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Q9WUL0

- TOP1_RAT

UniProt

Q9WUL0 - TOP1_RAT

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Protein

DNA topoisomerase 1

Gene
Top1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

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.

Catalytic activityi

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

Sites

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin DNA binding Source: RGD
  3. DNA binding Source: RGD
  4. DNA topoisomerase type I activity Source: RGD
  5. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: InterPro
  6. 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
Complete GO annotation...

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.

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei10 – 101Phosphoserine By similarity
Modified residuei59 – 591Phosphoserine By similarity
Cross-linki105 – 105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Inferred
Modified residuei114 – 1141Phosphoserine By 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) Inferred
Modified residuei174 – 1741N6-acetyllysine By similarity
Modified residuei282 – 2821N6-acetyllysine By similarity
Modified residuei508 – 5081Phosphoserine; by CK2 By 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.
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.

Family & Domainsi

Region

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

Compositional bias

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

Sequence similaritiesi

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

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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: July 9, 2014
This is version 98 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

Similar proteinsi