CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013386
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 7 
Protein Synonyms/Alias
 Deubiquitinating enzyme 7; Herpesvirus-associated ubiquitin-specific protease; rHAUSP; Ubiquitin thioesterase 7; Ubiquitin-specific-processing protease 7 
Gene Name
 Usp7 
Gene Synonyms/Alias
 Hausp 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
279DKPVGTKKLTKSFGWubiquitination[1]
323CVEGTIPKLFRGKMVubiquitination[1]
336MVSYIQCKEVDYRSDubiquitination[1]
825MNYFQVAKTVAQRLNubiquitination[1]
870RDLLQFFKPRQPKKLubiquitination[1]
883KLYYQQLKMKITDFEubiquitination[1]
1034SLLDIQEKEFEKFKFubiquitination[1]
1097SRYTYLEKAIKIHN*ubiquitination[1]
Reference
 [1] 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
 Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53- dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. 
Sequence Annotation
 DOMAIN 69 196 MATH.
 REGION 1 209 Interaction with TSPYL5 (By similarity).
 REGION 54 209 Interaction with p53/TP53 and MDM2 (By
 REGION 71 206 Necessary for nuclear localization (By
 ACT_SITE 224 224 Nucleophile (By similarity).
 ACT_SITE 465 465 Proton acceptor (By similarity).
 MOD_RES 19 19 Phosphoserine (By similarity).
 MOD_RES 870 870 N6-acetyllysine; alternate (By
 MOD_RES 964 964 Phosphoserine (By similarity).
 MOD_RES 1085 1085 N6-acetyllysine (By similarity).
 MOD_RES 1097 1097 N6-acetyllysine (By similarity).
 CROSSLNK 870 870 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Developmental protein; DNA damage; DNA repair; Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein; Protease; Reference proteome; Thiol protease; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1103 AA 
Protein Sequence
MNHQQQQQQQ QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVALS DGHSNAEEDM 60
EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL 120
QCNAESDSTS WSCHAQAVLK IINYRDDDKS FSRRISHLFF HKENDWGFSN FMAWSEVTDP 180
EKGFIDDDKV TFEVFVQADA PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR 240
KAVYMMPTEG DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL 300
CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKEVDY RSDRREDYYD IQLSIKGKKN 360
IFESFVDYVA VEQLDGDNKY DAGEHGLQEA EKGVKFLTLP PVLHLQLMRF MYDPQTDQNI 420
KINDRFEFPE QLPLDEFLQK TDPKDPANYI LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK 480
FDDDVVSRCT KEEAIEHNYG GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ 540
LVERLQEEKR IEAQKRKERQ EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN 600
SSLAEFVQSL SQTMGFPQDQ IRLWPMQARS NGTKRPAMLD NEADGSKTMI ELSDNENPWT 660
IFLETVDPEL AASGATLPKF DKDHDVMLFL KMYDPKTRSL NYCGHIYTPI SCKIRDLLPV 720
MCDRAGFIQD TSLILYEEVK PNLTERIQDY DVSLDKALDE LMDGDIIVFQ KDDPENDNSE 780
LPTAKEYFRD LYHRVDVIFC DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF 840
FKSQGYRDGP GNPLRHNYEG TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL 900
NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGDEASGRL RLLEIVSYKI IGVHQEDELL 960
ECLSPATSRT FRIEEIPLDQ VNIDKENEML ITVAHFHKEV FGTFGIPFLL RIHQGEHFRE 1020
VMKRIQSLLD IQEKEFEKFK FAIVMMGRHQ YINEDEYEVN LKDFEPQPGN MSHPRPWLGL 1080
DHFNKAPKRS RYTYLEKAIK IHN 1103 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
 GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:RGD.
 GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
 GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
 GO:0006917; P:induction of apoptosis; IDA:RGD.
 GO:0010216; P:maintenance of DNA methylation; ISS:UniProtKB.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
 GO:0031647; P:regulation of protein stability; IDA:RGD.
 GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
 GO:0006283; P:transcription-coupled nucleotide-excision repair; ISS:UniProtKB.
 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