Curated Information
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Curated Information Page
PubMed Id: 9843217 
Khanna KK, et al. (1998) ATM associates with and phosphorylates p53: mapping the region of interaction. Nat Genet 20, 398-400 9843217
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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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
Characterization
 Methods used to characterize site in vivo immunoprecipitation, phospho-antibody
 Relevant cell lines - cell types - tissues:  AT1ABR (lymphoblastoid), C3ABR (lymphoblastoid)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE ATM (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE ATM (human) genetic knockout/knockin of upstream enzyme, activation of upstream enzyme in patients diagnosed with Ataxia-Telangiectasia
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
Cd(2+) increase
ionizing radiation increase
Cd(2+), ionizing radiation augment treatment-induced increase
Cd(2+), ionizing radiation, siRNA inhibit treatment-induced increase
Cd(2+), LLnL, ionizing radiation augment treatment-induced increase
Cd(2+), LLnL, ionizing radiation, siRNA inhibit treatment-induced increase


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