Curated Information
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Curated Information Page
PubMed Id: 21979951 
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.
Huang Q, et al. (2011) Akt2 kinase suppresses glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-mediated apoptosis in ovarian cancer cells via phosphorylating GAPDH at threonine 237 and decreasing its nuclear translocation. J Biol Chem 286, 42211-20 21979951
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T237-p - GAPDH (human)
Orthologous residues
GAPDH (human): T237‑p, GAPDH (mouse): T235‑p, GAPDH (rat): T235‑p
Characterization
 Methods used to characterize site in vivo immunoprecipitation, mutation of modification site, western blotting
 Disease tissue studied:  ovarian cancer
 Relevant cell lines - cell types - tissues:  OVCAR3 (ovarian), SKOV-3 (ovarian)
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt2 (human) transfection of wild-type enzyme, pharmacological activator of upstream enzyme, co-immunoprecipitation, transfection of dominant-negative enzyme, activation of upstream enzyme, pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
H2O2 increase
wortmannin H2O2 inhibit treatment-induced increase
siRNA H2O2 inhibit treatment-induced increase siRNA Akt2
Downstream Regulation
 Effect of modification (function):  intracellular localization
 Effect of modification (process):  apoptosis, inhibited
 Comments:  increases cell survival


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