Curated Information

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Curated Information Page

PubMed Id: 10882136

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.

Peters RT, Liao SM, Maniatis T (2000) IKKepsilon is part of a novel PMA-inducible IkappaB kinase complex. Mol Cell 5, 513-22 10882136

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 (human)

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Orthologous residues

IkB‑alpha (human): S32‑p, IkB‑alpha (mouse): S32‑p, IkB‑alpha (rat): S32‑p

Characterization

Methods used to characterize site in vivo: mutation of modification site

Relevant cell lines - cell types - tissues: HeLa (cervical), Jurkat (T lymphocyte)

Cellular systems studied: cell lines

Species studied: human

Upstream Regulation

Potential in vivo enzymes for site:

Type	Enzyme	Evidence	Notes
KINASE	IKK-beta (human)	mutation in upstream enzyme recognition motif
KINASE	IKK-epsilon (human)	mutation in upstream enzyme recognition motif

Treatments, proteins and their effect on site modification:

Treatments	Referenced Treatments	Manipulated Protein	Referenced Protein	Effect	Notes
phorbol ester				increase
TNF				increase

Downstream Regulation

Effect of modification (function): protein degradation

S36-p - IkB-alpha (human)

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