Detail Information for IndEnz0002001063
IED ID IndEnz0002001063
Enzyme Type ID protease001063
Protein Name Ubiquitin carboxyl-terminal hydrolase 20
EC 3.4.19.12
Deubiquitinating enzyme 20
Ubiquitin thioesterase 20
Ubiquitin-specific-processing protease 20
VHL-interacting deubiquitinating enzyme 2
Gene Name Usp20 Kiaa1003 Vdu2
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 MGDARDLCPHLDCIGEVTKEDLLLKSKGTCQSCGVAGPNLWACLQVTCPYVGCGESFADHSSIHAQVKKHNLTVNLTTFRVWCYACEREVFLEQRLAVHLASSSARLSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLISEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPMVAAVAALTDARDSDSSDTDERRDGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSKAEMELLISDEAGRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMASLDEQSREAQPPSPRSTSPCQTPEPDNEAHIRSSSRPCSPVHHHHEGHSKLSSSPPRASPVRMGPSYVLKKAQVPSTGGRRRKEQSYRSVISDVFNGSVLSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGACGDSYSSQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLCLPEILCVHLKRFRHEVMYSFKVSSHVSFPLEGLDLRPFLAKECTSQVTTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNVEAYVLFYRKSSEEAMRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNHTFLCSHGGIPPNKYHYIDDLVVILPQSVWEHLYSRFGGGPAVNHLYVCSICQVEIEALAKRRRVEIDTFIKLNKAFQAEESPAVIYCISMHWFREWEAFVKGKDSEPPGPIDNSRIAQVKGSGHIQLKQGADCGQISEETWTYLSSLYGGGPEIAIRQSVAQLPDPESLHGEQKIEAETRAL
Enzyme Length 916
Uniprot Accession Number Q8C6M1
Absorption
Active Site ACT_SITE 154; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 645; /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: Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Compositional bias (3); Domain (3); Erroneous initiation (1); Metal binding (12); Modified residue (9); Region (1); Sequence conflict (2); Zinc finger (1)
Keywords Cytoplasm;Cytoskeleton;Endocytosis;Hydrolase;Metal-binding;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
Modified Residue MOD_RES 112; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9Y2K6"; MOD_RES 132; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"; MOD_RES 134; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9Y2K6"; MOD_RES 259; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:Q9Y2K6"; MOD_RES 306; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9Y2K6"; MOD_RES 369; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:15345747"; MOD_RES 378; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17242355"; MOD_RES 410; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9Y2K6"; MOD_RES 415; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
Post Translational Modification PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal degradation. {ECO:0000250}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 11217851; 12466851; 14610273; 18799693; 21267068; 23341629; 26839314; 30354204; 30538132; 30814308; 33177714; 33420925;
Motif
Gene Encoded By
Mass 102,140
Kinetics
Metal Binding METAL 8; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 10; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 30; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 33; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 43; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 48; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 53; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 60; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 64; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 70; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 83; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 86; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502
Rhea ID
Cross Reference Brenda