Curated Information
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Curated Information Page
PubMed Id: 20682772 
This page summarizes selected information from the article 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.
Perrinjaquet M, Vilar M, Ibáñez CF (2010) Protein-tyrosine phosphatase SHP2 contributes to GDNF neurotrophic activity through direct binding to phospho-Tyr687 in the RET receptor tyrosine kinase. J Biol Chem 285, 31867-75 20682772
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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Y687-p - Ret (human)
Orthologous residues
Ret (human): Y687‑p, Ret iso2 (human): Y687‑p, Ret iso3 (human): , Ret (mouse): Y688‑p, Ret iso2 (mouse): Y688‑p, Ret iso4 (mouse): Y637‑p, Ret (rat): Y688‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Disease tissue studied:  adrenal cancer, pheochromocytoma
 Relevant cell lines - cell types - tissues:  'neuron, sympathetic', COS (fibroblast), PC-12 (chromaffin)
 Cellular systems studied:  cell lines, primary cultured cells
 Species studied:  monkey, rat
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  cell growth, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
SHP-2 (human) SH2 Induces enzymatic activity, induced pull-down assay
 Comments:  this interaction is enhanced in Ret S696A mutant

S696-p - Ret (human)
Orthologous residues
Ret (human): S696‑p, Ret iso2 (human): S696‑p, Ret iso3 (human): , Ret (mouse): S697‑p, Ret iso2 (mouse): S697‑p, Ret iso4 (mouse): S646‑p, Ret (rat): S697‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Disease tissue studied:  adrenal cancer, pheochromocytoma
 Relevant cell lines - cell types - tissues:  'neuron, sympathetic', COS (fibroblast), PC-12 (chromaffin)
 Cellular systems studied:  cell lines, primary cultured cells
 Species studied:  monkey, rat
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKACA (human) pharmacological activator of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
forskolin increase
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Comments:  inhibits interaction of SHP2 with Ret Y687

Y1062-p - Ret (human)
Orthologous residues
Ret (human): Y1062‑p, Ret iso2 (human): Y1062‑p, Ret iso3 (human): Y586‑p, Ret (mouse): Y1063‑p, Ret iso2 (mouse): Y1063‑p, Ret iso4 (mouse): , Ret (rat): Y1063‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site
 Disease tissue studied:  adrenal cancer, pheochromocytoma
 Relevant cell lines - cell types - tissues:  'neuron, sympathetic', COS (fibroblast), PC-12 (chromaffin)
 Cellular systems studied:  cell lines, primary cultured cells
 Species studied:  monkey, rat
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Effect of modification (process):  cell growth, altered
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
SHP-2 (human) Induces co-immunoprecipitation
 Comments:  through Gab2/Grb2/Shc complex


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