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Protein

DNA topoisomerase 1

Gene

TOP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 rotates around the intact phosphodiester bond on the opposing 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 (By similarity). 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 similarity5 Publications

Catalytic activityi

ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.PROSITE-ProRule annotation3 Publications

Enzyme regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei723O-(3'-phospho-DNA)-tyrosine intermediatePROSITE-ProRule annotation7 Publications1

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA topoisomerase type I activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • chromatin remodeling Source: UniProtKB
  • chromosome segregation Source: GO_Central
  • circadian regulation of gene expression Source: UniProtKB
  • circadian rhythm Source: UniProtKB
  • DNA replication Source: GO_Central
  • DNA topological change Source: UniProtKB
  • embryonic cleavage Source: Ensembl
  • phosphorylation Source: UniProtKB
  • programmed cell death Source: UniProtKB
  • protein sumoylation Source: Reactome
  • response to drug Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Biological processi

Biological rhythms, Host-virus interaction

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:HS04730-MONOMER.
BRENDAi5.99.1.2. 2681.
ReactomeiR-HSA-4615885. SUMOylation of DNA replication proteins.
SIGNORiP11387.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 1 (EC:5.99.1.2)
Alternative name(s):
DNA topoisomerase I
Gene namesi
Name:TOP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11986. TOP1.

Subcellular locationi

  • Nucleusnucleolus 1 Publication
  • Nucleusnucleoplasm 1 Publication

  • 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.

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • perikaryon Source: Ensembl
  • replication fork protection complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving TOP1 is found in a form of therapy-related myelodysplastic syndrome. Translocation t(11;20)(p15;q11) with NUP98.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi103K → R: Localizes in both nucleoplasm and nucleoli; when associated with R-117 or R-153. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-117 and R-153. 1 Publication1
Mutagenesisi117K → R: 5-fold decrease in sumoylation. Localizes in both nucleoplasm and nucleoli; when associated with or without R-103 or R-153. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-103 and R-153. 1 Publication1
Mutagenesisi153K → R: Localizes in both nucleoplasm and nucleoli; when associated with R-103 or R-117. Almost complete loss of sumoylation, concentrates in nucleoli and no clearing from nucleoli on CPT treatment; when associated with R-103 and R-117. 1 Publication1
Mutagenesisi532K → A: Almost abolishes enzyme activity. 1 Publication1
Mutagenesisi532K → R: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi723Y → F: No change in CPT-induced clearing from nuclei. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi7150.
OpenTargetsiENSG00000198900.
PharmGKBiPA353.

Chemistry databases

ChEMBLiCHEMBL1781.
DrugBankiDB00762. Irinotecan.
DB04967. Lucanthone.
DB05630. Sodium stibogluconate.
DB01030. Topotecan.

Polymorphism and mutation databases

BioMutaiTOP1.
DMDMi12644118.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001452012 – 765DNA topoisomerase 1Add BLAST764

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources1
Modified residuei10PhosphoserineCombined sources1
Modified residuei57PhosphoserineCombined sources1
Cross-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
Modified residuei112PhosphoserineCombined sources1
Cross-linki117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateCurated
Cross-linki153Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki158Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei172N6-acetyllysineBy similarity1
Modified residuei280N6-acetyllysineCombined sources1
Cross-linki336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei506Phosphoserine; by CK21 Publication1

Post-translational modificationi

Sumoylated. Lys-117 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.1 Publication
Phosphorylation at Ser-506 by CK2 increases binding to supercoiled DNA and sensitivity to camptothecin.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP11387.
MaxQBiP11387.
PaxDbiP11387.
PeptideAtlasiP11387.
PRIDEiP11387.

2D gel databases

SWISS-2DPAGEP11387.

PTM databases

iPTMnetiP11387.
PhosphoSitePlusiP11387.
SwissPalmiP11387.

Miscellaneous databases

PMAP-CutDBP11387.

Expressioni

Tissue specificityi

Endothelial cells.1 Publication

Gene expression databases

BgeeiENSG00000198900.
CleanExiHS_TOP1.
GenevisibleiP11387. HS.

Organism-specific databases

HPAiCAB009058.
HPA019039.

Interactioni

Subunit structurei

Monomer. Interacts with SV40 Large T antigen; this interactions allows viral DNA replication.8 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei316Interaction with DNA1
Sitei364Interaction with DNA1
Sitei412Interaction with DNA1
Sitei443Interaction with DNA1
Sitei501Interaction with DNA1
Sitei532Interaction with DNA1
Sitei574Interaction with DNA1
Sitei632Interaction with DNA1
Sitei650Interaction with DNA1

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005197EBI-876302,EBI-375543
MYCP011062EBI-876302,EBI-447544
NKX3-1Q998016EBI-876302,EBI-1385894

Protein-protein interaction databases

BioGridi113003. 152 interactors.
DIPiDIP-36356N.
IntActiP11387. 61 interactors.
MINTiMINT-94018.
STRINGi9606.ENSP00000354522.

Chemistry databases

BindingDBiP11387.

Structurei

Secondary structure

1765
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi205 – 207Combined sources3
Beta strandi220 – 222Combined sources3
Beta strandi236 – 238Combined sources3
Beta strandi240 – 242Combined sources3
Beta strandi245 – 247Combined sources3
Helixi251 – 261Combined sources11
Turni262 – 265Combined sources4
Helixi267 – 270Combined sources4
Helixi272 – 285Combined sources14
Helixi288 – 293Combined sources6
Helixi297 – 299Combined sources3
Helixi303 – 317Combined sources15
Helixi321 – 338Combined sources18
Beta strandi339 – 343Combined sources5
Beta strandi346 – 351Combined sources6
Beta strandi358 – 360Combined sources3
Beta strandi364 – 366Combined sources3
Turni368 – 371Combined sources4
Helixi379 – 381Combined sources3
Beta strandi383 – 385Combined sources3
Beta strandi396 – 398Combined sources3
Beta strandi402 – 405Combined sources4
Beta strandi413 – 417Combined sources5
Turni419 – 421Combined sources3
Beta strandi424 – 427Combined sources4
Beta strandi431 – 433Combined sources3
Helixi434 – 464Combined sources31
Helixi470 – 485Combined sources16
Turni495 – 497Combined sources3
Helixi504 – 506Combined sources3
Helixi509 – 511Combined sources3
Beta strandi514 – 518Combined sources5
Beta strandi521 – 530Combined sources10
Helixi532 – 534Combined sources3
Beta strandi536 – 542Combined sources7
Helixi545 – 553Combined sources9
Turni554 – 557Combined sources4
Turni564 – 567Combined sources4
Helixi570 – 580Combined sources11
Beta strandi581 – 583Combined sources3
Helixi586 – 605Combined sources20
Beta strandi608 – 610Combined sources3
Helixi612 – 625Combined sources14
Turni626 – 631Combined sources6
Helixi640 – 643Combined sources4
Helixi644 – 673Combined sources30
Helixi678 – 710Combined sources33
Beta strandi712 – 714Combined sources3
Turni721 – 723Combined sources3
Helixi726 – 735Combined sources10
Helixi740 – 742Combined sources3
Helixi746 – 751Combined sources6
Helixi753 – 758Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A31X-ray2.10A175-765[»]
1A35X-ray2.50A175-765[»]
1A36X-ray2.80A175-765[»]
1EJ9X-ray2.60A203-765[»]
1K4SX-ray3.20A174-765[»]
1K4TX-ray2.10A174-765[»]
1LPQX-ray3.14A202-765[»]
1NH3X-ray3.10A203-765[»]
1R49X-ray3.13A174-765[»]
1RR8X-ray2.60C203-765[»]
1RRJX-ray2.30A201-765[»]
1SC7X-ray3.00A174-765[»]
1SEUX-ray3.00A174-765[»]
1T8IX-ray3.00A174-765[»]
1TL8X-ray3.10A174-765[»]
DisProtiDP00075.
ProteinModelPortaliP11387.
SMRiP11387.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11387.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni425 – 426Interaction with DNA2
Regioni488 – 493Interaction with DNA6
Regioni585 – 587Interaction with DNA3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi23 – 204Lys-richAdd BLAST182

Sequence similaritiesi

Belongs to the type IB topoisomerase family.Curated

Phylogenomic databases

eggNOGiKOG0981. Eukaryota.
COG3569. LUCA.
GeneTreeiENSGT00390000016347.
HOVERGENiHBG007988.
InParanoidiP11387.
KOiK03163.
OMAiVMDNHKE.
OrthoDBiEOG091G02KT.
PhylomeDBiP11387.
TreeFamiTF105281.

Family and domain databases

CDDicd00659. Topo_IB_C. 1 hit.
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.

P11387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK EKDREKSKHS
60 70 80 90 100
NSEHKDSEKK HKEKEKTKHK DGSSEKHKDK HKDRDKEKRK EEKVRASGDA
110 120 130 140 150
KIKKEKENGF SSPPQIKDEP EDDGYFVPPK EDIKPLKRPR DEDDADYKPK
160 170 180 190 200
KIKTEDTKKE KKRKLEEEED GKLKKPKNKD KDKKVPEPDN KKKKPKKEEE
210 220 230 240 250
QKWKWWEEER YPEGIKWKFL EHKGPVFAPP YEPLPENVKF YYDGKVMKLS
260 270 280 290 300
PKAEEVATFF AKMLDHEYTT KEIFRKNFFK DWRKEMTNEE KNIITNLSKC
310 320 330 340 350
DFTQMSQYFK AQTEARKQMS KEEKLKIKEE NEKLLKEYGF CIMDNHKERI
360 370 380 390 400
ANFKIEPPGL FRGRGNHPKM GMLKRRIMPE DIIINCSKDA KVPSPPPGHK
410 420 430 440 450
WKEVRHDNKV TWLVSWTENI QGSIKYIMLN PSSRIKGEKD WQKYETARRL
460 470 480 490 500
KKCVDKIRNQ YREDWKSKEM KVRQRAVALY FIDKLALRAG NEKEEGETAD
510 520 530 540 550
TVGCCSLRVE HINLHPELDG QEYVVEFDFL GKDSIRYYNK VPVEKRVFKN
560 570 580 590 600
LQLFMENKQP EDDLFDRLNT GILNKHLQDL MEGLTAKVFR TYNASITLQQ
610 620 630 640 650
QLKELTAPDE NIPAKILSYN RANRAVAILC NHQRAPPKTF EKSMMNLQTK
660 670 680 690 700
IDAKKEQLAD ARRDLKSAKA DAKVMKDAKT KKVVESKKKA VQRLEEQLMK
710 720 730 740 750
LEVQATDREE NKQIALGTSK LNYLDPRITV AWCKKWGVPI EKIYNKTQRE
760
KFAWAIDMAD EDYEF
Length:765
Mass (Da):90,726
Last modified:December 1, 2000 - v2
Checksum:i6FBED540BCF7BE28
GO

Sequence cautioni

The sequence CAA36834 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145A → V in AAA61207 (PubMed:2833744).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052592214G → S.Corresponds to variant rs6029542dbSNPEnsembl.1
Natural variantiVAR_036555326K → R in breast cancer; somatic mutation. 1 Publication1
Natural variantiVAR_010666370M → T in CPT-resistant leukemia. 1 Publication1
Natural variantiVAR_007530533D → G in CPT-resistant leukemia. 1 PublicationCorresponds to variant rs267607131dbSNPEnsembl.1
Natural variantiVAR_010667722N → S in CPT-resistant leukemia. 1 Publication1
Natural variantiVAR_007531729T → A in CPT-resistant lung cancer. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03250 mRNA. Translation: AAA61207.1.
M60706
, M60688, M60689, M60690, M60691, M60692, M60693, M60694, M60695, M60696, M60697, M60698, M60699, M60700, M60701, M60702, M60703, M60704, M60705 Genomic DNA. Translation: AAA61206.1.
AK292943 mRNA. Translation: BAF85632.1.
AL035652, AL022394 Genomic DNA. Translation: CAI19767.1.
AL022394, AL035652 Genomic DNA. Translation: CAI42886.1.
CH471077 Genomic DNA. Translation: EAW75994.1.
CH471077 Genomic DNA. Translation: EAW75995.1.
X52601 Genomic DNA. Translation: CAA36834.1. Sequence problems.
U07804 mRNA. Translation: AAB60379.1.
U07806 mRNA. Translation: AAB60380.1.
X16479 mRNA. Translation: CAA34500.2.
M27913 mRNA. Translation: AAA61208.1.
CCDSiCCDS13312.1.
PIRiA30887. ISHUT1.
RefSeqiNP_003277.1. NM_003286.3.
UniGeneiHs.472737.

Genome annotation databases

EnsembliENST00000361337; ENSP00000354522; ENSG00000198900.
GeneIDi7150.
KEGGihsa:7150.
UCSCiuc002xjl.4. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03250 mRNA. Translation: AAA61207.1.
M60706
, M60688, M60689, M60690, M60691, M60692, M60693, M60694, M60695, M60696, M60697, M60698, M60699, M60700, M60701, M60702, M60703, M60704, M60705 Genomic DNA. Translation: AAA61206.1.
AK292943 mRNA. Translation: BAF85632.1.
AL035652, AL022394 Genomic DNA. Translation: CAI19767.1.
AL022394, AL035652 Genomic DNA. Translation: CAI42886.1.
CH471077 Genomic DNA. Translation: EAW75994.1.
CH471077 Genomic DNA. Translation: EAW75995.1.
X52601 Genomic DNA. Translation: CAA36834.1. Sequence problems.
U07804 mRNA. Translation: AAB60379.1.
U07806 mRNA. Translation: AAB60380.1.
X16479 mRNA. Translation: CAA34500.2.
M27913 mRNA. Translation: AAA61208.1.
CCDSiCCDS13312.1.
PIRiA30887. ISHUT1.
RefSeqiNP_003277.1. NM_003286.3.
UniGeneiHs.472737.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A31X-ray2.10A175-765[»]
1A35X-ray2.50A175-765[»]
1A36X-ray2.80A175-765[»]
1EJ9X-ray2.60A203-765[»]
1K4SX-ray3.20A174-765[»]
1K4TX-ray2.10A174-765[»]
1LPQX-ray3.14A202-765[»]
1NH3X-ray3.10A203-765[»]
1R49X-ray3.13A174-765[»]
1RR8X-ray2.60C203-765[»]
1RRJX-ray2.30A201-765[»]
1SC7X-ray3.00A174-765[»]
1SEUX-ray3.00A174-765[»]
1T8IX-ray3.00A174-765[»]
1TL8X-ray3.10A174-765[»]
DisProtiDP00075.
ProteinModelPortaliP11387.
SMRiP11387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113003. 152 interactors.
DIPiDIP-36356N.
IntActiP11387. 61 interactors.
MINTiMINT-94018.
STRINGi9606.ENSP00000354522.

Chemistry databases

BindingDBiP11387.
ChEMBLiCHEMBL1781.
DrugBankiDB00762. Irinotecan.
DB04967. Lucanthone.
DB05630. Sodium stibogluconate.
DB01030. Topotecan.

PTM databases

iPTMnetiP11387.
PhosphoSitePlusiP11387.
SwissPalmiP11387.

Polymorphism and mutation databases

BioMutaiTOP1.
DMDMi12644118.

2D gel databases

SWISS-2DPAGEP11387.

Proteomic databases

EPDiP11387.
MaxQBiP11387.
PaxDbiP11387.
PeptideAtlasiP11387.
PRIDEiP11387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361337; ENSP00000354522; ENSG00000198900.
GeneIDi7150.
KEGGihsa:7150.
UCSCiuc002xjl.4. human.

Organism-specific databases

CTDi7150.
DisGeNETi7150.
GeneCardsiTOP1.
H-InvDBHIX0015818.
HIX0040702.
HGNCiHGNC:11986. TOP1.
HPAiCAB009058.
HPA019039.
MIMi126420. gene.
neXtProtiNX_P11387.
OpenTargetsiENSG00000198900.
PharmGKBiPA353.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0981. Eukaryota.
COG3569. LUCA.
GeneTreeiENSGT00390000016347.
HOVERGENiHBG007988.
InParanoidiP11387.
KOiK03163.
OMAiVMDNHKE.
OrthoDBiEOG091G02KT.
PhylomeDBiP11387.
TreeFamiTF105281.

Enzyme and pathway databases

BioCyciZFISH:HS04730-MONOMER.
BRENDAi5.99.1.2. 2681.
ReactomeiR-HSA-4615885. SUMOylation of DNA replication proteins.
SIGNORiP11387.

Miscellaneous databases

ChiTaRSiTOP1. human.
EvolutionaryTraceiP11387.
GeneWikiiTOP1.
GenomeRNAii7150.
PMAP-CutDBP11387.
PROiP11387.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198900.
CleanExiHS_TOP1.
GenevisibleiP11387. HS.

Family and domain databases

CDDicd00659. Topo_IB_C. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiTOP1_HUMAN
AccessioniPrimary (citable) accession number: P11387
Secondary accession number(s): A8KA78
, E1P5W3, O43256, Q12855, Q12856, Q15610, Q5TFY3, Q9UJN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 2000
Last modified: November 30, 2016
This is version 194 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.