Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 16709574 
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
This page summarizes selected information from the record 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.
Download Sites

T167-p - BAX (human)
Orthologous residues
BAX (human): T167‑p, BAX iso2 (human): , BAX iso5 (human): , BAX iso8 (human): , BAX (mouse): T167‑p, BAX (rat): T167‑p
 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):  activity, induced, intracellular localization
 Effect of modification (process):  apoptosis, induced

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.