IED ID | IndEnz0002012790 |
Enzyme Type ID | protease012790 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase 25 EC 3.4.19.12 Deubiquitinating enzyme 25 Ubiquitin thioesterase 25 Ubiquitin-specific-processing protease 25 mUSP25 |
Gene Name | Usp25 |
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 | MTVEQNVLQQSAAQKHQQTFLNQLREITGINDAQILQQALKDSNGNLELAVAFLTAKNAKTPPQEETGYYQTALPGNDRYISVGSQADANVIDLTGDDKDDLQRAIALSLAESNRAFRETGITDEEQAISRVLEASIAENKACLKRTPIEVWRDSRNPYDRKRQEKAPVGLKNVGNTCWFSAVIQSLFNLLEFRRLVLNYKPPSNAQDLPRNQKEHRNLPFMRELRYLFALLVGTKRKYVDPSRAVEILKDAFKSNDSQQQDVSEFTHKLLDWLEDAFQMKAEEETDEEKPKNPMVELFYGRFLAMGVLEGKKFENTEMFGQYPLQVNGFKDLHECLEAAMIEGEIESLHSDNSGKSGQEHWFTELPPVLTFELSRFEFNQALGRPEKIHNKLEFPQVLYLDRYMHRNREITRIKREEIKRLKDYLTVLQQRLERYLSYGSGPKRFPLVDVLQYALEFASSKPVCTSPVDDIDASSSASGPLPSQSLPSTTEQQGPCASDLPGSSSPASGAALPLRSVIHKPFTQSRIPPDLPMHPAPRHITEEELCVLESCLHRWRTEIENDTRDLQESISRIHRTIELMYSDKSMIQVPYRLHAVLVHEGQANAGHYWAYIFDHRESRWMKYNDIAVTKSSWEELVRDSFGGYRNASAYCLMYIDDKAQFLIQEEFNKETGQALVGMETLPPDLRDFVEEDNQRFEKELEEWDTQLAQRSLQEKLLAAPKLREAEASATTAQAGGADYLEQPSRSDLSKHWKEETLRVIAKASHDLEDKGPETVLQSAIKLEYSRLVKLAQEDTPPETDYRLHHVLVYFIQNQAPKKIIEKTLLEQFGDRNLSFDERCHNIMKVAQAKLEMIKPEEVNLEEYEEWHADYKKFRETTMYLITGLENFQRESYIDSLLFLLCAYQNNKELLSKGPYRGHDGELISHYRRECLLKLNEQAAELFESGEDGDVNNGLIIMNEFIVPFLPLLLVDDMEEKDILAVEDMRNRWCSYLGQEMEANLQEKLTDFLPKLLDCSTEIKGFHEPPKLPSYSAHELCERFARIMLSLSRTPADGR |
Enzyme Length | 1055 |
Uniprot Accession Number | P57080 |
Absorption | |
Active Site | ACT_SITE 178; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 608; /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 hydrolyzes ubiquitin moieties conjugated to substrates and thus, functions to process newly synthesized Ubiquitin, to recycle ubiquitin molecules or to edit polyubiquitin chains and prevents proteasomal degradation of substrates. Hydrolyzes both 'Lys-48'- and 'Lys-63'-linked tetraubiquitin chains (By similarity). {ECO:0000250}.; FUNCTION: The muscle-specific isoform (USP25m) may have a role in the regulation of muscular differentiation and function. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Compositional bias (1); Cross-link (2); Domain (4); Helix (4); Modified residue (2); Motif (1); Region (3); Sequence conflict (4) |
Keywords | 3D-structure;Alternative splicing;Coiled coil;Cytoplasm;Hydrolase;Isopeptide bond;Nucleus;Phosphoprotein;Protease;Reference proteome;Repeat;Thiol protease;Ubl conjugation;Ubl conjugation pathway |
Interact With | |
Induction | INDUCTION: Induced by type I interferons (IFNA and IFNB1) produced in response to lipopolysaccharide (LPS) and viral infection (HIV-1 and SeV viruses) (at protein level). {ECO:0000269|PubMed:27129230}. |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16501887}. Nucleus {ECO:0000269|PubMed:16501887}. Note=The longer muscle-specific isoform (USP25m) Some transient punctuate nuclear location in myotubes during myocyte development. |
Modified Residue | MOD_RES 85; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9UHP3; MOD_RES 740; /note=Phosphotyrosine; /evidence=ECO:0000250|UniProtKB:Q9UHP3 |
Post Translational Modification | PTM: Acetylated. {ECO:0000250}.; PTM: Sumoylation impairs binding to and hydrolysis of ubiquitin chains. Sumoylated preferentially with SUMO2 or SUMO3. Desumoylated by SENP1. Regulated by ubiquitination on the same residue (By similarity). {ECO:0000250}.; PTM: Preferentially monoubiquitinated but can also be polyubiquitinated. Autodeubiquitinated. Ubiquitination activates the enzymatic activity either by preventing sumoylation or by allowing novel interactions (By similarity). {ECO:0000250}.; PTM: Phosphorylation in the C-terminal by SYK regulates USP25 cellular levels. {ECO:0000250}. |
Signal Peptide | |
Structure 3D | NMR spectroscopy (1) |
Cross Reference PDB | 1VDL; |
Mapped Pubmed ID | 11217851; 12466851; 12466854; 12466855; 12520002; 16141072; 16602821; 21267068; 21677750; 23042150; 23453926; 23674823; 25313962; 26305951; 26811477; 29773651; 30886164; 33523861; |
Motif | MOTIF 89..95; /note=Required for SUMO paralog-specific binding |
Gene Encoded By | |
Mass | 121,420 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |