Curated Information
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Curated Information Page
PubMed Id: 11572860 
Yamasaki S, et al. (2001) Docking protein Gab2 is phosphorylated by ZAP-70 and negatively regulates T cell receptor signaling by recruitment of inhibitory molecules. J Biol Chem 276, 45175-83 11572860
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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Y614-p - Gab2 (human)
Orthologous residues
Gab2 (human): Y614‑p, Gab2 (mouse): Y603‑p, Gab2 (rat): Y603‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, immunoprecipitation, mutation of modification site
 Relevant cell lines - cell types - tissues:  293T (epithelial), 293T (epithelial) [Gab2 (human)], 293T (epithelial) [ZAP70 (human)], Jurkat (T lymphocyte)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ZAP70 (human) transfection of wild-type enzyme
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
SHP-2 (human) Not reported not reported co-immunoprecipitation
 Comments:  This site is involved in suppression of T cell activation


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