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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53.

FEBS letters | Dec 22, 1997

The tumor suppressor p53 is degraded by the ubiquitin-proteasome system. p53 was polyubiquitinated in the presence of E1, UbcH5 as E2 and MDM2 oncoprotein. A ubiquitin molecule bound MDM2 through sulfhydroxy bond which is characteristic of ubiquitin ligase (E3)-ubiquitin binding. The cysteine residue in the carboxyl terminus of MDM2 was essential for the activity. These data suggest that the MDM2 protein, which is induced by p53, functions as a ubiquitin ligase, E3, in human papillomavirus-uninfected cells which do not have E6 protein.

Pubmed ID: 9450543 RIS Download

Mesh terms: Amino Acid Sequence | Cell Extracts | HeLa Cells | Humans | Ligases | Molecular Sequence Data | Nuclear Proteins | Proto-Oncogene Proteins | Proto-Oncogene Proteins c-mdm2 | Sequence Analysis | Tumor Suppressor Protein p53 | Ubiquitin-Conjugating Enzymes | Ubiquitins

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