| IED ID | IndEnz0002010827 |
| Enzyme Type ID | protease010827 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 19 EC 3.4.19.12 Deubiquitinating enzyme 19 Ubiquitin thioesterase 19 Ubiquitin-specific-processing protease 19 |
| Gene Name | Usp19 |
| Organism | Rattus norvegicus (Rat) |
| 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 Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MSAGTSATGPRRGPPGLEEATSKKKQKDRANQESKDGDPRRVSMPRKEPTKDELLLDWRQSSDKVVVKLRVGTGPICLEEVDAAFTDTDCVVRLPDGRQWGGVFFAKIQSSCTKVQTRKGGLLQLALPKKVPLLTWPSLLKKPLGTQELVPGLRCQENGQELSPIALEPGSEPRRAKQEARNQKRAQGRGEVGSGASPGAQAGPSAKRAVHLCRGPEGEGSMDGPGPQGDAPSFLSDSATQVEAEEQLHVPPVNPQTSLLGSEKNLALLTVEKTVSPRSDSVSPVMIRNRDPEKDDHFKEEMAVGADPAALADEPESMVNLAFVKNDSYEKGPDSVVVHVYVKESRRDTSRVLFREQDFTLIFQTRDGNFLRLHPGCGPHTIFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEAPATRVGGAKVAVPTGPTPLDSTPPGGGPLPLTGQEEARAVEKEKPKARSEDSGLDGVVARTPLEHVTPKPEPHLASPKPTCMVPPMPHSPVSGDSVEEDEEEEKKVCLPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHQAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKVLPIYYFAREPHSKPIKFLVSVSKENSSASEVLESLSQSVHVKPESLRLAEVIKNRFHRVFLPSHSLDAVSPTDVLLCFELLSPELAKERVVVLEVQQRPQVPSIPISKCAACQRKQQSEDEKLKRCTRCYRVGYCNQFCQKTHWPDHKGLCRPENIGYPFLVSVPASRLTYARLAQLLEGYARYSVSVFQPPFQPGRMALESQSPGCTTLLSTSSLEAGDSEREPIQPSELQLVTPVAEGDTGAHRMWPPADRGPVPSTSGISSEMLASGPMEGCSLLAGERVSRPEAAVPGYQHSRESVSAHTPQFFIYKIDASSREQRLEDKGDTPLELGDDCSLALVWRNNERLQEFVLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRNLDLSKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPSDRSSQRSDVGWRLFDDSTVTTVDESQVVTRYAYVLFYRRRNSPVERPPRAAHAEHHPDLGPAAEAAASQASRIWQELEAEEEMVPEGPGPLGPWGPQDWVGPPPRGPTTSDEGCLRYFVLGTVAALVALVLNVFYPLVSQSRWR |
| Enzyme Length | 1357 |
| Uniprot Accession Number | Q6J1Y9 |
| Absorption | |
| Active Site | ACT_SITE 545; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 1204; /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 that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing thier ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked ubiquitin chains (By similarity). {ECO:0000250, ECO:0000269|PubMed:19015242, ECO:0000269|PubMed:19773579}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (4); Domain (3); Metal binding (8); Modified residue (2); Mutagenesis (1); Region (7); Topological domain (2); Transmembrane (1); Zinc finger (1) |
| Keywords | Direct protein sequencing;Endoplasmic reticulum;Hydrolase;Membrane;Metal-binding;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease;Transmembrane;Transmembrane helix;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | |
| Induction | INDUCTION: By streptozotocin and fasting in skeletal muscle. {ECO:0000269|PubMed:15562254}. |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19015242}; Single-pass membrane protein {ECO:0000269|PubMed:19015242}. |
| Modified Residue | MOD_RES 221; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q3UJD6; MOD_RES 283; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 150,302 |
| Kinetics | |
| Metal Binding | METAL 830; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 833; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 847; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 850; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 856; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 860; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 868; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 872; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.19.12; |