CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031889
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 
Protein Synonyms/Alias
  
Gene Name
 USP24 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23RKALRLAKNDINEAVubiquitination[1]
163SPVSTFQKEPHGWVVubiquitination[2]
309IEDSTLSKSVKNAIDubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
488EITRSFIKQTYQKQDubiquitination[1, 7, 8]
496QTYQKQDKSIIQDLKubiquitination[5, 8]
980ESSSQSSKSPSLSSKubiquitination[7]
1132SLCGTPEKSSYRQLSubiquitination[7]
1196VGSSQPIKESNSLCPubiquitination[7]
1467SQQDFHPKCSTANSRubiquitination[7, 8]
1604KIFKMWNKELYVREQubiquitination[1, 2, 3, 4, 7, 8, 9]
1739WESGRSIKYDEQIRFubiquitination[8]
1937DRLSILTKLVKKGEKubiquitination[3, 7]
2394SNETSTGKTFQRTISubiquitination[1, 7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Hydrolase; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2460 AA 
Protein Sequence
MTTLLCMGFS DPATIRKALR LAKNDINEAV ALLTNERPGL DYGGYEPMDS GGLSESDENC 60
RRFMDRCMPE AFKKLLTSSA VHKWGTEIHE GIYNMLMLLI ELVAERIKQD PIPTGLLGVL 120
TMAFNPDNEY HFKNRMKVSQ RNWAEVFGEG NMFAVSPVST FQKEPHGWVV DLVNKFGELG 180
GFAAIQAKLH SEDIELGAVS ALIQPLGVCA EYLNSSVVQP MLDPVILTTI QDVRSVEEKD 240
LKDKRLVSIP ELLSAVKLLC MRFQPDLVTI VDDLRLDILL RMLKSPHFSA KMNSLKEVTK 300
LIEDSTLSKS VKNAIDTDRL LDWLVENSVL SIALEGNIDQ AQYCDRIKGI IELLGSKLSL 360
DELTKIWKIQ SGQSSTVIEN IHTIIAAAAV KFNSDQLNHL FVLIQKVLDV LWELAHLPTL 420
PSSLIQQALE EHLTILSDAY AVKEAIKRSY IIKCIEDIKR SSQLNNPQFV WVVPALRQLH 480
EITRSFIKQT YQKQDKSIIQ DLKKNFEIVK LVTGSLIACH RLAAAVAGPG GLSGSTLVDG 540
RYTYREYLEA HLKFLAFFLQ EATLYLGWNR AKEIWECLVT GQDVCELDRE MCFEWFTKGQ 600
HDLESDVQQQ LFKEKILKLE SYEITMNGFN LFKTFFENVN LCDHRLKRQG AQLYVEKLEL 660
IGMDFIWKIA MESPDEEIAN EAIQLIINYS YINLNPRLKK DSVSLHKKFI ADCYTRLEAA 720
SSALGGPTLT HAVTRATKML TATAMPTVAT SVQSPYRSTK LVIIERLLLL AERYVITIED 780
FYSVPRTILP HGASFHGHLL TLNVTYESTK DTFTVEAHSN ETIGSVRWKI AKQLCSPVDN 840
IQIFTNDSLL TVNKDQKLLH QLGFSDEQIL TVKTSGSGTP SGSSADSSTS SSSSSSGVFS 900
SSYAMEQEKS LPGVVMALVC NVFDMLYQLA NLEEPRITLR VRKLLLLIPT DPAIQEALDQ 960
LDSLGRKKTL LSESSSQSSK SPSLSSKQQH QPSASSILES LFRSFAPGMS TFRVLYNLEV 1020
LSSKLMPTAD DDMARSCAKS FCENFLKAGG LSLVVNVMQR DSIPSEVDYE TRQGVYSICL 1080
QLARFLLVGQ TMPTLLDEDL TKDGIEALSS RPFRNVSRQT SRQMSLCGTP EKSSYRQLSV 1140
SDRSSIRVEE IIPAARVAIQ TMEVSDFTST VACFMRLSWA AAAGRLDLVG SSQPIKESNS 1200
LCPAGIRNRL SSSGSNCSSG SEGEPVALHA GICVRQQSVS TKDSLIAGEA LSLLVTCLQL 1260
RSQQLASFYN LPCVADFIID ILLGSPSAEI RRVACDQLYT LSQTDTSAHP DVQKPNQFLL 1320
GVILTAQLPL WSPTSIMRGV NQRLLSQCME YFDLRCQLLD DLTTSEMEQL RISPATMLED 1380
EITWLDNFEP NRTAECETSE ADNILLAGHL RLIKTLLSLC GAEKEMLGSS LIKPLLDDFL 1440
FRASRIILNS HSPAGSAAIS QQDFHPKCST ANSRLAAYEV LVMLADSSPS NLQIIIKELL 1500
SMHHQPDPAL TKEFDYLPPV DSRSSSGFVG LRNGGATCYM NAVFQQLYMQ PGLPESLLSV 1560
DDDTDNPDDS VFYQVQSLFG HLMESKLQYY VPENFWKIFK MWNKELYVRE QQDAYEFFTS 1620
LIDQMDEYLK KMGRDQIFKN TFQGIYSDQK ICKDCPHRYE REEAFMALNL GVTSCQSLEI 1680
SLDQFVRGEV LEGSNAYYCE KCKEKRITVK RTCIKSLPSV LVIHLMRFGF DWESGRSIKY 1740
DEQIRFPWML NMEPYTVSGM ARQDSSSEVG ENGRSVDQGG GGSPRKKVAL TENYELVGVI 1800
VHSGQAHAGH YYSFIKDRRG CGKGKWYKFN DTVIEEFDLN DETLEYECFG GEYRPKVYDQ 1860
TNPYTDVRRR YWNAYMLFYQ RVSDQNSPVL PKKSRVSVVR QEAEDLSLSA PSSPEISPQS 1920
SPRPHRPNND RLSILTKLVK KGEKKGLFVE KMPARIYQMV RDENLKFMKN RDVYSSDYFS 1980
FVLSLASLNA TKLKHPYYPC MAKVSLQLAI QFLFQTYLRT KKKLRVDTEE WIATIEALLS 2040
KSFDACQWLV EYFISSEGRE LIKIFLLECN VREVRVAVAT ILEKTLDSAL FYQDKLKSLH 2100
QLLEVLLALL DKDVPENCKN CAQYFFLFNT FVQKQGIRAG DLLLRHSALR HMISFLLGAS 2160
RQNNQIRRWS SAQAREFGNL HNTVALLVLH SDVSSQRNVA PGIFKQRPPI SIAPSSPLLP 2220
LHEEVEALLF MSEGKPYLLE VMFALRELTG SLLALIEMVV YCCFCNEHFS FTMLHFIKNQ 2280
LETAPPHELK NTFQLLHEIL VIEDPIQVER VKFVFETENG LLALMHHSNH VDSSRCYQCV 2340
KFLVTLAQKC PAAKEYFKEN SHHWSWAVQW LQKKMSEHYW TPQSNVSNET STGKTFQRTI 2400
SAQDTLAYAT ALLNEKEQSG SSNGSESSPA NENGDRHLQQ GSESPMMIGE LRSDLDDVDP 2460 
Gene Ontology
 GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
 GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19.
 IPR015940; UBA/transl_elong_EF1B_N_euk. 
Pfam
 PF00443; UCH 
SMART
  
PROSITE
 PS50030; UBA
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3 
PRINTS