Abstract
Sequence analysis is a powerful tool to obtain structural and functional information about genes and their products. Here we show that TSG101, a gene subjected to somatic mutations in breast cancer, contains an amino terminal domain that is a homologue of ubiquitin conjugating enzymes (UBCs) and not, as previously proposed, DNA-binding domains. As the UBC active site residue is replaced in the TSG101 sequence in a similar manner to several other members of the UBC family, we propose a role for TSG101 in regulating the ubiquitination of short-lived gene products.
| Original language | English |
|---|---|
| Pages (from-to) | 467-9 |
| Number of pages | 3 |
| Journal | Journal of Molecular Medicine |
| Volume | 75 |
| Issue number | 7 |
| Publication status | Published - Jul 1997 |
Keywords
- Amino Acid Sequence
- Animals
- Breast Neoplasms
- Chickens
- DNA-Binding Proteins
- Endosomal Sorting Complexes Required for Transport
- Female
- Humans
- Ligases
- Mice
- Molecular Sequence Data
- Saccharomyces cerevisiae
- Sequence Homology, Amino Acid
- Transcription Factors
- Ubiquitin-Conjugating Enzymes
- Ubiquitins