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Q80Z37

- TOPRS_MOUSE

UniProt

Q80Z37 - TOPRS_MOUSE

Protein

E3 ubiquitin-protein ligase Topors

Gene

Topors

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Functions as an E3 ubiquitin-protein ligase and as a E3 SUMO1-protein ligase. Probable tumor suppressor involved in cell growth, cell proliferation and apoptosis that regulates p53/TP53 stability through ubiquitin-dependent degradation. May regulate chromatin modification through sumoylation of several chromatin modification-associated proteins. May be involved in DNA-damage-induced cell death through IKBKE sumoylation.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri104 – 14340RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. antigen binding Source: Ensembl
    2. DNA binding Source: Ensembl
    3. protein binding Source: MGI
    4. SUMO ligase activity Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: UniProtKB
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
    3. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
    4. maintenance of protein location in nucleus Source: Ensembl
    5. positive regulation of transcription, DNA-templated Source: MGI
    6. positive regulation of ubiquitin-protein transferase activity Source: Ensembl
    7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    8. protein K48-linked ubiquitination Source: Ensembl
    9. protein localization to nucleus Source: UniProtKB
    10. protein monoubiquitination Source: Ensembl
    11. protein sumoylation Source: UniProtKB
    12. regulation of cell proliferation Source: MGI
    13. ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    DNA damage, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase Topors (EC:6.3.2.-)
    Alternative name(s):
    SUMO1-protein E3 ligase Topors
    Topoisomerase I-binding RING finger protein
    Topoisomerase I-binding arginine/serine-rich protein
    Tumor suppressor p53-binding protein 3
    Short name:
    p53-binding protein 3
    Short name:
    p53BP3
    Gene namesi
    Name:Topors
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:2146189. Topors.

    Subcellular locationi

    Nucleus 2 Publications. NucleusPML body By similarity
    Note: Localizes to discrete nuclear foci which partly overlap with PML nuclear bodies. Targeted to PML nuclear bodies upon DNA damage By similarity.By similarity

    GO - Cellular componenti

    1. centriole Source: Ensembl
    2. ciliary basal body Source: BHF-UCL
    3. gamma-tubulin complex Source: Ensembl
    4. nuclear speck Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. photoreceptor connecting cilium Source: BHF-UCL
    7. PML body Source: UniProtKB
    8. spindle pole Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10331033E3 ubiquitin-protein ligase ToporsPRO_0000232627Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei99 – 991PhosphoserineBy similarity
    Modified residuei500 – 5001PhosphoserineBy similarity
    Cross-linki561 – 561Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei585 – 5851PhosphoserineBy similarity
    Modified residuei718 – 7181Phosphoserine; by PLK1By similarity
    Modified residuei861 – 8611PhosphoserineBy similarity
    Modified residuei863 – 8631PhosphoserineBy similarity
    Modified residuei1016 – 10161Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation at Ser-99 regulates the E3 ubiquitin-protein ligase activity but not the SUMO1-protein ligase activity. Phosphorylation at Ser-718 increases the E3 ubiquitin-protein ligase activity versus the E3 SUMO1-protein ligase activity resulting in increased p53/TP53 ubiquitination and degradation By similarity.By similarity
    Sumoylated.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ80Z37.

    PTM databases

    PhosphoSiteiQ80Z37.

    Expressioni

    Inductioni

    By genotoxic agents such as cisplatin and camptothecin.1 Publication

    Gene expression databases

    BgeeiQ80Z37.
    CleanExiMM_TOPORS.
    GenevestigatoriQ80Z37.

    Interactioni

    Subunit structurei

    Interacts with TOP1. Interacts with the SUMO1 conjugating enzyme UBE2I. Interacts with SUMO1. Interacts with NKX3-1; polyubiquitinates NKX3-1 and induces its proteasomal degradation. Interacts with SIN3A; sumoylates SIN3A. Interacts with IKBKE; induced by DNA damage By similarity. Interacts with p53/TP53. Interacts with PARK7/DJ-1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi222976. 2 interactions.
    IntActiQ80Z37. 1 interaction.
    MINTiMINT-1789728.
    STRINGi10090.ENSMUSP00000046843.

    Structurei

    3D structure databases

    ProteinModelPortaliQ80Z37.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni52 – 376325Required for DNA-bindingBy similarityAdd
    BLAST
    Regioni438 – 654217Interaction with SUMO1By similarityAdd
    BLAST
    Regioni438 – 574137Sumoylation and localization to discrete nuclear fociBy similarityAdd
    BLAST
    Regioni457 – 879423Interaction with TOP1By similarityAdd
    BLAST
    Regioni457 – 731275Interaction with p53/TP53By similarityAdd
    BLAST
    Regioni851 – 91464Interaction with UBE2IBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi579 – 787209Arg-richAdd
    BLAST
    Compositional biasi877 – 89216Lys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri104 – 14340RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG244178.
    GeneTreeiENSGT00530000064170.
    HOVERGENiHBG080410.
    InParanoidiQ80Z37.
    KOiK10631.
    OMAiLLNRTEH.
    OrthoDBiEOG722J8G.
    PhylomeDBiQ80Z37.
    TreeFamiTF339497.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF00097. zf-C3HC4. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q80Z37-1 [UniParc]FASTAAdd to Basket

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    MGSQPPPPGS PLSREEGEAP PLVPAEEGRR RSRRVRLRGS CRHRPSLLSR     50
    RELASNGPAV PATASSEIMA SAAKEFKMDN FSPKAGTSKL QQTVPADASP 100
    DSKCPICLDR FDNVSYLDRC LHKFCFRCVQ EWSKNKAECP LCKQPFDSIF 150
    HSVRAEDDFK EYVLRPSYNG SFTNPEVRRF RYRTTMTRER SASLYSPSST 200
    VSRRTTTPPD SGVLFEGLGI STRPRDVDIP QFMRQMALRG PTTTDERSLR 250
    KIQEQDIINF RRTLYRAGVR VRSIEDGGRY RDISAEFFRR NPACLHRLVP 300
    WLKRELTVLF GAHGSLVNIV QHIIMSNVTR YDLESQAFVS DLRPFLLNRT 350
    EHFIHEFISF ARSPFNMAAF DQHANYDCPP SSEEGSRSDS SVITISPDEA 400
    ETQELDMNAS TVRQAPWDDE TPGPSYSSSE QVHVGVSSLL NSSDSSDEEL 450
    VSGGTTSQIQ GVQTNDDVNN DSDSSSDNCV IVGFVKPLAE RTPELVELSS 500
    DSEELGPYEK VETVKTQEQE QSYSSGDSDV SRASSPRSVL GKDEQMSKSH 550
    CDSDTRISSK KEEKRSTSLP APRDSSSTRG DRVCSPYNHR HRKGGRSRSS 600
    DSRSQSRSGH DPRNHRKHGK KRLRNKRSRS RESSSRPRAR KDKKRSRTRD 650
    SSWSRRSQTL SLSSGSTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSKY 700
    KWEYTYYSRN KDRDGYESSY RRRTLSRAHY SRQSSSPEFR IQSFSERTNA 750
    RKKNHSERKY YYYERRRSRS VSSNRSRTTS AGPDRVRNEK PGGKRKYKTR 800
    HLEGTSEEAQ PAREFTSKGK DSHYQKSKLD GSYKNESDSF SDSRSSDRET 850
    KHKRRRRRTR SLSVEIVYEG KATDTSKHHK KKKKKHKKKH KKHHGDNTSR 900
    SPVVITIDSD SDGESEVKAG IECSNGSLPQ PIQDGAFETK DVVTIEDELG 950
    VLDKDCDVTA LADDLSTSQT VENCDSPAVP VEQTLDVREE STFASDLESQ 1000
    SSNVSIQAEP SRPVPSPRTS LSSVSPGRDC DVS 1033
    Length:1,033
    Mass (Da):117,082
    Last modified:June 1, 2003 - v1
    Checksum:i3A99C00491D7EFD2
    GO

    Sequence cautioni

    The sequence AAH37141.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401S → F in BAB69457. (PubMed:15703819)Curated
    Sequence conflicti623 – 6231L → P in AAH40797. (PubMed:15489334)Curated
    Sequence conflicti657 – 6571S → A in BAB69457. (PubMed:15703819)Curated
    Sequence conflicti682 – 6821S → A in AAH40797. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB072395 mRNA. Translation: BAB69457.1.
    AB104865 mRNA. Translation: BAC65157.1.
    BC037141 mRNA. Translation: AAH37141.1. Sequence problems.
    BC040797 mRNA. Translation: AAH40797.1.
    AK044564 mRNA. Translation: BAC31981.2.
    AK134075 mRNA. Translation: BAE22003.1.
    AK140250 mRNA. Translation: BAE24298.1.
    AK143025 mRNA. Translation: BAE25253.1.
    AK153743 mRNA. Translation: BAE32164.1.
    CCDSiCCDS38710.1.
    RefSeqiNP_598858.2. NM_134097.3.
    UniGeneiMm.251548.

    Genome annotation databases

    EnsembliENSMUST00000042575; ENSMUSP00000046843; ENSMUSG00000036822.
    GeneIDi106021.
    KEGGimmu:106021.
    UCSCiuc008shi.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB072395 mRNA. Translation: BAB69457.1 .
    AB104865 mRNA. Translation: BAC65157.1 .
    BC037141 mRNA. Translation: AAH37141.1 . Sequence problems.
    BC040797 mRNA. Translation: AAH40797.1 .
    AK044564 mRNA. Translation: BAC31981.2 .
    AK134075 mRNA. Translation: BAE22003.1 .
    AK140250 mRNA. Translation: BAE24298.1 .
    AK143025 mRNA. Translation: BAE25253.1 .
    AK153743 mRNA. Translation: BAE32164.1 .
    CCDSi CCDS38710.1.
    RefSeqi NP_598858.2. NM_134097.3.
    UniGenei Mm.251548.

    3D structure databases

    ProteinModelPortali Q80Z37.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 222976. 2 interactions.
    IntActi Q80Z37. 1 interaction.
    MINTi MINT-1789728.
    STRINGi 10090.ENSMUSP00000046843.

    PTM databases

    PhosphoSitei Q80Z37.

    Proteomic databases

    PRIDEi Q80Z37.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000042575 ; ENSMUSP00000046843 ; ENSMUSG00000036822 .
    GeneIDi 106021.
    KEGGi mmu:106021.
    UCSCi uc008shi.1. mouse.

    Organism-specific databases

    CTDi 10210.
    MGIi MGI:2146189. Topors.

    Phylogenomic databases

    eggNOGi NOG244178.
    GeneTreei ENSGT00530000064170.
    HOVERGENi HBG080410.
    InParanoidi Q80Z37.
    KOi K10631.
    OMAi LLNRTEH.
    OrthoDBi EOG722J8G.
    PhylomeDBi Q80Z37.
    TreeFami TF339497.

    Miscellaneous databases

    NextBioi 358016.
    PROi Q80Z37.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q80Z37.
    CleanExi MM_TOPORS.
    Genevestigatori Q80Z37.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DJ-1 restores p53 transcription activity inhibited by Topors/p53BP3."
      Shinbo Y., Taira T., Niki T., Iguchi-Ariga S.M.M., Ariga H.
      Int. J. Oncol. 26:641-648(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PARK7 AND TP53, SUBCELLULAR LOCATION.
      Strain: C57BL/6.
    2. "Topors, a p53 and topoisomerase I-binding RING finger protein, is a coactivator of p53 in growth suppression induced by DNA damage."
      Lin L., Ozaki T., Takada Y., Kageyama H., Nakamura Y., Hata A., Zhang J.H., Simonds W.F., Nakagawara A., Koseki H.
      Oncogene 24:3385-3396(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION, INDUCTION.
    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].
      Tissue: Mammary gland and Mammary tumor.
    4. "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 1-824.
      Strain: C57BL/6J.
      Tissue: Corpora quadrigemina, Lung, Retina and Thymus.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiTOPRS_MOUSE
    AccessioniPrimary (citable) accession number: Q80Z37
    Secondary accession number(s): Q3U5B5
    , Q3UPZ1, Q3USN3, Q3UZ55, Q8BXP2, Q8CFF5, Q8CGC8, Q920L3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 97 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3