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

Bischoff, J. R., Friedman, P. N., Marshak, D. R., Prives, C., Beach, D. (June 1990) Human p53 is phosphorylated by p60-cdc2 and cyclin B-cdc2. Proc Natl Acad Sci U S A, 87 (12). pp. 4766-70. ISSN 0027-8424 (Print)0027-8424 (Linking)

[img]
Preview
PDF (Paper)
Beach PNAS 1990.pdf - Published Version

Download (1526Kb) | Preview
URL: http://www.ncbi.nlm.nih.gov/pubmed/2141171
DOI: 10.1073/pnas.87.12.4766

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.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Animals Bivalvia CDC2 Protein Kinase Cell Cycle Cell Line Cyclins Homeostasis Humans Invertebrate Hormones/*metabolism Molecular Sequence Data Oncogene Proteins/isolation & purification/*metabolism Peptide Mapping Peptides/chemical synthesis Phosphoproteins/isolation & purification/*metabolism Phosphorylation Protein Kinases/*metabolism Serine Tumor Suppressor Protein p53
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > Cyclins
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > cdc2
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > p53
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
CSHL Authors:
Communities: CSHL labs > Beach lab
Depositing User: Matt Covey
Date: June 1990
Date Deposited: 28 Mar 2016 19:54
Last Modified: 09 Nov 2017 20:41
PMCID: PMC54198
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32295

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving