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Q04750

- TOP1_MOUSE

UniProt

Q04750 - TOP1_MOUSE

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Protein

DNA topoisomerase 1

Gene

Top1

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).By similarity

Catalytic activityi

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

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: Ensembl
  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. poly(A) RNA binding Source: Ensembl

GO - Biological processi

  1. chromatin remodeling Source: RefGenome
  2. chromosome segregation Source: RefGenome
  3. DNA replication Source: MGI
  4. DNA topological change Source: MGI
  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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytoplasmic mRNA processing body Source: Ensembl
  3. nucleolus Source: RefGenome
  4. nucleoplasm Source: Ensembl
  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 – 11RemovedBy similarity
Chaini2 – 767766DNA topoisomerase 1PRO_0000145202Add
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-acetyllysine1 Publication
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).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

BgeeiQ04750.
CleanExiMM_TOP1.
ExpressionAtlasiQ04750. baseline and differential.
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.
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

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

        10         20         30         40         50
MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKDKDREKSK
60 70 80 90 100
HSNSEHKDSE KKHKEKEKTK HKDGSSEKHK DKHKDRDKER RKEEKIRAAG
110 120 130 140 150
DAKIKKEKEN GFSSPPRIKD EPEDDGYFAP PKEDIKPLKR LRDEDDADYK
160 170 180 190 200
PKKIKTEDIK KEKKRKSEEE EDGKLKKPKN KDKDKKVAEP DNKKKKPKKE
210 220 230 240 250
EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPESV KFYYDGKVMK
260 270 280 290 300
LSPKAEEVAT FFAKMLDHEY TTKEIFRKNF FKDWRKEMTN DEKNTITNLS
310 320 330 340 350
KCDFTQMSQY FKAQSEARKQ MSKEEKLKIK EENEKLLKEY GFCVMDNHRE
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 FPGKDSIRYY NKVPVEKRVF
560 570 580 590 600
KNLQLFMENK QPEDDLFDRL NTGILNKHLQ DLMEGLTAKV FRTYNASITL
610 620 630 640 650
QQQLKELTAP DENVPAKILS YNRANRAVAI LCNHQRAPPK TFEKSMMNLQ
660 670 680 690 700
SKIDAKKDQL ADARRDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL
710 720 730 740 750
MKLEVQATDR EENKQIALGT SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ
760
REKFAWAIDM TDEDYEF
Length:767
Mass (Da):90,876
Last modified:July 24, 2007 - v2
Checksum:i4EA654244F07D5C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911R → P in AAA40466. 1 PublicationCurated
Sequence conflicti121 – 1211E → D in BAA00950. (PubMed:8096488)Curated
Sequence conflicti129 – 1291A → V in AAA40466. 1 PublicationCurated
Sequence conflicti161 – 1611Missing in AAA40466. 1 PublicationCurated
Sequence conflicti167 – 1671S → L in AAA40466. 1 PublicationCurated
Sequence conflicti277 – 2771R → W in AAA40466. 1 PublicationCurated
Sequence conflicti292 – 2921E → G in BAA00950. (PubMed:8096488)Curated
Sequence conflicti522 – 5221G → V in AAA40466. 1 PublicationCurated
Sequence conflicti533 – 5331G → W in AAA40466. 1 PublicationCurated
Sequence conflicti762 – 7621D → Y in AAA40466. 1 PublicationCurated

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...
MobiDBi 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

Bgeei Q04750.
CleanExi MM_TOP1.
ExpressionAtlasi Q04750. baseline and differential.
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: October 29, 2014
This is version 120 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