| IED ID | IndEnz0002013120 |
| Enzyme Type ID | protease013120 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 20 EC 3.4.19.12 Deubiquitinating enzyme 20 Ubiquitin thioesterase 20 Ubiquitin-specific-processing protease 20 |
| Gene Name | usp20 |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MADAEDFCPHLDSIGEVTKEDLILKSKGTCESCGVGGPNLWACLQDGCQSVGCGESYADHSTLHAQDFPSPAHPLKSVPIAVGDDGESESDEDDIKPRGLTGMKNIGNSCYMNAALQALSNCPPLTQFFLECGGLVRTDKKPALCKSYQKLVSELWHKKRPSYVVPSSLYHGIKLINPLFRGYSQQDTQEFLRCLMDQLHEELKEPILPENQEQEEEERDDQREGERGGTTEEDFLSCDSGGEMGDGEGGGGVGTLSEMELLIREEVGRGLSEKEKLKERKLSYCHRRTSSEQADEDADVDTAMIPEPDNDAYMHCSSRSCSPHPVESISKHSSTPPRSSPLRTAHSYVLKKAQVLSGGKKRSEVRYRSVISDIFDGSILSLVQCLTCDRVSTTIETFQDLSLPIPGKEDLAKLHSTIHQSTVIKAGTCGDSYAAQGWLAFVMDYIRRFVVSCIPSWFWGPMITLEDCLAAFFAADELKGDNMYSCERCKKLRNGVKYCKVLRLPEVLCIHLKRFRHEVMYSFKIGSHVSFPLEGLNLRPFLAKECVSRITTYDLLAVICHHGSASSGHYISYCQNVINGQWYEFDDQYVTEVHETVVQNAEAYVLFYRKSSEEAERERQKVVSLAAMKESGLLQFYISREWLNKFNTFAEPGPISNQSFLCAHGGIPPNKYHYIDDLVVILPQSVWEYLYNRFGGGPAVNHLYVCSICQVEIEALAKRRKTEIDTFIKLNKAFQAEEAPSVIYCISMQWFREWEAFVKAKDSDPPGPIDNSKVALTKSSGHVQLKQGADYGQISEETWNYLLNIYGGGPEIAIRQTVAQYQDPEHLHGEQKIEAETRAG |
| Enzyme Length | 840 |
| Uniprot Accession Number | B1WBD7 |
| Absorption | |
| Active Site | ACT_SITE 110; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 569; /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. 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); Domain (3); Metal binding (4); Region (2); Zinc finger (1) |
| Keywords | Cytoplasm;Cytoskeleton;Endocytosis;Hydrolase;Metal-binding;Protease;Repeat;Thiol protease;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 | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 94,092 |
| Kinetics | |
| Metal Binding | METAL 30; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 33; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 53; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 60; /note=Zinc; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502 |
| Rhea ID | |
| Cross Reference Brenda |