Member database | Pfam |
Pfam type | domain |
Short name | BRCC36_C |
Author | El-Gebali S;0000-0003-1378-5495 Smart A;0000-0002-6965-5633 |
Sequence Ontology | 0000417 |
Description
This is the C-terminal domain of BRCC36, a Zn2+ dependent deubiquitinating enzyme, present in Camponotus floridanus. BRCC36 hydrolyzes lysine linked ubiquitin chains as part of macromolecular complexes that participate in either interferon signalling or DNA-damage recognition. The domain consists of 2 non canonical helices. The domain interacts hydrophobically with helices alpha 4 and alpha 5 of KIAA0157 in the form of a coiled coil helical bundle. This interaction helps establish the association of BRCC36 with KIAA0157, a pseudo-DUB MPN- protein that is essential for the activity of BRCC36
[1].
References
1.Higher-Order Assembly of BRCC36-KIAA0157 Is Required for DUB Activity and Biological Function. Zeqiraj E, Tian L, Piggott CA, Pillon MC, Duffy NM, Ceccarelli DF, Keszei AF, Lorenzen K, Kurinov I, Orlicky S, Gish GD, Heck AJ, Guarne A, Greenberg RA, Sicheri F. Mol. Cell 59, 970-83, (2015). View articlePMID: 26344097