Curated Information
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Curated Information Page
PubMed Id: 11579209 
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.
Ravichandran LV, Chen H, Li Y, Quon MJ (2001) Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor. Mol Endocrinol 15, 1768-80 11579209
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S50-p - PTP1B (human)
Orthologous residues
PTP1B (human): S50‑p, PTP1B (mouse): S50‑p, PTP1B (rat): S50‑p, PTP1B (chicken): S50‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Disease tissue studied:  liver cancer
 Relevant cell lines - cell types - tissues:  3T3 (fibroblast) [SHP-2 (mouse), homozygous knockout], COS (fibroblast), HepG2 (hepatic)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt1 (human) pharmacological inhibitor of upstream enzyme, transfection of constitutively active enzyme, pharmacological activator of upstream enzyme, modification site within consensus motif, transfection of dominant-negative enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
insulin increase
wortmannin insulin inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited, molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
InsR (human) Disrupts co-immunoprecipitation


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