pFAK (391) bound to NCAM1:pFyn Multiple phosphorylated FAK bound to NCAM:pFyn Phosphorylation of FAK by Src kinase Authored: Garapati, P V, 2009-02-24 10:31:15 EC Number: 2.7.10 Edited: Garapati, P V, 2009-02-24 10:58:20 Phosphorylation of Tyr397 in FAK triggers the phosphorylation of other tyrosine residues (Tyr407, Tyr576, Tyr577, Tyr861 and Tyr925) in a Src-dependent manner. The initial phosphorylation of FAK at Tyr397 is thought to create a high-affinity binding site for SH2 domains, enabling formation of a signalling complex between FAK and members of the Src-family kinases. Tyr-576 and Tyr-577 are located in the central catalytic domain and their phosphorylation is required for the maximum kinase activity of FAK. The tyrosine phosphorylation of these residues is likely to be mediated by Src (or other members of the src family). Pubmed12387730 Pubmed7529876 Reactome Database ID Release 43391866 Reactome, http://www.reactome.org ReactomeREACT_18385 Reviewed: Maness, PF, Walmod, PS, 2009--0-5- has a Stoichiometric coefficient of 5