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Q9WUL0 (TOP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 1

EC=5.99.1.2
Alternative name(s):
DNA topoisomerase I
Gene names
Name:Top1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length767 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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

Subunit structure

Monomer By similarity.

Subcellular location

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.

Post-translational modification

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.

Miscellaneous

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

Sequence similarities

Belongs to the type IB topoisomerase family.

Ontologies

Keywords
   Cellular componentNucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionIsomerase
Topoisomerase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from Biological aspect of Ancestor. Source: RefGenome

DNA topological change

Inferred from direct assay PubMed 1332866. Source: RGD

cellular response to luteinizing hormone stimulus

Inferred from expression pattern PubMed 2822514. Source: RGD

chromatin remodeling

Inferred from Biological aspect of Ancestor. Source: RefGenome

chromosome segregation

Inferred from Biological aspect of Ancestor. Source: RefGenome

organ regeneration

Inferred from expression pattern PubMed 1332866. Source: RGD

rRNA transcription

Inferred from mutant phenotype PubMed 3033639. Source: RGD

response to cAMP

Inferred from expression pattern PubMed 2822514. Source: RGD

response to gamma radiation

Inferred from expression pattern PubMed 2853856. Source: RGD

response to temperature stimulus

Inferred from expression pattern PubMed 9076473. Source: RGD

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 1332866. Source: RGD

replication fork protection complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from direct assay PubMed 10469141. Source: RGD

DNA topoisomerase type I activity

Inferred from direct assay PubMed 1332866. Source: RGD

DNA topoisomerase type II (ATP-hydrolyzing) activity

Inferred from electronic annotation. Source: InterPro

chromatin DNA binding

Inferred from direct assay PubMed 1332866. Source: RGD

protein complex binding

Inferred from direct assay PubMed 2851418. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 767766DNA topoisomerase 1
PRO_0000145203

Regions

Region427 – 4282Interaction with DNA By similarity
Region490 – 4956Interaction with DNA By similarity
Region587 – 5893Interaction with DNA By similarity
Compositional bias23 – 206184Lys-rich

Sites

Active site7251O-(3'-phospho-DNA)-tyrosine intermediate By similarity
Site3181Interaction with DNA By similarity
Site3661Interaction with DNA By similarity
Site4141Interaction with DNA By similarity
Site4451Interaction with DNA By similarity
Site5031Interaction with DNA By similarity
Site5341Interaction with DNA By similarity
Site5761Interaction with DNA By similarity
Site6341Interaction with DNA By similarity
Site6521Interaction with DNA By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue101Phosphoserine By similarity
Modified residue591Phosphoserine By similarity
Modified residue1141Phosphoserine By similarity
Modified residue1741N6-acetyllysine By similarity
Modified residue2821N6-acetyllysine By similarity
Modified residue5081Phosphoserine; by CK2 By similarity
Cross-link105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Cross-link119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link155Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable

Sequences

Sequence LengthMass (Da)Tools
Q9WUL0 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 79103F06DA61D73D

FASTA76790,760
        10         20         30         40         50         60 
MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKDKDREKSK HSNSEHKDSE 

        70         80         90        100        110        120 
KKHKEKEKTK HKDGSSDKHK DKHKDRDKEK RKEEKIRAAG DAKIKKEKEN GFSSPPRIKD 

       130        140        150        160        170        180 
EPEDDGYFAP PKEDIKPLKR PRDEDDADYK PKKIKTEDIK KEKKRKLEEE EDGKLKKPKN 

       190        200        210        220        230        240 
KDKDKKVAEP DNKKKKAKKE EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPEGV 

       250        260        270        280        290        300 
KFYYDGKVMK LSPKAEEVAT FFAKMLDHEY TTKEIFRKNF FKDWRKEMTN DEKNTITNLS 

       310        320        330        340        350        360 
KCDFTQMSQY FKAQSEARKQ MSKEEKLKIK EENEKLLKEY GFCVMDNHRE RIANFKIEPP 

       370        380        390        400        410        420 
GLFRGRGNHP KMGMLKRRIM PEDIIINCSK DAKVPSPPPG HKWKEVRHDN KVTWLVSWTE 

       430        440        450        460        470        480 
NIQGSIKYIM LNPSSRIKGE KDWQKYETAR RLKKCVDKIR NQYREDWKSK EMKVRQRAVA 

       490        500        510        520        530        540 
LYFIDKLALR AGNEKEEGET ADTVGCCSLR VEHINLHPEL DGQEYVVEFD FPGKDSIRYY 

       550        560        570        580        590        600 
NKVPVEKRVF KNLQLFMENK QPEDDLFDRL NTGILNKHLQ DLMEGLTAKV FRTYNASITL 

       610        620        630        640        650        660 
QQQLKELTAP DENVPAKILS YNRANRAVAI LCNHQRAPPK TFEKSMMNLQ SKIDAKKDQL 

       670        680        690        700        710        720 
ADARKDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL MKLEVQATDR EENKQIALGT 

       730        740        750        760 
SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ REKFAWAIDM TDEDYEF 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF140782 mRNA. Translation: AAD30137.1.
RefSeqNP_072137.1. NM_022615.1.
UniGeneRn.91572.

3D structure databases

ProteinModelPortalQ9WUL0.
SMRQ9WUL0. Positions 201-767.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249131. 1 interaction.
IntActQ9WUL0. 1 interaction.

Chemistry

BindingDBQ9WUL0.
ChEMBLCHEMBL1075164.

PTM databases

PhosphoSiteQ9WUL0.

Proteomic databases

PaxDbQ9WUL0.
PRIDEQ9WUL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64550.
KEGGrno:64550.
UCSCRGD:621246. rat.

Organism-specific databases

CTD7150.
RGD621246. Top1.

Phylogenomic databases

eggNOGCOG3569.
HOGENOMHOG000105469.
HOVERGENHBG007988.
KOK03163.
PhylomeDBQ9WUL0.
TreeFamTF105281.

Gene expression databases

GenevestigatorQ9WUL0.

Family and domain databases

Gene3D1.10.10.41. 1 hit.
1.10.132.10. 1 hit.
2.170.11.10. 2 hits.
3.90.15.10. 1 hit.
InterProIPR011010. 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]
PfamPF14370. Topo_C_assoc. 1 hit.
PF01028. Topoisom_I. 1 hit.
PF02919. Topoisom_I_N. 1 hit.
[Graphical view]
PRINTSPR00416. EUTPISMRASEI.
SMARTSM00435. TOPEUc. 1 hit.
[Graphical view]
SUPFAMSSF56349. SSF56349. 2 hits.
SSF56741. SSF56741. 1 hit.
PROSITEPS00176. TOPOISOMERASE_I_EUK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio613440.
PROQ9WUL0.

Entry information

Entry nameTOP1_RAT
AccessionPrimary (citable) accession number: Q9WUL0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families