Tag | Content |
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CPLM ID | CPLM-015609 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ubiquitin carboxyl-terminal hydrolase 34 |
Protein Synonyms/Alias | Deubiquitinating enzyme 34; Ubiquitin thioesterase 34; Ubiquitin-specific-processing protease 34 |
Gene Name | USP34 |
Gene Synonyms/Alias | KIAA0570; KIAA0729 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
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333 | AAKAQLSKQSSFASL | ubiquitination | [1] | 1423 | KAAGDHAKGLHIPRL | ubiquitination | [1, 2] | 1817 | CKTYTMDKQPLNTGE | ubiquitination | [1, 2] | 1917 | TCSHCGKKVRAEKRA | ubiquitination | [2] | 1949 | FNMVTMMKEKVNTHF | ubiquitination | [1, 2] | 1951 | MVTMMKEKVNTHFSF | ubiquitination | [1] | 2068 | TYDSVTDKFMDFSFE | ubiquitination | [1] | 2357 | ILSLAEEKYRPAALE | ubiquitination | [2] | 3202 | DEGATPIKRRRVSSD | ubiquitination | [2] |
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Reference | [1] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties. Chen Z, Zhou Y, Song J, Zhang Z. Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [ PMID: 23603789] [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW. Nature. 2013 Apr 18;496(7445):372-6. [ PMID: 23503661] |
Functional Description | 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. |
Sequence Annotation | ACT_SITE 1903 1903 Nucleophile (Probable). ACT_SITE 2164 2164 Proton acceptor (By similarity). MOD_RES 352 352 Phosphoserine. MOD_RES 649 649 Phosphoserine. MOD_RES 2488 2488 Phosphoserine. MOD_RES 2545 2545 Phosphothreonine (By similarity). MOD_RES 3358 3358 Phosphoserine. MOD_RES 3359 3359 Phosphoserine. MOD_RES 3406 3406 Phosphoserine. |
Keyword | Alternative splicing; Complete proteome; Hydrolase; Phosphoprotein; Polymorphism; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway; Wnt signaling pathway. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 3546 AA |
Protein Sequence | MRRKNSYYVW QKIFQIQFPL YTAYKHNTHP TIEDISTQES NILGAFCDMN DVEVPLHLLR 60 YVCLFCGKNG LSLMKDCFEY GTPETLPFLI AHAFITVVSN IRIWLHIPAV MQHIIPFRTY 120 VIRYLCKLSD QELRQSAARN MADLMWSTVK EPLDTTLCFD KESLDLAFKY FMSPTLTMRL 180 AGLSQITNQL HTFNDVCNNE SLVSDTETSI AKELADWLIS NNVVEHIFGP NLHIEIIKQC 240 QVILNFLAAE GRLSTQHIDC IWAAAQLKHC SRYIHDLFPS LIKNLDPVPL RHLLNLVSAL 300 EPSVHTEQTL YLASMLIKAL WNNALAAKAQ LSKQSSFASL LNTNIPIGNK KEEEELRRTA 360 PSPWSPAASP QSSDNSDTHQ SGGSDIEMDE QLINRTKHVQ QRLSDTEESM QGSSDETANS 420 GEDGSSGPGS SSGHSDGSSN EVNSSHASQS AGSPGSEVQS EDIADIEALK EEDEDDDHGH 480 NPPKSSCGTD LRNRKLESQA GICLGDSQGM SERNGTSSGT GKDLVFNTES LPSVDNRMRM 540 LDACSHSEDP EHDISGEMNA THIAQGSQES CITRTGDFLG ETIGNELFNC RQFIGPQHHH 600 HHHHHHHHHD GHMVDDMLSA DDVSCSSSQV SAKSEKNMAD FDGEESGCEE ELVQINSHAE 660 LTSHLQQHLP NLASIYHEHL SQGPVVHKHQ FNSNAVTDIN LDNVCKKGNT LLWDIVQDED 720 AVNLSEGLIN EAEKLLCSLV CWFTDRQIRM RFIEGCLENL GNNRSVVISL RLLPKLFGTF 780 QQFGSSYDTH WITMWAEKEL NMMKLFFDNL VYYIQTVREG RQKHALYSHS AEVQVRLQFL 840 TCVFSTLGSP DHFRLSLEQV DILWHCLVED SECYDDALHW FLNQVRSKDQ HAMGMETYKH 900 LFLEKMPQLK PETISMTGLN LFQHLCNLAR LATSAYDGCS NSELCGMDQF WGIALRAQSG 960 DVSRAAIQYI NSYYINGKTG LEKEQEFISK CMESLMIASS SLEQESHSSL MVIERGLLML 1020 KTHLEAFRRR FAYHLRQWQI EGTGISSHLK ALSDKQSLPL RVVCQPAGLP DKMTIEMYPS 1080 DQVADLRAEV THWYENLQKE QINQQAQLQE FGQSNRKGEF PGGLMGPVRM ISSGHELTTD 1140 YDEKALHELG FKDMQMVFVS LGAPRRERKG EGVQLPASCL PPPQKDNIPM LLLLQEPHLT 1200 TLFDLLEMLA SFKPPSGKVA VDDSESLRCE ELHLHAENLS RRVWELLMLL PTCPNMLMAF 1260 QNISDEQSND GFNWKELLKI KSAHKLLYAL EIIEALGKPN RRIRRESTGS YSDLYPDSDD 1320 SSEDQVENSK NSWSCKFVAA GGLQQLLEIF NSGILEPKEQ ESWTVWQLDC LACLLKLICQ 1380 FAVDPSDLDL AYHDVFAWSG IAESHRKRTW PGKSRKAAGD HAKGLHIPRL TEVFLVLVQG 1440 TSLIQRLMSV AYTYDNLAPR VLKAQSDHRS RHEVSHYSMW LLVSWAHCCS LVKSSLADSD 1500 HLQDWLKKLT LLIPETAVRH ESCSGLYKLS LSGLDGGDSI NRSFLLLAAS TLLKFLPDAQ 1560 ALKPIRIDDY EEEPILKPGC KEYFWLLCKL VDNIHIKDAS QTTLLDLDAL ARHLADCIRS 1620 REILDHQDGN VEDDGLTGLL RLATSVVKHK PPFKFSREGQ EFLRDIFNLL FLLPSLKDRQ 1680 QPKCKSHSSR AAAYDLLVEM VKGSVENYRL IHNWVMAQHM QSHAPYKWDY WPHEDVRAEC 1740 RFVGLTNLGA TCYLASTIQQ LYMIPEARQA VFTAKYSEDM KHKTTLLELQ KMFTYLMESE 1800 CKAYNPRPFC KTYTMDKQPL NTGEQKDMTE FFTDLITKIE EMSPELKNTV KSLFGGVITN 1860 NVVSLDCEHV SQTAEEFYTV RCQVADMKNI YESLDEVTIK DTLEGDNMYT CSHCGKKVRA 1920 EKRACFKKLP RILSFNTMRY TFNMVTMMKE KVNTHFSFPL RLDMTPYTED FLMGKSERKE 1980 GFKEVSDHSK DSESYEYDLI GVTVHTGTAD GGHYYSFIRD IVNPHAYKNN KWYLFNDAEV 2040 KPFDSAQLAS ECFGGEMTTK TYDSVTDKFM DFSFEKTHSA YMLFYKRMEP EEENGREYKF 2100 DVSSELLEWI WHDNMQFLQD KNIFEHTYFG FMWQLCSCIP STLPDPKAVS LMTAKLSTSF 2160 VLETFIHSKE KPTMLQWIEL LTKQFNNSQA ACEWFLDRMA DDDWWPMQIL IKCPNQIVRQ 2220 MFQRLCIHVI QRLRPVHAHL YLQPGMEDGS DDMDTSVEDI GGRSCVTRFV RTLLLIMEHG 2280 VKPHSKHLTE YFAFLYEFAK MGEEESQFLL SLQAISTMVH FYMGTKGPEN PQVEVLSEEE 2340 GEEEEEEEDI LSLAEEKYRP AALEKMIALV ALLVEQSRSE RHLTLSQTDM AALTGGKGFP 2400 FLFQHIRDGI NIRQTCNLIF SLCRYNNRLA EHIVSMLFTS IAKLTPEAAN PFFKLLTMLM 2460 EFAGGPPGMP PFASYILQRI WEVIEYNPSQ CLDWLAVQTP RNKLAHSWVL QNMENWVERF 2520 LLAHNYPRVR TSAAYLLVSL IPSNSFRQMF RSTRSLHIPT RDLPLSPDTT VVLHQVYNVL 2580 LGLLSRAKLY VDAAVHGTTK LVPYFSFMTY CLISKTEKLM FSTYFMDLWN LFQPKLSEPA 2640 IATNHNKQAL LSFWYNVCAD CPENIRLIVQ NPVVTKNIAF NYILADHDDQ DVVLFNRGML 2700 PAYYGILRLC CEQSPAFTRQ LASHQNIQWA FKNLTPHASQ YPGAVEELFN LMQLFIAQRP 2760 DMREEELEDI KQFKKTTISC YLRCLDGRSC WTTLISAFRI LLESDEDRLL VVFNRGLILM 2820 TESFNTLHMM YHEATACHVT GDLVELLSIF LSVLKSTRPY LQRKDVKQAL IQWQERIEFA 2880 HKLLTLLNSY SPPELRNACI DVLKELVLLS PHDFLHTLVP FLQHNHCTYH HSNIPMSLGP 2940 YFPCRENIKL IGGKSNIRPP RPELNMCLLP TMVETSKGKD DVYDRMLLDY FFSYHQFIHL 3000 LCRVAINCEK FTETLVKLSV LVAYEGLPLH LALFPKLWTE LCQTQSAMSK NCIKLLCEDP 3060 VFAEYIKCIL MDERTFLNNN IVYTFMTHFL LKVQSQVFSE ANCANLISTL ITNLISQYQN 3120 LQSDFSNRVE ISKASASLNG DLRALALLLS VHTPKQLNPA LIPTLQELLS KCRTCLQQRN 3180 SLQEQEAKER KTKDDEGATP IKRRRVSSDE EHTVDSCISD MKTETREVLT PTSTSDNETR 3240 DSSIIDPGTE QDLPSPENSS VKEYRMEVPS SFSEDMSNIR SQHAEEQSNN GRYDDCKEFK 3300 DLHCSKDSTL AEEESEFPST SISAVLSDLA DLRSCDGQAL PSQDPEVALS LSCGHSRGLF 3360 SHMQQHDILD TLCRTIESTI HVVTRISGKG NQAAS 3395 |
Gene Ontology | GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB. GO:0004221; F:ubiquitin thiolesterase activity; IDA:UniProtKB. GO:0004843; F:ubiquitin-specific protease activity; IDA:UniProtKB. GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IDA:UniProtKB. GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB. GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |