7en4

Structural highlights

Function

UBL1_YEAST Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or RUB1. Preferentially cleaves ubiquitin from peptides and small adducts.^{[1] [2] [3] [4]}

References

1. ↑ Liu CC, Miller HI, Kohr WJ, Silber JI. Purification of a ubiquitin protein peptidase from yeast with efficient in vitro assays. J Biol Chem. 1989 Dec 5;264(34):20331-8. PMID:2555355
2. ↑ Linghu B, Callis J, Goebl MG. Rub1p processing by Yuh1p is required for wild-type levels of Rub1p conjugation to Cdc53p. Eukaryot Cell. 2002 Jun;1(3):491-4. PMID:12455997
3. ↑ Yu HA, Kim SG, Kim EJ, Lee WJ, Kim DO, Park K, Park YC, Seo JH. Characterization of ubiquitin C-terminal hydrolase 1 (YUH1) from Saccharomyces cerevisiae expressed in recombinant Escherichia coli. Protein Expr Purif. 2007 Nov;56(1):20-6. Epub 2007 Jul 18. PMID:17709260 doi:http://dx.doi.org/10.1016/j.pep.2007.07.005
4. ↑ Dennissen FJ, Kholod N, Hermes DJ, Kemmerling N, Steinbusch HW, Dantuma NP, van Leeuwen FW. Mutant ubiquitin (UBB+1) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3). FEBS Lett. 2011 Aug 19;585(16):2568-74. doi: 10.1016/j.febslet.2011.06.037. Epub , 2011 Jul 6. PMID:21762696 doi:http://dx.doi.org/10.1016/j.febslet.2011.06.037