Curated Information
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Curated Information Page
PubMed Id: 15465828 
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.
Buss H, et al. (2004) Phosphorylation of serine 468 by GSK-3beta negatively regulates basal p65 NF-kappaB activity. J Biol Chem 279, 49571-4 15465828
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S468-p - NFkB-p65 (human)
Orthologous residues
NFkB‑p65 (human): S468‑p, NFkB‑p65 (mouse): S467‑p, NFkB‑p65 (rat): S468‑p
Characterization
 Methods used to characterize site in vivo electrophoretic mobility shift, mutation of modification site, phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  HeLa (cervical)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE GSK3B (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE GSK3B (human) modification site within consensus motif, pharmacological inhibitor of upstream enzyme, phospho-antibody, electrophoretic mobility shift
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
calyculin A increase
lithium calyculin A inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Effect of modification (process):  transcription, altered


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