Curated Information
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Curated Information Page
PubMed Id: 15849198 
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.
Doyle SL, Jefferies CA, O'Neill LA (2005) Bruton's tyrosine kinase is involved in p65-mediated transactivation and phosphorylation of p65 on serine 536 during NFkappaB activation by lipopolysaccharide. J Biol Chem 280, 23496-501 15849198
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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 phospho-antibody
 Relevant cell lines - cell types - tissues:  293T (epithelial), macrophage-bone marrow, U373 MG (glial)
 Cellular systems studied:  cell lines, primary cells
 Species studied:  human, mouse
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
LPS increase
LFM-A13 LPS inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (function):  activity, induced


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