IED ID | IndEnz0002012056 |
Enzyme Type ID | protease012056 |
Protein Name |
Ubiquitin carboxyl-terminal hydrolase 24 EC 3.4.19.12 Deubiquitinating enzyme 24 Ubiquitin thioesterase 24 Ubiquitin-specific-processing protease 24 |
Gene Name | Usp24 |
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 | MESEEEQHMTTLLCMGFSDPATIRKALRLAKNDINEAVALLTNERPGLDYGGYEPMDSGGPSPGPGGGPRGDSGSDGSGPSRGGSTGGGGGFDPPPAYHEVVDAEKNDENGNCSGEGIEFPTTNLYELESRVLTDHWSIPYKREESLGKCLLASTYLARLGLSESDENCKRFMERCMPEAFKKLLTSSAVHKWGTEIHEGIYNMLMLLIELVAERMKQDPIPIGLLGVLTMAFNPDNEYHFKNRMKVSQRNWAEVFGEGNMFAISPVSTFQKEPHGWVVDLVNKFGELGGFAAIQAKLHSEDIELGAVSALVQPLGVCAEYLNSSVVQPMLDPVILTTIQDVRSVEEKDLKDKRLVSIPELLSAIKLLCMRFQPALVTTVDALRLDILLRMLKSPHFSAKMNSLKEVTKLIEDSTLSKSVKNAIDTDRLLDWLVENSVLSIALEGNIDQAQYCDRIKGIIELLGSKLSLDELTKIWKIQSGQSSTVIENIHTIIAAAAVKFNADQLNHLFVLIQKSWETESDRVRQKLLSLIGRIGREARFEATSGKVLDVLWELAHLPTLPSSLIQQALEEHLTILSDAYAVKEAVKRSYIIKCIEDIKRPGEWSSLEKNKKDGFKSSQLNNPQFVWVVPALRQLHEITRSFIKQTYQKQDKSIIQDLKKNFEIVKLVTGSLLACHRLAAAVAGPGGLTGLTLVDGRYTYREYLEAHLKFLAFFLQEATLYLGWNRAKEIWECLVTGQDVCELDREMCFEWFTKGQHDLESDVQQQLFKEKILKLESYEITMNGFNLFKTFFENVNLCDHRLKRQGAQLYVEKLELVGMDFIWKIAMESPDEEIANEAIQLIINYSYINLNPRLKKDSVSLHKKFIADCYTRLEAASSALGGPTLTHAVTRATKMLTATAMPTVATSVQSPYRSTKLVIIERLLLLAERYVITIEDFYSVPRTILPHGASFHGHLLTLNVTYESTKDTFTVEAHSNETIGSVRWKIAKQLCSPVDNIQIFTNDSLLTVNKDQKLLHQLGFSDEQVLTVKTSGSGTPSGSSADSSTSSSSSSSGAFSSSYAMEQEKSLPGVVMALVCNVFDMLYQLANLEEPRITLRVRKLLLLIPTDPAIQEALDQLDSLGRKKTLLSETSSQSSKSPSLSSKQQHQPSASSILESLFRSFAPGMSTFRVLYNLEVLSSKLMPTADDDMARSCAKSFCENFLKAGGLSLVVNVMQRDSIPSEVDYETRQGVYSICLQLARFLLVGQTMPTSLDEDLTKDGIEALSSRPFRNVSRQTSRQMSLCGTPEKSSYRQLSVSDRSSIRVEEIIPAARVAIQTMEASDFTATVACFMRLSWAAAAGRLDLVGSSQPIKESNSLFPAGIRSRLSSSGSNCSSSSEGEPAALHAGICVRQQSVSTKDALIAGEALSLLVTCLQLRSQQLASFYSLPCVADFIIDILLGSPSAEIRRVACDQLYTLSQTDTSAHPEVQKPNQFLLGVILTAQLPLWSPTSIMRGVNQRLLSQCMEYFDLRCQLLDDLTTSEMDQLRISPATMLEDEITWLDNFEPNRTADCETSEADNILLAGHLRLIKTLLSLCGAEKEMLGSSLIKPLLDDFLFRASRIIVNSHSPASSAAISQQDFHPKCSTVNSRLAAYEVLVMLADSSPSNLQIITKELLSMHHQPDPALTKEFDYLPPVDSRSSSGFVGLRNGGATCYMNAVFQQLYMQPGLPESLLSVDDDTDNPDDSVFYQVQSLFGHLMESKLQYYVPENFWKIFKMWNKELYVREQQDAYEFFTSLIDQMDEYLKKMGREQIFKNTFQGIYSDQKICKDCPHRYEREEAFMALNLGVTSCQSLEISLDQFVRGEVLEGSNAYYCEKCKEKRITVKRTCIKSLPSVLVIHLMRFGFDWESGRSIKYDEQIRFPWMLNMEPYTVAGMARQDSSSEVGENGRNMDQGGGGSPRKKVALTENYELVGVIVHSGQAHAGHYYSFIKDRRGCGKGKWYKFNDTVIEEFDLNDETLEYECFGGEYRPKVYDQTNPYTDVRRRYWNAYMLFYQRVSDQNSPVLPKKSRVSVVRQEAEDLSLSAPSSPEISPQSSPRPHRPNNDRLSILTKLVKKGEKKGLFVEKMPARIYQMVRDENLKFMKNRDVYSSDYFSFVLSLASLNATKLKHPYYPCMAKVSLQLAIQFLFQTYLRTKKKLRVDTEEWIATIEALLSKSLDACQWLVEYFISSEGRELVKVFLLECSVREVRVAVATILEKTLDSALFYQDKLKSLHQLLEVLLALLDKDVPENCKNCAQYFSLFNTFVQKQGIRAGDLLLRHSALRHMISFLLGVSRQNSQIRRWSSAQAREFGNLHNTVALLVLHSDVSSQRNVAPGIFKQRPPISVAPSSPLLPLHEEVEALLFLSEGKPYLLEVMFALRELTGSLLALMEMVVYCCFCNEHFSFTMLHFIKNQLETAPPHELKNTFQLLHEVLVIEDPIQVERVKFVFETENGLLALMHHSNHVDSSRCYQCVKFLVTLAQKCPAAKEYFKENSHHWSWAVQWLQKKMSEHYWTPQSNVSNETSTGKTFQRTISAQDTLAYATALLNEKEQSGSSNGSESSPANENGERHLQQGSESPMMIGELRSDLDDVDP |
Enzyme Length | 2617 |
Uniprot Accession Number | B1AY13 |
Absorption | |
Active Site | ACT_SITE 1695; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 1967; /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: Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Deubiquitinates DDB2, preventing its proteasomal degradation (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Alternative sequence (2); Chain (1); Compositional bias (1); Domain (2); Modified residue (11); Region (6) |
Keywords | Alternative splicing;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9UPU5"; MOD_RES 85; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9UPU5"; MOD_RES 939; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:17947660"; MOD_RES 1138; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1282; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9UPU5"; MOD_RES 1940; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 2044; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"; MOD_RES 2074; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:17242355"; MOD_RES 2558; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q9UPU5"; MOD_RES 2562; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 2601; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079" |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10725249; 11217851; 12466851; 12520002; 14610273; 18799693; 21267068; 21677750; 24855944; 26811477; 33355202; |
Motif | |
Gene Encoded By | |
Mass | 294,001 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |