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Q04750

- TOP1_MOUSE

UniProt

Q04750 - TOP1_MOUSE

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Protein
DNA topoisomerase 1
Gene
Top1, Top-1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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. DNA binding Source: UniProtKB-KW
  3. DNA topoisomerase type I activity Source: MGI
  4. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: InterPro
  5. chromatin binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. DNA replication Source: MGI
  2. DNA topological change Source: MGI
  3. chromatin remodeling Source: RefGenome
  4. chromosome segregation Source: RefGenome
  5. embryonic cleavage Source: MGI
  6. response to drug Source: Ensembl
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
Synonyms:Top-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:98788. 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. cytoplasm Source: MGI
  2. cytoplasmic mRNA processing body Source: Ensembl
  3. nucleolus Source: RefGenome
  4. nucleoplasm Source: UniProtKB-SubCell
  5. nucleus Source: MGI
  6. perikaryon Source: MGI
  7. 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 1
PRO_0000145202Add
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-acetyllysine1 Publication
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

MaxQBiQ04750.
PaxDbiQ04750.
PRIDEiQ04750.

PTM databases

PhosphoSiteiQ04750.

Miscellaneous databases

PMAP-CutDBQ04750.

Expressioni

Gene expression databases

ArrayExpressiQ04750.
BgeeiQ04750.
CleanExiMM_TOP1.
GenevestigatoriQ04750.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi204275. 3 interactions.
IntActiQ04750. 2 interactions.
MINTiMINT-1868161.

Structurei

3D structure databases

ProteinModelPortaliQ04750.
SMRiQ04750. Positions 203-767.

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

eggNOGiCOG3569.
GeneTreeiENSGT00390000016347.
HOGENOMiHOG000105469.
HOVERGENiHBG007988.
InParanoidiQ04750.
KOiK03163.
OMAiEFDFPGK.
OrthoDBiEOG7CVPX5.
PhylomeDBiQ04750.
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.

Q04750-1 [UniParc]FASTAAdd to Basket

« Hide

MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKDKDREKSK    50
HSNSEHKDSE KKHKEKEKTK HKDGSSEKHK DKHKDRDKER RKEEKIRAAG 100
DAKIKKEKEN GFSSPPRIKD EPEDDGYFAP PKEDIKPLKR LRDEDDADYK 150
PKKIKTEDIK KEKKRKSEEE EDGKLKKPKN KDKDKKVAEP DNKKKKPKKE 200
EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPESV 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 ADARRDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL 700
MKLEVQATDR EENKQIALGT SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ 750
REKFAWAIDM TDEDYEF 767
Length:767
Mass (Da):90,876
Last modified:July 24, 2007 - v2
Checksum:i4EA654244F07D5C1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911R → P in AAA40466. 1 Publication
Sequence conflicti121 – 1211E → D in BAA00950. 1 Publication
Sequence conflicti129 – 1291A → V in AAA40466. 1 Publication
Sequence conflicti161 – 1611Missing in AAA40466. 1 Publication
Sequence conflicti167 – 1671S → L in AAA40466. 1 Publication
Sequence conflicti277 – 2771R → W in AAA40466. 1 Publication
Sequence conflicti292 – 2921E → G in BAA00950. 1 Publication
Sequence conflicti522 – 5221G → V in AAA40466. 1 Publication
Sequence conflicti533 – 5331G → W in AAA40466. 1 Publication
Sequence conflicti762 – 7621D → Y in AAA40466. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10061 mRNA. Translation: BAA00950.1.
L20632 mRNA. Translation: AAA40466.1.
AL590414, AL591673 Genomic DNA. Translation: CAM20297.1.
AL591673, AL590414 Genomic DNA. Translation: CAM25349.1.
CCDSiCCDS16995.1.
PIRiJU0144.
RefSeqiNP_033434.2. NM_009408.2.
UniGeneiMm.217233.

Genome annotation databases

EnsembliENSMUST00000109468; ENSMUSP00000105094; ENSMUSG00000070544.
GeneIDi21969.
KEGGimmu:21969.
UCSCiuc008nqy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10061 mRNA. Translation: BAA00950.1 .
L20632 mRNA. Translation: AAA40466.1 .
AL590414 , AL591673 Genomic DNA. Translation: CAM20297.1 .
AL591673 , AL590414 Genomic DNA. Translation: CAM25349.1 .
CCDSi CCDS16995.1.
PIRi JU0144.
RefSeqi NP_033434.2. NM_009408.2.
UniGenei Mm.217233.

3D structure databases

ProteinModelPortali Q04750.
SMRi Q04750. Positions 203-767.
ModBasei Search...

Protein-protein interaction databases

BioGridi 204275. 3 interactions.
IntActi Q04750. 2 interactions.
MINTi MINT-1868161.

Chemistry

BindingDBi Q04750.
ChEMBLi CHEMBL2814.

PTM databases

PhosphoSitei Q04750.

Proteomic databases

MaxQBi Q04750.
PaxDbi Q04750.
PRIDEi Q04750.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000109468 ; ENSMUSP00000105094 ; ENSMUSG00000070544 .
GeneIDi 21969.
KEGGi mmu:21969.
UCSCi uc008nqy.1. mouse.

Organism-specific databases

CTDi 7150.
MGIi MGI:98788. Top1.

Phylogenomic databases

eggNOGi COG3569.
GeneTreei ENSGT00390000016347.
HOGENOMi HOG000105469.
HOVERGENi HBG007988.
InParanoidi Q04750.
KOi K03163.
OMAi EFDFPGK.
OrthoDBi EOG7CVPX5.
PhylomeDBi Q04750.
TreeFami TF105281.

Miscellaneous databases

ChiTaRSi TOP1. mouse.
NextBioi 301666.
PMAP-CutDB Q04750.
PROi Q04750.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q04750.
Bgeei Q04750.
CleanExi MM_TOP1.
Genevestigatori Q04750.

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

« Hide 'large scale' publications
  1. "Cloning of the mouse cDNA encoding DNA topoisomerase I and chromosomal location of the gene."
    Koiwai O., Yasui Y., Sakai Y., Watanabe T., Ishii K., Yanagihara S., Andoh T.
    Gene 125:211-216(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Cloning and characterization of mouse topoisomerase I cDNA."
    Hui C.-F., Lo C.K., Hwang J.
    Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-174, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTOP1_MOUSE
AccessioniPrimary (citable) accession number: Q04750
Secondary accession number(s): A2A4B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: July 24, 2007
Last modified: July 9, 2014
This is version 118 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi