The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein

Oncogene. 2001 Sep 6;20(39):5538-42. doi: 10.1038/sj.onc.1204824.


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).

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Antibodies / immunology
  • Cell Cycle
  • Cell Line
  • Humans
  • Jurkat Cells
  • Oncogene Proteins / chemistry
  • Oncogene Proteins / immunology
  • Oncogene Proteins / metabolism*
  • Retinoblastoma Protein / metabolism*
  • Tumor Cells, Cultured
  • Ubiquitin Thiolesterase
  • Ubiquitin-Specific Proteases
  • Ubiquitins / metabolism


  • Antibodies
  • Oncogene Proteins
  • Retinoblastoma Protein
  • USP4 protein, human
  • Ubiquitins
  • Ubiquitin Thiolesterase
  • Ubiquitin-Specific Proteases