Curated Information
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Home > Curated Information Page > PubMed Id: 23686307
Zou Z, et al. (2014) Brd4 maintains constitutively active NF-κB in cancer cells by binding to acetylated RelA. Oncogene 33, 2395-404 23686307
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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K310-ac - NFkB-p65 (human)
Modsite: KRtyEtFksIMkksP SwissProt Entrez-Gene
Orthologous residues
NFkB‑p65 (human): K310‑ac, NFkB‑p65 (mouse): K310‑ac, NFkB‑p65 (rat): K310‑ac
Characterization
Methods used to characterize site in vivo immunoprecipitation, modification-specific antibody, western blotting
Disease tissue studied:  lung cancer, non-small cell lung cancer, non-small cell lung adenocarcinoma
Relevant cell lines - cell types - tissues:  A549 (pulmonary), HEK293T (epithelial)
Cellular systems studied:  cell lines
Species studied:  human
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
ACETYLTRANSFERASE p300 (human) transfection of wild-type enzyme
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
BRD4 (human) Induces transcription, induced co-immunoprecipitation, pull-down assay