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The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.

Oncogene | Sep 6, 2001

The ubiquitin pathway is involved in the proteolytic turnover of many short-lived cellular regulatory proteins. Since selective degradation of substrates of this system requires the covalent attachment of a polyubiquitin chain to the substrates, degradation could be counteracted by de-ubiquitinating enzymes (or isopeptidases) which selectively remove the polyubiquitin chain. Unp is a human isopeptidase with still poorly understood biological functions. Here, we show that cellular Unp specifically interacts with the retinoblastoma gene product (pRb).

Pubmed ID: 11571652 RIS Download

Mesh terms: Amino Acid Motifs | Antibodies | Cell Cycle | Cell Line | Humans | Jurkat Cells | Oncogene Proteins | Retinoblastoma Protein | Tumor Cells, Cultured | Ubiquitin Thiolesterase | Ubiquitins

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Associated grants

  • Agency: NCI NIH HHS, Id: 5RO1-CA81755
  • Agency: NCI NIH HHS, Id: P30-CA16087
  • Agency: NCI NIH HHS, Id: R01-CA76584
  • Agency: NIGMS NIH HHS, Id: R01-GM57587
  • Agency: NCI NIH HHS, Id: R21-CA66229

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