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

First Author  Hauser HP Year  1998
Journal  J Cell Biol Volume  141
Issue  6 Pages  1415-22
PubMed ID  9628897 Mgi Jnum  J:48143
Mgi Id  MGI:1266878 Doi  10.1083/jcb.141.6.1415
Citation  Hauser HP, et al. (1998) A giant ubiquitin-conjugating enzyme related to IAP apoptosis inhibitors. J Cell Biol 141(6):1415-22
abstractText  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.
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