Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 2141171.
- Also identified by PMC identifier 54198.
- No licence information is recorded for this record.
- Because redistribution is not established, this page shows the abstract only. Follow the links below for the full text.
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.
Medical subject headings
- Invertebrate Hormones
- Oncogene Proteins
- Phosphoproteins
- Protein Kinases