| IED ID | IndEnz0002001062 |
| Enzyme Type ID | protease001062 |
| 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 hVDU2 |
| Gene Name | USP20 KIAA1003 LSFR3A VDU2 |
| 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 | MGDSRDLCPHLDSIGEVTKEDLLLKSKGTCQSCGVTGPNLWACLQVACPYVGCGESFADHSTIHAQAKKHNLTVNLTTFRLWCYACEKEVFLEQRLAAPLLGSSSKFSEQDSPPPSHPLKAVPIAVADEGESESEDDDLKPRGLTGMKNLGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSEVWHKKRPSYVVPTSLSHGIKLVNPMFRGYAQQDTQEFLRCLMDQLHEELKEPVVATVALTEARDSDSSDTDEKREGDRSPSEDEFLSCDSSSDRGEGDGQGRGGGSSQAETELLIPDEAGRAISEKERMKDRKFSWGQQRTNSEQVDEDADVDTAMAALDDQPAEAQPPSPRSSSPCRTPEPDNDAHLRSSSRPCSPVHHHEGHAKLSSSPPRASPVRMAPSYVLKKAQVLSAGSRRRKEQRYRSVISDIFDGSILSLVQCLTCDRVSTTVETFQDLSLPIPGKEDLAKLHSAIYQNVPAKPGACGDSYAAQGWLAFIVEYIRRFVVSCTPSWFWGPVVTLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEILCIHLKRFRHEVMYSFKINSHVSFPLEGLDLRPFLAKECTSQITTYDLLSVICHHGTAGSGHYIAYCQNVINGQWYEFDDQYVTEVHETVVQNAEGYVLFYRKSSEEAMRERQQVVSLAAMREPSLLRFYVSREWLNKFNTFAEPGPITNQTFLCSHGGIPPHKYHYIDDLVVILPQNVWEHLYNRFGGGPAVNHLYVCSICQVEIEALAKRRRIEIDTFIKLNKAFQAEESPGVIYCISMQWFREWEAFVKGKDNEPPGPIDNSRIAQVKGSGHVQLKQGADYGQISEETWTYLNSLYGGGPEIAIRQSVAQPLGPENLHGEQKIEAETRAV |
| Enzyme Length | 914 |
| Uniprot Accession Number | Q9Y2K6 |
| Absorption | |
| Active Site | ACT_SITE 154; /note="Nucleophile"; ACT_SITE 643; /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. {ECO:0000269|PubMed:12056827, ECO:0000269|PubMed:12865408, ECO:0000269|PubMed:15776016, ECO:0000269|PubMed:19424180}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (5); Chain (1); Compositional bias (2); Domain (3); Erroneous initiation (1); Helix (2); Metal binding (12); Modified residue (9); Mutagenesis (2); Natural variant (2); Region (2); Sequence conflict (8); Turn (5); Zinc finger (1) |
| Keywords | 3D-structure;Cytoplasm;Cytoskeleton;Endocytosis;Hydrolase;Metal-binding;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | P13196; Q7L4P6; Q8N7W2-2; Q969F0; Q8IYA8; P43364-2; Q99750; O43597; P36406; O95292; Q53XM7 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:23486064}. Note=According to PubMed:12865408, it localizes in the endoplasmic reticulum; however the relevance of such result is unclear. |
| Modified Residue | MOD_RES 112; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 132; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 134; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 258; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:17081983"; MOD_RES 305; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 368; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8C6M1"; MOD_RES 377; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"; MOD_RES 408; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 413; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" |
| Post Translational Modification | PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal degradation. {ECO:0000269|PubMed:12056827}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 6KCZ; |
| Mapped Pubmed ID | 19615732; 19851296; 20198315; 21282530; 21525354; 22552337; 24923443; 25416956; 25666616; 25708858; 28167606; 29487085; 29867130; 31278784; 32354117; 32943575; 33529762; 33792613; |
| Motif | |
| Gene Encoded By | |
| Mass | 102,003 |
| 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 |