Curated Information
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Curated Information Page
PubMed Id: 11078726 
Blaydes JP, et al. (2001) Stoichiometric phosphorylation of human p53 at Ser315 stimulates p53-dependent transcription. J Biol Chem 276, 4699-708 11078726
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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S315-p - p53 (human)
Orthologous residues
p53 (human): S315‑p, p53 (mouse): S309‑p, p53 iso2 (mouse): S312‑p, p53 (rat): S313‑p, p53 (rabbit): S313‑p, p53 (monkey): S315‑p
 Methods used to characterize site in vivo mutation of modification site, phospho-antibody, western blotting
 Disease tissue studied:  bone cancer, breast cancer, melanoma skin cancer
 Relevant cell lines - cell types - tissues:  A375 (melanocyte), MCF-7 (breast cell), Saos-2 (bone cell), SF9
 Cellular systems studied:  cell lines
 Species studied:  human, insect
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CDK1 (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CDK1 (human) pharmacological inhibitor of upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
UV increase
roscovitine UV inhibit treatment-induced increase
Downstream Regulation
 Effect of modification (process):  transcription, induced

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