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Q6A4J8

- UBP7_MOUSE

UniProt

Q6A4J8 - UBP7_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 7

Gene

Usp7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (13 Sep 2004)
      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.3 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 binding Source: UniProtKB
    3. ubiquitin-specific protease activity Source: UniProtKB
    4. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. multicellular organismal development Source: UniProtKB-KW
    2. protein deubiquitination Source: UniProtKB
    3. regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    4. transcription-coupled nucleotide-excision repair Source: UniProtKB
    5. 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

    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
    Short name:
    mHAUSP
    Ubiquitin thioesterase 7
    Ubiquitin-specific-processing protease 7
    Gene namesi
    Name:Usp7
    Synonyms:Hausp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:2182061. Usp7.

    Subcellular locationi

    Nucleus 1 Publication. 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: MGI
    2. nucleus Source: UniProtKB
    3. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Led to early embryonic lethality. Show disorganized germinal layers without the formation of a proamniotic cavity. Many of the surviving cells were trophoblastic giant cells with large nuclei.1 Publication

    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_0000268006Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Phosphoserine1 Publication
    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.By similarity
    Not sumoylated.By similarity
    Polyubiquitinated. Ubiquitinated at Lys-870 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ6A4J8.
    PaxDbiQ6A4J8.
    PRIDEiQ6A4J8.

    PTM databases

    PhosphoSiteiQ6A4J8.

    Expressioni

    Tissue specificityi

    Expressed at high levels in brain, lung, thymus and testis. Expressed at low levels in the liver.1 Publication

    Developmental stagei

    Expressed in embryo at 3.5 and from 7.5 to 10.5 dpc (at protein level).

    Gene expression databases

    CleanExiMM_USP7.
    GenevestigatoriQ6A4J8.

    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 By similarity. Interacts with p53/TP53. Interacts with DNMT1 and UHRF1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi232963. 4 interactions.
    DIPiDIP-38603N.
    IntActiQ6A4J8. 2 interactions.
    MINTiMINT-4139284.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6A4J8.
    SMRiQ6A4J8. Positions 64-555, 561-1084.
    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.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

    eggNOGiCOG5077.
    HOGENOMiHOG000160240.
    HOVERGENiHBG018029.
    KOiK11838.
    PhylomeDBiQ6A4J8.

    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: Q6A4J8-1) [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 QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVTLS     50
    DGHSNAEEDM EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI 100
    MVMPRFYPDR PHQKSVGFFL QCNAESDSTS WSCHAQAVLK IINYRDDDKS 150
    FSRRISHLFF HEENDWGFSN FMAWSEVTDP EKGFIDDDKV TFEVFVQADA 200
    PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR KAVYMMPTEG 250
    DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL 300
    CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKDVDY 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 NEADGNKTMI 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 ELGDKASGRL RLLEIVSYKI 950
    IGVHQEDELL ECLSPATSRT FRIEEIPLDQ VDIDKENEML ITVAHFHKEV 1000
    FGTFGIPFLL RIHQGEHFRE VMKRIQSLLD IQEKEFEKFK FAIVMMGRHQ 1050
    YINEDEYEVN LKDFEPQPGN MSHPRPWLGL DHFNKAPKRS RYTYLEKAIK 1100
    IHN 1103
    Length:1,103
    Mass (Da):128,475
    Last modified:September 13, 2004 - v1
    Checksum:i989DFE733F0D961E
    GO
    Isoform 2 (identifier: Q6A4J8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-27: MNHQQQQQQQQKAGEQQLSEPEDMEME → MASSTSPPRS...CPWNEGIEYQ

    Show »
    Length:1,143
    Mass (Da):132,749
    Checksum:i38F6764A2D063600
    GO
    Isoform 3 (identifier: Q6A4J8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         974-974: E → ECLQ
         1094-1103: YLEKAIKIHN → LGLC

    Show »
    Length:1,100
    Mass (Da):127,996
    Checksum:i3E5FE589370B8006
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621E → K in BAE22671. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2727MNHQQ…DMEME → MASSTSPPRSPSGGILTQDT IYFPQSNIISELLPWYLRYT PPEVPSTSVITKFILVNCPW NEGIEYQ in isoform 2. 1 PublicationVSP_021952Add
    BLAST
    Alternative sequencei974 – 9741E → ECLQ in isoform 3. 1 PublicationVSP_021953
    Alternative sequencei1094 – 110310YLEKAIKIHN → LGLC in isoform 3. 1 PublicationVSP_021954

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF548565 mRNA. Translation: AAQ12339.1.
    AK075830 mRNA. Translation: BAC35992.1.
    AK135814 mRNA. Translation: BAE22671.1.
    BC100666 mRNA. Translation: AAI00667.1.
    CCDSiCCDS49755.1. [Q6A4J8-1]
    RefSeqiNP_001003918.2. NM_001003918.2.
    UniGeneiMm.295330.

    Genome annotation databases

    GeneIDi252870.
    KEGGimmu:252870.
    UCSCiuc007ycx.1. mouse. [Q6A4J8-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF548565 mRNA. Translation: AAQ12339.1 .
    AK075830 mRNA. Translation: BAC35992.1 .
    AK135814 mRNA. Translation: BAE22671.1 .
    BC100666 mRNA. Translation: AAI00667.1 .
    CCDSi CCDS49755.1. [Q6A4J8-1 ]
    RefSeqi NP_001003918.2. NM_001003918.2.
    UniGenei Mm.295330.

    3D structure databases

    ProteinModelPortali Q6A4J8.
    SMRi Q6A4J8. Positions 64-555, 561-1084.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 232963. 4 interactions.
    DIPi DIP-38603N.
    IntActi Q6A4J8. 2 interactions.
    MINTi MINT-4139284.

    Protein family/group databases

    MEROPSi C19.016.

    PTM databases

    PhosphoSitei Q6A4J8.

    Proteomic databases

    MaxQBi Q6A4J8.
    PaxDbi Q6A4J8.
    PRIDEi Q6A4J8.

    Protocols and materials databases

    DNASUi 252870.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 252870.
    KEGGi mmu:252870.
    UCSCi uc007ycx.1. mouse. [Q6A4J8-1 ]

    Organism-specific databases

    CTDi 7874.
    MGIi MGI:2182061. Usp7.

    Phylogenomic databases

    eggNOGi COG5077.
    HOGENOMi HOG000160240.
    HOVERGENi HBG018029.
    KOi K11838.
    PhylomeDBi Q6A4J8.

    Miscellaneous databases

    ChiTaRSi USP7. mouse.
    NextBioi 387363.
    PROi Q6A4J8.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_USP7.
    Genevestigatori Q6A4J8.

    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. "Identification and characterization of murine mHAUSP encoding a deubiquitinating enzyme that regulates the status of p53 ubiquitination."
      Lim S.-K., Shin J.-M., Kim Y.-S., Baek K.-H.
      Int. J. Oncol. 24:357-364(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH TP53, MUTAGENESIS OF CYS-224.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-545 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 832-1103.
      Strain: C57BL/6J.
      Tissue: Egg and Stomach.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 214-1103 (ISOFORM 3).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "Inactivation of HAUSP in vivo modulates p53 function."
      Kon N., Kobayashi Y., Li M., Brooks C.L., Ludwig T., Gu W.
      Oncogene 29:1270-1279(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    6. "Usp7 and Uhrf1 control ubiquitination and stability of the maintenance DNA methyltransferase Dnmt1."
      Qin W., Leonhardt H., Spada F.
      J. Cell. Biochem. 112:439-444(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DNMT1 AND UHRF1, MUTAGENESIS OF CYS-224.

    Entry informationi

    Entry nameiUBP7_MOUSE
    AccessioniPrimary (citable) accession number: Q6A4J8
    Secondary accession number(s): Q3UX92, Q496Y5, Q8BW01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: September 13, 2004
    Last modified: October 1, 2014
    This is version 84 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3