Curated Information
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Curated Information Page
PubMed Id: 10421793 
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.
Shimada T, et al. (1999) IKK-i, a novel lipopolysaccharide-inducible kinase that is related to IkappaB kinases. Int Immunol 11, 1357-62 10421793
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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S32-p - IkB-alpha (mouse)
Orthologous residues
IkB‑alpha (human): S32‑p, IkB‑alpha (mouse): S32‑p, IkB‑alpha (rat): S32‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE IKKE (mouse)
 Comments:  minor site

S36-p - IkB-alpha (mouse)
Orthologous residues
IkB‑alpha (human): S36‑p, IkB‑alpha (mouse): S36‑p, IkB‑alpha (rat): S36‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE IKKE (mouse)

S172-p - IKKE (mouse)
Orthologous residues
IKKE (human): S172‑p, IKKE (mouse): S172‑p, IKKE (rat): S172‑p
Characterization
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE IKKE (mouse)
Downstream Regulation
 Effect of modification (function):  enzymatic activity, induced


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