Abstract Src protein-tyrosine kinase contains a myristoylation motif, a unique region, an Src homology (SH) 3 domain, an SH2 domain, a catalytic domain, and a C-terminal tail. The C-terminal tail contains a Tyr residue, Tyr 527. Phosphorylation of Tyr 527 triggers Src inactivation, caused by Tyr (P) 527 binding to the SH2 domain.
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