Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q07050

- TOP1_CRIGR

UniProt

Q07050 - TOP1_CRIGR

Protein

DNA topoisomerase 1

Gene

TOP1

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Enzyme regulationi

    Specifically inhibited by camptothecin (CPT), a plant alkaloid with antitumor activity.

    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 binding Source: UniProtKB
    2. DNA binding Source: UniProtKB
    3. DNA topoisomerase type I activity Source: UniProtKB
    4. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: InterPro

    GO - Biological processi

    1. DNA topological change Source: UniProtKB

    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
    Synonyms:TOP-1
    OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
    Taxonomic identifieri10029 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

    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. chromosome Source: InterPro
    2. nucleolus Source: UniProtKB
    3. nucleoplasm Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 767766DNA topoisomerase 1PRO_0000145200Add
    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

    PRIDEiQ07050.

    Interactioni

    Subunit structurei

    Monomer.

    Structurei

    3D structure databases

    ProteinModelPortaliQ07050.
    SMRiQ07050. 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

    HOVERGENiHBG007988.
    KOiK03163.

    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.

    Q07050-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKEKDREKSK    50
    HSNSEHKDSE KKHKEKEKTK HKDGSSEKHK DKHKDRDKEK RKEEKIRASG 100
    DAKIKKEKEN GFSSPPRIKD EPDDDGYFAP PKEDIKPLKR PRDEDDADYK 150
    PKKIKTEDIK KEKKRKLEEE EDGKLKKTKN KDKDKKGAES DNKKKKPKKE 200
    EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPEGV KFYYDGKVMK 250
    LSPKAEEVAT FFAKMLDHEY TTKEIFRKNF FKDWRKEMTN DEKNVITNLS 300
    KCDFTQMSQY FKDQSEARKQ MSKEEKLKIK EENEKLLKEY GFCVMDNHRE 350
    RIANFKIEPP GLFRGRGNHP KMGMLKRRIM PEDIIINCSK DAKVPSPPPG 400
    HKWKEVRHDN KVTWLVSWTE NIQGSIKYIM LNPSSRIKGE KDWQKYETAR 450
    RLKKCVDKIR NQYREDWKSK EMKVRQRAVA LYFIDKLALR AGNEKEEGET 500
    ADTVSCCSLR VEHINLHPEL DGQEYVVEFD FPGKDSIRYY NKVPVEKRVF 550
    KNLQLFMENK QPEDDLFDRL NTGILNKHLQ DLMEGLTAKV FRTYNASITL 600
    QQQLKELTAP DENVPAKILS YNRANRAVAI LCNHQRAPPK TFEKSMMNLQ 650
    SKIDAKKDQL ADARRDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL 700
    MKLEVQATDR EENKQIALGT SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ 750
    REKFAWAIDM TDEDYEF 767
    Length:767
    Mass (Da):90,868
    Last modified:October 1, 1994 - v1
    Checksum:i347336D424EF35A9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti505 – 5051S → G in CPT-resistant cell.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21624 mRNA. Translation: CAA79747.1.
    Z21625 mRNA. Translation: CAA79748.1.
    PIRiA49546.
    RefSeqiNP_001230963.1. NM_001244034.1.

    Genome annotation databases

    GeneIDi100689046.
    KEGGicge:100689046.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z21624 mRNA. Translation: CAA79747.1 .
    Z21625 mRNA. Translation: CAA79748.1 .
    PIRi A49546.
    RefSeqi NP_001230963.1. NM_001244034.1.

    3D structure databases

    ProteinModelPortali Q07050.
    SMRi Q07050. Positions 201-767.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q07050.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100689046.
    KEGGi cge:100689046.

    Organism-specific databases

    CTDi 7150.

    Phylogenomic databases

    HOVERGENi HBG007988.
    KOi K03163.

    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. "Cloning of Chinese hamster DNA topoisomerase I cDNA and identification of a single point mutation responsible for camptothecin resistance."
      Tanizawa A., Bertrand R., Kohlhagen G., Tabuchi A., Jenkins J., Pommier Y.
      J. Biol. Chem. 268:25463-25468(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiTOP1_CRIGR
    AccessioniPrimary (citable) accession number: Q07050
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 90 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.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3