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.
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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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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