Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7YR26

- TOP1_CHLAE

UniProt

Q7YR26 - TOP1_CHLAE

(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)

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. Involved in the circadian transcription of the core circadian clock component ARNTL/BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the ARNTL/BMAL1 promoter.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
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Biological processi

Biological rhythms

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 By similarity. Nucleusnucleoplasm By similarity
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 – 11RemovedBy similarity
Chaini2 – 767766DNA topoisomerase 1PRO_0000145199Add
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
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.
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.

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

« Hide

        10         20         30         40         50
MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKEKDREKSK
60 70 80 90 100
HSNSEHKDSE KKHKEKEKTK HKDGSSEKHK DKHKDRDKEK RKEEKVRASG
110 120 130 140 150
DAKIKKEKEN GFSSPPQIKD EPEDDGYFVP PKEDIKPLKR PRDEDDADYK
160 170 180 190 200
PKKIKTEDIK KEKKRKLEEE EDGKLRKPKN KDKDKKVPEP DNKKKKPKKE
210 220 230 240 250
EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPDSV KFYYDGKVMK
260 270 280 290 300
LSPKAEEVAT FFAKMLDHEY TTKEIFRKNF FKDWRKEMTN EEKNIITNLS
310 320 330 340 350
KCDFTQMSQY FKAQTEARKQ MSKEEKLKIK EENEKLLKEY GFCIMDNHKE
360 370 380 390 400
RIANFKIEPP GLFRGRGNHP KMGMLKRRIM PEDIIINCSK DAKVPSPPPG
410 420 430 440 450
HKWKEVRHDN KVTWLVSWTE NIQGSIKYIM LNPSSRIKGE KDWQKYETAR
460 470 480 490 500
RLKKCVDKIR NQYREDWKSK EMKVRQRAVA LYFIDKLALR AGNEKEEGET
510 520 530 540 550
ADTVGCCSLR VEHINLHPEL DGQEYVVEFD FLGKDSIRYY NKVPVEKRVF
560 570 580 590 600
KNLQLFMENK QPEDDLFDRL NTGILNKHLQ DLMEGLTAKV FRTYNASITL
610 620 630 640 650
QQQLKELTAP DENIPAKILS YNRANRAVAI LCNHQRAPPK TFEKSMMNLQ
660 670 680 690 700
SKIDAKKEQL ADARRDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL
710 720 730 740 750
MKLEVQATDR EENKQIALGT SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ
760
REKFAWAIDM ADEDYEF
Length:767
Mass (Da):90,954
Last modified:October 1, 2003 - v1
Checksum:i3E6B4B6738923A5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB089321 mRNA. Translation: BAC78678.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB089321 mRNA. Translation: BAC78678.1 .

3D structure databases

ProteinModelPortali Q7YR26.
SMRi Q7YR26. Positions 201-767.
ModBasei Search...
MobiDBi 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: November 26, 2014
This is version 71 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