Curated Information
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Curated Information Page
PubMed Id: 16046471 
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.
Schwabe RF, Sakurai H (2005) IKKbeta phosphorylates p65 at S468 in transactivaton domain 2. FASEB J 19, 1758-60 16046471
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.
Download Sites

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 mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  brain cancer, glioblastoma, glioma, breast cancer, liver cancer, lymphoma, B cell lymphoma
 Relevant cell lines - cell types - tissues:  HeLa (cervical), Hep3B (hepatic), hepatocyte-liver, Jurkat (T lymphocyte), MCF-7 (breast cell), MEF (fibroblast), SKW 6.4 (B lymphocyte), U251 (glial)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE IKKB (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE IKKB (human) pharmacological inhibitor of upstream enzyme, pharmacological activator of upstream enzyme, transfection of dominant-negative enzyme, phospho-antibody, co-immunoprecipitation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase
calyculin A TNF augment treatment-induced increase
PS-1145 TNF inhibit treatment-induced increase
SB203580 TNF no effect upon treatment-induced increase
PD98059 TNF no effect upon treatment-induced increase
LY294002 TNF no effect upon treatment-induced increase
SP600125 TNF no effect upon treatment-induced increase
GSK-3 inhibitor I TNF no effect upon treatment-induced increase
IL-1b increase
calyculin A IL-1b augment treatment-induced increase
PS-1145 IL-1b inhibit treatment-induced increase
SB203580 IL-1b no effect upon treatment-induced increase
PD98059 IL-1b no effect upon treatment-induced increase
LY294002 IL-1b no effect upon treatment-induced increase
SP600125 IL-1b no effect upon treatment-induced increase
GSK-3 inhibitor I IL-1b no effect upon treatment-induced increase
phorbol ester increase
Downstream Regulation
 Effect of modification (process):  transcription, altered

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 mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  brain cancer, glioblastoma, glioma, breast cancer, liver cancer, lymphoma, B cell lymphoma
 Relevant cell lines - cell types - tissues:  HeLa (cervical), Hep3B (hepatic), hepatocyte-liver, Jurkat (T lymphocyte), MCF-7 (breast cell), MEF (fibroblast), SKW 6.4 (B lymphocyte), U251 (glial)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE IKKB (human)
KINASE IKKA (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TNF increase
IL-1b increase


Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.