| IED ID | IndEnz0002012316 |
| Enzyme Type ID | protease012316 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 45 EC 3.4.19.12 Deubiquitinating enzyme 45 Ubiquitin thioesterase 45 Ubiquitin-specific-processing protease 45 |
| Gene Name | Usp45 |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MRVKDPSKDLPEKGKRNKRPLLPHDEDSSDDIAVGLTCQHVSYAVSVNHVKKAVAESLWSVCSECLKERRFCDGQPVLPADVWLCLKCGLQGCGKNSESQHSLRHFKSSGTESHCVVISLSTWVIWCYECNEKLSTHCNKKVLAQIVDFLQKHAFKTQTGAFSRIIKLCEEKREAGEIKKGKKGCTVPSVKGITNLGNTCFFNAVIQNLAQTYILFELMNEIKEDGTKFKISLSSAPQLEPLVVELSSPGPLTSALFLFLHSMKEAEKGPLSPKVLFNQLCQKAPRFKGFQQQDSQELLHHLLDAVRTEETKRIQASILKAFNNPTTKTADDETRKKVKAYGKEGVKMNFIDRIFIGELTSTVMCEECANISTMKDPFIDISLPIIEERVSKPVLLGKMSKCRSLQETDQDHNKGTVTVGNAHQPRASRKHSSPNDKNQLSHDRKHLRKWPSEEEKTVVTHPKNDNLEASPPASTLSTEASLNESLTDGSERDASLESSVDADSEASEPEIASKQPVLLRSRGDSCGHAEQHPHLPLASELPQAKETHGGEEEMAEAIAELHLSGTVTGNRDFHREKQPLNVPNNLCFSEGKHTRLHSAQNAFQTLSQSYVTTSKECSVQSCLYQFTSMELLMGNNKLLCEDCTEKRRKCHKETSSAEKKAGGVYTNARKQLLISAVPAILILHLKRFHQAGLSLRKVNRHVDFPLTLDLAPFCAATCKNISVGEKVLYGLYGIVEHSGSMRGGHYTAYVKVRVPSRKLSECITGRKTAAGLKEPDGELGGHWVHVSDTYVQVVPESRALSAQAYLLFYERIL |
| Enzyme Length | 813 |
| Uniprot Accession Number | Q8K387 |
| Absorption | |
| Active Site | ACT_SITE 200; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 745; /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; Evidence={ECO:0000250|UniProtKB:Q70EL2}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Catalyzes the deubiquitination of SPDL1 (By similarity). Plays a role in the repair of UV-induced DNA damage via deubiquitination of ERCC1, promoting its recruitment to DNA damage sites (By similarity). May be involved in the maintenance of photoreceptor function (PubMed:30573563). May play a role in normal retinal development (By similarity). Plays a role in cell migration (By similarity). {ECO:0000250|UniProtKB:E9QG68, ECO:0000250|UniProtKB:Q70EL2, ECO:0000269|PubMed:30573563}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (1); Chain (1); Compositional bias (3); Domain (1); Erroneous initiation (1); Metal binding (12); Modified residue (4); Region (3); Sequence conflict (1); Zinc finger (1) |
| Keywords | Alternative splicing;Cytoplasm;Hydrolase;Metal-binding;Nucleus;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Photoreceptor inner segment {ECO:0000250|UniProtKB:Q70EL2}. Cytoplasm {ECO:0000250|UniProtKB:Q70EL2}. Nucleus {ECO:0000250|UniProtKB:Q70EL2}. |
| Modified Residue | MOD_RES 28; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 29; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 507; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 525; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11217851; 12466851; 12904583; 14610273; 18799693; 7808216; |
| Motif | |
| Gene Encoded By | |
| Mass | 90,361 |
| Kinetics | |
| Metal Binding | METAL 38; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 40; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 62; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 65; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 85; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 88; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 93; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 101; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 105; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 114; /note=Zinc 3; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 127; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502; METAL 130; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00502 |
| Rhea ID | |
| Cross Reference Brenda |