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Q9WUL0

- TOP1_RAT

UniProt

Q9WUL0 - TOP1_RAT

Protein

DNA topoisomerase 1

Gene

Top1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells By similarity.By similarity

    Catalytic activityi

    ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei318 – 3181Interaction with DNABy similarity
    Sitei366 – 3661Interaction with DNABy similarity
    Sitei414 – 4141Interaction with DNABy similarity
    Sitei445 – 4451Interaction with DNABy similarity
    Sitei503 – 5031Interaction with DNABy similarity
    Sitei534 – 5341Interaction with DNABy similarity
    Sitei576 – 5761Interaction with DNABy similarity
    Sitei634 – 6341Interaction with DNABy similarity
    Sitei652 – 6521Interaction with DNABy similarity
    Active sitei725 – 7251O-(3'-phospho-DNA)-tyrosine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. chromatin DNA binding Source: RGD
    2. DNA binding Source: RGD
    3. DNA topoisomerase type I activity Source: RGD
    4. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: InterPro
    5. protein complex binding Source: RGD

    GO - Biological processi

    1. cellular response to luteinizing hormone stimulus Source: RGD
    2. chromatin remodeling Source: RefGenome
    3. chromosome segregation Source: RefGenome
    4. DNA replication Source: RefGenome
    5. DNA topological change Source: RGD
    6. organ regeneration Source: RGD
    7. response to cAMP Source: RGD
    8. response to gamma radiation Source: RGD
    9. response to temperature stimulus Source: RGD
    10. rRNA transcription Source: RGD

    Keywords - Molecular functioni

    Isomerase, Topoisomerase

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA topoisomerase 1 (EC:5.99.1.2)
    Alternative name(s):
    DNA topoisomerase I
    Gene namesi
    Name:Top1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621246. Top1.

    Subcellular locationi

    Nucleusnucleolus. Nucleusnucleoplasm
    Note: Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumolyated forms found in both nucleoplasm and nucleoli By similarity.By similarity

    GO - Cellular componenti

    1. fibrillar center Source: RGD
    2. nucleoplasm Source: UniProtKB-SubCell
    3. nucleus Source: RGD
    4. replication fork protection complex Source: RefGenome

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 767766DNA topoisomerase 1PRO_0000145203Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei10 – 101PhosphoserineBy similarity
    Modified residuei59 – 591PhosphoserineBy similarity
    Cross-linki105 – 105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Modified residuei114 – 1141PhosphoserineBy similarity
    Cross-linki119 – 119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Cross-linki155 – 155Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Modified residuei174 – 1741N6-acetyllysineBy similarity
    Modified residuei282 – 2821N6-acetyllysineBy similarity
    Modified residuei508 – 5081Phosphoserine; by CK2By similarity

    Post-translational modificationi

    Sumoylated. Lys-119 is the main site of sumoylation. Sumoylation plays a role in partitioning TOP1 between nucleoli and nucleoplasm. Levels are dramatically increased on camptothecin (CPT) treatment By similarity.By similarity
    Phosphorylation at Ser-508 by CK2 increases binding to supercoiled DNA and sensitivity to camptothecin.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ9WUL0.
    PRIDEiQ9WUL0.

    PTM databases

    PhosphoSiteiQ9WUL0.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9WUL0.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi249131. 1 interaction.
    IntActiQ9WUL0. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9WUL0.
    SMRiQ9WUL0. Positions 201-767.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni427 – 4282Interaction with DNABy similarity
    Regioni490 – 4956Interaction with DNABy similarity
    Regioni587 – 5893Interaction with DNABy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi23 – 206184Lys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the type IB topoisomerase family.Curated

    Phylogenomic databases

    eggNOGiCOG3569.
    HOGENOMiHOG000105469.
    HOVERGENiHBG007988.
    KOiK03163.
    PhylomeDBiQ9WUL0.
    TreeFamiTF105281.

    Family and domain databases

    Gene3Di1.10.10.41. 1 hit.
    1.10.132.10. 1 hit.
    2.170.11.10. 2 hits.
    3.90.15.10. 1 hit.
    InterProiIPR011010. DNA_brk_join_enz.
    IPR013034. DNA_topo_domain1.
    IPR001631. TopoI.
    IPR018521. TopoI_AS.
    IPR025834. TopoI_C_dom.
    IPR014711. TopoI_cat_a-hlx-sub_euk.
    IPR014727. TopoI_cat_a/b-sub_euk.
    IPR013500. TopoI_cat_euk.
    IPR008336. TopoI_DNA-bd_euk.
    IPR013030. TopoI_DNA-bd_mixed-a/b_euk.
    IPR013499. TopoI_euk.
    [Graphical view]
    PfamiPF14370. Topo_C_assoc. 1 hit.
    PF01028. Topoisom_I. 1 hit.
    PF02919. Topoisom_I_N. 1 hit.
    [Graphical view]
    PRINTSiPR00416. EUTPISMRASEI.
    SMARTiSM00435. TOPEUc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56349. SSF56349. 2 hits.
    SSF56741. SSF56741. 1 hit.
    PROSITEiPS00176. TOPOISOMERASE_I_EUK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9WUL0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKDKDREKSK    50
    HSNSEHKDSE KKHKEKEKTK HKDGSSDKHK DKHKDRDKEK RKEEKIRAAG 100
    DAKIKKEKEN GFSSPPRIKD EPEDDGYFAP PKEDIKPLKR PRDEDDADYK 150
    PKKIKTEDIK KEKKRKLEEE EDGKLKKPKN KDKDKKVAEP DNKKKKAKKE 200
    EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPEGV KFYYDGKVMK 250
    LSPKAEEVAT FFAKMLDHEY TTKEIFRKNF FKDWRKEMTN DEKNTITNLS 300
    KCDFTQMSQY FKAQSEARKQ MSKEEKLKIK EENEKLLKEY GFCVMDNHRE 350
    RIANFKIEPP GLFRGRGNHP KMGMLKRRIM PEDIIINCSK DAKVPSPPPG 400
    HKWKEVRHDN KVTWLVSWTE NIQGSIKYIM LNPSSRIKGE KDWQKYETAR 450
    RLKKCVDKIR NQYREDWKSK EMKVRQRAVA LYFIDKLALR AGNEKEEGET 500
    ADTVGCCSLR VEHINLHPEL DGQEYVVEFD FPGKDSIRYY NKVPVEKRVF 550
    KNLQLFMENK QPEDDLFDRL NTGILNKHLQ DLMEGLTAKV FRTYNASITL 600
    QQQLKELTAP DENVPAKILS YNRANRAVAI LCNHQRAPPK TFEKSMMNLQ 650
    SKIDAKKDQL ADARKDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL 700
    MKLEVQATDR EENKQIALGT SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ 750
    REKFAWAIDM TDEDYEF 767
    Length:767
    Mass (Da):90,760
    Last modified:November 1, 1999 - v1
    Checksum:i79103F06DA61D73D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF140782 mRNA. Translation: AAD30137.1.
    RefSeqiNP_072137.1. NM_022615.1.
    UniGeneiRn.91572.

    Genome annotation databases

    GeneIDi64550.
    KEGGirno:64550.
    UCSCiRGD:621246. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF140782 mRNA. Translation: AAD30137.1 .
    RefSeqi NP_072137.1. NM_022615.1.
    UniGenei Rn.91572.

    3D structure databases

    ProteinModelPortali Q9WUL0.
    SMRi Q9WUL0. Positions 201-767.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249131. 1 interaction.
    IntActi Q9WUL0. 1 interaction.

    Chemistry

    BindingDBi Q9WUL0.
    ChEMBLi CHEMBL1075164.

    PTM databases

    PhosphoSitei Q9WUL0.

    Proteomic databases

    PaxDbi Q9WUL0.
    PRIDEi Q9WUL0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 64550.
    KEGGi rno:64550.
    UCSCi RGD:621246. rat.

    Organism-specific databases

    CTDi 7150.
    RGDi 621246. Top1.

    Phylogenomic databases

    eggNOGi COG3569.
    HOGENOMi HOG000105469.
    HOVERGENi HBG007988.
    KOi K03163.
    PhylomeDBi Q9WUL0.
    TreeFami TF105281.

    Miscellaneous databases

    NextBioi 613440.
    PROi Q9WUL0.

    Gene expression databases

    Genevestigatori Q9WUL0.

    Family and domain databases

    Gene3Di 1.10.10.41. 1 hit.
    1.10.132.10. 1 hit.
    2.170.11.10. 2 hits.
    3.90.15.10. 1 hit.
    InterProi IPR011010. DNA_brk_join_enz.
    IPR013034. DNA_topo_domain1.
    IPR001631. TopoI.
    IPR018521. TopoI_AS.
    IPR025834. TopoI_C_dom.
    IPR014711. TopoI_cat_a-hlx-sub_euk.
    IPR014727. TopoI_cat_a/b-sub_euk.
    IPR013500. TopoI_cat_euk.
    IPR008336. TopoI_DNA-bd_euk.
    IPR013030. TopoI_DNA-bd_mixed-a/b_euk.
    IPR013499. TopoI_euk.
    [Graphical view ]
    Pfami PF14370. Topo_C_assoc. 1 hit.
    PF01028. Topoisom_I. 1 hit.
    PF02919. Topoisom_I_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00416. EUTPISMRASEI.
    SMARTi SM00435. TOPEUc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56349. SSF56349. 2 hits.
    SSF56741. SSF56741. 1 hit.
    PROSITEi PS00176. TOPOISOMERASE_I_EUK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequencing of rat topoisomerase I between sensitive and camptothecin-resistant C6 glioblastoma cell lines."
      Pourquier P., Gioffre C., Ueng L.-M., Robert J., Pommier Y.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Glioblastoma.

    Entry informationi

    Entry nameiTOP1_RAT
    AccessioniPrimary (citable) accession number: Q9WUL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3