| IED ID | IndEnz0002011129 |
| Enzyme Type ID | protease011129 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 4 EC 3.4.19.12 Deubiquitinating enzyme 4 Ubiquitin thioesterase 4 Ubiquitin-specific-processing protease 4 |
| Gene Name | Usp4 |
| 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 | MAEGRGTHERPDVETQKTELGALMGTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTIQDAGLYQGQVLVIEPQNEDGTWPRQTLQSKSSTAPSRNFTTSSKPSASPYSSMSASLIANGDSTNSSGMHNSGVSRGGAGFSASYNCQEPPSPHIQPGLCGLGNLGNTCFMNSALQCLSNTGPLTEYFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDTHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFILDGLHEDLNRVKKKPYLEPKDANGRPDAVVAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRIMEVFLVPADPHCRPIQYRVTVPLMGAISDLCEALSKLSGIAAENMVVTDVYNHRFHKIFQMDEGLSHITPRDDIFVYEICTTPMDGSEYITLPVYFREKKSRPSSTSSGAVLYGQPLLVSVPKHRLTLESLYQAVCERISRYIKQPLPEEFLSSPLEPGACNGSRGSYEGDEEEMDHQEEGKEQLSEVEESGEDSQGGDPTETTQKAKGPPRHKRLFTFSLVNSCGTADINSLATDGKLLKLNSRSTLAIDWDSETRSLYFDEQESEACEKHTSMSQPQKKKKAAIALRECIELFTTMETLGEHDPWYCPTCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPVRALNMSEFVCDRAARPYVYDLIAVSNHYGAMGVGHYTAYAKNRLNGKWYYFDDSSVSLASEDQIVTKAAYVLFYQRRDDECPSTSSPVSFPGSDGGAKLSSSQQDLGEEEAYTMDTN |
| Enzyme Length | 961 |
| Uniprot Accession Number | B2GUZ1 |
| Absorption | |
| Active Site | ACT_SITE 311; /evidence=ECO:0000255|PROSITE-ProRule:PRU01035; ACT_SITE 879; /evidence=ECO:0000255|PROSITE-ProRule:PRU01035 |
| Activity Regulation | ACTIVITY REGULATION: The completion of the deubiquitinase reaction is mediated by the DUSP and ubiquitin-like 1 domains which promotes the release of ubiquitin from the catalytic site enabling subsequent reactions to occur. {ECO:0000250|UniProtKB:Q13107}. |
| 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:0000250|UniProtKB:Q13107}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins. Deubiquitinates PDPK1. Deubiquitinates TRIM21. Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface. May regulate mRNA splicing through deubiquitination of the U4 spliceosomal protein PRPF3. This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP. May also play a role in the regulation of quality control in the ER. {ECO:0000250|UniProtKB:Q13107}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Compositional bias (1); Domain (4); Metal binding (4); Modified residue (3); Motif (2); Region (9) |
| Keywords | Cytoplasm;Hydrolase;Metal-binding;Nucleus;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation;Ubl conjugation pathway;Zinc |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Nucleus {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. Note=Shuttles between the nucleus and cytoplasm. Exported to the cytoplasm in a CRM1-dependent manner and recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The relative amounts found in the nucleus and cytoplasm vary according to the cell type. {ECO:0000250|UniProtKB:P35123, ECO:0000250|UniProtKB:Q13107}. |
| Modified Residue | MOD_RES 655; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 674; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 679; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:P35123 |
| Post Translational Modification | PTM: Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated. {ECO:0000250|UniProtKB:Q13107}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 27114249; 28755289; |
| Motif | MOTIF 133..141; /note=Nuclear export signal; /evidence=ECO:0000250|UniProtKB:P35123; MOTIF 765..770; /note=Nuclear localization signal; /evidence=ECO:0000250|UniProtKB:P35123 |
| Gene Encoded By | |
| Mass | 108,373 |
| Kinetics | |
| Metal Binding | METAL 461; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q13107; METAL 464; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q13107; METAL 797; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q13107; METAL 800; /note=Zinc; /evidence=ECO:0000250|UniProtKB:Q13107 |
| Rhea ID | |
| Cross Reference Brenda |