Curated Information
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Curated Information Page
PubMed Id: 11571274 
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.
Burma S, et al. (2001) ATM phosphorylates histone H2AX in response to DNA double-strand breaks. J Biol Chem 276, 42462-7 11571274
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S140-p - H2AX (mouse)
Orthologous residues
H2AX (human): S140‑p, H2AX (mouse): S140‑p, H2AX (rat): S140‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  MEF (fibroblast)
 Cellular systems studied:  primary cultured cells
 Species studied:  mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ATM (mouse)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ATM (mouse) genetic transfer of wild-type enzyme, genetic knockout/knockin of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
neocarzinostatin increase
bleomycin increase
ionizing radiation increase
wortmannin decrease
etoposide increase
Downstream Regulation
 Effect of modification (function):  activity, induced


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