT MOD_RES 55 55 N6-succinyllysine; alternate (By FT similarity). FT MOD_RES 77 77 N6-acetyllysine; alternate. FT MOD_RES 77 77 N6-succinyllysine; alternate (By FT similarity). FT VAR_SEQ 1 3 MSQ -> MWGDLWLLPPASANPGTGTE (in isoform FT 2). FT /FTId=VSP_000068. FT VAR_SEQ 1 3 MSQ -> MPAF (in isoform 3). FT /FTId=VSP_038680. FT VAR_SEQ 1 3 MSQ -> MSQHRAGRRGGVGKRGVRGRELGGQGKYGAGCSE FT CGTRRIAARGE (in isoform 4). FT /FTId=VSP_043437. FT VAR_SEQ 1 3 MSQ -> MERWGKGLHGLEERGDSVPIPKHRAGRRGGVGKR FT GVRGRELGGQGKYGAGCSECGTRRIAARGE (in FT isoform 5). FT /FTId=VSP_043438. FT VAR_SEQ 43 87 ERPGMLDFTGKAKWDAWNELKGTSKEDAMKAYINKVEELKK FT KYGI -> GMQSGGWKGICSSKQAQQLRLEVPGNFTLKLPE FT ALLFRWGMVMVPEVEKTMFRILSVSSSNRIQILVLEGLYWP FT SPAATLY (in isoform 6). FT /FTId=VSP_044114. FT VARIANT 39 39 D -> N (in dbSNP:rs8192504). FT /FTId=VAR_048160. FT VARIANT 71 71 M -> V (in dbSNP:rs8192506). FT /FTId=VAR_048161. FT VARIANT 86 86 G -> R (in dbSNP:rs8192507). FT /FTId=VAR_048162. FT HELIX 3 12 FT HELIX 13 15 FT HELIX 22 36 FT HELIX 50 60 FT TURN 61 64 FT HELIX 67 85 SQ SEQUENCE 87 AA; 10044 MW; B343A309F1B1AE28 CRC64; MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTERPGMLDF TGKAKWDAWN ELKGTSKEDA MKAYINKVEE LKKKYGI // ID ACD_HUMAN Reviewed; 544 AA. AC Q96AP0; Q562H5; Q9H8F9; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 09-JUL-2014, entry version 101. DE RecName: Full=Adrenocortical dysplasia protein homolog; DE AltName: Full=POT1 and TIN2-interacting protein; GN Name=ACD; Synonyms=PIP1, PTOP, TINT1, TPP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MOTIF, SUBCELLULAR LOCATION, RP INTERACTION WITH POT1 AND TINF2, FUNCTION, AND VARIANT ALA-518. RX PubMed=15181449; DOI=10.1038/ncb1142; RA Liu D., Safari A., O'Connor M.S., Chan D.W., Laegeler A., Qin J., RA Songyang Z.; RT "PTOP interacts with POT1 and regulates its localization to RT telomeres."; RL Nat. Cell Biol. 6:673-680(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ALA-518. RC TISSUE=Duodenum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 65-544, AND ALTERNATIVE SPLICING RP (ISOFORM 1). RX PubMed=15537664; DOI=10.1093/hmg/ddi011; RA Keegan C.E., Hutz J.E., Else T., Adamska M., Shah S.P., Kent A.E., RA Howes J.M., Beamer W.G., Hammer G.D.; RT "Urogenital and caudal dysgenesis in adrenocortical dysplasia (acd) RT mice is caused by a splicing mutation in a novel telomeric RT regulator."; RL Hum. Mol. Genet. 14:113-123(2005). RN [6] RP INTERACTION WITH POT1 AND TINF2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=15231715; DOI=10.1101/gad.1215404; RA Ye J.Z.-S., Hockemeyer D., Krutchinsky A.N., Loayza D., Hooper S.M., RA Chait B.T., de Lange T.; RT "POT1-interacting protein PIP1: a telomere length regulator that RT recruits POT1 to the TIN2/TRF1 complex."; RL Genes Dev. 18:1649-1654(2004). RN [7] RP IDENTIFICATION IN THE SHELTERIN COMPLEX. RX PubMed=15316005; DOI=10.1074/jbc.M409047200; RA Ye J.Z.-S., Donigian J.R., van Overbeek M., Loayza D., Luo Y., RA Krutchinsky A.N., Chait B.T., de Lange T.; RT "TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 RT complex on telomeres."; RL J. Biol. Chem. 279:47264-47271(2004). RN [8] RP IDENTIFICATION IN THE SHELTERIN COMPLEX. RX PubMed=15383534; DOI=10.1074/jbc.M409293200; RA Liu D., O'Connor M.S., Qin J., Songyang Z.; RT "Telosome, a mammalian telomere-associated complex formed by multiple RT telomeric proteins."; RL J. Biol. Chem. 279:51338-51342(2004). RN [9] RP FUNCTION OF THE SHELTERIN COMPLEX. RX PubMed=16166375; DOI=10.1101/gad.1346005; RA de Lange T.; RT "Shelterin: the protein complex that shapes and safeguards human RT telomeres."; RL Genes Dev. 19:2100-2110(2005). RN [10] RP FUNCTION IN SHELTERIN COMPLEX ASSEMBLY. RX PubMed=16880378; DOI=10.1073/pnas.0605303103; RA O'Connor M.S., Safari A., Xin H., Liu D., Songyang Z.; RT "A critical role for TPP1 and TIN2 interaction in high-order telomeric RT complex assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 103:11874-11879(2006). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP INTERACTION WITH OBFC1. RX PubMed=19648609; DOI=10.1074/jbc.M109.021105; RA Wan M., Qin J., Songyang Z., Liu D.; RT "OB fold-containing protein 1 (OBFC1), a human homolog of yeast Stn1, RT associates with TPP1 and is implicated in telomere length RT regulation."; RL J. Biol. Chem. 284:26725-26731(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP FUNCTION. RX PubMed=20231318; DOI=10.1101/gad.1881810; RA Zaug A.J., Podell E.R., Nandakumar J., Cech T.R.; RT "Functional interaction between telomere protein TPP1 and RT telomerase."; RL Genes Dev. 24:613-622(2010). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 90-250, FUNCTION, SUBUNIT, RP AND IDENTIFICATION IN A COMPLEX WITH POT1 AND SINGLE-STRANDED RP TELOMERIC DNA. RX PubMed=17237768; DOI=10.1038/nature05454; RA Wang F., Podell E.R., Zaug A.J., Yang Y., Baciu P., Cech T.R., Lei M.; RT "The POT1-TPP1 telomere complex is a telomerase processivity factor."; RL Nature 445:506-510(2007). CC -!- FUNCTION: Component of the shelterin complex (telosome) that is CC involved in the regulation of telomere length and protection. CC Shelterin associates with arrays of double-stranded TTAGGG repeats CC added by telomerase and protects chromosome ends; without its CC protective activity, telomeres are no longer hidden from the DNA CC damage surveillance and chromosome ends are inappropriately CC processed by DNA repair pathways. Promotes binding of POT1 to CC single-stranded telomeric DNA. Modulates the inhibitory effects of CC POT1 on telomere elongation. The ACD-POT1 heterodimer enhances CC telomere elongation by increasing telomerase processivity. Plays a CC role in shelterin complex assembly. May play a role in CC organogenesis. CC -!- SUBUNIT: Component of the shelterin complex (telosome) composed of CC TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Forms heterodimers with CC POT1. Identified in a complex with POT1 and single-stranded CC telomeric DNA. Interacts with STN1/OBFC1 and TINF2. CC -!- INTERACTION: CC Q9H668:OBFC1; NbExp=4; IntAct=EBI-717666, EBI-746930; CC Q9NUX5:POT1; NbExp=3; IntAct=EBI-717666, EBI-752420; CC Q9NUX5-2:POT1; NbExp=3; IntAct=EBI-717666, EBI-752435; CC Q9BSI4-3:TINF2; NbExp=5; IntAct=EBI-717666, EBI-717418; CC Q92900:UPF1; NbExp=3; IntAct=EBI-717666, EBI-373471; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, telomere. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96AP0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96AP0-2; Sequence=VSP_019066; CC -!- SEQUENCE CAUTION: CC Sequence=AAX82621.1; Type=Erroneous initiation; Note=Translation N-terminally extended; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY502940; AAS80318.1; -; mRNA. DR EMBL; AK023726; BAB14658.1; -; mRNA. DR EMBL; AC010530; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC016904; AAH16904.1; -; mRNA. DR EMBL; AY971883; AAX82621.1; ALT_INIT; Genomic_DNA. DR CCDS; CCDS10842.1; -. [Q96AP0-2] DR CCDS; CCDS42181.1; -. [Q96AP0-1] DR RefSeq; NP_001075955.1; NM_001082486.1. [Q96AP0-1] DR RefSeq; NP_001075956.1; NM_001082487.1. DR RefSeq; NP_075065.2; NM_022914.2. [Q96AP0-2] DR UniGene; Hs.78019; -. DR PDB; 2I46; X-ray; 2.70 A; A/B=90-250. DR PDBsum; 2I46; -. DR ProteinModelPortal; Q96AP0; -. DR SMR; Q96AP0; 90-241. DR BioGrid; 122379; 65. DR DIP; DIP-29611N; -. DR IntAct; Q96AP0; 10. DR MINT; MINT-1387856; -. DR STRING; 9606.ENSP00000377496; -. DR PhosphoSite; Q96AP0; -. DR DMDM; 296439451; -. DR MaxQB; Q96AP0; -. DR PaxDb; Q96AP0; -. DR PRIDE; Q96AP0; -. DR Ensembl; ENST00000219251; ENSP00000219251; ENSG00000102977. [Q96AP0-2] DR Ensembl; ENST00000393919; ENSP00000377496; ENSG00000102977. [Q96AP0-1] DR GeneID; 65057; -. DR KEGG; hsa:65057; -. DR UCSC; uc002etp.4; human. [Q96AP0-2] DR UCSC; uc002etq.4; human. [Q96AP0-1] DR CTD; 65057; -. DR GeneCards; GC16M067691; -. DR H-InvDB; HIX0013152; -. DR HGNC; HGNC:25070; ACD. DR HPA; HPA057660; -. DR MIM; 609377; gene. DR neXtProt; NX_Q96AP0; -. DR PharmGKB; PA134882431; -. DR eggNOG; NOG81452; -. DR HOGENOM; HOG000033778; -. DR HOVERGEN; HBG080817; -. DR InParanoid; Q96AP0; -. DR KO; K11114; -. DR OMA; WEEKEFG; -. DR OrthoDB; EOG7HHWSJ; -. DR PhylomeDB; Q96AP0; -. DR TreeFam; TF338536; -. DR Reactome; REACT_115566; Cell Cycle. DR Reactome; REACT_120956; Cellular responses to stress. DR EvolutionaryTrace; Q96AP0; -. DR GeneWiki; ACD_(gene); -. DR GenomeRNAi; 65057; -. DR NextBio; 67230; -. DR PRO; PR:Q96AP0; -. DR Bgee; Q96AP0; -. DR CleanEx; HS_ACD; -. DR CleanEx; HS_TPP1; -. DR Genevestigator; Q96AP0; -. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL. DR GO; GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl. DR GO; GO:0006886; P:intracellular protein transport; IMP:BHF-UCL. DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL. DR GO; GO:0060381; P:positive regulation of single-stranded telomeric DNA binding; IDA:BHF-UCL. DR GO; GO:0051973; P:positive regulation of telomerase activity; IDA:BHF-UCL. DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; ISS:BHF-UCL. DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IMP:BHF-UCL. DR GO; GO:0035282; P:segmentation; IEA:Ensembl. DR GO; GO:0001501; P:skeletal system development; IEA:Ensembl. DR GO; GO:0032202; P:telomere assembly; IMP:BHF-UCL. DR GO; GO:0016233; P:telomere capping; IGI:BHF-UCL. DR GO; GO:0000723; P:telomere maintenance; IDA:MGI. DR GO; GO:0001655; P:urogenital system development; IEA:Ensembl. DR InterPro; IPR028631; ACD. DR PANTHER; PTHR14487; PTHR14487; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosome; Complete proteome; KW DNA-binding; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Telomere. FT CHAIN 1 544 Adrenocortical dysplasia protein homolog. FT /FTId=PRO_0000239019. FT REGION 244 337 Interaction with POT1. FT MOTIF 97 99 PWI. FT COMPBIAS 354 442 Ser-rich. FT MOD_RES 111 111 Phosphoserine. FT VAR_SEQ 120 122 Missing (in isoform 2). FT /FTId=VSP_019066. FT VARIANT 301 301 T -> M (in dbSNP:rs72547495). FT /FTId=VAR_060224. FT VARIANT 518 518 V -> A (in dbSNP:rs6979). FT /FTId=VAR_060225. FT CONFLICT 224 224 C -> R (in Ref. 2; BAB14658). FT HELIX 99 104 FT STRAND 105 107 FT STRAND 113 122 FT STRAND 142 147 FT STRAND 152 157 FT HELIX 159 163 FT STRAND 180 192 FT STRAND 201 215 FT HELIX 224 226 FT HELIX 228 238 SQ SEQUENCE 544 AA; 57733 MW; D2FDF242DA98C483 CRC64; MPGRCQSDAA MRVNGPASRA PAGWTSGSLH TGPRAGRPRA QARGVRGRGL LLRPRPAKEL PLPRKGGAWA PAGNPGPLHP LGVAVGMAGS GRLVLRPWIR ELILGSETPS SPRAGQLLEV LQDAEAAVAG PSHAPDTSDV GATLLVSDGT HSVRCLVTRE ALDTSDWEEK EFGFRGTEGR LLLLQDCGVH VQVAEGGAPA EFYLQVDRFS LLPTEQPRLR VPGCNQDLDV QKKLYDCLEE HLSESTSSNA GLSLSQLLDE MREDQEHQGA LVCLAESCLT LEGPCTAPPV THWAASRCKA TGEAVYTVPS SMLCISENDQ LILSSLGPCQ RTQGPELPPP DPALQDLSLT LIASPPSSPS SSGTPALPGH MSSEESGTSI SLLPALSLAA PDPGQRSSSQ PSPAICSAPA TLTPRSPHAS RTPSSPLQSC TPSLSPRSHV PSPHQALVTR PQKPSLEFKE FVGLPCKNRP PFPRTGATRG AQEPCSVWEP PKRHRDGSAF QYEYEPPCTS LCARVQAVRL PPQLMAWALH FLMDAQPGSE PTPM // ID ACE2_HUMAN Reviewed; 805 AA. AC Q9BYF1; C7ECU1; Q6UWP0; Q86WT0; Q9NRA7; Q9UFZ6; DT 02-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, sequence version 2. DT 09-JUL-2014, entry version 129. DE RecName: Full=Angiotensin-converting enzyme 2; DE EC=3.4.17.23; DE AltName: Full=ACE-related carboxypeptidase; DE AltName: Full=Angiotensin-converting enzyme homolog; DE Short=ACEH; DE AltName: Full=Metalloprotease MPROT15; DE Contains: DE RecName: Full=Processed angiotensin-converting enzyme 2; DE Flags: Precursor; GN Name=ACE2; ORFNames=UNQ868/PRO1885; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, RP AND ENZYME REGULATION. RC TISSUE=Heart; RX PubMed=10969042; DOI=10.1161/01.RES.87.5.e1; RA Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., RA Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., RA Breitbart R.E., Acton S.; RT "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) RT converts angiotensin I to angiotensin 1-9."; RL Circ. Res. 87:E1-E9(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, RP GLYCOSYLATION, FUNCTION, AND ENZYME REGULATION. RC TISSUE=Lymphoma; RX PubMed=10924499; DOI=10.1074/jbc.M002615200; RA Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., RA Turner A.J.; RT "A human homolog of angiotensin-converting enzyme. Cloning and RT functional expression as a captopril-insensitive carboxypeptidase."; RL J. Biol. Chem. 275:33238-33243(2000). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, RP SUBCELLULAR LOCATION, AND ENZYME REGULATION. RC TISSUE=Testis; RX PubMed=15231706; DOI=10.1210/en.2004-0443; RA Douglas G.C., O'Bryan M.K., Hedger M.P., Lee D.K.L., Yarski M.A., RA Smith A.I., Lew R.A.; RT "The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is RT selectively expressed by adult Leydig cells of the testis."; RL Endocrinology 145:4703-4711(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-638. RC TISSUE=Lung, and Testis; RX PubMed=15937940; DOI=10.1002/ajmg.a.30779; RA Itoyama S., Keicho N., Hijikata M., Quy T., Phi N.C., Long H.T., RA Ha L.D., Ban V.V., Matsushita I., Yanai H., Kirikae F., Kirikae T., RA Kuratsuji T., Sasazuki T.; RT "Identification of an alternative 5'-untranslated exon and new RT polymorphisms of angiotensin-converting enzyme 2 gene: lack of RT association with SARS in the Vietnamese population."; RL Am. J. Med. Genet. A 136:52-57(2005). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Suzuki Y., Watanabe M., Sugano S.; RT "Cloning, expression analysis and chromosomal localization of a novel RT ACE like enzyme."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Southan C., Burgess N.; RT "MPROT15 polypeptide and MPROT15 polynucleotide."; RL Patent number JP11318472, 24-NOV-1999. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Li K.K.B., Yip C.W., Hon C.C., Lam C.Y., Leung F.C.C.; RT "Comparative susceptibility to SARS-CoV mediated by ACE2 protein of 15 RT different species."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-26. RG SeattleSNPs variation discovery resource; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-805 (ISOFORM 1). RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [13] RP PROTEIN SEQUENCE OF 679-689, IDENTIFICATION BY MASS SPECTROMETRY, AND RP INTERACTION WITH ITGB1. RX PubMed=15276642; DOI=10.1016/j.bbadis.2004.05.005; RA Lin Q., Keller R.S., Weaver B., Zisman L.S.; RT "Interaction of ACE2 and integrin beta1 in failing human heart."; RL Biochim. Biophys. Acta 1689:175-178(2004). RN [14] RP TISSUE SPECIFICITY. RX PubMed=12459472; DOI=10.1016/S0014-5793(02)03640-2; RA Harmer D., Gilbert M., Borman R., Clark K.L.; RT "Quantitative mRNA expression profiling of ACE 2, a novel homologue of RT angiotensin converting enzyme."; RL FEBS Lett. 532:107-110(2002). RN [15] RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND COFACTOR. RX PubMed=11815627; DOI=10.1074/jbc.M200581200; RA Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., RA Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., RA Nichols A., Tummino P.; RT "Hydrolysis of biological peptides by human angiotensin-converting RT enzyme-related carboxypeptidase."; RL J. Biol. Chem. 277:14838-14843(2002). RN [16] RP FUNCTION, INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN, GLYCOSYLATION, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14647384; DOI=10.1038/nature02145; RA Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A., RA Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H., RA Farzan M.; RT "Angiotensin-converting enzyme 2 is a functional receptor for the SARS RT coronavirus."; RL Nature 426:450-454(2003). RN [17] RP INDUCTION. RX PubMed=15151696; DOI=10.1186/1741-7015-2-19; RA Goulter A.B., Goddard M.J., Allen J.C., Clark K.L.; RT "ACE2 gene expression is up-regulated in the human failing heart."; RL BMC Med. 2:19-19(2004). RN [18] RP TISSUE SPECIFICITY. RX PubMed=15141377; DOI=10.1002/path.1570; RA Hamming I., Timens W., Bulthuis M.L.C., Lely A.T., Navis G.J., RA van Goor H.; RT "Tissue distribution of ACE2 protein, the functional receptor for SARS RT coronavirus. A first step in understanding SARS pathogenesis."; RL J. Pathol. 203:631-637(2004). RN [19] RP INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN. RX PubMed=15452268; DOI=10.1128/JVI.78.20.11429-11433.2004; RA Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M., RA Sullivan J.L., Farzan M., Choe H.; RT "Efficient replication of severe acute respiratory syndrome RT coronavirus in mouse cells is limited by murine angiotensin-converting RT enzyme 2."; RL J. Virol. 78:11429-11433(2004). RN [20] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90. RC TISSUE=Bile; RX PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200; RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., RA Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; RT "A proteomic analysis of human bile."; RL Mol. Cell. Proteomics 3:715-728(2004). RN [21] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=15671045; DOI=10.1093/eurheartj/ehi114; RA Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S., RA Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E., RA Johnston C.I.; RT "Myocardial infarction increases ACE2 expression in rat and humans."; RL Eur. Heart J. 26:369-375(2005). RN [22] RP INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN, AND MUTAGENESIS. RX PubMed=15791205; DOI=10.1038/sj.emboj.7600640; RA Li W., Zhang C., Sui J., Kuhn J.H., Moore M.J., Luo S., Wong S.-K., RA Huang I.-C., Xu K., Vasilieva N., Murakami A., He Y., Marasco W.A., RA Guan Y., Choe H., Farzan M.; RT "Receptor and viral determinants of SARS-coronavirus adaptation to RT human ACE2."; RL EMBO J. 24:1634-1643(2005). RN [23] RP PROTEOLYTIC CLEAVAGE. RX PubMed=15983030; DOI=10.1074/jbc.M505111200; RA Lambert D.W., Yarski M., Warner F.J., Thornhill P., Parkin E.T., RA Smith A.I., Hooper N.M., Turner A.J.; RT "Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated RT ectodomain shedding of the severe-acute respiratory syndrome- RT coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 RT (ACE2)."; RL J. Biol. Chem. 280:30113-30119(2005). RN [24] RP INTERACTION WITH HCOV-NL63 SPIKE GLYCOPROTEIN. RX PubMed=15897467; DOI=10.1073/pnas.0409465102; RA Hofmann H., Pyrc K., van der Hoek L., Geier M., Berkhout B., RA Poehlmann S.; RT "Human coronavirus NL63 employs the severe acute respiratory syndrome RT coronavirus receptor for cellular entry."; RL Proc. Natl. Acad. Sci. U.S.A. 102:7988-7993(2005). RN [25] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [26] RP PROTEOLYTIC CLEAVAGE. RX PubMed=21563828; DOI=10.1021/bi200525y; RA Lai Z.W., Hanchapola I., Steer D.L., Smith A.I.; RT "Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site RT identification: determinants and constraints."; RL Biochemistry 50:5182-5194(2011). RN [27] RP SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND INTERACTION WITH RP TMPRSS2. RX PubMed=21068237; DOI=10.1128/JVI.02062-10; RA Shulla A., Heald-Sargent T., Subramanya G., Zhao J., Perlman S., RA Gallagher T.; RT "A transmembrane serine protease is linked to the severe acute RT respiratory syndrome coronavirus receptor and activates virus entry."; RL J. Virol. 85:873-882(2011). RN [28] RP FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE. RX PubMed=24227843; DOI=10.1128/JVI.02202-13; RA Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., RA Poehlmann S.; RT "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by RT TMPRSS2 augments entry driven by the severe acute respiratory syndrome RT coronavirus spike protein."; RL J. Virol. 88:1293-1307(2014). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-615, X-RAY CRYSTALLOGRAPHY RP (3.0 ANGSTROMS) OF 19-615 IN COMPLEX WITH MLN-4760, DISULFIDE BONDS, RP AND GLYCOSYLATION AT ASN-53; ASN-90; ASN-103; ASN-322; ASN-432 AND RP ASN-546. RX PubMed=14754895; DOI=10.1074/jbc.M311191200; RA Towler P., Staker B., Prasad S.G., Menon S., Tang J., Parsons T., RA Ryan D., Fisher M., Williams D., Dales N.A., Patane M.A., RA Pantoliano M.W.; RT "ACE2 X-ray structures reveal a large hinge-bending motion important RT for inhibitor binding and catalysis."; RL J. Biol. Chem. 279:17996-18007(2004). CC -!- FUNCTION: Carboxypeptidase which converts angiotensin I to CC angiotensin 1-9, a peptide of unknown function, and angiotensin II CC to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin- CC 13 and dynorphin-13 with high efficiency. May be an important CC regulator of heart function. In case of human coronaviruses SARS CC and HCoV-NL63 infections, serve as functional receptor for the CC spike glycoprotein of both coronaviruses. CC -!- CATALYTIC ACTIVITY: Angiotensin II + H(2)O = angiotensin-(1-7) + CC L-phenylalanine. CC -!- COFACTOR: Binds 1 zinc ion per subunit. CC -!- COFACTOR: Binds 1 chloride ion per subunit. CC -!- ENZYME REGULATION: Activated by chloride and fluoride, but not CC bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the CC ACE inhibitors linosipril, captopril and enalaprilat. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=6.9 uM for angiotensin I; CC KM=2 uM for angiotensin II; CC KM=6.8 uM for apelin-13; CC KM=5.5 uM for dynorphin-13; CC pH dependence: CC Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6 CC to 9; CC -!- SUBUNIT: Interacts with ITGB1. Interacts with SARS-CoV and HCoV- CC NL63 spike glycoprotein. Interacts with the catalytically active CC form of TMPRSS2. CC -!- SUBCELLULAR LOCATION: Processed angiotensin-converting enzyme 2: CC Secreted. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BYF1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BYF1-2; Sequence=VSP_014901, VSP_014902; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells from small and CC large arteries, and in arterial smooth muscle cells. Expressed in CC lung alveolar epithelial cells, enterocytes of the small CC intestine, Leydig cells and Sertoli cells (at protein level). CC Expressed in heart, kidney, testis, and gastrointestinal system. CC -!- INDUCTION: Up-regulated in failing heart. CC -!- PTM: N-glycosylation on Asn-90 may limit SARS infectivity. CC -!- PTM: Proteolytic cleavage by ADAM17 generates a secreted form. CC Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and CC HPN/TMPRSS1. CC -!- SIMILARITY: Belongs to the peptidase M2 family. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/ace2/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF291820; AAF99721.1; -; mRNA. DR EMBL; AF241254; AAF78220.1; -; mRNA. DR EMBL; AY623811; AAT45083.1; -; mRNA. DR EMBL; AB193259; BAD99266.1; -; mRNA. DR EMBL; AB193260; BAD99267.1; -; mRNA. DR EMBL; AB046569; BAB40370.1; -; mRNA. DR EMBL; E39033; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; GQ262784; ACT66268.1; -; mRNA. DR EMBL; AY358714; AAQ89076.1; -; mRNA. DR EMBL; AY217547; AAO25651.1; -; Genomic_DNA. DR EMBL; CH471074; EAW98892.1; -; Genomic_DNA. DR EMBL; BC039902; AAH39902.1; -; mRNA. DR EMBL; BC048094; AAH48094.2; -; mRNA. DR EMBL; AL110224; CAB53682.1; -; mRNA. DR CCDS; CCDS14169.1; -. [Q9BYF1-1] DR PIR; T14762; T14762. DR RefSeq; NP_068576.1; NM_021804.2. [Q9BYF1-1] DR UniGene; Hs.178098; -. DR PDB; 1R42; X-ray; 2.20 A; A=1-615. DR PDB; 1R4L; X-ray; 3.00 A; A=1-615. DR PDB; 1XJP; Model; -; B=19-615. DR PDB; 2AJF; X-ray; 2.90 A; A/B=19-615. DR PDB; 3D0G; X-ray; 2.80 A; A/B=56-615. DR PDB; 3D0H; X-ray; 3.10 A; A/B=56-615. DR PDB; 3D0I; X-ray; 2.90 A; A/B=56-615. DR PDB; 3KBH; X-ray; 3.31 A; A/B/C/D=19-615. DR PDB; 3SCI; X-ray; 2.90 A; A/B=19-615. DR PDB; 3SCJ; X-ray; 3.00 A; A/B=19-615. DR PDB; 3SCK; X-ray; 3.00 A; A/B=83-615. DR PDB; 3SCL; X-ray; 3.00 A; A/B=83-615. DR PDBsum; 1R42; -. DR PDBsum; 1R4L; -. DR PDBsum; 1XJP; -. DR PDBsum; 2AJF; -. DR PDBsum; 3D0G; -. DR PDBsum; 3D0H; -. DR PDBsum; 3D0I; -. DR PDBsum; 3KBH; -. DR PDBsum; 3SCI; -. DR PDBsum; 3SCJ; -. DR PDBsum; 3SCK; -. DR PDBsum; 3SCL; -. DR ProteinModelPortal; Q9BYF1; -. DR SMR; Q9BYF1; 19-615. DR BioGrid; 121864; 3. DR DIP; DIP-44689N; -. DR IntAct; Q9BYF1; 1. DR MINT; MINT-4538816; -. DR STRING; 9606.ENSP00000252519; -. DR BindingDB; Q9BYF1; -. DR ChEMBL; CHEMBL2096989; -. DR DrugBank; DB00691; Moexipril. DR GuidetoPHARMACOLOGY; 1614; -. DR MEROPS; M02.006; -. DR PhosphoSite; Q9BYF1; -. DR DMDM; 71658783; -. DR PaxDb; Q9BYF1; -. DR PRIDE; Q9BYF1; -. DR Ensembl; ENST00000252519; ENSP00000252519; ENSG00000130234. [Q9BYF1-1] DR Ensembl; ENST00000427411; ENSP00000389326; ENSG00000130234. [Q9BYF1-1] DR GeneID; 59272; -. DR KEGG; hsa:59272; -. DR UCSC; uc004cxa.1; human. [Q9BYF1-1] DR CTD; 59272; -. DR GeneCards; GC0XM015489; -. DR HGNC; HGNC:13557; ACE2. DR HPA; CAB026174; -. DR HPA; HPA000288; -. DR MIM; 300335; gene. DR neXtProt; NX_Q9BYF1; -. DR PharmGKB; PA425; -. DR eggNOG; NOG71044; -. DR HOGENOM; HOG000292210; -. DR HOVERGEN; HBG000265; -. DR InParanoid; Q9BYF1; -. DR KO; K09708; -. DR OMA; RDGANEG; -. DR OrthoDB; EOG76HQ13; -. DR PhylomeDB; Q9BYF1; -. DR TreeFam; TF312861; -. DR BRENDA; 3.4.15.1; 2681. DR Reactome; REACT_17015; Metabolism of proteins. DR SABIO-RK; Q9BYF1; -. DR ChiTaRS; ACE2; human. DR EvolutionaryTrace; Q9BYF1; -. DR GeneWiki; Angiotensin-converting_enzyme_2; -. DR GenomeRNAi; 59272; -. DR NextBio; 65154; -. DR PMAP-CutDB; Q9BYF1; -. DR PRO; PR:Q9BYF1; -. DR Bgee; Q9BYF1; -. DR CleanEx; HS_ACE2; -. DR Genevestigator; Q9BYF1; -. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL. DR GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0045121; C:membrane raft; TAS:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0004180; F:carboxypeptidase activity; IDA:UniProtKB. DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB. DR GO; GO:0001948; F:glycoprotein binding; IPI:BHF-UCL. DR GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0001618; F:virus receptor activity; IMP:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; TAS:BHF-UCL. DR GO; GO:0002005; P:angiotensin catabolic process in blood; IC:BHF-UCL. DR GO; GO:0002003; P:angiotensin maturation; TAS:Reactome. DR GO; GO:0003051; P:angiotensin-mediated drinking behavior; IMP:BHF-UCL. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IC:BHF-UCL. DR GO; GO:0032800; P:receptor biosynthetic process; IMP:BHF-UCL. DR GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IDA:BHF-UCL. DR GO; GO:0042127; P:regulation of cell proliferation; TAS:BHF-UCL. DR GO; GO:0001817; P:regulation of cytokine production; IC:BHF-UCL. DR GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL. DR GO; GO:0003081; P:regulation of systemic arterial blood pressure by renin-angiotensin; IMP:BHF-UCL. DR GO; GO:0019229; P:regulation of vasoconstriction; IC:BHF-UCL. DR GO; GO:0042312; P:regulation of vasodilation; IC:BHF-UCL. DR GO; GO:0009615; P:response to virus; IDA:GOC. DR GO; GO:0046718; P:viral entry into host cell; TAS:UniProtKB. DR InterPro; IPR001548; Peptidase_M2. DR PANTHER; PTHR10514; PTHR10514; 1. DR Pfam; PF01401; Peptidase_M2; 1. DR PRINTS; PR00791; PEPDIPTASEA. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Carboxypeptidase; Cell membrane; KW Chloride; Complete proteome; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Host-virus interaction; Hydrolase; KW Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease; KW Reference proteome; Secreted; Signal; Transmembrane; KW Transmembrane helix; Zinc. FT SIGNAL 1 17 Potential. FT CHAIN 18 805 Angiotensin-converting enzyme 2. FT /FTId=PRO_0000028570. FT CHAIN 18 708 Processed angiotensin-converting enzyme FT 2. FT /FTId=PRO_0000292268. FT TOPO_DOM 18 740 Extracellular (Potential). FT TRANSMEM 741 761 Helical; (Potential). FT TOPO_DOM 762 805 Cytoplasmic (Potential). FT REGION 30 41 Interaction with SARS-CoV spike FT glycoprotein. FT REGION 82 84 Interaction with SARS-CoV spike FT glycoprotein. FT REGION 353 357 Interaction with SARS-CoV spike FT glycoprotein. FT REGION 652 659 Essential for cleavage by ADAM17. FT REGION 697 716 Essential for cleavage by TMPRSS11D and FT TMPRSS2. FT ACT_SITE 375 375 FT ACT_SITE 505 505 FT METAL 374 374 Zinc; catalytic. FT METAL 378 378 Zinc; catalytic. FT METAL 402 402 Zinc; catalytic. FT BINDING 169 169 Chloride. FT BINDING 273 273 Substrate. FT BINDING 345 345 Substrate. FT BINDING 346 346 Substrate; via carbonyl oxygen. FT BINDING 371 371 Substrate. FT BINDING 477 477 Chloride. FT BINDING 481 481 Chloride. FT BINDING 515 515 Substrate. FT CARBOHYD 53 53 N-linked (GlcNAc...) (Probable). FT CARBOHYD 90 90 N-linked (GlcNAc...). FT CARBOHYD 103 103 N-linked (GlcNAc...). FT CARBOHYD 322 322 N-linked (GlcNAc...) (Probable). FT CARBOHYD 432 432 N-linked (GlcNAc...). FT CARBOHYD 546 546 N-linked (GlcNAc...). FT CARBOHYD 690 690 N-linked (GlcNAc...) (Potential). FT DISULFID 133 141 FT DISULFID 344 361 FT DISULFID 530 542 FT VAR_SEQ 555 555 F -> L (in isoform 2). FT /FTId=VSP_014901. FT VAR_SEQ 556 805 Missing (in isoform 2). FT /FTId=VSP_014902. FT VARIANT 26 26 K -> R (in dbSNP:rs4646116). FT /FTId=VAR_023082. FT VARIANT 638 638 N -> S (in dbSNP:rs183135788). FT /FTId=VAR_023083. FT MUTAGEN 24 26 QAK->KAE: Slightly inhibits interaction FT with SARS-CoV spike glycoprotein. FT MUTAGEN 31 31 K->D: Abolishes interaction with SARS-CoV FT spike glycoprotein. FT MUTAGEN 37 37 E->A: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 38 38 D->A: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 41 41 Y->A: Strongly inhibits interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 68 68 K->D: Slightly inhibits interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 82 84 MYP->NFS: Inhibits interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 110 110 E->P: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 135 136 PD->SM: No effect on interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 160 160 E->R: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 192 192 R->D: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 219 219 R->D: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 239 239 H->Q: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 309 309 K->D: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 312 312 E->A: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 324 324 T->A: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 338 340 NVQ->DDR: No effect on interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 350 350 D->A: No effect on interaction with SARS- FT CoV spike glycoprotein. FT MUTAGEN 353 353 K->H,A,D: Abolishes interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 355 355 D->A: Strongly inhibits interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 357 357 R->A: Strongly inhibits interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 359 359 L->K,A: No effect on interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 383 383 M->A: Slightly inhibits interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 389 389 P->A: Slightly inhibits interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 393 393 R->A: Slightly inhibits interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 425 427 SPD->PSN: Slightly inhibits interaction FT with SARS-CoV spike glycoprotein. FT MUTAGEN 465 467 KGE->QDK: No effect on interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 559 559 R->S: Slightly inhibits interaction with FT SARS-CoV spike glycoprotein. FT MUTAGEN 603 603 F->T: No effect on interaction with SARS- FT CoV spike glycoprotein. FT CONFLICT 18 18 Q -> H (in Ref. 12; CAB53682). FT CONFLICT 508 508 N -> D (in Ref. 8; AAQ89076). FT CONFLICT 631 631 K -> R (in Ref. 5; BAB40370). FT HELIX 23 52 FT HELIX 56 77 FT TURN 78 82 FT HELIX 85 87 FT HELIX 91 100 FT HELIX 104 107 FT HELIX 110 129 FT STRAND 131 134 FT STRAND 137 143 FT TURN 144 146 FT HELIX 148 154 FT HELIX 158 171 FT HELIX 173 193 FT STRAND 196 198 FT HELIX 199 204 FT TURN 205 207 FT TURN 213 215 FT HELIX 220 251 FT TURN 253 255 FT STRAND 258 260 FT HELIX 264 266 FT STRAND 267 271 FT HELIX 276 278 FT HELIX 279 282 FT TURN 284 287 FT TURN 294 297 FT HELIX 298 300 FT HELIX 304 316 FT TURN 317 319 FT HELIX 327 330 FT STRAND 338 340 FT STRAND 347 352 FT STRAND 355 359 FT HELIX 366 384 FT TURN 385 387 FT HELIX 390 392 FT HELIX 400 413 FT HELIX 415 420 FT TURN 422 426 FT HELIX 432 446 FT HELIX 449 465 FT STRAND 466 468 FT HELIX 470 472 FT HELIX 473 483 FT STRAND 486 488 FT HELIX 499 502 FT HELIX 504 507 FT HELIX 514 531 FT TURN 532 534 FT HELIX 539 541 FT HELIX 548 558 FT TURN 559 562 FT HELIX 566 574 FT STRAND 575 578 FT HELIX 582 598 FT STRAND 600 602 FT STRAND 607 609 SQ SEQUENCE 805 AA; 92463 MW; 8EE6EB0A931550E8 CRC64; MSSSSWLLLS LVAVTAAQST IEEQAKTFLD KFNHEAEDLF YQSSLASWNY NTNITEENVQ NMNNAGDKWS AFLKEQSTLA QMYPLQEIQN LTVKLQLQAL QQNGSSVLSE DKSKRLNTIL NTMSTIYSTG KVCNPDNPQE CLLLEPGLNE IMANSLDYNE RLWAWESWRS EVGKQLRPLY EEYVVLKNEM ARANHYEDYG DYWRGDYEVN GVDGYDYSRG QLIEDVEHTF EEIKPLYEHL HAYVRAKLMN AYPSYISPIG CLPAHLLGDM WGRFWTNLYS LTVPFGQKPN IDVTDAMVDQ AWDAQRIFKE AEKFFVSVGL PNMTQGFWEN SMLTDPGNVQ KAVCHPTAWD LGKGDFRILM CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF HEAVGEIMSL SAATPKHLKS IGLLSPDFQE DNETEINFLL KQALTIVGTL PFTYMLEKWR WMVFKGEIPK DQWMKKWWEM KREIVGVVEP VPHDETYCDP ASLFHVSNDY SFIRYYTRTL YQFQFQEALC QAAKHEGPLH KCDISNSTEA GQKLFNMLRL GKSEPWTLAL ENVVGAKNMN VRPLLNYFEP LFTWLKDQNK NSFVGWSTDW SPYADQSIKV RISLKSALGD KAYEWNDNEM YLFRSSVAYA MRQYFLKVKN QMILFGEEDV RVANLKPRIS FNFFVTAPKN VSDIIPRTEV EKAIRMSRSR INDAFRLNDN SLEFLGIQPT LGPPNQPPVS IWLIVFGVVM GVIVVGIVIL IFTGIRDRKK KNKARSGENP YASIDISKGE NNPGFQNTDD VQTSF // Swissknife_1.75/examples/varsplic.dat.gz0000644005110600510130000052701707606253205020644 0ustar ecastroSwissProt>sprot.varsplic1}s8+p0ɩ#z5 "GR$ASܺmZz$ %Ǚskי] $ hhE:OV2"E\^(I1wҳɸzs;Ja[kYliáN$ #hxZUM*rnE&CG3EeeaY-w_V\7j%oVg?9.GR2NKӜw04_~짱ֲZU,'b/j$o\ϳ(kd|-8'T[ \.n{RbU\!]n0b=܂'lq-)h_>\tY]Ujyg˪.0OS:/.soX9>k_?%({/Xh2bC"=#o<1I@2% /jJI q~u8b9_ށ^ևfo.W a(r/Vz:{G|q= c6oTI~R=7Ţ rd]mܯ/I0W5D%_WKyW.\ܖ%>!460`ȴAIJ'@&, ie{:'H}{Zwh ꮘdr)n@4āyqu7+ `V]+HQu;Jv岘 = KIϭX\}[v]|)f=:܊Xŗ3{M[oh;*6۽]gm P^ ^Y`D1t-}>MLvL@Зi[\-#^丂: T 7E_U )`\%tfA&†جj2k7)b6[ Uo O`@g&VB,V :2k>/dmE3Tm$G[=Ϫ2;n&a1ÆAy7Vp#Q-e9(!_Dt^_W3.ov~4e GAH6P-g>C2[fjT+bP`˨( @&K, u,0fꬹTK+Wè\ݩ,4QZKaYJAU>vU Qf~]dg_ R H-'^ :r2Wl3v=+) Zbq] 3Rץ5D%jP>-f8"diV]#j8XKXAQ[Zյ/=d+RsU%;RŮJfyY")f )mhs4IhϊrueW+)1BDTɗ7`0S.sDJҁgS\eU@*L,8@?!lMP3ršϸz4e1UbKe[banӧjj>Y:éQq%ZyW_fC>X*gխl/yB/UA7sU`=sXQ>K_RRʞ^V%B"P,7UF(J2 rU0dWźWG"Uxkh63葎i0a}BT9`I>T\.ҲL LrX@A9zAUI%L~[`v¾l$Ja{=js`CWR$]V*e˵]ߣ|!uU3X]D{L%N[s1+`to"i %Ōj#NvE/9Oޘc#nso*1/רÆ})#xp̯g:z%#6 PR.WwJ>I)qHLw3epI.ٻM򷽹mck*VCt k%QlFPwA0)&[ʤ{HWcP'Q׻ռ"yn`!@oVK r)lVyJa_q+h?DtqbvW})(&zAkXw/V;| ܺ.TsbǗzhHJ*+z9߆gzÂ,*py1Gg§6`&ѕTA ;օGFB\pycS>9{,|߇Շ?KԗF7pK(@4@ܼ=&InV\\o@]l5&`n5Ad])Flt8,遡@ka##n$|Ga]>E_^Jq/x`pw>ҽ` Rg%ʧ0v%5; =t#P(U8.;V,8 ѩ{cG _5轒9'R@U@.gly8A&Z.!1#2&]=i[x"> 1Y )u)$JPN=:=e)pi2/=#Ŏ-b0ŘrZ=q\v! ~kݍ|Y>Kk,yTDBDG7,"$7ch-ޯ^gjCUn_ ,1*z,2a6̑b&Z~&`C@%ec,:{?O0+:[b,3,@an/6rc LN4QSP`A۴t:v`2FYE$`#HBi,8fSLM=.GnqAf;)ƙi0iUԍa t| (/S%qӘ%[2OxB;iP)64q(Π lj>c}Kt=!vΏ@iu1s@,=J유z `;ֿWIц;Tx{G"Wߟ\pp9hF5i/ 2мF:bu[+Mrڔ2*TjQFHz++֜;Cpȑ7s -2QuB[qlN^#&=x[ޏb*6ݖ\n[kuۃsţm90ZA[wVfThӺöFRӵSu J"U3 yV;\=pK>Ѽ||5C'sX~59辴?vDw}Q*PSuF!FM}͔$B88Rh?$$ 4?ɀq$vȅ&%" V"bIl-bgŠOl_šF?Fe)4bfi` K6Ie8ٖD6CWl mJdHhӎ#5kĔrnIdHhӲwO"DB#mN%IR溡[56%I$3$dN|E6uIЦ5!S,."&2sߞDD$2l6-, m&=fjJP m$^ '&ؠ2MB w0u'}n,Aw5 lYfSǾIf0}0045NH6Өƶ)Z>\ip IHGV64 dc6 C7)GH"]FOGDc UifQgQ*S!5ё=JvRSLb!\38u^)n$Pl”|k #5xc>'㬾hhʛ)~_Ef.,Z0"? nֲ;4/u_}|So=Ǩ4³AL@o>tY>Q*yNHRyw]^3])kXP/Gz0&&Zdq Req]^5#D" nL XS o;SY;msxS@[еnohaU-G~^Vl ii[u#qrcs#Mk󪖣_/fJ^WW35 v`=B7ct `t ؽFr&_1p56 . -R~&,L,p 5˷<85M3pə1࠺uŨ -׃f<ϑG8~᫪(}aDn>ɃOZ6țtvzGg6݆Z7O&bΎt7A4_ (K-'6I4-Fݘ/R}+}+H(rS_!BfB-Ʃ-'y~nn4:(c` "{Bf']ȬgFZ!k@kU>`#vVmjCfSG$$2P";s#EbDL#Vqĉx.N 'LBXñ Pen`R# lĈD\7!'&XlC`m@‰~9gl_ Yĉ6Z^"NL(V81W0M=s?#+ PpbD,̲Pѯl0VĤ Fe>,$NL(V81i_"_%D P{;\)AXbDLbۧ>kI#NL'XB濸dg.^Cvi\3 dg,iℎ<5^^a /kW+g2ϱ{!\պ7^A Ro\d4^WKU|<>>81,E'mO-x$  }'Cg/Nl3Wr]$w<é>MNլl%DM%W~Vᝐ$ރ@ C3jg  OTպ9(_XSAnEEz-;x+Csn1 aQ-+ tB?Nb}]~P0, =S'O4!oBy 1X۷ߤIԢ"7D46ePlA@뻘tvl FzX`U4dnGU@S{R9AR`9F~!ɴSž<^6nsHa ~#Gf~''Ohgg_ s:Y(%ѽN?!xH i?kws?Y4{Jcۏ}qFkYO}(5~50O!sw~@^=zLr>[N>mŭ}}m90XhGN}mwGuHvt1:uPwt#t!Ύ{nN5]]' a;wٜ=vc(ִ㏛}截3Sv$^ZWG?tJάy![)3@'8I,pEVqJ`1fxZs€I f>#TlFĴEߡܲ,;R6IDMH(<y3 iŕ_Ṡ\# d87[aqLʎg6nI8!3zl>[zމq8.HC|DZS AC>g@eLyNŌ4H2jДz2Ȑ&\ _ǃ"V/ ߃^yAǼSqe&Jt HHhpe1l%2 V>3BzNZPJ;j8$Y b!iLNi{]ty,Vl(Sccar)t1c u DNF?9q""@`X)"|Ah.ȜvH `>n`aĂv^^FYIAD`І$ 9r-(\t(ȏEƜ8a!AbEۻ}s.F qXa5fB͝*[r7e hL-|i_ͺmdY;n0 cj4.qItyo=:;5C{s7TeόnHȺ]J(5(ðK!zAӹTÜ]F9MTJ#νEAMv9H/@ uѵWs]Kq˫]~c+&>`ŋhrů`8BT7(ƆWjOiPSwy ɽޯs3S 'G{z>Py-Apdz\zlz;ٞ)X 'GXa7dpὀeS|C} ˣѹc~J؊zK^ ( wz(wϛ[Xs׻vHY4-ъC{ܷVileW|,2C0mhmsSo%@u}whΧve䶁}|Enzccw}+ +,N - TD!ma2Ûc!}0]QcH%0"tKcyu-U؄=L_oa\).<#ƸG/ c&P.WsJlLeF~mz"gZio6zZ'XfScR3LfUcASqkWB͑!CQ}>M^^JRny@0W\{at׹&FAazL^@zh[ 6utfO=;f +ItK“[^2Ša +qAc0r|^VVnB<#&*{h @qAFA)cmF sF}%ܫy̡>5HCHH'вQ u侈s9zy^J ghVx`] y' 2lx? oJflwoʥzTTSƤЇެ'7@oZGvD={Sx+[I,o'Wk2~Gs.s'с0'$jJJn{;BϽ)$íUp厬٩Om|JmS7 i7Osg~2&9!ӻsx:_OIk%N?oo@~BZ~@vuz֟aݭ5 臭=JtZ>T#r"+FyFòN/1slǜum>)MSo$] 7`"O~ӻڠ?ZaF0ζmJ`nzu@%/6/D7 1?9]UfߦiϠ#dbu׼%p1 ""{]g\)+BN$ s발ywae c8)]!$e'lֻhLeu@\ T7_V$hooB'V0#ٔųY|]ݺE@.{D8;Jk.um_x&I%v/I[z8%!`rcMڏܫP]鄱0xTsá(HWڗv㉄>8Z]kb5U F + `6(▮ClqvMN7qqШ7WMehJ2cuz #߷ShDwra.W|-QW ]G8Z^^ bϠWb/ =]zWqD(ET1ϧ)[y8e/L:N`{-w KhcGk:`cMc*=McVaZ{:}/?2? lLĞ H`yn TnKEPT'Y![ljmF =XbC  :Tg?od(q0IcU]P{c◮B{BإDwuQ̸I}AӲ]'ExAHh^B3^s:9N5U8;䒷EssCwr zƠ)pD+@]yMS[Db>o: ;O >Xb~]1V#x نa SAf ȧ\Q fi:}Ӟ,aS#9ٓ|*s2o2P1C}*L+30~c@7ʧ> Uv:쁍L5ʧ90~̡|J~CΎ_N٪L{ ˜Tg|;ЖX=94M5~pȧ;<~;1}?2~ oΦڟ`2:̚Θz}}ug<ϓ0#q尟'ДycLIow`SsvTXT- #V,dϸWb8u0+YqaAYbZPPCaHyI@ȪZE&U0O" ЛrQh-<*sQ0[x"/6oN\\Ą3y4g^^yhBA /pB2, 5,1zWTeNBK]r8#,$Chp^GhZ\.U2}I35N\H nlֲLFMh<5ngv#(auk 3gU=oso/ a >E~H'}2R`xC w#Wu4Gn?wa=.1qA>!wf?pR2 $an>ޕ<̗Mـ6u3/czX~uBGE.->gp3tџ0 E ~*zSm5;KoI]&ԭ `y1mhMٜeT޻=,P٧?F!HElncN:٤=w;~q|"nu<4F6݇Ij{508뛓/!Ykf ^xZáM@O|ycWw(PTQ(FX*,EOsQ/d蹼x7}B}Bc[]l:VUMj<|#"o >~?:'b_Jh\c\W%<'WpyqЈwX-<`V@kXk-Ӛ|2bOgo+3_auŦeҝ:0p08|-\x%$;F`2{> 9 tA lBAjPfZq\QKN⣂(7 ʞ8?Bl-tA<:ʿҴ7+>.5^> g!j0~`/drJ~單߾ DT}@fx'/O{:`\IhF o<ܥA\"1ߓωk_7Vki`j @Q$xָv.KVlA^JTegN WodPs[O]xoxڿ <=:W3rr!SMSSnR#5k#䎅15J1iZ@9f^sD . +Hh8Ic ]gК:kF:%YK V"\x&2%b&]OEk$cZ|qt!`Z'xQfËyxOtV]x#D =~M5wB~Cɽӫ>_zし? !d&s…lt t?8)I뉣h4 >! n ?XLjWg]I7똵Psߢfuܭ6sF)kO.D k؂y]|> 6\=TX/ 0UQ)g귫f}""9-~q?ߕtBEbOPͺZXue0y˘eLAn*AqV0RT\3ba`Ȧ$ MX)Iɬ(]r1aitNtHJEFdaqdYafT4MYv.r0)%e'}0{#JfKdRazJ  $\@`W JֶUfD*QK^(k^hUQ*1 QS˜V%C" 2)QhBS*Le'FV1 FM%E4JYK4BRb8\rib^`,ć̀RZȥP?sH'yPc!TS 4IB29r\3+mH07*)Dj#-j`FDŽZ_S#M!7Fuq Ei*TR)2`CAFTkc 1R#VFae.&b ëZe3*jx8jl-\/A(rߖl23+=" Kj[GdPk^"B+MPA"'VzHD;'wf}}95KHl˛chW 8:+DT9`RJWo]='a7`=xN:;O!wmˍHWXQr@iּt2f[/Ƭ}]> ( ʗdw+F=\rUFmwvRӕNovuI-߭|z2za3[- 1 jmjqsV{٨%" ,$۩*+J B2UVeQ` _C"ctz5ۚrAwR~TBFV&vR(W{9f""nSbT&FEHkPͷ.G%XM\%ed~GHtnM`.wvO'I=WMv oEX!NYe z^ vrը :ABap,iGv^fX&yZoCz uȟ=/4Fwռ*CeT^o/VX}tL>V)4,گ:/M?XJOӴd֟G)7Xhz=Ni IX80{ܢN{*B&lX+^LQ M!W^I`^:72ssԇ]aGNκVUY-[(pNFH6'GK]]jUbT'Ɉ즣.sXud {{-DٺH/5̉5\?V6/zgUO64M YW**4:xj#(YL>Կq'= aI-ri'! {EaK^O Z!揢[Dr'-Y2T\ +/eQRk2_f/ ڤp zd!ʔ}QmhO^zw0궙wϪb/EJ㷬->O&c퉘;YJ~zk>y/SvERmb!xpgɳjƺ Dv&QM>DvOܸ|~^}wUj fSV⩘ Z;/W%O;;,S-#oZ>; R`DDu޷}/EwfF2Sۤm(sY;ORw5{<ROq,fvʳE~;[ᔽ7gQ6Zh8쾢 g.˒&?5h'2m41M`c`^|4 aV^, 氢@rh! ńJɒ,Ƕo"T\4/0Ǟr!oa9Xxڡ,LEԐ׊?P u~= ^bͧҟp{[Oaރ"[}*EJ O5n\F :|U?_nXd)vrkʙ ̭K o'U¥J2AUs+,vWx ׊ng_d\IΫ%YΕZRzْWK~$ՒFtNFWr :H[>r0ɷRmyw[ohU?Hԁ{/O.5#üx_SǗeȞUc3ۓadc HwD51j Q/]Ɩ$B2~4"KzүH,#M׍olcF g3n ]Xe1e,;4G["'Snj%I~$ M[aL;miǛp: U+ݟp{ئv@EHmn:?5ZinܱL3"g{GﾊS$Fk3fSjQ9mqyfCyO݈Ҍ7Vc]?HgEp .po25|,$sL%)dz Pxjp5MJfja3T%Q&0ٓy,%%7Q仾oQA8QqE̜0f< |VQbfz=Ë81I RR1;x%$L`FAQkB{yc0H({F#nݤCoƝ!gF!tGwxC} `NfI¸a|(=xtFD\> ?R(obw{Qޡ>$Ϟe\'0% ~kQam7ɷv?r ߊ[!FUAHl+t4H㝀I|)w9u$e*HЇWffST &a'Is3=O$AK ״*WqF*^!n/qw؁UkSC᠃4lAտ~?k 3å  c'cj`<p2dR#cl,J"?BQ2 izvϛ WG5,v~ ,A(5 XWXⅨ*Qdł7%&UUƶK-pKqY!fSx-҄eLo@x(*p%d9-!vD{":[Na&&{8obGWғw#a$_M| X\]ޕQ +_0< |Քl(H6iF.IcpiP~E0p2x~Aǡa58=ۀy پeYV†R_IWD3k+-(@{j=jU`2yN}n?jG©©©qjeqjk5GHL I9g,xYp= 0 n܆}0W|~a$k{ i?wX;n g~ 1IǪAFB)d C !r8Ժ*]m00I;="8YIFG!CZad#"េafer!Gx9Lô9$rAGבIy z5ۜ>52ԫ94S?}|&ИS8WpBFhH_aEYԧ.AVX̵rr .pף:e=om9Tg,x=orD+kV熏Fզ? NUOh 'K_N`L%ELcK>KkޫkшAF)C)ܱD0n-ljIR o۝=MWuieL,n1"n~=֢6%߈S?;K e3Z(/ms\ܩ Kz~S9oah.(+Ŋcu}WphM0dD?kwHJ}l u>PHi8D}ɚgut>}53 z"˺<`5kh*IWPMTɃn:-,Cǃ-62QW8 ns$胲NoTMX'82C5}lK jF?bA,af͝;nAiIvE|WWc1?AvLGP1NGR+hFG.z [xo4$Nfxfietι#6;2wtRS6#eõ ~:gqL ٴu-Jj3ISӨ9!BcZNjh $'pLެ5p=Dhu]BVM'qLɐ[Z^ХT:Dh d3C{ou #]O!Vgs,aYW,yS()ٌ9Rq>pOs0b眱< DO9?IJ|#__yyD#ʥg\HKX,krn_z4ݔ u? ~/G3*;2e)k+-u"-Z>upFa)jO9ZChE4wQzc!D[ľ(Xy x>GRNE,X)N<?*WE V1҂,LL*4O QQfQ_pc~ | W+a|>S+23¹Tܣo ܓq?{țmtOH$a.٣{mHtoO󀁷Pu}WeOznY-|}Xu}!ֽ6MҴ=h{lܝ癅ihv]EJ?f0C_˝ObInw` 3)45_bknlj^zy}޻9{5zͶƓW.hdb,U<>47M4M)xqQGU9JZޕ |3?r1䭕 Db}`%inY׋8q[1 Lsmí݇i-Ҧ O=[#е>5,]!*fq6Kn][shinkFyW|^k:$L`KOޚ$Md>GLIֈ}%=@Ç@zt? Kջn-%w +3 qeU_Aoݺ[}WmkL/ʶMf6kp}Y? .֔-45k;v~"-pث8VuSOSSnkSapS\α]ĶSSFsÄLvSʭO< T=k+дC۸1!O?8E1M%B ]u*!?GgIBq +${ ' h>Vr4'aLG` ~ ?Rx)U+:(OX)O+_K.\B~V$)$r>ɂǤ` ȯ?& 8L'%{SIIse3^)OJ)ϡd;L'yWy(&l2."6(٭~;_$h763^oIe[X)dm[0ߠX-vf7bF"7|Kktbb*8x^3d|W ME_O}zx.<- fă!rU}y.D(v6߱j׌nJkmow'7RڗU`$,*3/a-JѦKہg]M= [V EZ_OK3"0r]oQܵ"n5E_`|KN~C`6{7[pqi~ m;2Upsi>H}7jG aioR{eN{)h_ %i[F~o 7jj8 {%sy=j7bf"a %DqOHB[d(U7>&4[3h>zOUm { Tc#}5mh}إEkh=>ExZ{o% w̡[T}8ʡwVoՔ%'!~Ր#4QI>xU!K|ۮ^g"A6f"e#UOl7Ad&ZIMb -(>@ݒUZFݑqT{Weɣ7daP2$00ӕ MXS&cqUp ~3Ȍ&KpjL !$R䚫شdY\ԉ~D#-۲$,CZp;'3xS`,+!V(yD%JGn J|!hs}%̓,yļC`'AO]8- dd2g㘔YJ8~HϣqF*^|4"qdlyIW0?aFBOgQO@\Φ9˂tL)L3R)aʐGEH4QT3󌅤)b4>," rN0A!a*^OJ/B{C[jL0۞8Z Ë ƣsT)rʬmB]2(Ky3h7ks045Se_Yt>~B?:bH0R7nŷ{]J|S0gSPÁ([~.({f?<=^JO7S ً:0 8fu+og &[dW$ 6EWblUaY.Ta;F `kDRWBJю3~"0U|FњjKU0"囮« pzdQ|Uh2tg~0ݑW;I6pKWiW.3]u+59֍HF73uwNVoVkQ賏D0^!eE1->Jz lD c?V>Ù5T8M$N Ub}q'`8i;7 0.}Yn ?3ʹNJcUc0ֆ;Nwڛ31ڜنZ|iC"49l`eQIIFbe%eWF'T>FovMFϣm{uNR˨5Pdy56vz6wˬK7Ko:5ԝQ$ps)L6IIeI_2ėaWy~)e\K$_V/$_ |IR:_/+^9RK"DK/\*RK"%˜~)%2(xŸ(A|)}ÿ IEp\H/A|)%XIzI_JpS%L%A|)%A| zI_JzI^~g˃ImYLrQ ,}+(ܲQDI>=-Yr/bL5I~_|j*4 (ܧQ[zõ#}`'5ho-I?P*KLP8Օ\h׺a\B8[ 'C?'OB7 XT*uU"1ns_>ED?BMSV—_O]uYg`Z=&bG?/Zq{]Ȇ,֓:+r[ެ(vmAʗ1Pj:\qQ9ay4v.%c剺+剃s_z sQqӮ?p,Ow4yT5SkCdfksfR'rѮPũWhC*IGjȈo<Ŧ Ms1~wkDY9%=ꐆF3eeCZh foF:!T@3zeؾmwbμ8pCVe9(JBFe3F$E`HV!ddZJ$/ITZF#Ih#c$R#8t} ITHѫq 58Q# Ac䧨 xI!y\qQQUbHVd$R"1RK$ɂZ"ɔ,,b$J!B2ĤBMkkn$rDݕ}I!~Icwb{-g2~%ӱz*S۩$D\.ȋ_$*%sT&BxƼJIsHCR`I6-H܈sqHʊHdN1'i\XTHCIњJX+Iqq ὃ;w5`gq.{$IU:_KL+>Ͱ8@4`_%$rY;|UZ.irCAdbBxg ,+߉8_ޓbdCLDfab jFXN_mos CXR z{`CkB뒼AB`YNj_XY(Av1KY#x*^ ru 9PgIB%6%os:Tp[Cue(DX,]qlhI9mw縆,R.+)68h Qp~: 3IxLA$:9/U $@L>(!wa]yI)h9/s&9ͳ,c.qj08e9pE1Mr͕eK"ʶAHX0fQ̱Q &HIefRt\ΓGvsPiT8SR -^(Rc TC,Ң2aSe^"f*\̭IeHs,ƨLJAtK4s[Lj -̖V>5_V7aggSan h_8/naq8׆{?LL٫[γ';Ϟ-7]6;^p(G6<E7mOۄQaPE hL<D'"F$E5((ZAQ Q>EP{(AQ(j ~< 9QT̬V1§Ԛ "AOk I e5H]k| [ӒmBӺS5H@ȔQ>LASL)_*=2eM=2H |)…GGZ)#h)ȴ|GRq)d)#h)#h)=2H |)#|DםkqQ|1M:%LG`+&ҧfO:sޒPi]OE(^>mg>W3 M~'L›՗~emɤo`bhNo/P6`}AI d!Wm?_Dh6CB)j%@C|/k-[~Z5t$;_V hӷ[ էz?7LEҜyl ˺1 {Px۟OaxS^3 SP{w~?N@5(#\¶!j ;\5*zL\Dī5:#uuӀer}[st/~Ą7:oOWߖ_5?I[r,LQm%'lYsCy]G/j.s>rYHH0` ‹E|n/w|&wY` 8oaHЙVz |{l2&ƪۛL_Ί'^8My"\-~vtmj~R[oЖꭋzwza *iF=2d~<7ܧab8HpUi((=fΕ_U%t2' 'JWD?/2Ѱr*ԂIH Uyۊxb/~FV s̘Vo4ް5r,7;u5oI hTI[7Q]lDJv:N2OQ "9}`.#6{{}|Wkϓ* =WPz٫m_c2 %EPY(lX ڄ̓lx_/O8IhDׯOU$ {vG-΃x޶]-zjO]Z݁rhК?)Ӗq+C #:bM1x?ч nKj<}ioZ`PVofhlA@q^ە5i4jt琬t;}ct.*t{tn7w|43qWȼwKC@h״.71lMG!bm]B$~ )8t.m zd]ӽA@ߔ&tWa9ܫڭ;'6l3! >!Ű~^`VĦzs#e'%YwcW˓/ 3ZzQ,- 1gQrg%7OG[n֨o-Тr/*fHk3Ap/D wLCoB=A\GDve?a5ޚߗ7O؛MmeMm1֞71`Lqq ԩg{L=޿tpȾL2=^H5f{kE a|``{tFrޘ?)+EL=kM\sjEF~*l4-UIN;TNI~JL/DPγc2euR[~u /"JKyD[3."BkgtFY x9Z#uf w9k..B(-(KKX ~-7fŏV;w;]Z ~n9*^i1ܒMs8׉wo[wNlԑbuQ(>V`~8#ħxmaOA"JLh-JKSePi*aYReT$BI J IM+eE8,*2f7&'3 B(WlpkRKf3Sc$#٤ȥH:L΅ 62*x$16[2rKp|2VtDZ)2!K^+QZi3I:%l^j,"3'3jt8&%C((/h38r[-lYiCU"0iX(4%3e(-eT9ϋ||PxTbb3uV$VŘ qKsjDcOBT&L0ƦN Q,xXQX9(.dH0=)eTrEGL\+ 0Sy)PBI`U2g*Fk"1AxQdX' \VĐN)תVaadIjbfJfAi#lZ^oWtV/Q構Y)3^,2sI8U(mթK: R.$m"fM >0$D!d8b9/jk`IcM$_A%K[& 1/Ĝ ԓdi1Ee* Aq 9Od0LŸ\DE.cYᓪ6{=Ui D- >pV2L~X;g_6 Ӳ`EnZs,O4^|MX @UdlU}"Q^<-"a :A6 +ҪrhPBдt#RpI$-J-i~ \AwkZ#׻?[)w ɂWs??_Dg[NvyŖUq]^[ #<*)z?6^(8mGO&NCa:=TN__041 wh/VWlqґ'𰾺Pdd_]}y}zuC!2z^~u/Sh46_VHkknieޤ*+@B"@ v)n\Vb֒ȫú_u M6ٳs yC?s{ǩo: to@S7'ouS`J񤮬qd8*rS4C㘔s g^zjA+>8pFWՖo/"<߬ bAx"uL'!'$M\W9dF%N|^/G@.Ўj}G^n>8n{nrsT݊TJ->Pz~ޕGcq'Ys]qnm}j-ʅ h"0.֟CUK`vwnaP0Ӆ3Rduc }$٥TU| fOU]EjBSuJcswj},x۝W_K O+$OJD=Ke~>j`f^W;lu' ꄻϵu)Ǹ [^Xe>Ǡ̜bsTm睃gH,f =ݚ$#`EoNhB,4ј%:b[Vk~x!hɦX7(jd$S 潖G5]sV}r.%-ҭڭ֭X[AbzbnF݊zA z^лޭnw^0mhA|'XxO']N-O1:źrcbK]n5Ϣ5ԎqD/z&ߖ ?-XC6M쟞 ˣ46C|Qn?= }hF|9H(g+.έa\g<0M(޸,KuTcG1Z ͝4Mu=f[ÂĢCVmff@̥V@#ʲ`G2j ´, ˙&ofAJZ %60;̢H26!0(g1M፲IfR6E'3bmE.q2 Kef Cl@0I0%#)ciԞGY$IH-+ͨq'va̒)#Lh|]\6f, &mukXx28=FaiPrC/()O^$2A(c&H!_d$ >sx7=<D$YgYd#:yXqyNCI  s9Y$0-LFlיZvFUX2J/6,V#MGYb_Q[VoHa%6Shɔ<՛L|J01Al׍,0Cz ؿ!Mjb.; -ya`1xS!df$$|̰ rQkfMC^{n29X,M9&ngf y ?Il sҘDxo4&2?%czABa _XgʦpAo̒4#nԇQ2'ws^S,WƷwg00PqD^lM&ȑxN #-!|G)4fa˱n&dfC Βh S@dv j24Apj=+fR1Z8>M_ a/ EWUYE7U܃-.ՎI?l-}9+`d #l>jS큆/źb ;D:vEim7 zAnȍY#I3 L{зG9X?g,ps߃8KYb8K Β"΂THRc&ֳ8gr\YN,0Z2eZj8KH%BI%B4P 2Hd0Ԃaj)" J%B4P $BP M3ZtZ$B@%!P `DOZx a8,3ZaficxOÞ'xKD=-noB6P2~C.7vAߥ' ?7:9y4mtsp8P KA][{o'qT 4 UQ®+Knu)ѸZGr&{އ>|dSؑѩ^C#6mNa=4'O: :DjQIrvgu; ( @AiۈTmp }WYQw oE`NU&ὡP,4~?y*QS%etEeઽ̠* ^5׻P4@) 0,KwN5Cd*l_rZ'#ԁoLlvM0֝`9l&:M Ir뜦gb pYd bN:a"jvQ2;uicz4K3KfHz44 <09Ad0a=0iX,b$OLdYu`, vh1/ -0hpßHe(gOd8ghjJ#7#`fa&cC$sIb< mȼYӥv؜ֲaaP6 aT1M\L8 G& gYLPk)r}.Y:B-W}2 /ʂ'gJm1e#4 ~1eSV)X+p7{#h7 -[bEǟ;Z-v[Na,㦪/08Ajɠ#F|ƀ4&Fuqpp)& /RDၿv=ő@)֦Ukpt 1_ m8*@G0^d3)]Y T+m[q"9\נRZT`|@j%L׷X@YOz :o o*"1a(BȞӵ>1VTW)CnxqcubnF7h鴹B5od܇&_ R0oR\0lJᘄ;o .:=O_%[T7 ʻixw` hjEqK`) ]-J>x*sd!ؚ0~ =Q,Kj;||ʻtb"|\A1kQ͹:Ox)e(\]\7s<kYW+"f[lTAkXė/0^UJr_02eZ}݇Mw0Xr[26ܢ"s[kKPo5_J@iY `Vs^Q\+^b.?_RtW,+ET)PV("IE|QsPb/ab }.;12fHHK;l^nJgv *>+Kl>=6ŸZs;9܈f">q/І1-Pr׋spkl-CX}&I\-#ߠKgG Y6(аl ?w} }#6Z4Uګ.lWhF_e])gNʴ$îG]  *ծ] /H~c9VucxwzKe|z;E~, G-;آO&R~BD5Xʨ7+:KDdz=:C):Gǭgq_.xcy1e08?wp<(Fgh CնL-e8;#yjgvy5j-wufaw-i%ƄtΒ{$B (@>W>Cq?QƽL;ސN~R8GSS46G$N%,@ݺ ( A4>$CX4xq2u? v,D]R6'`(NDNv=: bX|e??dSl;L?"KI=Ej#UUNֱ&\o1؋! '#'9KwWW}nPré T45 Fˆ]TPyE~O)am.O!d{@ ,pQ /rZr&r&r&W? *gHMo"L`܃"rjf 돆ܠ?~@NxՒJPWH ~K@zT@:pD!M 3Fj_5GRNۗGQﰋ>-sYu{hED#4'Qdcm[vm.fI]}'m@7-d1!Rmb8X! 늡 h|3$1\bYN͢vL)f~e1 ?ub4rfrg21ͼ0yfcv ;nA+yN$9:"+M($$u \'b8<880Cl#CC]ϡio'79@ˢbE ko˫v_VzxCBGw:VfybNB6NgMS,I>IE|$g-Gٻq%W𘩊\"LL   |Rd"d'o7HJM$gN6UU-!<` N%Js͓:[ӡ9l\m4Bru]A~{). CXi+X*6,2y`A-+3fpW~-BR+x9C%uWw; l 6p%]"r@*vJ!^Gs.? _IxQW  حBM ؕ5(0_;8=a2.[lجU}ը|n/vvݾ?.Rfhl{A-0/{1/gi8 E:q;/N*$~sWϼW^>Ox} `{U'Ю}I׸mu˟Yrھ+b]D 6u%zs 6<8=^bښU; -Fܜ'% ~ x!_0aE5"vs+tJ}v,ѶtߜZq{ tnD߫4OC#*~0"^3w\#`4E-ǣdQq~EZݧnp48,P*Dqy}|Os)]%w1*p'-.> Gul#'6gqlÈ~s;X:8mڕz]y+:&t?EVP$y2%PJ-hNYe!uaR^akt,D<6 9+=3%HjHFɟz6 el0gJ*)M"HOgFUYBe|4?0>3l1ltQL`C:1h4 'C VQkR Sn#ٰ,La.(OH,fp֤\ G(M \2J")ELX"8$Ҙ,- N<%\c,632"2 L :Ie&45 N#PY1yin@I'JeJMYZhkc)3d&ŴFebEi9hAqbHɜEY*NPR)8R1-x(yaeRR0|i36M3LOqx$KBY.EIhE&u)SBLnh1l'6YIa\5\S:K: 6ˡ#i e%҄`ђZVrZZV$20 o 7sbOKmei3͘EلL qX74y6D< 1174%FT6lqSI:$'JMɥ@:C\0p?ΌI=e5!)> PL-fd;bqGbaj KX*t)3d31gse9sP(|X S)gP*QBUF6ĘÈô]aS#ML =ER R(`U(6eBPYC"5dJGKHaBR|¢\| #gY$F%ySgxko1uzi$QTM,<>c|Ub$ӊٳmlՆЛ^p~w88O[8+nSG;NRsQ@srw]FWщqSդ6؃=kv??ȝ;'.}`Z#OܐnPBd_zjeg;߀^_Itۻƽ`}UDg:{Z/ܶߏHO~^o7Q#X"O,ulY_KiշS*rAY4cQ}sI?o]V LHTɩ a{BfH !> D=G= 'm{:e|Z"5QyDٗoVgSu\]\,Tk xw3r z^7 HE QUz}!q=Xߜ#qu};_mxCpw[sO_N{h\~7~GiGϸhrtTq,H^C'\ӌZ}9X㤁<)poX`bľ 'yIA?;F큕]]" Dԩg //1X93+pj~<"ɝnaW 5"͒o\PKlM9^S[6AV y]i ZQ0imX~g|A09B“Jd4LAi0z{?2 Ǔqrthim3Eqf;(?gQЛo><ˇ;0~>k/vL >3{&&߰w]ߎʠA-Z3f]ᷧTK3V_;/ߡ(S`t(+* ~ +wWsJzzAm5h D 5&<υ憷̫bz ^mP1g`yôKuMݰS =~6|6?p{L{mk腺U~z{K`lRm3t_ӳAVtS-$`GI\zx$b2hxttKGeA2Xb>͊M+gEB ͬP3Qb+ƍ'iNu!W`T+Tqj4%_ލ#g.,"֘Jc߃[W/?'ڧ|:̟Q7qN;u uVuCn=47cu ca!=>F=BQTRʩZ-0y Z!`3 _ͩ $+/!gdF|ķ 0qMUHdi -~g\hyZF~ܞ:Yn0Md$9̈Lu)%`c mb"̮n$)uT$1+/NKHcD\d&0=y1u|Ѕ4<>+•"&UL˸(;rX?$BsC-Ԁ!+јn\ˣԭ1.ZS -HY 04RtʔFitr @Fu4ebdlR6"Y"M06QࣦM>G7# ;鉫EFU9m9\]74t+)eB'#$j:`=of_ NG˪&veiUzBׅ5ݶ"UJ;Nz.=e3:8 T제7qzGf~q+%g#t7 NR`wtwZ7iяƊqE/A$bn7µ2|5nL]h4|Ov|ߺ!T/҄R$qd2 %`h5`b9Y.Ks)x4, /ǡ)L"쪐 f1OeʱDbh'iAbJS] -8!HABѳ'5#VHb4 K1\K<95)䲘q ٌRn$lR0 kFFPWDy)f:M%x=Fi<'+,8$c$ !U1?!4U$Fj-8#i!U XLKXiN`fG*D(HS}u ϡ+܂4xr5C%,\J-H4S0%ybS$ 2iK "Li%lBTDTpKl'64UrKڇR@t +Rkc d(AMVP x#S\7Th F'6xZ Y?mx]_򮮻miܵ='ʊ$JLHɑmѾcm_3 )R8{j:33 t1WGѥHuBәV Q V@QlIBm 3)HJr8˜ƈBت%*t)A6 ހ! ZfZl ߐ LD >} {DotNgC3ofy׵W] u_󸈺\x&,!*Nkrsxbxsv('?qkۗhnrr\ZS ,I3iO6\Y3}p=5$wQ- bE\4>p[YG4 g"&7p%oVX68L+ͭ[ ;\imsMLiXH!W`ahAPFMAM[YOͣ8y kLI 6Ih鯐)/UGS7]ϠN]хV}^]k4rκZΩM0F~qK+X}D.`ÌYll=Ļ݄l,}o} {0^xX灱<_m/><޼"5[C ^]KlЍ vҏt?(fЧ'~(^^ݿZ[hb 0V{r Vlso(Y›ts!7ईl&dͦN'ekbНM=w >`Fp͛LH):U~R}|g\[eX& ?<>p|޻3h!({,8(1(]0sFKܑ8B cސDLO1p3vYxυNfC*glQ?1{]]Tb.@ ٿW` g.OdbMbI\HիvK38|vMe@C L%1-͟j<`5o~~  !ObL;3al>/)#B'*My H{oxy!Ufsל6U ?9J1+d4(HpV·ְMZ7ߚ~6HyOP3F^᭘u&gꌜz%\85vdrZ]wr1:t9qmf n%-X!ҷ|6M1ۊk?;mFh}?=ª2]A4sAC,&ְ'կ<|$BP/PȝOd7uD0Jә%%Ӫ_6d.$.CU{~\_ѥjiA &i)D]!/cwy/o*X&jdMNfr>_C Km݀cȹ9o?9{fVDu?̣COzwZmk{gu} r_]?š^գ~.ms/PG;O 갳g?'`8,5Agw;iָyݞظ}aj%Lq~NKu[Ud-%IW DX$;$RЫ4" jX->ʿ{’ܧ!@ rӴGz}$qiTxzf\?ӨlۗHZK~/GpBl̶4smi"[8-͗g[l[|9z؈wzM1Ky.Ozr8 u1A;4JP[f*\_/5e*]*) a~cW-f5>d[Y"Wd^G6{3w%~?뮺{X_m„@Bĩ ۡT-au}XZwnUYU{ʮ;dIóR{sחazx@mG۵}p"խEõ}jЅ p^hG62ƾZ\peYqݴj8.Yj yhͰx sH*miwȩ*Xߵ 8gy3f[gK#b+:_)F>,I5%33&wgx>vkg:I&SwwMdMFY{Yz3g9|Pr.cƒ|`;toޣeht=U ̢]d C٘iד#),ft:PCqXUP}#}`[Cp0˽xs$,vdl@AkΔL9N3_'r!͉L&/x_]7$JBqLS8-5P-PQ.q0As$jFڏ ,9g-GL}Oī9*ImJɫ0{9G9- WlD?0[jʥHyȢ=%0c.iN!I7RCBuXг>7ܒ3mLޅ XM(åo"UyN68RjzBD&vo9tey!dӭ bgowDӳWę4ړCܹ0~E_oLlx4H%yar񆨂(*i 2M$E䉈sa@[ϸ)?"54#qD"*"X/M͠7F&|(9IyD>,BX&DJ1AChv Vs̜(X` 裡# @1Ѕ5d?KUtV#BmsED>MˀSPF)4OSO( E!b(@ReMbBvȊQD)9 ]KyD#ddKNr':3 9;oq^J%(gQqggeҀawB B)H|qҁg((2$H9H;,ϢB <2ybBG&9tAr䍦C>%FQĒn>Gpf &09ltHEq^LJBhɘ9Ta4Qe)P#wJR u(AEѥsa0<ʄ46쒙P"$4C04 GZE#YYhGQQBM8#H2D%O)JWVx 4TUDz!{GbOw +JD}0Rsـ<@5qڻÇjϡhIHuAFuK9) t#d6ҠW5z[`va~IW{wW>Wʆ{9![oxb{.[Q~n5M{x6{d:8#l~P߾9}Љ۝ӻs|9yz:щUm{\"E/›?]}|CyvfOo+x5I[(rs/m|L׶")SU0A`_\j{) )J,ٝIWix^\9&Σɢ'/6c3є>+ވSH|'=M$xO*]פ]ɚq{ݽc?O'|>#/[f;8r@xZsJ73߇XȾ57ݷl=nJ*p(y9sϜ3$N8ae>#p5~ǀoZן?6~DO %b/4wJB* 9xj^=曖Mjq /b985aX\ʎm! 11uJrplwΨ)ebN;ګBx FʄgIٿ,oƣ`J9. #j!_Vu4D*gaz:ߙ^*n fR=B9Brb7d¨ajtiҨ3TX T0ja&@߶~&*J7AI Y6T4`xhq,pF]hBWzzUI7 53Cc˙Lm/yd$2,՛zYJ@t?1a(@U J]̕)s4{Hb@=PB0'm&bm럠M6m7odv 3iG~/)\=P="cO_tY}$zbÙ4k^H#0Hn^# 9`!|/d˞H=t:Qq3i!9Zh6}}fDkNgff& 9'4LihoHb=4E_ӣaOkY9Bf$}OH[rM;a Z/OQ; y@3l|:Œsyڻ9/i=`ޤSXceYp>`<1kΪ hq+\# iqPkP<%75XoC vc{F{k2!T%a"a\)QAIQӆeVBY%WiE I IԒ2JkOi`jɄQzŗUʋƬ\"EBx x$%.'" ԝvxp<^1*rǝ*x``gLf#OF 0! &QZJ @mtꈣ¦F3w¦"ܟE x->z67_78Rg|?5 ăο{{PX3k DDmتLmi5OPAyVk-ɴLJ[sbp˸ِX²#U7OC*neQv{9-Hz\#\IDgsog١gZmWAB;U-{6GkUkZ7e/:rH]bkzB=ߞ D1O7;b &c70γGxgsk:Yxqs;|M3ײ=jmDgqYY~JtvtH8Z ܌:wj_76 Crfel e! "VamBh7zLnYIPcA X'nnJaqXta>G 6#=̿ s1'~X _6/A󋞲,uK#J&Gk!HdT-`m>>[0%J2ċ˞:HwiwE;8<wXhNB/G[˂CKr|6҉5w+C`c95E.Oqu7s4e0p===Uĕmy$=~ TE:)A$`Q|0U'j z yY_Qap }<\bʌ">@u މ5ݷmmZͰB  u]Y/$SPEXcuygP-L2h,9^3xCKgɱ),-qÖmm#$6$uX]Pݎl= fw JO~ -R`\4}rjcb)Q2xcAm-(ϴHH2m@Spy"؉ɽx:$Dʷ ZC {(3afVy$1K!cݻўl`:Y1S{6]ڞrJ( dU<ͽ4f78t\zŸ'.Μng,%V}MY*ؑyX*(ߺa_fsO0'r>5W9- C .I xsa+?\ߴw{<i~udM)R Ed~# Y}ז|j4{wGy҇IZOo 7jA|e;9gO[6Z 7n{d%X=h5^cVm>:;LF \7-~'pڳ%'׃T}ny.R组HN]^+}(=>Ӽl[}^}FHI x6]"PmQ| agOO'?[vpV뻧/AnG1z;wa7rmMC[X<Du@a"ynٱg a}ltY})ؗNa vb-_~N6v7_f7VZ]#65c6:-WYcl ;sw2.iGkls ?et78}nO i;% aV> )zA8QOv NCC=ꣻ/vAI-PW-;\x?W(VPA9s~8`Ht8~UqRO hᝒ"&"a4JX.ˬ;-F4jSqNV)B%MKEޖ{?Xtm^eE5M_쇐^C>e0vH7&x2zC&4@^g)>m)L@퇱3mSxq.C|:; )Y !T̝ ~W:80=pB{0\0Jb! ۬#n;H'C&]e'_B al]paxo޴4Yi; H]DDw+֣ mmA0˜ ,qq P [Z< haEsn+tm?u:nVR;vdz umk?3uL3OE^kt8q3qޑ5AOA"c" F7WYal'@loÝ zs:u<%0U9D7l}"7_tx𻣗n҅ީݺ[ռ|/xf1򿺿y9EO-xvr(|[Kr[hdQAne?Vo9tj{W\]9 %=#(l.կ/*=m@erϋG +[y3] 6/ڳ[ӻiuMQ2APE@#C,c}ݢX#;49 =LBG/jejNHcphn)҉*Pq0|A&pBUq ^Hj:E7^vɱl,wxrlX~t.r|UL?KvԳDwtl=[FY>4_[?\>Wua"{{^ a&Â30#pRT`SMCdp<5{6ړ c.W[ OnPy f9c$v̌J぀* nUmO8bCPCL|7L-C2+-2r\|p?@ߐfwfWp#Iŗ83_Ï= Z% ~DK#5sUR%8+=o gȔ-q>#>j|S-qB1no|b5+ZTY}aZ=A?ԪQℹDJc?W6ՎTϤ7x!ν(.:#J}rsr.Zb)"-߂<#k7Wͩ{_J)M;X 7z&v}])QkzT'sL nuzO)@0}&{ g!Fyr \ rċg ̉r4nsX|C ߭Q7瀞%ugmK(^lU:s!@*7()McPP #0W79hFVfXJyQ3U@*&]u#QY\usm"<ёΩ%F$L_ZefKBkK2SM2 Y]*onmUܼz,P 3nAo5^iAUX?<1"-K:ֹUcK2%ޭ2_bػܗ$2Y佲G6 nC)+>Pȝ5k\ 7w7LhxsY xs:wJ-"Xv|s&`pi y\zf/PenG:P -E`\76t6~I b'Mm.1˩xZ+Q7e6([gz[Uodÿ ~.׼jzJIuz\M 3pZ~2)wSSm?X$C=۝Rr~s=SWj}۱X~m>n6g̪hwCM^W(`kt“p܊^z*=`y9jrSY6M\'u{c:٫ۋӫIQ[aioGr[gc^rIg2/{X7~/قfe-#Ӳ ӵF$0ZJ:}wg^Fep:hQJ1SDpC~Zq;{#p,歭[d~L{Ajd~dr36.t5ոR~ Eۗ@De~4U/Ա/Nx01n3#a⵮8ih򚦶4:B:lY@E]~ΎD4abWXQg;b'q{tOw8:w/F{aMov7枏@aSN?Q9^tx#oh0Бph:2?"R}O2W3'kJ^,LA_&5(:~ cttqX), ?E"԰A,AF],4Dsocƚ%{uGRU]6)%ZxdPѱ${`So¿ң9ui>~'<6pG ,&a`(4/!ʮ$ TH6-G0SH lj"{OA N1wv?*6uD#YSq=7˳4 d:qԐixSM,O#@Ey!Kr~x7zKƞ`ŭ@!3Dn;F11pDi63odpBvC!^x%jě&FYR#0:K a Zoi|Ӗ7tiֈ70fV2 P#Д=94(*S@=L- ^0AG!\#,.5C `E̤(4Kb)HZ E ˢED\E7 5,Q`d2HqϘkI7dq.OJLcKT] Y2!rQ8uaBBԈ8 ,D*EfN(հ9$bTob36uaiKa",C>\3ىq +D"LfsL}uD ,K2A8>^ e }LON8xq=%C+&D#L0 2#s z}m1e1xD,[[Ǐ| "X#t10`q~XC1,i R``FrJn YhMayI0WqB8᱉Px98%D˦Ny1=5R858&X{No82ʅ0f ݆5E^H{ހm3 DIuk.%2b|˹v0 ~$5oufy/pAqANR=1b>"])ǃ^gt/`~,yyNwU3L"rݗ]Ys=ghvI'SkN\Q$.DA|zD )!Z3;_nд0 $3&׏}C+eBcexJ^WdъҘ*LypyPwP=->[ l#QF*Cd}YTqN;Q/r|B DJdU C: ܾh8fR"=fA|W3,>'>̚Թ[.o1O 7:v@"ew 1uv5:ԅ{ЧR;zqkˣ='Rt$$(~YNCq=q=Taw_;NN9 ~x3h?QTxwZ z3J|f|`7r󼆕sT֫?D?DĭΈӰ#90XOqZ֧|O'nrh~ C,]mHMU~Kr}^hHoBEcY*pXאּkW&&{]z4&u|Mrnç^FuF6Er.{cѹ0G~9-56"eg8KZi)NKءL,H? (F:q#>fM0#;5N SK=ee̙6V)`0H0tdl<2;4#.?c=pX}dO83#3!a5wfY){Cʩ ; tm0'9B.ҳ@e܉-f2.8fV\pOT0],RϏb!jlL >A 8XLsl'й-6Kt`$ &7P7|lia͸քv熒b؈(&~&axo,CɔqE7] 4V ]yڜ8dJE/37_CzV! ZK 4 ~3٘ݻ=1 ~de9@Jm1 |}edcnzSbK6R0+Rr §4([.h鵩~+0f4O6B?>:[(? ]~ForꔗBcS>U.t`4Z`r&z1ikzkF GC}Tn&主gń2C@^hRq9,j qUTDGxnKsg.ĬX!xu{t}1=s]{]wtFD-)4<-|OChth$ ?W rM,aTnjFc:AtC Bu?Z;dEV62WWzV۳A^z'=$x Wθ_gNJ>ӿccI?ާx %\:Wy 2[/<ߗ0KdtzlStG Q 6/ш׃B3GH}(*FKqWM4i0ߒ\\gTӠ++.RH<>əU#WGTΫ[M~s8d Ʉ4o^FA άt΃R\lc呣#\E}{wo0'Ɖ33؝ <_SAQ3t(7dX]fZrG%/m6-t5{R!)^B=;c p0p^"h CsZL( NgP>CNj|gp] C@X!O?V%}ݟd`ar*nV,[1(49(}'hdԞ4Iei.ڽnn_qkOEd/a~jum> Vw}1V68T@k6ĩ+'߯&8XiA9γ?f7sCI% 6NMj) C&ɟZ` -`hbo` (4iit69@=ea}dSZ֓<AtP2a'[(oI )Gsz 6C{ƪ>\0$?hZ~: ̓h^{u-4f0$-9ɋh.;I}D )_(+z1^e m$X1R <ď0eĹz~:dK Q"=_dl׺YZU{Wf7$B'hػԆMs4D|mnW۽(vɘq-mp+E`7M.j!=_&tC*Vj'U=Gdul8O@oO@`Μﰩ6)㌵d( ~iDQ5j&Fv}&^=VQe=-L=36E5eN Mb]2/>*,70M,z߰UOcg ?Ih_0zkOMO'BMfUl6 "j@Q1H ^1z*R[H%3; TA" mZ_?ў=??́B \̶P}Ue[LJ+p)+?1}x\PvVZek>vzр cigsuϤq`3K6Ɠv!Oә|moS>Þ>I3AӱbŶ~ N%Wlj{QM.^Ϝ۝2s5tku$~"A0gqNM/V%ᐩj Qq. r֑ s(WC0aLž2R{&a]X,sԒչo6DQ0Q;U(7}O1<ֺpM?Wku+VQ ^8BE_d gT`H%*[FruԱز{ivXGS;.|3k*UQy*g2z;WgWȽ~ j+lkPMQpڏxtTh:J#>Hpܗ.=fk$E7wO^ 8@xS9^M$v.? K'Ck6tFp<25")}v] n)hJr0`vȐeWef|r? |7 #˷s*(u~Igf;e1r$B?G!sWݩ#l @u9T! | Sza}nL0-LCҎbX@N 2G~(+XYFy-{rpS«"6tXhX)ܬ.tQ4wp3ͩMLs3AD#}Kh!6 9 sgሐM%v& k*c=aS3e?|pZiGmv. ZF+ (s1d/,A2m`F@DQ(H"qdu ܅Q3Xk-o=|t`'%dG37׽{\ pH>Z'%% IJs*yA=Hofv;v_i$/6_vF1hA~7,4Oqʮ;!Lҧ.xOgRQ!]P5,pܑ@6>ݩg'󅼥:^eTBKI¡רFp: E$_ǷY:k}]ojc;`׮J%*Id~h-%eGNQ9l>%2<q2_; ü&_ƚJ$&#f:e;Bgnz3d 7$`,M0 ďi`v[v6n|1Ί1:0W? j%*+<VX4x\;F,"Aex$!3MfVQw-VYT䘬7"-jKBo8Kߣ cnŲ2/:OHܬX&Udx2 Nﱝ>Hd At52_4?]1Rq'Fe3Rf0"atTЫRj g3 լltz@Tfiha ̯"fфYrABy Wv(VD']%\Yu5neˆYwL|#s (OAТ5ADHuzf$ }aպtɕb-OX8*wBgrW/E:x :+znq9T[ؤwɩ$d+kESb$}0Γ_lװD!Kɝ\SM~uR V-hjguWE>ѨmPC}@ Ϙ0WajuF[ { x͓u+4VG;),_ִ>| Of6fso[}^ThLZ $CJMC^ɮIHz]4lըvΨ)LVXEuDw_Au4ƊInr9z|m8<_YE಺aYݫ掋@1N{Հ$M)m?3'L=# p* lP p)04?,nwhf0a!h3FH[r5˅RSʃZʕϑnm>[˷ *I;+O7+B=*xW *= uGT4x?Ђ#(Ά6=*1A D,g]5G%x$e3}v8F,tb#cm|[pmcMlQ\3#bWn}`n'A:ŗJ~缢Ȫ8if{x8❧Jѽ(lG7 vQ7Ȏ߄R8SgE`%MxJ^<&7,Ǝτ1QQ`3$yhA3q4TlBlbtb|bjBy4 )@L $c$Id!f l'Pt"c&BK,a&q2\Xzm FID>(LV4q (#h,, Y h E1= \!] )M33pl Brlל g2ws9{Qeȭ`qp-ZjlFP})-h[7$uHd`MIf0oy=U MVhj >aɲo_2B8ʐEBba0ߓv_ M ' Ϗn/{#83=/lnxhMs0:m1'?-˱Mv(m9ls!\w3ySM΄nvF0>I:eQˤi_*:rj(" ;OQBR@n|,7hCwQZI{ ۝oX v7(=8]\ge&%K^&0#uwqۛT2ͥë A `0̗Xz%G l5[joYTU/A.lf=QY}2tٗ@=h; m{,7CLlvI,Kg+ܺjtJ^/jdVʋ졒"\J~Emr3i(%Ͻ2+-vG|,{iݛm+ya@9*t#+X?.W:$XQ^8k BBDcDRtyY^8W#9,Q=K` $B- F߾4X:[R֏;Biق-BԷ_)YYhj qՠt3 2^]ĖU }k]kLL6upHVvd2~\vY)jdjr}Dϑ/G|^4[OWzlpB^TT[ѽĠv;aS<Ǿ|l}m'[Xr\(ZDo㇮z h.mf'}hc"hZz9A&X6blsp,VOŏwO TcNZS#, }$ 0bwC12Qs6OX9#VY`{Iv~\]F9ʮ 7u$ o |e: pO1ȹBnZ M0-S(fJqT5ڎTuEO^*EX'Al\,6n!R$"*np}2+W^L瘇[#\p!hބ@|߼|5 8JV6Hg=09h޻~>J$pN,h>? g*O"c2Ps~qjP3"ǙUydV-]yܪ?$jv"LYZ KMkKFg$Mն'W/_Lk^\M`c9ǯޝ]{컥ić4F-s"U6: 8$ZydN/˴ؓ,gdأ!a~uB8Eq\ws#*N-X푴FR׫Ȃ[9]Z#f_FxTA~ j.2^X"pWH% OW#U,.0Wu>S)BYJ63Id{#1d'㭖4vi4~88qOOۗ J_z֤O츎!a3񜼎746A0ޟ<Lj bR0u/oIQE KS:ϑzylw@zVwI(4'ͳz3 ~_M>HO,_oU>#uvqd7e?z}9(qդՏ'\zy .nQHmkA\ONKT#WwP#/0RAoB*<#?v#yyo%Bݥ,$Ū>2ϻo.o^- ltk Ĥ. Oī]9&ndM'w[SrU!W'߁)}_T>x;~:$mɠ]_6ջ;SuwPN}|f}FU򽎐=º/˻1JLg Mff/5eGEA00i=OȀ${O>խ#>gm}> +87UlɷL cůQbbro 7n|ø^߾Wȗ1.&r]қs nJϨ }~.G@=9\9A6s ńTpNepMn/,Xi~,D0k;Mx2>%VoHۓc?Djڏ$5]W{]u1W6">\Loڹ;\Jx/F"Xp.nf𜽱=?t8C+?]`9?:D_3 a*&IJx᭑On"Zn" /S4zZ_Z9mG}op]#uV{Us!gܷSϣYs..qcz1vwc.0]5 z/8kmϼ;ac ' 0 ϧksI`q ~``KGcˠYeú6.EGOtN6cjF}|`s<+ǽhZϛ2G/_aҜ0ق1Ms ͐Λs048㍠44ey G#'Ҫ{1 %r)h_,L>H[;^x0?p:hgnpF +?(C~#ޖ YLRĆhMd*$4)dN+4TqAZZHZn MLxfXʔЖg*5`!f-}eiu3d-K`H +)MYZL !ذ̡q(K}BrKuEi,V)4`RyeRVHƊh^ Az޹cU mGCIZW h]>ΡMmJX;#UjQ U𕊢"p]]t:,TejZcɴ*Z|Zc 0M 04ײL4UL=)x捂zG(TD+LYQ. gI\90e:" 3 u LҬHd#D5PtHPxk?rї9ɢLC:ndQ&  ]qBnqn=?e^=eZ9hņ"Z^LcMQ0O~  p*p.y+H$۫٫~*omوzb+,]1 c ֧ Z=k"CoZD0Q:1\.h`SHhuʲ !(-0fA\}76h1  .h1 ؉1h1 i Zs0z0, Z`̂, Z`̂3?TMy#:QV[<.ߡ?+,xfP%ҕ }T^(p?ZsΧ t<95oeʄg>med|lʄy<\A,\&2Jo,Zk4M (iRŕ}E_g!nHƞƝ-x|: 4^,2v[dϑS$Ƀ Vdl}wY<ř(c>3Dc︄[FWk/??Kp (A?m?љCg7tR^~q us[r 1M̻rƈ u3wnv], Lߎd,}BrHEg%X t`j r{ !6g`&.z ˊK5<7^ Z8ۇn:Vk\I6_]'Im$^tLEgUN] 謂` |?c*0@cj.]nO-n},ig*OENcӮA K:nSCxn5C1 |I]Y.!鮟*$0rN3Nfǂ( I_tXeC  >h<1ă#_ubטCec+#}R[ l"ׄ2r<Y EijuDm](Qk6)אj[XYUV@5LM-)\ ( B)L.u a6 &uqA;ew$3U$R& _$ePk#S'_?(6##5gvEt D~ܗxBķ1]QxQ"F,GZemmJ̶VdRZN+g,XVJ+1 ieMH牐挔J#@8Z`Cr)U :6۫ST$1.c LI$2k!geڦ-tP@2;e [FT3Uy+%g{2f{:f{Bf+S+ۓ+#z=%z<`$M `v7?pԐ}ӧ 6MI=ow15pPrXo}"ۗۨ˿LcINymγ|4UΧp5 g'G^h)6[,.;)+sۃ <ڸۻj~$ζ|Wk`I>,L\Z_"p?05z ^a{N8[9MA0xG=&'C }+;P'jW$F\г$h1"b#E؃Om>ɩ‘ٷoNz}qjh'Y_QXR }Urk"| {vs=>僈(g`p H/@EZr'&J}w}FH.v* qy |O (PEhց_>-oǥR/@eziG7AȊIwD f?Og9=aaeD}NutѸ_6^lܭ{lCڇb@G'rՅEv!hp̆x2Hoa q'G}Y;Z^)s}C2wnX̜}!ޟb*b<`2 q0 ^$ t@ĉ8.69^De0;C}רt"`£w;ò|>ןE(R#qǃ?\L0 x̨9vcw|M6X';FAhn 8fI@:{ǀd&:$QǨR@Ah4Z~V~H ͉ Uh>@st@[`:[KWWt5k >bT(uvp硵֡sG ;]@(烻Lyv9x.Gx8l>z<@îj5캞жKX89|ö\m'dr{y0_N^n𤻘_l\Z8q8;p/;Ŗqo~3wymL_nLj0ۑ3sa<P*xlH| }bAr'@l惽;OtZ>3,}!q)R|yp~MX|6?fҏyᩅ?;,vղri(L/1twՄ%'y2B)<f{ps6,>ב섐Am0CF$Ώ!eV0 % n`i6'7q荙o\c&٣"u Z5F=90`rY} Ql cgϟsLcd&݇DCaDDJQA ¶Ɔ}[6DL2#v@uI 2E1M Lc'SRi!W, 2!Y&mr!Cb|=yC*}y^hlf xvPP`*w/ d$IR徦ϝhX@S")> EKkv1H؉F?dT4uЭRIEpe 5[pkG+|P<1#o*d%`vO<1&0?.g$A1 ߿tXsgmP:t4Jrw&U^]Uf,@UI6Z[D\{:PkMDNu)VJx'Q# "SYZW5\DFW*S\zN4׵FI/71J(Ìpڀ۪f|Gͦ?/B\X۽}ƌ=;=^. |pA "Vb\qΘ>cꗑg|^p pT )t<3Ex<, 2$Vh9`Tji han>}j-$VVB67τ ۭyǍdcQj8`1,{*$%R0k*ƾ$ 'Gh/ *~/?d/w|ת"sazNË/0TYI'2ժ (EMTjT^i*nORo k547YB vFZy Po HunJm嶀J[@--`[RFiKeS3dM멧 1Z`^TjmJ-Pn k ؖ2J[(m)ZD1*%m´wնZ[@%v5.|Pn k o ؖ2J[(m)Vx^0p ̰&L}Pm 8h [@-`[<~[QRFiKuBm^^ -k\Pn 5.|-eQRa 3N-8h [@--eQRFУd?z}]$*RWNXF =Q.]R7A*FCZj"dE']'vu"qoޕdDFvF'k;(R=kVx9Q &eɊY|F4v'4:~v=";vc ;3L^B~|G")r)eJ#;RD Ei5@Rfq`Gd٩1'P HU?zTQB;Q=SQ홊V]쭊 '*&ޘ*` aHl)|F`$f&<Ows{ b_)p|r8i0rj1Eo,pTK(+%dKgHR1HQCGku@?Qa Ay\e|4KdQe_2pڗ6Ȕk(ޜn.Oe£ ?DUͫ_2#t❢"₪)z^RJC4ԡ[]Y{fFM|7F vHOMscʑ'S"Yg2 CkxF hhP\D~D̘dBƶ]TO )jxC0r]Adx>-6,Yt";N$I9ZaF ,s:B%3,2G^hI3d(skY7釞ITFdٰmlS{#"-|ЍsexIؾmmlqvP$g Y{l3Ëdžc;H0rY2e2ΦkFQ #_rb241b;p)cl;l3v8fI8slI;BˤkZpYKN|*na&ظmy1 Y8аz"^]ɲoRIC-MGhq>eYa#j xAS_%ǣ#pwx!Zh2苡tUvv8:JEg8e,TWҠsAy`>9x B#(}^J/?ŊswJ["M*#7HP%QO}zWKu 1A/ _Y 7!s 9.WȊ.>>@|xE0otԞ|q]ZD:{JY' QK׹5.E6w:Ge#ֽe2)߲IE?]3.W1||9VOSsyξmya;phz?WjjWY?Ny+OX8bH Ƀ UzRD>U0}mS>:~~+Nտi`r׋bIF7X)*ܯky+ZȻ4QE}ADtX-萇6j~0RQ_dQfn5>kN*|˶Ed~5Nχ_~7De<7o`"8 @d $."~r8SN#!NWN}[J\~Hx)pUȰsha+8p" dUCLxd}H+x jLԲN>"lcw gr-#>fPHր P^msG5Q| /O㮴);)VǫމteZL հ"TC SN\h55H/!wϏ鶶H503O )J0X|5QShX3.i%}= Ny A?1h- (-uv5\A.2Be&<%տ4v|h+BWے3q <5+~Sӗ~wp:G4QQe& MTmmzK@Pj ؖ2[i4i8o>ŇuyK׮_8~2Xenr"+l|*єB{'.q%q#Bz?.y_~o6q׋Lƥxq?vWXuN7h@PBRWܞ*ek役tQݢwK1l*f/F3~Jz&=d9>r=??^Qxa\}J?qi 6fK+{jtIxalF?1tbtIݗh|Pd3& ٯ;9V{?f>1LV lw~}E$Ym\MIRO*eˊ/{&mJ9\-h4/SXceeRʯ?{w77YNԜj,}{VgZ@^u5U9ZO4Ң[u]cD9 :kw]/J5:84?U2$L~'v O_]ƁZ%şw &\Ǫ<Qg>]ɀ/2lw>|M g22

*b#t% R9X0yB*(:I9B2fVOc͎%qm9t 瓉{Ա ٮi=#s' iB{ 'h i^`HF702$GD ǁM,4fI|Tgvh{$IԙF8$Y`CeCJԏyYgNYcx~ Y\}Ll~K 8ః]vMPv!.nP{ |ŧM[s[a ?=2Ȓ4AqMo HHrG$ĬOԇ3mJ5]jM'uCRUI*?!!h7GvMw+2-cd|30VA5G&_-7 Rcz,`̛c;][`?l^E4C`N"8`jSɋCUx0) o a ﰬ.I 9%/V3A kzV%+q>Yv+ƘcCw }ir#wk-/+JT7Xi!`^tȑJnzX1p^!)I_`*+Ѝ'ePEfȯk*Dk1JMEK8`%+no]SHf|Ym+f%VdO(Xaٱpwp{fՊKq|1'߮ͪ,uk\ ȮkVeՇɠC/GCyf8,O/G]BVK[Kh+f \ׯ,:vW"nYq #l7է+{Z"F겋p(wqh.^?gr¢yW(Z}6}̖iL}ʭV.Cwܱт 37-ȢC"C 4 W)θt<  4漯;Ʒ켯;F%[|V}qW|iY /c=k󸱭4E^g}|To(|^ZcW7䇂+@)}z 7H>ubMun]SaR Rtbinh WAn"Ћ*adi7 KW o7  @aLk!w4P*:Ȓ^LNU`F @U0!$U@~AT B\ulJ*W88t%,S JWA*W4U0'`J*WAB@ JUO 6$ T9\ 1 D6ԟpWADZzV]U*~vYEivY#~(DE>#} v$0FvI#_ۅ}+`ĄG,y+{z mbx+0YI~*)>˵\]Nb U)IWj2ЇA)8W_0߶,װḊgpVk`CO⋐y69RaC3_ J ?ly5l"}A.;zAS ##EWZ]V.wlE11c8 K4E"MURK޿xhAJxUuCi[h vPa?T`G{Պ/Ngp#(i?nl:s-9 4PBnہ&z:f7Tg"83dRu22 ^ |_K4ɃP Pc05i`A 0d^T[\]pDԞcX~Bz &we3P){M[*)?U BY?!r׼e _ UI+ QvZLrR)OJ_Zy| doqSoPx-;.ᢖu\/_P,'Fx ;{bB_L5p1FL`ȃ03GI@ӵztt6.vl)1L]_jv+hh] Cd"FZQwi٨/`0_-z 'YO.aSuW+w)1Azz_;eQ_+*2͕ևb9yxaA. ?M}K0bqj3ՓhGvUʛ^9lWF`&/վS8(Od4hcdhUYu( aHԲ]V41kb8896_Wv fp^+àCfb}`oD{]G=шeŌҞ`4 %f 剨C%YLEe9gd(67#o{r h%7&ʷux-G}>aR{aۄgM0!ldW&AKE}9m~p 3!eZDACA8j#Va=X6 oT @|jiz)KC'K=ɒjjWDϛHC3+u#E[v5ξTW_af-n>`YC&{aixj 2` .I)Pr[/6+'6BwN(H_[|g ֊sIv5.iڨԺ" [2pؼu0)eLYP^z`D0^qWWư^qkp)`-cmMĺ /KBd@YV|1xlAom(#:#6h.& r={nC7o5RZ)ni "巷(r$aɄ;Kz^=dyfM5y(0^"^mmf3ažP0:'vՊWbXxI\hCw5 φԑgm+c~ۼsyt۔3TnŰH04b/4R;AqioFHd-1]hW . s&k†sL+Ǟ$jxc Ϋ3B6,B>~c-l͏qWV#n tH5Pept^s[6`Cd3kjT{->cViS#5ТK O&)Ѫfٯ?_{˗涸^a‹;Z-wlȡmawwZ!A_fbȆ4OՁrY3C!36$uA>vܾ.Ng}-Sz1\P4 i~4 =1ʽƴel\R Z;썆T+A֥wPKud"%d&0fв|3X./#/'.+h# d߈A7,k64MM\_U>Q7<z:ݡvtǓn%[aog#HR*|幔X`{q"ID({n0N= }nQW'/+k2Bmv? #o jB#B^G`NbOSn3uA rpՎdWOXw|rgjmؘܜj U&Ųz; ?1'"]iDWt\Dz{PJcCR\|<^\s5Kԏ˚7cTځL vL_ওUnMk?ʷU9ߚZѮR_Z#*9xc|LzoOBId>RG:ʲ(kS2GorG9e|e#o#( o`ԑ'Gʪܑ'¸ݑg_kyŨakYe:Vk#+ St~MmFuo8WL  &-b)*$K~u$gFdYVŪ8A hOw%tKY H.+'sT\r(2e74}0yI]+*[X2e!4K\dll_2x攗ih]7sY=\CR5qxS1y;l+A)eD+VpMqLFr#@x\UsƍLJ*TGv87bhtsւ*ǘi*m)&PTM++vS"ԑP܇&WfWFccw`ir\BZ.5?ewF."CeYvQ %4 R+c<詆y@s)P% qu;EYh [)dAphDZI#l1H!@P t  C+)d2J(JJ;Ƃj +-| %L)h0y (X=iƔW iì*C3, VB8ԪuymK`"n0}8j/d.zI󴁺N/>.&2Ѐ S._K1l .!%6I~?,]A:Gjm av0/="%APz}E|سľ퓛s폟qQ߫eᤣ\c`cFt]%Τѽ6ێ(^g7ud=ӓOlq0'=!w@=: Nt!M3)xpe_yz2}nBk؆KIU8hc NJ@h5`TM4= w REKo[ڙz33yn2@;S/(K֙z o xv^b`*D+olIm0PJ D:Lt^XzlGZ&MԊ+h,t;Rc9[={@45b; X#:C3 W\|>99U#1= q;Q -BB] vGJ,~.kc _0߉kdGq m:;v>ԯr8慸 ^= `G@n­lL30GPUL =#*<_-OArwNeCZgc2]F@eFYV>FtңCeӈ@暠F>(a~  )aWڹ.$#k$@KAe.;eyxb4/5Y|ֶ,aqQ(] Oti3ړ hFu pT8yeOAl|sgnNmLf3z?$|PEHn "I}~5_Ϸ2N?`^zW^~<9#WvaHLOad/?4W;QѯVܗsaJ"9.VpP!\أ秗ӭINjΥ=~Qu#y|_˳ob?_~zp(Ћa>u!Ar:\1} ̩R?VGT9Lz8c {9$qRtwnߡ_<\2ɓÓᐛ<%t`6W޼ ̛_n€pgyo&T1+ryLZڮ}s~\_?o3EP|1ce( ͎*}t\3gv c d=)J4cp1Iw>;?R*Y_Uې܂ N̹ ~'bDYWnck0,Ylwl^tK *YoFVXuh je[S+Dg@3E/ULV|7[_xwSP(J!h-IHx/!O>ܝ_^Axwyq, Cװ] +̯Q Gxc]\f~`ɒ|<]uHNsN|ޜur:&bn/xpT~"t;xnSƸUx?GdK[cesЙ ZkZFBpwvF=79%dsyK\b9߹<.<ޥOa g hX a>/H<3^}/L[<]\^V2FZ^pc-c!Ȗq\FlfKr.m,i^.~FS/糱~K>94BKU.ZO#jƁtv3>D$5ҁlɛ՛b=fi:el*RRJ5ǥkI~H|e 'JR_\m,buv>'Bx%W&WL "O`+X ]xNЪ` hwmcmո-& l dh\ۼaY:T57Sr s1naecZEKrUh'n=+ux7m2oڸl)3X8C" ݵ5tۿҏI]` %%VYJ>ϯ?{7! %ʩLMŶ@ ^z=rG׏f'`uőˢā_)<23E48a梌U9͈Ƞꤾ+ bz- Iqa{p`Fs۴(#n @3̩ E9!qrq]4i$son;(dY@M?pkV5eyrxH0eiWsm䙛' (#Cr61"0x)5E Qiƹ s&0raɉ(p>sS\4/yyL(M/#Nv|/-(wcu(`&BoqB@̙9R18E@;Xc$B9Lq~ie(N(̳8{IlK0C"GJsYN~LUm:j:z%IqFaibz*}~~-W7\1Gc kiiMlqWr?Mu3*x4XȚTV X2VK%+Ue{ŵ#"y]C#j272'C[${9|ksȯSKh(<-:%_tTtklָw hHv:EI>t\_,ЭbC2+^ɮճQcJVahXV[Оݑ\5exp|"g\JxXgdrC}<M'xb 'xdL4urAݮv=7zPgLݝ vÎ$ߔ CoZ @2UfBaĬ;˶C}H?ZLߓfH4fG( '8\P{ｊ)s*ZSW4'6~ v=(ܪXT4,A%% _B;d<zp ^g z>  |a \]~x48r>պ^pwX?7*IeUŕ(7eܓiӉ"DX:Q{F˼yhxxtY]bYKJ`Y3,*mx$c"Rd^"Pӊg|;S cyپCcLoR]\_d+Ss5ݽrwx~٣랈b>W3E,{8 n_DD}*by_,v;TqT$f4L'Օ[=g +Mh\|.x:CiӗW˹J :l3W46:pg<'r4BH>+M(l*4\;frQF|^j9)gzsGM 2|.b+ڊ ;ɮ={ ՚VZ}My2"D (ُRO1i\S׉K'~G9uԱGe9 =jg9L7ro00N0-g3aZe8%A |3^c@$< n7"2S/=z}/z}vȭȇA綈4 _8@ nfYNf45O,0Lmr?NTd$ ~r?;Dpĵ94lFvq&'b Q۳i3\V3߆ӗa8X"q ,d8o羟b(.q8-&i ڠX/3Od_@}A7CDoEh'CC F^$`0 /rȐR;`X`kᦄ"2aЇ4sCF*o8#9.W>sX2Glf Ʉo5{dNbcO6[Hm^o嶟Y#l#L؋]&N3My4+:"T$2 :,sXf#Y U^7^V]'̣4/1puMP:qpAB3YHy$Gs #8e@  a0#`3uf-wCn"9ˢ+`H1ͅkgú@qcIcZX܎Yw`,uaq#@ txcT?73Cl{Gl-8VW%Oo:h#M9P\ `IYϸ$tPb۞/r//Q;v282ƸSt]Ga?Va5ѝWic1;2]~²:voͪl_dv!/m?Vif2LٽoKQsU[ǃ\_zpڹ4DUo20j뱩ij2`ζ=&ɶ$%y+pĔA79{ Ȩ1X-嫯v;FeF7nbX>yU̩^lL3_vLl=\--`W'syfXQnq=B/ޕz]PCUE T4AeY.?@%#-EeS^h$9)ЬoFj\tޔ:LN s/nkgwԣk~~q.>3$ڟ Az8W2cK_˷mZvr|^@[JCeN !,,êUr}|xVe( ߔ[t#V(h,2}'Af~ S8 ]l P|- 5*0)7hWVJVr_I"p+ nr#E'ӭö~}jԐUs?=ft̏;SGi:L*Uw`&܀,z U(]y.ޡ6Qgy ~6C$P]Fi#/fЧ2[o{g׷8Z!{_genhl4A3^q玃ϲ~OxiĒIv-(¿+RպJ]av (v?˅M{)^LfJnֿV$9MU!ߥdr4hH1-Rǘ:9=2jfc&aklK` ~DCꑌN3&1,"bǴ_i p UB&,OڀS9aeIĐ8fYI-i Ip DŽ(l8֬23nA6c$AyEyj |yNj!EcsG!s̲ib̧B3rYl>NC7X~(˹ϩp,OLʰfpq*b? 0:(XN Ƹ[nj⫢H2=f`e( #Ys~}}=J,vxx]Aru0LŃ3 pN\m0(F Qgxc~JPcmbToj.+t6ڃF@mI> }'jvXz8˻/E,$,ځՁn# 0]r v:&&W'l#o\O*GSxn|Y`^y^W[Vab LQ~@dg}K\1\ȳ3mvMFO[ߠ۝/d&A.[}v[ =]Cuf.] U/+XkL=CyzXW3X_\} ,[6_@-FN!3x0Ԧlj~HER~ U*#e|ԓ,Oeju / LiÇ j ü1Nx= [RV UI`ޮu69ص1GpH oiWffQymVn~i:M6cSe}$~$H{nڿԩTt!-7$)Bg[>:hq6ژ]U;b4dA33ORy;-,Gr݉ڽt+;ÖP-䩀}V!r9UG&qMxut][s:+|F)&R̛4oV2r,,+s~v@2mV [ -.N2= =Ƈf]K!3AHM.{~߱ޭ6M%q yz`QɛAw,̞^xĩDބP‰Bֆ^ ɤ5+@8/6g -|oppPӏ%-1fe_|`|lb h[Yѯ5e"0Yxx~nҜbMlwx|jSݬ48ROoy3W;^ װGℚ>2l60E&\ p/-rN epH]ݑvrSoWi{}7_ kq]r97;C$^qض˃Xe~^n1ǯ|>H<f{Fk Zw &ZMXmoZq ͑ } #Iޥ8/ОXtZxbm \6x2 ٔ_F(S8{^H_ɗ?tcm?4qy{f+܂Ǹ\,"ǸDƱe|ЁA" -LG.%LzyŎ>!-;vB]?/91U0㓆őAv僘I\nZ,=hv+,V?[Pi|\ފ)I s5oh4 xL7ha0 &㨆G;'Fm=9 yo ۑrs{Sc a0q1B-Oo F6Md oܓMZ?8F3op?c ^?C/J.C=\W|" |?`,[ Qq [r|WJ|ꦕ!~~{ 7@ =uG}>uBTROM>5-x)'߇_&fꁔ`Ⱦ\FNwLOod>';7s;;K `~x#hp׷c+kc=@6]aL~SZ͂q(0b>`zStg=ԚD'V'$,Vk-юh u2i\V2a/4L/96>7RJǮщS"EHoLk\Sg1ecwlYc<ƙ؂W KÑOV"`pyh7쵓^޷T^gy{Խ0\=P?<݉31,1 >Bګ-&'Fe>"rU"r_6nD C3iOSzUDS&p-ީ]Wt]a2ȈÓ&]ipf 0K/mL9'-odCo#-?5jp3D^M=q~M_\G&CpwG i:ޔOhx4w؄s)t|_}C- _{7ߣwNWAm. lRB6 EdݮPFAϟ~("?K_p*nm۾t;fٮ~7 g8~q/oY; ᩝlW;YnE0ZI@ B1ROYsHY^N-$vhiP߲ xT>YE=pvd:kk4 m2aqLjZ5[DVU6Utjj(j(j(j(j(j(j(j(XjkR&^KMx-5ZjՔVCVCVC~f'jt T+3`s`a,T>ʷ8*|`u2$'_S c= ܞ:}%ғÊ?Zr-%gw\'/h|Qai0B-U)_0]kLn6p>gLmsbHk\*?[4U(t8!gZ>712?waܛ8ѽiO <$, (P( [R0/- qfe[]{jN{2Fʄz*}6y-lJSL"nM^u;~Iu!]n/TXɹO*ӶW[)쳢~IM4' }S>):*8s֙ZSiWOKܨey>ͳpZNsҫóvyR1nߩ=&cR-2L%p҄<+\g:U %.:uZ }YJSVb gM2 ݾ8YuC~*𒮻c}u:/:tb(Z^ctc"+0fӚ@*tDnjKY<@SK4|\G.^IJYKI ᫻T'Bg g+e$a.y }u4*-TQQM8]VaA1EƢDhi:̳CE5&.s@,jFfX0u9)P-" ׼"i2X "deT(^WiΒy!IeuNi5XPO OB#RT1b?p:Xhe*N(3mAAJâ *8H*q.+T0I+B3TY]da⑕5\Qeu&2L\CueP+$EGYy2^+:-"e^*j!/Y"X$a52f+1GVЬrV%)#/˲S?BX$eDpe@0QGS(pyKh d0b'F╠>kY6@E(#-ʋ &7a~p qƒf1&n؏*AU,C@?𴜅lW,"1 `EL ӲKNAڜx^2Bi yy~`ṽgl!ρ>bp%͊sZ$K 0P݌E%oòPMy5QrjikX`X"y1UvY倽_U95$}* vR,0f^Ur)S!i1gA `vrM/NLK H4 ,{L,'u2𿒀 tT :l ,^@ 6_zm.VןcKujN6_>.i]{lN]yX YX> |a"u9(v 'eb{+/!0.NZ WX/FIq0 ۇ_Ũi>'UXlDO=v!>6؅L<;&7b*/ZX-VfBڼ(ɇQϝY K̓>㚬G4/X>m>c%ǎI.}׻{w+\kӍXَhtR_ñG㱶zMhk[ %{oi%]]W?_'+o ؉a#sv؄el29VEXޑ*ez:+JFՌ c#b m3 F]e&뎱 8c)y9`9ooGs5^w-W-W?0WUk'wHgj`LU\ 4j<˺o?^s@;ՐFxnʺ00vR9|e)LUjGչR9=\܌q6r5EmWV2Z<ܗT*]M^јf~ZbP(먑L\2go_owB967G !H@z!ATQ@R @b+h Ve!cqsn@g5 }@c'fsh@#*J @$/(ktRH@),:V(Ǵ@EJ*xL;!k4FQ( 1 ܅ťeR((J7 \pRM 9F))(0RZV R`k&0 \DVkb =R1 FQ@h Ps1&$FO+ '@J hHIQ`'VҪ(d5Q`ggVҪliF`R(0ZQZקo{ RW O+z# 'Q`|zz3AoHoc8kC+ygFgO=PۃoXow ,;|tw7ОrOwRny"~xXzEгG7} 6BG?뛽:*"? WmW-'85RԿuquŧPQ62md8ql#FƱc62mdȸqm#@3]!zVu*^0}<@h};m)8# pO%;Jt9=)prz'Zs\q^8UϾ2SCoxkJemTk h[ED[EѨ<<=<՚۩x:ږ/}Gt-WJ6[]O&MK1eHDc}9pY7'cߺZCr;[Gl"ENk)s*Epq;LGç-流6HbHQu՘L8',*W)xz`V̢V xex}Ukw> {uZ!FI7QfV1fe2k7/-CieznUIQYT9GeBP΢.=x ->ώ!n$>Q< cݏኰ+)꼎,SB[LIe-=%Zߓ$ =t0Ro*= MU'.f) !u@q¢)',o6DtӺ$}O!)&D5QJ(gq'i@{o (JiCNc43&.= /m< YE0ϲatVBguYBE)O=9h}OM22^')دQG%(uvjHI݃ Bñ*@{*9(uOyZ$Pb!R̚9iAꞼI]I0Jo,Ca3a[o칻GEܽBK~`\?c(1\PS ,xo^??}onnH寗 x %˞z]%%Zf3L ;ǗoT%7Zg :v Pt9 vd^r=$ @Ƚ$6& UJ4Q?ᠺUZ23UUN|۫|[4~X^_iE% ?ޗŎ+q]M2jqx`H|xU~@y_uyƌ?ÀP9A{hL#V$ Gm@;a$ KC,&Z6폆}cdx+Y@&ǜ0A} 6׼ɬ9˿-T Pqpم[ ɿEa\q8 ܣm%}8ط@yN6XFͷEIȾfX#UTij L*j0ޖ0mA`2 5 0)KH k@6 百( 4LR0 y ʍA0% Pv?v*o0 jo k|j&zQa 2ƈdU+ [/ Eb?EejkT66?%k!H["?h(Wjl~aAe6?_9T5=W+ZzK'_FxqL H?չtd=ƒyT/~V/bE%˕?  C+_3l?5&"Zf־JB񿜇 Sc: ]8CA?\@V{C(>/kJP/*[Po@GmQod_%{P*PICY>ՓA?wP  cx5m!1(n)"~\*.~w=.wҺo^?~q?ɣ_~& X֛4z7֨nq+i5 Dzi]^n-o7_8X=oZ]^on6SJذ{[TaSg#}Zsz]fE??=]""{;LMW8?,7śO׏].d%lyr[ LlW;]‹ ein}"j $oK PlB7'r?Mɢ.R8.3>z"qLދ^p8NpJ}![t"WWwl~ //vJ> v[[]-],SNXks{գȓ9-1e\FhMS!ikL18o$Mw#Sui_.4zib]g4WYk`A$*N4xdGeiH@i&kGvyVފe`vc)>Vc FϚ10|]msȲ+SSRwq+©ݪ Z] >=ox9{N*Cf43==/ŏQ(~ RX@? QHJc>H~,zQXH?ŏDcYcW.ɏeDc 1J?%? e-,Uqx` eO<4-=V]E}b]{/ڿJ? cay*>CA[և*hz }v|(KNjWA ٕb)1&Ւh Rg!>,_n<-]va@biGxѭm[ΝUeaPz-*+SDYjd{MTW}juCWxͲk1Zӕ~_Ħb- /y?ӵ~iNm~w+zW1ǖֿa[`|j^ѿ#+:/*,v|w=%LqmK0j,{duqS[u[rZ˅5Vu֩{ؓ- wbUqwRtBj&s`.b\-l(\Bq ^y-~E)DEB@pVI>?p2ː"7)ԿYIWs?URwNZȉq[80Y?e?#ɖ%ه$HAt 'yNuu[FFT x8ק!pہ2PcX*sꐷՠ8&HžO0@ƒQ _G]NV jV +Ϛ#NUA8VqjD.~Β, #=O;s0kT=z5sxLM-ro'#qlPѠQ yɡ'3luK9=T 쭡yFUyz™&sskN$ucy({izCFeINx8.̍/o9-\/3r?%5 +j yl9%fks ~}4^Vܵ &{q_çu۰jA3p^>maصIQ}V|.7Fc/cfwr-oߠQT 6~"leG4V G|}#73XH.  ratj(Ghe0A]8wo1|]ʗ9xk<2yM=ڋ]&lϿG WoasfT$Ѽp~ a2O8o&?\73?~t VҀ1qB8E \RV;&<\ٓ]؈IuE{ h[M.]wa\&wzh*߇s̕KRJb13h%5P%s_v#\Pz+ȓ$d/ oK;)}~:88v=v8f񼏠Lb6l6|! ( 8c؇d'aD؈$P\D( &qI2Mc%`G4/l.px>'*ҏф,^.)8h0,Ґ"v ?d3Bx""C:EsmPbE,`yY0)@~"44ͅxibDŽ, 'a:N$%0̠pC"1hN$f K *L d4 3"1?&@qL$f ѦA Db)V`Rk0)RzL01ݴ[YK ;njH\|{v~0A؁`엏eݓ7r`qU>@;;,ܖ.2 \?_1ptjӵ\C^OwUOvWl[k$?H{q.5ZI<!( x5f&pA=IۖaAs_1#5e3o6mFv 7YVņ)hAki~جW I:0*&b$IuAiJP1YTEΠטQl@ɄyI9@Vr%_ àWy z-Ìl%9dz:gv|^״Laۖw/{S:ə^UY*XVhH+Vg2z;”ΌUy["#*rk@cuݵ;f2=o.Gtt<DܡEr:xݱQF:A Fe`l8' M5Fan^5su`ل\Gi'bv릛1ݰZ>5p8ז,nfQ]㊮w 0 tHlllۘ;vy3eFEɌ@̕WM:"Z~%Jl{|4!^ŦlweЃu>YuA>0#*\~yŪ*di=|bͯWtn$}ڭOtR=C[5N Xhzeu8a /E4ݦ l3[g!1:!3Oy22E_[\`c1\A "1Nj \nX f(TE94jn7\/˫smt`hTr$#h:IL?MBjnFy=ϳ֯ogqby]#|[%Sot""[g;n{\df[jw|d]}P}D:3X|pk–r khxuO% V Ʊ xve0Ue !QI<k^x:IG=$L$!mq >3FAQ1o)|2e58I6/e7F`1M0gˁ=Ժ!A b6=b5$ݤr+`~he^y._TQ> ]L80f {2fCݶf@?px~˗/WJ8-qz:^OwwO?N㴙gJ]5dfbin`DH;t)357VmteZ]e*AeޓӤ9l[BYsR 601}_F?F /AF̉uK7&]Wz =)j\BL"$t1fD{9"Q\HSGg #8Ӷ4-\uFF#!M:JK?|ʰ'T,g!`) $C8"i0b*eIJ7gJQ /(Nn׽Wy@.7*hƒ ^f)۝}Ðk3f,gi/m6whhgi&qfig[H4EB[7>m>ۮFlW|M3Z5b{6%ݿrdڧ K) I,y%;ϯ ]Ɋ335[3]afڧڧ媾m,OS'\by>[WfylSmȯf+fݶclU+ #;$  b}tYB.=w㸦>@>k699,SHW"* ~- #, X,#i:.i4Ky%((,$$$$ V\2H(`$L`P]\I2/`P`X2H2GF FB#d 1Cu3% 83& ER#ddd (#d^Eu#K&)%Ē Ƒa F FR#`P= FR=1g E`d3 &K&9GuR2/`$L0I1 `HCu#-ZH ;\ 05>_)[Jq53[iQ,݁:F%/ys ,yDDŊLnZ]inTl=t`e`!o=I`קna](`jQGbo6pjAvA٫]3-X;;gJN,ֺeT֞cʦ{qr9K FQQ]!BWZ⫇wFV:n#kE嫆 P< 7ԮVX~d4'bT ',ƹVBy¢~(;Ͽ&d|[o5X mFj<>~Lu Ed0Oq,e$MAdAV^y`ʄeVy܄UM& X*>.,K7 Ç:4|xiX? 0~ph -iK0nAm:}kKmo lQ`9Ȣ0; ^P1Յ@3k@;d-Ҷsb"/ntnd>}0ϲє}2tLH>>cnJ!rϻ}&3= G3HrW O,gKϐ Dۧ@lxS}f3nggCiD}n}Wnق̋@ys~)Zn>S\e'` rhfph^SG63usFufN$ӏ`O;TbvU Wכ-Ef[k|;$?EW=z5r94 apNÅ1t,ɯ|/YTwܗ(8==P:qyU?$=6[Ge$5dSiCA>ۡCU*+㦾yTT:VWE7uҜx{".}XeiXA XL+e94ZdFVma$W'@|Bw==uѳmw]0-^imZ56A=.' #s`ht BVAX?|kw4 wNG.n] b"]CkԒf_V}e 8U3ﻩw{Vk nhň-o7}'#:a] ,5E0/ Y?TK``Fl?ѵua^.yV٤\"H}]:Q=!LMX`j5N#{n|\Ղϧ#oѺc 5=NhPض}0!{]ք鲰$ؘ7VX֫Ւdo.'0O;+cYT@N% mr!VnxF8\B}к٭/5Zg-+䡂%PlhZXn,?זm-[OE^&7/Zq䴂qZ6.l!G%D2wlIEf+{Y}VzM^~>_wo~B)}Zl.+Xl6۟澦q%^HQ^.Qm?VwzN|}.U ҭ|Ўވs2O5`l˴ML(T%e_?F g}F5t֌l6?W] AoS v 31bi3,`}.loaZq~Uvz4z_=T@hѭ}/ b oV 7Ջ -*o}XQ.= :)Z@ 6yLg(GMO"vG!巶F`hF^x^e?,- >h]$^^N18m%o & *.~@O(=(hc۠AZ8yQ n7eQ[| AR7WpQ]^B;lP L-_ |V/{DIxEc N^a=8cn0gV@WL4@ +BF1.3`y5_|&Ő`w1Ex&L*i-qv5XM%+;-P`֘׷z+4X#]-L/±|L*x6}bm |ڿ9y!<[F˫4/37ıø[4u?xP,g!sQwGiZ(l/;Hi1֑-SPŕ9_]L}tʼnQX2t~P,8DA1@"%-x@ p2-/Ɉr v DȞiA>((^1Uf+R$@1F KEڷHJx- j̒][lα1bd-#QLQ 0Ҿl 3PǷF]۬ئ?k <ǵF0vN'yr/838Pqp/8`MϼB҄ ^ uM{TS/8 G)yyd½$-Y^p0{K'#'!L ɸ@^pRR5 {IM@O^p^pRD"H' Σ { KO^patb|l>̶pax4 4-g,M pLs[+0N;:۷516[|Mm3 jKacjٻm%W1!J@% M ~mYcr=~HYI6wwT$k@@}4ry_7kWxc.P*6ä/H!'gՀwfc$0z|wL,4DZXoy-t3_<=v&ZX1&bu;b_/p>sKșR: PНgzWwJt6DM~DroIN[jI~/d;pEv{/2zf*B/+H/RT/wpz%ށOfc'>,WX&;1[􅵥WcƼ>QVCX}1X@u ,mQz||+׺6K3`^6d![:Gj0u]Q]}t#aQ}&+LEgɭea~iv]vdͷF䇵,#g4l;<+_|#Ur ?,E=lcVq3ɏ <uj4e㱎C*W~"%Sq~@_.V6 '7WQG_|lL{{s쮸Ot^@l?6]ؖƵe7̲^Cm*1650O6t0Q%CDddhZzE ;9gdr9ˤ-z!V!l?b*rB!.tҒ<Eul.3k{T!Yޜu:nɮTYLHS[ MT?FKvwJ&2=&~ed&ׅ.-zQ4F/Pr`q xs4*wP=|+iǛE=[%ߤ^ A?XBT$]n;cP2n.~̈́y`-'^o$E=z5WǤ0>{)ao7@*Iѿ c ߢs3{A^%,.0pS 8G123Iaoxqxlj馐}M;*a~۶xpF̅ /PhG1e~=WppiA҂7 NF1ߞ?h\bvL ~;+= ?l;Fg{1fch3?H!>s!|qwNgH`Olcc-?ށW~1}lhmZv)\?{൑,Ao~dAyg _8#TQƋsK#2PoS}rePB{ߡ[ ZS_YɖsZs!'*%tkn5z_ o}kim:^da&?]3HmǛ{BD0@<`:=R\%U,ӧ!Gk Ln?!d\?v.LzBH>mATD}l%]c7Nw#N֌(.[c ҃? DIDuolSKh Ү{43*Dp4RڹH7x G5 )Kp4 ?ZW"%$ uv&Q ro]%2PF)F;WbYj UL6/|S)\&f,y#{M;lVם& J)a34p疉`vR07-B2lF W$0H9faء1Dy駾[x؜IP4$cqB#&iPFS7J񼰄&d :CT`@0LxBSE_)<x4:!+(eͧjT(p"(P b3fY%>gL&0µ f;pXM$Yk8syT«>ˑsZ8! r5<,6vfit2N&7`h.5d~A'~iϴ"~O}RER3_smmD$ aia/e[=[>(thesW=~98֏92ZUϽPVI 7Fj]DDy$[,-ϏH+ LB) gͅUˉfD-u&նZPVqs ݾ>&5rst=Ki(*Ȟ]4mqZmȗE>+솓tZ(z_L<]]kx3h5@UMR?6 9/{3]<Ӄ-ծ~ȖRG’{UA=HbVLBrƙ4:V =j&?Ȩ4i& V(рo&`f!bU>p.aUU/s`hvg@i}er5Ⱓmj9 9;a P&\4sPL |>g@פ4Y:,':,gI 4× o|,)j w`9cq9,g /$bP<:Xn>XN0'ɏC: C,l_0Z7߁ ςoSs*ID/ 4hcg޾q }}usMhjkkvb< ^?UE)t┒%' аЃNJp4ȰS^)Ifew4ws[Y^>Ks'CDzE(rE6KQI4B1 #XelZI϶=73,)`.J&>ydhsQ`4u"'w"* 7%%0i:#SvhRfX;\eOmVl;1yHNÖkŵ-sسYUp_S-KxBo<3sױZ!< Ј |~+ >Epmsmgy~C)XǯI lmFV2yx!'>J'7pGdxǺDW[6܆7^-|߸|Au[l3o`Kz?66.Apƨ A?hw9D$@/(eE1+d](`ů(wxI@Q؏WQM2*M"Ԩ"XC5&I5_F#p)ݒ̪EY@=fOwM=puMmߐN Fg`,eR02I'`\ R ff4K9ɓpNgq>ω;- =RAE` D f^dp;yR ,cԙ ֨)1&cL1'2Qn02Lxs$ʘhK/r񂁉崄j0LBĄ  Mv>h;I϶$sƝس҇6VBXEmH :+ө(NyV>Ԗ{<7*b42oQ /fp 8J03$ycy ՠ( +l~Ne|0K@ `ByEVB93a) ~'~3h}֑[b 0GE%kfIgUǗifM*%tdp|԰h4PY B=Qu埫E[,yby˫uu[B[,s;o-B Zot V'Ε0Ǔj*n$'EEDA ~A/*U`/**)JN*4\QoY U6Ū *ފD:>}n+@#$~I7GV5ԚXVMcGHР M@ Эkti+\^/q96!aY>+wsE :1oP.y;V`]5j? gUh<_/vTĚ@NjaMS~\Pz^~*9Y==D f=>-jX]6t٥Aki6['{Ii2dF{FIjǀ7I]x~-tfQ5Ins9ZD*޾7:ME-qؑ%ԸᲖꭢ_9LwTqIeLԍQ cW}^mNIU&`1~}Wy7Uv{+˟-}GZP[}9-m2p%Aۻ%抻/OV9D74!n!p.˷d-ijXsqoy&9o /WǭU.zd(`_ >ެ{r;R ; 6|lT`3J|S4a )`8iYq÷jECxz\~{XЍ FJǸþW}\6ؚv=s8`5~Zq`òp [$]c赮k fw) 8:FZFCݴ5DZ;Z}y YX՜t5wp` _@Ύ埜i-[-mNgj1KYlHrmV, z_o7;tbæ fږ7۶#ZZȱ%܈FPPјH#]ͬ@DJvlX'O_09HmJHV':PCEug[Dn abrh8S̺D񳡙{gL4gyjT'R؍v:wFPn/Qf6P̽5iXx<-qZw/c]>slqz=?st\E*C8οُ eɘf$Y+4mXe^OSOܼDEHwKd]YŘ;İv{Y 3dYd7o. !kS4>.뤾DԅnU5H6}I hh{WO(?h (ׯU܉.K5:9nn=TPJ⊊HᔢX%nҁhdߋ#62¢IODNAu5\y4Q8;V6Dqy.foq7@;{,`h> #l&VR#4Gk=crݚ:t6/0KXbqŬs+,gIq@3Qzg0~}bhR~ޟ^RmI?s{ȰZJ"c2k:PL8 ƈo/Ok(1|Ipyb kb1p+K$V}J[>Q׮}TxcbP8uUZYg8u*錤TVXˠU$7Gh*q澟.N޽9ıF 5F[$Gn+"󱕴o1vMlw$F؍hzS uj [J-BCIFц2o}O% yX=ҝLaZŹ1qh`{Fu|3ɴ`{s3tRp4%,Js!`v*|D-bVy+A!+q@2*$X,SF<,g"hrFP"8n)iL&φDLCxJZ~$" 2ybc.c$y,Hxe? yR2n[-.4iDDV""r`ձdưHvs*$?m2$#>|,wxǹTsޙh_Pbk<3,;1,w#ۻv0& cY9 ф x6GJL:&-0T謙,iXGs*Da!3Uut?o0DUP42uoH,hΙ8Ȟ \Ps_92ࢆq2i-TТ_Fݖ#Lby4?yBz CK䎍+Q(rڦt`vrN,v{no4,F7n==q&E݄*[_Xo`d FI\%;}注] {T_v0\{+S$|q )vh.>[ꠛi hc¢UslslP.U g&)m{Bj&J9,Kx}̘X$O S p[`.ԙəRhp1mYǹaxsɫ>v8p Ǘ,N\EAfT(p݁uߚ>Tv%gB]9&hWPWvM֘.DtOS'Vx'g$^gTXx#t\4FcE}Q-} _cP5&ɫ+BZ6> kB5j :gD6&e;1m*Q᳘Wy,&(U ,RV6"g g9D.r trMŪY@4h˜F*Q:3ARF"h(5~.43$ZWqKLiɒu,JNʺ5Aڂ%e%MH8;(B [0SҌ BBO˔XRV g$OJ0zYD Oc_ Z2ZlĠ(ºәO' Q',A bT ;]y1$U,*0fdʦ2RQJXQbV$˜gEa>3H  RR0q VnM\*-wkۘDDԫ8ا#4܏2vߘay#C aD[[%7{š f򯗷;3MG?1MWߎx-ե<9v9@7=f/+_w_ou9q [4׀w$2eyH G&%`[ +iK?\󴮟!Sζ=FV.労-w%n)nH0jÒLTX\ ot9YOyOEX%4䶺] @-ګst>ˡw_J92=u-]r2,&n%FHyvbPSgI\'@snX"7Q2-O!nڵ&!B*Y Վ)I oHxдGm-玾K?utimƣ>{df<}xy̌3\c©PҦ hŢ`ERqA #z@mT"ۺ(0P pq^ՙ6`랶(w󺁑J~a>ZMǿ6A)oKX-riLKu#áDJH@D-B1 |RFa2i]59“J^d O*Vږq $kAKJf9]<M+d۲ジnBES\$ⰣIH9cJN ~"Bk~YJNamKyQӄdABqν(7B& $I(_TmA>+k],"Y2 a'"%)TST8|+޶,YːbSȃ J.H"&T,2ALS4|2>y2;O:'KED^wW?/_Ӊ_^ {/( )r'̽'>y2_.T=/|G3I : ‘|y~YVHZ ۡW|y;Z/$.5GRU,6Һ_/Q~fX`샎6ޢD!C=7$w-<3 sa Ql$}1=8=(ARb?=-z OiTh[aN|UF ZЄ㠍Y-q&exVk;,7GYMc;&=;4ɶ̹DžF7 N+wHzրcKy׷wgel>)_u-n<=YeBD?Μ[#"&RM ݵf>x=_q?rqaiuy]ASqx].PQ`Az)~}=7ϒ6^}Yu/w@'W߮n)/0}U^?5ʅ/PbE&#׭Jo0ʤ7G3M=˟^^lEB vv?&pZT#JP+(cU9VIpS.^/6b矁^ռ60=lA+=.w :CЈ+t׻u_k :06Y,aAME0ɇ&Oˏzz tO?|S/<J cˋƍߗIV؋\uEn9<*h OZ,NwEXim#Hc"sE ke{.aSf;TB)$30Z߽3=۶_*+T+aDž_}׋ǻ]8!tY{5UC5.h5qbm~9Ҷ[(4Z^mN W_&0ׂw!1q } %a7/lMEFw]{GY?t/h}[L(fCjXۯěuy#{1:XrDw#T[m09qy4)JV<s5՜E\qb(qc+<í{ϫ+ogG m#C6HLpva(Ĝm.6 5-ױ|-E5h8,rL% b5|s Ѧ" DRP_^5@8%qƈFhc؈ KRXĂ31LmbiP5  ӆNfK(N+6Y<1 63-Y$ifR'Ӓ4g$LS ª"S eq] ,cpii$/iu$'Jdf/D4 ύnLV28b,`P4422Y fES"!&XkE)ɄV@ aJ K2k}de˜)T$ `z^&$jF2̴~L[39frXsXae2f50 I"ZD&\iBcA#mQD97DeR6 FHO4(̌ᙊ(A5DN#ͳ:VObMzEN#ۿ!=N,zpE$D琣U\z7Ŀ^;V~hG'>de ߿`uG]|'<O\2wWk]:;?rqrmp1EԫƗ$;؇ſ-KOcn~!z "w r=Z!j@N@^1s}a^= գyն[հn=ۺ@@g b$Ov=_pd0bxK* 쁩/.-bPV9M./q~!T!xו)9'!G3f{ggw Xa"ŏ Y'y= @<;CE<=ڟtm}cW!} ; yFRh`>xu};ާij92R 9;V~;<\ {@`6OpF/e%YȄУ(4Ia LRWXR"Kt,(:N&\2U)-JeʞAHeR1)m!yBl4\[չL8,0Md ɈFu"t!eGT)=rؠQ69OJ [pІ .pL5ѱS[RN2cLhTPDiKR"6'6+UJYZ0"Xì%SLeH!,691E4#UBbj$X11#X 1@)k7&-x&$:1ڐ¤9oa+ L")Ec JB KD.2ƌpfq$4S+c`(X*M2VBu- Ɠ/&6OMBZPhG/CeE9BR@oYS(%M$̭BI< 5kG%iIYʠL3X-%Mi<JFZG[.cZh]G8o]{鴋M9v@},'Ǧ|w[VGMru56sac"7xtcEus2;NvtMեg.E,iFs.-~껅:w2keN@d>;Eg\.K7ݵIȣPl3GMM>ϣh Zio| 8̺j@O3)-ap)5$,x (:G9&$Wiµ (/1a)2}eq] e& ;Y ߸~ĉRMsxJ}8Ò_c+?c%q 8K`0$b4_5$Jf %xiH3pz( wI ;??E'H9)\-TOLki&ܿ}tD[Wq^C݀Xt&%l&2E~ҟEy{qK(|y>UBOBao3O1)<)lKm_@=7.ff[ }n;#n'i?~Epc4^M1Vs}%dFb?W'֞yR렃d`F/XozCO )%`s!$F<,B:{!Llq$2`93%$")p#YZEHB0-H!Ybxr(YKrj rBqL'j*gyA6yEj.<]Bdj"V*Ĭ/))ȰR()HZƉY^tVLU,11 ~ZJCo$g4)yD3I%zES>+xf1!3 I8 HʄX# pܦ) r&蠼 .@UhAИ*@ K*) P#A(6,Vvư Bciim@E\"6c}p)'K)uκ66iVe t0 '* (IP"$Ѡt?)ȶ&õH a (4', e&#& e u!KPPY $uY:]A4f΄R:FD)yIiX"T rE氒&@>4v`pҷ>IOA2r05~z923b!~d.g'y\iQhv}u^]7'ʤa|{nZjOi=wW[D즯.ܧ=*ə'ۢg4nikհYoeEeZT"bK/+b\^dJ7XœP=$\Ϛ=cvy곇4z@e'C@GP엷zwoyǫkg_8nq\m5QvMWbɿUͦZAC^,+LT5mn=TzgOfO._zz*n-r}muu\b6#=<4 '?&L:?q͈bLG9a3tkՆq]D>7y䩸|pN}gֱw|K^֟KןMskp5uRzZW [gWvNA^*ﺧ0>+14=!?w7w -Q^s.U}+돋MK@/L7v yM]VSVW?!-Prח٢<~U`?\\y+"_ڑ 0X`PYϖէz_/޿̙CUh׏KSf(Տk3>dzC[Y,a ޼+PFuxEb܃?n{@u-?.\vxmpY92-`gֳ걩UYiڀAt5Y*Ep r} S̀UpnWln{վ^0NwwmY8(忁u~;=ݦrnT N\/ Ract"c"%>☍w3V0f֦sߒ z3K\>q "˴_BGlvz ڳ7\_{1?&nՙ|w+q] wͻrarͶ`\}"#S:yъ֛˻(U7.*q/j=9\=4 .ncU~cۛ<+_~j96OhXZw2Xo64[o}\>{J7AjY-nBDmnPD<ԨHDZ-pJ_&D ¾ zZbq R)މzu< ')[>jM*ڱLBK U6wnk@E+ZP.vDs9FhԤW^_ȕn2+$\__Ӆ;Bp:stn"_mSw%ޭ~Ys % =e OTge6Rc; ??!k|i %I&k75j҃:qVp/ḷm;a@A͸ָP U~z7x09N~AbOv Ip;" ^ѓzaYo;"*rVXal{c-6#w함Jfm +'fa-KDVXk0cn+PasK{X1`/p~< }KK$kmnG3Uc`9)QnJɎ&qŶ~d )Jl'ڻS3#hYfϰ6q>\%fuYkCr 'IG-e;(P\xYsDpi]#ɧk$Ɣ.~u~suzw1}tSLq{< aNכ#Xv}Up 7X(!Nv[<}`,_<7🢹6栺=02K6 N?{]lAϼ|~wx lsݦf}:;2ф`pIUT?y]@^j?4v$4zړ}w@i-dӥRV%b/e _aA*46X 4zҲ4)-寨GwQ Wa Gu=zS;02Mfl2> wMd%VR.L0 5:bPR*YiZ3Qy7AB3p@F!R%/fBYx$"ЄRpa*0aI|k}zd3?z4՟3R44#Ac&1;^xѫ&]BwyjdEk8wGدn1ƶz*d1.pp[qR`4 ٖf hJb1rj^ s ^}AG}e|uNOׅ ? V͸ $nx.u+rO-i0|;ͦo3Wu0[߮ϰWXTQY?y)8!gxه~lRir+`!`?:QǾw?2\TgjUqROi59dשvr8hu\Bh|Ũɩ~v$x*Pui8{h&޷!E@x:zdI/FMsIɪڋ bp*dd/Vw>D>^_ǎZzہ8h03J.s48fl!iw #D$%+stU}kKeJQE!4-hSB" c B ⇼ʬU~Y?pеi޸8>@Dƴaiܐfx;55ɬv+:CYhw7}L55S=B_1`^|rwdkD8x9VQv`r*>o0޷vc/‰ ¼3چwr ½3 sOSs8%e9pEM1P=n p62\p;: ao[H ͭ{tL]X>gH0V)>y~v~ ܳxޛmP_cR_'WN:^3k,DӼZ,cx`ڪzک]*HYr1cVW<ظ Q.{v3#]:>!T;o׽Uo o ]kp )9Ch|Vg2|V b~3wmKCMsSR/S'6G ;CinO#ؠ5 ;i.Z&(\ÖaOQB44(7k9Uja9mad].N@Λ@K97QB?m 2ņ\ajin#nwڨ4$~TZp.)^b8C Nׅ.oFF`H7 !]ISf.Sc t 5KX"s^%WOj%5|tk#/gwb#pKzwm|xzek0HL|;YdEd{zdG]Ut2A&=S߀L nJ_ ս$uMaPi3n$m=S?E9V%2yzZa5xOTր1O4~da3n d-eq⪰Sqp3^=2 m 7{큏<) N{h<䔃s. ; s8;*Ck'5|[eĊ8+-ntU^JB;Ԡdw 9`ෂЇ (Y@?.cFj'ޟ4."a^i"uTDeNL4mJ_5rkE! Ja ScAB8Y_QK~hq7ۃKHO<`ܟb쑤w*1!`6MlrRTwG1Q`} BPLKCM \$LMT&cK'D# ! xS o|'8$E(lo5<qMrE\j4!1kRC eZ,5\/S)d~ 8*%i^FJ)SXZǩVtYrY& !HgT肈4<-B7Zeh 'R\aF”a. Y*ҩ+澜4\VFI21K!B40 q#LGQUce3\%<%b"22 /A8tJd$ KL[&H5büƆ]ZfeHHKFcH!+0LT1e:4&7DYAAbhECO *2 +P/ oJ*cĉ.sCELIAd')X!!U:rm(Y`^K" 3*wC5LO<1e$ʸ΁LBf XCcodX[͗׼P@"6ޖpq͆k0)5j&ߣ7^ɘ掇7Ŗ+k U:gi,aZ U$'f×%Y;La{9؜ %Z/>-YQg|Bmq[pY\I>gI}I}\|m[rA`t%Yz3!ċ ZEтY/QU'ӻQ7tƺ˜f"W8r\DhUov\l&>\Ռ#$?r &yEDXAEgc0}?`K&#P4e冥cŘ?3īFp[GsLi.Wݭ~ezyNvQk{zaBp %v/$Tl7;=XM7(hW56^ثDe_a|}X]!+gѫwYGG3%0ܟa`]-P \a \EYn= ;`h4i'1( QP 06xpF`ћ߈pp|r {mLta-[= ƂRCcWU<} { ԧvK|~wۇň#Z§Yxk֬a ߒ}ܰN4vcɼUV5$^P4O8CY迣r_,Goky!;_y 6d?Ez i]՞8k,QC?pi"6gYa]mhhƮ M*8- LV'e.wRWt;/xc:-B׮uSe.$>\'"a!>:Ɓx*2"-֮Ɵ8jz>'Aa%^"IN j Hs'7X5#e}9Oꀗw~;~~{i^$Ȇ$_2 kI'$gH#g e{D _!wvҧ=2{3/c%$˿(:="d=r/0ծc?:'ω5#?`(Ψa&{ X*|z\ū>u<9nNS>Q _jI/K5/|>n`}nJܚMyc-ؤ;I9bÒGjT6XLu G8ʃj}po:<_'h'Ц3҅(} O@&|˹S95 ZX}2xOqv޸Ł ьy/5%0{ƾ 3<8=1Q[yt&Ϩ>dvJLZrQ*h=CzSכM/|pp9pxVq@/bEH2˼oq#rOLJO8H'}%Oz'@{P8:{P8ߪ=y-zqa E>N*u=OḪRu'O^]jvO3aғb/)֓׃bԑNwbU̾rʅS.|ޢJ<8Jr߸m6َTCW*?8M凞6|Q8ujY:){S&) B)Sx˞>5MT-h{qAIY^2)}4Hrǔ84IH,e }AqL Zq^D f%^T2a?J\VEJa黩C0w C-r$tI_^8ED(eQ|%%LPPiT~Ge K48crR'%()(^WZw]ZER!NΌG<)%|/+?28i2J}7 dV]J:"XN͈G=e;"P/b?&BS\ i/4*䥥EIX$>q5QE(.;ڡضj$ĢUihN&I4JPUDХG27 KZr83GR?UqBl;"s.̦NV%vIE6&V%GcNOBqbF;rP$%n.IPHYZfI]6)J߳YGvЩޥsN ϏJ0 yл S1)t"*B)XbJg5lhF"i2LZJ! gq:)t$9{ND+R(²"B=׉ 'HKXS7,+˳Fwvvy25al4dn)l.]#;ϧf2jof; s-Ojn>-nVh~i3i/[7Wk~9;b@}+h=Mf]\WuԾ0eJJzu(8ޠ=y@v7X{kvsG/(If' =qFQ$sMFzb?`f%-4Sj[RV6WۏK ׯo0vdwO7wϪ2S R_FP{Ew _-}k nVWH| ,)MzHpWy6 S4CRV.׾; X-n,~] *5ګ=9o!L$[gk@ cۍ\7FmsFƒ\H$'jޗ)Q#҆cYL4iq{z,u.ذwF8t=#Hp~ 1j.tsIZ򆗫>\Ř`puodFij'p8[/՚̱7km>)bG wnazrrM#6p ¿f;w$h:gݬk]9:Б󊎳71SRBoz57Gr72FțWhbzn2nS5cRU9A8 NCs|ng(xe_o<g -v$/XbS8'촿E`ie%.^Ѳeׇi{5$/&{&D3*ZQ0@,Xz1atƾ|"TF )3z*<91W3C C.áIؓ0\wq<0. p(׵|[AڃCY 8E 8T88q(ڏCC@qrPP!áGIJC*z.UPp-{]*Iơ?C98UPQfJJbT_ǡ(peYjYQKQ$9"Ch`Nm FQХ#AD -E!UAQͧ"1q&A*qS?-]&TW$&-*4Sa `y^|cf8hy҅?ʏS3pmԡa;\;$dS/LϓA&%jTcBџRY! Bt@&>z4 MGGWDz+kor(ܮNj@YH,jkcٔKՉ~.Ͻ3܏3t"ʼ(. 7Nl@/Js+ e"m^V9r1=~%%zoP*5#0YJ(~.1!DAiuEKMjyEiK Qsaߣ* D]L#JZB:]|ޙIe2r5##劭 Gڝٲk)1kx GIJLHhɁL[8_'o].8ӥ. 4pd\[?9sejFo;ғoѻy!fF߃< yn^ӳta=лs>'3` EXs5\3 ]̔3pLYB\\ݳ&K=>rYIa}/OË@yi*8{,\ߋՂgi_q6X x Ej>Wê_.E7MU1:*qɭ/}`s.&:z lΐ| +? ?0nUs"L*ńxI_WfRc՘Tcv͑*b:k+ss2fqsW'"3\:B$FU̲ts]-C$7q{"٬=E|n.߇\*28t5U~O3$Jxr/]FՇ3c޽~1Pu1n_+j{7K7OMxH,@<<1#ON!7+ƍwiqL<?n`m s#0|<` k4p @Ffzqh`;ǡ 4hvިǠ!a,OF=%pW1(ғŹBH6G}/!{j,} 1q֣ ߓ|rxZ "G^ ~[ GULMqݮz'jG`ř gGuIrP&U&Y#('K%{(L!EaQ&Ia<Ġrr-&NIW 㞘2k`2ur֡Lez4L(&D;XcFm2LCCFC`[9J*4L$3Lm7h@D nQ&Ѐ2(< (Ѐ2e (ZD8G*LEm2( h@ (d(Lpe<P&8ـ2jЀ2QTpB D"T<#Ǣe R(P2ٚ"2.1T3LP&fCT_e]21L4^Ԁ25N+LA[Q2ue-׀2Qj@#(Gv 4w- (-C -`PbSerej4LAPep&2UP&Ѐ2](eRՀ2$(,}1ىMXT1 ݯ'CO_M'ϸ x?GbK!˻n!˧ \vĆ{(wJjf|YPě?\"һ ]?y{~K|u7 tg:c֣u[I>xe$NUOwKC1뷟6s˦l!O7uWlqm zA%=zXy9yȽ1V Yçavo@qpšC|s 5W;bi2l߾D٫:tsatZ4=r@Ԡk͂pM tP!Z20,S; "޷$ N 8BFC?@Z_>V\Byr2r Gm(^: ܭ8䚉VOSGZ(9& pVsYO|s~\`q*p}RPg2幌Whjs,^Q40,Nm0ϴS+ce\U=l3wO"N :}Igߙ1qDtύqW4Odr+2R&Yki.Ot$i1v7׀?bM;= us%hY:8.s{Er%2z XdbryNc#U0oل mrJoގ4MupY T BiH#jr@'lO1;uKzr|ri~Ok3#p@Tom6'gə&430)g\=ebŷ,afH,08] f셂7 "8Yɲ( FD]MLRZ 2p[ wN'K #߭|l_-ya0cۓ/Ϗ,QٽZSX5 yv`"&od?ezxjyCt5YRecMڍO߭ɣ(rG H(?gw|j:unU"&(OF=zptc]ğ9;x4%}3(b? '(οo`B"2fGRgT(LKq6Kx/B1}T(ՏB]@/wc8nPØHtm"EOϢWiws1hz~.nNN'+ۣN3:'ωOc!O#t`~cYFXG;SJ>{K,"8\_ybEt1m[nG{N'm}X>0 ecVZۛ[m9陎_D y uo$2aAmLMDQj7w9GCBr #h6&T&ɾ$io?/ڦy)*\,_v>H+WҜ6 ޗǷ'\Kw;F/~cl(ͯ\zt&Ი 4D0 ?|6aTZDȵNȂԌC P+[QzckEk%B*(4 $% $g LMꪢi$bӝd:fע5Y ϗ$w\U2ǹsx.yYWH/BmsۈU\C #ϋMaUISEtC*08EۨEh^R,X %j"KZ2Pډ6"lIY|^VDe,LJT:ע$dAkCעE)yaLU,xB|+VUPc/";-bj&x&Y.0rd*P8$^h°K a M%"8*h4邐TZP97ԄC}Myq8xC⩀r<Qvv~:^39D-'2< ?>~/7?Xo|?" 1|z&j~^''7h˫.~Eb|A,?uQ8y6&/c@8Zw~#覝[=6^{T~Y8m~K?M"h;hǿ'`0N6~-5ӝ8OzCL1&lpj3G[?o> o> Fo?kl3y>8>fdߵ.E"ҫZ9-8 ȥ̑_#<"v ѺJ 1RRύ"Xss{.,(k(FIՔ]?9oӒIC^*F+9r.Chu[:UM1;y]fʠ FFiTQW66*h{($(o1̼fEQ Q 1\g- W.*9ȏW,`@My s.\ .J''uCQ՚Ep'9Aز)\C`S -)@#0R6*`=lmCk,U6"Cĸ@&ɨ͉5EmwS3PrQSjhTɒ4JPb%$y4[aYt!r(wܮH2(5xK:G}FjW*Sv:\+ʢ G'PhZLfJSF5\ $MTm h/T?B009IQE*r!-q<^G𰢲NV!m=aۃ(7mGcIav;x?kxro6PK$u^W=Ev]<.x@o^]%em4,~n?C= ҂/ x]_8pdkO}j|@NeW>A>m8^?d6y3h/F;FNNN;P-<rNmKwq?bF*8omgwTD +wmgX_/bGTU3ouWb[.tYy;ϗc/ +s p[ޓkJl7x/ ߮k2-\hbtҢ~F.wsןyh{MtlR:vox\&:ǘ@7i!6nӶg0=lC71eM7A{Pw1brqc,FGnnH_xK0]F!Ɨ,pM"_`րݮ~Fm4Y  .gWl\'}}ۻ$\)aٸl S~ܬa8wf6A/Ё+J//[,o׋%jxߖK^o>KGqsZW\it;X\:@Y\~P^hhAK(X/hśۻ8B` @-׮VW+4w^A;] x}7:! 빇x #1{[t?7xx\ , tRp{ЬC=d׷ٕaQ;ܢa!bsw_cyuZ.(qnrW(֯9e԰I8aS 4El^ ?㸆2+`y:~ Tt:mYU:VP~/WwKZUdvnO`xޒ.5z}?5-|eW]aLxvqhf^5afUk:1݄IV{x0lrf6;!Pxw'T _a>O+h"g8UUGOl X~#qz!>9=%wIP hw8=EMTN&'gQeie{X/}1ñυa{0lJ 6U"ly6 O+ Ԟ+xZ鉞퐓6t ٸ _v{,ǖ*9F}NWMv>1ȯ+#%9N_YbJep_Sx^Xa+/sl%6IPKߑz4H5=iC$3rmue_ݍFv!o5ɯq <(D@GD騥:Qvv6 1 nsD 06.iMwag3.jXYPvJZ3CDSp/a|WI♤m"7߄4m.'˚1V80C"%'~mtIZfD2QtTqkyf`<)BƠ :J[iRIj.IP͊/̡YzN\skH沺 n¯l"ILࢤf9Iǵ)؉[h` m, [p4$76.C-Hr FhJBȡ>Z4y&1$-t|M3)4X251) 9$5,P&':gPduM:1o9i2J*euF ^5",|{ ~ Rơ/ɒA.ϣڐN[4=/`@al(VU\3*]':h*D!)#r!\ɠQ&$C/HQlNic"5|I 0ҠwZcn43mĶrDm2]!uPB|?BlOw8G$z"B=*<=RM" 4WGt[2_Ű֏*dܚ_1*"vd[Qtt2=Yכdյ@~n[# ՎY4d>ݿc{9,twG{05vcOUT&x4:DLeŒfi̖Q5^v 3(wO~GC"hs>h䔟GC;uhh(>:ޯkX :&JWb&Oz944mz=2i(AcݼDN;W!ӝrrl1 9|_>rXQBFIL7=5lNRR"~޾yڝ>#'c`ğ{jm @*gx/c3G?;|;Z;m>{ƶ5ۑ^MϵUb%{(4x~Gٽ""ɿ߭)W za0'! ^TLkS,TĢ 08lxVA9:h{WT PRhl(]5rpkl(88΋C&h*ސ[DX:f? S2|>" Hfft'`H'` rx+`kbq>+PEstSN`;KXb<*gf) 6q^ > \<4 *OYraMjĬI1zUg8 FVh`K+* =&~Ҫ8*Er%1MyHVo« vD4-ƛAWА1N2&٫0XA[*< `$"j%Q%,NH2شJhb(P/|Ƃ*kUA` @XS ]UϦP>/S*O iYLsDRD%{ @V&,T.&"$]J?HY2ò5Y6ՁS-k9l[bnd@))-^sYxб0RL߯=Yn GSS{PLj`̓Yk/E[f~y̨؆]S~Z?{8sRbv4ii=6w/auVZoҎEiX0bЅfA7GY' َ [oYD3{'1=[k60\:.7Dy2 RnWq!a[IjqQoޓ;ߣ'M7_w5j!M5"yeWjˊnr-|NNzqsb #75ĎW-7^-+A8ʧNtjefNtK߶OTk=KBYd#?kٙ=1mk6<60xUƐh2Ȩz8m7a"Ԭ6Yc} 94[{FO_?zuŠ4vX]Kz^Mj~#x D3ܑf?Iֲ۷h#aG6zf'Z  Ή 1:vU}#zHư|y}RyK6^Ajj=|.۪]e\v^on>[,ZvtHxԚ\ ; XĶ+<7M繸ߌe}+3S>=c$Ҹ>\*'˴Rb=d!u55m=>ifM!Lޥ;?"QFAqh|&23^`art{9JRdM"C0Xl'7GЩ8p }F/qr ٩OEeM BVPDNauMPRXp$FU6l m;9S$P׿XfjOa5b{TQjp Ag0ٲŜyGӎ+W8y\1bs?[WhpڮU J+3ƞfvAdq4W&UCQcT{- ?᫐=D5,CBdm+o0)o4q[[ll2KwMu<wc;*a׷໎fw^?]%Ys|WaC#Sy5 Iu^RJ2s+_xbb(ޓ ] ʐ1쐅>-Y䈶_!&t5=DBE:4&qhB!m-.D1Z6L6Z3ػS9oEֶffh y5}kl[{v^uoCf iB\^̴6 ۝Z2jcգ=RwljDû4dH)2kL χgE`$OB.01\ 4]YDe'βE`$+ A,2`nI6m'*2<!ð^A 2) ݤ(312a8}ݰB|K![l'G`s=oo͝tdOý }ݮnbgf5$}p\7ecDN7˟TM%SG˿Q'F5Ѵ#zTrN?쇮cclZcc6״<5穊 ;lMxpԳfk|KOp5鄃1XMp.W 0 #P V/;<;|_4` cB&=iC&[x%%GE;X*^^և䌒sܑVkd7uI/*V@v~G,͎=5$7 f]qTݳK:],h/Rnsj_/zʹ51u'Sױu9yya{yy=tnuYiQ0&44Ph {Rs*4 |]txjmڍ غcP`/% ߂ǫgxqQx=:xaxxǣx8x|"<>Gx\^OxvxTx4 ^ ſzh&\*{ }o{ Pl=] #p-%iR1vF՞CL33lqqGlǪs螮[k릳WzWRQ_ʝȹM$*/ee n :cq;Atbt 8^zv9֎kArK࿶/.p"؝8ft@-WU zWJMx V%`q GYF^OP@?~?Cy|3~K )/8kCf@$63Ct8GӇհkiY=!6޵GT<huRr8/5jW.RG*\` ҷ2JΊoH\Zf iڿqN>wjF)BWqpUHG̛z&GP݁b5؏n{#gZc\m4Ükٶ-9e=mOuȵYnXvR!z d/ڐ@k rjQC914c{ϾI^rےfsx)>(6 gWPnQ?I#f}s \w=ft@V~-$Ye$w@U==@tB㱥i0 >*3P;,)6mb#:LcRp%z^v7}3;c;M4_K 㦽>_ju_^dJا#x7hsh׏.S,`e@B(o#Ty3^AaPk\?'sZrE^_.; 7^t2NnLWtY?&in $ҍoٻ"b:S5IٙfbGd yi|az]ZuXROK #sy90 oێ蕛K {"Kv8OhHB1)rTø|\E_QxJ'~J.m:"ʧ_ rD4Of LǴL얗Ρ ~ükw%qCav"0 b:RlгP]UX"[*QBO6WQ 1d@f[BKA|YC"piB*&OBpSK艤|2>.&Dyٖ)BcV >eS:@pm7fS yP$*J&1wvXU%b>fG2YQ}fKjaV`\Q]AfNCVyzW.PӢ$1K15M&͍`KLn.#1NtaAA>8-!7 qE;䣋$7FBj64.<{U;+Z8 -FTLp_PC>7XbmvlqG-3θ/>ٔ__Dwؠ|aTl+z}^l̎.,1x+zۍE $ye%)kkҭg2j3>>@[E&s6?s^|[~\Wh4m>hofD)#"Gf'TCC\ y 8dȍ)ED ϥD/7[˷z‡ߵ\̪#$}b<^hڦghvt'cԝfC㕣v_7C5aʅeSTτzo: ~"UIn` U;l>6*`Xa0G0lW`Xü _0 0+`8|0 _#0·\6r!|  t f ?]}ą^{Ԉ~g6-y e(lDzb ٺh%wknժK SbݡE]ֵv^byWMJdsM+iڵ`R)auZaKUPZBUz! q2ŗ4zYHU|BLZ1gɌ"]Q" ^=l2qp?}GAن׏+ʭݒ^t-t)$4@9@B ؊*P3=HexՊ#8' [ R~ KxkNKN!S):o):~SP6vP5${ 4z^gpn4{bNH H@> pDf=Yq>0Ec"6qH{E$/wܾc Swissknife_1.75/examples/benchmark.pl0000644005110600510130000000564710366115237020176 0ustar ecastroSwissProt#!/usr/bin/perl # ************************************************************* # # Purpose: # Run a Perl benchmark using the Swissknife modules. # # Usage: # benchmark.pl -file filename -repeats int # # ************************************************************* # ** Initialisation use vars qw($opt_file $opt_repeats $tmpsource $tmptarget $opt_debug $opt_warn); use SWISS::Entry; use Benchmark; use Getopt::Long; use strict; # * Global constants # Read an entire record at a time $/ = "\/\/\n"; $opt_debug = 0; $opt_warn = 1; $tmpsource = '/tmp/perlBenchSource' . $$; $tmptarget = '/tmp/perlBenchTarget' . $$; # * Variables my ($codeStart, $codeStop, $code); # * Read options &GetOptions("file=s", "repeats=i"); unless ($opt_file && $opt_repeats =~ /\A\d+\Z/) { die "Usage: benchmark.pl -file filename -repeats int\n"; }; system "cp $opt_file $tmpsource"; # ** Main print "*** Swissknife Benchmark and Test suite *** \n"; $codeStart = ' open (IN, $tmpsource) || die "Could not open $opt_file"; open (ZERO, ">/dev/null"); open (OUT, ">$tmptarget"); while () {'; $codeStop = '}; close IN; close OUT; '; # Read only $code = '$entry = SWISS::Entry->fromText($_);'; timethis ($opt_repeats, $codeStart . $code . $codeStop, 'Read only: '); # Read and write entries to /dev/null $code = ' $entry = SWISS::Entry->fromText($_); print ZERO $entry->toText;'; timethis ($opt_repeats, $codeStart . $code . $codeStop, 'Read/Write NULL: '); # Read and write entries to /tmp $code = ' $entry = SWISS::Entry->fromText($_); print OUT $entry->toText;'; timethis ($opt_repeats, $codeStart . $code . $codeStop, 'Read/Write: '); # Add AC $code = ' $entry = SWISS::Entry->fromText($_); $entry->ACs->add(Q12345); print OUT $entry->toText;'; timethis ($opt_repeats, $codeStart . $code . $codeStop, 'Read/Write/addAC: '); # Read and write entries, fullparse $code = ' $entry = SWISS::Entry->fromText($_,1); print OUT $entry->toText;'; timethis ($opt_repeats, $codeStart . $code . $codeStop, 'Read/Write/Fullparse: '); # Force update $code = ' $entry = SWISS::Entry->fromText($_,1); $entry->update(1); print OUT $entry->toText;'; timethis ($opt_repeats, $codeStart . $code . $codeStop, 'Read/Write/Fp/Update: '); # Compare the entry to itself $code = ' $entry = SWISS::Entry->fromText($_); $entry->equal($entry);'; timethis ($opt_repeats, $codeStart . $code . $codeStop, 'Read/equals: '); # Complex modifications of entries $code = ' $entry = SWISS::Entry->fromText($_); $entry->ACs->add("Q1", "Q2"); $entry->IDs->list([]); $entry->IDs->add("NEW_ID"); $pfs = $entry->Stars->pf; $pfs->add("PFAM test line"); $entry->Stars->pf($pfs); $entry->Stars->fl->add("TESTFLAG"); $entry->DRs->del("PFAM"); $entry->OCs; $entry->DRs->del("EMBL"); $entry->Stars->translate; print OUT $entry->toText;'; timethis ($opt_repeats, $codeStart . $code . $codeStop, 'Read/Write/Modify: '); Swissknife_1.75/examples/example.pl0000755005110600510130000000204510061537274017670 0ustar ecastroSwissProt#!/usr/bin/env perl use SWISS::Entry; use SWISS::KW; # Read an entire record at a time local $/ = "\n//\n"; while (<>){ # Read the entry $entry = SWISS::Entry->fromText($_); # Print the primary accession number of each entry. print $entry->AC, "\n"; # If the entry has a SWISS-2DPAGE crossreference if ($entry->DRs->get('SWISS-2DPAGE')) { # Add the pseudo-keyword 'Gelelectrophoresis' my $kw = new SWISS::KW; $kw->text('Gelelectrophoresis'); $entry->KWs->add($kw); }; # Print all keywords foreach my $kw ($entry->KWs->elements) { print $kw->text, ", "; } print "\n"; # Print number and Comments for all references # (courtesy of Dan Bolser) foreach my $ref ($entry->Refs->elements){ my $rn = $ref->RN; # Reference Number print "RN:\t$rn\n"; my $rc = $ref->RC; # Reference Comment(s) foreach my $type (keys %$rc){ # Comment type foreach (@{$rc->{$type}}){ # Comment text print join( "\t", "RC:", $type, $_->text), "\n"; } } } print "\n\n"; } Swissknife_1.75/examples/evTest.pl0000755005110600510130000000235707563750766017535 0ustar ecastroSwissProt#!/sw/arch/bin/perl use SWISS::Entry; use Data::Dumper; use Carp; # Read an entire record at a time $/ = "\/\/\n"; $opt_warn=3; my @kws = ('Transferase', 'Kinase'); while (<>){ my $entry = SWISS::Entry->fromText($_); # get a valid evidence tag my $tag = $entry->EV->updateEvidence('P', 'TestProgram1', '-', 'RU000044'); # For each of the keywords in question ... foreach my $kw (@kws) { # Check if the keyword is already there $matchedKWs = $entry->KWs->filter(SWISS::ListBase::attributeEquals('text', $kw)); # Security check, there might be duplicates if ($matchedKWs->size > 1) { croak("More than one KW matches $kw in $_"); } my $kwObject; if ($matchedKWs->size == 0) { # Create the keyword object $kwObject = new SWISS::KW; $kwObject->text($kw); $kwObject->addEvidenceTag($tag); $entry->KWs->add($kwObject); } else { # add the evidence tag $kwObject = $matchedKWs->head(); $kwObject->addEvidenceTag($tag); } } # Delete another evidence tag, just to see the method. map {$_->deleteEvidenceTag('EC2')} $entry->KWs->elements(); # Output the entry print $entry->toText(); } Swissknife_1.75/Swissknife.ppd0000644005110600510130000000073013155517103016704 0ustar ecastroSwissProt Handle entries in Swiss-Prot format Edouard de Castro <edouard.decastro@isb-sib.ch> Paul Kersey <pkersey@ebi.ac.uk> Henning Hermjakob <hhe@ebi.ac.uk> Wolfgang Fleischmann <wfl@ebi.ac.uk> Swissknife_1.75/Build.PL0000644005110600510130000000126712366141075015360 0ustar ecastroSwissProtuse strict; use Module::Build; #PPM archive build script #to build ActivePerl distribution my $build=Module::Build->new ( module_name => 'Swissknife', requires => { 'perl' => '5.6.1' }, dist_version_from => 'lib/SWISS/Entry.pm', create_makefile_pl => 'traditional', create_readme => 'README', license => 'gpl', dist_author => [ 'Edouard de Castro ', 'Paul Kersey ', 'Henning Hermjakob ', 'Wolfgang Fleischmann ', ], dist_abstract=> 'Handle entries in Swiss-Prot format', ); $build->create_build_script; Swissknife_1.75/Makefile.PL0000644005110600510130000000051010225167564016027 0ustar ecastroSwissProtuse ExtUtils::MakeMaker; # See lib/ExtUtils/MakeMaker.pm for details of how to influence # the contents of the Makefile that is written. WriteMakefile( 'NAME' => 'SWISS', 'VERSION_FROM' => 'lib/SWISS/Entry.pm', # finds $VERSION 'PL_FILES' => {}, # avoid using Build.PL which is only for ActivePerl build );