Curated Information
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PubMed Id: 19363025 
Hurd PJ, et al. (2009) Phosphorylation of histone H3 Thr-45 is linked to apoptosis. J Biol Chem 284, 16575-83 19363025
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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T45-p - H3 (human)
Orthologous residues
H3 (human): T45‑p, H3 (mouse): T45‑p, H3 iso2 (mouse): T45‑p, H3 iso3 (mouse): T45‑p, H3 (rat): T45‑p, H3 iso3 (rat): T45‑p, H3 (pig): T45‑p, H3 (chicken): T45‑p, H3 (cow): T45‑p
 Methods used to characterize site in vivo mass spectrometry, mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  leukemia
 Relevant cell lines - cell types - tissues:  HL60 (myeloid)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE PKCD (human) activation 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
calyculin A increase
staurosporine decrease
InSolution decrease
PKC inhibitor decrease
G-CSF decrease
Downstream Regulation
 Effect of modification (process):  apoptosis, induced

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