CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032149
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 
Protein Synonyms/Alias
  
Gene Name
 USP7 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
82FVRNLPWKIMVMPRFubiquitination[1, 2, 3]
132INYRDDEKSFSRRISubiquitination[1]
224FFTNQLRKAVYMMPTubiquitination[2]
238TEGDDSSKSVPLALQubiquitination[2, 4]
256YELQHSDKPVGTKKLacetylation[3]
256YELQHSDKPVGTKKLubiquitination[2]
296DNVENKMKGTCVEGTubiquitination[2]
319MVSYIQCKEVDYRSDubiquitination[2]
339YDIQLSIKGKKNIFEubiquitination[1, 4, 5]
404PQTDQNIKINDRFEFubiquitination[1, 2, 3, 4, 5, 6]
423PLDEFLQKTDPKDPAubiquitination[4]
460LNPKGDGKWCKFDDDubiquitination[2, 7]
463KGDGKWCKFDDDVVSubiquitination[1, 2]
474DVVSRCTKEEAIEHNubiquitination[2]
507LVYIRESKLSEVLQAubiquitination[2]
579KVKYTVFKVLKNSSLubiquitination[2]
665ATLPKFDKDHDVMLFubiquitination[2]
679FLKMYDPKTRSLNYCubiquitination[2]
696IYTPISCKIRDLLPVubiquitination[2]
808MNYFQVAKTVAQRLNubiquitination[1, 2, 3, 4, 5]
825PMLLQFFKSQGYRDGubiquitination[1, 2, 6]
853RDLLQFFKPRQPKKLacetylation[3, 8, 9]
853RDLLQFFKPRQPKKLubiquitination[1, 2, 3, 4, 5, 6, 7]
859FKPRQPKKLYYQQLKubiquitination[2, 4]
866KLYYQQLKMKITDFEubiquitination[1, 2, 5, 6]
898EITLYPDKHGCVRDLacetylation[3]
898EITLYPDKHGCVRDLubiquitination[2]
910RDLLEECKKAVELGEubiquitination[2]
911DLLEECKKAVELGEKubiquitination[2]
918KAVELGEKASGKLRLacetylation[3]
918KAVELGEKASGKLRLubiquitination[2, 3, 4, 6]
1017SLLDIQEKEFEKFKFubiquitination[1, 2, 3]
1023EKEFEKFKFAIVMMGubiquitination[2]
1068LGLDHFNKAPKRSRYacetylation[8, 9]
1080SRYTYLEKAIKIHN*ubiquitination[1, 2, 3, 4, 5, 7]
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] 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]
 [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] 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] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [9] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
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
 1086 AA 
Protein Sequence
MAGNHRLGLE AGDTDDPPRI TQNPVINGNV ALSDGHNTAE EDMEDDTSWR SEATFQFTVE 60
RFSRLSESVL SPPCFVRNLP WKIMVMPRFY PDRPHQKSVG FFLQCNAESD STSWSCHAQA 120
VLKIINYRDD EKSFSRRISH LFFHKENDWG FSNFMAWSEV TDPEKGFIDD DKVTFEVFVQ 180
ADAPHGVAWD SKKHTGYVGL KNQGATCYMN SLLQTLFFTN QLRKAVYMMP TEGDDSSKSV 240
PLALQRVFYE LQHSDKPVGT KKLTKSFGWE TLDSFMQHDV QELCRVLLDN VENKMKGTCV 300
EGTIPKLFRG KMVSYIQCKE VDYRSDRRED YYDIQLSIKG KKNIFESFVD YVAVEQLDGD 360
NKYDAGEHGL QEAEKGVKFL TLPPVLHLQL MRFMYDPQTD QNIKINDRFE FPEQLPLDEF 420
LQKTDPKDPA NYILHAVLVH SGDNHGGHYV VYLNPKGDGK WCKFDDDVVS RCTKEEAIEH 480
NYGGHDDDLS VRHCTNAYML VYIRESKLSE VLQAVTDHDI PQQLVERLQE EKRIEAQKRK 540
ERQEAHLYMQ VQIVAEDQFC GHQGNDMYDE EKVKYTVFKV LKNSSLAEFV QSLSQTMGFP 600
QDQIRLWPMQ ARSNGTKRPA MLDNEADGNK TMIELSDNEN PWTIFLETVD PELAASGATL 660
PKFDKDHDVM LFLKMYDPKT RSLNYCGHIY TPISCKIRDL LPVMCDRAGF IQDTSLILYE 720
EVKPNLTERI QDYDVSLDKA LDELMDGDII VFQKDDPEND NSELPTAKEY FRDLYHRVDV 780
IFCDKTIPND PGFVVTLSNR MNYFQVAKTV AQRLNTDPML LQFFKSQGYR DGPGNPLRHN 840
YEGTLRDLLQ FFKPRQPKKL YYQQLKMKIT DFENRRSFKC IWLNSQFREE EITLYPDKHG 900
CVRDLLEECK KAVELGEKAS GKLRLLEIVS YKIIGVHQED ELLECLSPAT SRTFRIEEIP 960
LDQVDIDKEN EMLVTVAHFH KEVFGTFGIP FLLRIHQGEH FREVMKRIQS LLDIQEKEFE 1020
KFKFAIVMMG RHQYINEDEY EVNLKDFEPQ PGNMSHPRPW LGLDHFNKAP KRSRYTYLEK 1080
AIKIHN 1086 
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
 IPR002083; MATH.
 IPR024729; Pept_C19_dom.
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19.
 IPR008974; TRAF-like. 
Pfam
 PF00917; MATH
 PF00443; UCH
 PF12436; USP7 
SMART
 SM00061; MATH 
PROSITE
 PS50144; MATH
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3 
PRINTS