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Q9NS56

- TOPRS_HUMAN

UniProt

Q9NS56 - TOPRS_HUMAN

Protein

E3 ubiquitin-protein ligase Topors

Gene

TOPORS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Functions as an E3 ubiquitin-protein ligase and as an 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.7 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri103 – 14240RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. antigen binding Source: UniProtKB
    2. DNA binding Source: UniProtKB
    3. DNA topoisomerase binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. SUMO ligase activity Source: UniProtKB
    6. ubiquitin-protein transferase activity Source: UniProtKB
    7. 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: Ensembl
    4. maintenance of protein location in nucleus Source: UniProtKB
    5. negative regulation of apoptotic process Source: BHF-UCL
    6. photoreceptor cell outer segment organization Source: BHF-UCL
    7. positive regulation of transcription, DNA-templated Source: Ensembl
    8. positive regulation of ubiquitin-protein transferase activity Source: BHF-UCL
    9. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    10. protein K48-linked ubiquitination Source: BHF-UCL
    11. protein localization to nucleus Source: UniProtKB
    12. protein monoubiquitination Source: BHF-UCL
    13. protein sumoylation Source: UniProtKB
    14. regulation of cell proliferation Source: Ensembl
    15. retina layer formation Source: BHF-UCL
    16. retinal cone cell development Source: BHF-UCL
    17. retinal rod cell development Source: BHF-UCL
    18. transcription, DNA-templated Source: UniProtKB
    19. 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
    Synonyms:LUN, TP53BPL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:21653. TOPORS.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Retinitis pigmentosa 31 (RP31) [MIM:609923]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi76 – 761K → R: No effect on sumoylation. 1 Publication
    Mutagenesisi98 – 981S → A: Loss of phosphorylation but no effect on E3 ubiquitin-protein ligase activity. 1 Publication
    Mutagenesisi98 – 981S → D: Increase in E3 ubiquitin-protein ligase activity and increased binding to UBE2D1. No effect on SUMO1-protein ligase activity. 1 Publication
    Mutagenesisi131 – 1311W → A: Abrogates E3 ubiquitin-protein ligase activity. 1 Publication
    Mutagenesisi301 – 3011K → R: No effect on sumoylation. 1 Publication
    Mutagenesisi485 – 4851K → R: No effect on sumoylation. 1 Publication
    Mutagenesisi560 – 5601K → R: Strongly reduces sumoylation. 1 Publication
    Mutagenesisi718 – 7181S → A: Loss of phosphorylation by PLK1 and increases in p53/TP53 stability. 1 Publication
    Mutagenesisi921 – 9211K → R: No effect on sumoylation. 1 Publication

    Keywords - Diseasei

    Retinitis pigmentosa

    Organism-specific databases

    MIMi609923. phenotype.
    Orphaneti791. Retinitis pigmentosa.
    PharmGKBiPA134979531.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10451045E3 ubiquitin-protein ligase ToporsPRO_0000232626Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei98 – 981Phosphoserine5 Publications
    Modified residuei499 – 4991Phosphoserine1 Publication
    Cross-linki560 – 560Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei585 – 5851Phosphoserine1 Publication
    Modified residuei718 – 7181Phosphoserine; by PLK11 Publication
    Modified residuei864 – 8641Phosphoserine2 Publications
    Modified residuei866 – 8661Phosphoserine3 Publications
    Modified residuei1028 – 10281PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylation at Ser-98 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 SUMO1-protein ligase activity resulting in increased p53/TP53 ubiquitination and degradation.6 Publications
    Sumoylated.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NS56.
    PaxDbiQ9NS56.
    PRIDEiQ9NS56.

    PTM databases

    PhosphoSiteiQ9NS56.

    Expressioni

    Tissue specificityi

    Expressed at highest levels in testis and at lower levels in adrenal gland, bone marrow, brain, colon, heart, kidney, liver, muscle, ovary, pancreas, placenta, prostate, skeletal muscle, skin, small intestine, spleen, stomach, testis, thymus, thyroid and uterus. Expressed in the alveolar epithelium of the lung. Expression is commonly decreased in colon adenocarcinomas and lung cancers.3 Publications

    Inductioni

    By genotoxic agents such as cisplatin and camptothecin.1 Publication

    Gene expression databases

    BgeeiQ9NS56.
    CleanExiHS_TOPORS.
    GenevestigatoriQ9NS56.

    Interactioni

    Subunit structurei

    Interacts with PARK7/DJ-1 By similarity. Interacts with TOP1. Interacts with p53/TP53; can both ubiquitinate and sumoylate p53/TP53. 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 similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Rep68P031323EBI-1996473,EBI-7387242From a different organism.

    Protein-protein interaction databases

    BioGridi115505. 48 interactions.
    IntActiQ9NS56. 17 interactions.
    MINTiMINT-94004.
    STRINGi9606.ENSP00000353735.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NS56.
    SMRiQ9NS56. Positions 100-147.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 195195E3 ubiquitin-protein ligase activityAdd
    BLAST
    Regioni51 – 374324Required for DNA-bindingAdd
    BLAST
    Regioni437 – 654218Interaction with SUMO1Add
    BLAST
    Regioni437 – 574138Required for sumoylation and localization to discrete nuclear fociAdd
    BLAST
    Regioni456 – 882427Interaction with TOP1Add
    BLAST
    Regioni456 – 731276Interaction with p53/TP53Add
    BLAST
    Regioni854 – 91764Interaction with UBE2IAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi579 – 788210Arg-richAdd
    BLAST
    Compositional biasi854 – 89542Lys-richAdd
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri103 – 14240RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG244178.
    HOGENOMiHOG000231723.
    HOVERGENiHBG080410.
    InParanoidiQ9NS56.
    KOiK10631.
    OMAiLLNRTEH.
    OrthoDBiEOG722J8G.
    PhylomeDBiQ9NS56.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NS56-1) [UniParc]FASTAAdd to Basket

    Also known as: LUN-1

    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

    MGSQPPLGSP LSREEGEAPP PAPASEGRRR SRRVRLRGSC RHRPSFLGCR     50
    ELAASAPARP APASSEIMAS AAKEFKMDNF SPKAGTSKLQ QTVPADASPD 100
    SKCPICLDRF DNVSYLDRCL HKFCFRCVQE WSKNKAECPL CKQPFDSIFH 150
    SVRAEDDFKE YVLRPSYNGS FVTPDRRFRY RTTLTRERNA SVYSPSGPVN 200
    RRTTTPPDSG VLFEGLGIST RPRDVEIPQF MRQIAVRRPT TADERSLRKI 250
    QEQDIINFRR TLYRAGARVR NIEDGGRYRD ISAEFFRRNP ACLHRLVPWL 300
    KRELTVLFGA HGSLVNIVQH IIMSNVTRYD LESQAFVSDL RPFLLNRTEH 350
    FIHEFISFAR SPFNMAAFDQ HANYDCPAPS YEEGSHSDSS VITISPDEAE 400
    TQELDINVAT VSQAPWDDET PGPSYSSSEQ VHVTMSSLLN TSDSSDEELV 450
    TGGATSQIQG VQTNDDLNND SDDSSDNCVI VGFVKPLAER TPELVELSSD 500
    SEDLGSYEKM ETVKTQEQEQ SYSSGDSDVS RCSSPHSVLG KDEQINKGHC 550
    DSSTRIKSKK EEKRSTSLSS PRNLNSSVRG DRVYSPYNHR HRKRGRSRSS 600
    DSRSQSRSGH DQKNHRKHHG KKRMKSKRSR SRESSRPRGR RDKKRSRTRD 650
    SSWSRRSQTL SLSSESTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSRY 700
    KWEYTYYSRN KDRDGYESSY RRRTLSRAHY SRQSSSPEFR VQSFSERTNA 750
    RKKNNHSERK YYYYERHRSR SLSSNRSRTA STGTDRVRNE KPGGKRKYKT 800
    RHLEGTNEVA QPSREFASKA KDSHYQKSSS KLDGNYKNES DTFSDSRSSD 850
    RETKHKRRKR KTRSLSVEIV YEGKATDTTK HHKKKKKKHK KKHKKHHGDN 900
    ASRSPVVITI DSDSDKDSEV KEDTECDNSG PQDPLQNEFL APSLEPFETK 950
    DVVTIEAEFG VLDKECDIAT LSNNLNNANK TVDNIPPLAA SVEQTLDVRE 1000
    ESTFVSDLEN QPSNIVSLQT EPSRQLPSPR TSLMSVCLGR DCDMS 1045
    Length:1,045
    Mass (Da):119,198
    Last modified:October 1, 2000 - v1
    Checksum:i3DA635FDB5C83B77
    GO
    Isoform 2 (identifier: Q9NS56-2) [UniParc]FASTAAdd to Basket

    Also known as: LUN-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-65: Missing.
         66-66: E → M

    Show »
    Length:980
    Mass (Da):112,344
    Checksum:i85E2A39A2978B20E
    GO

    Sequence cautioni

    The sequence AAC98530.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1252CF → K in AAC98530. (PubMed:10415337)Curated
    Sequence conflicti257 – 2571N → S in AAD23379. (PubMed:10352183)Curated
    Sequence conflicti308 – 3081F → S in AAD23379. (PubMed:10352183)Curated
    Sequence conflicti922 – 9221E → G in AAD23379. (PubMed:10352183)Curated
    Sequence conflicti1040 – 10401R → K in AAD23379. (PubMed:10352183)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti154 – 1541A → T.1 Publication
    Corresponds to variant rs17855104 [ dbSNP | Ensembl ].
    VAR_037629
    Natural varianti517 – 5171E → K.1 Publication
    Corresponds to variant rs17855103 [ dbSNP | Ensembl ].
    VAR_037630
    Natural varianti749 – 7491N → D.1 Publication
    Corresponds to variant rs17857515 [ dbSNP | Ensembl ].
    VAR_037631
    Natural varianti812 – 8121P → R.
    Corresponds to variant rs36034138 [ dbSNP | Ensembl ].
    VAR_037632

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6565Missing in isoform 2. 1 PublicationVSP_017916Add
    BLAST
    Alternative sequencei66 – 661E → M in isoform 2. 1 PublicationVSP_017917

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF098300 mRNA. Translation: AAD23379.1.
    AB045732 mRNA. Translation: BAB03714.1.
    AB045733 mRNA. Translation: BAB03715.1.
    AL353671 Genomic DNA. Translation: CAH71253.1.
    AL353671 Genomic DNA. Translation: CAH71254.1.
    BC060884 mRNA. Translation: AAH60884.1.
    U82939 mRNA. Translation: AAC98530.1. Different initiation.
    CCDSiCCDS56566.1. [Q9NS56-2]
    CCDS6527.1. [Q9NS56-1]
    RefSeqiNP_001182551.1. NM_001195622.1. [Q9NS56-2]
    NP_005793.2. NM_005802.4. [Q9NS56-1]
    UniGeneiHs.589962.

    Genome annotation databases

    EnsembliENST00000360538; ENSP00000353735; ENSG00000197579. [Q9NS56-1]
    ENST00000379858; ENSP00000369187; ENSG00000197579. [Q9NS56-2]
    GeneIDi10210.
    KEGGihsa:10210.
    UCSCiuc003zrb.3. human. [Q9NS56-1]
    uc003zrc.3. human. [Q9NS56-2]

    Polymorphism databases

    DMDMi74752935.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF098300 mRNA. Translation: AAD23379.1 .
    AB045732 mRNA. Translation: BAB03714.1 .
    AB045733 mRNA. Translation: BAB03715.1 .
    AL353671 Genomic DNA. Translation: CAH71253.1 .
    AL353671 Genomic DNA. Translation: CAH71254.1 .
    BC060884 mRNA. Translation: AAH60884.1 .
    U82939 mRNA. Translation: AAC98530.1 . Different initiation.
    CCDSi CCDS56566.1. [Q9NS56-2 ]
    CCDS6527.1. [Q9NS56-1 ]
    RefSeqi NP_001182551.1. NM_001195622.1. [Q9NS56-2 ]
    NP_005793.2. NM_005802.4. [Q9NS56-1 ]
    UniGenei Hs.589962.

    3D structure databases

    ProteinModelPortali Q9NS56.
    SMRi Q9NS56. Positions 100-147.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115505. 48 interactions.
    IntActi Q9NS56. 17 interactions.
    MINTi MINT-94004.
    STRINGi 9606.ENSP00000353735.

    PTM databases

    PhosphoSitei Q9NS56.

    Polymorphism databases

    DMDMi 74752935.

    Proteomic databases

    MaxQBi Q9NS56.
    PaxDbi Q9NS56.
    PRIDEi Q9NS56.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360538 ; ENSP00000353735 ; ENSG00000197579 . [Q9NS56-1 ]
    ENST00000379858 ; ENSP00000369187 ; ENSG00000197579 . [Q9NS56-2 ]
    GeneIDi 10210.
    KEGGi hsa:10210.
    UCSCi uc003zrb.3. human. [Q9NS56-1 ]
    uc003zrc.3. human. [Q9NS56-2 ]

    Organism-specific databases

    CTDi 10210.
    GeneCardsi GC09M032496.
    GeneReviewsi TOPORS.
    HGNCi HGNC:21653. TOPORS.
    MIMi 609507. gene.
    609923. phenotype.
    neXtProti NX_Q9NS56.
    Orphaneti 791. Retinitis pigmentosa.
    PharmGKBi PA134979531.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244178.
    HOGENOMi HOG000231723.
    HOVERGENi HBG080410.
    InParanoidi Q9NS56.
    KOi K10631.
    OMAi LLNRTEH.
    OrthoDBi EOG722J8G.
    PhylomeDBi Q9NS56.
    TreeFami TF339497.

    Miscellaneous databases

    ChiTaRSi TOPORS. human.
    GeneWikii TOPORS.
    GenomeRNAii 10210.
    NextBioi 38656.
    PROi Q9NS56.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NS56.
    CleanExi HS_TOPORS.
    Genevestigatori Q9NS56.

    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. "Interaction between human topoisomerase I and a novel RING finger/arginine-serine protein."
      Haluska P. Jr., Saleem A., Rasheed Z., Ahmed F., Su E.W., Liu L.F., Rubin E.H.
      Nucleic Acids Res. 27:2538-2544(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TOP1, SUBCELLULAR LOCATION.
    2. "Cloning and characterization of LUN, a novel RING-finger protein that is highly expressed in lung and specifically binds to a palindromic sequence."
      Chu D., Kakazu N., Gorrin-Rivas M.J., Lu H.P., Kawata M., Abe T., Ueda K., Adachi Y.
      J. Biol. Chem. 276:14004-14013(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PUTATIVE DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Lung.
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1), VARIANTS THR-154; LYS-517 AND ASP-749.
      Tissue: Placenta.
    5. "Identification of a novel gene encoding a p53-associated protein."
      Zhou R., Wen H., Ao S.-Z.
      Gene 235:93-101(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-1045 (ISOFORM 1), INTERACTION WITH TP53, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "The topoisomerase I-binding RING protein, topors, is associated with promyelocytic leukemia nuclear bodies."
      Rasheed Z.A., Saleem A., Ravee Y., Pandolfi P.P., Rubin E.H.
      Exp. Cell Res. 277:152-160(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "The DNA topoisomerase I binding protein topors as a novel cellular target for SUMO-1 modification: characterization of domains necessary for subcellular localization and sumolation."
      Weger S., Hammer E., Engstler M.
      Exp. Cell Res. 290:13-27(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUMO1 AND UBE2I, SUBCELLULAR LOCATION, SUMOYLATION, MUTAGENESIS OF LYS-76; LYS-301; LYS-485; LYS-560 AND LYS-921.
    8. "Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53."
      Rajendra R., Malegaonkar D., Pungaliya P., Marshall H., Rasheed Z., Brownell J., Liu L.F., Lutzker S., Saleem A., Rubin E.H.
      J. Biol. Chem. 279:36440-36444(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TRP-131.
    9. "Expression of LUN gene that encodes a novel RING finger protein is correlated with development and progression of non-small cell lung cancer."
      Oyanagi H., Takenaka K., Ishikawa S., Kawano Y., Adachi Y., Ueda K., Wada H., Tanaka F.
      Lung Cancer 46:21-28(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REDUCED EXPRESSION IN LUNG CANCERS.
    10. "The topoisomerase I- and p53-binding protein topors is differentially expressed in normal and malignant human tissues and may function as a tumor suppressor."
      Saleem A., Dutta J., Malegaonkar D., Rasheed F., Rasheed Z., Rajendra R., Marshall H., Luo M., Li H., Rubin E.H.
      Oncogene 23:5293-5300(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, REDUCED EXPRESSION IN COLON CANCERS.
    11. "Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo."
      Weger S., Hammer E., Heilbronn R.
      FEBS Lett. 579:5007-5012(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUMOYLATION.
    12. "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: FUNCTION, INDUCTION.
    13. Cited for: INVOLVEMENT IN RP31.
    14. "TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins."
      Pungaliya P., Kulkarni D., Park H.J., Marshall H., Zheng H., Lackland H., Saleem A., Rubin E.H.
      J. Proteome Res. 6:3918-3923(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SIN3A.
    15. "Identification of phosphorylation sites of TOPORS and a role for serine 98 in the regulation of ubiquitin but not SUMO E3 ligase activity."
      Park H.J., Zheng H., Kulkarni D., Kerrigan J., Pungaliya P., Saleem A., Rubin E.H.
      Biochemistry 47:13887-13896(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-98; SER-499; SER-585 AND SER-866, MUTAGENESIS OF SER-98, IDENTIFICATION BY MASS SPECTROMETRY.
    16. "Ubiquitination by TOPORS regulates the prostate tumor suppressor NKX3.1."
      Guan B., Pungaliya P., Li X., Uquillas C., Mutton L.N., Rubin E.H., Bieberich C.J.
      J. Biol. Chem. 283:4834-4840(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NKX3-1, SUBCELLULAR LOCATION.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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. "Plk1-mediated phosphorylation of Topors regulates p53 stability."
      Yang X., Li H., Zhou Z., Wang W.H., Deng A., Andrisani O., Liu X.
      J. Biol. Chem. 284:18588-18592(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PLK1, PHOSPHORYLATION AT SER-718 BY PLK1, MUTAGENESIS OF SER-718, SUBCELLULAR LOCATION.
    20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-864 AND SER-866, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "SUMOylation-dependent localization of IKKepsilon in PML nuclear bodies is essential for protection against DNA-damage-triggered cell death."
      Renner F., Moreno R., Schmitz M.L.
      Mol. Cell 37:503-515(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH IKBKE, SUBCELLULAR LOCATION.
    22. "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-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "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-98; SER-864 AND SER-866, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTOPRS_HUMAN
    AccessioniPrimary (citable) accession number: Q9NS56
    Secondary accession number(s): O43273
    , Q6P987, Q9NS55, Q9UNR9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 18, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 117 of the entry and version 1 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

    Caution

    Was originally thought to bind to the palindromic consensus sequence 5'-TCCCAGCACTTTGGGA-3' and to regulate the transcription of numerous genes in the lung.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3