Curated Information
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Curated Information Page
PubMed Id: 15469940 
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.
Liu Q, et al. (2004) Aurora-A abrogation of p53 DNA binding and transactivation activity by phosphorylation of serine 215. J Biol Chem 279, 52175-82 15469940
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S215-p - p53 (human)
Orthologous residues
p53 (human): S215‑p, p53 (mouse): S209‑p, p53 iso2 (mouse): S212‑p, p53 (rat): S213‑p, p53 (rabbit): S212‑p, p53 (monkey): S215‑p
Characterization
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, electrophoretic mobility shift, mutation of modification site
 Relevant cell lines - cell types - tissues:  HCT116 (intestinal) [p53 (human)]
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE AurA (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE AurA (human) antisense inhibition of upstream enzyme
Downstream Regulation
 Effect of modification (function):  activity, inhibited
 Effect of modification (process):  transcription, altered


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