Detail Information for IndEnz0002012056
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