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
Molecular Function: protein phosphorylated amino acid binding; protein binding; SH3/SH2 adaptor activity; ephrin receptor binding; SH2 domain binding
Biological Process: regulation of transcription from RNA polymerase II promoter; platelet activation; regulation of Rac protein signal transduction; regulation of Rho GTPase activity; positive regulation of signal transduction; nerve growth factor receptor signaling pathway; activation of MAPKK activity; regulation of actin cytoskeleton organization and biogenesis; insulin receptor signaling pathway; ephrin receptor signaling pathway; innate immune response; blood coagulation
SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.