Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251185 |
Tyr460 |
AVTTEAIyEEIDAHQ |
in vitro |
|
pmid |
sentence |
11711534 |
Tyr-457, located in the presumed Src SH2 binding site, is the predominant tyrosine residue that is phosphorylated by Fyn.Fyn can phosphorylate Srcasm, and association of these molecules relies on cooperative binding between the SH2 and SH3 domains of Fyn and corresponding canonical binding sites in Srcasm. Srcasm is capable of interacting with Grb2 and the regulatory subunit of phosphoinositide 3-kinase, p85, in a phosphorylation-dependent manner. The evidence suggests that Srcasm may help promote Src family kinase signaling in cells. |
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