| IED ID | IndEnz0002011084 |
| Enzyme Type ID | protease011084 |
| Protein Name |
Ubiquitin carboxyl-terminal hydrolase 34 EC 3.4.19.12 Deubiquitinating enzyme 34 Ubiquitin thioesterase 34 Ubiquitin-specific-processing protease 34 |
| Gene Name | Usp34 Kiaa0570 Murr2 |
| 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 | MCENCADLVEVLNEISDIEGGDGLQLRKEHTLKIFAYINSWTQRQCLCCFKEYKHLEIFNQVVCALINLVIAQVQVLRDQLCKHCTTINIDSTWQDESNQAEEPLSIDRECNEGNTERQKSIEKKSNSTRTCNLTEEESSKSSDPFSLWNTDEKEKLLLCVAKIFQIQFPLYTAYKHNTHPTIEDISTQESNILGAFCDMNDVEVPLHLLRYVCLFCGKNGLSLMKDCFEYGTPETLPFLIAHAFITVVSNIRIWLHIPAVMQHIIPFRTYVIRYLCKLSDQELRQSAARNMADLMWSTVKEPLDTTLCFDKESLDLAFKYFMSPTLTMRLAGLSQITNQLHTFNDVCNNESLVSDTETSIAKELADWLISNNVVEHIFGPNLHIEIIKQCQVILNFLAAEGRLSTQHIDCIWAAAQLKHCSRYIHDLFPSLIKNLDPVPLRHLLNLVSALEPGVHTEQTLYLASMLIKALWNNALAAKAQLSKQSSFASLLNTNMPIGNKKEEEELRRAAPSPWSPAASPQSSDNSDTHQSGASDIEMDEQLINRNKHVQQRLSDTEESMQGSSDETANSGEDGSSGPGSSSGHSDGSSNEVNSSHASQSAGSPGSEVQSEDIADIEALKEEEEEEEEEEEEEEEEDDEEEEDEEEDDDDDDDHGHNPAKNTCGTELRNRKLENPAGICLGESQGTSERNGTNSGTGKDLVFNTEPLPSVDNRIRMLDACAHSEDPEHGISGEVSSAHLAQGSQEACITRSGDFLGETIGNELFNCRQFIGPQHHHHHHHHHHHHHHHHHHHHHHHDGHMVDDMLSADDVSCSSSQVSAKSEKNMADFDGEESGCEEELVQINSHAELTSHLQQHLPNLASIYHEHLSQGPAVHKHQFSSNAVTDINLDNVCKKGNTLLWDIVQDDDAINLSEGLINEAEKLLCSLVCWFTDRQIRMRFIEGCLENLGNNRSVVISLRLLPKLFGTFQQFGSSYDTHWITMWAEKELNMMKLFFDNLVYYIQGIREGRQKHALYSHSAEVQVRLQFLTCVFSTLGSPDHFRLSLEQVDILWHCLVEDSECYDDALHWFLNQVRSKDQHAMGMETYKHLFLEKMPQLKPETISMTGLNLFQHLCNLARLATSAYDGGSNSELCGMDQFWGIALRAQSGDVSRAAIQYINSYYINGKTGLEKEQEFISKCMESLMIASSSLEQESHSSLTVIERGLLMLKTHLEAFRRRFAYHLRQWQIEGTGISSHLKALSDKQSLPLRVVCQPAGLPDKMTIEMYPSDQVADLRAEVTHWYENLQKEQINQQAQLQEFGQSSRKGEFPGGLMGPVRMISSGHELTTDYDEKALHELGFKDMQMVFVSLGAPRRERKGEGVQLPASCLPPPQKDNIPMLLLLQEPHLTTLFDLLEMLASFKPPSGKVAVDDSESLKCEELHLHAENLSRRVWELLMLLPTCPNMLTAFQNVSDEQSNDGLNWKELLKIKSAHKLLYALEIIEALGKPNRRIRRESTGSYSDLYPDSDDSSEDQVENSKNSWTCKFVAAGGLQQLLEIFNSAILEPKEQESWTVWQLDCLACLLKLICQFAVDPSDLDLAYHDVFAWSGIAESHRKRTWPGKSRKAAGDHAKSLHIPRLTEVFLVLVQGTSLIQRLMSVAYTYDNLAPRVLKAQSDHRSRHEVSHYSMWLLVSWAHCCSLVKSSLADSDHLQDWLKQLTLLIPETAVRHESCNGLYKLSLSGLDGGDSIHRSFLLLAASTLLKFLPDAQALKPPRIDDYEEEPLLKPGCKEYFWLLCKLVDNIHIKDASQTTLLDLDALARHLADCIRSREILDHLDGSIEDDGLSGLLRLATSVIKHKPPFKFSREGQEFLRDIFNLLFLLPSLKDRRQPKCKSHSCRAAAYDLLVEMVKGSVENYRLIHNWVMAQHMQSHAPYKWDYWPHEDVRAECRFVGLTNLGATCYLASTIQQLYMIPEARQAVFTAKYSEDMKHKTTLLELQKMFTYLMESECKAYNPRPFCKTYTMDKQPLNTGEQKDMTEFFTDLITKVEEMSPELKNTVKSLFGGVITNNVVSLDCEHVSQTAEEFYTVRCQVADMKNIYESLDEVTIKDTLEGDNMYTCSHCGKKVRAEKRACFKKLPRILSFNTMRYTFNMVTMMKEKVNTHFSFPLRLDMTPYTEDFLMGKSDRKEGFKDVGDRSKDTESYEYDLIGVTVHTGTADGGHYYSFIRDIVNPHAYKNNKWYLFNDAEVKPFDSAQLASECFGGEMTTKTYDSVTDKFMDFSFEKTHSAYMLFYKRMEPEEENGREYKFDVSSELLEWIWHDNMQFLQDKNIFEHTYFGFMWQLCSCIPSTLPDPKAVSLMTAKLSTSFVLETFIHSKEKPTMLQWIELLTKQFNNSQAACEWFLDRMADDDWWPMQILIKCPNQIVRQMFQRLCIHVIQRLRPVHAHLYLQPGMEDGSDDMDASVEDIGGRSCVTRFVRTLLLIMEHGVKPHSKHLTEYFAFLYEFAKMGEEESQFLLSLQAISTMVHFYMGTKGPENPQVEVLSEEEGEEEEEEEDILSLAEEKYRPAALEKMIALVALLVEQSRSERHLTLSQTDMAALTGGKGFPFLFQHIRDGINIRQTCNLIFSLCRYNNRLAEHIVSMLFTSIAKLTPEAANPFFKLLTMLMEFAGGPPGMPPFASYILQRIWEVIEYNPSQCLDWLAVQTPRNKLAHSWVLQNMENWVERFLLAHNYPRVRTSAAYLLVSLIPSNSFRQMFRSTRSLHIPTRDLPLSPDTTVVLHQVYNVLLGLLSRAKLYVDAAVHGTTKLVPYLSFMTYCLISKTEKLMFSTYFMDLWNLFQPKLSEPAIATNHNKQALLSFWYNVCADCPENIRLIVQNPVVTKNIAFNYILADHDDQDVVLFNRGMLPAYYGILRLCCEQSPAFTRQLASHQNIQWAFKNLTPHASQYPGAVEELFNLMQLFIAQRPDMREEELEDIKQFKKTTISCYLRCLDGRSCWTTLISAFRILLESDEDRLLVVFNRGLILMTESFNTLHMMYHEATACHVTGDLVELLSIFLSVLKSTRPYLQRKDVKQALIQWQERIEFAHKLLTLLNSYSPPELRNACIDVLKELVLLSPHDFLHTLVPFLQHNHCTYHHSNIPMSLGPYFPCRENIKLIGGKSNIRPPRPELNMCLLPTMVETSKGKDDVYDRMLLDYFFSYHQFIHLLCRVAINCEKFTETLVKLSVLVAYEGLPLHLALFPKLWTELCQTQSAMSKNCIKLLCEDPVFAEYIKCILMDERTFLNNNIVYTFMTHFLLKVQSQVFSEANCASLISTLITNLINQYQNLQSDFTNRVEISKASAALNGDLRALALLLSVHTPKQLNPALIPTLQELLNKCRTCLQQRNSLQEQEAKERKTKDDEGATPVKRRRVSSDEEHTVDSCIGDIKTETREVLTPTSTSDNETRDSSIIDPGTEQDLPSPENSSVKEYRMEGPSSFSEDGSHIRSQHAEEQSNNGRFDDCKEFKDHCSKDTTLAEDESEFPSTSISAVLSDLADLRSCDGQALSSQDPEAAVSLSCGHSRGLISHMQQHDILDTLCRTIESTIHVVTRISGKGNQAAS |
| Enzyme Length | 3582 |
| Uniprot Accession Number | Q6ZQ93 |
| Absorption | |
| Active Site | ACT_SITE 1940; /note="Nucleophile"; /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093"; ACT_SITE 2201; /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:Q70CQ2}; |
| DNA Binding | |
| EC Number | 3.4.19.12 |
| Enzyme Function | FUNCTION: Ubiquitin hydrolase that can remove conjugated ubiquitin from AXIN1 and AXIN2, thereby acting as a regulator of Wnt signaling pathway. Acts as an activator of the Wnt signaling pathway downstream of the beta-catenin destruction complex by deubiquitinating and stabilizing AXIN1 and AXIN2, leading to promote nuclear accumulation of AXIN1 and AXIN2 and positively regulate beta-catenin (CTNBB1)-mediated transcription. Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. {ECO:0000250|UniProtKB:Q70CQ2}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Alternative sequence (4); Chain (1); Compositional bias (8); Domain (1); Erroneous initiation (1); Modified residue (12); Region (6); Sequence caution (1); Sequence conflict (1) |
| Keywords | Alternative splicing;Hydrolase;Phosphoprotein;Protease;Reference proteome;Thiol protease;Ubl conjugation pathway;Wnt signaling pathway |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | MOD_RES 352; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q70CQ2"; MOD_RES 486; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 487; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 490; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 1506; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 2525; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:21183079"; MOD_RES 3395; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 3396; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 3418; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 3423; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q70CQ2"; MOD_RES 3443; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 3539; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q70CQ2" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 12520002; 12904583; 14610273; 17967808; 18799693; 21677750; 26273529; 26811477; 30181118; 32212276; |
| Motif | |
| Gene Encoded By | |
| Mass | 408,214 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |