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P16284 (PECA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet endothelial cell adhesion molecule

Short name=PECAM-1
Alternative name(s):
EndoCAM
GPIIA'
PECA1
CD_antigen=CD31
Gene names
Name:PECAM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length738 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.14 Ref.19 Ref.21

Subunit structure

Interacts with PTPN11; Tyr-713 is critical for PTPN11 recruitment. Forms a complex with BDKRB2 and GNAQ. Interacts with BDKRB2 and GNAQ. Ref.17 Ref.19 Ref.21

Subcellular location

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. Ref.19 Ref.21 Ref.25

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. Ref.19 Ref.21 Ref.25

Tissue specificity

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). Ref.15 Ref.21

Domain

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

Post-translational modification

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. Ref.13 Ref.18 Ref.21

Palmitoylation by ZDHHC21 is necessary for cell surface expression in endothelial cells. Ref.16 Ref.25

Sequence similarities

Contains 6 Ig-like C2-type (immunoglobulin-like) domains.

Ontologies

Keywords
   Biological processCell adhesion
Phagocytosis
   Cellular componentCell junction
Cell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell recognition

Traceable author statement Ref.3. Source: ProtInc

diapedesis

Inferred from direct assay Ref.21. Source: UniProtKB

extracellular matrix organization

Traceable author statement. Source: Reactome

glomerular endothelium development

Inferred from expression pattern PubMed 17464107. Source: UniProtKB

leukocyte migration

Traceable author statement. Source: Reactome

phagocytosis

Inferred from direct assay Ref.14. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement Ref.5. Source: ProtInc

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay PubMed 9290466. Source: BHF-UCL

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 17464107. Source: UniProtKB

platelet alpha granule membrane

Traceable author statement. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P16284-1)

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.
Isoform Delta12 (identifier: P16284-2)

The sequence of this isoform differs from the canonical sequence as follows:
     664-681: Missing.
Isoform Delta13 (identifier: P16284-3)

The sequence of this isoform differs from the canonical sequence as follows:
     682-702: Missing.
Isoform Delta14 (identifier: P16284-4)

The sequence of this isoform differs from the canonical sequence as follows:
     703-721: Missing.
Isoform Delta14-15 (identifier: P16284-5)

The sequence of this isoform differs from the canonical sequence as follows:
     703-729: Missing.
     730-738: RTEGSLDGT → ENGRLP
Isoform Delta15 (identifier: P16284-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727
Chain28 – 738711Platelet endothelial cell adhesion molecule
PRO_0000014895

Regions

Topological domain28 – 601574Extracellular Potential
Transmembrane602 – 62019Helical; Potential
Topological domain621 – 738118Cytoplasmic Potential
Domain35 – 12187Ig-like C2-type 1
Domain145 – 23389Ig-like C2-type 2
Domain236 – 31580Ig-like C2-type 3
Domain328 – 40174Ig-like C2-type 4
Domain424 – 49370Ig-like C2-type 5
Domain499 – 59193Ig-like C2-type 6
Region721 – 73818May play a role in cytoprotective signaling

Amino acid modifications

Modified residue6901Phosphotyrosine; by FER Ref.21
Modified residue7131Phosphotyrosine; by FER Ref.13 Ref.21
Lipidation6221S-palmitoyl cysteine Ref.16 Ref.25
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation841N-linked (GlcNAc...) Ref.23
Glycosylation1511N-linked (GlcNAc...) Ref.22
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Ref.22 Ref.23
Glycosylation3441N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation4531N-linked (GlcNAc...) Ref.22
Glycosylation5511N-linked (GlcNAc...) Ref.23
Disulfide bond57 ↔ 109 Potential
Disulfide bond152 ↔ 206 Potential
Disulfide bond256 ↔ 304 Potential
Disulfide bond347 ↔ 386 Potential
Disulfide bond431 ↔ 476 Potential
Disulfide bond523 ↔ 572 Potential

Natural variations

Alternative sequence664 – 68118Missing in isoform Delta12.
VSP_011806
Alternative sequence682 – 70221Missing in isoform Delta13.
VSP_011807
Alternative sequence703 – 72927Missing in isoform Delta14-15.
VSP_011808
Alternative sequence703 – 72119Missing in isoform Delta14.
VSP_011809
Alternative sequence722 – 7298Missing in isoform Delta15.
VSP_011810
Alternative sequence730 – 7389RTEGSLDGT → ENGRLP in isoform Delta14-15 and isoform Delta15.
VSP_011811
Natural variant1251L → V. Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.26 Ref.27
Corresponds to variant rs668 [ dbSNP | Ensembl ].
VAR_013145
Natural variant3041C → Y.
Corresponds to variant rs7209607 [ dbSNP | Ensembl ].
VAR_059402
Natural variant5631S → I.
Corresponds to variant rs12953 [ dbSNP | Ensembl ].
VAR_059403
Natural variant5631S → N. Ref.2 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11
Corresponds to variant rs12953 [ dbSNP | Ensembl ].
VAR_059404
Natural variant6701R → G. Ref.2 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11
Corresponds to variant rs1131012 [ dbSNP | Ensembl ].
VAR_059405

Experimental info

Mutagenesis891K → A: Lacks homophilic binding ability and is distributed over the entire plasma membrane. Ref.21
Mutagenesis6221C → A: 6-fold decrease in association with membrane microdomains. Ref.16
Mutagenesis6901Y → 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. Ref.19 Ref.21
Mutagenesis7131Y → 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. Ref.19 Ref.21
Sequence conflict61A → T in BAF83381. Ref.7
Sequence conflict8 – 125GATMW → ADV Ref.1
Sequence conflict801V → M in AAK84009. Ref.11
Sequence conflict971P → L in AAK84011. Ref.11
Sequence conflict3291E → K in AAF91460. Ref.11
Sequence conflict4301R → H in AAF91451. Ref.11

Secondary structure

..... 738
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: C57BBFA200A407A6

FASTA73882,536
        10         20         30         40         50         60 
MQPRWAQGAT MWLGVLLTLL LCSSLEGQEN SFTINSVDMK SLPDWTVQNG KNLTLQCFAD 

        70         80         90        100        110        120 
VSTTSHVKPQ HQMLFYKDDV LFYNISSMKS TESYFIPEVR IYDSGTYKCT VIVNNKEKTT 

       130        140        150        160        170        180 
AEYQLLVEGV PSPRVTLDKK EAIQGGIVRV NCSVPEEKAP IHFTIEKLEL NEKMVKLKRE 

       190        200        210        220        230        240 
KNSRDQNFVI LEFPVEEQDR VLSFRCQARI ISGIHMQTSE STKSELVTVT ESFSTPKFHI 

       250        260        270        280        290        300 
SPTGMIMEGA QLHIKCTIQV THLAQEFPEI IIQKDKAIVA HNRHGNKAVY SVMAMVEHSG 

       310        320        330        340        350        360 
NYTCKVESSR ISKVSSIVVN ITELFSKPEL ESSFTHLDQG ERLNLSCSIP GAPPANFTIQ 

       370        380        390        400        410        420 
KEDTIVSQTQ DFTKIASKSD SGTYICTAGI DKVVKKSNTV QIVVCEMLSQ PRISYDAQFE 

       430        440        450        460        470        480 
VIKGQTIEVR CESISGTLPI SYQLLKTSKV LENSTKNSND PAVFKDNPTE DVEYQCVADN 

       490        500        510        520        530        540 
CHSHAKMLSE VLRVKVIAPV DEVQISILSS KVVESGEDIV LQCAVNEGSG PITYKFYREK 

       550        560        570        580        590        600 
EGKPFYQMTS NATQAFWTKQ KASKEQEGEY YCTAFNRANH ASSVPRSKIL TVRVILAPWK 

       610        620        630        640        650        660 
KGLIAVVIIG VIIALLIIAA KCYFLRKAKA KQMPVEMSRP AVPLLNSNNE KMSDPNMEAN 

       670        680        690        700        710        720 
SHYGHNDDVR NHAMKPINDN KEPLNSDVQY TEVQVSSAES HKDLGKKDTE TVYSEVRKAV 

       730 
PDAVESRYSR TEGSLDGT 

« Hide

Isoform Delta12 [UniParc].

Checksum: AAD7D2166EE7137B
Show »

FASTA72080,479
Isoform Delta13 [UniParc].

Checksum: 84A04E34A9EF7619
Show »

FASTA71780,207
Isoform Delta14 [UniParc].

Checksum: 41B823F2ACEEE3AB
Show »

FASTA71980,419
Isoform Delta14-15 [UniParc].

Checksum: 9245FAAEFDFCF5E2
Show »

FASTA70879,261
Isoform Delta15 [UniParc].

Checksum: 50DEEBC45F1864E9
Show »

FASTA72781,378

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

CD31 entry

Functional Glycomics Gateway - Glycan Binding

PECAM-1

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37780 mRNA. Translation: AAA36186.1.
M28526 mRNA. Translation: AAA36429.1.
L34657 expand/collapse EMBL AC list , 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.
PIRA40096.
RefSeqNP_000433.4. NM_000442.4.
UniGeneHs.376675.
Hs.514412.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KY5NMR-A686-738[»]
ProteinModelPortalP16284.
SMRP16284. Positions 704-738.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111201. 20 interactions.
IntActP16284. 14 interactions.
MINTMINT-1198729.

PTM databases

PhosphoSiteP16284.

Polymorphism databases

DMDM129747.

2D gel databases

UCD-2DPAGEP16284.

Proteomic databases

PRIDEP16284.

Protocols and materials databases

DNASU5175.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5175.
KEGGhsa:5175.

Organism-specific databases

CTD5175.
GeneCardsGC17M062399.
HGNCHGNC:8823. PECAM1.
MIM173445. gene.
neXtProtNX_P16284.
PharmGKBPA33167.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG059434.
KOK06471.
PhylomeDBP16284.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

GenevestigatorP16284.

Family and domain databases

Gene3D2.60.40.10. 5 hits.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTSM00409. IG. 3 hits.
[Graphical view]
PROSITEPS50835. IG_LIKE. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16284.
GeneWikiCD31.
GenomeRNAi5175.
NextBio20032.
PMAP-CutDBP16284.
PROP16284.
SOURCESearch...

Entry information

Entry namePECA1_HUMAN
AccessionPrimary (citable) accession number: P16284
Secondary accession number(s): A8K3S7 expand/collapse secondary AC list , D3DU31, Q6LDA9, Q8TBH1, Q96RF5, Q96RF6, Q9NP65, Q9NPB7, Q9NPG9, Q9NQS9, Q9NQT0, Q9NQT1, Q9NQT2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries