| IED ID | IndEnz0002013318 |
| Enzyme Type ID | protease013318 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 17 USP17 EC 3.4.19.12 Deubiquitinating enzyme 17-like protein 2 Deubiquitinating protein 3 DUB-3 Ubiquitin carboxyl-terminal hydrolase 17-like protein 2 Ubiquitin thioesterase 17-like protein 2 Ubiquitin-specific-processing protease 17-like protein 2 |
| Gene Name | USP17L2 DUB3 USP17 USP17H USP17I USP17J USP17K USP17L USP17M |
| 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 | MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSSEARVDLCDDLAPVARQLAPRKKLPLSSRRPAAVGAGLQNMGNTCYENASLQCLTYTPPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKLAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEGQWYKMDDAKVTACSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDERLVERATQESTLDHWKFPQEQNKTKPEFNVRKVEGTLPPNVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTTRTDQESVNTGTLASLQGRTRRSKGKNKHSKRALLVCQ |
| Enzyme Length | 530 |
| Uniprot Accession Number | Q6R6M4 |
| Absorption | |
| Active Site | ACT_SITE 89; /note=Nucleophile; ACT_SITE 334; /note=Proton acceptor; /evidence=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; Evidence={ECO:0000269|PubMed:14699124, ECO:0000269|PubMed:20228808, ECO:0000269|PubMed:20368735}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Regulates cell proliferation by deubiquitinating and inhibiting RCE1 thereby controlling the small GTPases NRAS and HRAS localization and activation. In parallel, mediates deubiquitination of CDC25A, preventing CDC25A degradation by the proteasome during the G1/S and G2/M phases promoting cell-cycle progression. Also regulates cell proliferation and apoptosis through deubiquitination of SUDS3 a regulator of histone deacetylation. Through activation of the Rho family GTPases RAC1A, CDC42 and RHOA, regulates cell migration. Through the cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains of the cytoplasmic innate immune receptors DDX58 and IFIH1 stimulates the cellular response to viral infection. {ECO:0000269|PubMed:14699124, ECO:0000269|PubMed:17109758, ECO:0000269|PubMed:19188362, ECO:0000269|PubMed:20147298, ECO:0000269|PubMed:20228808, ECO:0000269|PubMed:20368735, ECO:0000269|PubMed:20388806, ECO:0000269|PubMed:21239494, ECO:0000269|PubMed:21448158}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Domain (1); Mutagenesis (1); Natural variant (1); Region (3); Sequence conflict (13) |
| Keywords | Apoptosis;Cell cycle;Endoplasmic reticulum;Hydrolase;Nucleus;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
| Interact With | |
| Induction | INDUCTION: Up-regulated by IL4/interleukin-4, IL6/interleukin-6 and chemokines including CXCL8 and CXCL12 (at protein level). Up-regulated during the G1/S transition of the cell cycle. {ECO:0000269|PubMed:14699124, ECO:0000269|PubMed:20388806, ECO:0000269|PubMed:21448158}. |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21239494}. Endoplasmic reticulum {ECO:0000269|PubMed:19188362}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 19615732; 19718026; 23773437; 24704006; 25776484; 26617781; 28061504; 28067227; 28198361; 28288134; 30057199; 30628680; 30718431; 30778200; 30935108; |
| Motif | |
| Gene Encoded By | |
| Mass | 59,619 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |