Curated Information
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Curated Information Page
PubMed Id: 10806218 
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 SP, Ma WY, Dong Z (2000) ERKs and p38 kinases mediate ultraviolet B-induced phosphorylation of histone H3 at serine 10. J Biol Chem 275, 20980-4 10806218
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S11-p - H3 (mouse) ▲
Orthologous residues
H3 (human): S11‑p, H3 (mouse): S11‑p, H3 iso2 (mouse): S11‑p, H3 iso3 (mouse): S11‑p, H3 (rat): S11‑p, H3 iso3 (rat): S11‑p, H3 (pig): S11‑p, H3 (chicken): S11‑p, H3 (cow): S11‑p
Characterization
 Methods used to characterize site in vivo:  phospho-antibody, western blotting
 Relevant cell lines - cell types - tissues:  JB6 C141 (epidermal)
 Cellular systems studied:  cell lines
 Species studied:  mouse
 Enzymes shown to modify site in vitro: 
Type Enzyme
KINASE p38-alpha (human)
KINASE ERK2 (mouse)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
UV increase
SB202190 UV inhibit treatment-induced increase
PD98059 UV inhibit treatment-induced increase
UV ERK2 (mouse) inhibit treatment-induced increase dominant negative
UV p38-alpha (mouse) inhibit treatment-induced increase dominant negative


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