UniProtKB - P11387 (TOP1_HUMAN)
Protein
DNA topoisomerase 1
Gene
TOP1
Organism
Homo sapiens (Human)
Status
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
Miscellaneous
Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.
Catalytic activityi
- ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.PROSITE-ProRule annotation3 Publications EC:5.6.2.1
Activity regulationi
Specifically inhibited by camptothecin (CPT), a plant alkaloid with antitumor activity.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 723 | O-(3'-phospho-DNA)-tyrosine intermediatePROSITE-ProRule annotation7 Publications | 1 |
GO - Molecular functioni
- ATP binding Source: CAFA
- chromatin binding Source: UniProtKB
- DNA binding Source: UniProtKB
- DNA topoisomerase type I (single strand cut, ATP-independent) activity Source: UniProtKB
- double-stranded DNA binding Source: CAFA
- protein domain specific binding Source: CAFA
- protein serine/threonine kinase activity Source: CAFA
- RNA binding Source: UniProtKB
- RNA polymerase II proximal promoter sequence-specific DNA binding Source: UniProtKB
- single-stranded DNA binding Source: CAFA
- supercoiled DNA binding Source: CAFA
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
- peptidyl-serine phosphorylation Source: CAFA
- phosphorylation Source: UniProtKB
- programmed cell death Source: UniProtKB
- response to drug Source: UniProtKB
- viral process Source: UniProtKB-KW
Keywordsi
Molecular function | DNA-binding, Isomerase, Topoisomerase |
Biological process | Biological rhythms, Host-virus interaction |
Enzyme and pathway databases
BRENDAi | 5.99.1.2 2681 |
Reactomei | R-HSA-4615885 SUMOylation of DNA replication proteins |
SIGNORi | P11387 |
Names & Taxonomyi
Protein namesi | Recommended name: DNA topoisomerase 1 (EC:5.6.2.1PROSITE-ProRule annotation3 Publications)Alternative name(s): DNA topoisomerase I |
Gene namesi | Name:TOP1 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:11986 TOP1 |
MIMi | 126420 gene |
neXtProti | NX_P11387 |
Subcellular locationi
Nucleus
- nucleolus 1 Publication
- nucleoplasm 1 Publication
Note: Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli.
Nucleus
- fibrillar center Source: HPA
- nucleolus Source: UniProtKB
- nucleoplasm Source: UniProtKB
- nucleus Source: UniProtKB
- replication fork protection complex Source: GO_Central
Other locations
- P-body Source: UniProtKB
- perikaryon Source: Ensembl
- protein-DNA complex Source: CAFA
Keywords - Cellular componenti
NucleusPathology & 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 NUP98.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 103 | K → 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 Publication | 1 | |
Mutagenesisi | 117 | K → 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 Publication | 1 | |
Mutagenesisi | 153 | K → 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 Publication | 1 | |
Mutagenesisi | 532 | K → A: Almost abolishes enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 532 | K → R: Strongly reduced enzyme activity. 1 Publication | 1 | |
Mutagenesisi | 723 | Y → F: No change in CPT-induced clearing from nuclei. 1 Publication | 1 |
Keywords - Diseasei
Proto-oncogeneOrganism-specific databases
DisGeNETi | 7150 |
OpenTargetsi | ENSG00000198900 |
PharmGKBi | PA353 |
Miscellaneous databases
Pharosi | P11387 |
Chemistry databases
ChEMBLi | CHEMBL1781 |
DrugBanki | DB07354 2,3-DIMETHOXY-12H-[1,3]DIOXOLO[5,6]INDENO[1,2-C]ISOQUINOLIN-6-IUM DB08159 4-(5,11-DIOXO-5H-INDENO[1,2-C]ISOQUINOLIN-6(11H)-YL)BUTANOATE DB05482 7-ethyl-10-hydroxycamptothecin DB04690 Camptothecin DB05806 Cositecan DB04882 Edotecarin DB05129 Elsamitrucin DB11254 Hexylresorcinol DB00762 Irinotecan DB04967 Lucanthone DB06159 Rubitecan DB05630 Sodium stibogluconate DB01030 Topotecan DB06069 XMT-1001 |
DrugCentrali | P11387 |
Polymorphism and mutation databases
BioMutai | TOP1 |
DMDMi | 12644118 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources1 Publication | |||
ChainiPRO_0000145201 | 2 – 765 | DNA topoisomerase 1Add BLAST | 764 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources1 Publication | 1 | |
Modified residuei | 2 | PhosphoserineCombined sources | 1 | |
Modified residuei | 10 | PhosphoserineCombined sources | 1 | |
Modified residuei | 57 | PhosphoserineCombined sources | 1 | |
Cross-linki | 101 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 103 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateCurated | ||
Cross-linki | 103 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Modified residuei | 112 | PhosphoserineCombined sources | 1 | |
Cross-linki | 117 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate | ||
Cross-linki | 117 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources | ||
Cross-linki | 117 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Cross-linki | 134 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 148 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 153 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateCurated | ||
Cross-linki | 153 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Cross-linki | 158 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 164 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 172 | N6-acetyllysine; alternateBy similarity | 1 | |
Cross-linki | 172 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Cross-linki | 204 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 280 | N6-acetyllysineCombined sources | 1 | |
Cross-linki | 336 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 506 | Phosphoserine; by CK21 Publication | 1 | |
Cross-linki | 549 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 642 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 700 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Cross-linki | 712 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources |
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 conjugationProteomic databases
EPDi | P11387 |
jPOSTi | P11387 |
MassIVEi | P11387 |
MaxQBi | P11387 |
PaxDbi | P11387 |
PeptideAtlasi | P11387 |
PRIDEi | P11387 |
ProteomicsDBi | 52766 |
2D gel databases
SWISS-2DPAGEi | P11387 |
PTM databases
iPTMneti | P11387 |
PhosphoSitePlusi | P11387 |
SwissPalmi | P11387 |
Miscellaneous databases
PMAP-CutDBi | P11387 |
Expressioni
Tissue specificityi
Endothelial cells.1 Publication
Gene expression databases
Bgeei | ENSG00000198900 Expressed in 232 organ(s), highest expression level in trabecular bone tissue |
Genevisiblei | P11387 HS |
Organism-specific databases
HPAi | CAB009058 HPA019039 |
Interactioni
Subunit structurei
(Microbial infection) Interacts with SV40 Large T antigen; this interactions allows viral DNA replication.
1 PublicationSites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 316 | Interaction with DNA | 1 | |
Sitei | 364 | Interaction with DNA | 1 | |
Sitei | 412 | Interaction with DNA | 1 | |
Sitei | 443 | Interaction with DNA | 1 | |
Sitei | 501 | Interaction with DNA | 1 | |
Sitei | 532 | Interaction with DNA | 1 | |
Sitei | 574 | Interaction with DNA | 1 | |
Sitei | 632 | Interaction with DNA | 1 | |
Sitei | 650 | Interaction with DNA | 1 |
Binary interactionsi
GO - Molecular functioni
- protein domain specific binding Source: CAFA
Protein-protein interaction databases
BioGridi | 113003, 209 interactors |
CORUMi | P11387 |
DIPi | DIP-36356N |
ELMi | P11387 |
IntActi | P11387, 93 interactors |
MINTi | P11387 |
STRINGi | 9606.ENSP00000354522 |
Chemistry databases
BindingDBi | P11387 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P11387 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P11387 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 425 – 426 | Interaction with DNA | 2 | |
Regioni | 488 – 493 | Interaction with DNA | 6 | |
Regioni | 585 – 587 | Interaction with DNA | 3 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 23 – 204 | Lys-richAdd BLAST | 182 |
Sequence similaritiesi
Belongs to the type IB topoisomerase family.Curated
Phylogenomic databases
eggNOGi | KOG0981 Eukaryota COG3569 LUCA |
GeneTreei | ENSGT00940000155006 |
InParanoidi | P11387 |
KOi | K03163 |
OMAi | CSLKYEH |
OrthoDBi | 303947at2759 |
PhylomeDBi | P11387 |
TreeFami | TF105281 |
Family and domain databases
CDDi | cd00659 Topo_IB_C, 1 hit |
DisProti | DP00075 |
Gene3Di | 1.10.10.41, 1 hit 1.10.132.10, 1 hit 2.170.11.10, 1 hit 3.90.15.10, 1 hit |
InterProi | View protein in InterPro IPR011010 DNA_brk_join_enz IPR013034 DNA_topo_DNA_db_N_dom1 IPR013030 DNA_topo_DNA_db_N_dom2 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 IPR036202 TopoI_DNA-bd_euk_N_sf IPR013499 TopoI_euk |
Pfami | View protein in Pfam PF14370 Topo_C_assoc, 1 hit PF01028 Topoisom_I, 1 hit PF02919 Topoisom_I_N, 1 hit |
PRINTSi | PR00416 EUTPISMRASEI |
SMARTi | View protein in SMART SM00435 TOPEUc, 1 hit |
SUPFAMi | SSF56349 SSF56349, 1 hit SSF56741 SSF56741, 1 hit |
PROSITEi | View protein in PROSITE PS00176 TOPOISOMERASE_I_EUK, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P11387-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence CAA36834 differs from that shown. Reason: Erroneous gene model prediction.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 145 | A → V in AAA61207 (PubMed:2833744).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_052592 | 214 | G → S. Corresponds to variant dbSNP:rs6029542Ensembl. | 1 | |
Natural variantiVAR_036555 | 326 | K → R in breast cancer; somatic mutation. 1 Publication | 1 | |
Natural variantiVAR_010666 | 370 | M → T in CPT-resistant leukemia. 1 Publication | 1 | |
Natural variantiVAR_007530 | 533 | D → G in CPT-resistant leukemia. 1 PublicationCorresponds to variant dbSNP:rs267607131EnsemblClinVar. | 1 | |
Natural variantiVAR_010667 | 722 | N → S in CPT-resistant leukemia. 1 Publication | 1 | |
Natural variantiVAR_007531 | 729 | T → A in CPT-resistant lung cancer. 1 Publication | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | J03250 mRNA Translation: AAA61207.1 M60706 M60705 Genomic DNA Translation: AAA61206.1 AK292943 mRNA Translation: BAF85632.1 AL035652 Genomic DNA No translation available. AL022394 Genomic DNA No translation available. 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 |
CCDSi | CCDS13312.1 |
PIRi | A30887 ISHUT1 |
RefSeqi | NP_003277.1, NM_003286.3 |
Genome annotation databases
Ensembli | ENST00000361337; ENSP00000354522; ENSG00000198900 |
GeneIDi | 7150 |
KEGGi | hsa:7150 |
UCSCi | uc002xjl.4 human |
Keywords - Coding sequence diversityi
Chromosomal rearrangement, PolymorphismSimilar proteinsi
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 M60705 Genomic DNA Translation: AAA61206.1 AK292943 mRNA Translation: BAF85632.1 AL035652 Genomic DNA No translation available. AL022394 Genomic DNA No translation available. 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 |
CCDSi | CCDS13312.1 |
PIRi | A30887 ISHUT1 |
RefSeqi | NP_003277.1, NM_003286.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1A31 | X-ray | 2.10 | A | 175-765 | [»] | |
1A35 | X-ray | 2.50 | A | 175-765 | [»] | |
1A36 | X-ray | 2.80 | A | 175-765 | [»] | |
1EJ9 | X-ray | 2.60 | A | 203-765 | [»] | |
1K4S | X-ray | 3.20 | A | 174-765 | [»] | |
1K4T | X-ray | 2.10 | A | 174-765 | [»] | |
1LPQ | X-ray | 3.14 | A | 202-765 | [»] | |
1NH3 | X-ray | 3.10 | A | 203-765 | [»] | |
1R49 | X-ray | 3.13 | A | 174-765 | [»] | |
1RR8 | X-ray | 2.60 | C | 203-765 | [»] | |
1RRJ | X-ray | 2.30 | A | 201-765 | [»] | |
1SC7 | X-ray | 3.00 | A | 174-765 | [»] | |
1SEU | X-ray | 3.00 | A | 174-765 | [»] | |
1T8I | X-ray | 3.00 | A | 174-765 | [»] | |
1TL8 | X-ray | 3.10 | A | 174-765 | [»] | |
SMRi | P11387 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGridi | 113003, 209 interactors |
CORUMi | P11387 |
DIPi | DIP-36356N |
ELMi | P11387 |
IntActi | P11387, 93 interactors |
MINTi | P11387 |
STRINGi | 9606.ENSP00000354522 |
Chemistry databases
BindingDBi | P11387 |
ChEMBLi | CHEMBL1781 |
DrugBanki | DB07354 2,3-DIMETHOXY-12H-[1,3]DIOXOLO[5,6]INDENO[1,2-C]ISOQUINOLIN-6-IUM DB08159 4-(5,11-DIOXO-5H-INDENO[1,2-C]ISOQUINOLIN-6(11H)-YL)BUTANOATE DB05482 7-ethyl-10-hydroxycamptothecin DB04690 Camptothecin DB05806 Cositecan DB04882 Edotecarin DB05129 Elsamitrucin DB11254 Hexylresorcinol DB00762 Irinotecan DB04967 Lucanthone DB06159 Rubitecan DB05630 Sodium stibogluconate DB01030 Topotecan DB06069 XMT-1001 |
DrugCentrali | P11387 |
PTM databases
iPTMneti | P11387 |
PhosphoSitePlusi | P11387 |
SwissPalmi | P11387 |
Polymorphism and mutation databases
BioMutai | TOP1 |
DMDMi | 12644118 |
2D gel databases
SWISS-2DPAGEi | P11387 |
Proteomic databases
EPDi | P11387 |
jPOSTi | P11387 |
MassIVEi | P11387 |
MaxQBi | P11387 |
PaxDbi | P11387 |
PeptideAtlasi | P11387 |
PRIDEi | P11387 |
ProteomicsDBi | 52766 |
Genome annotation databases
Ensembli | ENST00000361337; ENSP00000354522; ENSG00000198900 |
GeneIDi | 7150 |
KEGGi | hsa:7150 |
UCSCi | uc002xjl.4 human |
Organism-specific databases
CTDi | 7150 |
DisGeNETi | 7150 |
GeneCardsi | TOP1 |
HGNCi | HGNC:11986 TOP1 |
HPAi | CAB009058 HPA019039 |
MIMi | 126420 gene |
neXtProti | NX_P11387 |
OpenTargetsi | ENSG00000198900 |
PharmGKBi | PA353 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0981 Eukaryota COG3569 LUCA |
GeneTreei | ENSGT00940000155006 |
InParanoidi | P11387 |
KOi | K03163 |
OMAi | CSLKYEH |
OrthoDBi | 303947at2759 |
PhylomeDBi | P11387 |
TreeFami | TF105281 |
Enzyme and pathway databases
BRENDAi | 5.99.1.2 2681 |
Reactomei | R-HSA-4615885 SUMOylation of DNA replication proteins |
SIGNORi | P11387 |
Miscellaneous databases
ChiTaRSi | TOP1 human |
EvolutionaryTracei | P11387 |
GeneWikii | TOP1 |
GenomeRNAii | 7150 |
Pharosi | P11387 |
PMAP-CutDBi | P11387 |
PROi | PR:P11387 |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000198900 Expressed in 232 organ(s), highest expression level in trabecular bone tissue |
Genevisiblei | P11387 HS |
Family and domain databases
CDDi | cd00659 Topo_IB_C, 1 hit |
DisProti | DP00075 |
Gene3Di | 1.10.10.41, 1 hit 1.10.132.10, 1 hit 2.170.11.10, 1 hit 3.90.15.10, 1 hit |
InterProi | View protein in InterPro IPR011010 DNA_brk_join_enz IPR013034 DNA_topo_DNA_db_N_dom1 IPR013030 DNA_topo_DNA_db_N_dom2 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 IPR036202 TopoI_DNA-bd_euk_N_sf IPR013499 TopoI_euk |
Pfami | View protein in Pfam PF14370 Topo_C_assoc, 1 hit PF01028 Topoisom_I, 1 hit PF02919 Topoisom_I_N, 1 hit |
PRINTSi | PR00416 EUTPISMRASEI |
SMARTi | View protein in SMART SM00435 TOPEUc, 1 hit |
SUPFAMi | SSF56349 SSF56349, 1 hit SSF56741 SSF56741, 1 hit |
PROSITEi | View protein in PROSITE PS00176 TOPOISOMERASE_I_EUK, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TOP1_HUMAN | |
Accessioni | P11387Primary (citable) accession number: P11387 Secondary accession number(s): A8KA78 Q9UJN0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | December 1, 2000 | |
Last modified: | November 13, 2019 | |
This is version 223 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 20
Human chromosome 20: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - SIMILARITY comments
Index of protein domains and families - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references