Curated Information
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Curated Information Page
PubMed Id: 12697749 
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.
Yuan ZQ, et al. (2003) AKT2 inhibition of cisplatin-induced JNK/p38 and Bax activation by phosphorylation of ASK1: implication of AKT2 in chemoresistance. J Biol Chem 278, 23432-40 12697749
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S83-p - ASK1 (human)
Orthologous residues
ASK1 (human): S83‑p, ASK1 iso5 (human): S163‑p, ASK1 (mouse): S90‑p, ASK1 (rat): S54‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial), A2780 (ovarian)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Akt2 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Akt2 (human) transfection of constitutively active enzyme, transfection of dominant-negative enzyme
Downstream Regulation
 Effect of modification (function):  enzymatic activity, inhibited


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