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Protein

Ubiquitin carboxyl-terminal hydrolase 7

Gene

USP7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN, KMT2E/MLL5 and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148, PubMed:26678539). 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 (PubMed:15053880, PubMed:16845383, PubMed:18566590, PubMed:20153724). Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent transcription regulation, cell growth repression and apoptosis (PubMed:25283148). 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 (PubMed:11923872). Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity (PubMed:16964248). 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 (PubMed:18716620). Deubiquitinates KMT2E/MLL5 preventing KMT2E/MLL5 proteasomal-mediated degradation (PubMed:26678539). 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 (PubMed:22466611, PubMed:22466612). 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 (PubMed:21745816, PubMed:22411829). Deubiquitinates alkylation repair enzyme ALKBH3. OTUD4 recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the repair of alkylated DNA lesions (PubMed:25944111). Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex (PubMed:20601937). Able to mediate deubiquitination of histone H2B; it is however unsure whether this activity takes place in vivo (PubMed:20601937). Exhibits a preference towards 'Lys-48'-linked ubiquitin chains (PubMed:22689415). Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222).17 Publications
(Microbial infection) Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection.3 Publications

Caution

Was reported to interact with UBXN6 but the corresponding article has been retracted (PubMed:18768758).

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).8 Publications

Activity regulationi

Inhibited by N-ethyl-maleimide (NEM) and divalent cations. Tolerates high concentrations of NaCl but is inhibited at concentrations of 195 mM and higher.1 Publication

pH dependencei

Active from pH 7.0 to 9.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei223Nucleophile6 Publications2 Publications1
Active sitei464Proton acceptor1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDevelopmental protein, Hydrolase, Protease, Thiol protease
Biological processDNA damage, DNA repair, Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-HSA-5689880 Ub-specific processing proteases
R-HSA-6781823 Formation of TC-NER Pre-Incision Complex
R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-HSA-8948747 Regulation of PTEN localization
SignaLinkiQ93009
SIGNORiQ93009

Protein family/group databases

MEROPSiC19.016

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 7 (EC:3.4.19.127 Publications)
Alternative name(s):
Deubiquitinating enzyme 7
Herpesvirus-associated ubiquitin-specific protease
Ubiquitin thioesterase 7
Ubiquitin-specific-processing protease 7
Gene namesi
Name:USP7Imported
Synonyms:HAUSP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000187555.14
HGNCiHGNC:12630 USP7
MIMi602519 gene
neXtProtiNX_Q93009

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi164D → A: Decreased binding to p53/TP53 and MDM2. 1 Publication1
Mutagenesisi165W → A: Loss of binding to p53/TP53 and MDM2. 1 Publication1
Mutagenesisi223C → A: Complete loss of activity. Localized in the nucleus and does not inhibit FOXO4-dependent transcriptional activity. 7 Publications1
Mutagenesisi223C → S: No effect on p53/TP53 and PTEN binding but is defective in deubiquitinating p53/TP53 and PTEN. Partial loss of KMT2E/mml5 deubiquitination. Decreases deubiquitinase activity toward 'Lys-48'-polyubiquitinated ALKBH3. 9 Publications1
Mutagenesisi456H → A: Complete loss of activity. 1 Publication1
Mutagenesisi464H → A: Complete loss of activity. 1 Publication1

Organism-specific databases

DisGeNETi7874
OpenTargetsiENSG00000187555
PharmGKBiPA37255

Chemistry databases

ChEMBLiCHEMBL2157850

Polymorphism and mutation databases

BioMutaiUSP7
DMDMi212276477

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000806261 – 1102Ubiquitin carboxyl-terminal hydrolase 7Add BLAST1102

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18PhosphoserineCombined sources1 Publication1
Modified residuei49PhosphoserineBy similarity1
Modified residuei869N6-acetyllysine; alternateCombined sources1
Cross-linki869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki882Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei963PhosphoserineCombined sources1 Publication1
Modified residuei1084N6-acetyllysineCombined sources1
Modified residuei1096N6-acetyllysineCombined sources1

Post-translational modificationi

Isoform 1: Phosphorylated. Isoform 1 is phosphorylated at positions Ser-18 and Ser-963. Isoform 2: Not phosphorylated.1 Publication
Isoform 1: Polyneddylated. Isoform 2: Not Polyneddylated.
Isoform 1 and isoform 2: Not sumoylated.
Isoform 1 and isoform 2: Polyubiquitinated by herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110; leading to its subsequent proteasomal degradation. Isoform 1: Ubiquitinated at Lys-869.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ93009
PaxDbiQ93009
PeptideAtlasiQ93009
PRIDEiQ93009
ProteomicsDBi75669

PTM databases

iPTMnetiQ93009
PhosphoSitePlusiQ93009

Expressioni

Tissue specificityi

Widely expressed. Overexpressed in prostate cancer.1 Publication

Inductioni

Up-regulated in regulatory T-cells (Treg).1 Publication

Gene expression databases

BgeeiENSG00000187555 Expressed in 234 organ(s), highest expression level in testis
CleanExiHS_USP7
ExpressionAtlasiQ93009 baseline and differential
GenevisibleiQ93009 HS

Organism-specific databases

HPAiCAB008108
HPA015641

Interactioni

Subunit structurei

Monomer. Homodimer. Part of a complex with DAXX, MDM2, RASSF1 and USP7 (PubMed:18566590). Part of a complex with DAXX, MDM2 and USP7 (PubMed:16845383). Interacts with MDM2; the interaction is independent of p53/TP53. Interacts with DAXX; the interaction is direct and independent of MDM2 and p53/TP53 (PubMed:16845383). Component of a complex composed of KMT2E/MLL5 (isoform 3), OGT (isoform 1) and USP7; the complex stabilizes KMT2E/MLL5, preventing KMT2E/MLL5 ubiquitination and proteosomal-mediated degradation (PubMed:26678539). Interacts (via MATH domain) with KMT2E/MLL5 isoform 3 (PubMed:26678539). Interacts with OGT isoform 1 (PubMed:26678539). Interacts with FOXO4; the interaction is enhanced in presence of hydrogen peroxide and occurs independently of p53/TP53 (PubMed:16964248). Interacts with p53/TP53; the interaction is enhanced in response to DNA damage (PubMed:25283148). Interacts with TSPYL5; this impairs interaction with p53/TP53 (PubMed:21170034). Interacts with PTEN; the interaction is direct (PubMed:18716620). Interacts with ATXN1 and the strength of interaction is influenced by the length of the poly-Gln region in ATXN1 (PubMed:12093161). A weaker interaction seen with mutants having longer poly-Gln regions (PubMed:12093161). Interacts with KIAA1530/UVSSA (PubMed:22466611, PubMed:22466612). Interacts with ABRAXAS2; the interaction is direct (PubMed:25283148). Identified in a complex with TP53/p53 and ABRAXAS2 (PubMed:25283148). Interacts with MEX3C and antagonizes its ability to degrade mRNA (PubMed:22863774). Interacts with DNMT1 and UHRF1 (PubMed:21745816, PubMed:22411829). Interacts with FOXP3 (PubMed:23973222). Interacts (via MATH domain) with RNF220. Associated component of the Polycomb group (PcG) multiprotein PRC1-like complex (PubMed:20601937). Interacts with EPOP (By similarity). Interacts with OTUD4 and USP9X; the interaction is direct (PubMed:25944111).By similarity16 Publications
(Microbial infection) Isoform 1 and isoform 2 interact with herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 (PubMed:9034339, PubMed:14506283, PubMed:16160161, PubMed:18590780). Binding to ICP0/VMW110 may modulate the substrate specificity or activity of USP7 to stabilize viral proteins.4 Publications
(Microbial infection) Interacts with Epstein-Barr virus EBNA1. EBNA1 shows a 10-fold higher affinity than p53/TP53 and can compete with it for USP7 binding.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113622, 349 interactors
CORUMiQ93009
DIPiDIP-29053N
ELMiQ93009
IntActiQ93009, 153 interactors
MINTiQ93009
STRINGi9606.ENSP00000343535

Chemistry databases

BindingDBiQ93009

Structurei

Secondary structure

11102
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

DisProtiDP00941
ProteinModelPortaliQ93009
SMRiQ93009
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ93009

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini68 – 195MATHPROSITE-ProRule annotationAdd BLAST128
Domaini214 – 521USPAdd BLAST308

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 208Interaction with TSPYL51 PublicationAdd BLAST208
Regioni53 – 208Interaction with p53/TP53, MDM2 and EBNA11 PublicationAdd BLAST156
Regioni70 – 205Necessary for nuclear localizationAdd BLAST136
Regioni622 – 801Interaction with ICP0/VMW1101 PublicationAdd BLAST180

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 10Poly-Gln7

Domaini

The C-terminus plays a role in its oligomerization.By similarity

Sequence similaritiesi

Belongs to the peptidase C19 family.Curated

Phylogenomic databases

eggNOGiKOG1863 Eukaryota
COG5077 LUCA
GeneTreeiENSGT00760000119158
HOGENOMiHOG000160240
HOVERGENiHBG018029
InParanoidiQ93009
KOiK11838
OMAiPDKEWEN
OrthoDBiEOG091G01BK
PhylomeDBiQ93009
TreeFamiTF105667

Family and domain databases

Gene3Di2.60.210.10, 1 hit
InterProiView protein in InterPro
IPR002083 MATH/TRAF_dom
IPR038765 Papain_like_cys_pep_sf
IPR001394 Peptidase_C19_UCH
IPR008974 TRAF-like
IPR024729 USP7_ICP0-binding_dom
IPR029346 USP_C
IPR018200 USP_CS
IPR028889 USP_dom
PfamiView protein in Pfam
PF00917 MATH, 1 hit
PF00443 UCH, 1 hit
PF14533 USP7_C2, 1 hit
PF12436 USP7_ICP0_bdg, 1 hit
SMARTiView protein in SMART
SM00061 MATH, 1 hit
SUPFAMiSSF49599 SSF49599, 1 hit
SSF54001 SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS50144 MATH, 1 hit
PS00972 USP_1, 1 hit
PS00973 USP_2, 1 hit
PS50235 USP_3, 1 hit

Sequences (3+)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q93009-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MNHQQQQQQQ KAGEQQLSEP EDMEMEAGDT DDPPRITQNP VINGNVALSD
60 70 80 90 100
GHNTAEEDME DDTSWRSEAT FQFTVERFSR LSESVLSPPC FVRNLPWKIM
110 120 130 140 150
VMPRFYPDRP HQKSVGFFLQ CNAESDSTSW SCHAQAVLKI INYRDDEKSF
160 170 180 190 200
SRRISHLFFH KENDWGFSNF MAWSEVTDPE KGFIDDDKVT FEVFVQADAP
210 220 230 240 250
HGVAWDSKKH TGYVGLKNQG ATCYMNSLLQ TLFFTNQLRK AVYMMPTEGD
260 270 280 290 300
DSSKSVPLAL QRVFYELQHS DKPVGTKKLT KSFGWETLDS FMQHDVQELC
310 320 330 340 350
RVLLDNVENK MKGTCVEGTI PKLFRGKMVS YIQCKEVDYR SDRREDYYDI
360 370 380 390 400
QLSIKGKKNI FESFVDYVAV EQLDGDNKYD AGEHGLQEAE KGVKFLTLPP
410 420 430 440 450
VLHLQLMRFM YDPQTDQNIK INDRFEFPEQ LPLDEFLQKT DPKDPANYIL
460 470 480 490 500
HAVLVHSGDN HGGHYVVYLN PKGDGKWCKF DDDVVSRCTK EEAIEHNYGG
510 520 530 540 550
HDDDLSVRHC TNAYMLVYIR ESKLSEVLQA VTDHDIPQQL VERLQEEKRI
560 570 580 590 600
EAQKRKERQE AHLYMQVQIV AEDQFCGHQG NDMYDEEKVK YTVFKVLKNS
610 620 630 640 650
SLAEFVQSLS QTMGFPQDQI RLWPMQARSN GTKRPAMLDN EADGNKTMIE
660 670 680 690 700
LSDNENPWTI FLETVDPELA ASGATLPKFD KDHDVMLFLK MYDPKTRSLN
710 720 730 740 750
YCGHIYTPIS CKIRDLLPVM CDRAGFIQDT SLILYEEVKP NLTERIQDYD
760 770 780 790 800
VSLDKALDEL MDGDIIVFQK DDPENDNSEL PTAKEYFRDL YHRVDVIFCD
810 820 830 840 850
KTIPNDPGFV VTLSNRMNYF QVAKTVAQRL NTDPMLLQFF KSQGYRDGPG
860 870 880 890 900
NPLRHNYEGT LRDLLQFFKP RQPKKLYYQQ LKMKITDFEN RRSFKCIWLN
910 920 930 940 950
SQFREEEITL YPDKHGCVRD LLEECKKAVE LGEKASGKLR LLEIVSYKII
960 970 980 990 1000
GVHQEDELLE CLSPATSRTF RIEEIPLDQV DIDKENEMLV TVAHFHKEVF
1010 1020 1030 1040 1050
GTFGIPFLLR IHQGEHFREV MKRIQSLLDI QEKEFEKFKF AIVMMGRHQY
1060 1070 1080 1090 1100
INEDEYEVNL KDFEPQPGNM SHPRPWLGLD HFNKAPKRSR YTYLEKAIKI

HN
Length:1,102
Mass (Da):128,302
Last modified:November 4, 2008 - v2
Checksum:iF1A5A5C421396E45
GO
Isoform 2 (identifier: Q93009-2)
Also known as: USP7 beta
Sequence is not available
Note: No experimental confirmation available.
Length:
Mass (Da):
Isoform 3 (identifier: Q93009-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MNHQQQQQQQKAGEQQLSEPEDMEM → MAGNHRLGL

Note: No experimental confirmation available.
Show »
Length:1,086
Mass (Da):126,269
Checksum:i0CC92229880D2E2B
GO

Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5H2X1F5H2X1_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
509Annotation score:
H3BND8H3BND8_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
909Annotation score:
H3BQD1H3BQD1_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
159Annotation score:
H3BRA2H3BRA2_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
130Annotation score:
H3BUV0H3BUV0_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
109Annotation score:
H3BTM1H3BTM1_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
117Annotation score:
H3BMF6H3BMF6_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
91Annotation score:
I3L2D8I3L2D8_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
68Annotation score:
H3BRI4H3BRI4_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
47Annotation score:
H3BVA7H3BVA7_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP7
17Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti201H → I AA sequence (PubMed:9034339).Curated1
Sequence conflicti205W → P AA sequence (PubMed:9034339).Curated1
Sequence conflicti207S → Q AA sequence (PubMed:9034339).Curated1
Sequence conflicti1045M → T in CAA96580 (PubMed:9034339).Curated1
Sequence conflicti1066Q → T AA sequence (PubMed:9034339).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0548841 – 25MNHQQ…EDMEM → MAGNHRLGL in isoform 3. 1 PublicationAdd BLAST25

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72499 mRNA Translation: CAA96580.1
AK302771 mRNA Translation: BAH13801.1
AC022167 Genomic DNA No translation available.
CH471112 Genomic DNA Translation: EAW85194.1
CCDSiCCDS32385.1 [Q93009-1]
CCDS66941.1 [Q93009-3]
RefSeqiNP_001308787.1, NM_001321858.1
NP_003461.2, NM_003470.2 [Q93009-1]
UniGeneiHs.386939

Genome annotation databases

EnsembliENST00000344836; ENSP00000343535; ENSG00000187555 [Q93009-1]
ENST00000381886; ENSP00000371310; ENSG00000187555 [Q93009-3]
GeneIDi7874
KEGGihsa:7874
UCSCiuc002czk.4 human [Q93009-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72499 mRNA Translation: CAA96580.1
AK302771 mRNA Translation: BAH13801.1
AC022167 Genomic DNA No translation available.
CH471112 Genomic DNA Translation: EAW85194.1
CCDSiCCDS32385.1 [Q93009-1]
CCDS66941.1 [Q93009-3]
RefSeqiNP_001308787.1, NM_001321858.1
NP_003461.2, NM_003470.2 [Q93009-1]
UniGeneiHs.386939

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NB8X-ray2.30A/B208-560[»]
1NBFX-ray2.30A/B/E208-560[»]
1YY6X-ray1.70A54-204[»]
1YZEX-ray2.00A/B/C54-205[»]
2F1WX-ray1.65A53-206[»]
2F1XX-ray2.30A/B53-200[»]
2F1YX-ray1.70A53-198[»]
2F1ZX-ray3.20A/B43-560[»]
2FOJX-ray1.60A54-205[»]
2FOOX-ray2.20A54-205[»]
2FOPX-ray2.10A54-205[»]
2KVRNMR-A537-664[»]
2XXNX-ray1.60A63-205[»]
2YLMX-ray2.70A560-1084[»]
3MQRX-ray1.80A54-205[»]
3MQSX-ray2.40C54-205[»]
4JJQX-ray1.95A54-205[»]
4KG9X-ray1.70A54-205[»]
4M5WX-ray2.24A207-560[»]
4M5XX-ray2.19A/B207-560[»]
4PYZX-ray2.84A/B537-793[»]
4WPHX-ray2.92A/B535-888[»]
4WPIX-ray3.40A/B535-888[»]
4YOCX-ray2.92C560-1102[»]
4YSIX-ray1.02A63-205[»]
4Z96X-ray2.85A560-1083[»]
4Z97X-ray3.00A560-1083[»]
5C56X-ray2.69A560-1102[»]
5C6DX-ray2.29A/B561-881[»]
5FWIX-ray3.40C207-882[»]
5GG4X-ray3.11A/B/C/D560-890[»]
5J7TX-ray3.20A211-881[»]
5JTJX-ray3.32A209-554[»]
A1084-1102[»]
5JTVX-ray3.31A/C/E/G207-554[»]
A/C/E/G882-1102[»]
5KYBX-ray2.20A/B208-554[»]
5KYCX-ray1.43B208-554[»]
5KYDX-ray1.62A208-554[»]
5KYEX-ray1.97A/B208-554[»]
5KYFX-ray1.45B208-554[»]
5N9RX-ray2.23A/B207-560[»]
5N9TX-ray1.73A/B207-560[»]
5NGEX-ray2.35A/B208-560[»]
5NGFX-ray2.33A/B208-560[»]
5UQVX-ray2.84A/B208-554[»]
5UQXX-ray2.23A/B208-555[»]
5VS6X-ray2.27A/B208-560[»]
5VSBX-ray1.85A/B208-560[»]
5VSKX-ray3.33A/B208-560[»]
5WHCX-ray2.55A/B209-554[»]
6F5HX-ray2.16A/B207-560[»]
DisProtiDP00941
ProteinModelPortaliQ93009
SMRiQ93009
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113622, 349 interactors
CORUMiQ93009
DIPiDIP-29053N
ELMiQ93009
IntActiQ93009, 153 interactors
MINTiQ93009
STRINGi9606.ENSP00000343535

Chemistry databases

BindingDBiQ93009
ChEMBLiCHEMBL2157850

Protein family/group databases

MEROPSiC19.016

PTM databases

iPTMnetiQ93009
PhosphoSitePlusiQ93009

Polymorphism and mutation databases

BioMutaiUSP7
DMDMi212276477

Proteomic databases

EPDiQ93009
PaxDbiQ93009
PeptideAtlasiQ93009
PRIDEiQ93009
ProteomicsDBi75669

Protocols and materials databases

DNASUi7874
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344836; ENSP00000343535; ENSG00000187555 [Q93009-1]
ENST00000381886; ENSP00000371310; ENSG00000187555 [Q93009-3]
GeneIDi7874
KEGGihsa:7874
UCSCiuc002czk.4 human [Q93009-1]

Organism-specific databases

CTDi7874
DisGeNETi7874
EuPathDBiHostDB:ENSG00000187555.14
GeneCardsiUSP7
H-InvDBiHIX0038590
HGNCiHGNC:12630 USP7
HPAiCAB008108
HPA015641
MIMi602519 gene
neXtProtiNX_Q93009
OpenTargetsiENSG00000187555
PharmGKBiPA37255
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1863 Eukaryota
COG5077 LUCA
GeneTreeiENSGT00760000119158
HOGENOMiHOG000160240
HOVERGENiHBG018029
InParanoidiQ93009
KOiK11838
OMAiPDKEWEN
OrthoDBiEOG091G01BK
PhylomeDBiQ93009
TreeFamiTF105667

Enzyme and pathway databases

ReactomeiR-HSA-5689880 Ub-specific processing proteases
R-HSA-6781823 Formation of TC-NER Pre-Incision Complex
R-HSA-6781827 Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6804757 Regulation of TP53 Degradation
R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-HSA-8948747 Regulation of PTEN localization
SignaLinkiQ93009
SIGNORiQ93009

Miscellaneous databases

ChiTaRSiUSP7 human
EvolutionaryTraceiQ93009
GeneWikiiUSP7
GenomeRNAii7874
PROiPR:Q93009
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000187555 Expressed in 234 organ(s), highest expression level in testis
CleanExiHS_USP7
ExpressionAtlasiQ93009 baseline and differential
GenevisibleiQ93009 HS

Family and domain databases

Gene3Di2.60.210.10, 1 hit
InterProiView protein in InterPro
IPR002083 MATH/TRAF_dom
IPR038765 Papain_like_cys_pep_sf
IPR001394 Peptidase_C19_UCH
IPR008974 TRAF-like
IPR024729 USP7_ICP0-binding_dom
IPR029346 USP_C
IPR018200 USP_CS
IPR028889 USP_dom
PfamiView protein in Pfam
PF00917 MATH, 1 hit
PF00443 UCH, 1 hit
PF14533 USP7_C2, 1 hit
PF12436 USP7_ICP0_bdg, 1 hit
SMARTiView protein in SMART
SM00061 MATH, 1 hit
SUPFAMiSSF49599 SSF49599, 1 hit
SSF54001 SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS50144 MATH, 1 hit
PS00972 USP_1, 1 hit
PS00973 USP_2, 1 hit
PS50235 USP_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiUBP7_HUMAN
AccessioniPrimary (citable) accession number: Q93009
Secondary accession number(s): A6NMY8, B7Z815, H0Y3G8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 4, 2008
Last modified: October 10, 2018
This is version 205 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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