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. 2022 May 11;10(5):1112. doi: 10.3390/biomedicines10051112

Figure 1.

Figure 1

Regulation of Src non-receptor tyrosine kinase activity. (A) Src consists of several domains including SH1, SH2, SH3 and SH4 domains. Important Tyr phosphorylation sites of Y527, Y416 and Y213 are noted. (B) Tyr527 phosphorylated by C-terminal Src kinase (CSK) binds to SH2 domain in Src, leading to the inhibition of Src activity. Phosphorylated Tyr213 of Src interferes with SH2 domain binding to p-Tyr527 residue of Src. Dephosphorylation of Src Tyr527 by receptor protein tyrosine phosphatase α activates Src and Tyr416 phosphorylation acquires a fully activation.