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: 17977820 
Palkowitsch L, Leidner J, Ghosh S, Marienfeld RB (2008) Phosphorylation of Serine 68 in the I{kappa}B Kinase (IKK)-binding Domain of NEMO Interferes with the Structure of the IKK Complex and Tumor Necrosis Factor-{alpha}-induced NF-{kappa}B Activity. J Biol Chem 283, 76-86 17977820
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
Download Sites

S43-p - IKKG (human)
Orthologous residues
IKKG (human): S43‑p, IKKG iso2 (human): S111‑p, IKKG (mouse): S43‑p
 Enzymes shown to modify site in vitro
Type Enzyme

S68-p - IKKG (human)
Orthologous residues
IKKG (human): S68‑p, IKKG iso2 (human): S136‑p, IKKG (mouse): S68‑p
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 Relevant cell lines - cell types - tissues:  293 (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase
okadaic acid increase
ionomycin, phorbol ester no change compared to control
Downstream Regulation
 Effect of modification (function):  molecular association, regulation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
IKKG (human) Disrupts chemical cross-linking
IKKB (human) Disrupts co-immunoprecipitation
 Comments:  phosphorylation attenuates amino-terminal protein dimerization; decreases TNF-alpha-induced NF-kB and IKKalpha activity.

S85-p - IKKG (human)
Orthologous residues
IKKG (human): S85‑p, IKKG iso2 (human): S153‑p, IKKG (mouse): S85‑p
 Enzymes shown to modify site in vitro
Type Enzyme

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.