Curated Information
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Curated Information Page
PubMed Id: 7509446 
This page summarizes selected information from the article referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
Schaller MD, et al. (1994) Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 14, 1680-8 7509446
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Y397-p - FAK (chicken)
Orthologous residues
FAK (human): Y397‑p, FAK iso2 (human): Y216‑p, FAK iso5 (human): Y397‑p, FAK (mouse): Y428‑p, FAK iso3 (mouse): Y397‑p, FAK iso4 (mouse): Y397‑p, FAK (rat): Y397‑p, FAK (chicken): Y397‑p, FAK iso5 (chicken):
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, peptide sequencing, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  CE (embryonic)
 Cellular systems studied:  cell lines
 Species studied:  chicken
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE FAK (chicken)
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 electrophoretic visualization, co-immunoprecipitation


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