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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1990 Jun;87(12):4766–4770. doi: 10.1073/pnas.87.12.4766

Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2.

J R Bischoff 1, P N Friedman 1, D R Marshak 1, C Prives 1, D Beach 1
PMCID: PMC54198  PMID: 2141171

Abstract

The human anti-oncoprotein p53 is shown to be a substrate of cdc2. The primary site of phosphorylation is serine-315. Serine-315 is phosphorylated by both p60-cdc2 and cyclin B-cdc2 enzymes. The phosphorylation of p53 is cell cycle-dependent. The abundance of p53 also oscillates during the cell cycle. The protein is largely absent from cells that have just completed division but accumulates in cells during G1 phase. Phosphorylation by cdc2 might regulate the antiproliferative activity of p53.

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Selected References

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