| IED ID | IndEnz0002013007 |
| Enzyme Type ID | protease013007 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 8 EC 3.4.19.12 Deubiquitinating enzyme 8 Ubiquitin thioesterase 8 Ubiquitin-specific-processing protease 8 |
| Gene Name | UBP8 YMR223W YM9959.05 |
| 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 | MSICPHIQQVFQNEKSKDGVLKTCNAARYILNHSVPKEKFLNTMKCGTCHEINSGATFMCLQCGFCGCWNHSHFLSHSKQIGHIFGINSNNGLLFCFKCEDYIGNIDLINDAILAKYWDDVCTKTMVPSMERRDGLSGLINMGSTCFMSSILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGALNTKQASSSSTSTNRQTGFIYLLTCAWKINQNLAGYSQQDAHEFWQFIINQIHQSYVLDLPNAKEVSRANNKQCECIVHTVFEGSLESSIVCPGCQNNSKTTIDPFLDLSLDIKDKKKLYECLDSFHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLNGSNRKLDDFIEFPTYLNMKNYCSTKEKDKHSENGKVPDIIYELIGIVSHKGTVNEGHYIAFCKISGGQWFKFNDSMVSSISQEEVLKEQAYLLFYTIRQVN |
| Enzyme Length | 471 |
| Uniprot Accession Number | P50102 |
| Absorption | |
| Active Site | ACT_SITE 146; /note="Nucleophile"; ACT_SITE 427; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093" |
| 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; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Functions as histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. Together with SGF11, is required for histone H2B deubiquitination. {ECO:0000269|PubMed:10026213, ECO:0000269|PubMed:14660634, ECO:0000269|PubMed:15657441}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (23); Chain (1); Domain (1); Helix (21); Metal binding (8); Mutagenesis (5); Turn (7); Zinc finger (1) |
| Keywords | 3D-structure;Hydrolase;Metal-binding;Nucleus;Protease;Reference proteome;Thiol protease;Transcription;Transcription regulation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | Q12060 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (1); X-ray crystallography (9) |
| Cross Reference PDB | 3M99; 3MHH; 3MHS; 4FIP; 4FJC; 4FK5; 4WA6; 4ZUX; 6AQR; 6T9L; |
| Mapped Pubmed ID | 10688190; 11076031; 11805826; 11805837; 11893486; 12052880; 12151331; 12213658; 12816519; 14563679; 14660704; 14718168; 15171247; 15282323; 15506919; 15657442; 15721261; 15786493; 15988024; 16429126; 16554755; 16568953; 16611979; 16705165; 16756492; 16855026; 16888622; 17118266; 17337012; 17566592; 17643376; 17786152; 18374642; 18488019; 18562693; 18718879; 18719252; 18805098; 18978833; 19077548; 19226466; 19229139; 19239896; 19246994; 19330770; 19411170; 19489724; 19536198; 19561118; 19734957; 19756577; 19834536; 20074044; 20090412; 20363118; 20395473; 20434206; 20439497; 20489023; 20621284; 20699646; 20800707; 21074715; 21179020; 21320604; 21490951; 21602906; 21628526; 21685874; 21734642; 21937884; 21954323; 21984211; 22056669; 22084422; 22094418; 22178374; 22248620; 22345607; 22426530; 22567346; 22723847; 22771212; 22771944; 23057668; 23144132; 23208446; 23209445; 23586741; 23645753; 23731471; 23762321; 23917692; 23964287; 24021962; 24025678; 24040048; 24040173; 24136112; 24307402; 24904600; 24911582; 25043177; 25136098; 25171917; 25216679; 25228644; 25441028; 25473596; 25509853; 25526805; 25658705; 25705722; 25802992; 25947383; 26051071; 26241481; 26344768; 26456335; 26503604; 26503781; 26613948; 26811423; 26912860; 27057639; 27112564; 27250769; 27693354; 27737893; 27741413; 27769718; 30150323; 31969703; 32788380; 33115507; 8982460; |
| Motif | |
| Gene Encoded By | |
| Mass | 53,623 |
| Kinetics | |
| Metal Binding | METAL 46; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 49; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 60; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 63; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 68; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 73; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 77; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 83; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502 |
| Rhea ID | |
| Cross Reference Brenda |