Curated Information
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Curated Information Page
PubMed Id: 16709574 
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.
Kim BJ, Ryu SW, Song BJ (2006) JNK- and p38 kinase-mediated phosphorylation of Bax leads to its activation and mitochondrial translocation and to apoptosis of human hepatoma HepG2 cells. J Biol Chem 281, 21256-65 16709574
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T167-p - Bax (human) ▲
Orthologous residues
Bax (human): T167‑p, Bax iso5 (human): ‑, Bax iso8 (human): ‑, Bax (mouse): T167‑p
Characterization
 Methods used to characterize site in vivo:  2D analysis, mutation of modification site
 Relevant cell lines - cell types - tissues:  HepG2 (hepatic), MEF (fibroblast) [IGF1R (mouse)]
 Cellular systems studied:  cell lines
 Species studied:  human
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
staurosporine increase
Downstream Regulation
 Effect of modification (function):  activation, intracellular localization
 Effect of modification (process):  apoptosis, induced


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