Curated Information
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Curated Information Page
PubMed Id: 8824286 
Chen HC, Appeddu PA, Isoda H, Guan JL (1996) Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J Biol Chem 271, 26329-34 8824286
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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Y397-p - FAK (human)
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 immunoprecipitation, mutation of modification site, western blotting
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast)
 Cellular systems studied:  cell lines
 Species studied:  mouse
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
PDGF increase
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced, molecular association, regulation
 Effect of modification (process):  cell adhesion, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
PIK3R1 (human) SH2 Induces cell adhesion, altered pull-down assay, in vitro
 Comments:  in vitro and in vivo


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