CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015532
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; Murr2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1076FLNQVRSKDQHAMGMubiquitination[1]
1243HLKALSDKQSLPLRVubiquitination[1]
2256TYDSVTDKFMDFSFEubiquitination[1, 2]
3137FPCRENIKLIGGKSNubiquitination[1, 2]
Reference
 [1] 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]
 [2] 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] 
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 (By similarity). 
Sequence Annotation
 ACT_SITE 1940 1940 Nucleophile (By similarity).
 ACT_SITE 2201 2201 Proton acceptor (By similarity).
 MOD_RES 352 352 Phosphoserine (By similarity).
 MOD_RES 2525 2525 Phosphoserine.
 MOD_RES 2582 2582 Phosphothreonine.
 MOD_RES 3395 3395 Phosphoserine (By similarity).
 MOD_RES 3396 3396 Phosphoserine (By similarity).
 MOD_RES 3443 3443 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Hydrolase; Phosphoprotein; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3582 AA 
Protein Sequence
MCENCADLVE VLNEISDIEG GDGLQLRKEH TLKIFAYINS WTQRQCLCCF KEYKHLEIFN 60
QVVCALINLV IAQVQVLRDQ LCKHCTTINI DSTWQDESNQ AEEPLSIDRE CNEGNTERQK 120
SIEKKSNSTR TCNLTEEESS KSSDPFSLWN 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 LEPGVHTEQT LYLASMLIKA LWNNALAAKA 480
QLSKQSSFAS LLNTNMPIGN KKEEEELRRA APSPWSPAAS PQSSDNSDTH QSGASDIEMD 540
EQLINRNKHV QQRLSDTEES MQGSSDETAN SGEDGSSGPG SSSGHSDGSS NEVNSSHASQ 600
SAGSPGSEVQ SEDIADIEAL KEEEEEEEEE EEEEEEEDDE EEEDEEEDDD DDDDHGHNPA 660
KNTCGTELRN RKLENPAGIC LGESQGTSER NGTNSGTGKD LVFNTEPLPS VDNRIRMLDA 720
CAHSEDPEHG ISGEVSSAHL AQGSQEACIT RSGDFLGETI GNELFNCRQF IGPQHHHHHH 780
HHHHHHHHHH HHHHHHHDGH MVDDMLSADD VSCSSSQVSA KSEKNMADFD GEESGCEEEL 840
VQINSHAELT SHLQQHLPNL ASIYHEHLSQ GPAVHKHQFS SNAVTDINLD NVCKKGNTLL 900
WDIVQDDDAI NLSEGLINEA EKLLCSLVCW FTDRQIRMRF IEGCLENLGN NRSVVISLRL 960
LPKLFGTFQQ FGSSYDTHWI TMWAEKELNM MKLFFDNLVY YIQGIREGRQ KHALYSHSAE 1020
VQVRLQFLTC VFSTLGSPDH FRLSLEQVDI LWHCLVEDSE CYDDALHWFL NQVRSKDQHA 1080
MGMETYKHLF LEKMPQLKPE TISMTGLNLF QHLCNLARLA TSAYDGGSNS ELCGMDQFWG 1140
IALRAQSGDV SRAAIQYINS YYINGKTGLE KEQEFISKCM ESLMIASSSL EQESHSSLTV 1200
IERGLLMLKT HLEAFRRRFA YHLRQWQIEG TGISSHLKAL SDKQSLPLRV VCQPAGLPDK 1260
MTIEMYPSDQ VADLRAEVTH WYENLQKEQI NQQAQLQEFG QSSRKGEFPG GLMGPVRMIS 1320
SGHELTTDYD EKALHELGFK DMQMVFVSLG APRRERKGEG VQLPASCLPP PQKDNIPMLL 1380
LLQEPHLTTL FDLLEMLASF KPPSGKVAVD DSESLKCEEL HLHAENLSRR VWELLMLLPT 1440
CPNMLTAFQN VSDEQSNDGL NWKELLKIKS AHKLLYALEI IEALGKPNRR IRRESTGSYS 1500
DLYPDSDDSS EDQVENSKNS WTCKFVAAGG LQQLLEIFNS AILEPKEQES WTVWQLDCLA 1560
CLLKLICQFA VDPSDLDLAY HDVFAWSGIA ESHRKRTWPG KSRKAAGDHA KSLHIPRLTE 1620
VFLVLVQGTS LIQRLMSVAY TYDNLAPRVL KAQSDHRSRH EVSHYSMWLL VSWAHCCSLV 1680
KSSLADSDHL QDWLKQLTLL IPETAVRHES CNGLYKLSLS GLDGGDSIHR SFLLLAASTL 1740
LKFLPDAQAL KPPRIDDYEE EPLLKPGCKE YFWLLCKLVD NIHIKDASQT TLLDLDALAR 1800
HLADCIRSRE ILDHLDGSIE DDGLSGLLRL ATSVIKHKPP FKFSREGQEF LRDIFNLLFL 1860
LPSLKDRRQP KCKSHSCRAA AYDLLVEMVK GSVENYRLIH NWVMAQHMQS HAPYKWDYWP 1920
HEDVRAECRF VGLTNLGATC YLASTIQQLY MIPEARQAVF TAKYSEDMKH KTTLLELQKM 1980
FTYLMESECK AYNPRPFCKT YTMDKQPLNT GEQKDMTEFF TDLITKVEEM SPELKNTVKS 2040
LFGGVITNNV VSLDCEHVSQ TAEEFYTVRC QVADMKNIYE SLDEVTIKDT LEGDNMYTCS 2100
HCGKKVRAEK RACFKKLPRI LSFNTMRYTF NMVTMMKEKV NTHFSFPLRL DMTPYTEDFL 2160
MGKSDRKEGF KDVGDRSKDT ESYEYDLIGV TVHTGTADGG HYYSFIRDIV NPHAYKNNKW 2220
YLFNDAEVKP FDSAQLASEC FGGEMTTKTY DSVTDKFMDF SFEKTHSAYM LFYKRMEPEE 2280
ENGREYKFDV SSELLEWIWH DNMQFLQDKN IFEHTYFGFM WQLCSCIPST LPDPKAVSLM 2340
TAKLSTSFVL ETFIHSKEKP TMLQWIELLT KQFNNSQAAC EWFLDRMADD DWWPMQILIK 2400
CPNQIVRQMF QRLCIHVIQR LRPVHAHLYL QPGMEDGSDD MDASVEDIGG RSCVTRFVRT 2460
LLLIMEHGVK PHSKHLTEYF AFLYEFAKMG EEESQFLLSL QAISTMVHFY MGTKGPENPQ 2520
VEVLSEEEGE EEEEEEDILS LAEEKYRPAA LEKMIALVAL LVEQSRSERH LTLSQTDMAA 2580
LTGGKGFPFL FQHIRDGINI RQTCNLIFSL CRYNNRLAEH IVSMLFTSIA KLTPEAANPF 2640
FKLLTMLMEF AGGPPGMPPF ASYILQRIWE VIEYNPSQCL DWLAVQTPRN KLAHSWVLQN 2700
MENWVERFLL AHNYPRVRTS AAYLLVSLIP SNSFRQMFRS TRSLHIPTRD LPLSPDTTVV 2760
LHQVYNVLLG LLSRAKLYVD AAVHGTTKLV PYLSFMTYCL ISKTEKLMFS TYFMDLWNLF 2820
QPKLSEPAIA TNHNKQALLS FWYNVCADCP ENIRLIVQNP VVTKNIAFNY ILADHDDQDV 2880
VLFNRGMLPA YYGILRLCCE QSPAFTRQLA SHQNIQWAFK NLTPHASQYP GAVEELFNLM 2940
QLFIAQRPDM REEELEDIKQ FKKTTISCYL RCLDGRSCWT TLISAFRILL ESDEDRLLVV 3000
FNRGLILMTE SFNTLHMMYH EATACHVTGD LVELLSIFLS VLKSTRPYLQ RKDVKQALIQ 3060
WQERIEFAHK LLTLLNSYSP PELRNACIDV LKELVLLSPH DFLHTLVPFL QHNHCTYHHS 3120
NIPMSLGPYF PCRENIKLIG GKSNIRPPRP ELNMCLLPTM VETSKGKDDV YDRMLLDYFF 3180
SYHQFIHLLC RVAINCEKFT ETLVKLSVLV AYEGLPLHLA LFPKLWTELC QTQSAMSKNC 3240
IKLLCEDPVF AEYIKCILMD ERTFLNNNIV YTFMTHFLLK VQSQVFSEAN CASLISTLIT 3300
NLINQYQNLQ SDFTNRVEIS KASAALNGDL RALALLLSVH TPKQLNPALI PTLQELLNKC 3360
RTCLQQRNSL QEQEAKERKT KDDEGATPVK RRRVSSDEEH TVDSCIGDIK TETREVLTPT 3420
STSDNETRDS SIIDPGTEQD LPSPENSSVK EYRMEGPSSF SEDGSHIRSQ HAEEQSNNGR 3480
FDDCKEFKDH CSKDTTLAED ESEFPSTSIS AVLSDLADLR SCDGQALSSQ DPEAAVSLSC 3540
GHSRGLISHM QQHDILDTLC RTIESTIHVV TRISGKGNQA AS 3582 
Gene Ontology
 GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
 GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
 GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; ISS:UniProtKB.
 GO:0071108; P:protein K48-linked deubiquitination; ISS: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