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Q4VSI4

- UBP7_RAT

UniProt

Q4VSI4 - UBP7_RAT

Protein

Ubiquitin carboxyl-terminal hydrolase 7

Gene

Usp7

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (05 Jul 2005)
      Previous versions | rss
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    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 – 2241NucleophilePROSITE-ProRule annotation
    Active sitei465 – 4651Proton acceptorPROSITE-ProRule annotation

    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

    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.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB
    3. PML body Source: UniProtKB-SubCell

    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 – 191PhosphoserineBy similarity
    Modified residuei870 – 8701N6-acetyllysine; alternateBy similarity
    Cross-linki870 – 870Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
    Modified residuei964 – 9641PhosphoserineBy similarity
    Modified residuei1085 – 10851N6-acetyllysineBy similarity
    Modified residuei1097 – 10971N6-acetyllysineBy 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.By similarity2 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.By similarity

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ4VSI4.
    SMRiQ4VSI4. Positions 64-555.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini69 – 196128MATHPROSITE-ProRule annotationAdd
    BLAST
    Domaini215 – 522308USPAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 209209Interaction with TSPYL5By similarityAdd
    BLAST
    Regioni54 – 209156Interaction with p53/TP53 and MDM2By similarityAdd
    BLAST
    Regioni71 – 206136Necessary for nuclear localizationBy 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.Curated
    Contains 1 MATH domain.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    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: October 1, 2014
    This is version 68 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