Curated Information
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Curated Information Page
PubMed Id: 15356145 
Arnaud M, et al. (2004) Phosphorylation of Grb2-associated binder 2 on serine 623 by ERK MAPK regulates its association with the phosphatase SHP-2 and decreases STAT5 activation. J Immunol 173, 3962-71 15356145
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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S623-p - Gab2 (human)
Orthologous residues
Gab2 (human): S623‑p, Gab2 (mouse): S612‑p, Gab2 (rat): S612‑p
Characterization
 Methods used to characterize site in vivo electrophoretic mobility shift, immunoprecipitation, mutation of modification site
 Relevant cell lines - cell types - tissues:  Kit225 (T lymphocyte) [Gab2 (human)], Kit225 (T lymphocyte) [MEK1 (human)]
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ERK2 (human)
KINASE ERK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ERK1 (human) pharmacological inhibitor of upstream 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) Disrupts activity, induced, phosphorylation co-immunoprecipitation
 Comments:  Phosphorylation of this site decreases Gab2 interaction with SHP-2, but leads to increased SHP-2 phosphorylation and activation; also increased phosphorylation of ERK, but decreased activation of STAT5.


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