The breast cancer gene product TSG101: a regulator of ubiquitination?

C P Ponting, Y D Cai, P Bork

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)467-9
Number of pages3
JournalJournal of Molecular Medicine
Volume75
Issue number7
Publication statusPublished - 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

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