swissknife-1.67/0000755000175100017510000000000011040133466013514 5ustar moellermoellerswissknife-1.67/README0000755000175100017510000000462011037374764014417 0ustar moellermoellerOVERVIEW -------- Swissknife is a Perl module for creating and parsing Swiss-Prot files. AVAILABILITY ------------ The latest version of Swissknife is available from: ftp://ftp.ebi.ac.uk/pub/software/swissprot/Swissknife/ http://swissknife.sf.net/ 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) 1999-2006, 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, wfl@ebi.ac.uk Alexandre Gattiker, gattiker@isb-sib.ch Henning Hermjakob, hhe@ebi.ac.uk Paul Kersey, pkersey@ebi.ac.uk Eric Jain, ejain@isb-sib.ch 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-1.67/Makefile.PL0000644000175100017510000000051010225167564015474 0ustar moellermoelleruse 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 $VERSION 'PL_FILES' => {}, # avoid using Build.PL which is only for ActivePerl build ); swissknife-1.67/COPYING0000644000175100017510000004312707323534077014572 0ustar moellermoeller GNU GENERAL PUBLIC LICENSE Version 2, June 1991 Copyright (C) 1989, 1991 Free Software Foundation, Inc. 59 Temple Place, Suite 330, Boston, MA 02111-1307 USA Everyone is permitted to copy and distribute verbatim copies of this license document, but changing it is not allowed. Preamble The licenses for most software are designed to take away your freedom to share and change it. By contrast, the GNU General Public License is intended to guarantee your freedom to share and change free software--to make sure the software is free for all its users. This General Public License applies to most of the Free Software Foundation's software and to any other program whose authors commit to using it. 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If this is what you want to do, use the GNU Library General Public License instead of this License. swissknife-1.67/lib/0000755000175100017510000000000011040133466014262 5ustar moellermoellerswissknife-1.67/lib/SWISS/0000755000175100017510000000000011040133466015172 5ustar moellermoellerswissknife-1.67/lib/SWISS/KWs.pm0000644000175100017510000000376410366115237016254 0ustar moellermoellerpackage SWISS::KWs; use vars qw($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; my $line; my @tmp; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'KW'})/m){ foreach $line (split /\n/m, $1) { $self->{indentation} += $line =~ s/^ //; $line = SWISS::TextFunc->cleanLine($line); @tmp = SWISS::TextFunc->listFromText($line, ';\s*', '\.\s*'); push (@{$self->list()}, map {SWISS::KW->fromText($_)} @tmp); } } $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-1.67/lib/SWISS/OH.pm0000644000175100017510000000251510432340022016031 0ustar moellermoellerpackage 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-1.67/lib/SWISS/OXs.pm0000644000175100017510000000606010366115237016251 0ustar moellermoellerpackage 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; my $taxids; 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(/\,\s+/, $taxids)); } else { warn ("Parse error in OX line $line"); } } } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my (@tmp, @lines); my $newText = ''; my $lastElementRef; my $listRef; if ($self->NCBI_TaxID()->size > 0) { @tmp = map {$_->toText} $self->NCBI_TaxID->elements(); $newText = "NCBI_TaxID\=". join(", ", @tmp) . "\;"; my $prefix = "OX "; my $col = $SWISS::TextFunc::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{'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 $taxid->text, "\n"; } swissknife-1.67/lib/SWISS/CCinteraction.pm0000644000175100017510000000646210366115237020273 0ustar moellermoellerpackage SWISS::CCinteraction; use vars qw($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-1.67/lib/SWISS/OCs/0000755000175100017510000000000011040133466015656 5ustar moellermoellerswissknife-1.67/lib/SWISS/OCs/Oracle.pm0000644000175100017510000003104307563757202017441 0ustar moellermoellerpackage SWISS::OCs::Oracle; use DBI; use DBD::Oracle; use Exporter; use Carp; use SWISS::TextFunc; use SWISS::OCs; use Utils qw(_print_args); my $connection=undef; my $CACHING=1; my %SWISSID2TAXID=(); my %TAXID2OC=(); my $TAXID2OC_counter=0; BEGIN { #print STDERR "Loading package SWISS::OCs::Oracle.pm\n"; } sub _connect { carp "Connecting..." if $main::opt_debug; $connection = DBI->connect('dbi:Oracle:','/@PRDB1','', {PrintError => 1, RaiseError => 1}) || die "Cannot connect to server: $DBI::errstr\n"; } sub _disconnect { if ($connection){ carp "Disconnecting..." if $main::opt_debug; $connection->disconnect; undef $connection; } } sub fetch_by_swiss_id { my $self = shift; my $oscode = shift; my $tax_id = oscode2tax_id($swiss_id); if ($tax_id){ return $self->fetch_by_tax_id($tax_id); } else { carp "swiss_id '$swiss_id' not found" if $main::opt_warn; } return undef; } sub fetch_by_emblacs { &_print_args; my $self = shift; my @emblacs = @_; my $tax_id = emblacs2tax_id(@emblacs); if ($tax_id){ return $self->fetch_by_tax_id($tax_id); } return undef; } sub fetch_by_species { &_print_args; my $self = shift; my $species = shift; return undef; } sub ncbi_scientific2tax_id { &_print_args; my $species = shift; _connect() unless $connection; unless ($FETCH_NCBISCI2TAXID){ $FETCH_NCBISCI2TAXID = $connection->prepare(q{ select tax_id from datalib.ntx_synonym where upper_name_txt = ? and name_class = 'scientific name' }) || die "$DBI:errstr"; } if ($FETCH_NCBISCI2TAXID->execute(uc($species))){ my ($tax_id) = $FETCH_NCBISCI2TAXID->fetchrow_array; return $tax_id; } else { return undef; } } sub ncbi_synonym2tax_id { &_print_args; my $species = shift; _connect() unless $connection; unless ($FETCH_NCBISYN2TAXID){ $FETCH_NCBISYN2TAXID = $connection->prepare(q{ select tax_id from datalib.ntx_synonym where upper_name_txt = ? }) || die "$DBI:errstr"; } if ($FETCH_NCBISYN2TAXID->execute(uc($species))){ my ($tax_id) = $FETCH_NCBISYN2TAXID->fetchrow_array; return $tax_id; } else { return undef; } } sub ncbi_fullos2tax_id { &_print_args; my $species = shift; unless ($FETCH_NCBIFULL2TAXID){ _connect() unless $connection; $FETCH_NCBIFULL2TAXID = $connection->prepare(q{ select tax_id, fullname from opd$wfl.v_ntx_fullname where fulluppername = ? }) || die "$DBI:errstr"; } if ($FETCH_NCBIFULL2TAXID->execute(uc($species))){ my ($tax_id) = $FETCH_NCBIFULL2TAXID->fetchrow_array; return $tax_id; } else { return undef; } } sub ncbi_fullos2tax_id_bulk { &_print_args; my $species = shift; unless ($FETCH_NCBIFULL2TAXIDBULK){ _connect() unless $connection; $FETCH_NCBIFULL2TAXIDBULK = $connection->prepare(q{ select tax_id, fullname from ops$wfl.tmp_ntx_fullname where fulluppername = ? }) || die "$DBI:errstr"; } if ($FETCH_NCBIFULL2TAXIDBULK->execute(uc($species))){ my ($tax_id) = $FETCH_NCBIFULL2TAXIDBULK->fetchrow_array; return $tax_id; } else { return undef; } } sub swiss_scientific2tax_id { &_print_args; my $species = shift; my $tax_id; _connect() unless $connection; unless ($FETCH_SWISSSCI2TAXID){ $FETCH_SWISSSCI2TAXID = $connection->prepare(q{ select tax_id from OPS$WFL.Swiss_synonym where upper_name_txt = ? and name_class = 'scientific name' }) || die "$DBI:errstr"; } if ($FETCH_SWISSSCI2TAXID->execute(uc($species))){ ($tax_id) = $FETCH_SWISSSCI2TAXID->fetchrow_array; return $tax_id; } else { return undef; } } sub swiss_synonym2tax_id { &_print_args; my $species = shift; my $tax_id; _connect() unless $connection; unless ($FETCH_SWISSSYN2TAXID){ $FETCH_SWISSSYN2TAXID = $connection->prepare(q{ select tax_id from OPS$WFL.Swiss_synonym where upper_name_txt = ? and name_class = 'synonym' }) || die "$DBI:errstr"; } if ($FETCH_SWISSSYN2TAXID->execute(uc($species))){ ($tax_id) = $FETCH_SWISSSYN2TAXID->fetchrow_array; return $tax_id; } else { return undef; } } sub swiss_fullos2tax_id { &_print_args; my $species = shift; my $tax_id = $SWISSFULL2TAXID{$species}; return $tax_id if $tax_id; unless (%SWISSFULL2TAXID){ _connect() unless $connection; carp "Loading swissfull->tax_id cache\n" if $main::opt_debug; my $sth = $connection->prepare (q{ select tax_id, fulluppername from OPS$WFL.V_swiss_fullname where tax_id is not null }) || die "$DBI:errstr"; $sth->execute || die "$DBI:errstr"; while (my ($tax_id,$full_os) = $sth->fetchrow_array){ printf "got :%7d, %s\n",$tax_id,$full_os if $main::opt_debug>4; $SWISSFULL2TAXID{$full_os}=$tax_id; } $sth->finish(); } return $SWISSFULL2TAXID{uc($species)}; } sub taxid2swissosline { &_print_args; my $tax_id = shift; my $osline; unless ($FETCH_TAXID2SWISSOSLINEBULK){ _connect() unless $connection; $FETCH_TAXID2SWISSOSLINEBULK = $connection->prepare (q{ select fullname from OPS$WFL.Tmp_swiss_fullname where tax_id = ? }) || die "$DBI:errstr"; } if ($FETCH_TAXID2SWISSOSLINEBULK->execute($tax_id)){ ($osline) = $FETCH_TAXID2SWISSOSLINEBULK->fetchrow_array; return $osline; } else { return undef; } } sub taxid2ncbiosline { &_print_args; my $tax_id = shift; my $osline; unless ($FETCH_TAXID2NCBIOSLINEBULK){ _connect() unless $connection; $FETCH_TAXID2NCBIOSLINEBULK = $connection->prepare (q{ select fullname from OPS$WFL.Tmp_ntx_fullname where tax_id = ? }) || die "$DBI:errstr"; } if ($FETCH_TAXID2NCBIOSLINEBULK->execute($tax_id)){ ($osline) = $FETCH_TAXID2NCBIOSLINEBULK->fetchrow_array; return $osline; } else { return undef; } } sub taxid2osline { &_print_args; my $tax_id = shift; return taxid2swissosline($tax_id) || taxid2ncbiosline($tax_id); } sub swiss_fullos2tax_idbulk { &_print_args; my $os = shift; my $tax_id; unless ($FETCH_SWISSFULL2OSLINE){ _connect() unless $connection; $FETCH_SWISSFULL2OSLINE = $connection->prepare (q{ select tax_id from OPS$WFL.Tmp_swiss_fullname where fulluppername = (?) }) || die "$DBI:errstr"; } if ($FETCH_SWISSFULL2OSLINE->execute(uc($os))){ ($tax_id) = $FETCH_SWISSFULL2OSLINE->fetchrow_array; return $tax_id; } else { return undef; } } sub swiss_fullos2osline { &_print_args; my $os = shift; my $osline; unless ($FETCH_SWISSFULL2OSLINE){ _connect() unless $connection; $FETCH_SWISSFULL2OSLINE = $connection->prepare (q{ select fullname from OPS$WFL.Tmp_swiss_fullname where fulluppername = ? }) || die "$DBI:errstr"; } if ($FETCH_SWISSFULL2OSLINE->execute(uc($os))){ ($osline) = $FETCH_SWISSFULL2OSLINE->fetchrow_array; return $osline; } else { return undef; } } sub ncbi_fullos2osline { &_print_args; my $os = shift; my $osline; unless ($FETCH_NCBIFULL2OSLINE){ _connect() unless $connection; $FETCH_NCBIFULL2OSLINE = $connection->prepare (q{ select fullname from OPS$WFL.Tmp_ntx_fullname where fulluppername = upper(?) }) || die "$DBI:errstr"; } if ($FETCH_NCBIFULL2OSLINE->execute(uc($os))){ ($osline) = $FETCH_NCBIFULL2OSLINE->fetchrow_array; return $osline; } else { return undef; } } sub fetch_by_tax_id { &_print_args; my $self = shift; my $tax_id = shift; my $longline; # taxnodes as returned from oracle my @nodes; # array of taxnodes my $result; # result: either undef or SWISS::OCs object if ($CACHING && ($result=$TAXID2OC{$tax_id})){ return $result; } unless ($FETCH_OC){ _connect() unless $connection; $FETCH_OC = $connection->prepare (q{ select swiss_ocline(?) from dual }) || die "$DBI:errstr"; } $FETCH_OC->execute($tax_id); ($longline) = $FETCH_OC->fetchrow_array; return undef unless $longline; @nodes = SWISS::TextFunc->listFromText($longline, ';\s*', '.\s*'); if (@nodes){ $result = new SWISS::OCs(); $result->add(@nodes); if ($CACHING){ %TAXID2OC=() if $TAXID2OC_counter++ > 1000; $TAXID2OC{$tax_id}=$result; } return $result; } return undef; } sub fetch_by_tax_id_do_not_use_this_anymore { &_print_args; my $self = shift; my $tax_id = shift; my $result; if ($CACHING && ($result=$TAXID2OC{$tax_id})){ return $result; } unless ($FETCH_TAXANDPARENT){ _connect() unless $connection; $FETCH_TAXANDPARENT = $connection->prepare(q{ select tax_id, rank from datalib.ntx_tax_node where hidden = 0 and not rank in ('species','subspecies','varietas','forma') start with tax_id = ? connect by tax_id = prior parent_id }) || die "$DBI:errstr"; } my @nodes=(); $FETCH_TAXANDPARENT->execute($tax_id); while(my ($id,$rank)=$FETCH_TAXANDPARENT->fetchrow_array){ my $name = tax_id2scientific_name($id); unshift @nodes,$name; } if (@nodes){ $result = new SWISS::OCs(); $result->add(@nodes); if ($CACHING){ %TAXID2OC=() if $TAXID2OC_counter++ > 1000; $TAXID2OC{$tax_id}=$result; } return $result; } return undef; } sub oscode2tax_id { &_print_args; my $oscode = shift; unless (%SWISSID2TAXID){ _connect() unless $connection; carp "Loading oscode->tax_id cache\n" if $main::opt_debug; my $sth = $connection->prepare(q{ select distinct oscode, tax_id from ops$wfl.Swiss_synonym where tax_id is not null }) || die "$DBI:errstr"; $sth->execute || die "$DBI:errstr"; while (my ($sid,$tid) = $sth->fetchrow_array){ $SWISSID2TAXID{$sid}=$tid; } $sth->finish(); } return $SWISSID2TAXID{$oscode}; } sub tax_id2swiss_scientific { &_print_args; my $tax_id = shift; unless ($FETCH_SWISS_SCI){ _connect() unless $connection; $FETCH_SWISS_NAME = $connection->prepare (q{ select name_txt from ops$wfl.swiss_synonym where tax_id = ? and name_class = 'scientific name' }); } if ($FETCH_SWISS_NAME->execute($tax_id)){ my ($sci_name) = $FETCH_SWISS_NAME->fetchrow_array; return $sci_name; } else { return tax_id2ncbi_scientific($tax_id); } } sub tax_id2ncbi_scientific { &_print_args; my $tax_id = shift; unless ($FETCH_SCI_NAME){ _connect() unless $connection; $FETCH_SCI_NAME = $connection->prepare(q{ select name_txt from ops$wfl.v_ntx_synonym where tax_id = ? and name_class = 'scientific name' }) || die "$DBI:errstr"; } if ($FETCH_SCI_NAME->execute($tax_id)){ my ($sci_name) = $FETCH_SCI_NAME->fetchrow_array; return $sci_name; } else { return undef; } } sub tax_id2scientific_name { &_print_args; my $tax_id = shift; return tax_id2swiss_scientific($tax_id) || tax_id2ncbi_scientific($tax_id); } sub tax_id2superregnum { &_print_args; my $tax_id = shift; unless ($FETCH_SUPERREGNUM){ _connect() unless $connection; $FETCH_SUPERREGNUM = $connection->prepare (q{select sr.superregnum from ops$wfl.Swiss_superregnum sr where sr.tax_id in (select n.tax_id from DATALIB.Ntx_tax_node n start with n.tax_id = ? connect by n.tax_id = prior n.parent_id) }) || die "$DBI:errstr"; } if ($FETCH_SUPERREGNUM->execute($tax_id)){ my ($superregnum) = $FETCH_SUPERREGNUM->fetchrow_array; return $superregnum; } else { return undef; } } sub emblacs2tax_id { &_print_args; my @emblacs = @_; unless ($FETCH_TAXID_BY_EMBLAC){ _connect() unless $connection; $FETCH_TAXID_BY_EMBLAC = $connection->prepare( 'select organism as taxid '. ' from datalib.sourcefeature,datalib.seqfeature,datalib.dbentry '. ' where sourcefeature.featid = seqfeature.featid '. ' and seqfeature.bioseqid = dbentry.bioseqid '. ' and dbentry.primaryacc# = ?' ) || die "$DBI:errstr"; } my %tax_ids = (); foreach $emblac (@emblacs) { $FETCH_TAXID_BY_EMBLAC->execute($emblac) || die "$DBI:errstr"; if ($FETCH_TAXID_BY_EMBLAC->rows()){ while (($tax_id) = $FETCH_TAXID_BY_EMBLAC->fetchrow_array){ $tax_ids{$tax_id}++; } } else { #print STDERR "!!!!DEAD primary emblac $emblac\n" if $main::opt_warn; } } return keys %tax_ids; } DESTROY { _disconnect() if $dbh; } 1; swissknife-1.67/lib/SWISS/OCs.pm0000644000175100017510000000372610366115237016232 0ustar moellermoellerpackage SWISS::OCs; use vars qw($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-1.67/lib/SWISS/dr_ord0000644000175100017510000000236211040130670016363 0ustar moellermoeller#============== #DR lines order #============== #Last updated: June 13, 2008 # EMBL 0 PIR 1 RefSeq 1 UniGene 1 PDB 1 PDBsum 1 HSSP 1 SMR 1 DisProt 1 DIP 1 IntAct 1 MEROPS 1 PeroxiBase 1 PptaseDB 1 REBASE 1 GlycoSuiteDB 1 PhosphoSite 1 PhosSite 1 SWISS-2DPAGE 1 2DBase-Ecoli 1 Aarhus/Ghent-2DPAGE 1 ANU-2DPAGE 1 COMPLUYEAST-2DPAGE 1 Cornea-2DPAGE 1 DOSAC-COBS-2DPAGE 1 ECO2DBASE 1 HSC-2DPAGE 1 OGP 1 PHCI-2DPAGE 1 PMMA-2DPAGE 1 Rat-heart-2DPAGE 1 REPRODUCTION-2DPAGE 1 Siena-2DPAGE 1 World-2DPAGE 1 PeptideAtlas 1 ProMEX 1 Ensembl 1 GeneID 1 GenomeReviews 2 KEGG 1 NMPDR 1 TIGR 1 VectorBase 1 AGD 1 BuruList 1 CGD 2 CYGD 1 dictyBase 2 EchoBASE 1 EcoGene 2 euHCVdb 1 FlyBase 2 GeneDB_Spombe 2 GeneFarm 1 Gramene 2 H-InvDB 1 HGNC 2 HPA 1 LegioList 1 Leproma 2 ListiList 1 MaizeGDB 2 MIM 1 MGI 2 MypuList 1 Orphanet 2 PharmGKB 1 PhotoList 1 PseudoCAP 1 RGD 2 SagaList 1 SGD 2 StyGene 2 SubtiList 2 TAIR 1 TubercuList 1 WormBase 2 WormPep 1 ZFIN 2 HOGENOM 1 HOVERGEN 1 BioCyc 1 Reactome 1 BindingDB 1 DrugBank 2 LinkHub 1 ArrayExpress 1 CleanEx 1 GermOnline 1 GO 2 HAMAP 1 InterPro 2 Gene3D 2 PANTHER 2 Pfam 2 PIRSF 2 PRINTS 2 ProDom 2 SMART 2 TIGRFAMs 2 PROSITE 2 swissknife-1.67/lib/SWISS/ACs.pm0000644000175100017510000000647110366115237016214 0ustar moellermoellerpackage 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. $self->sort(); return 1; } 1; # says use was ok __END__ =head1 Name SWISS::ACs =head1 Description B represents the AC (accession) lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The SWISS-PROT format has recently been changed to multiple AC lines. This module will read Ordinary AC lines AC P10585; The old temporary format (for internal use only) AC Q57333; O08291; O08202; O08292; O08203; O08293; O08204; O08294; ** O08205; O08295; O08206; O08296; O08207; O08297; O08208; O08298; ** O08213; and the new format. AC Q57333; O08291; O08202; O08292; O08203; O08293; O08204; O08294; AC O08205; O08295; O08206; O08296; O08207; O08297; O08208; O08298; AC O08213; But, SWISS::ACs will DROP funny ** comment lines that are sometimes found following an AC line: AC Q48558; P71434; ** MERGED 2 TREMBL ENTRIES. This module will always write the new format with multiple AC lines. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C This is an array containing a list of all the accession numbers associated with this entry. The first member will be the primary accession number, and any following are the secondary accession numbers. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item sort This method sorts the secondary AC numbers alphanumerically, i.e. all but the first. The primary AC number must never be sorted. =back swissknife-1.67/lib/SWISS/DRs.pm0000644000175100017510000002451310366115237016233 0ustar moellermoellerpackage SWISS::DRs; use vars qw($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 ($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; } } $newText .= ($indent . $tag . " " . (join "; ", grep {!/_HIDDEN_/ && !/$SWISS::TextFunc::evidencePattern/} @$dr) . '.'); # add evidence tags $newText .= $self->getEvidenceTagsString($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 for my $ty ([\@visibleDR, 1], [\@hiddenDR, 2]) { my ($drtype, $field_number) = @$ty; 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 {$$_[1]} $self->get('EMBL'); return SWISS::TextFunc->uniqueList(@emblacs); } # * Private methods/functions sub _dbIndex { my $dbname = uc shift; my $index; $index = index $DBorder, ' ' . $dbname . ' '; if ($main::opt_warn) { if ($index == -1) { carp "Database name $dbname not found."; } } # unknown databases should be at the end, not at the beginning if ($index == -1) { $index = length $DBorder; } return $index; } # * Filter functions # true if the first element of a DR line (the DB name) matches $dbTargetName # false otherwise sub dbName{ my ($dbTargetName) = @_; return sub { my $ref = shift; my $dbSourceName = @{$ref}[0]; return ($dbSourceName =~ /^$dbTargetName$/); } } # false if the first element of a DR line (the DB name) matches $dbTargetName # true otherwise sub notDbName{ my ($dbTargetName) = @_; return sub { my $ref = shift; my $dbSourceName = @{$ref}[0]; return ($dbSourceName !~ /^$dbTargetName$/); } } sub deleteUnlessEvidenceCategories { my ($self, $evidenceCategories, @patterns) = @_; my @result; my ($i, $pat, $element); # do nothing if the list is empty unless ($self->size() > 0) { return $self->elements(); }; # If first list element is an array if (ref @{$self->list()}[0] eq 'ARRAY') { ELEMENT: foreach $element (@{$self->list()}) { # if $element has an evidence tag with a category in # $evidenceCategories, don't delete it my $evidenceTagPosition = SWISS::ListBase::evidenceTagPosition($element); if ((defined $$element[$evidenceTagPosition]) && ($$element[$evidenceTagPosition] =~ /E[$evidenceCategories]/)) { CORE::push(@result, $element); next ELEMENT; }; # do the actual deletion if pattern matches for ($i=0; $i <= $#patterns; $i++) { if ($patterns[$i] && ($$element[$i] !~ /^$patterns[$i]$/)){ CORE::push(@result, $element); next ELEMENT; } } }; return $self->set(@result); } else { # An undefined data type carp "deleteUnlessEvidenceCategory is currently not implemented for elements of type " . ref @{$self->list}[0]; return undef; } } 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 Writing methods =over =item deleteUnlessEvidenceCategories $evidenceCategories, @patterns Like del, but deletes an item only if the item has no evidence tags, or if the evidence tags are not in one of the categories given in $evidenceCategories. Example: $entry->DRs->deleteUnlessEvidenceCategories('CA', 'FlyBase') will only delete Flybase DR lines which do not have the evidence category 'A' or 'C'. =back =head2 Filter functions =over =item dbName($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: $entry->DRs->add(['_HIDDEN_', 'PS12345', 'XXX_PAT', 'FALSE_POS_1']); swissknife-1.67/lib/SWISS/OX.pm0000644000175100017510000000222310366115237016063 0ustar moellermoellerpackage SWISS::OX; use vars qw($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 . $self->getEvidenceTagsString; } 1; __END__ =head1 Name SWISS::OX =head1 Description B represents one tax id from the OX line. The container object holding all tax ids is SWISS::OXs. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C One tax id. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head1 Example see documentation of OXs.pm swissknife-1.67/lib/SWISS/DEs.pm0000644000175100017510000005275011037664070016222 0ustar moellermoellerpackage SWISS::DEs; use vars qw($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:/) { # 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:/ ? 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; } } } 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) = @_; my $de = SWISS::DE->fromText($str); $de->category($cat); $de->type($type); $de->hide_in_old($hide_in_old); $self->push($de); }, 'Contains' => sub { my ($str,$is_new_list,$cat,$type,$hide_in_old) = @_; 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); $obj->item(-1)->push($de); }, 'Includes' => sub{ my ($str,$is_new_list,$cat,$type,$hide_in_old) = @_; 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); $obj->item(-1)->push($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 = {}; 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 } if (/(Fragments?)/) { $self->hasFragment(my $flag = $1);# !($1) doesn't work } $_; } sort {$b cmp $a} split '; *', $flags; next; } $cat = $1 if $line =~ s/^ *(\w+): *//;# category: RecName: | AltName: my ($type,$val) = split '= *', $line; $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 $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) if $by_mode->{$mode}; $is_new_list = 0; } foreach my $f (grep {/^precursor/i} @flags) { # to be compatible with old format!: # if there are flags to be added to main name: # Note: DE text method will show 'precursor', toText will hide it # this was due to the constraint of using sk to convert new format back # into old one during a transitory period! my $str = $self->head->text . ' '.lc($f); $self->head->text($str); # at the same time store precursor flag $self->{isPrecursor} = 1; } } 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 (old format) into clean new names # Note: in old format name and their type were mixed '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 $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'); $str_out .= (($type ne 'Short' && $type ne 'EC') || $cat ne $last_cat ? "$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; } } } # build flags 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 { 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-1.67/lib/SWISS/Stars.pm0000644000175100017510000002702710366115237016642 0ustar moellermoellerpackage 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::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 $type = ref($self) || carp "Ok, $self is not an object of mine!"; 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"}) { return $self->{$name} = $fullname->fromText($self->{_textRef}); } else { # check if name is a valid object tag if (length $name == 2) { $self->{$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; # Recursively call toText for the subobjects foreach $subObject (grep {length $_ == 2} sort keys %$self) { if ($self->{$subObject}->{_dirty}) { $self->{$subObject}->toText($self->{_textRef}, $subObject); $self->{_dirty} = 1; } } if ($self->{_dirty}) { # add header, unless it's already there unless ( ${$self->{_textRef}} =~ /$headerPattern/) { if ($self->aa->size) { ${$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 footer, unless it's already there unless ( ${$self->{_textRef}} =~ /$footerPattern/) { if (${$self->{_textRef}} =~ /\n\*\*\S{2} .*/) { ${$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; # Make sure all subobjects are parsed if $force is set. if ($force) { @subObjects = ${$self->{'_textRef'}} =~ /\*\*(\w\w) .*/g; @subObjects = SWISS::TextFunc->uniqueList(@subObjects); } else { @subObjects = grep {length $_ == 2} sort keys %$self; } # Recursively call the subobjects foreach $subObject (@subObjects) { $self->$subObject()->{_dirty} = 1; $self->$subObject()->update(); } $self->{_dirty} = 1; return 1; } sub insertLineGroup { my ($class, $textRef, $text, $tag) = @_; my ($currentTag); # remove old lines with the tag in question $$textRef =~ s/^(\*\*$tag .*\n)//gm; # find the insertion position # [This should be optimised!] while ($$textRef =~ /^\*\*(..).*/gm) { if ($1 gt $tag) { $$textRef = $` . $text . $& . $'; return 1; } }; $$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; my $subObject; # Recursively call sort for the subobjects 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-1.67/lib/SWISS/TextFunc.pm0000644000175100017510000004146310475633110017302 0ustar moellermoellerpackage SWISS::TextFunc; use vars qw( $AUTOLOAD @ISA @EXPORT_OK @lineObjects @linePattern %linePattern $evidencePattern $evidencePatternReversed $textWrapPattern1 $textWrapPattern2 $lineLength $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 = '\{(E[ACIP]\d+\,?)*\}'; # and its reversed form for the parsing of the DE lines $evidencePatternReversed = '\}(\,?\d+[ACIP]E)*\{'; # General pattern and last-resort pattern # for wrapping text fields. # Cut either at a whitespace that is not part of an EC or TC # number, e.g. "(EC 1.1.1.1)"; or at a dash that is followed # either by a letter/digit or an opening round or square bracket # (so as not to cut at "->" or "--" or "-," etc). # Also do not cut at a dash that is preceeded by a space, # because this dash might indicate a suffix. $textWrapPattern1 = '(?\-])'; $lineLength = 75; $lineLengthStar = 80; $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; # produce one funck off long string $text = (join $sep, @{$list}) . $end; # 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 = ''; # @separators might be empty # as a last resort, wrap anywhere push @separators, $textWrapPattern1, $textWrapPattern2, ''; # use multiple separators for some FT lines my ($separator1, $border, $separator2, $longWordChar); if (ref $separators[0] eq "ARRAY") { ($separator1, $border, $separator2, $longWordChar) = @{$separators[0]}; $separators[0] = $separator1; } $prefix=$prefix1; TEXT:while ($text) { # use multiple separators for some FT lines $width = $columns - length ($prefix); if (defined($separator1) and $separators[0] eq $separator1) { if (($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 $w1 = $cutPos - $sepLength; if ($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; my $inEnd; my $inRef; my $inDR; 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-1.67/lib/SWISS/KW.pm0000644000175100017510000000220110366115237016052 0ustar moellermoellerpackage 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 . $self->getEvidenceTagsString; } 1; __END__ =head1 Name SWISS::KW =head1 Description Each KW object represents one keyword. The container object for all keywords of an entry is SWISS::KWs =head1 Inherits from SWISS::BaseClass =head1 Attributes =over =item C The text of the keyword. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back swissknife-1.67/lib/SWISS/OGs.pm0000644000175100017510000000650010366115237016227 0ustar moellermoellerpackage SWISS::OGs; use vars qw($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 = ''; my $lastElementRef; my $listRef; @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, $SWISS::TextFunc::linePattern{'OG'}); } # OGs must never be sorted, overwrite the inherited sort method. sub sort { return 1; } 1; __END__ =head1 Name SWISS::OGs =head1 Description B represents the OG lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OGs object is a container object which holds a list of SWISS::OG objects. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each list element is a SWISS::OG object. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back swissknife-1.67/lib/SWISS/GN.pm0000644000175100017510000000406110366115237016043 0ustar moellermoellerpackage SWISS::GN; use vars qw($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 $orfname; } 1; __END__ =head1 Name SWISS::GN.pm =head1 Description B represents one gene name from the GN line. The container object for several synonym gene names is SWISS::GeneGroup. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C One gene name. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Reading/Writing methods =over =item toMixedCase(@regexps) Convert gene names to mixed case, according to one or more regular expressions. This is typically useful for converting uppercase ORF numbers to mixed case. E.g. the E.coli gene "B1563" converted with the regexp '(b(\d{4}(\.\d)?))' will yield the gene name "b1563". The method also supports fused gene names, e.g. "B0690/B0691" is converted to "b0690/b0691". The method changes the text of the SWISS::GN object and also returns the new text value. =back swissknife-1.67/lib/SWISS/GNs.pm0000644000175100017510000005303610366115237016234 0ustar moellermoellerpackage SWISS::GNs; use vars qw($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; $p = -1; if ($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-1.67/lib/SWISS/CRC64.pm0000644000175100017510000000443110366115237016321 0ustar moellermoellerpackage 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-1.67/lib/SWISS/EntryStore/0000755000175100017510000000000011040133466017310 5ustar moellermoellerswissknife-1.67/lib/SWISS/EntryStore/Release.pm0000644000175100017510000000225010366115237021233 0ustar moellermoeller# ************************************************************* # # Package: SWISS/knife # # Purpose: Fast access to SWISS-PROT entries via NDBM indexes # flat files. # # Usage: use SWISS::EntryStore::Release qw(%WR); # my $entry1 = $WR{'P39000'}; # # ************************************************************* package SWISS::EntryStore::Release; use vars qw(@ISA @EXPORT_OK %WR); use Env qw(WR INDEXES OSTYPE); use Exporter; use Fcntl; use Carp; use strict; use SWISS::Entry; use SWISS::EntryStore::Index; BEGIN { @EXPORT_OK = qw(%WR); @ISA = qw(Exporter); } die "Environment variable 'WR' is not defined.\n". "It should point to the current SWISS-PROT workrelease.\n" unless $WR; die "Environment variable 'OSTYPE' is not defined.\n". "It should contain the name of the operating system.\n" unless $OSTYPE; die "Environment variable 'INDEXES' is not defined.\n". "It should point to the directory where all indexes live.\n" unless $INDEXES; my ($wrname)=$WR=~m!/(\w+?)$!; tie %WR, 'SWISS::EntryStore::Index', {File => $WR, Index => $INDEXES."$wrname.spac.$OSTYPE", Access => O_RDWR|O_CREAT, }; swissknife-1.67/lib/SWISS/EntryStore/Index.pm0000644000175100017510000001326210366115237020727 0ustar moellermoeller# ************************************************************* # # Package: SWISS/knife # # Purpose: Fast access to a SWISS-PROT style flatfile # via NDBM index. # # Usage: use SWISS::EntryStore::Index; # tie %myhash, 'SWISS::EntryStore::Index', # {File => 'myswissfile.sp', # Index => 'myswissindex'.$ENV{OSTYPE}, # Access => O_RDWR|O_CREAT, # }; # # my $entry1 = $myhash{'P39000'}; # # foreach $entry (values %myhash){ # print $entry->toText(); # } # ************************************************************* package SWISS::EntryStore::Index; use Fcntl; use NDBM_File; use FileHandle; use Carp; use PROSITE::Entry; %MANDATORY_PARAMS = ( File => "Please specify a file name.\n", Index => "Please specify an index name.\n", ); %DEFAULT_PARAMS = ( Access => O_RDWR|O_CREAT, FileAccess => O_RDONLY, ); $PERMISSION = 0664; # RDONLY RDWR APPEND CREAT EXCL TRUNC sub TIEHASH { my $class = shift; my $params = shift; my %tmp = %$params; my $self = \%tmp; bless $self, $class; # set not specified parameters to their default foreach $param (keys %DEFAULT_PARAMS){ next if exists $self->{$param}; $self->{$param} = $DEFAULT_PARAMS{$param}; } # check if all the required parameters are set foreach $param (keys %MANDATORY_PARAMS){ next if $self->{$param}; die "Mandatory argument '$param' is missing. ". $MANDATORY_PARAMS{$param}; } $self->{FILE} = new FileHandle $self->{File}, $self->{FileAccess}; unless ($self->{FILE}){ croak "Cannot open file '$self->{File}'"; return 0; } $self->_build_index_files() if $self->_check_index_files(); my %INDEX; my $ok=tie(%INDEX, NDBM_File, $self->{Index}, $self->{Access}, $PERMISSION); if ($ok){ carp "Opened index '$self->{Index}'" if $main::opt_debug; $self->{INDEX}=\%INDEX; } else { croak "Cannot open index '$self->{Index}'" if $main::opt_debug; return 0; } return $self; } sub FETCH { my $self = shift; my $key = shift; # lookup the file position in the hash my $fpos = $self->{INDEX}->{$key}; # now fetch the entries from the flatfile if (defined $fpos){ my $save=$/; $/ = "\/\/\n"; my $fh=$self->{FILE}; seek $fh, $fpos, 0; my $flat=<$fh>; $/=$save; # we have got the flat entry and stuff it into an entry object if ($flat){ my $entry = SWISS::Entry->fromText($flat); return $entry; } } return undef; } sub STORE { my $self = shift; die "Storing is not permitted. Sorry"; } sub CLEAR { my $self = shift; die "Deleting is not permitted. Sorry"; } sub EXISTS { my $self = shift; my $key = shift; my $fpos = $self->{INDEX}->{$key}; return defined($fpos); } sub FIRSTKEY { my $self = shift; my $a = keys %{$self->{INDEX}}; return scalar each %{$self->{INDEX}} } sub NEXTKEY { my $self = shift; my $key = shift; return scalar each %{$self->{INDEX}} } # * private procedures sub _check_index_files { my $self = shift; my $index_name = $self->{Index}; # Check if both index files exist unless (-e "$index_name.dir"){ return "Can't find index file '$index_name.dir'"; } unless (-e "$index_name.pag"){ return "Can't find index file '$index_name.pag'"; } # Check if index is up-to-date my $idx_mtime = (stat "$index_name.dir")[9]; my $fh = $self->{FILE}; my $dat_mtime = (stat $fh)[9]; if ($dat_mtime > $idx_mtime) { return "Index '$index_name' is outdated."; } return 0; } sub _build_index_files { my $self = shift; # because some user may try to use the indices while # we are rebuilding them, we build them in a temporary place my $index_name=$self->{Index}; my $temp_name="$index_name.temp"; # but, we have to check if there are already temp files # which we take as a hint that somebody else is building them currently # and die gracefully. if (-e "$temp_name.dir" || -e "$temp_name.pag"){ die "someone is already rebuilding index $temp_name"; } # link the (empty) index file to the hash %INDEX, # and create the files $temp_name.dir and .pag, if necessary my %TMPINDEX; tie(%TMPINDEX, NDBM_File, $temp_name, O_RDWR|O_CREAT, 0600); my $fh = $self->{FILE}; my $save = $/; $/="\/\/\n"; # scan the flatfile and save the filepositions of the beginning # of every entry in the index my $curpos; # current position in flatfile my $count=0;# entry count my $flat; # flat entry for ($curpos = -1 ; defined($flat = <$fh>); $curpos = tell $fh) { my $id; # id of the current entry my $ac; # accession number(s) of the current entry $count++; ($id)=$flat=~/^ID\s\s\s(\w+)/ or next; $TMPINDEX{$id}=$curpos; $flat=~s/^[^\n]+\n//; ($ac)=$flat=~/^AC\s\s\s(\w+)/ or next; $TMPINDEX{$ac}=$curpos; # my submission for the totally obfuscated perl code contest: if ($flat=~/^(AC.*\n)+(\*\*\s\s\s[OPQ]\d.*\n)*/m){ $_ = $&; s/AC\s+//mg; s/\*\*\s+//mg; s/\s//mg; my @acs = split(';',$_); shift @acs; @TMPINDEX{@acs} = ($curpos) x @acs if @acs; } # actually, the secondary accession numbers are stored as well } untie %TMPINDEX; $/=$save; `mv $temp_name.dir $index_name.dir`; `mv $temp_name.pag $index_name.pag`; unless (-e "$index_name.dir" && -e "$index_name.pag"){ die "$0: couldnt built the indexes\n"; } chmod $PERMISSION, "$index_name.dir", "$index_name.pag"; carp "Build index '$index_name' ($count entries).\n" if $main::opt_debug; } # * debuggin sub _dump_index { my $self = shift; while (my ($key,$value) = each %{$self->{INDEX}}){ print "$key $value\n"; } } 1; swissknife-1.67/lib/SWISS/EntryStore/SPTR.pm0000644000175100017510000000222407563756337020465 0ustar moellermoeller# ************************************************************* # # Package: SWISS/knife # # Purpose: Fast access to SPTR entries via NDBM indexes # flat files. # # Usage: use SWISS::EntryStore::SPTR qw(%SPTR); # my $entry1 = $SPTR{'E1184836'}; # # $Revision: 1.1 $ # $State: Exp $ # $Date: 2002/11/11 16:37:51 $ # $Author: gatt $ # $Locker: $ # # ************************************************************* package SWISS::EntryStore::SPTR; use vars qw(@ISA @EXPORT_OK %SPTR); use Env qw(INDEXES OSTYPE); use Exporter; use Fcntl; use Carp; use strict; use SWISS::Entry; use SWISS::EntryStore::Index; BEGIN { @EXPORT_OK = qw(%SPTR); @ISA = qw(Exporter); } die "Environment variable 'OSTYPE' is not defined.\n". "It should contain the name of the operating system.\n" unless $OSTYPE; die "Environment variable 'INDEXES' is not defined.\n". "It should point to the directory where all indexes live.\n" unless $INDEXES; tie %SPTR, 'SWISS::EntryStore::Index', {File => '/net/nfs0/vol2/swissprot/projects/sptr/data/sptr.txl', Index => $INDEXES."sptr.ac.$OSTYPE", Access => O_RDWR|O_CREAT, }; swissknife-1.67/lib/SWISS/OG.pm0000644000175100017510000000243310366115237016045 0ustar moellermoellerpackage 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 $self->text =~ /Plasmid/i; } 1; __END__ =head1 Name SWISS::OGs =head1 Description B represents one organelle or plasmid name from the OG line. The container object holding all organelle or plasmid names is SWISS::OGs. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C One OG line element. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Specific methods =over =item isPlasmid =back swissknife-1.67/lib/SWISS/PE.pm0000644000175100017510000000240210615335130016031 0ustar moellermoellerpackage SWISS::PE; use vars qw($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 ($$textRef =~ /($SWISS::TextFunc::linePattern{'PE'})/m){ $text = $1; $self->{indentation} += $text =~ s/^ //; $text = SWISS::TextFunc->cleanLine($text); if ($text =~ s/($SWISS::TextFunc::evidencePattern)//) { $self->evidenceTags($1); } $self->text($text); } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; if ($self->text) { return $self->text . $self->getEvidenceTagsString; } } 1; __END__ =head1 Name SWISS::PE =head1 Description Indicates what kind of evidence there is for the existence of a protein. =head1 Inherits from SWISS::BaseClass =head1 Attributes =over =item C The type of evidence. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back swissknife-1.67/lib/SWISS/CCseq_caution.pm0000644000175100017510000000566310626343425020271 0ustar moellermoellerpackage SWISS::CCseq_caution; use vars qw($AUTOLOAD @ISA); use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; use SWISS::BaseClass; BEGIN { @ISA = ('SWISS::ListBase'); } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::CCseq_caution; my $text = $$textRef; $self->initialize(); $text =~ s/ +/ /g; $text =~ s/\s*-!-.*?:\s*//; while (length $text) { if ($text =~ s/^\s*Sequence=(.*?); Type=(.*?);(?: Positions=(.*?);)?(?: Note=(.*?);)?(?:\s*|\Z)//s) { my ($sequence, $type, $positions, $note, $evidence) = ($1, $2, $3, $4); my $arg = new SWISS::BaseClass; if (($evidence) = $sequence =~ /($SWISS::TextFunc::evidencePattern)/m) { my $quotedEvidence = quotemeta $evidence; $sequence =~ s/$quotedEvidence//m; } $arg->{'sequence'} = $sequence; $arg->{'type'} = $type; $arg->{'positions'} = $positions if defined $positions; $arg->{'note'} = $note if defined $note; $arg->evidenceTags($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 .= ";\n"; } } $text; } 1; __END__ =head1 Name SWISS::CCinteraction =head1 Description B represents a comment on the topic 'INTERACTION' within a Swiss-Prot or TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Comments on other topics are stored in other types of objects, such as SWISS::CC (see SWISS::CCs for more information). Collectively, comments of all types are stored within a SWISS::CCs container object. Each element of the list is a hash with the following keys: accession identifier xeno NbExp IntAct (array reference) =head1 Inherits from SWISS::ListBase.pm =head1 Methods =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back swissknife-1.67/lib/SWISS/Refs.pm0000644000175100017510000000367310366115237016446 0ustar moellermoellerpackage SWISS::Refs; use vars qw($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-1.67/lib/SWISS/BaseClass.pm0000644000175100017510000002241610366115237017403 0ustar moellermoellerpackage 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 = @_; $self->{'evidenceTags'} = '{' . (join ',', @tags) . '}'; $self->{'_dirty'} = 1; return; } sub addEvidenceTag { my $self = shift; my $tag = shift; unless ($self->{'evidenceTags'} =~ /[\{\,]$tag[\}\,]/) { if ($self->{'evidenceTags'} eq '{}') { $self->{'evidenceTags'} = '{' . $tag . '}'; } else { $self->{'evidenceTags'} =~ s/\}/\,$tag\}/; } } $self->{'_dirty'} = 1; return; } sub deleteEvidenceTag { my $self = shift; my $tag = shift; $self->{'evidenceTags'} =~ s/([\{\,])$tag([\,\}])/$1$2/; $self->{'evidenceTags'} =~ s/\,\,/\,/; $self->{'evidenceTags'} =~ s/\,\}/\}/; $self->{'evidenceTags'} =~ s/\{\,/\{/; $self->{'_dirty'} = 1; return; } sub hasEvidenceTag { my $self = shift; my $tag = shift; return $self->{'evidenceTags'} =~ /[\{\,]$tag[\}\,]/; } sub getEvidenceTags { my $self = shift; my $tmp = $self->{'evidenceTags'}; $tmp =~ tr/\{\}//d; return 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-1.67/lib/SWISS/CCbpc_properties.pm0000644000175100017510000001112210366115237020761 0ustar moellermoellerpackage 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'], ); %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 (@events, @newEvents, %events, $topic); 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; #grab any evidence tags my $ev = $ltext =~ s/\s*($SWISS::TextFunc::evidencePattern)// ? $1 : undef; if ($ltext =~ s/^(\S+)=// and length $ltext) { @content = [$1, $ltext, $ev]; } elsif (length $ltext) { @content = [undef, $ltext, $ev]; } while ($text =~ s/^(\S+)=(.*?)\s*(;\s*|\Z)//) { #take Note=, Vmax=, ... my ($field, $ltext) = ($1, $2); next unless length $ltext; my $ev = $ltext =~ s/\s*($SWISS::TextFunc::evidencePattern)// ? $1 : undef; push @content, [$field, $ltext, $ev]; } $self->{$property} = \@content; } else { #dangling text my ($ltext) = $text =~ s/(.*?)\s*(;\s*|\Z)//; my $ev = $ltext =~ s/\s*($SWISS::TextFunc::evidencePattern)// ? $1 : undef; push @{$self->{$last_property}}, [undef, $ltext, $ev]; } } $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, $value, $ev) = @$item; $value .= $ev if defined $ev; 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 fields in a given property in this comment. Each field is a reference to an array of [$field, $text, $evidence_tags]. $field is undefined for unnamed fields. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toString Returns a string representation of this comment. =back swissknife-1.67/lib/SWISS/CC.pm0000644000175100017510000001124210727215623016024 0ustar moellermoellerpackage SWISS::CC; use vars qw($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 ); } 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::CC; my $text = $$textRef; my ($topic, $comment, $evidence); if ($text ne '') { # split into topic and comment. if ($text =~ /\-\!\-\s+(.*?):\s*(.*)$/x ){ $topic = $1; $comment = $2; } else { $topic = ''; $comment = $text; } # Parse for evidence tags if (($evidence) = $comment =~ /($SWISS::TextFunc::evidencePattern)/m) { my $quotedEvidence = quotemeta $evidence; $comment =~ s/$quotedEvidence//m; } $self->{topic} = $topic; $self->{comment} = $comment; $self->evidenceTags($evidence); } else { $self->initialize; }; $self->{_dirty} = 0; return $self; } sub toString { my $self = shift; my $topic = $self -> {topic}; my $comment = $self -> {comment}; my $evidence = $self -> evidenceTags; my $text = "CC -!- "; if ($topic) { $text = $text . $topic . ": "; }; if ($comment) { $text = $text . $comment; }; my $terminalSemiColon = 0; if ($text =~ s/\;$//) { $terminalSemiColon = 1; } if ($evidence && ($evidence ne '{}')) { $text .= $evidence; } if ($terminalSemiColon) { $text .= ";" } else { $text .= '.'; } # specific fix for dealing with the format of 1 special CC section # note in general text wraping in comments is not guuaranteed to be read-safe # by SWISSKNIFE # this specific fix keeps wrapping correct for 1 strcutred CC line # a better alternative would be to implment this section as a new class if (defined($topic) and $topic =~ /^DATABASE|WEB RESOURCE$/) { my @texts = split /; /, $text; my $size = scalar @texts; my $newText = ""; my $currentLength = 0; my $lineLength = $SWISS::TextFunc::lineLength - 8; for (my $i = 0; $i < $size; $i++) { $texts[$i] .= ';' if $i<$size-1; if ($texts[$i] !~ /\S{$lineLength}/) { $text = SWISS::TextFunc->wrapOn('', "CC ", $SWISS::TextFunc::lineLength, $texts[$i] ); } else { $text = $texts[$i] . "\n"; } # extra manipulation my $potentialLength = $currentLength + (length $text) - 1; if (($currentLength != 0) && ($potentialLength < $SWISS::TextFunc::lineLength + 1)) { $newText =~ s/\n$/ /; $newText = $newText . $text; $currentLength = $currentLength + (length $text); } else { if ($i != 0) { $text = "CC " . $text; $currentLength = length $text; } else { $currentLength = (length $text) - 1; } $newText = $newText . $text; } } return $newText; } else { $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-1.67/lib/SWISS/Stars/0000755000175100017510000000000011040133466016266 5ustar moellermoellerswissknife-1.67/lib/SWISS/Stars/default.pm0000644000175100017510000000347710366115237020271 0ustar moellermoellerpackage 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 $newText = ''; # assemble new text if ($self->size > 0) { map ({$newText .= SWISS::TextFunc->wrapOn("\*\*$tag ", "\*\*$tag ", $SWISS::TextFunc::lineLengthStar, $_, ' ')} $self->elements); }; # insert new text SWISS::Stars::insertLineGroup($self, $textRef, $newText, $tag); # now the object is clean $self->{_dirty} = 0; return 1; } # No sorting by default. sub sort { return 1; }; 1; __END__ =head1 Name SWISS::default =head1 Description B is the default class to represent structured information in the "annotator's section" within an SWISS-PROT + TrEMBL entry. The "annotator's section" is not visible to the public. The structured part has line tags of the form '**xx'. See also the general description in Stars.html. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each line is stored as one element of the list. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back swissknife-1.67/lib/SWISS/Stars/aa.pm0000644000175100017510000000353210366115237017216 0ustar moellermoellerpackage SWISS::Stars::aa; use vars qw($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" 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-1.67/lib/SWISS/Stars/EV.pm0000644000175100017510000001510410366115237017145 0ustar moellermoellerpackage 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 ($$textRef =~ /((\*\*EV .*\n)+)/m) { $block = $1; # delete trailing dots and spaces $block =~ s/[\.\s]+\n/\n/gm; # unwrap multi-line evidence tags $block =~ s/\n\*\*EV\s{5}/ /gm; # now every comment is in a single line foreach $line (split /\n/, $block){ $line = SWISS::TextFunc->cleanLine($line); push (@{$self->list()}, [split(/\;\s*/, $line)]); }; }; # we have only read, so the object is still clean $self->{_dirty} = 0; return $self; } =head2 toText =cut sub toText { my $self = shift; my ($textRef) = @_; my $newText = ''; my $tag = 'EV'; # remove old lines $$textRef =~ s/^(\*\*$tag .*\n)//gm; $self->sort(); # assemble new lines map ({$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 $self = shift; my ($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; $self->{_dirty} = 1; return 1; }; =head2 addEvidence($category, $type, $initials, $attributes [, $date]) Title: addEvidence Usage: $evidenceTag = $entry->Stars->EV->addEvidence($category, $type, $initials, $attributes [, $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: $category: the evidence category. Currently one of 'A', 'C', 'I','P'. $type: the evidence type $initials: The initals of the person doing the update. For programs this should be '-'. $attributes: the attributes of the evidence $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 $self=shift; my ($category, $type, $initials, $attributes, $date) = @_; # set $date unless ($date) { $date = SWISS::TextFunc::currentSpDate; } return $self->_addEvidence($category, $type, $initials, $attributes, $date); } =head2 updateEvidence($category, $type, $initials, $attributes [, $date]) Title: updateEvidence Usage: $evidenceTag = $entry->Stars->EV->updateEvidence($category, $type, $initials, $attributes [, $date]) Function: updates the evidence to the EV block to $date or inserts it if it does not yet exist. Args: $category: the evidence category. Currently one of 'A', 'C', 'I','P'. $type: the evidence type $initials: The initals of the person doing the update. For programs this should be '-'. $attributes: the attributes of the evidence $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 $self=shift; my ($category, $type, $initials, $attributes, $date) = @_; # set $date unless ($date) { $date = SWISS::TextFunc::currentSpDate; } return $self->_addEvidence($category, $type, $initials, $attributes, $date, 1); } # if $update is set, the evidence date will be updated if the entry already # exists. sub _addEvidence{ my $self = shift; my ($category, $type, $initials, $attributes, $date, $update) = @_; my $evidenceTag = ''; # check the category unless ($category =~ /^[ACIP]$/){ croak("Wrong evidence category \'$category\'\n"); } # set $date unless ($date) { $date = SWISS::TextFunc::currentSpDate; } # if there is no other evidence in the entry, the tag is E1. if ($self->size == 0) { $evidenceTag = 'E' . $category . '1'; } else { # get the next available evidence tag my $currentTagNumber = 0; my $lastTagNumber = 0; map {($currentTagNumber) = @$_[0] =~ /\AE[ACIP](\d+)/; $lastTagNumber = max($lastTagNumber, $currentTagNumber)} $self->elements(); $evidenceTag = 'E' . $category . ($lastTagNumber + 1); } my $existingEvidence = $self->getObject(['.*', $type, $initials, $attributes]); # No evidence, insert new evidence if ($existingEvidence->size == 0) { $self->add([$evidenceTag, $type, $initials, $attributes, $date]); return $evidenceTag; } if ($existingEvidence->size > 1) { $main::opt_warn && carp("More than one piece of evidence for $type, $initials, $attributes. Using lowest numbered evidence tag.\n"); } # if $update is set, update the date of the evidence if ($update) { @{$existingEvidence->head()}[4] = $date; } $self->{_dirty} = 1; return @{$existingEvidence->head()}[0]; } sub max { my ($a, $b) = @_; if ($a > $b) { return $a; } else { return $b; } } 1; # says use was ok =head1 Name SWISS::Stars::EV.pm =head1 Description B represents the evidence section within an SWISS-PROT + TrEMBL entry. See http://www3.ebi.ac.uk/~sp/intern/projects/evidenceTags/index.html For a usage example, see evTest.pl in the Swissknife package. =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C Each element of the list describes one evidence, itself represented as an array. =back swissknife-1.67/lib/SWISS/CCcopyright.pm0000644000175100017510000000346310727215623017763 0ustar moellermoellerpackage SWISS::CCcopyright; use vars qw($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 # $text =~ s/(? text; } 1; __END__ =head1 Name SWISS::CCcopyright =head1 Description B represents the copyright statment within the comments block of a SWISS-PROT entry as specified in the user manual http://www.expasy.org/sprot/userman.html . Collectively, comments of all types are stored within a SWISS::CCs container object. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item topic The topic of this comment ('Copyright'). =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Reading/Writing methods =over =item toString Returns a string representation of this comment. =back swissknife-1.67/lib/SWISS/Ref.pm0000644000175100017510000003143411021531252016243 0ustar moellermoellerpackage SWISS::Ref; use vars qw($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 AGRICOLA PubMed 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 $ref; my ($line, $tmp, @tmp, %tmp); my ($token, $qualifiers, @qualifiers); my (%rc,%rx); my ($dbref, $dbid); my ($prematch, $match, $comment); # 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+/, $qualifiers); unless (grep(/$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 ($$textRef =~ /$SWISS::Ref::linePattern{'RT'}/m){ $match = $&; if ($match =~ /^\*\*/m) { $self->RT_comment($match); } else { my $line = SWISS::TextFunc->joinWith('', ' ', '(?cleanLine($_)} (split /\n/m, $match)); # Drop trailing spaces and embracing ""; $line =~ s/(\A\")|(\";\s*\Z)//g; $self->RT($line); } }; # Parse RL if ($$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 $textRef = shift; my $newText = ''; my ($rc, $topic, @tmp); my ($dbref, $dbid); my $ra; my $evidenceTags; 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, $self->RP, # cut at a whitespace, better not at a dash "\\s+(?!\\S{$longWordLength})"); }; # Format RC line if (defined $self->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; $rg .= ";" if $rg !~ /;$/; $newText .= SWISS::TextFunc->wrapOn('RG ','RG ', $SWISS::TextFunc::lineLength, $rg, ';\s+', '\s+'); } # 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; $self->{_dirty} = 1; } } } } } 1; __END__ =head1 Name SWISS::Ref.pm =head1 Description B represents a single reference of a SWISS-PROT + TREMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C The reference number. =item C The RP line(s), unwrapped as a string. =item C Zero or more RC lines. Data structure: {Token}[qualifier1, qualifierN]. A hash of arrays. Hash keys are the RC tokens, array elements are the qualifiers for that token. =item C References to bibliographic databases. Data structure: {Database}[identifier1, identifierN]. A hash of arrays. Hash keys are the names of bibliographic databases, array elements are the identifiers of the reference for that database. =item C The RG line(s), unwrapped as a string. =item C The list of Authors. An object of type SWISS::ListBase. =item C The publication title, unwrapped as a string. =item C The RL line. Data structure: String. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Writing methods =over =item add_MedlineID Add a RX line 'MEDLINE; nnnnnnnn.' to the reference. =item add_Author Add an author to the RA line of the reference. =item rc_sort Sort elements of the RC line alphabetically. swissknife-1.67/lib/SWISS/SQs.pm0000644000175100017510000001223310745675522016256 0ustar moellermoellerpackage SWISS::SQs; use vars qw($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 + $mwFloat/1e4; } 1; __END__ =head1 NAME B =head1 DESCRIPTION B represents the SQ lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C The amino acid sequence in string representation. =item C The sequence length. =item C The molecular weight. =item C The CRC checksum of the sequence. This is recalculated using the C module. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item update Should be called if the sequence has been modified. =back =head2 Specific methods =over =item calcMolWeight string Calculate the molecular weight for B. =back swissknife-1.67/lib/SWISS/OS.pm0000644000175100017510000000235510366115237016064 0ustar moellermoellerpackage SWISS::OS; use vars qw($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 . $self->getEvidenceTagsString; } 1; __END__ =head1 Name SWISS::KWs =head1 Description B represents one organism name from the OS line. The container object holding all organism lines is SWISS::OSs. =head1 Inherits from SWISS::BaseClass.pm =head1 Attributes =over =item C One organism name. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back swissknife-1.67/lib/SWISS/CCalt_prod.pm0000644000175100017510000012776210751636300017564 0ustar moellermoellerpackage SWISS::CCalt_prod; use vars qw($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; 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 = $$textRef; ($topic, @events) = ($text =~ /(.+?)(Event=.+?)(?=(Event=.*|$))/gm); for my $event (@events) { if ($event ne "") { push @newEvents, $event; } } my %eventHash; #print STDERR "HERE:$$textRef\n"; # want to be able to read old format data (i.e pre release 8.0) for my $event (@newEvents) { my ($eventType, $typeOnly, $comment, $namedForms, $rest, $isoformCount); 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; $comment =~ s/;\s*$//; $comment =~ s/^\s*//; # look for tags # if parsing old format entries, aggregate comments from all Event blocks if (my ($realComment, $commentTags) = ($comment =~ /(.+?)\{(.+?)\}$/)) { my @commentTags = split /,/, $commentTags; if (defined $eventHash{"Comment"}) { $eventHash{"Comment"} = $eventHash{"Comment"} . $realComment; } else { $eventHash{"Comment"} = $realComment; } $eventHash{"CommentTags"} = [($eventHash{"CommentTags"} ? @{$eventHash{"CommentTags"}} : ()), @commentTags] if $commentTags; } elsif ($comment) { $eventHash{"Comment"} .= $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 = $namedForm . ";"; my (@fields) = ($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+/, $value; my @realValues; foreach $value (@values) { if (my ($realData, $tags) = ($value =~ /(.+?)\{(.+?)\}$/)) { push @realValues, $realData; my (@tagValues) = split /,\s+/, $tags; ${$thisFormHash{"SynonymsTags"}}{$realData} = \@tagValues; } else { push @realValues, $value; } } $thisFormHash{$key} = \@realValues; } elsif ($key eq "IsoId" || $key eq "Sequence") { # complex data item, no synonyms my (@values) = split /,\s+/, $value; $thisFormHash{$key} = \@values; } elsif (my ($realData, $tags) = ($value =~ /(.+?)\{(.+?)\}$/)) { # simple data item, with tags $thisFormHash{$key} = $realData; my @tags = split /,/, $tags; my $tagKey = $key . "Tags"; $thisFormHash{$tagKey} = \@tags; } elsif ($key =~ /\w/) { # 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 $commentText = ${${$self->{'events'}}{$event}}{"Comment"} || ''; $commentText =~ s/\s+$//; my $evTags = $self -> getEvidenceTagsString($event, "Comment"); if (defined $evTags) { $commentText = $commentText . $evTags; } if ($commentText !~ /\;$/) { $commentText = $commentText . ";"; } 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 ne ';') { $headerText = "Comment=" . $commentText; $text = $text . SWISS::TextFunc-> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $headerText , '\s+'); } my $allFormsText; if (${${${${$self->{'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"}, $$namedForm{"Name"}); if (defined $synonymText) { $formText = $formText . $synonymText; } $formText = SWISS::TextFunc-> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText , '\s+'); $allFormsText = $allFormsText . $formText; my $nb_isoid = scalar @{$$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 $formText = ""; if (defined $$namedForm{"Note"}) { $formText = "Note=" . $$namedForm{"Note"}; my $evTags = $self -> getEvidenceTagsString($event, "Note", $$namedForm{"Name"}); if (defined $evTags) { $formText = $formText . $evTags; } if ($formText !~ /\;$/) { $formText = $formText . ";"; } } $formText = SWISS::TextFunc-> wrapOn("CC ", "CC ", $SWISS::TextFunc::lineLength, $formText , '\s+'); $allFormsText = $allFormsText . $formText; } } if (defined $allFormsText) { $text = $text . $allFormsText; } return $text; } sub _printList { # prepare fields that take a list of values my ($self, $keyText, $values, $name) = @_; my $count = 0; $keyText = $keyText . "="; for my $value (@$values) { if ($count != 0) { $keyText = $keyText . ", "; } $count ++; $keyText = $keyText . $value; # slightly ugly, misplaced fix, to fetch evidence tags (Synonyms only) if (defined $name) { my $evTags = $self -> 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} } 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) = @_; if (defined ${$self -> {'events'}}{$eventName}) { my %newForm; $newForm{"Name"} = $name; $newForm{"Synonyms"} = $synonyms; $newForm{"IsoId"} = $isoIds; $newForm{"Sequence"} = $featIds; $newForm{"Note"} = $note; push @{${${$self -> {'events'}}{$eventName}}{"FormsList"}}, \%newForm; } } sub getComment { my ($self, $eventName, $comment) = @_; if (defined ${$self -> {'events'}}{$eventName}) { return ${${$self -> {'events'}}{$eventName}}{"Comment"}; } 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, $comment) = @_; 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 ($$form{"Name"} eq $formName) { my @ret = splice (@{${${$self -> {'events'}}{$event}}{"FormsList"}}, $position, 1); if (scalar @{${${$self -> {'events'}}{$event}}{"FormsList"}} == 0) { delete ${${$self -> {'events'}}{$event}}{"FormsList"}; } return @ret; } $position++; } } return undef; } sub setComment { my ($self, $eventName, $comment) = @_; if (defined ${$self -> {'events'}}{$eventName}) { ${${$self -> {'events'}}{$eventName}}{"Comment"} = $comment; } } sub setFormName { my ($self, $event, $oldName, $newName) = @_; if (defined ${$self -> {'events'}}{$event}) { for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$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) { $$form{"Sequence"} = $featIds; return; } } } } sub setNote { my ($self, $event, $name, $note) = @_; if (defined ${$self -> {'events'}}{$event}) { for my $form (@{${${$self -> {'events'}}{$event}}{"FormsList"}}) { if ($$form{"Name"} eq $name) { $$form{"Note"} = $note; return; } } } } sub hasEvidenceTag { my ($self, $tag, $event, $type, $name, $synonym) = @_; if (defined ${$self -> {'events'}}{$event}) { if ($type eq 'Comment') { if (defined ${${$self -> {'events'}}{$event}}{'CommentTags'}) { for my $actualTag (@{${${$self -> {'events'}}{$event}}{'CommentTags'}}) { if ($actualTag eq $tag) { return 1; } } } } elsif ($type eq 'Name' || $type eq 'Note') { for my $form (@{${${$self -> {'events'}}{$event}}{'FormsList'}}) { if ($$form{"Name"} eq $name) { my $tagType = $type . "Tags"; if (defined $$form{$tagType}) { for my $actualTag (@{$$form{$tagType}}) { if ($actualTag eq $tag) { return 1; } } } } } } elsif ($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 $actualTag (@{${$$form{$tagType}}{$synonym}}) { if ($actualTag eq $tag) { return 1; } } } } } } } } } } return 0; } sub getEvidenceTags { my ($self, $event, $type, $name, $synonym) = @_; if (defined ${$self -> {'events'}}{$event}) { if ($type eq 'Comment') { if (defined ${${$self -> {'events'}}{$event}}{'CommentTags'}) { return @{${${$self -> {'events'}}{$event}}{'CommentTags'}}; } } elsif ($type eq 'Name' || $type eq 'Note') { for my $form (@{${${$self -> {'events'}}{$event}}{'FormsList'}}) { if ($$form{"Name"} eq $name) { my $tagType = $type . "Tags"; if (defined $$form{$tagType}) { return @{$$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 (@{$$form{"Synonyms"}}) { if ($synonym eq $actualSynonym) { # hash of tags for each synonym my $tagType = $type . "Tags"; if (defined ${$$form{$tagType}}{$synonym}) { return @{${$$form{$tagType}}{$synonym}}; } } } } } } } } return undef; } sub getEvidenceTagsString { my ($self, $event, $type, $name, $synonym) = @_; if (defined ${$self -> {'events'}}{$event}) { if ($type eq 'Comment') { if (defined ${${$self -> {'events'}}{$event}}{'CommentTags'}) { my $text = join ',', @{${${$self -> {'events'}}{$event}}{'CommentTags'}}; return "{" . $text . "}"; } } elsif ($type eq 'Name' || $type eq 'Note') { for my $form (@{${${$self -> {'events'}}{$event}}{'FormsList'}}) { if ($$form{"Name"} eq $name) { my $tagType = $type . "Tags"; if (defined $$form{$tagType}) { my $text = join ',', @{$$form{$tagType}}; 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 $text = join ',', @{${$$form{$tagType}}{$synonym}}; return "{" .$text . "}"; } } } } } } } } return undef; } sub setEvidenceTags { # don't allow tags to be added where there is no data my ($self, $tags, $event, $type, $name, $synonym) = @_; if (defined ${$self -> {'events'}}{$event}) { if ($type eq 'Comment' && (defined ${${$self -> {'events'}}{$event}}{'Comment'})) { ${${$self -> {'events'}}{$event}}{'CommentTags'} = $tags; } elsif ($type eq 'Name' || $type eq 'Note') { for my $form (@{${${$self -> {'events'}}{$event}}{'FormsList'}}) { if ($$form{"Name"} eq $name) { if (defined $$form{$type}) { my $tagType = $type . "Tags"; $$form{$tagType} = $tags; } } } } elsif ($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'})) { push @{${${$self -> {'events'}}{$event}}{'CommentTags'}}, $tag; } elsif ($type eq 'Name' || $type eq 'Note') { for my $form (@{${${$self -> {'events'}}{$event}}{'FormsList'}}) { if ($$form{"Name"} eq $name) { if (defined $$form{$type}) { my $tagType = $type . "Tags"; push @{$$form{$tagType}}, $tag; } } } } elsif ($type eq 'Synonyms') { for my $form (@{${${$self -> {'events'}}{$event}}{'FormsList'}}) { if ($$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}}, $tag; } } } } } } } sub deleteEvidenceTags { # this method looks strange but is basically simple # ferret out the requisite evidence tag and splice it from the relevent list my ($self, $tag, $event, $type, $name, $synonym) = @_; if (defined ${$self -> {'events'}}{$event}) { if ($type eq 'Comment') { my $offset = 0; if (defined @{${${$self -> {'events'}}{$event}}{'CommentTags'}}) { my @tags = @{${${$self -> {'events'}}{$event}}{'CommentTags'}}; for my $actualTag (@tags) { if ($tag eq $actualTag) { splice @tags, $offset, 1; } $offset ++; } if (scalar @tags == 0) { delete ${${$self -> {'events'}}{$event}}{'CommentTags'}; } } } elsif ($type eq 'Name' || $type eq 'Note') { 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"; ## 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"; ## 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"); 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. 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". =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". =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". =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". =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-1.67/lib/SWISS/ListBase.pm0000644000175100017510000004325710366115237017257 0ustar moellermoellerpackage 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, $pat, $element); # do nothing if the list is empty unless ($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; my $new; foreach $element ($self->elements()) { (&$filterFunc($element)) && (CORE::push(@matches, $element)); }; $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; # create a new object $new = new ref($self); $new->set($self->get(@elements)); return $new; }; # Evidence tag handling sub evidenceTagPosition { my ($arrayP) = @_; my $position = 0; if ($#$arrayP == -1) { return 0; } if (@$arrayP[$#$arrayP] =~ $SWISS::TextFunc::evidencePattern) { return $#$arrayP; } else { 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); @$arrayP[$evidenceTagPosition] = '{' . (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 = '{}'; } unless ($$evidenceTagPointer =~ /[\{\,]$tag[\}\,]/) { if ((!$$evidenceTagPointer) || ($$evidenceTagPointer eq '{}')) { $$evidenceTagPointer = '{' . $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/([\{\,])$tag([\,\}])/$1$2/; $$evidenceTagPointer =~ s/\,\,/\,/; $$evidenceTagPointer =~ s/\,\}/\}/; $$evidenceTagPointer =~ s/\{\,/\{/; $self->{'_dirty'} = 1; return $arrayP; } sub hasEvidenceTag { my ($self, $arrayP, $tag) = @_; unless (ref $arrayP eq 'ARRAY') { confess "$arrayP is not an array\n"; } my $evidenceTagPosition = evidenceTagPosition($arrayP); return @$arrayP[$evidenceTagPosition] =~ /[\{\,]$tag[\}\,]/; } sub getEvidenceTags { my ($self, $arrayP, $tag) = @_; unless (ref $arrayP eq 'ARRAY') { confess "$arrayP is not an array\n"; } my $tmp = @$arrayP[evidenceTagPosition($arrayP)]; $tmp =~ tr/\{\}//d; return split /\,/, $tmp; } sub getEvidenceTagsString { my ($self, $arrayP, $tag) = @_; unless (ref $arrayP eq 'ARRAY') { confess "$arrayP is not an array\n"; } my $tmp = @$arrayP[evidenceTagPosition($arrayP)] || ''; if ($tmp eq '{}') { return ''; } else { return $tmp; } } # return the intersection with another list # usage: @myary = $mylistbase->intersect(@otherary); # or @myary = $mylistbase->intersect($otherlistbase); sub intersect { my ($self, @other) = @_; # if argument is another ListBase, get its contents into @other my $arg = $other[0]; if ($arg && ref($arg) eq ref($self)){ warn "ListBase::intersect doesnt allow two ListBases as input\n" if $main::opt_warn && $#other>0; @other = @{$arg->list}; } my %other_hash = map {$_,1} @other; my @result = grep { $other_hash{$_}} @{$self->list}; return @result; } # return the union with another list # usage: @myary = $mylistbase->union(@otherary,...); # or @myary = $mylistbase->union($otherlistbase,...); sub union { my ($self, @args) = @_; my @other = @{$self->list}; my $arg; foreach $arg (@args){ my $kind = ref $arg; if (not $kind){ CORE::push(@other,$arg); } elsif ($kind eq ref($self)){ CORE::push(@other, @{$arg->list}); } elsif ($kind eq 'SCALAR'){ CORE::push(@other, $$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 $arrayPointer. =back swissknife-1.67/lib/SWISS/DTs.pm0000644000175100017510000001166411035646221016234 0ustar moellermoellerpackage SWISS::DTs; use vars qw($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); $entry->DTs->SQ_version(36); swissknife-1.67/lib/SWISS/CCrna_editing.pm0000644000175100017510000000464310366115237020236 0ustar moellermoellerpackage SWISS::CCrna_editing; use vars qw($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 ", *", $1) { my $ev = $pos =~ s/($SWISS::TextFunc::evidencePattern)// ? $1 : undef; if ($pos =~ /^[A-Za-z]/) { $self->{term} = $pos; } else { $self->add([$pos, $ev]); } } } $self->{note} = $1 if $text =~ /\bNote=(.*)/; $self->{_dirty} = 0; return $self; } sub toString { my $self = shift; my $text = "CC -!- RNA EDITING: " . $self->comment . "."; return SWISS::TextFunc->wrapOn('',"CC ", $SWISS::TextFunc::lineLength, $text); } sub topic { return "RNA EDITING"; } sub comment { my ($self) = @_; my $text = "Modified_positions="; if ($self->size) { $text .= join ", ", map { my ($pos, $ev) = @$_; $pos .= $ev if defined $ev; $pos; } @{$self->{list}}; } else { $text .= $self->{term} || "Undetermined"; } if (defined $self->{note} and length $self->{note}) { $text .= "; Note=" . $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. =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-1.67/lib/SWISS/IDs.pm0000644000175100017510000001033610512715457016223 0ustar moellermoellerpackage 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, $SWISS::TextFunc::linePattern{'ID'}); } # IDs must never be sorted, overwrite the inherited sort method. sub sort { return 1; } 1; __END__ =head1 Name SWISS::IDs.pm =head1 Description B represents the ID lines of a SWISS-PROT + TREMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C This is an array containing a list of all the IDs associated with this entry. The first member will be the primary ID, and any following are the secondary IDs which are not shown in the public section of the entry. =item dataClass The data class, either STANDARD or PRELIMINARY for data from releases prior to 9.0, or Reviewed or Unreviewed for data from later releases. =item moleculeType The molecule type, currently only PRT. =item length The protein length in amino acids. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item sort IDs must never be sorted, so this method does nothing (but it overwrites the inherited method). swissknife-1.67/lib/SWISS/GeneGroup.pm0000644000175100017510000001521410366115237017434 0ustar moellermoellerpackage SWISS::GeneGroup; use vars qw($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 ', +', $2); } if ($text =~ s/(^|; +)OrderedLocusNames=(.*?)(?=; |;\Z|\Z)//) { $self->OLN->set(map {SWISS::GN->fromText($_)} split ', +', $2); } my @names; if ($text =~ s/(^|; +)Synonyms=(.*?)(?=; |;\Z|\Z)//) { push @names, split ', +', $2; } if ($text =~ s/(^|; +)Name=(.*?)(?=; |;\Z|\Z)//) { unshift @names, split ', +', $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; my $line; my @tmp; 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); 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 $new; } 1; __END__ =head1 Name SWISS::GeneGroup.pm =head1 Description A B object contain all synonyms for a given gene name. See B for a description of the gene name format. =head1 Inherits from SWISS::BaseClass.pm (also implements many methods from SWISS::ListBase.pm) =head1 Attributes =over =item C Each list element is a SWISS::GN object, describing a primary name or synonym. Concatenation of Name and Synonyms lists. =item C Each list element is a SWISS::GN object, describing an OrderedLocusName. =item C Each list element is a SWISS::GN object, describing an ORFName. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Specific methods =over =item Name Returns the Name (primary name). =item Synonyms Returns the Synonyms. =item elements Concatenates all elements from Names, OLN and ORFNames in a single array. =back =head2 List manipulation methods Since GeneGroup was a previous implementation of SWISS::ListBase, the list manipulation methods below are provided to facilitate compatibility. =over =item size =item isEmpty =item elements =item filter =item get I<(deprecated)> =item head I<(deprecated)> =item tail I<(deprecated)> =item item I<(deprecated)> =item push I<(deprecated)> =item pop I<(deprecated)> =item shift I<(deprecated)> =item splice I<(deprecated)> =item unshift I<(deprecated)> =item set I<(deprecated)> =item add I<(deprecated)> =back swissknife-1.67/lib/SWISS/RCelement.pm0000644000175100017510000000254410366115237017421 0ustar moellermoellerpackage SWISS::RCelement; use vars qw($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; $self->{text} =~ s/^ *and +//; return; } 1; __END__ =head1 Name SWISS::RCelement.pm =head1 Description Each RCelement object represents one element of the RC line. The container object for all RCelements of an entry is SWISS::Ref. =head1 Inherits from SWISS::BaseClass =head1 Attributes =over =item C The text of the keyword. =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back =head2 Writing methods =over =item cleanText Remove potentially leading "and" from text. =back swissknife-1.67/lib/SWISS/Journal.pm0000644000175100017510000007333510366115237017163 0ustar moellermoellerpackage SWISS::Journal; use vars qw($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. 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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. 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Sci. 0967-1994,Zygote swissknife-1.67/lib/SWISS/Entry.pm0000644000175100017510000003244011037374436016646 0ustar moellermoellerpackage 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='1.67'; # * 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 $force = 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; my $lineObject; unless ($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/\([^()]+\([^\)]+\)+//; while ($os =~ /\(([^()]+)\)/g) { my $elem = $1; $organism.= ' ('.$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 $insertInternalComments to true. =item toFasta Return the entry in Fasta format. =item equal Returns True if two entries are equal, False otherwise =back The following methods are provided for your convenience. They are shortcuts for methods of the individual line objects. =over =item ID Returns the primary ID of the entry. =item AC Returns the primary AC of the entry. =item SQ Returns the sequence of the entry. =item EV Returns the EV (evidence) object of an entry. SWISS-PROT internal method. =back =head2 Data access methods =over =item text Returns the current text of the entry. B No update of the text is performed before. =item database_code Is it a SWISS-PROT, TREMBL or TREMBLNEW entry? database_code tries to find it out. Return values are S for SWISS-PROT, 3 for TREMBL, Q for TREMBLNEW, ? for unknown. =item isFragment Returns true if the DE line indicates a fragment, or of the entry contains a NON_CONS or NON_TER feature. =item isCurated Returns 1 if the entry is a curated entry, 0 otherwise. SWISS-PROT internal use only. swissknife-1.67/lib/SWISS/OHs.pm0000644000175100017510000000312210437124062016220 0ustar moellermoellerpackage SWISS::OHs; use vars qw($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 ($$textRef =~ /($SWISS::TextFunc::linePattern{OH})/m) { foreach $line (split /\n/m, $1) { $self->{indentation} += $line =~ s/^ //; $line = SWISS::TextFunc->cleanLine($line); push @{$self->list()}, SWISS::OH->fromText($line); } } $self->{_dirty} = 0; return $self; } sub toText { my $self = shift; my $textRef = shift; my $newText = ''; for (@{$self->list()}) { $newText .= 'OH ' . $_->toText . "\n"; } $self->{_dirty} = 0; return SWISS::TextFunc->insertLineGroup($textRef, $newText, $SWISS::TextFunc::linePattern{OH}); } # OXs must never be sorted, overwrite the inherited sort method. sub sort { return 1; } 1; __END__ =head1 Name SWISS::OHs =head1 Description B represents the OH lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . The OHs object is a container object which holds a list of SWISS::OH objects. =head1 Inherits from SWISS::BaseClass.pm =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =back swissknife-1.67/lib/SWISS/FTs.pm0000644000175100017510000002367011017746075016246 0ustar moellermoellerpackage SWISS::FTs; use vars qw($AUTOLOAD @ISA @EXPORT_OK %fields %KEYORDER); use Exporter; use Carp; use strict; use SWISS::TextFunc; use SWISS::ListBase; BEGIN { @EXPORT_OK = qw(); @ISA = ( 'Exporter', 'SWISS::ListBase'); %fields = ( ); } #initialization code: stuff DATA into hash { # Leading and trailing spaces are MANDATORY! local $/="\n"; my $index=0; my $line; while (defined ($line=)) { $line =~ s/\s+\z//; $index++; $KEYORDER{$_} = $index for split /\s+/, $line; } close DATA; } sub new { my $ref = shift; my $class = ref($ref) || $ref; my $self = new SWISS::ListBase; $self->rebless($class); return $self; } sub fromText { my $class = shift; my $textRef = shift; my $self = new SWISS::FTs; my $line; my $tmp; my $indentation = 0; my ($key, $from, $to, $description); # attributes of one feature if ($$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 = $1; } # Get the old-style Swiss-Prot evidence if ($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 .= ' '; $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 '{}')) { $description .= $evidenceTags; } if (length $description ) { $text = $description; # Add a dot at the end if the description does not consist only of # evidence tags. unless ($description =~ /\A$SWISS::TextFunc::evidencePattern\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" ); } else { $text = SWISS::TextFunc->wrapOn($prefix, "FT ", $SWISS::TextFunc::lineLength, $text, $SWISS::TextFunc::textWrapPattern1, "/|$SWISS::TextFunc::textWrapPattern2" ); }; # 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 $string =~ /(\d+)/; } return 0; } 1; =head1 Name SWISS::FTs =head1 Description B represents the FT (feature) lines within an SWISS-PROT + TrEMBL entry as specified in the user manual http://www.expasy.org/sprot/userman.html . =head1 Inherits from SWISS::ListBase.pm =head1 Attributes =over =item C An array of arrays. Each element is an array containing: a feature key, from position, to position, description, qualifier, FTId and an evidence tag. Example: ['CHAIN', 25, 126, 'Alpha chain', 'By similarity', '/FTId=PRO_0000023008', '{EC1}'] =back =head1 Methods =head2 Standard methods =over =item new =item fromText =item toText =item sort =back =cut __DATA__ INIT_MET SIGNAL PROPEP TRANSIT CHAIN PEPTIDE TOPO_DOM TRANSMEM DOMAIN REPEAT CA_BIND ZN_FING DNA_BIND NP_BIND REGION COILED MOTIF COMPBIAS ACT_SITE METAL BINDING SITE NON_STD MOD_RES LIPID CARBOHYD DISULFID CROSSLNK VAR_SEQ VARIANT MUTAGEN UNSURE CONFLICT NON_CONS NON_TER HELIX TURN STRAND swissknife-1.67/lib/SWISS/DE.pm0000644000175100017510000001252111037664121016024 0ustar moellermoellerpackage SWISS::DE; use vars qw($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-1.67/lib/SWISS/CCs.pm0000644000175100017510000002433511037377037016221 0ustar moellermoellerpackage 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; 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; my @tmp; 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) /- $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); } 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 @result; my $new; $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 ALLERGEN TOXIC DOSE BIOTECHNOLOGY PHARMACEUTICAL MISCELLANEOUS SIMILARITY CAUTION SEQUENCE CAUTION DATABASE WEB RESOURCE swissknife-1.67/lib/SWISS/OSs.pm0000644000175100017510000001140510366115237016243 0ustar moellermoellerpackage 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; my @tmp; if ($$textRef =~ /($SWISS::TextFunc::linePattern{'OS'})/m){ $line = $1; $self->{indentation} = $line =~ s/^ //mg; $line = SWISS::TextFunc->joinWith('', ' ', '(?cleanLine($_)} (split "\n", $line)); # complex expression for separator to make sure commas within brackets are # not regarded as separators. @tmp = SWISS::TextFunc->listFromText($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, @lines); my $newText = ''; my $lastElementRef; my $listRef; if ($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. =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-1.67/lib/SWISS/Ref/0000755000175100017510000000000011040133466015706 5ustar moellermoellerswissknife-1.67/lib/SWISS/Ref/PubMedIndex.pm0000644000175100017510000002120407563757501020430 0ustar moellermoellerpackage SWISS::Ref::PubMed; use Socket; use Carp; $caching = 0; $HOST = 'www.ncbi.nlm.nih.gov'; $PORT = 80; $PATH = '/htbin-post/Entrez/query?'; %CACHE=(); %REFCACHE=(); sub fetch_by_medlineid { my $self = new SWISS::Ref; my $medlineid = shift; carp "fetch_by_medlineid($medlineid) called" if $main::opt_debug>2; if ($caching) { my $cached=$REFCACHE{$medlineid}; if ($cached){ #print STDERR "!!!Cache hit '$medlineid'\n"; return $cached; } } my $page = get_pubmed_page("uid=$medlineid".'&form=6&dopt=l&db=m&html=no'); return unless $page; if ($page !~ /^UI - (\d+)/){ carp "Medline ID $medlineid not found" if $main::opt_warn>1; } elsif ($medlineid ne $1) { carp "Got medline ID $1 instead of $medlineid" if $main::opt_warn>1; } else { $self->fromMedlars(\$page); $REFCACHE{$medlineid}=$self if $caching; } return $self; } sub fetch_by_fields { my $ref = shift; my $self = new SWISS::Ref; carp "fetch_by_fields() called" if $main::opt_debug>2; my $query = toPubMedQuery($ref); #print STDERR "QUERY=$query\n"; my $head ='form=4&db=m&dopt=l&html=no&term='; # Have we asked this question already? my ($number,$id); if (defined $CACHE{$query}){ ($number,$id) = split(' ',$CACHE{$query}); if (defined $id){ #print STDERR "!!!POSITIVE cache hit '$id'\n"; return SWISS::Ref::PubMed::fetch_by_medlineid($id); } else { #print STDERR "!!!NEGATIVE cache hit\n"; return undef; } } else { $number = count_pubmed_page($head.$query); if ($number == 1){ my $page = get_pubmed_page($head.$query); $self->fromMedlars(\$page); $id = $self->get_MedlineID(); $CACHE{$query}="$number $id"; $REFCACHE{$id}=$self; return $self; } else { $CACHE{$query}= $number; return undef; } } return undef; } sub toPubMedQuery { my $ref = shift; $ref->unpackRL(); my @query=(); if (defined ($ref->issn)){ push @query, $ref->issn.'[JOUR]'; } elsif (defined ($ref->journal)) { my $issn = SWISS::Journal::name2issn($ref->journal); push @query, $issn.'[JOUR]' if $issn; } push @query, $ref->year."[PDAT]" if defined($ref->year) &&$ref->year; if (defined ($ref->volume)){ push @query, $ref->volume."[VOL]" if $ref->volume; } if (defined ($ref->pages)){ my ($firstpage)= $ref->pages =~ /^(\d+)/; push @query, $firstpage."[PAGE]" if $firstpage; } # journal,year,volume,pages is enough to query, but if something # is missing, we add the authors to the query unless (($ref->issn||$ref->journal)&& ($ref->year)&&($ref->volume)&&($ref->pages)) { if (defined ($ref->RA)){ my @au = @{$ref->RA()->list}; my $n=0; foreach $author (@au){ last if ++$n>10; $author =~ s/\.//g; $author =~ s/\s(Jr|II|III)$//ig; $author =~ s/(\w)-(\w)$/$1$2/g; $author =~ s/^(\w+).*/$1/; $author =~ tr/ /+/d; $query .= '+' unless $query; push @query, $author."[AUTH]"; } } } my $query = join('+AND+',@query); return $query; } sub count_pubmed_page { my $query = shift; # make sure the 'count' flag is set in the query string ($query =~ s/\&dopt=\w/&dopt=q/) || ($query .= '&dopt=q'); my ($code,$page) = web_get_retry($HOST,$PORT,$PATH.$query); if ($code ne 200) { return -1; } else { if ($page =~ /(\d+)/){ return $1; } else { return -1; } } } sub get_pubmed_page { my $query = shift; my ($code,$page) = web_get_retry($HOST,$PORT,$PATH.$query); if ($code eq 200 && $page){ $page =~ s/^Entrez Reports\n-+\n//m; $page =~ s/^No Documents Found[^\n]*\n//m; return $page; } else { return undef; } } sub web_get_retry { my ($code,$page); while (($code,$page)=web_get(@_)){ last if $code ne -1; carp "Retrying" if $main::opt_debug; } return ($code,$page); } sub web_get { my ($host,$port,$url) = @_; my $code = -1; my $page; my ($proto,$local_host,$local_sock,$remote_sock); my $sockaddr='S n a4 x8'; my ($status,$line,$info); my $save = $/; $/="\n"; $proto = getprotobyname('tcp'); chop($local_host=`hostname`); $local_sock=pack($sockaddr,AF_INET,0,(gethostbyname($local_host))[4]); $remote_sock=pack($sockaddr,AF_INET,$port,(gethostbyname($host))[4]); unless (socket(S, PF_INET, SOCK_STREAM, $proto)){ croak "socket: $!"; return -1; } setsockopt(S, SOL_SOCKET, SO_KEEPALIVE, pack("l",1)) or die "setsockopt: $!"; bind(S,$local_sock) || die "$0: bind: $!\n"; eval { connect(S, $remote_sock); }; if ($@){ croak "connect: $@"; return -1; } $_=select(S); $|=1; select($_); carp "URL=$url\n" if $main::opt_debug>1; print S "GET $url HTTP/1.0\rn" . "User-Agent: None/1.0\r\nAccept: */*\r\n\r\n"; if (defined(S) && defined($status=)){ chop($status); $status=~s/\r$//; ($code,$info)=($status=~m!^HTTP\S+\s+(\d\d\d)\s*(.*)$!i); carp "STATUS: $code - $info -\n" if $main::opt_debug>2; if ($code==200){ while(defined($line=)){ last if $line=~/^\r$/; carp "HEADER: ",$line if $main::opt_debug>3; } $page = ''; while(defined($line=)){ carp $line if $main::opt_debug>3; $page .= $line; } } } else { $code = '-1'; } close(S); $/=$save; return ($code,$page); } package SWISS::Ref; use SWISS::Journal; sub fromPubMed{ my $self = shift; my $medlineid = $self->get_MedlineID(); if ($medlineid){ return SWISS::Ref::PubMed::fetch_by_medlineid($medlineid); } else { return SWISS::Ref::PubMed::fetch_by_fields($self); } return undef; } sub fromMedlars { my $self = shift; my $textRef = shift; # Parse Medline ID if ($$textRef =~ /^UI - (\d+)/m){ $self->add_MedlineID($1); } # Parse RA while($$textRef =~ /^AU - (.*)/mg){ my $author = $1; my $suffix; if ($author =~ /et al/i) { $self->{'etal'}=1; next; } ($author =~ s/\sJr$//) && ($suffix=' JR.'); ($author =~ s/\s2nd$//) && ($suffix=' II.'); ($author =~ s/\s3rd$//) && ($suffix=' III.'); if ($author =~ /^(.*)\s([A-Z]+)$/){ $author = "$1 ".join('.',split('',$2))."."; } $author .= $suffix if $suffix; $self->add_Author($author); } # Parse RT if ($$textRef =~ /^TI - ([^\n]+(\s\s\s\s\s\s[^\n]+\n)*)/m){ my $title = $1; $title =~ s/\n\s+/\n/mg; $title =~ s/-\n/-/mg; $title =~ s/\n/ /mg; $title =~ s/^\[(.*)\]$/$1/mg; $title =~ s/[\.\s]+$//g; $title =~ s/\s\[see comments\]\s*//; $title =~ s/\s\[letter[^\]]*\]\s*//g; $title =~ s/\s\[comment[^\]]*\]\s*//g; $title =~ s/\s\[news\]\s*//; $title =~ s/\s\[editorial\]\s*//; #$title =~ s/ \[.+?\]$//mg; $self->RT($title); carp "Found title '$title'" if $main::opt_debug>1; } my ($journal,$vol,$pages,$year) = ('','0','0-0','0'); my $issn; # Parse Journal if ($$textRef =~ /^TA - (.*)/m){ $journal = $1; } # Parse ISSN if ($$textRef =~ /^IS - (\d\d\d\d-\d\d\d[\dXx])/m){ $issn = $1; carp "Found ISSN $issn" if $main::opt_debug>1; } else { carp "No ISSN found" if $main::opt_warn; } # Getting the proper journal name for Swissprot usage is tricky my $proper_name=''; # if pubmed has an issn which is in our lookup list (SWISS::Journal), # we take this looked-up name if ($issn && ($proper_name = SWISS::Journal::issn2name($issn))){ $journal = $proper_name; carp "Mapped ISSN $issn to '$proper_name'" if $main::opt_debug>2; } if (!$proper_name && ($proper_name = SWISS::Journal::name2swiss($journal))){ $journal = $proper_name; carp "Mapped journal '$name' to '$proper_name'" if $main::opt_debug>2; } if (!$proper_name && $main::opt_warn){ carp "Cant find the proper name for journal '$journal'"; } # Parse Volume if ($$textRef =~ /^VI - (.*)/m){ $vol = $1; $vol =~ s/^(\d+)\s+\S+.*$/$1/; } # Parse Pages if ($$textRef =~ /^PG - (.*)/m){ # handle the american way of paging "125-6" -> "125-126" $pages = $1; my $prefix; if ($pages =~ s/^(\D+)//) { $prefix = $1; } $pages =~ s/,.*$//; my ($from,$to)=split('-',$pages); if ($from && $to && $from>$to){ $pages = $from.'-'.substr($from,0,length($from)-length($to)).$to; } $pages = $prefix.$pages if $prefix; # reformat page '317' to SWISS-PROT format '317-317' if ($pages !~ /-/){ $pages = "$pages-$pages"; } } # Parse Year if ($$textRef =~ /^DP - (\d\d\d\d)/m){ $year = $1; } if ($main::opt_debug>1){ carp "Found reference '$journal|$vol|$pages|$year'"; } my $rl = "$journal $vol:$pages($year)"; $self->issn($issn) if $issn; $self->RL($rl); return $self; } 1; swissknife-1.67/lib/SWISS/Ref/Oracle.pm0000644000175100017510000001270607563757500017477 0ustar moellermoellerpackage SWISS::Ref; use DBI; use DBD::Oracle; use SWISS::Journal; my $dbh=undef; sub fromOracle{ my $self = shift; my $rn = $self->RN(); if ($rn && $rn>10000){ $self->fetch_by_pubid($rn); return $self; } my $muid = $self->get_MedlineID(); if ($muid){ $self->fetch_by_medlineid($muid); return $self; } } sub fetch_by_pubid { my $self = shift; my $pubid = shift; # print STDERR "fetch_by_pubid($pubid) called\n"; _connect() unless $dbh; $self->fetch_titleandyear($pubid); $self->fetch_authors($pubid); $self->fetch_journalarticle($pubid); $self->fetch_medlinexref($pubid); return $self; } sub fetch_by_medlineid { my $self = shift; my $medlineid = shift; print STDERR "fetch_by_medlineid($medlineid) called\n"; _connect() unless $dbh; unless ($STH_MEDLINE2PUBID){ $STH_MEDLINE2PUBID = $dbh->prepare(q{ select pubid from datalib.Pub_xref where primaryid = ? and dbcode='M' })|| die "$DBI::errstr"; } if ($STH_MEDLINE2PUBID->execute($medlineid)==1){ my ($pubid)=$STH_MEDLINE2PUBID->fetchrow_array; print STDERR "got PUBID $pubid\n"; $self->fetch_titleandyear($pubid); $self->fetch_authors($pubid); $self->fetch_journalarticle($pubid); } $self->fetch_authors($pubid); return $self; } sub fetch_titleandyear { my $self = shift; my $pubid = shift; unless ($STH_PUBLICATION){ $STH_PUBLICATION = $dbh->prepare(q{ select to_char(pubdate,'YYYY'),title from datalib.Publication where pubid = ? })|| die "$DBI::errstr"; } if ($STH_PUBLICATION->execute($pubid)==1){ my ($pubdate,$title)=$STH_PUBLICATION->fetchrow_array; $self->year($pubdate) if $pubdate; $self->RT($title) if $title; } } sub fetch_authors { my $self = shift; my $pubid = shift; # print STDERR "fetch_authors($pubid) called\n"; unless ($STH_PUBAUTHOR){ $STH_PUBAUTHOR = $dbh->prepare(q{ select surname,firstname from datalib.Pubauthor a, datalib.Person p where a.person = p.personid and a.pubid = ? })|| die "$DBI::errstr"; } $self->RA(); $STH_PUBAUTHOR->execute($pubid); while(my ($surname,$firstname)=$STH_PUBAUTHOR->fetchrow_array){ my $name; $name = $surname if $surname; $name .= " $firstname" if $firstname; $self->add_Author($name) if $name; } } sub fetch_journalarticle { my $self = shift; my $pubid = shift; # print STDERR "fetch_journalarticle($pubid) called\n"; unless ($STH_JOURNALARTICLE){ $STH_JOURNALARTICLE = $dbh->prepare(q{ select a.issn,jn.embl_abbrev,a.volume,a.issue,a.firstpage,a.lastpage from datalib.Journalarticle a, datalib.cv_journal jn where a.issn = jn.issn# and a.pubid = ? })|| die "$DBI::errstr"; } if ($STH_JOURNALARTICLE->execute($pubid)==1){ my ($issn,$name,$vol,$issue,$fpage,$lpage)= $STH_JOURNALARTICLE->fetchrow_array; if ($issn && $issn !~ /^EMBL/){ $self->issn($issn); my $proper_name = SWISS::Journal::issn2name($issn); if ($proper_name){ carp "Mapped ISSN $issn to '$proper_name'" if $main::opt_debug; $name = $proper_name; } } $self->volume($vol) if $vol; my $pages = '0-0'; $pages = (sprintf "%0d-%0d",$fpage,$lpage) if $fpage && $lpage; $self->pages($pages); my $year=$self->year(); $year |= '0'; $vol |= '0'; my $rl = "$name $vol:$pages($year)"; $self->RL($rl); } else { $self->fetch_acceptedarticle($pubid); } } sub fetch_acceptedarticle { my $self = shift; my $pubid = shift; unless ($STH_ACCEPTEDARTICLE){ $STH_ACCEPTEDARTICLE = $dbh->prepare(q{ select a.issn,jn.embl_abbrev,a.volume,a.issue,a.firstpage,a.lastpage from datalib.Accepted a, datalib.cv_journal jn where a.issn = jn.issn# and a.pubid = ? })|| die "$DBI::errstr"; } if ($STH_ACCEPTEDARTICLE->execute($pubid)==1){ my ($issn,$name,$vol,$issue,$fpage,$lpage)= $STH_ACCEPTEDARTICLE->fetchrow_array; if ($issn && $issn !~ /^EMBL/){ $self->issn($issn); my $proper_name = SWISS::Journal::issn2name($issn); if ($proper_name){ carp "Mapped ISSN $issn to '$proper_name'" if $main::opt_debug; $name = $proper_name; } } unless ($name) { $name=''; carp "No journal name" if $main::opt_warn; } $self->volume($vol) if $vol; $vol |= '0'; my $pages = '0-0'; $fpage |= '0'; $lpage |= $fpage; $pages = $fpage.'-'.$lpage if $fpage && $lpage; $self->pages($pages); my $year=$self->year(); $year |= '0'; my $rl = "$name $vol:$pages($year)"; $self->RL($rl); } } sub fetch_medlinexref { my $self = shift; my $pubid = shift; # print STDERR "fetch_medlinexref($pubid) called\n"; unless ($STH_MEDLINEXREF){ $STH_MEDLINEXREF = $dbh->prepare(q{ select primaryid from datalib.Pub_xref where pubid = ? and dbcode='M' })|| die "$DBI::errstr"; } if ($STH_MEDLINEXREF->execute($pubid)==1){ my ($muid) = $STH_MEDLINEXREF->fetchrow_array; $self->RX(); $self->add_MedlineID($muid); } } sub _connect { carp "Connecting..." if $main::opt_debug; $dbh = DBI->connect('dbi:Oracle:','/@PRDB1','', {PrintError => 1})|| die "Cannot connect to server: $DBI::errstr\n"; } sub _disconnect { if ($dbh){ carp "Disconnecting..." if $main::opt_debug; $dbh->disconnect; undef $dbh; } } BEGIN { #print STDERR "Loading package SWISS::Ref::Oracle.pm\n"; } DESTROY { # _disconnect() if $dbh; } 1; swissknife-1.67/lib/SWISS/Ref/TitleStore/0000755000175100017510000000000011040133466020004 5ustar moellermoellerswissknife-1.67/lib/SWISS/Ref/TitleStore/EMBLOracle.pm0000644000175100017510000000526407563757501022237 0ustar moellermoellerpackage SWISS::Ref::TitleStore::EMBLOracle; use Fcntl; use Carp; use DBI; use DBD::Oracle; use SWISS::Entry; use Utils qw(_print_args); %MANDATORY_PARAMS = ( ); %DEFAULT_PARAMS = ( Access => O_RDONLY, ); # RDONLY RDWR APPEND CREAT EXCL TRUNC sub TIEHASH { &_print_args; my $class = shift; my $params = shift; my %tmp = %$params if $params; my $self = {}; %$self=%tmp if %tmp; bless $self, $class; # set not specified parameters to their default foreach $param (keys %DEFAULT_PARAMS){ next if exists $self->{$param}; $self->{$param} = $DEFAULT_PARAMS{$param}; } # check if all the required parameters are set foreach $param (keys %MANDATORY_PARAMS){ next if $self->{$param}; die "Mandatory argument '$param' is missing. ". $MANDATORY_PARAMS{$param}; } print STDERR "Connecting...\n" if $main::opt_debug; $self->{CON} = DBI->connect('dbi:Oracle:','/@PRDB1','', {}); unless ($self->{CON}){ croak "Can't connect to server: $DBI::errstr\n"; return 0; } print STDERR "Connected.\n" if $main::opt_debug; return $self; } sub FETCH { &_print_args; my $self = shift; my $key = shift; my $connection=$self->{CON}; unless ($self->{CURSOR}){ $self->{CURSOR} = $connection->prepare (q{ select primaryid as medlineid, title from datalib.pub_xref, datalib.publication where pub_xref.primaryid=? and pub_xref.dbcode='M' and pub_xref.pubid=publication.pubid }) || die "$DBI::errstr"; } $self->{CURSOR}->execute($key) || die "$DBI::errstr"; my ($muid,$title)=$self->{CURSOR}->fetchrow_array; return $title; } sub STORE { &_print_args; my $self = shift; die "Storing is not permitted. Sorry"; } sub CLEAR { &_print_args; my $self = shift; die "Deleting is not permitted. Sorry"; } sub EXISTS { &_print_args; my $self = shift; my $key = shift; my $title = $self->FETCH($key); return $title ? 1 : 0; } sub FIRSTKEY { &_print_args; my $self = shift; my $connection=$self->{CON}; my $key = undef; if ($self->{KEYCURSOR}){ print STDERR "finishing keycursor\n"; $self->{KEYCURSOR}->finish(); } $self->{KEYCURSOR} = $connection->prepare (q{ select primaryid as medlineid from datalib.pub_xref }) || die "$DBI::errstr"; $self->{KEYCURSOR}->execute; ($key) = $self->{KEYCURSOR}->fetchrow_array; return $key; } sub NEXTKEY { &_print_args; my $self = shift; my $lastkey = shift; my $key = undef; ($key) = $self->{KEYCURSOR}->fetchrow_array; unless ($key){ $self->{KEYCURSOR}->finish; undef ($self->{KEYCURSOR}); } return $key; } # * debuggin 1; swissknife-1.67/lib/SWISS/Ref/PubMed.pm0000644000175100017510000002120407563757500017437 0ustar moellermoellerpackage SWISS::Ref::PubMed; use Socket; use Carp; $caching = 0; $HOST = 'www.ncbi.nlm.nih.gov'; $PORT = 80; $PATH = '/htbin-post/Entrez/query?'; %CACHE=(); %REFCACHE=(); sub fetch_by_medlineid { my $self = new SWISS::Ref; my $medlineid = shift; carp "fetch_by_medlineid($medlineid) called" if $main::opt_debug>2; if ($caching) { my $cached=$REFCACHE{$medlineid}; if ($cached){ #print STDERR "!!!Cache hit '$medlineid'\n"; return $cached; } } my $page = get_pubmed_page("uid=$medlineid".'&form=6&dopt=l&db=m&html=no'); return unless $page; if ($page !~ /^UI - (\d+)/){ carp "Medline ID $medlineid not found" if $main::opt_warn>1; } elsif ($medlineid ne $1) { carp "Got medline ID $1 instead of $medlineid" if $main::opt_warn>1; } else { $self->fromMedlars(\$page); $REFCACHE{$medlineid}=$self if $caching; } return $self; } sub fetch_by_fields { my $ref = shift; my $self = new SWISS::Ref; carp "fetch_by_fields() called" if $main::opt_debug>2; my $query = toPubMedQuery($ref); #print STDERR "QUERY=$query\n"; my $head ='form=4&db=m&dopt=l&html=no&term='; # Have we asked this question already? my ($number,$id); if (defined $CACHE{$query}){ ($number,$id) = split(' ',$CACHE{$query}); if (defined $id){ #print STDERR "!!!POSITIVE cache hit '$id'\n"; return SWISS::Ref::PubMed::fetch_by_medlineid($id); } else { #print STDERR "!!!NEGATIVE cache hit\n"; return undef; } } else { $number = count_pubmed_page($head.$query); if ($number == 1){ my $page = get_pubmed_page($head.$query); $self->fromMedlars(\$page); $id = $self->get_MedlineID(); $CACHE{$query}="$number $id"; $REFCACHE{$id}=$self; return $self; } else { $CACHE{$query}= $number; return undef; } } return undef; } sub toPubMedQuery { my $ref = shift; $ref->unpackRL(); my @query=(); if (defined ($ref->issn)){ push @query, $ref->issn.'[JOUR]'; } elsif (defined ($ref->journal)) { my $issn = SWISS::Journal::name2issn($ref->journal); push @query, $issn.'[JOUR]' if $issn; } push @query, $ref->year."[PDAT]" if defined($ref->year) &&$ref->year; if (defined ($ref->volume)){ push @query, $ref->volume."[VOL]" if $ref->volume; } if (defined ($ref->pages)){ my ($firstpage)= $ref->pages =~ /^(\d+)/; push @query, $firstpage."[PAGE]" if $firstpage; } # journal,year,volume,pages is enough to query, but if something # is missing, we add the authors to the query unless (($ref->issn||$ref->journal)&& ($ref->year)&&($ref->volume)&&($ref->pages)) { if (defined ($ref->RA)){ my @au = @{$ref->RA()->list}; my $n=0; foreach $author (@au){ last if ++$n>10; $author =~ s/\.//g; $author =~ s/\s(Jr|II|III)$//ig; $author =~ s/(\w)-(\w)$/$1$2/g; $author =~ s/^(\w+).*/$1/; $author =~ tr/ /+/d; $query .= '+' unless $query; push @query, $author."[AUTH]"; } } } my $query = join('+and+',@query); return $query; } sub count_pubmed_page { my $query = shift; # make sure the 'count' flag is set in the query string ($query =~ s/\&dopt=\w/&dopt=q/) || ($query .= '&dopt=q'); my ($code,$page) = web_get_retry($HOST,$PORT,$PATH.$query); if ($code ne 200) { return -1; } else { if ($page =~ /(\d+)/){ return $1; } else { return -1; } } } sub get_pubmed_page { my $query = shift; my ($code,$page) = web_get_retry($HOST,$PORT,$PATH.$query); if ($code eq 200 && $page){ $page =~ s/^Entrez Reports\n-+\n//m; $page =~ s/^No Documents Found[^\n]*\n//m; return $page; } else { return undef; } } sub web_get_retry { my ($code,$page); while (($code,$page)=web_get(@_)){ last if $code ne -1; carp "Retrying" if $main::opt_debug; } return ($code,$page); } sub web_get { my ($host,$port,$url) = @_; my $code = -1; my $page; my ($proto,$local_host,$local_sock,$remote_sock); my $sockaddr='S n a4 x8'; my ($status,$line,$info); my $save = $/; $/="\n"; $proto = getprotobyname('tcp'); chop($local_host=`hostname`); $local_sock=pack($sockaddr,AF_INET,0,(gethostbyname($local_host))[4]); $remote_sock=pack($sockaddr,AF_INET,$port,(gethostbyname($host))[4]); unless (socket(S, PF_INET, SOCK_STREAM, $proto)){ croak "socket: $!"; return -1; } setsockopt(S, SOL_SOCKET, SO_KEEPALIVE, pack("l",1)) or die "setsockopt: $!"; bind(S,$local_sock) || die "$0: bind: $!\n"; eval { connect(S, $remote_sock); }; if ($@){ croak "connect: $@"; return -1; } $_=select(S); $|=1; select($_); carp "URL=$url\n" if $main::opt_debug>1; print S "GET $url HTTP/1.0\rn" . "User-Agent: None/1.0\r\nAccept: */*\r\n\r\n"; if (defined(S) && defined($status=)){ chop($status); $status=~s/\r$//; ($code,$info)=($status=~m!^HTTP\S+\s+(\d\d\d)\s*(.*)$!i); carp "STATUS: $code - $info -\n" if $main::opt_debug>2; if ($code==200){ while(defined($line=)){ last if $line=~/^\r$/; carp "HEADER: ",$line if $main::opt_debug>3; } $page = ''; while(defined($line=)){ carp $line if $main::opt_debug>3; $page .= $line; } } } else { $code = '-1'; } close(S); $/=$save; return ($code,$page); } package SWISS::Ref; use SWISS::Journal; sub fromPubMed{ my $self = shift; my $medlineid = $self->get_MedlineID(); if ($medlineid){ return SWISS::Ref::PubMed::fetch_by_medlineid($medlineid); } else { return SWISS::Ref::PubMed::fetch_by_fields($self); } return undef; } sub fromMedlars { my $self = shift; my $textRef = shift; # Parse Medline ID if ($$textRef =~ /^UI - (\d+)/m){ $self->add_MedlineID($1); } # Parse RA while($$textRef =~ /^AU - (.*)/mg){ my $author = $1; my $suffix; if ($author =~ /et al/i) { $self->{'etal'}=1; next; } ($author =~ s/\sJr$//) && ($suffix=' JR.'); ($author =~ s/\s2nd$//) && ($suffix=' II.'); ($author =~ s/\s3rd$//) && ($suffix=' III.'); if ($author =~ /^(.*)\s([A-Z]+)$/){ $author = "$1 ".join('.',split('',$2))."."; } $author .= $suffix if $suffix; $self->add_Author($author); } # Parse RT if ($$textRef =~ /^TI - ([^\n]+(\s\s\s\s\s\s[^\n]+\n)*)/m){ my $title = $1; $title =~ s/\n\s+/\n/mg; $title =~ s/-\n/-/mg; $title =~ s/\n/ /mg; $title =~ s/^\[(.*)\]$/$1/mg; $title =~ s/[\.\s]+$//g; $title =~ s/\s\[see comments\]\s*//; $title =~ s/\s\[letter[^\]]*\]\s*//g; $title =~ s/\s\[comment[^\]]*\]\s*//g; $title =~ s/\s\[news\]\s*//; $title =~ s/\s\[editorial\]\s*//; #$title =~ s/ \[.+?\]$//mg; $self->RT($title); carp "Found title '$title'" if $main::opt_debug>1; } my ($journal,$vol,$pages,$year) = ('','0','0-0','0'); my $issn; # Parse Journal if ($$textRef =~ /^TA - (.*)/m){ $journal = $1; } # Parse ISSN if ($$textRef =~ /^IS - (\d\d\d\d-\d\d\d[\dXx])/m){ $issn = $1; carp "Found ISSN $issn" if $main::opt_debug>1; } else { carp "No ISSN found" if $main::opt_warn; } # Getting the proper journal name for Swissprot usage is tricky my $proper_name=''; # if pubmed has an issn which is in our lookup list (SWISS::Journal), # we take this looked-up name if ($issn && ($proper_name = SWISS::Journal::issn2name($issn))){ $journal = $proper_name; carp "Mapped ISSN $issn to '$proper_name'" if $main::opt_debug>2; } if (!$proper_name && ($proper_name = SWISS::Journal::name2swiss($journal))){ $journal = $proper_name; carp "Mapped journal '$name' to '$proper_name'" if $main::opt_debug>2; } if (!$proper_name && $main::opt_warn){ carp "Cant find the proper name for journal '$journal'"; } # Parse Volume if ($$textRef =~ /^VI - (.*)/m){ $vol = $1; $vol =~ s/^(\d+)\s+\S+.*$/$1/; } # Parse Pages if ($$textRef =~ /^PG - (.*)/m){ # handle the american way of paging "125-6" -> "125-126" $pages = $1; my $prefix; if ($pages =~ s/^(\D+)//) { $prefix = $1; } $pages =~ s/,.*$//; my ($from,$to)=split('-',$pages); if ($from && $to && $from>$to){ $pages = $from.'-'.substr($from,0,length($from)-length($to)).$to; } $pages = $prefix.$pages if $prefix; # reformat page '317' to SWISS-PROT format '317-317' if ($pages !~ /-/){ $pages = "$pages-$pages"; } } # Parse Year if ($$textRef =~ /^DP - (\d\d\d\d)/m){ $year = $1; } if ($main::opt_debug>1){ carp "Found reference '$journal|$vol|$pages|$year'"; } my $rl = "$journal $vol:$pages($year)"; $self->issn($issn) if $issn; $self->RL($rl); return $self; } 1; swissknife-1.67/Build.PL0000644000175100017510000000126010154041056015005 0ustar moellermoelleruse 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 => [ 'Alexandre Gattiker ', 'Paul Kersey ', 'Henning Hermjakob ', 'Wolfgang Fleischmann ', ], dist_abstract=> 'Handle entries in Swiss-Prot format', ); $build->create_build_script; swissknife-1.67/docs/0000755000175100017510000000000011040133466014444 5ustar moellermoellerswissknife-1.67/docs/SQs.html0000644000175100017510000000506111040133423016033 0ustar moellermoeller 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-1.67/docs/OS.html0000644000175100017510000000276711040133422015657 0ustar moellermoeller 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-1.67/docs/Stars.html0000644000175100017510000000553411040133423016426 0ustar moellermoeller 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-1.67/docs/DEs.html0000644000175100017510000001602511040133420015777 0ustar moellermoeller 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-1.67/docs/OH.html0000644000175100017510000000327311040133422015635 0ustar moellermoeller 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-1.67/docs/KW.html0000644000175100017510000000306711040133421015650 0ustar moellermoeller 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-1.67/docs/OHs.html0000644000175100017510000000303011040133422016007 0ustar moellermoeller 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-1.67/docs/GNs.html0000644000175100017510000001675711040133421016030 0ustar moellermoeller 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-1.67/docs/IDs.html0000644000175100017510000000475011040133421016006 0ustar moellermoeller 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-1.67/docs/index.html0000644000175100017510000003047411040130245016441 0ustar moellermoeller 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 ftp://ftp.ebi.ac.uk/pub/software/swissprot/Swissknife/.
The development version is now 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 secs ( 0.39 usr +  0.01 sys =  0.40 CPU)
          (warning: too few iterations for a reliable count)
Read/Write NULL:       :  1 secs ( 0.95 usr  0.05 sys =  1.00 cpu)
Read/Write:            :  1 secs ( 0.97 usr  0.10 sys =  1.07 cpu)
Read/Write/addAC:      :  2 secs ( 1.62 usr  0.08 sys =  1.70 cpu)
Read/Write/Fullparse:  : 23 secs (22.48 usr  0.17 sys = 22.65 cpu)
Read/Write/Fp/Update:  : 35 secs (34.40 usr  0.18 sys = 34.58 cpu)
Read/equals:           : 13 secs (13.67 usr  0.03 sys = 13.70 cpu)
Read/Write/Modify:     : 10 secs ( 9.52 usr  0.12 sys =  9.63 cpu)

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 ***
 
crc64...............ok
DEs.................ok
evidence............ok
formatProblems......ok
GNs.................ok
identity............ok
All tests successful.
Files=6,  Tests=12,  3 wallclock secs ( 3.19 cusr +  0.14 csys =  3.33 CPU)

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.
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/EV.pm Stars/EV.html Evidence section.
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 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.

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-1.67/docs/OSs.html0000644000175100017510000000341611040133422016032 0ustar moellermoeller 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.

Inherits from

SWISS::ListBase.pm

Attributes

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

Methods

Standard methods

new
fromText
toText
swissknife-1.67/docs/KWs.html0000644000175100017510000000355411040133422016035 0ustar moellermoeller 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-1.67/docs/CCseq_caution.html0000644000175100017510000000366511040133420020052 0ustar moellermoeller 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-1.67/docs/CRC64.html0000644000175100017510000000524611040133420016110 0ustar moellermoeller 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-1.67/docs/CCcopyright.html0000644000175100017510000000415411040133417017550 0ustar moellermoeller 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-1.67/docs/ListBase.html0000644000175100017510000002456711040133422017046 0ustar moellermoeller 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-1.67/docs/OGs.html0000644000175100017510000000325611040133422016020 0ustar moellermoeller 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-1.67/docs/CC.html0000644000175100017510000000415711040133417015622 0ustar moellermoeller 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-1.67/docs/Refs.html0000644000175100017510000000334711040133423016231 0ustar moellermoeller 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-1.67/docs/TextFunc.html0000644000175100017510000001144411040133424017070 0ustar moellermoeller 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-1.67/docs/OX.html0000644000175100017510000000314511040133423015654 0ustar moellermoeller 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-1.67/docs/Entry.html0000644000175100017510000001432611040133421016430 0ustar moellermoeller 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-1.67/docs/ACs.html0000644000175100017510000000555411040133417016005 0ustar moellermoeller 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-1.67/docs/DE.html0000644000175100017510000001062511040133420015614 0ustar moellermoeller 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-1.67/docs/BaseClass.html0000644000175100017510000001522311040133417017171 0ustar moellermoeller 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-1.67/docs/Ref.html0000644000175100017510000000675411040133423016053 0ustar moellermoeller 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-1.67/docs/FTs.html0000644000175100017510000000370611040133421016023 0ustar moellermoeller 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-1.67/docs/OG.html0000644000175100017510000000346711040133422015641 0ustar moellermoeller 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-1.67/docs/Stars/0000755000175100017510000000000011040133424015532 5ustar moellermoellerswissknife-1.67/docs/Stars/default.html0000644000175100017510000000340111040133424020042 0ustar moellermoeller 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-1.67/docs/Stars/EV.html0000644000175100017510000001070311040133424016733 0ustar moellermoeller SWISS::Stars::EV

new

toText

sort

addEvidence($category, $type, $initials, $attributes [, $date])

 Title:    addEvidence
 Usage:    $evidenceTag = $entry->Stars->EV->addEvidence($category,
                                                         $type, 
                                                         $initials,
                                                         $attributes 
                                                         [, $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:    $category: the evidence category. Currently one of 'A', 'C', 'I','P'.
          $type: the evidence type
          $initials: The initals of the person doing the update.
                     For programs this should be '-'.
          $attributes: the attributes of the evidence
          $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($category, $type, $initials, $attributes [, $date])

 Title:    updateEvidence
 Usage:    $evidenceTag = $entry->Stars->EV->updateEvidence($category, 
                                                            $type, 
                                                            $initials,
                                                            $attributes 
                                                            [, $date])
 Function: updates the evidence to the EV block to $date or inserts it 
           if it does not yet exist.
 Args:    $category: the evidence category. Currently one of 'A', 'C', 'I','P'.
          $type: the evidence type
          $initials: The initals of the person doing the update.
                     For programs this should be '-'.
          $attributes: the attributes of the evidence
          $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-1.67/docs/Stars/aa.html0000644000175100017510000000333211040133424017002 0ustar moellermoeller SWISS::Stars::aa

Name

SWISS::aa.pm

Description

SWISS/Stars/aa.pm represents the unstructured part of the ``annotator's 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
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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-1.67/docs/PE.html0000644000175100017510000000302611040133423015630 0ustar moellermoeller 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-1.67/docs/GN.html0000644000175100017510000000447311040133421015635 0ustar moellermoeller 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-1.67/docs/RCelement.html0000644000175100017510000000341311040133423017202 0ustar moellermoeller 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-1.67/docs/Journal.html0000644000175100017510000000073111040133421016734 0ustar moellermoeller SWISS::Journal

swissknife-1.67/docs/CCbpc_properties.html0000644000175100017510000000456711040133417020570 0ustar moellermoeller 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 fields in a given property in this comment. Each field is a reference to an array of [$field, $text, $evidence_tags]. $field is undefined for unnamed fields.

Standard methods

new
fromText
toString

Returns a string representation of this comment.

swissknife-1.67/docs/CCs.html0000644000175100017510000001043711040133420015775 0ustar moellermoeller 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-1.67/docs/CCinteraction.html0000644000175100017510000000366511040133420020057 0ustar moellermoeller 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-1.67/docs/OXs.html0000644000175100017510000000411411040133423016034 0ustar moellermoeller 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-1.67/docs/DTs.html0000644000175100017510000000734211040133420016020 0ustar moellermoeller 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-1.67/docs/CCrna_editing.html0000644000175100017510000000445211040133420020016 0ustar moellermoeller 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.

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-1.67/docs/CCalt_prod.html0000644000175100017510000003424011040133417017343 0ustar moellermoeller 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";
  
 ## 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";
 
 ## 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");
 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.

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''.

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''.

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''.

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''.

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-1.67/docs/DRs.html0000644000175100017510000001101511040133420016006 0ustar moellermoeller 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

Writing methods

deleteUnlessEvidenceCategories $evidenceCategories, @patterns

Like del, but deletes an item only if the item has no evidence tags, or if the evidence tags are not in one of the categories given in $evidenceCategories.

Example:

$entry->DRs->deleteUnlessEvidenceCategories('CA', 'FlyBase')

will only delete Flybase DR lines which do not have the evidence category 'A' or 'C'.

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-1.67/docs/GeneGroup.html0000644000175100017510000000762711040133421017230 0ustar moellermoeller 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-1.67/t/0000755000175100017510000000000011040133466013757 5ustar moellermoellerswissknife-1.67/t/formatProblems.txl0000644000175100017510000032217010745674514017530 0ustar moellermoellerID 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, and OS Salmonella enterica serovar Choleraesuis. 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, and Bacteriophage SP01. 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 TYEGKHNHHLLLSPPSSSTLPFNSPQLSKQTI->SLQPTR FT IIIICS: In ttg2-2; defects in trichome FT development, seed coat color and mucilage FT production. 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-1.67/t/annot.txl0000644000175100017510000006427610745674576015675 0ustar moellermoellerID 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-1.67/t/DEs.txl0000644000175100017510000004202010357506347015175 0ustar moellermoellerID 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-1.67/t/formatProblems.txl.expected0000644000175100017510000032212511037057007021313 0ustar moellermoellerID 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 DE (EC 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, and OS Salmonella enterica serovar Choleraesuis. 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 HSSP; Q06787; 2FMR.{EI1} DR MGI; MGI:104860; Fxr1h.{EI2} DR INTERPRO; IPR000958; -. DR PFAM; PF00013; KH-domain; 2. 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: 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 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, and OS Bacteriophage SP01. 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 // 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 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 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: 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 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: 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 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 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 TYEGKHNHHLLLSPPSSSTLPFNSPQLSKQTI->SLQPTRI FT IIICS: In ttg2-2; defects in trichome FT development, seed coat color and mucilage FT production. 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-1.67/t/fasta.txl0000644000175100017510000000411010674520145015610 0ustar moellermoellerID 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 // swissknife-1.67/t/test.pl0000644000175100017510000000072310366115237015303 0ustar moellermoeller#!/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-1.67/t/fasta.txl.expected0000644000175100017510000000162011037055440017406 0ustar moellermoeller>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 swissknife-1.67/t/evidence.txl0000644000175100017510000000541210626343425016303 0ustar moellermoellerID 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){EC3}. GN GOT2{EI1}. OS Bos taurus (Bovine){EI1}, OS Mus musculus (Mouse), and OS Rattus sp{EI2}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=126566, 55{EC2}; RN [1]{EI1} RP SEQUENCE FROM N.A. RC TISSUE=HEART; RA Palmisano A.; RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases. RN [2]{EI1} 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 RT sequence and crystallographic data."; RL FEBS Lett. 101:351-354(1979). CC -!- CATALYTIC ACTIVITY: L-ASPARTATE + 2-OXOGLUTARATE = OXALOACETATE + CC L-GLUTAMATE{EC3}. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE{EC3}. CC -!- SEQUENCE CAUTION: CC Sequence=CAI22254{EC1,EI1}; Type=Miscellaneous discrepancy; Positions=Several; Note=Translated as Gln; CC Sequence=CAI21743; Type=Erroneous gene model prediction; DR EMBL; Z25466; CAA80960.1; -.{EI1} DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Transferase{EC2}; Aminotransferase{EC2}. FT TRANSIT 1 29 MITOCHONDRION{EC2}. FT CHAIN 30 430 ASPARTATE AMINOTRANSFERASE{EC2}. FT BINDING 279 279 PYRIDOXAL PHOSPHATE (BY SIMILARITY){EC3}. FT VARIANT 3 3 A -> L{EC3}. 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-1.67/t/identity.txl.expected0000644000175100017510000277206011037062205020155 0ustar moellermoellerID 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; PR01251; AMPHIPHYSIN. DR PRINTS; PR01252; AMPHIPHYSIN1. DR PRINTS; PR00452; SH3DOMAIN. 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; 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 HSSP; Q01082; 1AA2. 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. ** ** ################# 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; 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 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}, OS Other Bacterium, and OS Salmonella enterica serovar Choleraesuis. 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 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; 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. 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 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; 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. 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 WormPep; R09F10.2; CE07436. DR WormPep; 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; WORMPEP_ADD; -; R09F10.2; 23-MAY-2004. **EV EI2; WORMPEP_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 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: 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 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 // swissknife-1.67/t/FTId.t0000644000175100017510000000140410265736434014745 0ustar moellermoeller# 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 ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}FTId.txl"; my $testout = "${where}FTId.txl.out"; my $expectedout = "${where}FTId.txl"; open (IN, $testin); open (OUT, ">$testout"); local $/ = "//\n"; while (){ $entry = SWISS::Entry->fromText($_, 1, 1); print OUT $entry->toText(); } close IN; close OUT; test 2, system('diff', $testout, $expectedout) == 0, "diff $testout $expectedout"; swissknife-1.67/t/GNs.t0000644000175100017510000000446010225167417014646 0ustar moellermoeller# Swissknife Test Harness Script for GNs # # Purpose: # Check whether the advanced parser in GNs works well. # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($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-1.67/t/util.t0000644000175100017510000000132110225167420015117 0ustar moellermoeller# 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 ($$;$) { my($num, $true,$msg) = @_; print($true ? "ok $num\n" : "not ok $num $msg\n"); } my $where = -d 't' ? "t/" : ""; my $testin = "${where}util.txl"; open (IN, $testin); use SWISS::Entry; # Check reply from isCurated(): # Read an entire record at a time $/ = "\/\/\n"; # Read the entries while (){ $entry = SWISS::Entry->fromText($_); push @results, $entry->isCurated(); } test 2, (join "",@results) eq "100"; swissknife-1.67/t/evidence.t0000644000175100017510000000602510626343425015740 0ustar moellermoeller## Swissknife Test Harness Script for evidence tags ## # * Test loading BEGIN { $| = 1; print "1..2\n"; use vars qw($loaded); $^W = 0; } END {print "not ok 1\n" unless $loaded;} $loaded = 1; print "ok 1\n"; # 1st test passes. sub test ($$;$) { my($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('EC2'); } $ev1 = $entry->Stars->EV->addEvidence('P', 'TestProgram1', '-', 'XXX', '10-JUL-2000'); $ev2 = $entry->Stars->EV->addEvidence('P', 'TestProgram2', '-', 'XXX', '10-JUL-2000'); $ev3 = $entry->Stars->EV->addEvidence('P', 'TestProgram3', '-', 'XXX', '10-JUL-2000'); $entry->DEs->setEvidenceTags($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, 'EC2'); $entry->DRs->deleteEvidenceTag($dr, $ev2); } # Check conditional delete $entry->DRs->add(['ZFIN', 'P123', 'Q1234', '{EA4}']); $entry->DRs->add(['ZFIN', 'P123', 'Q1234', '{EC6}']); $entry->DRs->deleteUnlessEvidenceCategories('C', 'ZFIN'); foreach $ft ($entry->FTs->elements) { $entry->FTs->addEvidenceTag($ft, 'EC2'); $entry->FTs->deleteEvidenceTag($ft, 'EC3'); } 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('EC2'); $os->deleteEvidenceTag('EC2'); } # 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-1.67/t/DEs.t0000644000175100017510000000322010225167417014623 0ustar moellermoeller# 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-1.67/t/util.txl0000644000175100017510000002142607432502662015502 0ustar moellermoellerID 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-1.67/t/FTId.txl0000644000175100017510000000073010265736434015312 0ustar moellermoellerID 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-1.67/t/fasta.t0000644000175100017510000000152310500233441015235 0ustar moellermoeller# 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-1.67/t/identity.txl0000644000175100017510000277166011037062152016363 0ustar moellermoellerID 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}, OS Other Bacterium, and OS Salmonella enterica serovar Choleraesuis. 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 WormPep; R09F10.2; CE07436. DR WormPep; 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; WORMPEP_ADD; -; R09F10.2; 23-MAY-2004. **EV EI2; WORMPEP_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 // swissknife-1.67/t/annot.t0000644000175100017510000000241410225167417015273 0ustar moellermoeller# 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-1.67/t/evidence.txl.expected0000644000175100017510000000634410626343425020110 0ustar moellermoellerHas evidence EP5. TRANSIT,1,29,MITOCHONDRION,,,{EC2}, CHAIN,30,430,ASPARTATE AMINOTRANSFERASE,,,{EC2}, BINDING,279,279,PYRIDOXAL PHOSPHATE,BY SIMILARITY,,{EC2}, VARIANT,3,3,A -> L,,/FTId=VAR_000001,{EC2}, VARIANT,3,3,A -> LFSJFSHLJSDHFLSJLFHSJLLSJKDHFLSKJFHJ,,/FTId=VAR_000002,{EC2}, 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){EP6,EP5}. GN GOT2{EI1}. OS Bos taurus (Bovine){EI1}, OS Mus musculus (Mouse), and OS Rattus sp{EI2}. 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,EC2} RP SEQUENCE FROM N.A. RC TISSUE=HEART; RA Palmisano A.; RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases. RN [2]{EI1,EC2} 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,EP4}. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE{EC3,EP4}. 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; DR EMBL; Z25466; CAA80960.1; -.{EI1,EC2} DR ZFIN; P123; Q1234.{EC6} DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.{EC2} KW Transferase{EP5}; Aminotransferase{EP5}; Key1{EP6}; Key2. FT TRANSIT 1 29 MITOCHONDRION{EC2}. FT CHAIN 30 430 ASPARTATE AMINOTRANSFERASE{EC2}. FT BINDING 279 279 PYRIDOXAL PHOSPHATE (BY SIMILARITY){EC2}. FT VARIANT 3 3 A -> L{EC2}. FT /FTId=VAR_000001. FT VARIANT 3 3 A -> LFSJFSHLJSDHFLSJLFHSJLLSJKDHFLSKJFHJ FT {EC2}. FT /FTId=VAR_000002. ** ** ################# INTERNAL SECTION ################## **EV EC2; Curator; MM; 06-SEP-1989. **EV EC3; Curator; TT; 10-JUN-1999. **EV EI1; EMBL; CAA80960.1; 03-SEP-1989. **EV EP4; TestProgram1; -; XXX; 10-JUL-2000. **EV EP5; TestProgram2; -; XXX; 10-JUL-2000. **EV EP6; TestProgram3; -; XXX; 10-JUL-2000. **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-1.67/t/crc64.t0000644000175100017510000000200710366115237015072 0ustar moellermoeller# 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-1.67/t/identity.t0000644000175100017510000000303110225167417016001 0ustar moellermoeller# 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-1.67/t/annot.txl.expected0000644000175100017510000014556710745674612017467 0ustar moellermoellerID 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 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 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; **IS Q9H165-8. **NI BCLLA 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 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 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; **IS Q9H165-8. **NI BCLLA 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: 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: 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-1.67/t/formatProblems.t0000644000175100017510000000470210331445707017151 0ustar moellermoeller# 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-1.67/t/GNs.txl.expected0000644000175100017510000000135510001532100016763 0ustar moellermoellerGN (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-1.67/t/DEs.txl.expected0000644000175100017510000001162710357506347017006 0ustar moellermoellerURIDINE 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-1.67/examples/0000755000175100017510000000000011040133466015332 5ustar moellermoellerswissknife-1.67/examples/benchmark.pl0000644000175100017510000000564710366115237017643 0ustar moellermoeller#!/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-1.67/examples/SWISS100.dat0000755000175100017510000034020607563750765017213 0ustar moellermoellerID UPA3_HUMAN STANDARD; PRT; 9 AA. AC P30089; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 11) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.6, ITS MW IS: 46 kDa. DR SWISS-2DPAGE; P30089; HUMAN. FT NON_TER 1 1 FT NON_TER 9 9 SQ SEQUENCE 9 AA; 1056 MW; 26F2B1BAF769C737 CRC64; XPLFPXTDF // ID UPA4_HUMAN STANDARD; PRT; 10 AA. AC P30090; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 12) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.8, ITS MW IS: 40.5 kDa. CC -!- MISCELLANEOUS: THIS SPOT IS ON A POSITION THOUGHT TO BE THAT OF CC ZN-ALPHA-2 GLYCOPROTEIN, BUT IT DOES NOT CORRESPOND TO THAT CC PROTEIN. DR SWISS-2DPAGE; P30090; HUMAN. FT NON_TER 1 1 FT UNSURE 4 4 FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1067 MW; 269492EB05A1A457 CRC64; XVPNTSEXSN // ID UPA5_HUMAN STANDARD; PRT; 10 AA. AC P30091; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 13) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.85, ITS MW IS: 40 kDa. CC -!- MISCELLANEOUS: THIS SPOT IS ON A POSITION THOUGHT TO BE THAT OF CC ZN-ALPHA-2 GLYCOPROTEIN, BUT IT DOES NOT CORRESPOND TO THAT CC PROTEIN. DR SWISS-2DPAGE; P30091; HUMAN. FT NON_TER 1 1 FT VARIANT 9 9 G -> Y. FT /FTId=VAR_000002. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1109 MW; C3DA94C732C32776 CRC64; NVQPKVLVGR // ID UPA6_HUMAN STANDARD; PRT; 9 AA. AC P30092; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 14) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5, ITS MW IS: 48 kDa. DR SWISS-2DPAGE; P30092; HUMAN. FT NON_TER 1 1 FT NON_TER 9 9 SQ SEQUENCE 9 AA; 935 MW; 5282F2CAA8676447 CRC64; XLNPGDVXT // ID UPA7_HUMAN STANDARD; PRT; 9 AA. AC P30093; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 18) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.05, ITS MW IS: 37 kDa. DR SWISS-2DPAGE; P30093; HUMAN. FT NON_TER 1 1 FT UNSURE 5 5 FT NON_TER 9 9 SQ SEQUENCE 9 AA; 1042 MW; 5C14477AEB0772C7 CRC64; SLVPEXPYQ // ID UPA8_HUMAN STANDARD; PRT; 10 AA. AC P30094; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 34) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 7.2, ITS MW IS: 16 kDa. DR SWISS-2DPAGE; P30094; HUMAN. FT NON_TER 1 1 FT VARIANT 4 4 S -> H. FT /FTId=VAR_000003. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 977 MW; 2EA6E0C77AE325B8 CRC64; IVGSKXPAVP // ID UPA9_HUMAN STANDARD; PRT; 10 AA. AC P30095; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 35) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 7.2, ITS MW IS: 15 kDa. DR SWISS-2DPAGE; P30095; HUMAN. FT NON_TER 1 1 FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1233 MW; 37AD72B409C681B7 CRC64; XNPTMFRDNE // ID UPAA_HUMAN STANDARD; PRT; 8 AA. AC P30096; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 36) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 7, ITS MW IS: 12 kDa. DR SWISS-2DPAGE; P30096; HUMAN. FT NON_TER 1 1 FT VARIANT 5 5 F -> P. FT /FTId=VAR_000004. FT NON_TER 8 8 SQ SEQUENCE 8 AA; 909 MW; 86677B59D1A72042 CRC64; VILTFYPG // ID UPAB_HUMAN STANDARD; PRT; 16 AA. AC P31935; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-FEB-1994 (Rel. 28, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 53) (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=PLASMA; RX MEDLINE=94147970; PubMed=8313871; RA Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., RA Balant L., Hochstrasser D.F.; RT "Plasma and red blood cell protein maps: update 1993."; RL Electrophoresis 14:1223-1231(1993). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.9, ITS MW IS: 41 kDa. DR SWISS-2DPAGE; P31935; HUMAN. FT NON_TER 1 1 FT NON_CONS 7 8 FT NON_TER 16 16 SQ SEQUENCE 16 AA; 1879 MW; D63C5047818114B2 CRC64; GFQFLXLAYL EETKPL // ID URA1_HUMAN STANDARD; PRT; 10 AA. AC P32118; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein from 2D-page of red blood cells (Spot 1) (Fragment). 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=ERYTHROCYTE; RX MEDLINE=94147970; PubMed=8313871; RA Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., RA Balant L., Hochstrasser D.F.; RT "Plasma and red blood cell protein maps: update 1993."; RL Electrophoresis 14:1223-1231(1993). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.4, ITS MW IS: 23 kDa. DR SWISS-2DPAGE; P32118; HUMAN. FT NON_TER 1 1 FT NON_TER 10 10 SQ SEQUENCE 10 AA; 977 MW; 723C65B1ADD0587B CRC64; TDEGIATTGL // ID URA6_HUMAN STANDARD; PRT; 10 AA. AC P32080; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein from 2D-page of red blood cells (Spot 17) (Fragment). 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=ERYTHROCYTE; RX MEDLINE=94147970; PubMed=8313871; RA Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., RA Balant L., Hochstrasser D.F.; RT "Plasma and red blood cell protein maps: update 1993."; RL Electrophoresis 14:1223-1231(1993). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.4, ITS MW IS: 65 kDa. DR SWISS-2DPAGE; P32080; HUMAN. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 965 MW; 63DDC8D86AE1EDDB CRC64; ASEAHXGAVN // ID URA7_HUMAN STANDARD; PRT; 10 AA. AC P34990; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein from 2D-page of red blood cells (Spot 2D-006HO) DE (Fragment). 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=ERYTHROCYTE; RA Golaz O., Hughes G.J., Frutiger S., Paquet N., Bairoch A., RA Pasquali C., Sanchez J.-C., Tissot J.-D., Appel R.D., Walzer C., RA Balant L., Hochstrasser D.F.; RL Submitted (FEB-1994) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.77, ITS MW IS: 26 kDa. DR SWISS-2DPAGE; P34990; HUMAN. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1161 MW; F72D82E9C44B1871 CRC64; XXHGENFXDI // 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 01-JUL-1993 (Rel. 26, 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 NON_TER 1 1 FT UNSURE 6 6 FT NON_CONS 6 7 FT NON_CONS 12 13 FT UNSURE 17 17 FT NON_TER 19 19 SQ SEQUENCE 19 AA; 2087 MW; EF7515F79D50DE12 CRC64; HIGLVRLTPT EVQEPIITA // ID UKA2_HUMAN STANDARD; PRT; 12 AA. AC P31144; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-JUL-1993 (Rel. 26, Last annotation update) DE Unknown protein from 2D-page of epidermal keratinocytes (Spot 1617) 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: 6.93, ITS MW IS: 81.6 kDa. DR AARHUS/GHENT-2DPAGE; 1617; IEF. FT NON_TER 1 1 FT NON_CONS 7 8 FT UNSURE 8 8 FT NON_TER 12 12 SQ SEQUENCE 12 AA; 1351 MW; D6CD4A5E75F2C1F6 CRC64; DYLGQHVHLG GR // ID UKA6_HUMAN STANDARD; PRT; 32 AA. AC P31942; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-JUL-1993 (Rel. 26, Last annotation update) DE Unknown protein from 2D-page of epidermal keratinocytes (Spot 2222) 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: 6.55, ITS MW IS: 37.6 kDa. DR AARHUS/GHENT-2DPAGE; 2222; IEF. FT NON_TER 1 1 FT UNSURE 1 1 FT UNSURE 11 11 FT NON_CONS 11 12 FT UNSURE 12 12 FT UNSURE 21 22 FT NON_CONS 22 23 FT NON_TER 32 32 SQ SEQUENCE 32 AA; 3641 MW; 8519D900183287B1 CRC64; DGMDNQGGYG SSEIKGFYDP PREMEEXEYE EA // ID UKAH_HUMAN STANDARD; PRT; 27 AA. AC P31944; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 01-JUL-1993 (Rel. 26, Last annotation update) DE Unknown protein from 2D-page of epidermal keratinocytes (Spot 6109) 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: 5.47, ITS MW IS: 31.5 kDa. DR AARHUS/GHENT-2DPAGE; 6109; IEF. FT NON_TER 1 1 FT UNSURE 8 8 FT NON_CONS 9 10 FT UNSURE 10 10 FT UNSURE 17 17 FT NON_CONS 17 18 FT UNSURE 25 27 FT NON_TER 27 27 SQ SEQUENCE 27 AA; 2977 MW; F8FE8DA4700D66D7 CRC64; DSPQTIPTYF QQAIDSRDPX ETVGGDE // ID UHA1_HUMAN STANDARD; PRT; 13 AA. AC P40928; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Unknown protein from 2D-page of heart (Spot 4304) (Fragment). 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=HEART; RX MEDLINE=95203287; PubMed=7895732; RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.; RT "The human myocardial two-dimensional gel protein database: update RT 1994."; RL Electrophoresis 15:1459-1465(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.7, ITS MW IS: 35.5 kDa. FT NON_TER 13 13 SQ SEQUENCE 13 AA; 1380 MW; 6617BA7A1E06AB1B CRC64; LXYPXEEDGG NXG // ID UHA2_HUMAN STANDARD; PRT; 9 AA. AC P40929; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Unknown protein from 2D-page of heart (Spot 5603) (Fragment). 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=HEART; RX MEDLINE=95203287; PubMed=7895732; RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.; RT "The human myocardial two-dimensional gel protein database: update RT 1994."; RL Electrophoresis 15:1459-1465(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.0, ITS MW IS: 55.3 kDa. FT NON_TER 9 9 SQ SEQUENCE 9 AA; 1104 MW; 8874B1BB5B01B2CA CRC64; FDVTEYTDD // ID UHA3_HUMAN STANDARD; PRT; 10 AA. AC P40930; DT 01-FEB-1995 (Rel. 31, Created) DT 01-FEB-1995 (Rel. 31, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Unknown protein from 2D-page of heart (Spot 7513) (Fragment). 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=HEART; RX MEDLINE=95203287; PubMed=7895732; RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.; RT "The human myocardial two-dimensional gel protein database: update RT 1994."; RL Electrophoresis 15:1459-1465(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.8, ITS MW IS: 47.3 kDa. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1049 MW; 6BBCDE41A041B76B CRC64; AVEPTITYVG // ID UHA4_HUMAN STANDARD; PRT; 23 AA. AC P49289; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Unknown protein from 2D-page of heart (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=HEART; RX MEDLINE=96007936; PubMed=7498159; RA Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., RA Ershova E.S., Egorov T.A., Musalyamov A.K.; RT "The major protein expression profile and two-dimensional protein RT database of human heart."; RL Electrophoresis 16:1160-1169(1995). CC -!- CAUTION: WAS ORIGINALLY (REF.1) THOUGHT TO BE MITOCHONDRIAL CC ACONITASE. FT NON_TER 1 1 FT NON_CONS 16 17 FT NON_TER 23 23 SQ SEQUENCE 23 AA; 2388 MW; 90EF513CEEB8B451 CRC64; DINGEVINEL AATAGAIMET NLK // ID UHA1_CANFA STANDARD; PRT; 14 AA. AC P99503; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein from 2D-page of heart tissue (Spot 11) (Fragment). OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Carnivora; Fissipedia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP SEQUENCE. RC TISSUE=HEART; RX MEDLINE=98163340; PubMed=9504812; RA Dunn M.J., Corbett J.M., Wheeler C.H.; RT "HSC-2DPAGE and the two-dimensional gel electrophoresis database of RT dog heart proteins."; RL Electrophoresis 18:2795-2802(1997). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.3, ITS MW IS: 19.6 kDa. DR HSC-2DPAGE; P99503; DOG. FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1149 MW; 3D9238888D8668C7 CRC64; AEAAAAPAPA AAPA // ID UHA2_CANFA STANDARD; PRT; 14 AA. AC P99506; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein from 2D-page of heart tissue (Spot 6109) (Fragment). OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Carnivora; Fissipedia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP SEQUENCE. RC TISSUE=HEART; RX MEDLINE=98163340; PubMed=9504812; RA Dunn M.J., Corbett J.M., Wheeler C.H.; RT "HSC-2DPAGE and the two-dimensional gel electrophoresis database of RT dog heart proteins."; RL Electrophoresis 18:2795-2802(1997). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.5, ITS MW IS: 28.2 kDa. DR HSC-2DPAGE; P99506; DOG. FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1563 MW; FDEDB617A3DEFADA CRC64; XLKGKVXVAX NQYL // ID UHA3_CANFA STANDARD; PRT; 13 AA. AC P56535; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein from 2D-page of heart tissue (Spot 7520) (Fragment). OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Carnivora; Fissipedia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP SEQUENCE. RC TISSUE=HEART; RX MEDLINE=98163340; PubMed=9504812; RA Dunn M.J., Corbett J.M., Wheeler C.H.; RT "HSC-2DPAGE and the two-dimensional gel electrophoresis database of RT dog heart proteins."; RL Electrophoresis 18:2795-2802(1997). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.9, ITS MW IS: 55.4 kDa. DR HSC-2DPAGE; P56535; DOG. FT NON_TER 13 13 SQ SEQUENCE 13 AA; 1457 MW; 9F5BD94B9306D76A CRC64; TXFITDPVEX VSE // ID UH03_RAT STANDARD; PRT; 12 AA. AC P56572; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Unknown protein from 2D-page of heart tissue (Spot P3) (Fragment). 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. RC STRAIN=WISTAR; TISSUE=HEART; RA Li X.-P., Pleissner K.-P., Scheler C., Regitz-Zagrosek V., Salikov J., RA Jungblut P.R.; RL Submitted (SEP-1998) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 8.3, ITS MW IS: 28 kDa. FT UNSURE 2 2 FT UNSURE 9 9 FT NON_TER 12 12 SQ SEQUENCE 12 AA; 1255 MW; 46F58D101DC33053 CRC64; SGHTKIKVAV DT // ID UH05_RAT STANDARD; PRT; 10 AA. AC P56573; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Unknown protein from 2D-page of heart tissue (Spot P5) (Fragment). 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. RC STRAIN=WISTAR; TISSUE=HEART; RA Li X.-P., Pleissner K.-P., Scheler C., Regitz-Zagrosek V., Salikov J., RA Jungblut P.R.; RL Submitted (SEP-1998) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 8.3, ITS MW IS: 30 kDa. FT UNSURE 9 9 OR P. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1269 MW; 00CBA4BB46C5BABB CRC64; FQYDSQYDGF // ID UH09_RAT STANDARD; PRT; 8 AA. AC P56575; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Unknown protein from 2D-page of heart tissue (Spot P9) (Fragment). 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. RC STRAIN=WISTAR; TISSUE=HEART; RA Li X.-P., Pleissner K.-P., Scheler C., Regitz-Zagrosek V., Salikov J., RA Jungblut P.R.; RL Submitted (SEP-1998) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 8.9, ITS MW IS: 42 kDa. FT NON_TER 8 8 SQ SEQUENCE 8 AA; 1029 MW; 9E0775A6C4140B06 CRC64; QERRQSPE // ID UH11_RAT STANDARD; PRT; 7 AA. AC P56576; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE Unknown protein from 2D-page of heart tissue (Spot P11) (Fragment). 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. RC STRAIN=WISTAR; TISSUE=HEART; RA Li X.-P., Pleissner K.-P., Scheler C., Regitz-Zagrosek V., Salikov J., RA Jungblut P.R.; RL Submitted (SEP-1998) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 8.5, ITS MW IS: 42 kDa. FT UNSURE 2 2 OR A. FT NON_TER 7 7 SQ SEQUENCE 7 AA; 775 MW; 6866DB040DC5A6B0 CRC64; QSAREQG // ID UE15_HORVU STANDARD; PRT; 15 AA. AC P34938; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown endosperm protein E-15/E-16/E-17 (Fragment). OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP SEQUENCE. RC STRAIN=CV. H354-295-2-5; TISSUE=STARCHY ENDOSPERM; RX MEDLINE=94170739; PubMed=8125056; RA Flengsrud R.; RT "Separation of acidic barley endosperm proteins by two-dimensional RT electrophoresis."; RL Electrophoresis 14:1060-1066(1993). CC -!- TISSUE SPECIFICITY: STARCHY ENDOSPERM. CC -!- DEVELOPMENTAL STAGE: GERMINATION. FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1735 MW; 2669969DDEAFD97F CRC64; XISSSTPPYD LNRFK // ID UC01_MAIZE STANDARD; PRT; 15 AA. AC P80607; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 113) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.3, ITS MW IS: 37.4 kDa. DR MAIZE-2DPAGE; P80607; COLEOPTILE. DR MAIZEDB; 123920; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1844 MW; 6F73A6DDCA0F05A5 CRC64; VPEGFDYELY NRNDI // ID UC03_MAIZE STANDARD; PRT; 18 AA. AC P80609; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 146) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.1, ITS MW IS: 29.3 kDa. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80609; COLEOPTILE. DR MAIZEDB; 123924; -. FT NON_TER 1 1 FT NON_CONS 9 10 FT NON_TER 18 18 SQ SEQUENCE 18 AA; 1938 MW; 6F513BEBC35881C0 CRC64; AAVSLLQNKL AYDGFLSK // ID UC04_MAIZE STANDARD; PRT; 14 AA. AC P80610; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 128) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.8, ITS MW IS: 34.6 kDa. DR MAIZE-2DPAGE; P80610; COLEOPTILE. DR MAIZEDB; 123926; -. FT NON_TER 1 1 FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1393 MW; C14451BA1116D4AD CRC64; ADEGFSATVR NGAV // ID UC05_MAIZE STANDARD; PRT; 28 AA. AC P80611; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 154) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.8, ITS MW IS: 35.3 kDa. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80611; COLEOPTILE. DR MAIZEDB; 123928; -. FT NON_TER 1 1 FT NON_CONS 15 16 FT NON_TER 28 28 SQ SEQUENCE 28 AA; 2932 MW; 9A3E0D47B441BA0E CRC64; DHPGVRDGTN IVLXKILPWG DEAYAAGG // ID UC06_MAIZE STANDARD; PRT; 15 AA. AC P80612; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 1131) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.8, ITS MW IS: 71.0 kDa. DR MAIZE-2DPAGE; P80612; COLEOPTILE. DR MAIZEDB; 123930; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1390 MW; 7005E22830F23D61 CRC64; AAAAPPRRGP SGPDA // ID UC07_MAIZE STANDARD; PRT; 22 AA. AC P80613; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 168) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.3, ITS MW IS: 48.9 kDa. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80613; COLEOPTILE. DR MAIZEDB; 123932; -. FT NON_TER 1 1 FT NON_CONS 14 15 FT NON_TER 22 22 SQ SEQUENCE 22 AA; 2287 MW; 27C17392942E6D09 CRC64; IILELAAVDS ASGKLLINGN FK // ID UC08_MAIZE STANDARD; PRT; 15 AA. AC P80614; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 159) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.4, ITS MW IS: 38.8 kDa. CC -!- SIMILARITY: BELONGS TO THE ZINC-CONTAINING ALCOHOL DEHYDROGENASE CC FAMILY. DR MAIZE-2DPAGE; P80614; COLEOPTILE. DR MAIZEDB; 123934; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1785 MW; 1978B1D6AB4DDF8D CRC64; NDWRNAMYPV VPGHE // ID UC09_MAIZE STANDARD; PRT; 32 AA. AC P80615; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 206) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.4, ITS MW IS: 16.9 kDa. CC -!- SIMILARITY: TO THE TOMATO ABSCISIC STRESS RIPENING PROTEINS. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80615; COLEOPTILE. DR MAIZEDB; 123936; -. FT NON_TER 1 1 FT NON_CONS 17 18 FT NON_CONS 24 25 FT NON_TER 32 32 SQ SEQUENCE 32 AA; 3249 MW; 8841DBE253F211D6 CRC64; ITEEVAAAAA VGAGGYVXXL GEAGHHHLFN HE // ID UC11_MAIZE STANDARD; PRT; 40 AA. AC P80617; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 207) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.2, ITS MW IS: 27.1 kDa. CC -!- SIMILARITY: BELONGS TO THE GST SUPERFAMILY. HSP26 FAMILY. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80617; COLEOPTILE. DR MAIZEDB; 123940; -. FT NON_TER 1 1 FT NON_CONS 13 14 FT NON_CONS 26 27 FT NON_CONS 35 36 FT NON_TER 40 40 SQ SEQUENCE 40 AA; 4475 MW; 2ACD4BF8F4908277 CRC64; GLAYEYLEQD LGKKSELLLA ANPVHKVYDF VXGMKPEVAK // ID UC12_MAIZE STANDARD; PRT; 40 AA. AC P80618; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 237) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.0, ITS MW IS: 21.7 kDa. CC -!- SIMILARITY: TO THE TOMATO ABSCISIC STRESS RIPENING PROTEINS. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80618; COLEOPTILE. DR MAIZEDB; 123942; -. FT NON_TER 1 1 FT NON_CONS 15 16 FT NON_CONS 25 26 FT NON_TER 40 40 SQ SEQUENCE 40 AA; 4426 MW; 2E4B14B6B37B34C2 CRC64; IEEEVAAAAA VGSGGXHHHH LFHHKXPEHA HRHKIEEEVA // ID UC13_MAIZE STANDARD; PRT; 15 AA. AC P80619; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 243) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.8, ITS MW IS: 56.9 kDa. CC -!- SIMILARITY: TO GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASES. DR MAIZE-2DPAGE; P80619; COLEOPTILE. DR MAIZEDB; 123946; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1739 MW; 02038EE7471AE038 CRC64; XGRNEFVIRL QXSEA // ID UC14_MAIZE STANDARD; PRT; 15 AA. AC P80620; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 258) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.9, ITS MW IS: 34.6 kDa. DR MAIZE-2DPAGE; P80620; COLEOPTILE. DR MAIZEDB; 123944; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1564 MW; CF0BBAA0B7DE6658 CRC64; AYGGDGGAYY EWSPA // ID UC15_MAIZE STANDARD; PRT; 14 AA. AC P80621; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 245) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.8, ITS MW IS: 35.7 kDa. DR MAIZE-2DPAGE; P80621; COLEOPTILE. DR MAIZEDB; 123947; -. FT NON_TER 1 1 FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1396 MW; C68949275F404CD2 CRC64; VSTLLPVVAA EEPA // ID UC16_MAIZE STANDARD; PRT; 15 AA. AC P80622; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 308) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.9, ITS MW IS: 18.6 kDa. DR MAIZE-2DPAGE; P80622; COLEOPTILE. DR MAIZEDB; 123948; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1796 MW; D331A518F7440BE7 CRC64; QVWYDREVTA FVEPG // ID UC17_MAIZE STANDARD; PRT; 15 AA. AC P80623; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 32) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.5, ITS MW IS: 42.7 kDa. DR MAIZE-2DPAGE; P80623; COLEOPTILE. DR MAIZEDB; 123949; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1554 MW; C0AFFF15FFECEEC8 CRC64; ALSVPVFAVA PLNKK // ID UC18_MAIZE STANDARD; PRT; 14 AA. AC P80624; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 263) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.1, ITS MW IS: 50.3 kDa. DR MAIZE-2DPAGE; P80624; COLEOPTILE. DR MAIZEDB; 123950; -. FT NON_TER 1 1 FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1485 MW; 2EF9116472A39458 CRC64; DVHSNTGIFG IHTS // ID UC19_MAIZE STANDARD; PRT; 15 AA. AC P80625; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 406) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.6, ITS MW IS: 18.4 kDa. DR MAIZE-2DPAGE; P80625; COLEOPTILE. DR MAIZEDB; 123951; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1672 MW; 1CF69D4DA8737F9D CRC64; NGRRYTTYGC SPPVT // ID UC20_MAIZE STANDARD; PRT; 15 AA. AC P80626; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 445) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.1, ITS MW IS: 45.3 kDa. CC -!- SIMILARITY: TO ADOMET SYNTHETASES. DR MAIZE-2DPAGE; P80626; COLEOPTILE. DR MAIZEDB; 123952; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1597 MW; D2EECE163EB10156 CRC64; TQVTVEYVNE GGAMV // ID UC21_MAIZE STANDARD; PRT; 18 AA. AC P80627; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 443) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.9, ITS MW IS: 26.5 kDa. CC -!- SIMILARITY: TO L-ASCORBATE PEROXIDASES. DR HSSP; P48534; 1APX. DR MAIZE-2DPAGE; P80627; COLEOPTILE. DR MAIZEDB; 123953; -. FT NON_TER 1 1 FT NON_TER 18 18 SQ SEQUENCE 18 AA; 1938 MW; F32F6FEF038BAB8A CRC64; AKNYPTVSAE YSXAVEKA // ID UC22_MAIZE STANDARD; PRT; 5 AA. AC P80628; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 474) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.1, ITS MW IS: 30.4 kDa. DR MAIZE-2DPAGE; P80628; COLEOPTILE. DR MAIZEDB; 123954; -. FT NON_TER 1 1 FT NON_TER 5 5 SQ SEQUENCE 5 AA; 654 MW; 72CB19C9C0300000 CRC64; IFFEV // ID UC23_MAIZE STANDARD; PRT; 15 AA. AC P80629; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 502) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.2, ITS MW IS: 45.0 kDa. DR MAIZE-2DPAGE; P80629; COLEOPTILE. DR MAIZEDB; 123955; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1557 MW; C974ED33E9A4EC28 CRC64; AGDKPGDALL DEWLG // ID UC24_MAIZE STANDARD; PRT; 7 AA. AC P80630; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 447) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.0, ITS MW IS: 30.0 kDa. DR MAIZE-2DPAGE; P80630; COLEOPTILE. DR MAIZEDB; 123956; -. FT NON_TER 1 1 FT NON_TER 7 7 SQ SEQUENCE 7 AA; 665 MW; 6DC1B5B33DC1B5D0 CRC64; STAKSTA // ID UC25_MAIZE STANDARD; PRT; 15 AA. AC P80631; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 77) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.9, ITS MW IS: 31.6 kDa. DR MAIZE-2DPAGE; P80631; COLEOPTILE. DR MAIZEDB; 123957; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1580 MW; 83C54CF0CE1614D0 CRC64; AIGGLSRSFP VEAFE // ID UC26_MAIZE STANDARD; PRT; 8 AA. AC P80632; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 907) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 7.0, ITS MW IS: 57.2 kDa. DR MAIZE-2DPAGE; P80632; COLEOPTILE. FT NON_TER 1 1 FT NON_TER 8 8 SQ SEQUENCE 8 AA; 990 MW; 9639D6DAB4176B1D CRC64; AEPRDQFK // ID UC27_MAIZE STANDARD; PRT; 15 AA. AC P80633; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 688) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.4, ITS MW IS: 48.4 kDa. CC -!- SIMILARITY: TO XENOPUS HISTONE-BINDING PROTEIN N1/N2 AND RABBIT CC AND HUMAN NUCLEAR AUTOANTIGENIC SPERM PROTEIN. DR MAIZE-2DPAGE; P80633; COLEOPTILE. DR MAIZEDB; 123958; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1853 MW; CA0E12A5DAED8DC7 CRC64; EREQLRDQVY DAMAE // ID UC28_MAIZE STANDARD; PRT; 15 AA. AC P80634; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 984) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.2, ITS MW IS: 27.7 kDa. DR MAIZE-2DPAGE; P80634; COLEOPTILE. DR MAIZEDB; 123959; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1631 MW; 45C554E40BE9E77F CRC64; XLEGAFVLNQ SQDAE // ID UC29_MAIZE STANDARD; PRT; 15 AA. AC P80635; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 45) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.9, ITS MW IS: 37.6 kDa. DR MAIZE-2DPAGE; P80635; COLEOPTILE. DR MAIZEDB; 123960; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1679 MW; 3D53086B16018BC1 CRC64; NPNPVPIPLV DIDYL // ID UC30_MAIZE STANDARD; PRT; 15 AA. AC P80636; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 662) DE (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.9, ITS MW IS: 32.3 kDa. DR MAIZE-2DPAGE; P80636; COLEOPTILE. DR MAIZEDB; 123961; -. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1545 MW; 3485190F4EF38018 CRC64; SGTSPLLPAI TFILD // ID UC31_MAIZE STANDARD; PRT; 19 AA. AC P80637; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 67) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.8, ITS MW IS: 41.7 kDa. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80637; COLEOPTILE. DR MAIZEDB; 123962; -. FT NON_TER 1 1 FT NON_CONS 10 11 FT NON_TER 19 19 SQ SEQUENCE 19 AA; 2439 MW; DFB2A5C15E50E5F5 CRC64; WILHDWDEDK XXXPYYNTI // ID UC32_MAIZE STANDARD; PRT; 49 AA. AC P80638; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 75) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.0, ITS MW IS: 38.0 kDa. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80638; COLEOPTILE. DR MAIZEDB; 123963; -. FT NON_TER 1 1 FT NON_CONS 11 12 FT NON_CONS 17 18 FT NON_CONS 23 24 FT NON_CONS 35 36 FT NON_CONS 41 42 FT NON_TER 49 49 SQ SEQUENCE 49 AA; 5577 MW; 4FF0389E13AD15BD CRC64; XADGAMINYV EAFPHIKCTV LAPEFGAYVA FEVYPGFSEY KEWSELFTK // ID UC34_MAIZE STANDARD; PRT; 14 AA. AC P80640; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 360) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.7, ITS MW IS: 41.1 kDa. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80640; COLEOPTILE. DR MAIZEDB; 123965; -. FT NON_TER 1 1 FT NON_CONS 8 9 FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1527 MW; DC525FF7B0BE682D CRC64; SIXEPLALSV FDEP // ID UC35_MAIZE STANDARD; PRT; 30 AA. AC P80641; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 365) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.3, ITS MW IS: 39.2 kDa. CC -!- SIMILARITY: TO THE ZINC-CONTAINING ALCOHOL DEHYDROGENASE FAMILY. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR MAIZE-2DPAGE; P80641; COLEOPTILE. DR MAIZEDB; 123966; -. FT NON_TER 1 1 FT NON_CONS 15 16 FT NON_TER 30 30 SQ SEQUENCE 30 AA; 3092 MW; 9717DBF2630E37A6 CRC64; HLGVVGLGGL GHVAVXQEAI ENLXADEFLI // ID UC36_MAIZE STANDARD; PRT; 52 AA. AC P80642; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of etiolated coleoptile (Spot 415) DE (Fragments). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; Liliopsida; Poales; Poaceae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE. RC TISSUE=COLEOPTILE; RA Touzet P., Riccardi F., Morin C., Damerval C., Huet J.-C., RA Pernollet J.-C., Zivy M., de Vienne D.; RT "The maize two dimensional gel protein database: towards an integrated RT genome analysis program."; RL Theor. Appl. Genet. 93:997-1005(1996). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.0, ITS MW IS: 27.2 kDa. CC -!- SIMILARITY: TO THE L-ASCORBATE PEROXIDASES. CC -!- CAUTION: THE ORDER OF THE PEPTIDES SHOWN IS UNCERTAIN. DR HSSP; P48534; 1APX. DR MAIZE-2DPAGE; P80642; COLEOPTILE. DR MAIZEDB; 123967; -. FT NON_TER 1 1 FT NON_CONS 8 9 FT NON_CONS 17 18 FT NON_CONS 24 25 FT NON_CONS 38 39 FT NON_CONS 45 46 FT NON_TER 52 52 SQ SEQUENCE 52 AA; 5840 MW; 70DE0034741CF335 CRC64; AKNYPTVSGS DHLRQVFXMG LSDQALLSDP VFRPLVEKXF FDDYAXRSGF EG // ID UXA2_CHLTR STANDARD; PRT; 10 AA. AC P38003; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Unknown protein from 2D-page from elementary body (Fragment). OS Chlamydia trachomatis. OC Bacteria; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=813; RN [1] RP SEQUENCE. RC STRAIN=L2/434/BU; RA Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M., RA Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G., RA Pallini V.; RL Submitted (SEP-1994) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.65, ITS MW IS: 26.5 kDa. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1019 MW; 49C285C6CAE862C7 CRC64; XXLVGXQASD // ID UXA4_CHLTR STANDARD; PRT; 5 AA. AC P38005; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Unknown protein from 2D-page from elementary body (Fragment). OS Chlamydia trachomatis. OC Bacteria; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=813; RN [1] RP SEQUENCE. RC STRAIN=L2/434/BU; RA Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M., RA Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G., RA Pallini V.; RL Submitted (SEP-1994) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.5, ITS MW IS: 28 kDa. FT NON_TER 5 5 SQ SEQUENCE 5 AA; 474 MW; 75BAA865AA800000 CRC64; XSGDS // ID UXA6_CHLTR STANDARD; PRT; 10 AA. AC P38007; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Unknown protein from 2D-page from elementary body (Fragment). OS Chlamydia trachomatis. OC Bacteria; Chlamydiales; Chlamydiaceae; Chlamydia. OX NCBI_TaxID=813; RN [1] RP SEQUENCE. RC STRAIN=L2/434/BU; RA Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M., RA Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G., RA Pallini V.; RL Submitted (SEP-1994) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.44, ITS MW IS: 38.6 kDa. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1243 MW; DAD39A33304B5339 CRC64; MNFKYIKKDG // ID UN04_CLOPA STANDARD; PRT; 14 AA. AC P81349; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 4 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.7, ITS MW IS: 45.7 kDa. FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1608 MW; D424A7069460EBD2 CRC64; MYEVXIVVVY AAQI // ID UN05_CLOPA STANDARD; PRT; 11 AA. AC P81350; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 5 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.9, ITS MW IS: 81.3 kDa. CC -!- SIMILARITY: TO YEAST YCR105W. FT NON_TER 11 11 SQ SEQUENCE 11 AA; 1337 MW; 412E71F1D9C33B17 CRC64; KYPLEKFQNI G // ID UN06_CLOPA STANDARD; PRT; 6 AA. AC P81351; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 6 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.0, ITS MW IS: 75.9 kDa. FT NON_TER 6 6 SQ SEQUENCE 6 AA; 657 MW; 605B1DC1A45A8000 CRC64; XNTAEI // ID UN07_CLOPA STANDARD; PRT; 14 AA. AC P81352; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 7 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.7, ITS MW IS: 89.1 kDa. FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1385 MW; B246D036EE3F42A6 CRC64; XXAKQSMDGN TAAA // ID UN10_CLOPA STANDARD; PRT; 13 AA. AC P81345; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 10 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.2, ITS MW IS: 52.5 kDa. FT NON_TER 13 13 SQ SEQUENCE 13 AA; 1447 MW; AEBE730C4B90C056 CRC64; MQXDIMIFTI GPA // ID UN12_CLOPA STANDARD; PRT; 13 AA. AC P81353; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 12 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.8, ITS MW IS: 42.7 kDa. FT VARIANT 4 4 L -> V. FT VARIANT 5 5 Q -> I. FT NON_TER 13 13 SQ SEQUENCE 13 AA; 1465 MW; 70AA9E98455D405B CRC64; MYVLQEINPG ITS // ID UN15_CLOPA STANDARD; PRT; 17 AA. AC P81354; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 15 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.1, ITS MW IS: 38.9 kDa. FT NON_TER 17 17 SQ SEQUENCE 17 AA; 2015 MW; 46F8D8DC14A1CB4A CRC64; XXEQKLEGMN EVIKMMD // ID UN19_CLOPA STANDARD; PRT; 9 AA. AC P81355; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 19 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.5, ITS MW IS: 38.0 kDa. FT VARIANT 8 8 M -> D. FT NON_TER 9 9 SQ SEQUENCE 9 AA; 1128 MW; E33E9B0AF5BB19DA CRC64; XXFESXEMR // ID UN23_CLOPA STANDARD; PRT; 29 AA. AC P81356; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 23 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.1, ITS MW IS: 32.7 kDa. FT VARIANT 26 26 Q -> E. FT NON_TER 29 29 SQ SEQUENCE 29 AA; 3144 MW; 4991308059BF3E75 CRC64; MGYDINXXLA QMXKGGVIMX XXXXXQAVI // ID UN37_CLOPA STANDARD; PRT; 14 AA. AC P81358; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 37 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.8, ITS MW IS: 44.7 kDa. FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1579 MW; 05384662DEF89210 CRC64; MYNNXTIEDQ GVKG // ID UN39_CLOPA STANDARD; PRT; 12 AA. AC P81359; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 39 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.4, ITS MW IS: 29.5 kDa. FT NON_TER 12 12 SQ SEQUENCE 12 AA; 1432 MW; 940561E66BD2CB01 CRC64; MIYSTEVVNM NM // ID UN41_CLOPA STANDARD; PRT; 13 AA. AC P81360; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 41 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.6, ITS MW IS: 29.5 kDa. FT NON_TER 13 13 SQ SEQUENCE 13 AA; 1402 MW; 738AECF1E66CA2CB CRC64; MIYSTEVSNM AGV // ID UN46_CLOPA STANDARD; PRT; 14 AA. AC P81362; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE Unknown protein CP 46 from 2D-page (Fragment). OS Clostridium pasteurianum. OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1501; RN [1] RP SEQUENCE. RC STRAIN=W5; RX MEDLINE=98291870; PubMed=9629918; RA Flengsrud R., Skjeldal L.; RT "Two-dimensional gel electrophoresis separation and N-terminal RT sequence analysis of proteins from Clostridium pasteurianum W5."; RL Electrophoresis 19:802-806(1998). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.4, ITS MW IS: 38.2 kDa. FT NON_TER 14 14 SQ SEQUENCE 14 AA; 1550 MW; 198078F4C0367170 CRC64; MIFNDLIGNN NIGD // ID UF01_MOUSE STANDARD; PRT; 5 AA. AC P38639; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Unknown protein from 2D-page of fibroblasts (P19) (Fragment). 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. RC TISSUE=FIBROBLAST; RX MEDLINE=95009907; PubMed=7523108; RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.; RT "Separation and sequencing of familiar and novel murine proteins RT using preparative two-dimensional gel electrophoresis."; RL Electrophoresis 15:735-745(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.6, ITS MW IS: 19 kDa. FT NON_TER 5 5 SQ SEQUENCE 5 AA; 717 MW; 7364087043100000 CRC64; WIGRW // ID UF02_MOUSE STANDARD; PRT; 9 AA. AC P38640; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Unknown protein from 2D-page of fibroblasts (P32) (Fragment). 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. RC TISSUE=FIBROBLAST; RX MEDLINE=95009907; PubMed=7523108; RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.; RT "Separation and sequencing of familiar and novel murine proteins RT using preparative two-dimensional gel electrophoresis."; RL Electrophoresis 15:735-745(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.0, ITS MW IS: 32 kDa. FT NON_TER 9 9 SQ SEQUENCE 9 AA; 1102 MW; 7E73EAB6D05B1AAB CRC64; MEDEIQDXI // ID UF03_MOUSE STANDARD; PRT; 7 AA. AC P38641; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Unknown protein from 2D-page of fibroblasts (P36) (Fragment). 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. RC TISSUE=FIBROBLAST; RX MEDLINE=95009907; PubMed=7523108; RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.; RT "Separation and sequencing of familiar and novel murine proteins RT using preparative two-dimensional gel electrophoresis."; RL Electrophoresis 15:735-745(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.1, ITS MW IS: 36 kDa. FT NON_TER 7 7 SQ SEQUENCE 7 AA; 842 MW; 6AA72B1DDB1B1180 CRC64; HEEAELD // ID UF04_MOUSE STANDARD; PRT; 7 AA. AC P38642; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Unknown protein from 2D-page of fibroblasts (P46) (Fragment). 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. RC TISSUE=FIBROBLAST; RX MEDLINE=95009907; PubMed=7523108; RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.; RT "Separation and sequencing of familiar and novel murine proteins RT using preparative two-dimensional gel electrophoresis."; RL Electrophoresis 15:735-745(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.0, ITS MW IS: 46 kDa. FT NON_TER 7 7 SQ SEQUENCE 7 AA; 766 MW; 68640AB777632700 CRC64; PKPPDRG // ID UF05_MOUSE STANDARD; PRT; 11 AA. AC P38643; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Unknown protein from 2D-page of fibroblasts (P48) (Fragment). 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. RC TISSUE=FIBROBLAST; RX MEDLINE=95009907; PubMed=7523108; RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.; RT "Separation and sequencing of familiar and novel murine proteins RT using preparative two-dimensional gel electrophoresis."; RL Electrophoresis 15:735-745(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.5, ITS MW IS: 48 kDa. FT NON_TER 11 11 SQ SEQUENCE 11 AA; 1328 MW; E54835E5CAAABAFA CRC64; KYIXXDDVIE L // ID UF06_MOUSE STANDARD; PRT; 8 AA. AC P38644; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-FEB-1995 (Rel. 31, Last annotation update) DE Unknown protein from 2D-page of fibroblasts (P50) (Fragment). 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. RC TISSUE=FIBROBLAST; RX MEDLINE=95009907; PubMed=7523108; RA Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.; RT "Separation and sequencing of familiar and novel murine proteins RT using preparative two-dimensional gel electrophoresis."; RL Electrophoresis 15:735-745(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.2, ITS MW IS: 50 kDa. FT NON_TER 8 8 SQ SEQUENCE 8 AA; 817 MW; A35DD878676B05B1 CRC64; HSEPGGAY // ID UN01_PINPS STANDARD; PRT; 15 AA. AC P81106; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of needles (S1247/S1248) (N150/N151) DE (Fragment). OS Pinus pinaster (Maritime pine). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Coniferopsida; Coniferales; Pinaceae; Pinus. OX NCBI_TaxID=71647; RN [1] RP SEQUENCE. RC TISSUE=NEEDLE; RA Plomion C., Costa P., Bahrman N., Frigerio J.M.; RT "Genetic analysis of needle proteins in maritime pine. 1. Mapping RT dominant and codominant protein markers assayed on diploid tissue, in RT a haploid-based genetic map."; RL Silvae Genetica 46:161-165(1997). RN [2] RP SEQUENCE. RC TISSUE=NEEDLE; RX MEDLINE=99274088; PubMed=10344291; RA Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A., RA Frigerio J.-M., Plomion C.; RT "Separation and characterization of needle and xylem maritime pine RT proteins."; RL Electrophoresis 20:1098-1108(1999). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.5, ITS MW IS: 62 kDa. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1670 MW; 29CE44CD51E98FCF CRC64; HEEQITQPSA TNDEA // ID UN02_PINPS STANDARD; PRT; 13 AA. AC P81667; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of needles (N55) (Fragments). OS Pinus pinaster (Maritime pine). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Coniferopsida; Coniferales; Pinaceae; Pinus. OX NCBI_TaxID=71647; RN [1] RP SEQUENCE. RC TISSUE=NEEDLE; RX MEDLINE=99274088; PubMed=10344291; RA Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A., RA Frigerio J.-M., Plomion C.; RT "Separation and characterization of needle and xylem maritime pine RT proteins."; RL Electrophoresis 20:1098-1108(1999). CC -!- INDUCTION: BY WATER-STRESS. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.4, ITS MW IS: 43 kDa. FT NON_TER 1 1 FT NON_CONS 7 8 FT NON_TER 13 13 SQ SEQUENCE 13 AA; 1559 MW; 966B5A43EF94B411 CRC64; FYSAPTRDNV FEL // ID UN03_PINPS STANDARD; PRT; 53 AA. AC P81670; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of needles (N140) (Fragments). OS Pinus pinaster (Maritime pine). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Coniferopsida; Coniferales; Pinaceae; Pinus. OX NCBI_TaxID=71647; RN [1] RP SEQUENCE. RC TISSUE=NEEDLE; RX MEDLINE=99274088; PubMed=10344291; RA Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A., RA Frigerio J.-M., Plomion C.; RT "Separation and characterization of needle and xylem maritime pine RT proteins."; RL Electrophoresis 20:1098-1108(1999). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.2, ITS MW IS: 25 kDa. FT NON_TER 1 1 FT VARIANT 4 4 I -> L. FT VARIANT 6 6 I -> L. FT NON_CONS 8 9 FT NON_CONS 18 19 FT VARIANT 19 19 V -> S. FT VARIANT 23 23 L -> Y. FT VARIANT 31 31 V -> L. FT NON_CONS 31 32 FT NON_CONS 46 47 FT VARIANT 49 49 T -> G. FT VARIANT 50 50 H -> G. FT NON_TER 53 53 SQ SEQUENCE 53 AA; 5829 MW; 02E454F846274220 CRC64; VENIVIGHME VVACADSRVS FNLVLTPAET VAYGNLPFDQ QLVLCEIITH PNF // ID UN04_PINPS STANDARD; PRT; 15 AA. AC P81673; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of needles (N143) (Fragment). OS Pinus pinaster (Maritime pine). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Coniferopsida; Coniferales; Pinaceae; Pinus. OX NCBI_TaxID=71647; RN [1] RP SEQUENCE. RC TISSUE=NEEDLE; RX MEDLINE=99274088; PubMed=10344291; RA Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A., RA Frigerio J.-M., Plomion C.; RT "Separation and characterization of needle and xylem maritime pine RT proteins."; RL Electrophoresis 20:1098-1108(1999). CC -!- INDUCTION: BY WATER-STRESS. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.2, ITS MW IS: 21 kDa. FT NON_TER 1 1 FT NON_TER 15 15 SQ SEQUENCE 15 AA; 1489 MW; CE4D85E99308227A CRC64; KKIEEEAAAA GATAE // ID UN05_PINPS STANDARD; PRT; 20 AA. AC P81674; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of needles (N147) (Fragments). OS Pinus pinaster (Maritime pine). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Coniferopsida; Coniferales; Pinaceae; Pinus. OX NCBI_TaxID=71647; RN [1] RP SEQUENCE. RC TISSUE=NEEDLE; RX MEDLINE=99274088; PubMed=10344291; RA Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A., RA Frigerio J.-M., Plomion C.; RT "Separation and characterization of needle and xylem maritime pine RT proteins."; RL Electrophoresis 20:1098-1108(1999). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.6, ITS MW IS: 36 kDa. FT NON_TER 1 1 FT NON_CONS 11 12 FT VARIANT 13 13 F -> I. FT VARIANT 14 14 Y -> E. FT VARIANT 15 15 R -> K. FT NON_TER 20 20 SQ SEQUENCE 20 AA; 2438 MW; 9F4E4678E086C298 CRC64; IIYDXVGQCD KDFYRPELPR // ID UN06_PINPS STANDARD; PRT; 7 AA. AC P81675; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Unknown protein from 2D-page of needles (N141) (Fragment). OS Pinus pinaster (Maritime pine). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Coniferopsida; Coniferales; Pinaceae; Pinus. OX NCBI_TaxID=71647; RN [1] RP SEQUENCE. RC TISSUE=NEEDLE; RX MEDLINE=99274088; PubMed=10344291; RA Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A., RA Frigerio J.-M., Plomion C.; RT "Separation and characterization of needle and xylem maritime pine RT proteins."; RL Electrophoresis 20:1098-1108(1999). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.6, ITS MW IS: 25 kDa. FT NON_TER 1 1 FT NON_TER 7 7 SQ SEQUENCE 7 AA; 823 MW; 69D76724486B5740 CRC64; LYGNLPF // ID WSP7_PINPS STANDARD; PRT; 35 AA. AC P81086; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Water stress responsive protein 7 (Fragments). OS Pinus pinaster (Maritime pine). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Coniferopsida; Coniferales; Pinaceae; Pinus. OX NCBI_TaxID=71647; RN [1] RP SEQUENCE. RC TISSUE=NEEDLE; RX MEDLINE=98418576; PubMed=9747804; RA Costa P., Bahrman N., Frigerio J.-M., Kremer A., Plomion C.; RT "Water-deficit-responsive proteins in maritime pine."; RL Plant Mol. Biol. 38:587-596(1998). CC -!- INDUCTION: BY WATER-STRESS. FT NON_TER 1 1 FT NON_CONS 15 16 FT NON_CONS 25 26 FT NON_TER 35 35 SQ SEQUENCE 35 AA; 3508 MW; CFC803D3AC70F48A CRC64; SDTTAGSYAE ALAELLTIDP SLIVTTVDTQ LAVAG // ID UXA4_YEAST STANDARD; PRT; 29 AA. AC P38012; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE Unknown protein from 2D-page (Spot 7260) (Fragments). OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE. RC STRAIN=S288C; RX MEDLINE=95203288; PubMed=7895733; RA Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., RA Volpe T., Warner J.R., McLaughlin C.S.; RT "Protein identifications for a Saccharomyces cerevisiae protein RT database."; RL Electrophoresis 15:1466-1486(1994). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.58, ITS MW IS: 32.4 kDa. CC -!- SIMILARITY: BELONGS TO A FAMILY THAT GROUPS DOG1, DOG2, GPP1 AND CC GPP2. DR YEPD; 7260; -. FT NON_TER 1 1 FT NON_CONS 7 8 FT NON_CONS 14 15 FT NON_TER 29 29 SQ SEQUENCE 29 AA; 2992 MW; 5F1E8E9CD41948B2 CRC64; YXEHSIKEVP GAVKVVVFED APAGIAAGK // ID UXB1_YEAST STANDARD; PRT; 10 AA. AC P99012; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Unknown protein from 2D-page (Spot 2D-000JYC) (Fragment). OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE. RC STRAIN=X2180-1A; RA Sanchez J.-C., Golaz O., Schaller D., Morch F., Frutiger S., RA Hughes G.J., Appel R.D., Deshusses J., Hochstrasser D.F.; RL Submitted (AUG-1995) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.71, ITS MW IS: 12.4 kDa. DR SWISS-2DPAGE; P99012; YEAST. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1074 MW; 9E7BEF7AEB0AF6C5 CRC64; XNSQXEXPVA // ID UXB2_YEAST STANDARD; PRT; 11 AA. AC P99013; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Unknown protein from 2D-page (Spot 2D-000K2F) (Fragment). OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycetes; Saccharomycetales; OC Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE. RC STRAIN=X2180-1A; RA Sanchez J.-C., Golaz O., Schaller D., Morch F., Frutiger S., RA Hughes G.J., Appel R.D., Deshusses J., Hochstrasser D.F.; RL Submitted (AUG-1995) to the SWISS-PROT data bank. CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 6.20, ITS MW IS: 9.2 kDa. DR SWISS-2DPAGE; P99013; YEAST. FT NON_TER 11 11 SQ SEQUENCE 11 AA; 1328 MW; EC38021C0DCB42DA CRC64; XVXXVYARKV Y // 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-JUL-1999 (Rel. 38, 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; Bovoidea; OC Bovidae; 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., RA Luu-The V., 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 CC OF HORMONAL STEROIDS. CC -!- CATALYTIC ACTIVITY: 3-BETA-HYDROXY-DELTA(5)-STEROID + NAD(+) = CC 3-OXO-DELTA(5)-STEROID + NADH (ACTS ON 3-BETA-HYDROXYANDROST-5-EN- CC 17-ONE TO FORM ANDROST-4-ENE-3,17-DIONE AND ON 3-BETA-HYDROXYPREGN CC -5-EN-20-ONE TO FORM PROGESTERONE). 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; -. DR PFAM; PF01073; 3Beta_HSD; 1. KW Steroidogenesis; Oxidoreductase; NAD; Isomerase; Mitochondrion; KW Multifunctional enzyme; Transmembrane; Endoplasmic reticulum. FT INIT_MET 0 0 FT NP_BIND 5 36 NAD (POTENTIAL). FT TRANSMEM 74 91 POTENTIAL. FT TRANSMEM 287 305 POTENTIAL. 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 3BH1_HUMAN STANDARD; PRT; 372 AA. AC P14060; Q14545; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 3 beta-hydroxysteroid dehydrogenase/delta 5-->4-isomerase type I DE (3BETA-HSD I) (Trophoblast antigen FDO161G) [Includes: 3-beta-hydroxy- DE delta(5)-steroid dehydrogenase (EC 1.1.1.145) (3-beta-hydroxy-5-ENE DE steroid dehydrogenase) (Progesterone reductase); steroid delta- DE isomerase (EC 5.3.3.1) (Delta-5-3-ketosteroid isomerase)]. GN HSD3B1 OR HSDB3A OR 3BH. 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., AND SEQUENCE OF 1-29. RX MEDLINE=89384668; PubMed=2779585; RA Luu-The V., Lachance Y., Labrie F., Leblanc G., Thomas J.L., RA Strickler R.C., Labrie C.; RT "Full length cDNA structure and deduced amino acid sequence of human RT 3 beta-hydroxy-5-ene steroid dehydrogenase."; RL Mol. Endocrinol. 3:1310-1312(1989). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RX MEDLINE=90228249; PubMed=2139411; RA Lorence M.C., Murry B.A., Trant J.M., Mason J.I.; RT "Human 3 beta-hydroxysteroid dehydrogenase/delta 5-->4isomerase from RT placenta: expression in nonsteroidogenic cells of a protein that RT catalyzes the dehydrogenation/isomerization of C21 and C19 RT steroids."; RL Endocrinology 126:2493-2498(1990). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=91186993; PubMed=2082186; RA Lorence M.C., Corbin C.J., Kamimura N., Mahendroo M.S., Mason J.I.; RT "Structural analysis of the gene encoding human 3 beta-hydroxysteroid RT dehydrogenase/delta 5-->4-isomerase."; RL Mol. Endocrinol. 4:1850-1855(1990). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=91056097; PubMed=2243100; RA Lachance Y., Luu-The V., Labrie C., Simard J., Dumont M., RA Launoit Y.D., Guerin S., Leblanc G., Labrie F.; RT "Characterization of human 3 beta-hydroxysteroid dehydrogenase/delta RT 5-delta 4-isomerase gene and its expression in mammalian cells."; RL J. Biol. Chem. 265:20469-20475(1990). RN [5] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RX MEDLINE=92015040; PubMed=1920284; RA Nickson D.A., McBride M.W., Zeinali S., Hawes C.S., Petropoulos A., RA Mueller U.W., Sutcliffe R.G.; RT "Molecular cloning and expression of human trophoblast antigen RT FDO161G and its identification as 3 beta-hydroxy-5-ene steroid RT dehydrogenase."; RL J. Reprod. Fertil. 93:149-156(1991). RN [6] RP SEQUENCE FROM N.A. RX MEDLINE=93018017; PubMed=1401999; RA Dumont M., Van L.T., Dupont E., Pelletier G., Labrie F.; RT "Characterization, expression, and immunohistochemical localization RT of 3 beta-hydroxysteroid dehydrogenase/delta 5-delta 4 isomerase in RT human skin."; RL J. Invest. Dermatol. 99:415-421(1992). 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 CC OF HORMONAL STEROIDS. CC -!- CATALYTIC ACTIVITY: 3-BETA-HYDROXY-DELTA-5-STEROID + NAD(+) = CC 3-OXO-DELTA-5-STEROID + NADH (ACTS ON 3-BETA-HYDROXYANDROST-5-EN- CC 17-ONE TO FORM ANDROST-4-ENE-3,17-DIONE AND ON 3-BETA-HYDROXYPREGN CC -5-EN-20-ONE TO FORM PROGESTERONE). 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 -!- TISSUE SPECIFICITY: PLACENTA AND SKIN. PREDOMINANTLY EXPRESSED IN CC MAMMARY GLAND TISSUE. CC -!- DISEASE: CONGENITAL DEFICIENCY OF 3BETA-HSD ACTIVITY CAUSES A CC SEVERE DEPLETION OF STEROID FORMATION FREQUENTLY LETHAL IN EARLY CC LIFE. THE CLASSICAL FORM OF THIS DISEASE INCLUDES THE ASSOCIATION CC OF SEVERE SALT-LOSING ADRENAL INSUFFICIENCY AND AMBIGUITY OF CC EXTERNAL GENITALIA IN BOTH SEXES. CC -!- SIMILARITY: BELONGS TO THE 3BETA-HSD FAMILY. DR EMBL; M27137; AAA36015.1; -. DR EMBL; M28392; AAA36001.1; ALT_SEQ. DR EMBL; M28162; AAA36001.1; JOINED. DR EMBL; M28391; AAA36001.1; JOINED. DR EMBL; M35493; AAA51538.1; -. DR EMBL; M63397; AAA51662.1; -. DR EMBL; M63395; AAA51662.1; JOINED. DR EMBL; M63396; AAA51662.1; JOINED. DR EMBL; M38180; AAA51831.1; -. DR EMBL; X53321; CAA37408.1; -. DR EMBL; X55997; CAA39469.1; -. DR EMBL; S45679; AAB23543.1; -. DR PIR; A32746; DEHUHS. DR PIR; A37400; A37400. DR PIR; S30509; S30509. DR MIM; 109715; -. DR INTERPRO; IPR002225; -. DR PFAM; PF01073; 3Beta_HSD; 1. KW Steroidogenesis; Oxidoreductase; NAD; Isomerase; Mitochondrion; KW Multigene family; Multifunctional enzyme; Transmembrane; KW Endoplasmic reticulum; Polymorphism. FT INIT_MET 0 0 FT NP_BIND 5 36 NAD (POTENTIAL). FT TRANSMEM 74 91 POTENTIAL. FT TRANSMEM 287 304 POTENTIAL. FT VARIANT 366 366 T -> N. FT /FTId=VAR_000005. SQ SEQUENCE 372 AA; 42120 MW; CE4F58A7734AE557 CRC64; TGWSCLVTGA GGFLGQRIIR LLVKEKELKE IRVLDKAFGP ELREEFSKLQ NKTKLTVLEG DILDEPFLKR ACQDVSVIIH TACIIDVFGV THRESIMNVN VKGTQLLLEA CVQASVPVFI YTSSIEVAGP NSYKEIIQNG HEEEPLENTW PAPYPHSKKL AEKAVLAANG WNLKNGGTLY TCALRPMYIY GEGSRFLSAS INEALNNNGI LSSVGKFSTV NPVYVGNVAW AHILALRALQ DPKKAPSIRG QFYYISDDTP HQSYDNLNYT LSKEFGLRLD SRWSFPLSLM YWIGFLLEIV SFLLRPIYTY RPPFNRHIVT LSNSVFTFSY KKAQRDLAYK PLYSWEEAKQ KTVEWVGSLV DRHKETLKSK TQ // ID UPA3_HUMAN STANDARD; PRT; 9 AA. AC P30089; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 11) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.6, ITS MW IS: 46 kDa. DR SWISS-2DPAGE; P30089; HUMAN. FT NON_TER 1 1 FT NON_TER 9 9 SQ SEQUENCE 9 AA; 1056 MW; 26F2B1BAF769C737 CRC64; XPLFPXTDF // ID UPA4_HUMAN STANDARD; PRT; 10 AA. AC P30090; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 12) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.8, ITS MW IS: 40.5 kDa. CC -!- MISCELLANEOUS: THIS SPOT IS ON A POSITION THOUGHT TO BE THAT OF CC ZN-ALPHA-2 GLYCOPROTEIN, BUT IT DOES NOT CORRESPOND TO THAT CC PROTEIN. DR SWISS-2DPAGE; P30090; HUMAN. FT NON_TER 1 1 FT UNSURE 4 4 FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1067 MW; 269492EB05A1A457 CRC64; XVPNTSEXSN // ID UPA5_HUMAN STANDARD; PRT; 10 AA. AC P30091; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 13) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 4.85, ITS MW IS: 40 kDa. CC -!- MISCELLANEOUS: THIS SPOT IS ON A POSITION THOUGHT TO BE THAT OF CC ZN-ALPHA-2 GLYCOPROTEIN, BUT IT DOES NOT CORRESPOND TO THAT CC PROTEIN. DR SWISS-2DPAGE; P30091; HUMAN. FT NON_TER 1 1 FT VARIANT 9 9 G -> Y. FT /FTId=VAR_000002. FT NON_TER 10 10 SQ SEQUENCE 10 AA; 1109 MW; C3DA94C732C32776 CRC64; NVQPKVLVGR // ID UPA6_HUMAN STANDARD; PRT; 9 AA. AC P30092; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 14) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5, ITS MW IS: 48 kDa. DR SWISS-2DPAGE; P30092; HUMAN. FT NON_TER 1 1 FT NON_TER 9 9 SQ SEQUENCE 9 AA; 935 MW; 5282F2CAA8676447 CRC64; XLNPGDVXT // ID UPA7_HUMAN STANDARD; PRT; 9 AA. AC P30093; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Unknown protein from 2D-page of plasma (Spot 18) (Fragment). 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=PLASMA; RX MEDLINE=93092937; PubMed=1459097; RA Hughes G.J., Frutiger S., Paquet N., Ravier F., Pasquali C., RA Sanchez J.-C., James R., Tissot J.-D., Bjellqvist B., RA Hochstrasser D.F.; RT "Plasma protein map: an update by microsequencing."; RL Electrophoresis 13:707-714(1992). CC -!- MISCELLANEOUS: ON THE 2D-GEL THE DETERMINED PI OF THIS UNKNOWN CC PROTEIN IS: 5.05, ITS MW IS: 37 kDa. DR SWISS-2DPAGE; P30093; HUMAN. FT NON_TER 1 1 FT UNSURE 5 5 FT NON_TER 9 9 SQ SEQUENCE 9 AA; 1042 MW; 5C14477AEB0772C7 CRC64; SLVPEXPYQ // swissknife-1.67/examples/evTest.pl0000755000175100017510000000235707563750766017202 0ustar moellermoeller#!/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-1.67/examples/example.pl0000755000175100017510000000204510061537274017335 0ustar moellermoeller#!/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, $_->text), "\n"; } } } print "\n\n"; } swissknife-1.67/examples/varsplic.dat.gz0000644000175100017510000052701707606253205020311 0ustar moellermoeller>sprot.varsplic1}s8+p0ɩ#z5 "GR$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"? 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