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Protein

Ubiquitin carboxyl-terminal hydrolase 7

Gene

USP7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148). 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, 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. 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. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. 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). Exhibits a preference towards 'Lys-48'-linked ubiquitin chains. Increases regulatory T-cells (Treg) suppressive capacity by deubiquitinating and stabilizing the transcription factor FOXP3 which is crucial for Treg cell function (PubMed:23973222).15 Publications

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).7 Publications

Enzyme 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 Publications1 Publication1
Active sitei464Proton acceptor1 Publication1

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: UniProtKB
  • p53 binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • thiol-dependent ubiquitin-specific protease activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • maintenance of DNA methylation Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • protein deubiquitination Source: UniProtKB
  • protein stabilization Source: BHF-UCL
  • regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • regulation of telomere capping Source: BHF-UCL
  • transcription-coupled nucleotide-excision repair Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: InterPro
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Thiol protease

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:HS10354-MONOMER.
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.
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:USP7
Synonyms:HAUSP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:12630. USP7.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nuclear body Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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. 7 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
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.

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.
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). 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 UBXN6 (PubMed:18768758). Interacts with ATXN1 and the strength of interaction is influenced by the length of the poly-Gln region in ATXN1. A weaker interaction seen with mutants having longer poly-Gln regions (PubMed:12093161). Interacts with KIAA1530/UVSSA (PubMed:22466611, PubMed:22466612). Interacts with FAM175B; the interaction is direct (PubMed:25283148). Identified in a complex with TP53/p53 and FAM175B (PubMed:25283148). Isoform 1 and isoform 2 interact with herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 (PubMed:9034339, PubMed:14506283, PubMed:16160161, PubMed:18590780). Interacts with Epstein-Barr virus EBNA1 (PubMed:14506283). EBNA1 shows a 10-fold higher affinity than p53/TP53 and can compete with it for USP7 binding (PubMed:14506283). Binding to ICP0/VMW110 may modulate the substrate specificity or activity of USP7 to stabilize viral proteins. Interacts with MEX3C and antagonizes its ability to degrade mRNA (PubMed:22863774). Interacts with DNMT1 and UHRF1 (PubMed:21745816). Interacts with FOXP3 (PubMed:23973222). Interacts (via MATH domain) with RNF220 (PubMed:25266658).26 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCORQ6W2J93EBI-302474,EBI-950027
BMI1P352267EBI-302474,EBI-2341576
CBX8Q9HC527EBI-302474,EBI-712912
DAXXQ9UER713EBI-302474,EBI-77321
EBNA1P032115EBI-302474,EBI-996522From a different organism.
MALP211453EBI-302474,EBI-3932027
MDM2Q0098718EBI-302474,EBI-389668
MDM4O1515115EBI-302474,EBI-398437
Mdm4O356184EBI-302474,EBI-2603376From a different organism.
MEX3CQ5U5Q33EBI-302474,EBI-2864451
MYD88Q998363EBI-302474,EBI-447677
PCGF2P352275EBI-302474,EBI-2129767
RB1P064008EBI-302474,EBI-491274
RING1Q065875EBI-302474,EBI-752313
RNF2Q994965EBI-302474,EBI-722416
SMAD3P840222EBI-302474,EBI-347161
TBCBQ994262EBI-302474,EBI-764356
TP53P0463717EBI-302474,EBI-366083
TSPYL5Q86VY44EBI-302474,EBI-3436472

GO - Molecular functioni

  • p53 binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113622. 330 interactors.
DIPiDIP-29053N.
IntActiQ93009. 143 interactors.
MINTiMINT-234628.
STRINGi9606.ENSP00000343535.

Chemistry databases

BindingDBiQ93009.

Structurei

Secondary structure

11102
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi67 – 77Combined sources11
Helixi78 – 80Combined sources3
Beta strandi90 – 92Combined sources3
Beta strandi95 – 105Combined sources11
Beta strandi106 – 110Combined sources5
Beta strandi113 – 122Combined sources10
Beta strandi131 – 140Combined sources10
Helixi146 – 148Combined sources3
Beta strandi150 – 159Combined sources10
Helixi160 – 162Combined sources3
Beta strandi164 – 172Combined sources9
Helixi173 – 176Combined sources4
Turni179 – 181Combined sources3
Beta strandi182 – 185Combined sources4
Beta strandi188 – 197Combined sources10
Beta strandi201 – 203Combined sources3
Turni209 – 211Combined sources3
Turni221 – 224Combined sources4
Helixi225 – 233Combined sources9
Helixi236 – 244Combined sources9
Beta strandi248 – 250Combined sources3
Turni252 – 254Combined sources3
Helixi256 – 269Combined sources14
Helixi277 – 283Combined sources7
Turni288 – 293Combined sources6
Helixi296 – 311Combined sources16
Turni315 – 318Combined sources4
Helixi319 – 324Combined sources6
Beta strandi326 – 338Combined sources13
Beta strandi340 – 352Combined sources13
Helixi360 – 367Combined sources8
Beta strandi371 – 373Combined sources3
Helixi375 – 377Combined sources3
Helixi382 – 384Combined sources3
Beta strandi385 – 387Combined sources3
Beta strandi389 – 397Combined sources9
Beta strandi400 – 406Combined sources7
Beta strandi409 – 412Combined sources4
Turni413 – 415Combined sources3
Beta strandi417 – 420Combined sources4
Beta strandi429 – 432Combined sources4
Helixi434 – 436Combined sources3
Beta strandi437 – 439Combined sources3
Beta strandi442 – 444Combined sources3
Beta strandi447 – 458Combined sources12
Beta strandi460 – 462Combined sources3
Beta strandi464 – 469Combined sources6
Beta strandi473 – 475Combined sources3
Beta strandi477 – 481Combined sources5
Beta strandi484 – 488Combined sources5
Helixi490 – 493Combined sources4
Helixi495 – 497Combined sources3
Turni504 – 506Combined sources3
Turni507 – 510Combined sources4
Beta strandi511 – 520Combined sources10
Helixi521 – 523Combined sources3
Helixi524 – 527Combined sources4
Helixi533 – 535Combined sources3
Helixi538 – 551Combined sources14
Helixi561 – 563Combined sources3
Beta strandi564 – 570Combined sources7
Helixi572 – 574Combined sources3
Turni575 – 577Combined sources3
Beta strandi580 – 584Combined sources5
Beta strandi588 – 597Combined sources10
Helixi602 – 613Combined sources12
Helixi617 – 619Combined sources3
Beta strandi620 – 628Combined sources9
Turni629 – 631Combined sources3
Beta strandi633 – 635Combined sources3
Helixi640 – 643Combined sources4
Beta strandi645 – 647Combined sources3
Helixi648 – 651Combined sources4
Turni652 – 654Combined sources3
Beta strandi656 – 664Combined sources9
Helixi668 – 671Combined sources4
Turni681 – 683Combined sources3
Beta strandi684 – 693Combined sources10
Turni694 – 697Combined sources4
Beta strandi698 – 708Combined sources11
Helixi714 – 716Combined sources3
Helixi717 – 724Combined sources8
Beta strandi732 – 739Combined sources8
Beta strandi742 – 745Combined sources4
Beta strandi749 – 752Combined sources4
Helixi753 – 756Combined sources4
Beta strandi757 – 759Combined sources3
Beta strandi764 – 770Combined sources7
Helixi773 – 777Combined sources5
Beta strandi778 – 780Combined sources3
Helixi783 – 792Combined sources10
Beta strandi793 – 800Combined sources8
Beta strandi809 – 814Combined sources6
Helixi819 – 829Combined sources11
Helixi834 – 836Combined sources3
Beta strandi837 – 840Combined sources4
Beta strandi846 – 848Combined sources3
Helixi861 – 865Combined sources5
Beta strandi866 – 868Combined sources3
Beta strandi870 – 872Combined sources3
Beta strandi875 – 880Combined sources6
Helixi885 – 890Combined sources6
Beta strandi894 – 899Combined sources6
Beta strandi905 – 910Combined sources6
Helixi918 – 928Combined sources11
Beta strandi933 – 935Combined sources3
Beta strandi939 – 945Combined sources7
Beta strandi948 – 953Combined sources6
Helixi959 – 961Combined sources3
Beta strandi969 – 974Combined sources6
Helixi977 – 979Combined sources3
Turni984 – 986Combined sources3
Beta strandi987 – 998Combined sources12
Beta strandi1003 – 1014Combined sources12
Helixi1017 – 1027Combined sources11
Helixi1032 – 1035Combined sources4
Beta strandi1039 – 1044Combined sources6
Beta strandi1047 – 1050Combined sources4
Turni1053 – 1055Combined sources3
Helixi1060 – 1062Combined sources3
Beta strandi1070 – 1072Combined sources3
Beta strandi1076 – 1080Combined sources5

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[»]
5J7TX-ray3.20A211-881[»]
5JTJX-ray3.32A209-554[»]
A1084-1102[»]
5JTVX-ray3.31A/C/E/G207-554[»]
A/C/E/G882-1102[»]
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
Contains 1 MATH domain.PROSITE-ProRule annotation
Contains 1 USP domain.Curated

Phylogenomic databases

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

Family and domain databases

InterProiIPR002083. MATH/TRAF_dom.
IPR001394. Peptidase_C19_UCH.
IPR008974. TRAF-like.
IPR024729. USP7_ICP0-binding_dom.
IPR029346. USP_C.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00917. MATH. 1 hit.
PF00443. UCH. 1 hit.
PF14533. USP7_C2. 1 hit.
PF12436. USP7_ICP0_bdg. 1 hit.
[Graphical view]
SMARTiSM00061. MATH. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50144. MATH. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

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

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

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[»]
5J7TX-ray3.20A211-881[»]
5JTJX-ray3.32A209-554[»]
A1084-1102[»]
5JTVX-ray3.31A/C/E/G207-554[»]
A/C/E/G882-1102[»]
ProteinModelPortaliQ93009.
SMRiQ93009.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113622. 330 interactors.
DIPiDIP-29053N.
IntActiQ93009. 143 interactors.
MINTiMINT-234628.
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.

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.
GeneCardsiUSP7.
H-InvDBHIX0038590.
HGNCiHGNC:12630. USP7.
HPAiCAB008108.
HPA015641.
MIMi602519. gene.
neXtProtiNX_Q93009.
OpenTargetsiENSG00000187555.
PharmGKBiPA37255.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:HS10354-MONOMER.
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.
SignaLinkiQ93009.
SIGNORiQ93009.

Miscellaneous databases

ChiTaRSiUSP7. human.
EvolutionaryTraceiQ93009.
GeneWikiiUSP7.
GenomeRNAii7874.
PROiQ93009.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000187555.
CleanExiHS_USP7.
ExpressionAtlasiQ93009. baseline and differential.
GenevisibleiQ93009. HS.

Family and domain databases

InterProiIPR002083. MATH/TRAF_dom.
IPR001394. Peptidase_C19_UCH.
IPR008974. TRAF-like.
IPR024729. USP7_ICP0-binding_dom.
IPR029346. USP_C.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF00917. MATH. 1 hit.
PF00443. UCH. 1 hit.
PF14533. USP7_C2. 1 hit.
PF12436. USP7_ICP0_bdg. 1 hit.
[Graphical view]
SMARTiSM00061. MATH. 1 hit.
[Graphical view]
SUPFAMiSSF49599. SSF49599. 1 hit.
PROSITEiPS50144. MATH. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUBP7_HUMAN
AccessioniPrimary (citable) accession number: Q93009
Secondary accession number(s): A6NMY8, B7Z815, H0Y3G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 4, 2008
Last modified: November 30, 2016
This is version 184 of the entry and version 2 of the sequence. [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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.