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. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold; Motility/polarity/chemotaxis; Oncoprotein
Cellular Component: cytoplasm; cytosol; nucleus; protein complex
Molecular Function: ephrin receptor binding; phosphotyrosine binding; protein binding; protein phosphorylated amino acid binding; protein self-association; SH2 domain binding; SH3 domain binding; SH3/SH2 adaptor activity
Biological Process: activation of MAPKK activity; ephrin receptor signaling pathway; regulation of actin cytoskeleton organization and biogenesis; regulation of cell shape; regulation of GTPase activity; regulation of protein binding; regulation of signal transduction; regulation of transcription from RNA polymerase II promoter; vascular endothelial growth factor receptor signaling pathway