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Q93009

- UBP7_HUMAN

UniProt

Q93009 - UBP7_HUMAN

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Protein

Ubiquitin carboxyl-terminal hydrolase 7

Gene
USP7, HAUSP
Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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. 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. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains.13 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).

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei223 – 2231Nucleophile
Active sitei464 – 4641Proton acceptor Inferred

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. p53 binding Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. protein C-terminus binding Source: UniProtKB
  5. transcription factor binding Source: UniProtKB
  6. ubiquitin protein ligase binding Source: UniProtKB
  7. ubiquitin-specific protease activity Source: UniProtKB
  8. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. maintenance of DNA methylation Source: UniProtKB
  2. multicellular organismal development Source: UniProtKB-KW
  3. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  4. protein deubiquitination Source: UniProtKB
  5. regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  6. transcription-coupled nucleotide-excision repair Source: UniProtKB
  7. ubiquitin-dependent protein catabolic process Source: InterPro
  8. 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

SignaLinkiQ93009.

Protein family/group databases

MEROPSiC19.016.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 7 (EC:3.4.19.12)
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
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:12630. USP7.

Subcellular locationi

Nucleus. Cytoplasm. NucleusPML body
Note: Present in a minority of ND10 nuclear bodies. Association with ICP0/VMW110 at early times of infection leads to an increased proportion of USP7-containing ND10. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX in speckled structures. Colocalized with PML and PTEN in promyelocytic leukemia protein (PML) nuclear bodies.5 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi164 – 1641D → A: Decreased binding to p53/TP53 and MDM2. 1 Publication
Mutagenesisi165 – 1651W → A: Loss of binding to p53/TP53 and MDM2. 1 Publication
Mutagenesisi223 – 2231C → A: Complete loss of activity. Localized in the nucleus and does not inhibit FOXO4-dependent transcriptional activity. 7 Publications
Mutagenesisi223 – 2231C → S: No effect on p53/TP53 and PTEN binding but is defective in deubiquitinating p53/TP53 and PTEN. 7 Publications
Mutagenesisi456 – 4561H → A: Complete loss of activity. 1 Publication
Mutagenesisi464 – 4641H → A: Complete loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA37255.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11021102Ubiquitin carboxyl-terminal hydrolase 7PRO_0000080626Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphoserine4 Publications
Modified residuei869 – 8691N6-acetyllysine; alternate1 Publication
Cross-linki869 – 869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei963 – 9631Phosphoserine2 Publications
Modified residuei1084 – 10841N6-acetyllysine1 Publication
Modified residuei1096 – 10961N6-acetyllysine1 Publication

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

MaxQBiQ93009.
PaxDbiQ93009.
PRIDEiQ93009.

PTM databases

PhosphoSiteiQ93009.

Expressioni

Tissue specificityi

Widely expressed. Overexpressed in prostate cancer.1 Publication

Gene expression databases

ArrayExpressiQ93009.
BgeeiQ93009.
CleanExiHS_USP7.
GenevestigatoriQ93009.

Organism-specific databases

HPAiCAB008108.
HPA015641.

Interactioni

Subunit structurei

Monomer. Homodimer. Part of a complex with DAXX, MDM2, RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7. Interacts with MDM2; the interaction is independent of p53/TP53. Interacts with DAXX; the interaction is direct and independent of MDM2 and p53/TP53. Interacts with FOXO4; the interaction is enhanced in presence of hydrogen peroxide and occurs independently of p53/TP53. Interacts with p53/TP53; the interaction is enhanced in response to DNA damage; the interaction is impaired by TSPYL5. Interacts with PTEN; the interaction is direct. Interacts with UBXN6. 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. Interacts with KIAA1530/UVSSA. Isoform 1 and isoform 2 interact with herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110. Interacts with Epstein-Barr virus EBNA1. EBNA1 shows a 10-fold higher affinity than p53/TP53 and can compete with it for USP7 binding. 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. Interacts with DNMT1 and UHRF1.22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BMI1P352267EBI-302474,EBI-2341576
CBX8Q9HC527EBI-302474,EBI-712912
DAXXQ9UER713EBI-302474,EBI-77321
EBNA1P032114EBI-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
RING1Q065874EBI-302474,EBI-752313
RNF2Q994964EBI-302474,EBI-722416
SMAD3P840222EBI-302474,EBI-347161
TBCBQ994262EBI-302474,EBI-764356
TP53P0463717EBI-302474,EBI-366083
TSPYL5Q86VY44EBI-302474,EBI-3436472

Protein-protein interaction databases

BioGridi113622. 198 interactions.
DIPiDIP-29053N.
IntActiQ93009. 105 interactions.
MINTiMINT-234628.
STRINGi9606.ENSP00000343535.

Structurei

Secondary structure

1
1102
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi67 – 7711
Helixi78 – 803
Beta strandi90 – 923
Beta strandi95 – 10410
Beta strandi113 – 12210
Beta strandi131 – 14010
Helixi146 – 1483
Beta strandi150 – 15910
Helixi160 – 1623
Beta strandi164 – 1729
Helixi173 – 1764
Turni179 – 1813
Beta strandi182 – 1854
Beta strandi188 – 19710
Beta strandi201 – 2033
Turni209 – 2113
Turni221 – 2244
Helixi225 – 2339
Helixi236 – 2449
Turni252 – 2543
Helixi256 – 26914
Helixi277 – 2837
Turni288 – 2936
Helixi296 – 31116
Turni315 – 3184
Helixi319 – 3246
Beta strandi326 – 33813
Beta strandi340 – 35213
Helixi360 – 3678
Beta strandi371 – 3733
Helixi375 – 3773
Helixi382 – 3843
Beta strandi389 – 3979
Beta strandi400 – 4067
Beta strandi409 – 4124
Turni413 – 4153
Beta strandi417 – 4204
Beta strandi429 – 4324
Helixi434 – 4363
Beta strandi437 – 4393
Beta strandi442 – 4443
Beta strandi447 – 45812
Beta strandi460 – 4623
Beta strandi464 – 4696
Beta strandi473 – 4753
Beta strandi477 – 4815
Beta strandi484 – 4885
Helixi490 – 4934
Helixi495 – 4973
Turni507 – 5104
Beta strandi511 – 52010
Helixi521 – 5233
Helixi524 – 5274
Helixi533 – 5353
Helixi538 – 55114
Helixi561 – 5633
Beta strandi564 – 5718
Helixi572 – 5754
Beta strandi580 – 5834
Turni586 – 5883
Beta strandi592 – 5976
Helixi602 – 61312
Helixi617 – 6193
Beta strandi620 – 6278
Beta strandi633 – 6353
Helixi640 – 6434
Beta strandi645 – 6473
Helixi648 – 6525
Beta strandi656 – 6649
Helixi667 – 6704
Turni671 – 6733
Turni681 – 6833
Beta strandi684 – 69310
Turni694 – 6974
Beta strandi698 – 70811
Helixi713 – 7153
Helixi717 – 7248
Beta strandi732 – 7398
Beta strandi742 – 7454
Beta strandi749 – 7524
Helixi753 – 7564
Beta strandi764 – 7707
Helixi773 – 7775
Beta strandi778 – 7803
Helixi783 – 79210
Beta strandi793 – 8008
Beta strandi809 – 8146
Helixi819 – 83012
Helixi834 – 8363
Beta strandi837 – 8404
Helixi861 – 8644
Beta strandi870 – 8723
Beta strandi875 – 8806
Helixi885 – 8895
Beta strandi894 – 8996
Beta strandi905 – 9106
Helixi918 – 9269
Beta strandi939 – 9457
Beta strandi948 – 9536
Helixi959 – 9613
Beta strandi969 – 9746
Helixi977 – 9793
Turni984 – 9863
Beta strandi987 – 99812
Beta strandi1002 – 101211
Helixi1017 – 102812
Helixi1032 – 10354
Beta strandi1039 – 10446
Beta strandi1047 – 10504
Turni1053 – 10553
Helixi1060 – 10623
Beta strandi1070 – 10723
Beta strandi1076 – 10805

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ93009.
SMRiQ93009. Positions 63-554, 560-1083.

Miscellaneous databases

EvolutionaryTraceiQ93009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 195128MATHAdd
BLAST
Domaini214 – 521308USPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 208208Interaction with TSPYL5Add
BLAST
Regioni53 – 208156Interaction with p53/TP53, MDM2 and EBNA1Add
BLAST
Regioni70 – 205136Necessary for nuclear localizationAdd
BLAST
Regioni622 – 801180Interaction with ICP0/VMW110Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 107Poly-Gln

Domaini

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

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 MATH domain.
Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5077.
HOGENOMiHOG000160240.
HOVERGENiHBG018029.
KOiK11838.
OMAiAMSDGHN.
OrthoDBiEOG75B84G.
PhylomeDBiQ93009.
TreeFamiTF105667.

Family and domain databases

InterProiIPR002083. MATH.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR008974. TRAF-like.
IPR028889. UCH/PAN2.
IPR024729. USP7_ICP0-binding_dom.
IPR029346. USP_C.
[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. Align

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

MNHQQQQQQQ KAGEQQLSEP EDMEMEAGDT DDPPRITQNP VINGNVALSD     50
GHNTAEEDME DDTSWRSEAT FQFTVERFSR LSESVLSPPC FVRNLPWKIM 100
VMPRFYPDRP HQKSVGFFLQ CNAESDSTSW SCHAQAVLKI INYRDDEKSF 150
SRRISHLFFH KENDWGFSNF MAWSEVTDPE KGFIDDDKVT FEVFVQADAP 200
HGVAWDSKKH TGYVGLKNQG ATCYMNSLLQ TLFFTNQLRK AVYMMPTEGD 250
DSSKSVPLAL QRVFYELQHS DKPVGTKKLT KSFGWETLDS FMQHDVQELC 300
RVLLDNVENK MKGTCVEGTI PKLFRGKMVS YIQCKEVDYR SDRREDYYDI 350
QLSIKGKKNI FESFVDYVAV EQLDGDNKYD AGEHGLQEAE KGVKFLTLPP 400
VLHLQLMRFM YDPQTDQNIK INDRFEFPEQ LPLDEFLQKT DPKDPANYIL 450
HAVLVHSGDN HGGHYVVYLN PKGDGKWCKF DDDVVSRCTK EEAIEHNYGG 500
HDDDLSVRHC TNAYMLVYIR ESKLSEVLQA VTDHDIPQQL VERLQEEKRI 550
EAQKRKERQE AHLYMQVQIV AEDQFCGHQG NDMYDEEKVK YTVFKVLKNS 600
SLAEFVQSLS QTMGFPQDQI RLWPMQARSN GTKRPAMLDN EADGNKTMIE 650
LSDNENPWTI FLETVDPELA ASGATLPKFD KDHDVMLFLK MYDPKTRSLN 700
YCGHIYTPIS CKIRDLLPVM CDRAGFIQDT SLILYEEVKP NLTERIQDYD 750
VSLDKALDEL MDGDIIVFQK DDPENDNSEL PTAKEYFRDL YHRVDVIFCD 800
KTIPNDPGFV VTLSNRMNYF QVAKTVAQRL NTDPMLLQFF KSQGYRDGPG 850
NPLRHNYEGT LRDLLQFFKP RQPKKLYYQQ LKMKITDFEN RRSFKCIWLN 900
SQFREEEITL YPDKHGCVRD LLEECKKAVE LGEKASGKLR LLEIVSYKII 950
GVHQEDELLE CLSPATSRTF RIEEIPLDQV DIDKENEMLV TVAHFHKEVF 1000
GTFGIPFLLR IHQGEHFREV MKRIQSLLDI QEKEFEKFKF AIVMMGRHQY 1050
INEDEYEVNL KDFEPQPGNM SHPRPWLGLD HFNKAPKRSR YTYLEKAIKI 1100
HN 1102
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525MNHQQ…EDMEM → MAGNHRLGL in isoform 3. VSP_054884Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011H → I AA sequence 1 Publication
Sequence conflicti205 – 2051W → P AA sequence 1 Publication
Sequence conflicti207 – 2071S → Q AA sequence 1 Publication
Sequence conflicti1045 – 10451M → T in CAA96580. 1 Publication
Sequence conflicti1066 – 10661Q → T AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_003461.2. NM_003470.2. [Q93009-1]
UniGeneiHs.386939.

Genome annotation databases

EnsembliENST00000344836; ENSP00000343535; ENSG00000187555. [Q93009-1]
ENST00000381886; ENSP00000371310; ENSG00000187555.
GeneIDi7874.
KEGGihsa:7874.
UCSCiuc002czl.2. human. [Q93009-1]

Polymorphism databases

DMDMi212276477.

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:
EMBL
GenBank
DDBJ
Links Updated
Z72499 mRNA. Translation: CAA96580.1 .
AK302771 mRNA. Translation: BAH13801.1 .
AC022167 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85194.1 .
CCDSi CCDS32385.1. [Q93009-1 ]
CCDS66941.1. [Q93009-3 ]
RefSeqi NP_003461.2. NM_003470.2. [Q93009-1 ]
UniGenei Hs.386939.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NB8 X-ray 2.30 A/B 208-560 [» ]
1NBF X-ray 2.30 A/B/E 208-560 [» ]
1YY6 X-ray 1.70 A 54-204 [» ]
1YZE X-ray 2.00 A/B/C 54-205 [» ]
2F1W X-ray 1.65 A 53-206 [» ]
2F1X X-ray 2.30 A/B 53-200 [» ]
2F1Y X-ray 1.70 A 53-198 [» ]
2F1Z X-ray 3.20 A/B 43-560 [» ]
2FOJ X-ray 1.60 A 54-205 [» ]
2FOO X-ray 2.20 A 54-205 [» ]
2FOP X-ray 2.10 A 54-205 [» ]
2KVR NMR - A 537-664 [» ]
2XXN X-ray 1.60 A 63-205 [» ]
2YLM X-ray 2.70 A 560-1084 [» ]
3MQR X-ray 1.80 A 54-205 [» ]
3MQS X-ray 2.40 C 54-205 [» ]
4JJQ X-ray 1.95 A 54-205 [» ]
4KG9 X-ray 1.70 A 54-205 [» ]
4M5W X-ray 2.24 A 207-560 [» ]
4M5X X-ray 2.19 A/B 207-560 [» ]
4PYZ X-ray 2.84 A/B 537-793 [» ]
ProteinModelPortali Q93009.
SMRi Q93009. Positions 63-554, 560-1083.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113622. 198 interactions.
DIPi DIP-29053N.
IntActi Q93009. 105 interactions.
MINTi MINT-234628.
STRINGi 9606.ENSP00000343535.

Chemistry

ChEMBLi CHEMBL2157850.

Protein family/group databases

MEROPSi C19.016.

PTM databases

PhosphoSitei Q93009.

Polymorphism databases

DMDMi 212276477.

Proteomic databases

MaxQBi Q93009.
PaxDbi Q93009.
PRIDEi Q93009.

Protocols and materials databases

DNASUi 7874.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000344836 ; ENSP00000343535 ; ENSG00000187555 . [Q93009-1 ]
ENST00000381886 ; ENSP00000371310 ; ENSG00000187555 .
GeneIDi 7874.
KEGGi hsa:7874.
UCSCi uc002czl.2. human. [Q93009-1 ]

Organism-specific databases

CTDi 7874.
GeneCardsi GC16M008985.
H-InvDB HIX0038590.
HGNCi HGNC:12630. USP7.
HPAi CAB008108.
HPA015641.
MIMi 602519. gene.
neXtProti NX_Q93009.
PharmGKBi PA37255.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5077.
HOGENOMi HOG000160240.
HOVERGENi HBG018029.
KOi K11838.
OMAi AMSDGHN.
OrthoDBi EOG75B84G.
PhylomeDBi Q93009.
TreeFami TF105667.

Enzyme and pathway databases

SignaLinki Q93009.

Miscellaneous databases

EvolutionaryTracei Q93009.
GeneWikii USP7.
GenomeRNAii 7874.
NextBioi 30332.
PROi Q93009.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q93009.
Bgeei Q93009.
CleanExi HS_USP7.
Genevestigatori Q93009.

Family and domain databases

InterProi IPR002083. MATH.
IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR008974. TRAF-like.
IPR028889. UCH/PAN2.
IPR024729. USP7_ICP0-binding_dom.
IPR029346. USP_C.
[Graphical view ]
Pfami PF00917. MATH. 1 hit.
PF00443. UCH. 1 hit.
PF14533. USP7_C2. 1 hit.
PF12436. USP7_ICP0_bdg. 1 hit.
[Graphical view ]
SMARTi SM00061. MATH. 1 hit.
[Graphical view ]
SUPFAMi SSF49599. SSF49599. 1 hit.
PROSITEi PS50144. MATH. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein."
    Everett R.D., Meredith M., Orr A., Cross A., Kathoria M., Parkinson J.
    EMBO J. 16:566-577(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    Tissue: Mammary cancer.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Testis.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product."
    Hong S., Kim S.J., Ka S., Choi I., Kang S.
    Mol. Cell. Neurosci. 20:298-306(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 705-1102 (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH ATXN1.
  6. "Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization."
    Li M., Chen D., Shiloh A., Luo J., Nikolaev A.Y., Qin J., Gu W.
    Nature 416:648-653(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53, MUTAGENESIS OF CYS-223.
  7. "Protein interaction domains of the ubiquitin-specific protease, USP7/HAUSP."
    Holowaty M.N., Sheng Y., Nguyen T., Arrowsmith C., Frappier L.
    J. Biol. Chem. 278:47753-47761(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INTERACTION WITH HERPESVIRUS 1 TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110 AND EBV EBNA1.
  8. "A dynamic role of HAUSP in the p53-Mdm2 pathway."
    Li M., Brooks C.L., Kon N., Gu W.
    Mol. Cell 13:879-886(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MDM2, MUTAGENESIS OF CYS-223.
  9. "Reciprocal activities between herpes simplex virus type 1 regulatory protein ICP0, a ubiquitin E3 ligase, and ubiquitin-specific protease USP7."
    Boutell C., Canning M., Orr A., Everett R.D.
    J. Virol. 79:12342-12354(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH HERPESVIRUS 1 TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110.
  10. Cited for: IDENTIFICATION IN A COMPLEX WITH DAXX AND MDM2, INTERACTION WITH DAXX, SUBCELLULAR LOCATION.
  11. Cited for: FUNCTION, INTERACTION WITH FOXO4, MUTAGENESIS OF CYS-223.
  12. "Biochemical characterization of USP7 reveals post-translational modification sites and structural requirements for substrate processing and subcellular localization."
    Fernandez-Montalvan A., Bouwmeester T., Joberty G., Mader R., Mahnke M., Pierrat B., Schlaeppi J.M., Worpenberg S., Gerhartz B.
    FEBS J. 274:4256-4270(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, PHOSPHORYLATION AT SER-18 AND SER-963, UBIQUITINATION AT LYS-869, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex."
    Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.
    EMBO J. 27:1863-1874(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH DAXX; RASSF1 AND MDM2, INTERACTION WITH DAXX AND MDM2.
  14. "AAA ATPase p97 and adaptor UBXD1 suppress MDM2 ubiquitination and degradation and promote constitutive p53 turnover."
    Zweitzig D.R., Shcherbik N., Haines D.S.
    Mol. Biol. Cell 19:5029-5029(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBXN6.
  15. "The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network."
    Song M.S., Salmena L., Carracedo A., Egia A., Lo-Coco F., Teruya-Feldstein J., Pandolfi P.P.
    Nature 455:813-817(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PTEN, MUTAGENESIS OF CYS-223, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-963, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Identification of a novel higher molecular weight isoform of USP7/HAUSP that interacts with the Herpes simplex virus type-1 immediate early protein ICP0."
    Antrobus R., Boutell C.
    Virus Res. 137:64-71(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HERPESVIRUS 1 TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE SPLICING (ISOFORM 2).
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-869; LYS-1084 AND LYS-1096, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Daxx is reciprocally regulated by Mdm2 and Hausp."
    Tang J., Qu L., Pang M., Yang X.
    Biochem. Biophys. Res. Commun. 393:542-545(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "TSPYL5 suppresses p53 levels and function by physical interaction with USP7."
    Epping M.T., Meijer L.A., Krijgsman O., Bos J.L., Pandolfi P.P., Bernards R.
    Nat. Cell Biol. 13:102-108(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSPYL5.
  24. "The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 and regulates the stability of UHRF1."
    Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V., Dobner T., Kremmer E., Kappler R., Langst G.
    Nucleic Acids Res. 39:8355-8365(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DNMT1 AND UHRF1, MUTAGENESIS OF CYS-223.
  25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "M phase phosphorylation of the epigenetic regulator UHRF1 regulates its physical association with the deubiquitylase USP7 and stability."
    Ma H., Chen H., Guo X., Wang Z., Sowa M.E., Zheng L., Hu S., Zeng P., Guo R., Diao J., Lan F., Harper J.W., Shi Y.G., Xu Y., Shi Y.
    Proc. Natl. Acad. Sci. U.S.A. 109:4828-4833(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UHRF1, MUTAGENESIS OF CYS-223.
  27. "Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes."
    Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., Frank R., van den Heuvel J., Kessler B.M., Jansch L., Franke R.
    ChemBioChem 13:1416-1420(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, LINKAGE SPECIFICITY.
  28. "The RNA-binding E3 ubiquitin ligase MEX-3C links ubiquitination with MHC-I mRNA degradation."
    Cano F., Bye H., Duncan L.M., Buchet-Poyau K., Billaud M., Wills M.R., Lehner P.J.
    EMBO J. 31:3596-3606(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEX3C.
  29. Cited for: FUNCTION, INTERACTION WITH UVSSA.
  30. "Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in transcription-coupled DNA repair."
    Zhang X., Horibata K., Saijo M., Ishigami C., Ukai A., Kanno S.I., Tahara H., Neilan E.G., Honma M., Nohmi T., Yasui A., Tanaka K.
    Nat. Genet. 44:593-597(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UVSSA.
  31. "Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde."
    Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E., Shi Y.
    Cell 111:1041-1054(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 208-560 IN COMPLEX WITH UBIQUITIN, MUTAGENESIS OF CYS-223; HIS-456 AND HIS-464, INTERACTION WITH TP53.
  32. "Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization."
    Saridakis V., Sheng Y., Sarkari F., Holowaty M.N., Shire K., Nguyen T., Zhang R.G., Liao J., Lee W., Edwards A.M., Arrowsmith C.H., Frappier L.
    Mol. Cell 18:25-36(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 54-205 IN COMPLEX WITH EBNA1, INTERACTION WITH EBV EBNA1.
  33. "Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway."
    Hu M., Gu L., Li M., Jeffrey P.D., Gu W., Shi Y.
    PLoS Biol. 4:228-239(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 43-560 IN COMPLEX WITH TP53 AND MDM2, INTERACTION WITH TP53 AND MDM2.
  34. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 54-205 IN COMPLEX WITH TP53 AND MDM2, INTERACTION WITH TP53 AND MDM2, MUTAGENESIS OF ASP-164 AND TRP-165.

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: September 3, 2014
This is version 158 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

External Data

Dasty 3

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