Curated Information
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Curated Information Page
PubMed Id: 9488723 
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.
Rogakou EP, et al. (1998) DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem 273, 5858-68 9488723
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S140-p - H2AX (human)
Orthologous residues
H2AX (human): S140‑p, H2AX (mouse): S140‑p, H2AX (rat): S140‑p
Characterization
 Methods used to characterize site in vivo 2D analysis, [32P] bio-synthetic labeling, electrophoretic mobility shift
 Disease tissue studied:  brain cancer, glioblastoma, glioma
 Relevant cell lines - cell types - tissues:  CHO (fibroblast) [EphB1 (human), transfection], HeLa (cervical), liver, SF268 (glial)
 Cellular systems studied:  cell lines, tissue
 Species studied:  hamster, human, mouse
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ionizing radiation increase
H2O2 no change compared to control


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