BAIT
ITGB3
BDPLT16, BDPLT2, CD61, GP3A, GPIIIa, GT
integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)
GO Process (36)
GO Function (9)
GO Component (16)
Gene Ontology Biological Process
- activation of protein kinase activity [IMP]
- angiogenesis involved in wound healing [TAS]
- apolipoprotein A-I-mediated signaling pathway [IMP]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell adhesion [TAS]
- cell growth [IMP]
- cell migration [IMP]
- cell-matrix adhesion [IDA, IMP]
- cell-substrate adhesion [IMP]
- extracellular matrix organization [TAS]
- heterotypic cell-cell adhesion [IMP]
- integrin-mediated signaling pathway [IDA, TAS]
- leukocyte migration [TAS]
- mesodermal cell differentiation [IEP]
- negative chemotaxis [IMP]
- negative regulation of lipid storage [IMP]
- negative regulation of lipid transport [IMP]
- negative regulation of lipoprotein metabolic process [IMP]
- negative regulation of low-density lipoprotein particle receptor biosynthetic process [IMP]
- negative regulation of macrophage derived foam cell differentiation [IMP]
- platelet activation [IMP, TAS]
- platelet aggregation [IMP]
- platelet degranulation [TAS]
- positive regulation of endothelial cell migration [IMP]
- positive regulation of endothelial cell proliferation [IMP]
- positive regulation of peptidyl-tyrosine phosphorylation [IMP]
- positive regulation of protein phosphorylation [TAS]
- positive regulation of vascular endothelial growth factor receptor signaling pathway [TAS]
- protein folding [IDA]
- regulation of bone resorption [TAS]
- smooth muscle cell migration [IMP]
- substrate adhesion-dependent cell spreading [IDA]
- tube development [TAS]
- viral entry into host cell [IMP]
- wound healing [IC]
Gene Ontology Molecular Function- cell adhesion molecule binding [IPI]
- extracellular matrix binding [IDA]
- fibronectin binding [IMP]
- identical protein binding [IPI]
- platelet-derived growth factor receptor binding [TAS]
- protease binding [IDA]
- protein binding [IPI]
- protein disulfide isomerase activity [IDA]
- vascular endothelial growth factor receptor 2 binding [IPI, TAS]
- cell adhesion molecule binding [IPI]
- extracellular matrix binding [IDA]
- fibronectin binding [IMP]
- identical protein binding [IPI]
- platelet-derived growth factor receptor binding [TAS]
- protease binding [IDA]
- protein binding [IPI]
- protein disulfide isomerase activity [IDA]
- vascular endothelial growth factor receptor 2 binding [IPI, TAS]
Gene Ontology Cellular Component
- alphav-beta3 integrin-vitronectin complex [TAS]
- cell surface [IDA]
- extracellular vesicular exosome [IDA]
- filopodium membrane [IDA]
- focal adhesion [IDA]
- integral component of plasma membrane [TAS]
- integrin alphav-beta3 complex [IDA]
- integrin complex [IDA]
- lamellipodium membrane [IDA]
- melanosome [IDA]
- microvillus membrane [IDA]
- nucleus [IDA]
- plasma membrane [IDA, TAS]
- platelet alpha granule membrane [TAS]
- receptor complex [IDA]
- ruffle membrane [IDA]
Homo sapiens
PREY
PECAM1
CD31, CD31/EndoCAM, GPIIA', PECA1, PECAM-1, endoCAM
platelet/endothelial cell adhesion molecule 1
GO Process (10)
GO Function (1)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Co-localization
Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.
Publication
PECAM-1/CD31 trans-homophilic binding at the intercellular junctions is independent of its cytoplasmic domain; evidence for heterophilic interaction with integrin alphavbeta3 in Cis.
PECAM-1/CD31 is a cell adhesion and signaling molecule that is enriched at the endothelial cell junctions. Alternative splicing generates multiple PECAM-1 splice variants, which differ in their cytoplasmic domains. It has been suggested that the extracellular ligand-binding property, homophilic versus heterophilic, of these isoforms is controlled by their cytoplasmic tails. To determine whether the cytoplasmic domains also regulate the cell ... [more]
Mol. Biol. Cell Sep. 01, 2000; 11(9);3109-21 [Pubmed: 10982404]
Throughput
- Low Throughput
Curated By
- BioGRID