CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019399
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 47 
Protein Synonyms/Alias
 Deubiquitinating enzyme 47; Ubiquitin thioesterase 47; Ubiquitin-specific-processing protease 47 
Gene Name
 USP47 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
122ANFEPGKKNFLHLTDacetylation[1]
122ANFEPGKKNFLHLTDubiquitination[2, 3, 4]
130NFLHLTDKDGEQPQIubiquitination[5]
287MFDALEQKWKQTEQAubiquitination[2, 4]
289DALEQKWKQTEQADLubiquitination[4]
304INELYQGKLKDYVRCubiquitination[5]
533RITQEDIKKTHGGSSubiquitination[4]
571KDPARNAKFLEVDEYubiquitination[4]
660LDCCRLVKYDEFHDYubiquitination[2]
724KVHVVDLKAESVAAPubiquitination[4]
782SVSSKTLKAEGFFRSubiquitination[4]
838QSPVSYSKRTAYQKAubiquitination[3, 4]
844SKRTAYQKAGGDSGNubiquitination[4]
1058WLMVHVDKRITLAAFubiquitination[5]
1274LDDIEFAKGRGTFPCubiquitination[4]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Ubiquitin-specific protease that specifically deubiquitinates monoubiquitinated DNA polymerase beta (POLB), stabilizing POLB thereby playing a role in base-excision repair (BER). Acts as a regulator of cell growth and genome integrity. May also indirectly regulates CDC25A expression at a transcriptional level. 
Sequence Annotation
 ACT_SITE 197 197 Nucleophile (By similarity).
 ACT_SITE 503 503 Proton acceptor (By similarity).
 MOD_RES 122 122 N6-acetyllysine.
 MOD_RES 832 832 Phosphoserine.
 MOD_RES 910 910 Phosphoserine.
 MOD_RES 1015 1015 Phosphothreonine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; DNA damage; DNA repair; Hydrolase; Phosphoprotein; Polymorphism; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1375 AA 
Protein Sequence
MVPGEENQLV PKEDVFWRCR QNIFDEMKKK FLQIENAAEE PRVLCIIQDT TNSKTVNERI 60
TLNLPASTPV RKLFEDVANK VGYINGTFDL VWGNGINTAD MAPLDHTSDK SLLDANFEPG 120
KKNFLHLTDK DGEQPQILLE DSSAGEDSVH DRFIGPLPRE GSGGSTSDYV SQSYSYSSIL 180
NKSETGYVGL VNQAMTCYLN SLLQTLFMTP EFRNALYKWE FEESEEDPVT SIPYQLQRLF 240
VLLQTSKKRA IETTDVTRSF GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL 300
YQGKLKDYVR CLECGYEGWR IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN 360
QYFCERCKKK CDARKGLRFL HFPYLLTLQL KRFDFDYTTM HRIKLNDRMT FPEELDMSTF 420
IDVEDEKSPQ TESCTDSGAE NEGSCHSDQM SNDFSNDDGV DEGICLETNS GTEKISKSGL 480
EKNSLIYELF SVMVHSGSAA GGHYYACIKS FSDEQWYSFN DQHVSRITQE DIKKTHGGSS 540
GSRGYYSSAF ASSTNAYMLI YRLKDPARNA KFLEVDEYPE HIKNLVQKER ELEEQEKRQR 600
EIERNTCKIK LFCLHPTKQV MMENKLEVHK DKTLKEAVEM AYKMMDLEEV IPLDCCRLVK 660
YDEFHDYLER SYEGEEDTPM GLLLGGVKST YMFDLLLETR KPDQVFQSYK PGEVMVKVHV 720
VDLKAESVAA PITVRAYLNQ TVTEFKQLIS KAIHLPAETM RIVLERCYND LRLLSVSSKT 780
LKAEGFFRSN KVFVESSETL DYQMAFADSH LWKLLDRHAN TIRLFVLLPE QSPVSYSKRT 840
AYQKAGGDSG NVDDDCERVK GPVGSLKSVE AILEESTEKL KSLSLQQQQD GDNGDSSKST 900
ETSDFENIES PLNERDSSAS VDNRELEQHI QTSDPENFQS EERSDSDVNN DRSTSSVDSD 960
ILSSSHSSDT LCNADNAQIP LANGLDSHSI TSSRRTKANE GKKETWDTAE EDSGTDSEYD 1020
ESGKSRGEMQ YMYFKAEPYA ADEGSGEGHK WLMVHVDKRI TLAAFKQHLE PFVGVLSSHF 1080
KVFRVYASNQ EFESVRLNET LSSFSDDNKI TIRLGRALKK GEYRVKVYQL LVNEQEPCKF 1140
LLDAVFAKGM TVRQSKEELI PQLREQCGLE LSIDRFRLRK KTWKNPGTVF LDYHIYEEDI 1200
NISSNWEVFL EVLDGVEKMK SMSQLAVLSR RWKPSEMKLD PFQEVVLESS SVDELREKLS 1260
EISGIPLDDI EFAKGRGTFP CDISVLDIHQ DLDWNPKVST LNVWPLYICD DGAVIFYRDK 1320
TEELMELTDE QRNELMKKES SRLQKTGHRV TYSPRKEKAL KIYLDGAPNK DLTQD 1375 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
 GO:0004843; F:ubiquitin-specific protease activity; IDA:UniProtKB.
 GO:0006284; P:base-excision repair; IMP:UniProtKB.
 GO:0034644; P:cellular response to UV; ISS:UniProtKB.
 GO:0035520; P:monoubiquitinated protein deubiquitination; IDA:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
 GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
 GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
 GO:0042493; P:response to drug; IMP:UniProtKB.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 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