Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P51866 (PECA1_BOVIN)

Entry version 119 (07 Apr 2021)
Sequence version 1 (01 Oct 1996)
Previous versions | rss
Add a publicationFeedback
Protein

Platelet endothelial cell adhesion molecule

Gene

PECAM1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. Tyr-689 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) and is also essential for the LBRC membrane to be targeted around migrating leukocytes. Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions. Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils. Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal. Promotes macrophage-mediated phagocytosis of apoptotic leukocytes by tethering them to the phagocytic cells; PECAM1-mediated detachment signal appears to be disabled in apoptotic leukocytes. Modulates bradykinin receptor BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells. Induces susceptibility to atherosclerosis.By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Platelet endothelial cell adhesion molecule
Short name:
PECAM-1
Alternative name(s):
CD_antigen: CD31
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PECAM1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini28 – 599ExtracellularSequence analysisAdd BLAST572
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei600 – 618HelicalSequence analysisAdd BLAST19
Topological domaini619 – 739CytoplasmicSequence analysisAdd BLAST121

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi689Y → F: Strongly reduced phosphorylation by FER. Abolishes phosphorylation by FER; when associated with F-714. 1 Publication1
Mutagenesisi714Y → F: Reduced phosphorylation by FER. Abolishes phosphorylation by FER; when associated with F-689. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 27By similarityAdd BLAST27
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001489428 – 739Platelet endothelial cell adhesion moleculeAdd BLAST712

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi57 ↔ 109PROSITE-ProRule annotation
Glycosylationi84N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi151N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi152 ↔ 206PROSITE-ProRule annotation
Disulfide bondi256 ↔ 304PROSITE-ProRule annotation
Glycosylationi301N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi320N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi347 ↔ 386PROSITE-ProRule annotation
Glycosylationi356N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi371N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi431 ↔ 476PROSITE-ProRule annotation
Glycosylationi435N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi446N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi453N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi522 ↔ 571PROSITE-ProRule annotation
Glycosylationi550N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi578N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi620S-palmitoyl cysteineBy similarity1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei689Phosphotyrosine; by FER1 Publication1
Modified residuei714Phosphotyrosine; by FER1 Publication1
Modified residuei730PhosphoserineBy similarity1
Modified residuei735PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on Ser and Tyr residues by src kinases after cellular activation (PubMed:12972546). Upon activation, phosphorylated on Ser-730 which probably initiates the dissociation of the membrane-interaction segment (residues 708-730) from the cell membrane allowing the sequential phosphorylation of Tyr-714 and Tyr-689 (By similarity). Constitutively phosphorylated on Ser-735 in resting platelets (By similarity). Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation (PubMed:12972546). In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation (By similarity).By similarity1 Publication
Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P51866

PRoteomics IDEntifications database

More...PRIDEi		P51866

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P51866

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Trans-homodimer (via Ig-like C2-type 1 and Ig-like C2-type 2 domains); trans-homodimerization is required for cell-cell interaction (By similarity).

Forms a complex with BDKRB2 and GNAQ (By similarity).

Interacts with BDKRB2 and GNAQ (By similarity).

Interacts with PTPN11; Tyr-714 is critical for PTPN11 recruitment (PubMed:12972546).

Interacts with FER (PubMed:12972546).

Interacts with CD177; the interaction is Ca2+-dependent; the interaction is direct (By similarity).

By similarity1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		9913.ENSBTAP00000040327

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P51866

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini35 – 120Ig-like C2-type 1Add BLAST86
Domaini145 – 213Ig-like C2-type 2Add BLAST69
Domaini236 – 315Ig-like C2-type 3Add BLAST80
Domaini328 – 403Ig-like C2-type 4Add BLAST76
Domaini424 – 493Ig-like C2-type 5Add BLAST70
Domaini499 – 590Ig-like C2-type 6Add BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni708 – 730Membrane-bound segment which detaches upon phosphorylationBy similarityAdd BLAST23
Regioni722 – 739May play a role in cytoprotective signalingBy similarityAdd BLAST18

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi687 – 692ITIM motif 1By similarity6
Motifi712 – 717ITIM motif 2By similarity6

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The Ig-like C2-type domains 2 and 3 contribute to formation of the complex with BDKRB2 and in regulation of its activity.By similarity

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QW63, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P51866

Database of Orthologous Groups

More...OrthoDBi		419506at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.10, 6 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR007110, Ig-like_dom
IPR036179, Ig-like_dom_sf
IPR013783, Ig-like_fold
IPR040878, Ig_C17orf99
IPR003599, Ig_sub

Pfam protein domain database

More...Pfami		View protein in Pfam
PF13895, Ig_2, 3 hits
PF17736, Ig_C17orf99, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00409, IG, 5 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48726, SSF48726, 5 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50835, IG_LIKE, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P51866-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQLRWTQRGM MWLGALLTLL LCSSLKGQEN SFTINSIHMQ ILPHSTVQNG 
        60         70         80         90        100
ENLTLQCLVD VSTTSRVKPL HQVLFYKDDV LLHNVSSRRN TESYLIPHVR 
       110        120        130        140        150
VCDSGRYKCN VILNNKEKTT PEYEVWVKGV SDPRVTLDKK EVIEGGVVVV 
       160        170        180        190        200
NCSVPEEKAP VHFTIEKFEL NIRGAKKKRE KTSQNQNFVT LEFTVEEQDR 
       210        220        230        240        250
TIRFQCQAKI FSGSNVESSR PIQSDLVTVR ESFSNPKFHI IPEGKVMEGD 
       260        270        280        290        300
DLQVKCTVQV THQAQSFPEI IIQKDREIVA HNSLSSEAVY SVMATTEHNG 
       310        320        330        340        350
NYTCKVEASR ISKVSSVVVN VTELFSKPKL ESSATHLDQG EDLNLLCSIP 
       360        370        380        390        400
GAPPANFTIQ KGGMTVSQTQ NFTKRVSEWD SGLYTCVAGV GRVFKRSNTV 
       410        420        430        440        450
QITVCEMLSK PSIFHDSRSE VIKGQTIEVS CQSVNGTAPI FYQLSNTSKP 
       460        470        480        490        500
VANQSVGSNK PAIFRVKPTK DVEYCCSADN CHSHSKMFSE VLRVKVIAPV 
       510        520        530        540        550
DEAQLVVLKG EVEPGEPIVF YCSVNEGSFP ITYKFYKEKE SKPFYQDTIN 
       560        570        580        590        600
ATQIMWHKTT ASKEYEGQYY CTASNRANLS KHVIQSNTLT VRVYLPLEKG 
       610        620        630        640        650
LIAVVVIGVI IVTLVLGAKC YFLKKAKAKQ MPVEMSRPAV PLLNSNNEKT 
       660        670        680        690        700
LSDAGTEADR HYGYNEDVGN HAMKPLNENK EPLTLDVEYT EVEVTSPEPH 
       710        720        730 
QGLGTKGTET ETVYSEIRKA DPDFVENRYS RTEGSLDGS
Length:739
Mass (Da):82,586
Last modified:October 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i23277383D52E0113
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
U35433 mRNA Translation: AAC48566.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35433 mRNA Translation: AAC48566.1

3D structure databases

SMRiP51866
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000040327

PTM databases

iPTMnetiP51866

Proteomic databases

PaxDbiP51866
PRIDEiP51866

Phylogenomic databases

eggNOGiENOG502QW63, Eukaryota
InParanoidiP51866
OrthoDBi419506at2759

Family and domain databases

Gene3Di2.60.40.10, 6 hits
InterProiView protein in InterPro
IPR007110, Ig-like_dom
IPR036179, Ig-like_dom_sf
IPR013783, Ig-like_fold
IPR040878, Ig_C17orf99
IPR003599, Ig_sub
PfamiView protein in Pfam
PF13895, Ig_2, 3 hits
PF17736, Ig_C17orf99, 1 hit
SMARTiView protein in SMART
SM00409, IG, 5 hits
SUPFAMiSSF48726, SSF48726, 5 hits
PROSITEiView protein in PROSITE
PS50835, IG_LIKE, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPECA1_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P51866
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 7, 2021
This is version 119 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again