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Q7YR26

- TOP1_CHLAE

UniProt

Q7YR26 - TOP1_CHLAE

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Protein
DNA topoisomerase 1
Gene
TOP1
Organism
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
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.

Enzyme regulationi

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

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

GO - Biological processi

  1. DNA topological change Source: UniProtKB
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
OrganismiChlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Taxonomic identifieri9534 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeChlorocebus

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. chromosome Source: InterPro
  2. nucleolus Source: UniProtKB
  3. nucleoplasm Source: UniProtKB
  4. nucleus Source: UniProtKB
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 1
PRO_0000145199Add
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

PRIDEiQ7YR26.

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ7YR26.
SMRiQ7YR26. 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-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

HOVERGENiHBG007988.

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.

Q7YR26-1 [UniParc]FASTAAdd to Basket

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MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKEKDREKSK    50
HSNSEHKDSE KKHKEKEKTK HKDGSSEKHK DKHKDRDKEK RKEEKVRASG 100
DAKIKKEKEN GFSSPPQIKD EPEDDGYFVP PKEDIKPLKR PRDEDDADYK 150
PKKIKTEDIK KEKKRKLEEE EDGKLRKPKN KDKDKKVPEP DNKKKKPKKE 200
EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPDSV KFYYDGKVMK 250
LSPKAEEVAT FFAKMLDHEY TTKEIFRKNF FKDWRKEMTN EEKNIITNLS 300
KCDFTQMSQY FKAQTEARKQ MSKEEKLKIK EENEKLLKEY GFCIMDNHKE 350
RIANFKIEPP GLFRGRGNHP KMGMLKRRIM PEDIIINCSK DAKVPSPPPG 400
HKWKEVRHDN KVTWLVSWTE NIQGSIKYIM LNPSSRIKGE KDWQKYETAR 450
RLKKCVDKIR NQYREDWKSK EMKVRQRAVA LYFIDKLALR AGNEKEEGET 500
ADTVGCCSLR VEHINLHPEL DGQEYVVEFD FLGKDSIRYY NKVPVEKRVF 550
KNLQLFMENK QPEDDLFDRL NTGILNKHLQ DLMEGLTAKV FRTYNASITL 600
QQQLKELTAP DENIPAKILS YNRANRAVAI LCNHQRAPPK TFEKSMMNLQ 650
SKIDAKKEQL ADARRDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL 700
MKLEVQATDR EENKQIALGT SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ 750
REKFAWAIDM ADEDYEF 767
Length:767
Mass (Da):90,954
Last modified:October 1, 2003 - v1
Checksum:i3E6B4B6738923A5D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB089321 mRNA. Translation: BAC78678.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB089321 mRNA. Translation: BAC78678.1 .

3D structure databases

ProteinModelPortali Q7YR26.
SMRi Q7YR26. Positions 201-767.
ModBasei Search...

Chemistry

BindingDBi Q7YR26.
ChEMBLi CHEMBL5265.

Proteomic databases

PRIDEi Q7YR26.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG007988.

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. "Human topoisomerase I promotes HIV-1 proviral DNA synthesis: Implications for the species specificity and cellular tropism of HIV-1 infection."
    Shoya Y., Tokunaga K., Sawa H., Maeda M., Ueno T., Yoshikawa T., Hasegawa H., Sata T., Kurata T., Hall W.W., Cullen B.R., Takahashi H.
    Proc. Natl. Acad. Sci. U.S.A. 100:8442-8447(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiTOP1_CHLAE
AccessioniPrimary (citable) accession number: Q7YR26
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: October 1, 2003
Last modified: July 9, 2014
This is version 69 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

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