| IED ID | IndEnz0002012489 |
| Enzyme Type ID | protease012489 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 6 EC 3.4.19.12 Deubiquitinating enzyme 6 Ubiquitin thioesterase 6 Ubiquitin-specific-processing protease 6 |
| Gene Name | UBP6 YFR010W |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSGETFEFNIRHSGKVYPITLSTDATSADLKSKAEELTQVPSARQKYMVKGGLSGEESIKIYPLIKPGSTVMLLGTPDANLISKPAKKNNFIEDLAPEQQVQQFAQLPVGFKNMGNTCYLNATLQALYRVNDLRDMILNYNPSQGVSNSGAQDEEIHKQIVIEMKRCFENLQNKSFKSVLPIVLLNTLRKCYPQFAERDSQGGFYKQQDAEELFTQLFHSMSIVFGDKFSEDFRIQFKTTIKDTANDNDITVKENESDSKLQCHISGTTNFMRNGLLEGLNEKIEKRSDLTGANSIYSVEKKISRLPKFLTVQYVRFFWKRSTNKKSKILRKVVFPFQLDVADMLTPEYAAEKVKVRDELRKVEKEKNEKEREIKRRKFDPSSSENVMTPREQYETQVALNESEKDQWLEEYKKHFPPNLEKGENPSCVYNLIGVITHQGANSESGHYQAFIRDELDENKWYKFNDDKVSVVEKEKIESLAGGGESDSALILMYKGFGL |
| Enzyme Length | 499 |
| Uniprot Accession Number | P43593 |
| Absorption | |
| Active Site | ACT_SITE 118; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 447; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
| Activity Regulation | ACTIVITY REGULATION: Activated by it's association with the proteasome. {ECO:0000269|PubMed:12408819}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Predominant proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Has proteasome-inhibitory activity and delays the degradation of ubiquitinated proteins to provide a time window allowing gradual deubiquitination of the substrate. Stabilizes the association of HUL5 with proteasomes and works in opposition to polyubiquitin elongation activity of HUL5. {ECO:0000269|PubMed:10527495, ECO:0000269|PubMed:12408819, ECO:0000269|PubMed:14581483, ECO:0000269|PubMed:17018280, ECO:0000269|PubMed:17190603, ECO:0000269|PubMed:9344467}. |
| Temperature Dependency | |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5-9. {ECO:0000269|PubMed:9344467}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (14); Chain (1); Compositional bias (1); Domain (2); Helix (14); Modified residue (2); Region (1); Turn (2) |
| Keywords | 3D-structure;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 389; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"; MOD_RES 470; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18407956" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (2); X-ray crystallography (1) |
| Cross Reference PDB | 1VJV; 5A5B; 5MPC; |
| Mapped Pubmed ID | 10603300; 11076031; 11566882; 11805826; 12073095; 14559899; 14645527; 14759368; 15117949; 15188770; 15451116; 15571806; 15610744; 15699485; 15905137; 15987637; 16284124; 16429126; 16554755; 16922378; 17418826; 17512408; 17900906; 18243380; 18467557; 18793193; 19067491; 19153599; 19188254; 19446323; 19447341; 19489724; 19536198; 19734957; 20074044; 20850176; 21427232; 21543789; 21587205; 21601516; 21658604; 21931558; 22214660; 22318722; 22350874; 22350895; 22350912; 22460800; 22529852; 22614003; 22729030; 23208446; 23341450; 23545414; 23672618; 23697803; 25073701; 25120264; 25333764; 25389291; 26130806; 26182356; 26262643; 26301997; 26450923; 26503604; 26503781; 27074503; 27234297; 27677933; 28115689; 31640922; |
| Motif | |
| Gene Encoded By | |
| Mass | 57,111 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |