| IED ID | IndEnz0002012027 |
| Enzyme Type ID | protease012027 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 10 EC 3.4.19.12 Deubiquitinating enzyme 10 Disrupter of telomere silencing protein 4 Ubiquitin thioesterase 10 Ubiquitin-specific-processing protease 10 |
| Gene Name | UBP10 DOT4 YNL186W N1619 |
| 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 | MTTQESIKPLVDRILSNPLQFNAAMISNKSNNNDTSAAPENSSYIVIGKQHNNNSNSTAIAATAESKQIKENNLIDRPNGKKTNTVPKSMAEALLLYTSKNDKDAADATGAKKSAELSTELSTEPPSSSSEDDKVGKEEEEEGEIFHEARDYVEPRKASLKERDNADKGDGEDIGEDIGEDIGEDIGEDIGEDIGENLGSPLATIDDSSNENEKEKRKELSTSISSDDEIEDDEDEDDMDYDSSAMEKELPEEEENDSSSKISEGEKKSLYQDLMENSTVEVNRYEPVNNTKENGNRNPKGEEEEEEEEELKHKSRSITPPVTISNLSNFYQFNENINDRGSLNSTRIVKNWGDKFTNLKPRGLLNHGVTCYTNAAVQAMLHIPSIQHYLFDILMGKYDSTISKNSVSYTLAETSKKMWLPVSKNPRKNVSASYINPKHLISRLDDINCMMSEWQQEDSHEYFMSLMSRLQEDSVPKGHKLIESIIYDIFGGLLKQIVTCKSCGSISKTEQPFYDLSLHLKGKKKLDPNSDLSSDSINGTSATTSTTTSNAATKPSLSSSSSVNLNNGSPFAAASDLSSANRRFSIEKSIKDFFNPELIKVDKEQKGYVCEKCHKTTNAVKHSSILRAPETLLVHLKKFRFNGTSSSKMKQAVSYPMFLDLTEYCESKELPVKYQLLSVVVHEGRSLSSGHYIAHCKQPDGSWATYDDEYINIISERDVLKEPNAYYLLYTRLTPKSVPLPLAKSAMATGNVTSKSKQEQAVNEPNNRPLKINSKKNNRKKWKKNKKRKFTK |
| Enzyme Length | 792 |
| Uniprot Accession Number | P53874 |
| Absorption | |
| Active Site | ACT_SITE 371; /note=Nucleophile; /evidence=ECO:0000255|PROSITE-ProRule:PRU01035; ACT_SITE 691; /note=Proton acceptor; /evidence=ECO:0000255|PROSITE-ProRule:PRU01035 |
| Activity Regulation | |
| 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; Evidence={ECO:0000269|PubMed:10490600}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinating enzyme involved in telomere and HM loci silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes (PubMed:9755194, PubMed:10490600, PubMed:14623890). Targets histone H2B for deubiquitination, thus helping to localize SIR2 to the telomere (PubMed:15721261, PubMed:17028327, PubMed:22056669). At silent chromatin, including telomeres and the rDNA locus, not only maintains low H2B 'Lys-123' ubiquitination (H2BK123Ub), but also low H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively) (PubMed:15721261, PubMed:15988024). Controls the proliferating-cell nuclear antigen PCNA/POL30 deubiquitination which is crucial for keeping TLS polymerases in check as well as for down-regulating the error-free bypass (PubMed:22829782). Deubiquitinates and stabilizes RPA190, the largest subunit of RNA polymerase I, to achieve optimal levels of ribosomes and cell growth (PubMed:22902402). Protects also nutrient transporters such as GAP1 from ubiquitin-dependent endocytosis (PubMed:11352638). {ECO:0000269|PubMed:10490600, ECO:0000269|PubMed:11352638, ECO:0000269|PubMed:14623890, ECO:0000269|PubMed:15721261, ECO:0000269|PubMed:15988024, ECO:0000269|PubMed:17028327, ECO:0000269|PubMed:22056669, ECO:0000269|PubMed:22829782, ECO:0000269|PubMed:22902402, ECO:0000269|PubMed:9755194}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (11); Domain (1); Mutagenesis (1); Region (7); Sequence conflict (1) |
| Keywords | 3D-structure;Chromosome;Hydrolase;Nucleus;Protease;Reference proteome;Telomere;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10490600}. Chromosome, telomere {ECO:0000269|PubMed:15721261}. Nucleus, nucleolus {ECO:0000269|PubMed:22902402}. Note=Preferentially localizes to silent chromatin (PubMed:15988024). {ECO:0000269|PubMed:15988024}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 6RR0; |
| Mapped Pubmed ID | 11076031; 11805826; 14690591; 15489197; 15556039; 15766533; 16429126; 16455487; 16554755; 16568953; 16606443; 16756492; 18355456; 18374642; 18467557; 18562693; 19165343; 19188254; 19489724; 19536198; 19734957; 20008511; 20074044; 20211662; 20439497; 21936842; 21937884; 23208446; 23547164; 23818500; 24025678; 25043177; 25136098; 25705722; 25947383; 26503604; 26503781; 26587833; 26783300; 27250769; 27737893; 27769718; 29288197; 31515872; 8982460; |
| Motif | |
| Gene Encoded By | |
| Mass | 88,531 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |