Curated Information

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PubMed Id: 9372954

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.

Ko LJ, et al. (1997) p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner. Mol Cell Biol 17, 7220-9 9372954

S33-p - p53 (human)

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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

Characterization

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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