Curated Information
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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.
Only sites from this record are displayed on this page. Click on the protein name to open the protein page, and on the RSD number to open the site page. For the complete dataset, click the download button, on the right.
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S43-p - IKKG (human)
Orthologous residues
IKKG (human): S43‑p, IKKG (mouse): S43‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE IKKB (human)

S68-p - IKKG (human)
Orthologous residues
IKKG (human): S68‑p, IKKG (mouse): S68‑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)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE IKKB (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase
okadaic acid increase
phorbol ester, ionomycin 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
IKKB (human) Disrupts co-immunoprecipitation
IKKG (human) Disrupts chemical cross-linking
 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 (mouse): S85‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE IKKB (human)


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