Curated Information
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Curated Information Page
PubMed Id: 9925639 
Tibbetts RS, et al. (1999) A role for ATR in the DNA damage-induced phosphorylation of p53. Genes Dev 13, 152-7 9925639
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
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S15-p - p53 (human)
Orthologous residues
p53 (human): S15‑p, p53 (mouse): S15‑p, p53 iso2 (mouse): S18‑p, p53 (rat): S15‑p, p53 (rabbit): S15‑p, p53 (monkey): S15‑p
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  AT3B-1 (prostate cell), GM847 (fibroblast), K562 (erythroid)
 Cellular systems studied:  cell lines
 Species studied:  human, rat
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ATR (human)
KINASE ATM (human)
 Comments:  Major phosphorylation site.
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ionizing radiation increase
UV increase

S37-p - p53 (human)
Orthologous residues
p53 (human): S37‑p, p53 (mouse): S34‑p, p53 iso2 (mouse): S37‑p, p53 (rat): S39‑p, p53 (rabbit): N37‑p, p53 (monkey): S37‑p
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ATR (human)

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