Curated Information
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Home > Curated Information Page > PubMed Id: 10816598
McLean GW, Fincham VJ, Frame MC (2000) v-Src induces tyrosine phosphorylation of focal adhesion kinase independently of tyrosine 397 and formation of a complex with Src. J Biol Chem 275, 23333-9 10816598
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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Y397-p - FAK (chicken)
Modsite: sVsETDDyAEIIDEE SwissProt Entrez-Gene
Orthologous residues
FAK (human): Y397‑p, FAK iso2 (human): Y216‑p, FAK iso5 (human): Y397‑p, FAK (mouse): Y397‑p, FAK iso2 (mouse): Y428‑p, FAK iso4 (mouse): Y397‑p, FAK iso9 (mouse): , FAK (rat): Y397‑p, FAK (chicken): Y397‑p, FAK iso5 (chicken):
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
fibronectin increase
low_temperature Src (chicken) decrease ts-LA29 v-Src mutant; permissive temperature (35 degree C)
low_temperature fibronectin Src (chicken) inhibit treatment-induced increase ts-LS29 v-Src mutant; permissive temperature (35 degree C)
heating fibronectin Src (chicken) inhibit treatment-induced increase ts-La29 v-Src mutant; restrictive temperature (41 degree C)
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Src (chicken) Induces co-immunoprecipitation