InterPro domain: IPR033864

scUBP14, also called deubiquitinating enzyme 14, glucose-induced degradation protein 6, ubiquitin thioesterase 14, or ubiquitin-specific-processing protease 14 (MEROPS identifier C19.083), is the Saccharomyces cerevisiae orthologue of human Isopeptidase T (USP5), a deubiquitinating enzyme known to bind the 29-linked polyubiquitin chains. scUBP14 has been identified as a K29-linked polyubiquitin binding protein as well. It is involved in K29-linked polyubiquitin metabolism by binding to the 29-linked Ub4 resin and serving as an internal positive control in budding yeast [ 1 , 2 ]. Members in this family contain two tandem ubiquitin-association (UBA) domains.

This entry corresponds to the UBA2 domain in Saccharomyces cerevisiae UBP14 and related proteins [ 3 ].

1. Mutants of the deubiquitinating enzyme Ubp14 decipher pathway diversity of ubiquitin-proteasome linked protein degradation. Biochem. Biophys. Res. Commun. 350, 329-33
2. In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome. EMBO J. 16, 4826-38
3. Identification of a novel 29-linked polyubiquitin binding protein, Ufd3, using polyubiquitin chain analogues. Biochemistry 43, 4844-54