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Article

A novel p53 phosphorylation site within the MDM2 ubiquitination signal: I. phosphorylation at SER269 in vivo is linked to inactivation of p53 function.

The Journal of biological chemistry - 26 Nov 2010

Fraser Jennifer A, Vojtesek Borivoj, Hupp Ted R

Abstract excerpt

p53 is a thermodynamically unstable protein containing a conformationally flexible multiprotein docking site within the DNA-binding domain. A combinatorial peptide chip used to identify the novel kinase consensus site RXSΦ(K/D) led to the discovery of a homologous phosphorylation site in the S10 β-strand of p53 at Ser(269). Overlapping peptide libraries confirmed that Ser(269) was a phosphoacceptor site in vitro,...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Proto-Oncogene Proteins c-mdm2

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Source

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Identifiers

PMID: 20851891
DOI: 10.1074/jbc.M110.143099
PMCID: PMC2988381

Genes

MDM2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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