Curated Information

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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.

S32-p - IkB-alpha (mouse)

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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)

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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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