Curated Information
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Curated Information Page
PubMed Id: 10521409 
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.
Sakurai H, et al. (1999) IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain. J Biol Chem 274, 30353-6 10521409
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S536-p - NFkB-p65 (human)
Orthologous residues
NFkB‑p65 (human): S536‑p, NFkB‑p65 (mouse): S534‑p, NFkB‑p65 (rat): S535‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site
 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 IKKA (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE IKKA (human) co-immunoprecipitation, transfection of wild-type enzyme, mutation in upstream enzyme recognition motif
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase
Downstream Regulation
 Effect of modification (function):  activity, induced


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