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A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors.

Ubiquitin-conjugating enzymes (UBC) catalyze the covalent attachment of ubiquitin to target proteins and are distinguished by the presence of a UBC domain required for catalysis. Previously identified members of this enzyme family are small proteins and function primarily in selective proteolysis pathways. Here we describe BRUCE (BIR repeat containing ubiquitin-conjugating enzyme), a giant (528-kD) ubiquitin-conjugating enzyme from mice. BRUCE is membrane associated and localizes to the Golgi compartment and the vesicular system. Remarkably, in addition to being an active ubiquitin-conjugating enzyme, BRUCE bears a baculovirus inhibitor of apoptosis repeat (BIR) motif, which to this date has been exclusively found in apoptosis inhibitors of the IAP-related protein family. The BIR motifs of IAP proteins are indispensable for their anti-cell death activity and are thought to function through protein-protein interaction. This suggests that BRUCE may combine properties of IAP-like proteins and ubiquitin-conjugating enzymes and indicates that the family of IAP-like proteins is structurally and functionally more diverse than previously expected.

Pubmed ID: 9628897


  • Hauser HP
  • Bardroff M
  • Pyrowolakis G
  • Jentsch S


The Journal of cell biology

Publication Data

June 15, 1998

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • DNA, Complementary
  • Gene Expression
  • Inhibitor of Apoptosis Proteins
  • Intracellular Membranes
  • Ligases
  • Membrane Proteins
  • Mice
  • Molecular Sequence Data
  • PC12 Cells
  • Rats
  • Sequence Homology, Amino Acid
  • Ubiquitin-Conjugating Enzymes
  • Viral Proteins