ITGB3
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]
VIM
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-Western
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
Group IVA cytosolic phospholipase A2 (cPLA2alpha) and integrin alphaIIbbeta3 reinforce each other's functions during alphaIIbbeta3 signaling in platelets.
Group IVA cytosolic phospholipase A(2) (cPLA(2)alpha) catalyzes release of arachidonic acid from glycerophospholipids, leading to thromboxane A(2) (TxA(2)) production. Some platelet agonists stimulate cPLA(2)alpha, but others require fibrinogen binding to alphaIIbbeta3 to elicit TxA(2). Therefore, relationships between cPLA(2)alpha and alphaIIbbeta3 were examined. cPLA(2)alpha and a cPLA(2)alpha binding partner, vimentin, coimmunoprecipitated with alphaIIbbeta3 from platelets, independent of fibrinogen binding. Studies with ... [more]
Throughput
- Low Throughput
Additional Notes
- Figure 2
Curated By
- BioGRID