Curated Information
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Curated Information Page
PubMed Id: 11604500 
Ruest PJ, et al. (2001) Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src. Mol Cell Biol 21, 7641-52 11604500
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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Y668-p - P130Cas (mouse)
Orthologous residues
P130Cas (human): Y664‑p, P130Cas iso2 (human): Y682‑p, P130Cas iso7 (human): Y682‑p, P130Cas iso8 (human): Y664‑p, P130Cas (mouse): Y668‑p, P130Cas (rat): Y762‑p, P130Cas iso2 (rat): Y668‑p
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Src (mouse)
KINASE FAK (mouse)
 Comments:  phosphorylation of this site is a result of cooperation of Fak and Src

Y670-p - P130Cas (mouse)
Orthologous residues
P130Cas (human): Y666‑p, P130Cas iso2 (human): Y684‑p, P130Cas iso7 (human): Y684‑p, P130Cas iso8 (human): Y666‑p, P130Cas (mouse): Y670‑p, P130Cas (rat): Y764‑p, P130Cas iso2 (rat): Y670‑p

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