Curated Information
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Curated Information Page
PubMed Id: 8943348 
Bazenet CE, Gelderloos JA, Kazlauskas A (1996) Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation. Mol Cell Biol 16, 6926-36 8943348
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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Y720-p - PDGFRA (human)
Orthologous residues
PDGFRA (human): Y720‑p, PDGFRA (mouse): Y720‑p, PDGFRA (rat): Y719‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phospho-antibody, phosphopeptide mapping
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout]
 Cellular systems studied:  cell lines
 Species studied:  mouse
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) Induces molecular association, regulation co-immunoprecipitation
 Comments:  Grb2 binds to the PDGFRalpha indirectly via tyrosine-phosphorylated SHP-2.


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