Detail Information for IndEnz0002011237
IED ID IndEnz0002011237
Enzyme Type ID protease011237
Protein Name Ubiquitin carboxyl-terminal hydrolase 27
EC 3.4.19.12
Deubiquitinating enzyme 27
Ubiquitin thioesterase 27
Ubiquitin-specific-processing protease 27
X-linked ubiquitin carboxyl-terminal hydrolase 27
Gene Name Usp27x Usp27
Organism Mus musculus (Mouse)
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 Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse)
Enzyme Sequence MCKDYVYDIDIEQIAKEEQGEALKLQASTSTEVSQQQCSVPGLGEKYPTWETTKPELELLGHNPRRRRIASSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDVGKVASNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCTSFWPMSPGRESSLNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMKKLPVVACFHFKRFEHSAKQRRKITTYISFPLELDMTPFMASSKETRVNGQLQLPTNSANNENKYSLFAVVNHQGTLESGHYTSFIRHHRDQWFKCDDAVITKASIKDVLDSEGYLLFYHKQVLEPEPEKVKEMTPQAY
Enzyme Length 438
Uniprot Accession Number Q8CEG8
Absorption
Active Site ACT_SITE 87; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 380; /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; Evidence={ECO:0000269|PubMed:27013495};
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). Negatively regulates DDX58/RIG-I by mediating 'Lys-63'-linked deubiquitination of DDX58/RIG-I, inhibiting type I interferon signaling (By similarity). Also regulates 'Lys-63'-linked ubiquitination level of MDA5/IFIH1 (By similarity). 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 (PubMed:27013495). By acting on BCL2L11 levels, may counteract the anti-apoptotic effects of MAPK activity (PubMed:27013495). {ECO:0000250|UniProtKB:A6NNY8, ECO:0000269|PubMed:27013495, ECO:0000269|PubMed:31534008}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Domain (1); Erroneous initiation (3); Frameshift (1); Mutagenesis (1); Sequence conflict (4)
Keywords Cytoplasm;Hydrolase;Immunity;Innate immunity;Nucleus;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:27013495}. Nucleus {ECO:0000269|PubMed:27013495}.
Modified Residue
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 12466851; 16602821; 21267068; 32027733;
Motif
Gene Encoded By
Mass 49,599
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda