Focal Adhesion Kinase (FAK) structure. FAK has the N-terminal, Kinase domain and the C-terminal domains. The N-terminal domain has Y-397-Y-autophosphorylation site. The Kinase domain has Y576/577 tyrosines important for catalytic activity of FAK. The C-terminal domain of FAK has Y861 and Y925 tyrosines. Different proteins bind to these domains and involved in motility and survival signaling, The N-terminal domain (205–422 a.a.) of FAK is involved in interaction with Src, RIP, p53, PI3Kinase, PIAS-1, PI3Kinase, Grb-7, EGFR/PDGFR, Ezrin, Bmx, Trio and others. Kinase domain is involved in binding with FIP200 protein. ASAP, p130Cas, Grb-2, Paxillin, Talin, RhoGEFp190 and other proteins bind C-terminal domain of FAK. Interactions of FAK and other proteins demonstrated by group are shown in Italics.