CRK: an adaptor protein with an SH2-SH3-SH3 domain structure. Recruits cytoplasmic proteins through SH2-phospho-tyrosine interaction. Phosphorylated by Abl, IGF-IR and EGFR. Phosphorylation induces a change in intramolecular folding and SH2 interactions, causing its rapid dissociation from the tyrosine kinase complex.
Protein type: Adaptor/scaffold; Motility/polarity/chemotaxis; Oncoprotein
Chromosomal Location of Human Ortholog: 10q24
Cellular Component: actin cytoskeleton; cytosol; extracellular exosome; membrane raft; plasma membrane; protein complex
Molecular Function: cytoskeletal protein binding; enzyme binding; ephrin receptor binding; insulin-like growth factor receptor binding; phosphotyrosine binding; protein binding; protein binding, bridging; protein domain specific binding; protein phosphorylated amino acid binding; protein self-association; SH2 domain binding; SH3 domain binding; SH3/SH2 adaptor activity
Biological Process: activation of JNK activity; activation of MAPKK activity; cellular response to endothelin; cellular response to insulin-like growth factor stimulus; cellular response to nitric oxide; cellular response to transforming growth factor beta stimulus; ephrin receptor signaling pathway; negative regulation of cell motility; negative regulation of natural killer cell mediated cytotoxicity; positive regulation of cell growth; positive regulation of smooth muscle cell migration; positive regulation of substrate adhesion-dependent cell spreading; regulation of actin cytoskeleton organization; regulation of cell motility; regulation of cell shape; regulation of cellular component movement; regulation of GTPase activity; regulation of protein binding; regulation of Rac protein signal transduction; regulation of signal transduction; response to cholecystokinin; response to hydrogen peroxide; response to peptide; response to yeast; SH2 domain-mediated complex assembly
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