| IED ID | IndEnz0002011800 |
| Enzyme Type ID | protease011800 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 19 EC 3.4.19.12 Deubiquitinating enzyme 19 Ubiquitin thioesterase 19 Ubiquitin-specific-processing protease 19 Zinc finger MYND domain-containing protein 9 |
| Gene Name | USP19 KIAA0891 ZMYND9 |
| 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 | MSGGASATGPRRGPPGLEDTTSKKKQKDRANQESKDGDPRKETGSRYVAQAGLEPLASGDPSASASHAAGITGSRHRTRLFFPSSSGSASTPQEEQTKEGACEDPHDLLATPTPELLLDWRQSAEEVIVKLRVGVGPLQLEDVDAAFTDTDCVVRFAGGQQWGGVFYAEIKSSCAKVQTRKGSLLHLTLPKKVPMLTWPSLLVEADEQLCIPPLNSQTCLLGSEENLAPLAGEKAVPPGNDPVSPAMVRSRNPGKDDCAKEEMAVAADAATLVDEPESMVNLAFVKNDSYEKGPDSVVVHVYVKEICRDTSRVLFREQDFTLIFQTRDGNFLRLHPGCGPHTTFRWQVKLRNLIEPEQCTFCFTASRIDICLRKRQSQRWGGLEAPAARVGGAKVAVPTGPTPLDSTPPGGAPHPLTGQEEARAVEKDKSKARSEDTGLDSVATRTPMEHVTPKPETHLASPKPTCMVPPMPHSPVSGDSVEEEEEEEKKVCLPGFTGLVNLGNTCFMNSVIQSLSNTRELRDFFHDRSFEAEINYNNPLGTGGRLAIGFAVLLRALWKGTHHAFQPSKLKAIVASKASQFTGYAQHDAQEFMAFLLDGLHEDLNRIQNKPYTETVDSDGRPDEVVAEEAWQRHKMRNDSFIVDLFQGQYKSKLVCPVCAKVSITFDPFLYLPVPLPQKQKVLPVFYFAREPHSKPIKFLVSVSKENSTASEVLDSLSQSVHVKPENLRLAEVIKNRFHRVFLPSHSLDTVSPSDTLLCFELLSSELAKERVVVLEVQQRPQVPSVPISKCAACQRKQQSEDEKLKRCTRCYRVGYCNQLCQKTHWPDHKGLCRPENIGYPFLVSVPASRLTYARLAQLLEGYARYSVSVFQPPFQPGRMALESQSPGCTTLLSTGSLEAGDSERDPIQPPELQLVTPMAEGDTGLPRVWAAPDRGPVPSTSGISSEMLASGPIEVGSLPAGERVSRPEAAVPGYQHPSEAMNAHTPQFFIYKIDSSNREQRLEDKGDTPLELGDDCSLALVWRNNERLQEFVLVASKELECAEDPGSAGEAARAGHFTLDQCLNLFTRPEVLAPEEAWYCPQCKQHREASKQLLLWRLPNVLIVQLKRFSFRSFIWRDKINDLVEFPVRNLDLSKFCIGQKEEQLPSYDLYAVINHYGGMIGGHYTACARLPNDRSSQRSDVGWRLFDDSTVTTVDESQVVTRYAYVLFYRRRNSPVERPPRAGHSEHHPDLGPAAEAAASQASRIWQELEAEEEPVPEGSGPLGPWGPQDWVGPLPRGPTTPDEGCLRYFVLGTVAALVALVLNVFYPLVSQSRWR |
| Enzyme Length | 1318 |
| Uniprot Accession Number | O94966 |
| Absorption | |
| Active Site | ACT_SITE 506; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 1165; /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 their 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. {ECO:0000269|PubMed:19465887, ECO:0000269|PubMed:21849505, ECO:0000269|PubMed:22128162, ECO:0000269|PubMed:22689415}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (8); Beta strand (9); Chain (1); Compositional bias (4); Domain (3); Erroneous initiation (3); Frameshift (1); Helix (2); Metal binding (8); Modified residue (1); Natural variant (1); Region (4); Sequence conflict (3); Topological domain (2); Transmembrane (1); Turn (2); Zinc finger (1) |
| Keywords | 3D-structure;Alternative splicing;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 | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19465887}; Single-pass membrane protein {ECO:0000269|PubMed:19465887}. |
| Modified Residue | MOD_RES 244; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (4); X-ray crystallography (1) |
| Cross Reference PDB | 1WH0; 4X3G; 6K7W; 6KHV; 6KQV; |
| Mapped Pubmed ID | 18985028; 19015242; 19615732; 19875381; 21264218; 22810585; 23500468; 24356957; 25036637; 26048142; 26808260; 26988033; 27129179; 27295555; 27517492; 27827840; 28391724; 29093475; 29531792; 29901692; 30386869; 30700749; 30716094; 32236633; 33094816; 33714979; 33978709; |
| Motif | |
| Gene Encoded By | |
| Mass | 145,651 |
| Kinetics | |
| Metal Binding | METAL 791; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 794; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 808; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 811; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 817; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 821; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 829; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134; METAL 833; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00134 |
| Rhea ID | |
| Cross Reference Brenda |