Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 16543145 
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.
Maurer U, et al. (2006) Glycogen synthase kinase-3 regulates mitochondrial outer membrane permeabilization and apoptosis by destabilization of MCL-1. Mol Cell 21, 749-60 16543145
Download Sites

S159-p - MCL1 (human)
Orthologous residues
MCL1 (human): S159‑p, MCL1 iso2 (human): S159‑p, MCL1 (mouse): S140‑p, MCL1 (rat): S139‑p
Characterization
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  FL5.12 (lymphoid), HeLa (cervical), Jurkat (T lymphocyte)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE GSK3B (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE GSK3B (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
MG132, LY294002 increase
CHIR-611, LY294002 decrease
MG132, CHIR-611, LY294002 decrease
IL-3 withdrawal increase
CHIR-611, LY294002, IL-3 withdrawal decrease
Downstream Regulation
 Effect of modification (function):  protein degradation
 Effect of modification (process):  apoptosis, altered


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.