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Q4VSI4

- UBP7_RAT

UniProt

Q4VSI4 - UBP7_RAT

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Protein

Ubiquitin carboxyl-terminal hydrolase 7

Gene
Usp7, Hausp
Organism
Rattus norvegicus (Rat)
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. 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.2 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).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei224 – 2241Nucleophile By similarity
Active sitei465 – 4651Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type endopeptidase activity Source: UniProtKB
  2. protein homodimerization activity Source: RGD
  3. ubiquitin-specific protease activity Source: UniProtKB
  4. ubiquitin thiolesterase activity Source: UniProtKB

GO - Biological processi

  1. maintenance of DNA methylation Source: UniProtKB
  2. multicellular organismal development Source: UniProtKB-KW
  3. positive regulation of apoptotic process Source: RGD
  4. protein deubiquitination Source: UniProtKB
  5. regulation of protein stability Source: RGD
  6. regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  7. transcription-coupled nucleotide-excision repair Source: UniProtKB
  8. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Thiol protease

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

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
Short name:
rHAUSP
Ubiquitin thioesterase 7
Ubiquitin-specific-processing protease 7
Gene namesi
Name:Usp7
Synonyms:Hausp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1306915. Usp7.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity. NucleusPML body By similarity
Note: Present in a minority of ND10 nuclear bodies. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX in speckled structures. Colocalized with PML and PTEN in promyelocytic leukemia protein (PML) nuclear bodies By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  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
Mutagenesisi224 – 2241C → S: Loss of p53/TP53-deubiquitinating activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11031103Ubiquitin carboxyl-terminal hydrolase 7PRO_0000268007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine By similarity
Modified residuei870 – 8701N6-acetyllysine; alternate By similarity
Cross-linki870 – 870Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Modified residuei964 – 9641Phosphoserine By similarity
Modified residuei1085 – 10851N6-acetyllysine By similarity
Modified residuei1097 – 10971N6-acetyllysine By similarity

Post-translational modificationi

Phosphorylated at positions Ser-19 and Ser-964 By similarity.
Polyneddylated.
Not sumoylated By similarity.
Ubiquitinated at Lys-870 By similarity. Polyubiquitinated.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ4VSI4.
PRIDEiQ4VSI4.

PTM databases

PhosphoSiteiQ4VSI4.

Expressioni

Tissue specificityi

Strongly expressed in the testis, spleen and brain. Weakly expressed in the stomach, small intestine, skeletal muscle and uterus.1 Publication

Gene expression databases

GenevestigatoriQ4VSI4.

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. Interacts with MEX3C and antagonizes its ability to degrade mRNA. Interacts with DNMT1 and UHRF1 By similarity.1 Publication

Protein-protein interaction databases

BioGridi261960. 4 interactions.
MINTiMINT-1365534.
STRINGi10116.ENSRNOP00000041134.

Structurei

3D structure databases

ProteinModelPortaliQ4VSI4.
SMRiQ4VSI4. Positions 64-555.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 196128MATHAdd
BLAST
Domaini215 – 522308USPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 209209Interaction with TSPYL5 By similarityAdd
BLAST
Regioni54 – 209156Interaction with p53/TP53 and MDM2 By similarityAdd
BLAST
Regioni71 – 206136Necessary for nuclear localization By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4 – 1714Gln-richAdd
BLAST

Domaini

The C-terminus plays a role in its oligomerization.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5077.
HOGENOMiHOG000160240.
HOVERGENiHBG018029.
InParanoidiQ4VSI4.
KOiK11838.
PhylomeDBiQ4VSI4.

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]

Sequencei

Sequence statusi: Complete.

Q4VSI4-1 [UniParc]FASTAAdd to Basket

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MNHQQQQQQQ QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVALS     50
DGHSNAEEDM EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI 100
MVMPRFYPDR PHQKSVGFFL QCNAESDSTS WSCHAQAVLK IINYRDDDKS 150
FSRRISHLFF HKENDWGFSN FMAWSEVTDP EKGFIDDDKV TFEVFVQADA 200
PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR KAVYMMPTEG 250
DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL 300
CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKEVDY RSDRREDYYD 350
IQLSIKGKKN IFESFVDYVA VEQLDGDNKY DAGEHGLQEA EKGVKFLTLP 400
PVLHLQLMRF MYDPQTDQNI KINDRFEFPE QLPLDEFLQK TDPKDPANYI 450
LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK FDDDVVSRCT KEEAIEHNYG 500
GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ LVERLQEEKR 550
IEAQKRKERQ EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN 600
SSLAEFVQSL SQTMGFPQDQ IRLWPMQARS NGTKRPAMLD NEADGSKTMI 650
ELSDNENPWT IFLETVDPEL AASGATLPKF DKDHDVMLFL KMYDPKTRSL 700
NYCGHIYTPI SCKIRDLLPV MCDRAGFIQD TSLILYEEVK PNLTERIQDY 750
DVSLDKALDE LMDGDIIVFQ KDDPENDNSE LPTAKEYFRD LYHRVDVIFC 800
DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF FKSQGYRDGP 850
GNPLRHNYEG TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL 900
NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGDEASGRL RLLEIVSYKI 950
IGVHQEDELL ECLSPATSRT FRIEEIPLDQ VNIDKENEML ITVAHFHKEV 1000
FGTFGIPFLL RIHQGEHFRE VMKRIQSLLD IQEKEFEKFK FAIVMMGRHQ 1050
YINEDEYEVN LKDFEPQPGN MSHPRPWLGL DHFNKAPKRS RYTYLEKAIK 1100
IHN 1103
Length:1,103
Mass (Da):128,431
Last modified:July 5, 2005 - v1
Checksum:iA542C4149E241C7C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY641530 mRNA. Translation: AAT68666.1.
RefSeqiNP_001019961.1. NM_001024790.1.
UniGeneiRn.72721.

Genome annotation databases

GeneIDi360471.
KEGGirno:360471.
UCSCiRGD:1306915. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY641530 mRNA. Translation: AAT68666.1 .
RefSeqi NP_001019961.1. NM_001024790.1.
UniGenei Rn.72721.

3D structure databases

ProteinModelPortali Q4VSI4.
SMRi Q4VSI4. Positions 64-555.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 261960. 4 interactions.
MINTi MINT-1365534.
STRINGi 10116.ENSRNOP00000041134.

PTM databases

PhosphoSitei Q4VSI4.

Proteomic databases

PaxDbi Q4VSI4.
PRIDEi Q4VSI4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 360471.
KEGGi rno:360471.
UCSCi RGD:1306915. rat.

Organism-specific databases

CTDi 7874.
RGDi 1306915. Usp7.

Phylogenomic databases

eggNOGi COG5077.
HOGENOMi HOG000160240.
HOVERGENi HBG018029.
InParanoidi Q4VSI4.
KOi K11838.
PhylomeDBi Q4VSI4.

Miscellaneous databases

NextBioi 672877.
PROi Q4VSI4.

Gene expression databases

Genevestigatori Q4VSI4.

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

  1. "HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerized."
    Lee H.-J., Kim M.-S., Kim Y.-K., Oh Y.-K., Baek K.-H.
    FEBS Lett. 579:4867-4872(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-224, POLYUBIQUITINATION, POLYNEDDYLATION.
    Tissue: Testis.
  2. "Molecular cloning of rHAUSP encoding a deubiquitinating enzyme in rat testis."
    Baek K.H., Lee H.J., Kim M.S., Kim Y.S., Seong M., Lee E.J., Lee M.Y.
    Oncol. Rep. 15:173-177(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION, MUTAGENESIS OF CYS-224.
    Tissue: Testis.

Entry informationi

Entry nameiUBP7_RAT
AccessioniPrimary (citable) accession number: Q4VSI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: July 5, 2005
Last modified: June 11, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi