Detail Information for IndEnz0002012790
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