Detail Information for IndEnz0002012761
IED ID IndEnz0002012761
Enzyme Type ID protease012761
Protein Name OTU domain-containing protein 5
EC 3.4.19.12
Deubiquitinating enzyme A
DUBA
Gene Name Otud5 DXImx46e Sfc7
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 MTILPKKKPPPPDADPANEPPPPGPLPPAPRRGAGVGVGGGGTGVGGGERDRDSGVVGARPRASPPPQGPLPGPPGALHRWALAVPPGAVAGPRPQQASPPPCGGPGGPGGGPGDALGATTAGVGAAGVVVGVGGTVGVGGCCSGPGHSKRRRQAPGVGAVGGASPEREEVGAGYNSEDEYEAAAARIEAMDPATVEQQEHWFEKALRDKKGFIIKQMKEDGACLFRAVADQVYGDQDMHEVVRKHCMDYLMKNADYFSNYVTEDFTTYINRKRKNNCHGNHIEMQAMAEMYNRPVEVYQYSTEPINTFHGIHQNEDEPIRVSYHRNIHYNSVVNPNKATIGVGLGLPSFKPGFAEQSLMKNAIKTSEESWIEQQMLEDKKRATDWEATNEAIEEQVARESYLQWLRDQEKQARQVRGPSQPRKASATCSSATAAASSGLEEWTSRSPRQRSSASSPEHPELHAELGIKPPSPGTVLALAKPPSPCAPGTSSQFSAGGDRATSPLVSLYPALECRALIQQMSPSAFGLNDWDDDEILASVLAVSQQEYLDSMKKNKVHREPPPDKS
Enzyme Length 566
Uniprot Accession Number Q3U2S4
Absorption
Active Site ACT_SITE 221; /evidence=ECO:0000255; ACT_SITE 224; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 329; /evidence=ECO:0000250
Activity Regulation ACTIVITY REGULATION: Inhibited by N-ethyl-maleimide (NEM). {ECO:0000250}.
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:0000250|UniProtKB:Q96G74};
DNA Binding
EC Number 3.4.19.12
Enzyme Function FUNCTION: Deubiquitinating enzyme that functions as negative regulator of the innate immune system. Acts via TRAF3 deubiquitination and subsequent suppression of type I interferon (IFN) production. Has peptidase activity towards 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave 'Lys-11'-linked ubiquitin chains (in vitro). Controls neuroectodermal differentiation through cleaving 'Lys-48'-linked ubiquitin chains to counteract degradation of select chromatin regulators such as ARID1A, HDAC2 and HCF1. {ECO:0000250|UniProtKB:Q96G74}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Alternative sequence (1); Chain (1); Compositional bias (3); Domain (1); Modified residue (6); Region (6); Sequence conflict (6)
Keywords Alternative splicing;Hydrolase;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway
Interact With Q80TP3
Induction
Subcellular Location SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96G74}.
Modified Residue MOD_RES 64; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96G74; MOD_RES 165; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 175; /note=Phosphotyrosine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 177; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 447; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q96G74; MOD_RES 502; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q96G74
Post Translational Modification PTM: Phosphorylation at Ser-177 is required for deubiquitinating activity. {ECO:0000250|UniProtKB:Q96G74}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11138001; 11217851; 12466851; 12520002; 12904583; 14610273; 18799693; 20548051; 21267068; 22245969; 25470037; 26496610; 32826889;
Motif
Gene Encoded By
Mass 60,306
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda