CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015608
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
484AAKAQLSKQSSFASLubiquitination[1]
858NLDNVCKKGNTLLWDubiquitination[2]
1039FLNQVRSKDQHAMGMubiquitination[2]
1134NGKTGLEKEQEFISKubiquitination[3]
1206HLKALSDKQSLPLRVubiquitination[2, 4]
1564RKRTWPGKSRKAAGDubiquitination[2]
1567TWPGKSRKAAGDHAKubiquitination[3]
1574KAAGDHAKGLHIPRLubiquitination[1, 2, 3, 4, 5]
1968CKTYTMDKQPLNTGEubiquitination[1, 2, 3, 4, 5]
2068TCSHCGKKVRAEKRAubiquitination[5]
2100FNMVTMMKEKVNTHFubiquitination[1, 2, 3, 5, 6, 7, 8]
2102MVTMMKEKVNTHFSFubiquitination[1, 2, 4]
2126TEDFLMGKSERKEGFubiquitination[2]
2219TYDSVTDKFMDFSFEubiquitination[1, 2, 3]
2508ILSLAEEKYRPAALEubiquitination[3]
3100FPCRENIKLIGGKSNubiquitination[2, 3, 4]
3322TLQELLSKCRTCLQQubiquitination[2]
3339SLQEQEAKERKTKDDacetylation[9]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [9] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786
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
MCENCADLVE VLNEISDVEG GDGLQLRKEH TLKIFTYINS WTQRQCLCCF KEYKHLEIFN 60
QVVCALINLV IAQVQVLRDQ LCKHCTTINI DSTWQDESNQ AEEPLNIDRE CNEGSTERQK 120
SIEKKSNSTR ICNLTEEESS KSSDPFSLWS TDEKEKLLLC VAKIFQIQFP LYTAYKHNTH 180
PTIEDISTQE SNILGAFCDM NDVEVPLHLL RYVCLFCGKN GLSLMKDCFE YGTPETLPFL 240
IAHAFITVVS NIRIWLHIPA VMQHIIPFRT YVIRYLCKLS DQELRQSAAR NMADLMWSTV 300
KEPLDTTLCF DKESLDLAFK YFMSPTLTMR LAGLSQITNQ LHTFNDVCNN ESLVSDTETS 360
IAKELADWLI SNNVVEHIFG PNLHIEIIKQ CQVILNFLAA EGRLSTQHID CIWAAAQLKH 420
CSRYIHDLFP SLIKNLDPVP LRHLLNLVSA LEPSVHTEQT LYLASMLIKA LWNNALAAKA 480
QLSKQSSFAS LLNTNIPIGN KKEEEELRRT APSPWSPAAS PQSSDNSDTH QSGGSDIEMD 540
EQLINRTKHV QQRLSDTEES MQGSSDETAN SGEDGSSGPG SSSGHSDGSS NEVNSSHASQ 600
SAGSPGSEVQ SEDIADIEAL KEEDEDDDHG HNPPKSSCGT DLRNRKLESQ AGICLGDSQG 660
MSERNGTSSG TGKDLVFNTE SLPSVDNRMR MLDACSHSED PEHDISGEMN ATHIAQGSQE 720
SCITRTGDFL GETIGNELFN CRQFIGPQHH HHHHHHHHHH DGHMVDDMLS ADDVSCSSSQ 780
VSAKSEKNMA DFDGEESGCE EELVQINSHA ELTSHLQQHL PNLASIYHEH LSQGPVVHKH 840
QFNSNAVTDI NLDNVCKKGN TLLWDIVQDE DAVNLSEGLI NEAEKLLCSL VCWFTDRQIR 900
MRFIEGCLEN LGNNRSVVIS LRLLPKLFGT FQQFGSSYDT HWITMWAEKE LNMMKLFFDN 960
LVYYIQTVRE GRQKHALYSH SAEVQVRLQF LTCVFSTLGS PDHFRLSLEQ VDILWHCLVE 1020
DSECYDDALH WFLNQVRSKD QHAMGMETYK HLFLEKMPQL KPETISMTGL NLFQHLCNLA 1080
RLATSAYDGC SNSELCGMDQ FWGIALRAQS GDVSRAAIQY INSYYINGKT GLEKEQEFIS 1140
KCMESLMIAS SSLEQESHSS LMVIERGLLM LKTHLEAFRR RFAYHLRQWQ IEGTGISSHL 1200
KALSDKQSLP LRVVCQPAGL PDKMTIEMYP SDQVADLRAE VTHWYENLQK EQINQQAQLQ 1260
EFGQSNRKGE FPGGLMGPVR MISSGHELTT DYDEKALHEL GFKDMQMVFV SLGAPRRERK 1320
GEGVQLPASC LPPPQKDNIP MLLLLQEPHL TTLFDLLEML ASFKPPSGKV AVDDSESLRC 1380
EELHLHAENL SRRVWELLML LPTCPNMLMA FQNISDEQSN DGFNWKELLK IKSAHKLLYA 1440
LEIIEALGKP NRRIRRESTG SYSDLYPDSD DSSEDQVENS KNSWSCKFVA AGGLQQLLEI 1500
FNSGILEPKE QESWTVWQLD CLACLLKLIC QFAVDPSDLD LAYHDVFAWS GIAESHRKRT 1560
WPGKSRKAAG DHAKGLHIPR LTEVFLVLVQ GTSLIQRLMS VAYTYDNLAP RVLKAQSDHR 1620
SRHEVSHYSM WLLVSWAHCC SLVKSSLADS DHLQDWLKKL TLLIPETAVR HESCSGLYKL 1680
SLSGLDGGDS INRSFLLLAA STLLKFLPDA QALKPIRIDD YEEEPILKPG CKEYFWLLCK 1740
LVDNIHIKDA SQTTLLDLDA LARHLADCIR SREILDHQDG NVEDDGLTGL LRLATSVVKH 1800
KPPFKFSREG QEFLRDIFNL LFLLPSLKDR QQPKCKSHSS RAAAYDLLVE MVKGSVENYR 1860
LIHNWVMAQH MQSHAPYKWD YWPHEDVRAE CRFVGLTNLG ATCYLASTIQ QLYMIPEARQ 1920
AVFTAKYSED MKHKTTLLEL QKMFTYLMES ECKAYNPRPF CKTYTMDKQP LNTGEQKDMT 1980
EFFTDLITKI EEMSPELKNT VKSLFGGVIT NNVVSLDCEH VSQTAEEFYT VRCQVADMKN 2040
IYESLDEVTI KDTLEGDNMY TCSHCGKKVR AEKRACFKKL PRILSFNTMR YTFNMVTMMK 2100
EKVNTHFSFP LRLDMTPYTE DFLMGKSERK EGFKEVSDHS KDSESYEYDL IGVTVHTGTA 2160
DGGHYYSFIR DIVNPHAYKN NKWYLFNDAE VKPFDSAQLA SECFGGEMTT KTYDSVTDKF 2220
MDFSFEKTHS AYMLFYKRME PEEENGREYK FDVSSELLEW IWHDNMQFLQ DKNIFEHTYF 2280
GFMWQLCSCI PSTLPDPKAV SLMTAKLSTS FVLETFIHSK EKPTMLQWIE LLTKQFNNSQ 2340
AACEWFLDRM ADDDWWPMQI LIKCPNQIVR QMFQRLCIHV IQRLRPVHAH LYLQPGMEDG 2400
SDDMDTSVED IGGRSCVTRF VRTLLLIMEH GVKPHSKHLT EYFAFLYEFA KMGEEESQFL 2460
LSLQAISTMV HFYMGTKGPE NPQVEVLSEE EGEEEEEEED ILSLAEEKYR PAALEKMIAL 2520
VALLVEQSRS ERHLTLSQTD MAALTGGKGF PFLFQHIRDG INIRQTCNLI FSLCRYNNRL 2580
AEHIVSMLFT SIAKLTPEAA NPFFKLLTML MEFAGGPPGM PPFASYILQR IWEVIEYNPS 2640
QCLDWLAVQT PRNKLAHSWV LQNMENWVER FLLAHNYPRV RTSAAYLLVS LIPSNSFRQM 2700
FRSTRSLHIP TRDLPLSPDT TVVLHQVYNV LLGLLSRAKL YVDAAVHGTT KLVPYFSFMT 2760
YCLISKTEKL MFSTYFMDLW NLFQPKLSEP AIATNHNKQA LLSFWYNVCA DCPENIRLIV 2820
QNPVVTKNIA FNYILADHDD QDVVLFNRGM LPAYYGILRL CCEQSPAFTR QLASHQNIQW 2880
AFKNLTPHAS QYPGAVEELF NLMQLFIAQR PDMREEELED IKQFKKTTIS CYLRCLDGRS 2940
CWTTLISAFR ILLESDEDRL LVVFNRGLIL MTESFNTLHM MYHEATACHV TGDLVELLSI 3000
FLSVLKSTRP YLQRKDVKQA LIQWQERIEF AHKLLTLLNS YSPPELRNAC IDVLKELVLL 3060
SPHDFLHTLV PFLQHNHCTY HHSNIPMSLG PYFPCRENIK LIGGKSNIRP PRPELNMCLL 3120
PTMVETSKGK DDVYDRMLLD YFFSYHQFIH LLCRVAINCE KFTETLVKLS VLVAYEGLPL 3180
HLALFPKLWT ELCQTQSAMS KNCIKLLCED PVFAEYIKCI LMDERTFLNN NIVYTFMTHF 3240
LLKVQSQVFS EANCANLIST LITNLISQYQ NLQSDFSNRV EISKASASLN GDLRALALLL 3300
SVHTPKQLNP ALIPTLQELL SKCRTCLQQR NSLQEQEAKE RKTKDDEGAT PIKRRRVSSD 3360
EEHTVDSCIS DMKTETREVL TPTSTSDNET RDSSIIDPGT EQDLPSPENS SVKEYRMEVP 3420
SSFSEDMSNI RSQHAEEQSN NGRYDDCKEF KDLHCSKDST LAEEESEFPS TSISAVLSDL 3480
ADLRSCDGQA LPSQDPEVAL SLSCGHSRGL FSHMQQHDIL DTLCRTIEST IHVVTRISGK 3540
GNQAAS 3546 
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
 IPR016024; ARM-type_fold.
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19. 
Pfam
 PF00443; UCH 
SMART
  
PROSITE
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3 
PRINTS