| IED ID | IndEnz0002011149 |
| Enzyme Type ID | protease011149 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 27 EC 3.4.19.12 Deubiquitinating enzyme 27 Ubiquitin carboxyl-terminal hydrolase 22-like Ubiquitin thioesterase 27 Ubiquitin-specific-processing protease 27 X-linked ubiquitin carboxyl-terminal hydrolase 27 |
| Gene Name | USP27X USP22L USP27 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MCKDYVYDKDIEQIAKEEQGEALKLQASTSTEVSHQQCSVPGLGEKFPTWETTKPELELLGHNPRRRRITSSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCTSFWPMSPGRESSVNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKESRMNGQLQLPTNSGNNENKYSLFAVVNHQGTLESGHYTSFIRHHKDQWFKCDDAVITKASIKDVLDSEGYLLFYHKQVLEHESEKVKEMNTQAY |
| Enzyme Length | 438 |
| Uniprot Accession Number | A6NNY8 |
| Absorption | |
| Active Site | ACT_SITE 87; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093, ECO:0000305|PubMed:31534008, ECO:0000305|PubMed:32027733"; ACT_SITE 380; /note="Proton acceptor"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093, ECO:0000305|PubMed:32027733" |
| 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:31534008, ECO:0000269|PubMed:32027733}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinase involved in innate antiviral immunity by mediating deubiquitination of CGAS and DDX58/RIG-I (PubMed:31534008, PubMed:32027733). Negatively regulates DDX58/RIG-I by mediating 'Lys-63'-linked deubiquitination of DDX58/RIG-I, inhibiting type I interferon signaling (PubMed:32027733). Also regulates 'Lys-63'-linked ubiquitination level of MDA5/IFIH1 (PubMed:32027733). Acts as a positive regulator of the cGAS-STING pathway by catalyzing 'Lys-48'-linked deubiquitination of CGAS, thereby promoting its stabilization (PubMed:31534008). Can reduce the levels of BCL2L11/BIM ubiquitination and stabilize BCL2L11 in response to the RAF-MAPK-degradation signal (By similarity). By acting on BCL2L11 levels, may counteract the anti-apoptotic effects of MAPK activity (By similarity). {ECO:0000250|UniProtKB:Q8CEG8, ECO:0000269|PubMed:31534008, ECO:0000269|PubMed:32027733}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Domain (1); Mutagenesis (3); Natural variant (1); Sequence conflict (2) |
| Keywords | Cytoplasm;Disease variant;Hydrolase;Immunity;Innate immunity;Mental retardation;Nucleus;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8CEG8}. Nucleus {ECO:0000250|UniProtKB:Q8CEG8}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19615732; 27013495; 27132940; 29497124; 30341066; 35018513; |
| Motif | |
| Gene Encoded By | |
| Mass | 49,630 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |