Curated Information
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Curated Information Page
PubMed Id: 9372954 
Ko LJ, et al. (1997) p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner. Mol Cell Biol 17, 7220-9 9372954
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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S33-p - p53 (human)
Orthologous residues
p53 (human): S33‑p, p53 (mouse): P33‑p, p53 iso2 (mouse): P36‑p, p53 (rat): P33‑p, p53 (rabbit): T33‑p, p53 (monkey): S33‑p
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  LNCaP (prostate cell), RKO (intestinal)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE CDK7 (human)
 Comments:  S33 phosphorylation in vitro requires all three subunit components of the CAK complex: CDK7, cyclin H, and p36MAT1.
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
ionizing radiation increase

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