The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.
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).
Mesh Terms:
Amino Acid Motifs, Antibodies, Cell Cycle, Cell Line, Humans, Jurkat Cells, Oncogene Proteins, Retinoblastoma Protein, Tumor Cells, Cultured, Ubiquitin Thiolesterase, Ubiquitins
Amino Acid Motifs, Antibodies, Cell Cycle, Cell Line, Humans, Jurkat Cells, Oncogene Proteins, Retinoblastoma Protein, Tumor Cells, Cultured, Ubiquitin Thiolesterase, Ubiquitins
Oncogene
Date: Sep. 06, 2001
PubMed ID: 11571652
View in: Pubmed Google Scholar
Download Curated Data For This Publication
11746
Switch View:
- Interactions 3