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UniProtKB - P16284 (PECA1_HUMAN)

Entry version 224 (12 Aug 2020)
Sequence version 2 (28 Mar 2018)
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Protein

Platelet endothelial cell adhesion molecule

Gene

PECAM1

Organism
Homo sapiens (Human)
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 (PubMed:19342684, PubMed:17580308). Tyr-690 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 (PubMed:19342684). Trans-homophilic interaction may play a role in endothelial cell-cell adhesion via cell junctions (PubMed:27958302). Heterophilic interaction with CD177 plays a role in transendothelial migration of neutrophils (PubMed:17580308). Homophilic ligation of PECAM1 prevents macrophage-mediated phagocytosis of neighboring viable leukocytes by transmitting a detachment signal (PubMed:12110892). 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 (PubMed:12110892). Modulates bradykinin receptor BDKRB2 activation (PubMed:18672896). Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in endothelial cells (PubMed:18672896). Induces susceptibility to atherosclerosis (By similarity).By similarity5 Publications
Does not protect against apoptosis.1 Publication

<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, Phagocytosis

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P16284

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-114608, Platelet degranulation
R-HSA-202733, Cell surface interactions at the vascular wall
R-HSA-210990, PECAM1 interactions
R-HSA-216083, Integrin cell surface interactions
R-HSA-432142, Platelet sensitization by LDL
R-HSA-6798695, Neutrophil degranulation

<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):
EndoCAM
GPIIA'
PECA1
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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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: Chromosome 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000261371.5

Human Gene Nomenclature Database

More...HGNCi		HGNC:8823, PECAM1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		173445, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P16284

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

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 – 601ExtracellularSequence analysisAdd BLAST574
<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>Transmembranei602 – 620HelicalSequence analysisAdd BLAST19
Topological domaini621 – 738CytoplasmicSequence analysisAdd BLAST118

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>Mutagenesisi52N → Q: Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-84 and Q-151. 1 Publication1
Mutagenesisi74L → E: Reduced homophilic cell adhesion; when associated with E-112; E-188 and E-190. 1 Publication1
Mutagenesisi84N → Q: Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-52 and Q-151. 1 Publication1
Mutagenesisi89K → A: Lacks homophilic binding ability and is distributed over the entire plasma membrane. 1 Publication1
Mutagenesisi112I → E: Reduced homophilic cell adhesion; when associated with E-74; E-188 and E-190. 1 Publication1
Mutagenesisi151N → Q: Probable loss of N-glycosylation. No effect on homophilic cell adhesion; when associated with Q-52 and Q-84. 1 Publication1
Mutagenesisi188F → E: Reduced homophilic cell adhesion; when associated with E-74; E-112 and E-190. 1 Publication1
Mutagenesisi190I → E: Reduced homophilic cell adhesion; when associated with E-74; E-112 and E-188. 1 Publication1
Mutagenesisi622C → A: 6-fold decrease in association with membrane microdomains. 1 Publication1
Mutagenesisi690Y → F: No effect on Tyr-713 phosphorylation. Inhibits targeted recycling of PECAM1 from the lateral border recycling compartment (LBRC) around transmigrating monocytes. Decreases phosphorylation. No effect on interaction with PTPN11. Loss of phosphorylation and loss of binding to PTPN11; when associated with F-713. 3 Publications1
Mutagenesisi713Y → F: Loss of Tyr-690 phosphorylation. Does not inhibit targeted recycling of PECAM1 from the lateral border recycling compartment (LBRC) around transmigrating monocytes. Decreases phosphorylation. Loss of interaction with PTPN11. Loss of phosphorylation and loss of binding to PTPN11; when associated with F-690. 3 Publications1

Organism-specific databases

DisGeNET

More...DisGeNETi		5175

Open Targets

More...OpenTargetsi		ENSG00000261371

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33167

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P16284, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PECAM1

Domain mapping of disease mutations (DMDM)

More...DMDMi		129747

<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 – 27Add 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_000001489528 – 738Platelet endothelial cell adhesion moleculeAdd BLAST711

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...) asparagineCombined sources1 Publication1
<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 annotationCombined sources2 Publications
Glycosylationi84N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Glycosylationi151N-linked (GlcNAc...) asparagineCombined sources2 Publications1
Disulfide bondi152 ↔ 206PROSITE-ProRule annotationCombined sources2 Publications
Disulfide bondi256 ↔ 304PROSITE-ProRule annotation
Glycosylationi301N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi320N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi344N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi347 ↔ 386PROSITE-ProRule annotation
Glycosylationi356N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi431 ↔ 476PROSITE-ProRule annotation
Glycosylationi453N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi523 ↔ 572PROSITE-ProRule annotation
Glycosylationi551N-linked (GlcNAc...) asparagine1 Publication1
<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>Lipidationi622S-palmitoyl cysteine1 Publication1
<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 residuei690Phosphotyrosine; by FER2 Publications1
Modified residuei713Phosphotyrosine; by FER3 Publications1
Modified residuei729Phosphoserine1 Publication1
Modified residuei734Phosphoserine1 Publication1

<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 after cellular activation by src kinases (PubMed:21464369, PubMed:9298995, PubMed:19342684, PubMed:18710921). Upon activation, phosphorylated on Ser-729 which probably initiates the dissociation of the membrane-interaction segment (residues 709-729) from the cell membrane allowing the sequential phosphorylation of Tyr-713 and Tyr-690 (PubMed:21464369). Constitutively phosphorylated on Ser-734 in resting platelets (PubMed:21464369). Phosphorylated on tyrosine residues by FER and FES in response to FCER1 activation (By similarity). In endothelial cells Fyn mediates mechanical-force (stretch or pull) induced tyrosine phosphorylation (PubMed:18710921).By similarity4 Publications
Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells and enrichment in membrane rafts.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-2602

Encyclopedia of Proteome Dynamics

More...EPDi		P16284

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P16284

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P16284

PeptideAtlas

More...PeptideAtlasi		P16284

PRoteomics IDEntifications database

More...PRIDEi		P16284

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		53335 [P16284-1]
53336 [P16284-2]
53337 [P16284-3]
53338 [P16284-4]
53339 [P16284-5]
53340 [P16284-6]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P16284-1 [P16284-1]

2D gel databases

University College Dublin 2-DE Proteome Database

More...UCD-2DPAGEi		P16284

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1610, 12 N-Linked glycans (5 sites)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P16284, 9 sites, 1 N-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P16284

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P16284

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P16284

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed on platelets and leukocytes and is primarily concentrated at the borders between endothelial cells (PubMed:18388311, PubMed:21464369). Expressed in human umbilical vein endothelial cells (HUVECs) (at protein level) (PubMed:19342684, PubMed:17580308). Expressed on neutrophils (at protein level) (PubMed:17580308). Isoform Long predominates in all tissues examined (PubMed:12433657). Isoform Delta12 is detected only in trachea (PubMed:12433657). Isoform Delta14-15 is only detected in lung (PubMed:12433657). Isoform Delta14 is detected in all tissues examined with the strongest expression in heart (PubMed:12433657). Isoform Delta15 is expressed in brain, testis, ovary, cell surface of platelets, human umbilical vein endothelial cells (HUVECs), Jurkat T-cell leukemia, human erythroleukemia (HEL) and U-937 histiocytic lymphoma cell lines (at protein level) (PubMed:12433657, PubMed:18388311).5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000261371, Expressed in tendon of biceps brachii and 248 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P16284, baseline and differential

<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 (PubMed:26702061, PubMed:27958302).

Forms a complex with BDKRB2 and GNAQ (PubMed:18672896).

Interacts with BDKRB2 and GNAQ (PubMed:18672896).

Interacts with PTPN11; Tyr-713 is critical for PTPN11 recruitment (PubMed:18388311, PubMed:19342684).

Interacts with FER (By similarity).

Interacts (via Ig-like C2-type domain 6) with CD177; the interaction is Ca2+-dependent; the interaction is direct (PubMed:17580308).

By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111201, 23 interactors

Protein interaction database and analysis system

More...IntActi		P16284, 21 interactors

Molecular INTeraction database

More...MINTi		P16284

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000457421

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P16284, protein

<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

Secondary structure

1738
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P16284

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P16284

<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 – 121Ig-like C2-type 1Add BLAST87
Domaini145 – 233Ig-like C2-type 2Add BLAST89
Domaini236 – 315Ig-like C2-type 3Add BLAST80
Domaini328 – 401Ig-like C2-type 4Add BLAST74
Domaini424 – 493Ig-like C2-type 5Add BLAST70
Domaini499 – 591Ig-like C2-type 6Add BLAST93

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>Regioni709 – 729Membrane-bound segment which detaches upon phosphorylation1 PublicationAdd BLAST21
Regioni721 – 738May play a role in cytoprotective signalingAdd 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>Motifi688 – 693ITIM motif 11 Publication6
Motifi711 – 716ITIM motif 21 Publication6

<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.

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QW63, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT01000000214398

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P16284

KEGG Orthology (KO)

More...KOi		K06471

Identification of Orthologs from Complete Genome Data

More...OMAi		PIYFTIE

Database of Orthologous Groups

More...OrthoDBi		419506at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P16284

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.10, 4 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
IPR003598, Ig_sub2

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00409, IG, 5 hits
SM00408, IGc2, 3 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>Sequences (6+)i

<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.

This entry describes 6 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 6 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform Long (identifier: P16284-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG 
        60         70         80         90        100
KNLTLQCFAD VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR 
       110        120        130        140        150
IYDSGTYKCT VIVNNKEKTT AEYQVLVEGV PSPRVTLDKK EAIQGGIVRV 
       160        170        180        190        200
NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE KNSRDQNFVI LEFPVEEQDR 
       210        220        230        240        250
VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI SPTGMIMEGA 
       260        270        280        290        300
QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 
       310        320        330        340        350
NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP 
       360        370        380        390        400
GAPPANFTIQ KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV 
       410        420        430        440        450
QIVVCEMLSQ PRISYDAQFE VIKGQTIEVR CESISGTLPI SYQLLKTSKV 
       460        470        480        490        500
LENSTKNSND PAVFKDNPTE DVEYQCVADN CHSHAKMLSE VLRVKVIAPV 
       510        520        530        540        550
DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK EGKPFYQMTS 
       560        570        580        590        600
NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 
       610        620        630        640        650
KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE 
       660        670        680        690        700
KMSDPNMEAN SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES 
       710        720        730 
HKDLGKKDTE TVYSEVRKAV PDAVESRYSR TEGSLDGT
Length:738
Mass (Da):82,522
Last modified:March 28, 2018 - v2
<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:i9D531D2DDCCB7F92
GO
Isoform Delta12 (identifier: P16284-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     664-681: Missing.

Show »
Length:720
Mass (Da):80,465
Checksum:iA87B2E6BF8844823
GO
Isoform Delta13 (identifier: P16284-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     682-702: Missing.

Show »
Length:717
Mass (Da):80,193
Checksum:iD9362D6FF1EC2AD7
GO
Isoform Delta14 (identifier: P16284-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     703-721: Missing.

Show »
Length:719
Mass (Da):80,405
Checksum:i3D445E64CFB5BBA8
GO
Isoform Delta14-15 (identifier: P16284-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     703-729: Missing.
     730-738: RTEGSLDGT → ENGRLP

Show »
Length:708
Mass (Da):79,247
Checksum:i9C3615328E16C7E4
GO
Isoform Delta15 (identifier: P16284-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     722-729: Missing.
     730-738: RTEGSLDGT → ENGRLP

Show »
Length:727
Mass (Da):81,364
Checksum:iB50CE0F2A7B04E6B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A075B727A0A075B727_HUMAN
Platelet endothelial cell adhesion ...
PECAM1
230Annotation score:

Annotation score:1 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>
A0A075B737A0A075B737_HUMAN
Platelet endothelial cell adhesion ...
PECAM1
134Annotation score:

Annotation score:1 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>
A0A075B728A0A075B728_HUMAN
Platelet endothelial cell adhesion ...
PECAM1
183Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti6A → T in BAF83381 (PubMed:14702039).Curated1
Sequence conflicti8 – 12GATMW → ADV (PubMed:2351935).Curated5
Sequence conflicti80V → M in AAK84009 (PubMed:17212705).Curated1
Sequence conflicti97P → L in AAK84011 (PubMed:17212705).Curated1
Sequence conflicti329E → K in AAF91460 (PubMed:17212705).Curated1
Sequence conflicti430R → H in AAF91451 (PubMed:17212705).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_013145125V → L4 PublicationsCorresponds to variant dbSNP:rs281865545EnsemblClinVar.1
Natural variantiVAR_059402304C → Y. Corresponds to variant dbSNP:rs7209607Ensembl.1
Natural variantiVAR_059403563S → I. Corresponds to variant dbSNP:rs12953Ensembl.1
Natural variantiVAR_059404563S → N7 PublicationsCorresponds to variant dbSNP:rs12953Ensembl.1
Natural variantiVAR_059405670R → G6 PublicationsCorresponds to variant dbSNP:rs1131012Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_011806664 – 681Missing in isoform Delta12. CuratedAdd BLAST18
Alternative sequenceiVSP_011807682 – 702Missing in isoform Delta13. CuratedAdd BLAST21
Alternative sequenceiVSP_011808703 – 729Missing in isoform Delta14-15. CuratedAdd BLAST27
Alternative sequenceiVSP_011809703 – 721Missing in isoform Delta14. CuratedAdd BLAST19
Alternative sequenceiVSP_011810722 – 729Missing in isoform Delta15. Curated8
Alternative sequenceiVSP_011811730 – 738RTEGSLDGT → ENGRLP in isoform Delta14-15 and isoform Delta15. Curated9

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
M37780 mRNA Translation: AAA36186.1
M28526 mRNA Translation: AAA36429.1
L34657 L34655 Genomic DNA Translation: AAA60057.1
JQ287500 mRNA Translation: AFA36630.1
AK290692 mRNA Translation: BAF83381.1
AC016489 Genomic DNA No translation available.
AC138744 Genomic DNA No translation available.
AC234063 Genomic DNA No translation available.
CH471109 Genomic DNA Translation: EAW94207.1
CH471109 Genomic DNA Translation: EAW94208.1
BC022512 mRNA Translation: AAH22512.1
BC051822 mRNA Translation: AAH51822.1
AF281287 mRNA Translation: AAF91446.1
AF281288 mRNA Translation: AAF91447.1
AF281289 mRNA Translation: AAF91448.1
AF281290 mRNA Translation: AAF91449.1
AF281291 mRNA Translation: AAF91450.1
AF281292 mRNA Translation: AAF91451.1
AF281293 mRNA Translation: AAF91452.1
AF281294 mRNA Translation: AAF91453.1
AF281295 mRNA Translation: AAF91454.1
AF281296 mRNA Translation: AAF91455.1
AF281297 mRNA Translation: AAF91456.1
AF281298 mRNA Translation: AAF91457.1
AF281299 mRNA Translation: AAF91458.1
AF281300 mRNA Translation: AAF91459.1
AF281301 mRNA Translation: AAF91460.1
AF393676 mRNA Translation: AAK84009.1
AF393677 mRNA Translation: AAK84010.1
AF393678 mRNA Translation: AAK84011.1
S66450 mRNA Translation: AAB28645.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS74132.1 [P16284-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A40096

NCBI Reference Sequences

More...RefSeqi		NP_000433.4, NM_000442.4 [P16284-1]
XP_005276937.1, XM_005276880.1 [P16284-6]
XP_005276938.1, XM_005276881.1 [P16284-4]
XP_005276939.1, XM_005276882.1 [P16284-3]
XP_011523191.1, XM_011524889.2 [P16284-1]
XP_011523192.1, XM_011524890.1 [P16284-1]
XP_016880227.1, XM_017024738.1 [P16284-1]
XP_016880228.1, XM_017024739.1 [P16284-2]
XP_016880229.1, XM_017024740.1 [P16284-4]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000563924; ENSP00000457421; ENSG00000261371 [P16284-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5175

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5175

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

CD31 entry

Functional Glycomics Gateway - Glycan Binding

PECAM-1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37780 mRNA Translation: AAA36186.1
M28526 mRNA Translation: AAA36429.1
L34657 L34655 Genomic DNA Translation: AAA60057.1
JQ287500 mRNA Translation: AFA36630.1
AK290692 mRNA Translation: BAF83381.1
AC016489 Genomic DNA No translation available.
AC138744 Genomic DNA No translation available.
AC234063 Genomic DNA No translation available.
CH471109 Genomic DNA Translation: EAW94207.1
CH471109 Genomic DNA Translation: EAW94208.1
BC022512 mRNA Translation: AAH22512.1
BC051822 mRNA Translation: AAH51822.1
AF281287 mRNA Translation: AAF91446.1
AF281288 mRNA Translation: AAF91447.1
AF281289 mRNA Translation: AAF91448.1
AF281290 mRNA Translation: AAF91449.1
AF281291 mRNA Translation: AAF91450.1
AF281292 mRNA Translation: AAF91451.1
AF281293 mRNA Translation: AAF91452.1
AF281294 mRNA Translation: AAF91453.1
AF281295 mRNA Translation: AAF91454.1
AF281296 mRNA Translation: AAF91455.1
AF281297 mRNA Translation: AAF91456.1
AF281298 mRNA Translation: AAF91457.1
AF281299 mRNA Translation: AAF91458.1
AF281300 mRNA Translation: AAF91459.1
AF281301 mRNA Translation: AAF91460.1
AF393676 mRNA Translation: AAK84009.1
AF393677 mRNA Translation: AAK84010.1
AF393678 mRNA Translation: AAK84011.1
S66450 mRNA Translation: AAB28645.1
CCDSiCCDS74132.1 [P16284-1]
PIRiA40096
RefSeqiNP_000433.4, NM_000442.4 [P16284-1]
XP_005276937.1, XM_005276880.1 [P16284-6]
XP_005276938.1, XM_005276881.1 [P16284-4]
XP_005276939.1, XM_005276882.1 [P16284-3]
XP_011523191.1, XM_011524889.2 [P16284-1]
XP_011523192.1, XM_011524890.1 [P16284-1]
XP_016880227.1, XM_017024738.1 [P16284-1]
XP_016880228.1, XM_017024739.1 [P16284-2]
XP_016880229.1, XM_017024740.1 [P16284-4]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KY5NMR-A686-738[»]
5C14X-ray2.80A/B28-229[»]
5GNIX-ray3.01A/B28-232[»]
SMRiP16284
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111201, 23 interactors
IntActiP16284, 21 interactors
MINTiP16284
STRINGi9606.ENSP00000457421

PTM databases

GlyConnecti1610, 12 N-Linked glycans (5 sites)
GlyGeniP16284, 9 sites, 1 N-linked glycan (1 site)
iPTMnetiP16284
PhosphoSitePlusiP16284
SwissPalmiP16284

Polymorphism and mutation databases

BioMutaiPECAM1
DMDMi129747

2D gel databases

UCD-2DPAGEiP16284

Proteomic databases

CPTACiCPTAC-2602
EPDiP16284
jPOSTiP16284
MassIVEiP16284
PeptideAtlasiP16284
PRIDEiP16284
ProteomicsDBi53335 [P16284-1]
53336 [P16284-2]
53337 [P16284-3]
53338 [P16284-4]
53339 [P16284-5]
53340 [P16284-6]
TopDownProteomicsiP16284-1 [P16284-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		58161, 3734 antibodies

The DNASU plasmid repository

More...DNASUi		5175

Genome annotation databases

EnsembliENST00000563924; ENSP00000457421; ENSG00000261371 [P16284-1]
GeneIDi5175
KEGGihsa:5175

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5175
DisGeNETi5175
EuPathDBiHostDB:ENSG00000261371.5

GeneCards: human genes, protein and diseases

More...GeneCardsi		PECAM1
HGNCiHGNC:8823, PECAM1
MIMi173445, gene
neXtProtiNX_P16284
OpenTargetsiENSG00000261371
PharmGKBiPA33167

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502QW63, Eukaryota
GeneTreeiENSGT01000000214398
InParanoidiP16284
KOiK06471
OMAiPIYFTIE
OrthoDBi419506at2759
PhylomeDBiP16284

Enzyme and pathway databases

PathwayCommonsiP16284
ReactomeiR-HSA-114608, Platelet degranulation
R-HSA-202733, Cell surface interactions at the vascular wall
R-HSA-210990, PECAM1 interactions
R-HSA-216083, Integrin cell surface interactions
R-HSA-432142, Platelet sensitization by LDL
R-HSA-6798695, Neutrophil degranulation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5175, 2 hits in 85 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PECAM1, human
EvolutionaryTraceiP16284

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CD31

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5175
PharosiP16284, Tbio

Protein Ontology

More...PROi		PR:P16284
RNActiP16284, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000261371, Expressed in tendon of biceps brachii and 248 other tissues
ExpressionAtlasiP16284, baseline and differential

Family and domain databases

Gene3Di2.60.40.10, 4 hits
InterProiView protein in InterPro
IPR007110, Ig-like_dom
IPR036179, Ig-like_dom_sf
IPR013783, Ig-like_fold
IPR040878, Ig_C17orf99
IPR003599, Ig_sub
IPR003598, Ig_sub2
PfamiView protein in Pfam
PF13895, Ig_2, 1 hit
PF17736, Ig_C17orf99, 1 hit
SMARTiView protein in SMART
SM00409, IG, 5 hits
SM00408, IGc2, 3 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_HUMAN
<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: P16284
Secondary accession number(s): A0A075B738
, A8K3S7, D3DU31, Q6LDA9, Q8TBH1, Q96RF5, Q96RF6, Q9NP65, Q9NPB7, Q9NPG9, Q9NQS9, Q9NQT0, Q9NQT1, Q9NQT2
<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: April 1, 1990
Last sequence update: March 28, 2018
Last modified: August 12, 2020
This is version 224 of the entry and version 2 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
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