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P16284

- PECA1_HUMAN

UniProt

P16284 - PECA1_HUMAN

Protein

Platelet endothelial cell adhesion molecule

Gene

PECAM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Induces susceptibility to atherosclerosis By similarity. Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions. 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. Prevents phagocyte ingestion of closely apposed viable cells by transmitting 'detachment' signals, and changes function on apoptosis, promoting tethering of dying cells to phagocytes (the encounter of a viable cell with a phagocyte via the homophilic interaction of PECAM1 on both cell surfaces leads to the viable cell's active repulsion from the phagocyte. During apoptosis, the inside-out signaling of PECAM1 is somehow disabled so that the apoptotic cell does not actively reject the phagocyte anymore. The lack of this repulsion signal together with the interaction of the eat-me signals and their respective receptors causes the attachment of the apoptotic cell to the phagocyte, thus triggering the process of engulfment). Isoform Delta15 is unable to protect against apoptosis. Modulates BDKRB2 activation. Regulates bradykinin- and hyperosmotic shock-induced ERK1/2 activation in human umbilical cord vein cells (HUVEC).By similarity2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell adhesion Source: UniProtKB-KW
    3. cell recognition Source: ProtInc
    4. diapedesis Source: UniProtKB
    5. extracellular matrix organization Source: Reactome
    6. glomerular endothelium development Source: UniProtKB
    7. leukocyte migration Source: Reactome
    8. phagocytosis Source: UniProtKB
    9. platelet activation Source: Reactome
    10. platelet degranulation Source: Reactome
    11. signal transduction Source: ProtInc

    Keywords - Biological processi

    Cell adhesion, Phagocytosis

    Enzyme and pathway databases

    ReactomeiREACT_12051. Cell surface interactions at the vascular wall.
    REACT_12519. PECAM1 interactions.
    REACT_13552. Integrin cell surface interactions.
    REACT_23879. Platelet sensitization by LDL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Platelet endothelial cell adhesion molecule
    Short name:
    PECAM-1
    Alternative name(s):
    EndoCAM
    GPIIA'
    PECA1
    CD_antigen: CD31
    Gene namesi
    Name:PECAM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:8823. PECAM1.

    Subcellular locationi

    Isoform Long : Cell membrane; Single-pass type I membrane protein. Cell membrane; Lipid-anchor. Cell junction
    Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.
    Isoform Delta15 : Cell junction
    Note: Localizes to the lateral border recycling compartment (LBRC) and recycles from the LBRC to the junction in resting endothelial cells.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-SubCell
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: UniProtKB
    6. platelet alpha granule membrane Source: Reactome

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi89 – 891K → A: Lacks homophilic binding ability and is distributed over the entire plasma membrane. 1 Publication
    Mutagenesisi622 – 6221C → A: 6-fold decrease in association with membrane microdomains. 1 Publication
    Mutagenesisi690 – 6901Y → F: 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. 2 Publications
    Mutagenesisi713 – 7131Y → F: 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. 2 Publications

    Organism-specific databases

    PharmGKBiPA33167.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Add
    BLAST
    Chaini28 – 738711Platelet endothelial cell adhesion moleculePRO_0000014895Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi57 ↔ 109PROSITE-ProRule annotation
    Glycosylationi84 – 841N-linked (GlcNAc...)1 Publication
    Glycosylationi151 – 1511N-linked (GlcNAc...)1 Publication
    Disulfide bondi152 ↔ 206PROSITE-ProRule annotation
    Disulfide bondi256 ↔ 304PROSITE-ProRule annotation
    Glycosylationi301 – 3011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi320 – 3201N-linked (GlcNAc...)2 Publications
    Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi347 ↔ 386PROSITE-ProRule annotation
    Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi431 ↔ 476PROSITE-ProRule annotation
    Glycosylationi453 – 4531N-linked (GlcNAc...)1 Publication
    Disulfide bondi523 ↔ 572PROSITE-ProRule annotation
    Glycosylationi551 – 5511N-linked (GlcNAc...)1 Publication
    Lipidationi622 – 6221S-palmitoyl cysteine2 Publications
    Modified residuei690 – 6901Phosphotyrosine; by FER2 Publications
    Modified residuei713 – 7131Phosphotyrosine; by FER3 Publications

    Post-translational modificationi

    Phosphorylated on Ser and Tyr residues after cellular activation. 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.By similarity3 Publications
    Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP16284.
    PRIDEiP16284.

    2D gel databases

    UCD-2DPAGEP16284.

    PTM databases

    PhosphoSiteiP16284.

    Miscellaneous databases

    PMAP-CutDBP16284.

    Expressioni

    Tissue specificityi

    Expressed on platelets and leukocytes and is primarily concentrated at the borders between endothelial cells. Isoform Long predominates in all tissues examined. Isoform Delta12 is detected only in trachea. Isoform Delta14-15 is only detected in lung. Isoform Delta14 is detected in all tissues examined with the strongest expression in heart. 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).2 Publications

    Gene expression databases

    GenevestigatoriP16284.

    Interactioni

    Subunit structurei

    Interacts with PTPN11; Tyr-713 is critical for PTPN11 recruitment. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNB1P352223EBI-716404,EBI-491549
    JUPP149237EBI-716404,EBI-702484
    PTPN11Q061247EBI-716404,EBI-297779
    PTPN6P293504EBI-716404,EBI-78260
    SRCP129313EBI-716404,EBI-621482

    Protein-protein interaction databases

    BioGridi111201. 21 interactions.
    IntActiP16284. 14 interactions.
    MINTiMINT-1198729.

    Structurei

    Secondary structure

    1
    738
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi709 – 72820
    Beta strandi731 – 7333

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KY5NMR-A686-738[»]
    ProteinModelPortaliP16284.
    SMRiP16284. Positions 704-738.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16284.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini28 – 601574ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini621 – 738118CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei602 – 62019HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 12187Ig-like C2-type 1Add
    BLAST
    Domaini145 – 23389Ig-like C2-type 2Add
    BLAST
    Domaini236 – 31580Ig-like C2-type 3Add
    BLAST
    Domaini328 – 40174Ig-like C2-type 4Add
    BLAST
    Domaini424 – 49370Ig-like C2-type 5Add
    BLAST
    Domaini499 – 59193Ig-like C2-type 6Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni721 – 73818May play a role in cytoprotective signalingAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG059434.
    KOiK06471.
    PhylomeDBiP16284.

    Family and domain databases

    Gene3Di2.60.40.10. 5 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view]
    SMARTiSM00409. IG. 3 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 4 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

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

    This isoform has been chosen as the 'canonical' 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

    MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG    50
    KNLTLQCFAD VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR 100
    IYDSGTYKCT VIVNNKEKTT AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV 150
    NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE KNSRDQNFVI LEFPVEEQDR 200
    VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI SPTGMIMEGA 250
    QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 300
    NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP 350
    GAPPANFTIQ KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV 400
    QIVVCEMLSQ PRISYDAQFE VIKGQTIEVR CESISGTLPI SYQLLKTSKV 450
    LENSTKNSND PAVFKDNPTE DVEYQCVADN CHSHAKMLSE VLRVKVIAPV 500
    DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK EGKPFYQMTS 550
    NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 600
    KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE 650
    KMSDPNMEAN SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES 700
    HKDLGKKDTE TVYSEVRKAV PDAVESRYSR TEGSLDGT 738
    Length:738
    Mass (Da):82,536
    Last modified:April 1, 1990 - v1
    Checksum:iC57BBFA200A407A6
    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):80,479
    Checksum:iAAD7D2166EE7137B
    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):80,207
    Checksum:i84A04E34A9EF7619
    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):80,419
    Checksum:i41B823F2ACEEE3AB
    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):79,261
    Checksum:i9245FAAEFDFCF5E2
    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):81,378
    Checksum:i50DEEBC45F1864E9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61A → T in BAF83381. (PubMed:14702039)Curated
    Sequence conflicti8 – 125GATMW → ADV(PubMed:2351935)Curated
    Sequence conflicti80 – 801V → M in AAK84009. 1 PublicationCurated
    Sequence conflicti97 – 971P → L in AAK84011. 1 PublicationCurated
    Sequence conflicti329 – 3291E → K in AAF91460. 1 PublicationCurated
    Sequence conflicti430 – 4301R → H in AAF91451. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti125 – 1251L → V.8 Publications
    Corresponds to variant rs668 [ dbSNP | Ensembl ].
    VAR_013145
    Natural varianti304 – 3041C → Y.
    Corresponds to variant rs7209607 [ dbSNP | Ensembl ].
    VAR_059402
    Natural varianti563 – 5631S → I.
    Corresponds to variant rs12953 [ dbSNP | Ensembl ].
    VAR_059403
    Natural varianti563 – 5631S → N.7 Publications
    Corresponds to variant rs12953 [ dbSNP | Ensembl ].
    VAR_059404
    Natural varianti670 – 6701R → G.6 Publications
    Corresponds to variant rs1131012 [ dbSNP | Ensembl ].
    VAR_059405

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei664 – 68118Missing in isoform Delta12. CuratedVSP_011806Add
    BLAST
    Alternative sequencei682 – 70221Missing in isoform Delta13. CuratedVSP_011807Add
    BLAST
    Alternative sequencei703 – 72927Missing in isoform Delta14-15. CuratedVSP_011808Add
    BLAST
    Alternative sequencei703 – 72119Missing in isoform Delta14. CuratedVSP_011809Add
    BLAST
    Alternative sequencei722 – 7298Missing in isoform Delta15. CuratedVSP_011810
    Alternative sequencei730 – 7389RTEGSLDGT → ENGRLP in isoform Delta14-15 and isoform Delta15. CuratedVSP_011811

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37780 mRNA. Translation: AAA36186.1.
    M28526 mRNA. Translation: AAA36429.1.
    L34657
    , L34631, L34637, L34638, L34639, L34640, L34641, L34642, L34644, L34645, L34649, 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.
    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.
    PIRiA40096.
    RefSeqiNP_000433.4. NM_000442.4.
    UniGeneiHs.376675.
    Hs.514412.

    Genome annotation databases

    GeneIDi5175.
    KEGGihsa:5175.

    Polymorphism databases

    DMDMi129747.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M37780 mRNA. Translation: AAA36186.1 .
    M28526 mRNA. Translation: AAA36429.1 .
    L34657
    , L34631 , L34637 , L34638 , L34639 , L34640 , L34641 , L34642 , L34644 , L34645 , L34649 , 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.
    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 .
    PIRi A40096.
    RefSeqi NP_000433.4. NM_000442.4.
    UniGenei Hs.376675.
    Hs.514412.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KY5 NMR - A 686-738 [» ]
    ProteinModelPortali P16284.
    SMRi P16284. Positions 704-738.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111201. 21 interactions.
    IntActi P16284. 14 interactions.
    MINTi MINT-1198729.

    PTM databases

    PhosphoSitei P16284.

    Polymorphism databases

    DMDMi 129747.

    2D gel databases

    UCD-2DPAGE P16284.

    Proteomic databases

    MaxQBi P16284.
    PRIDEi P16284.

    Protocols and materials databases

    DNASUi 5175.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5175.
    KEGGi hsa:5175.

    Organism-specific databases

    CTDi 5175.
    GeneCardsi GC17M062399.
    HGNCi HGNC:8823. PECAM1.
    MIMi 173445. gene.
    neXtProti NX_P16284.
    PharmGKBi PA33167.
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG059434.
    KOi K06471.
    PhylomeDBi P16284.

    Enzyme and pathway databases

    Reactomei REACT_12051. Cell surface interactions at the vascular wall.
    REACT_12519. PECAM1 interactions.
    REACT_13552. Integrin cell surface interactions.
    REACT_23879. Platelet sensitization by LDL.

    Miscellaneous databases

    EvolutionaryTracei P16284.
    GeneWikii CD31.
    GenomeRNAii 5175.
    NextBioi 20032.
    PMAP-CutDB P16284.
    PROi P16284.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori P16284.

    Family and domain databases

    Gene3Di 2.60.40.10. 5 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    [Graphical view ]
    SMARTi SM00409. IG. 3 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of CD31, a putative intercellular adhesion molecule closely related to carcinoembryonic antigen."
      Simmons D.L., Walker C., Power C., Pigott R.
      J. Exp. Med. 171:2147-2152(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    2. "Molecular characterization and functional analysis of the leukocyte surface protein CD31."
      Stockinger H., Gadd S.J., Eher R., Majdic O., Kasinrek W., Schreiber W., Strass B., Schnabl E., Knapp W.
      J. Immunol. 145:3889-3897(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
    3. "PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily."
      Newman P.J., Berndt M.C., Gorski J., White J.C. II, Lyman S., Paddock C., Muller W.A.
      Science 247:1219-1222(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    4. "Molecular and cellular properties of PECAM-1 (endoCAM/CD31): a novel vascular cell-cell adhesion molecule."
      Albelda S.M., Muller W.A., Buck C.A., Newman P.J.
      J. Cell Biol. 114:1059-1068(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    5. "Organization of the gene for human platelet/endothelial cell adhesion molecule-1 shows alternatively spliced isoforms and a functionally complex cytoplasmic domain."
      Kirschbaum N.E., Gumina R.J., Newman P.J.
      Blood 84:4028-4037(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG), VARIANT ASN-563.
    6. "Gene cloning and sequence analysis of human nasopharyngeal carcinoma resistance cells CNE1/R platelet/endothelial cell adhesion molecule."
      Wang R.-Y., Lun Y.-Z., Jiang Z.-X., Li X.
      Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
      Tissue: Lung.
    8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS VAL-125; ASN-563 AND GLY-670.
    10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
      Tissue: Brain.
    11. Robbins F.-M.Y., Yao H., Hurley C.K., Hartzman R.J.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-734 (ISOFORM LONG), VARIANTS VAL-125; ASN-563 AND GLY-670.
    12. "Identification of PECAM-1 in solid tumor cells and its potential involvement in tumor cell adhesion to endothelium."
      Tang D.G., Chen Y.Q., Newman P.J., Shi L., Gao X., Diglio C.A., Honn K.V.
      J. Biol. Chem. 268:22883-22894(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 507-584.
    13. "Tyrosine residue in exon 14 of the cytoplasmic domain of platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) regulates ligand binding specificity."
      Famiglietti J., Sun J., DeLisser H.M., Albelda S.M.
      J. Cell Biol. 138:1425-1435(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-713.
    14. "Apoptosis disables CD31-mediated cell detachment from phagocytes promoting binding and engulfment."
      Brown S., Heinisch I., Ross E., Shaw K., Buckley C.D., Savill J.
      Nature 418:200-203(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Tissue-specific distributions of alternatively spliced human PECAM-1 isoforms."
      Wang Y., Su X., Sorenson C.M., Sheibani N.
      Am. J. Physiol. 284:H1008-H1017(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    16. "Palmitoylation at Cys595 is essential for PECAM-1 localisation into membrane microdomains and for efficient PECAM-1-mediated cytoprotection."
      Sardjono C.T., Harbour S.N., Yip J.C., Paddock C., Tridandapani S., Newman P.J., Jackson D.E.
      Thromb. Haemost. 96:756-766(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-622, MUTAGENESIS OF CYS-622.
    17. "Regulation of G protein-coupled receptor activities by the platelet-endothelial cell adhesion molecule, PECAM-1."
      Yeh J.C., Otte L.A., Frangos J.A.
      Biochemistry 47:9029-9039(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BDKRB2 AND GNAQ.
    18. "Mechanotransduction in an extracted cell model: Fyn drives stretch- and flow-elicited PECAM-1 phosphorylation."
      Chiu Y.J., McBeath E., Fujiwara K.
      J. Cell Biol. 182:753-763(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    19. "An alternatively spliced isoform of PECAM-1 is expressed at high levels in human and murine tissues, and suggests a novel role for the C-terminus of PECAM-1 in cytoprotective signaling."
      Bergom C., Paddock C., Gao C., Holyst T., Newman D.K., Newman P.J.
      J. Cell Sci. 121:1235-1242(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS DELTA14-15 AND DELTA15), FUNCTION (ISOFORM DELTA15), SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-690 AND TYR-713, INTERACTION WITH PTPN11.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    21. "A novel and critical role for tyrosine 663 in platelet endothelial cell adhesion molecule-1 trafficking and transendothelial migration."
      Dasgupta B., Dufour E., Mamdouh Z., Muller W.A.
      J. Immunol. 182:5041-5051(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-690 AND TYR-713, MUTAGENESIS OF LYS-89; TYR-690 AND TYR-713, INTERACTION WITH PTPN11.
    22. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151; ASN-320 AND ASN-453.
      Tissue: Liver.
    23. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84; ASN-320 AND ASN-551.
      Tissue: Leukemic T-cell.
    24. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    25. "Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases."
      Marin E.P., Derakhshan B., Lam T.T., Davalos A., Sessa W.C.
      Circ. Res. 110:1336-1344(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION BY ZDHHC21, SUBCELLULAR LOCATION.
    26. "Polymorphism of adhesion molecule CD31 and its role in acute graft-versus-host disease."
      Behar E., Chao N.J., Hiraki D.D., Krishnaswamy S., Brown B.W., Zehnder J.L., Grumet F.C.
      N. Engl. J. Med. 334:286-291(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VAL-125.
    27. "Codon 125 polymorphism of CD31 and susceptibility to malaria."
      Casals-Pascual C., Allen S., Allen A., Kai O., Lowe B., Pain A., Roberts D.J.
      Am. J. Trop. Med. Hyg. 65:736-737(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VAL-125.

    Entry informationi

    Entry nameiPECA1_HUMAN
    AccessioniPrimary (citable) accession number: P16284
    Secondary accession number(s): A8K3S7
    , D3DU31, Q6LDA9, Q8TBH1, Q96RF5, Q96RF6, Q9NP65, Q9NPB7, Q9NPG9, Q9NQS9, Q9NQT0, Q9NQT1, Q9NQT2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 170 of the entry and version 1 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3