Curated Information
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Curated Information Page
PubMed Id: 11441012 
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.
Zhong S, et al. (2001) Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is mediated by MSK1. J Biol Chem 276, 33213-9 11441012
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S29-p - H3 (human)
Orthologous residues
H3 (human): S29‑p, H3 (mouse): S29‑p, H3 iso2 (mouse): S29‑p, H3 iso3 (mouse): S29‑p, H3 (rat): S29‑p, H3 iso3 (rat): S29‑p, H3 (pig): S29‑p, H3 (chicken): S29‑p, H3 (cow): S29‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  JB (epithelial)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE MSK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE MSK1 (human) transfection of dominant-negative enzyme, pharmacological inhibitor of upstream enzyme, transfection of wild-type enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
UV increase
H-89 UV inhibit treatment-induced increase


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