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UniProtKB - P11387 (TOP1_HUMAN)

Entry version 226 (22 Apr 2020)
Sequence version 2 (01 Dec 2000)
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Protein

DNA topoisomerase 1

Gene

TOP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei723O-(3'-phospho-DNA)-tyrosine intermediatePROSITE-ProRule annotation7 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Isomerase, Topoisomerase
Biological processBiological rhythms, Host-virus interaction

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		5.99.1.2 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-4615885 SUMOylation of DNA replication proteins

SIGNOR Signaling Network Open Resource

More...SIGNORi		P11387

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA topoisomerase 1 (EC:5.6.2.1PROSITE-ProRule annotation3 Publications)
Alternative name(s):
DNA topoisomerase I
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TOP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:11986 TOP1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		126420 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P11387

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...DisGeNETi		7150

Open Targets

More...OpenTargetsi		ENSG00000198900

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA353

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P11387 Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1781

Drug and drug target database

More...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
DB14962 Trastuzumab deruxtecan
DB06069 XMT-1001

DrugCentral

More...DrugCentrali		P11387

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TOP1

Domain mapping of disease mutations (DMDM)

More...DMDMi		12644118

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001452012 – 765DNA topoisomerase 1Add BLAST764

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1 Publication1
Modified residuei2PhosphoserineCombined sources1
Modified residuei10PhosphoserineCombined sources1
Modified residuei57PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki101Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateCurated
Cross-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
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-acetyllysine; alternateBy similarity1
Cross-linki172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei280N6-acetyllysineCombined sources1
Cross-linki336Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei506Phosphoserine; by CK21 Publication1
Cross-linki549Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki642Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki700Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki712Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		P11387

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P11387

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P11387

MaxQB - The MaxQuant DataBase

More...MaxQBi		P11387

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P11387

PeptideAtlas

More...PeptideAtlasi		P11387

PRoteomics IDEntifications database

More...PRIDEi		P11387

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		52766

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P11387

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P11387

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P11387

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P11387

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P11387

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Endothelial cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000198900 Expressed in trabecular bone tissue and 231 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P11387 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000198900 Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

Interacts with ERCC6 (PubMed:26030138).

8 Publications

(Microbial infection) Interacts with SV40 Large T antigen; this interactions allows viral DNA replication.

1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113003, 217 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P11387

Database of interacting proteins

More...DIPi		DIP-36356N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P11387

Protein interaction database and analysis system

More...IntActi		P11387, 100 interactors

Molecular INTeraction database

More...MINTi		P11387

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000354522

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P11387

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P11387 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1765
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P11387

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P11387

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni425 – 426Interaction with DNA2
Regioni488 – 493Interaction with DNA6
Regioni585 – 587Interaction with DNA3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi23 – 204Lys-richAdd BLAST182

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the type IB topoisomerase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0981 Eukaryota
COG3569 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155006

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_009193_0_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P11387

KEGG Orthology (KO)

More...KOi		K03163

Identification of Orthologs from Complete Genome Data

More...OMAi		CSLKYEH

Database of Orthologous Groups

More...OrthoDBi		303947at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P11387

TreeFam database of animal gene trees

More...TreeFami		TF105281

Family and domain databases

Conserved Domains Database

More...CDDi		cd00659 Topo_IB_C, 1 hit

Database of protein disorder

More...DisProti		DP00075

Gene3D Structural and Functional Annotation of Protein Families

More...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

Integrated resource of protein families, domains and functional sites

More...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

Pfam protein domain database

More...Pfami		View protein in Pfam
PF14370 Topo_C_assoc, 1 hit
PF01028 Topoisom_I, 1 hit
PF02919 Topoisom_I_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00416 EUTPISMRASEI

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00435 TOPEUc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56349 SSF56349, 1 hit
SSF56741 SSF56741, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00176 TOPOISOMERASE_I_EUK, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6FBED540BCF7BE28
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti145A → V in AAA61207 (PubMed:2833744).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_052592214G → S. Corresponds to variant dbSNP:rs6029542Ensembl.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 dbSNP:rs267607131EnsemblClinVar.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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS13312.1

Protein sequence database of the Protein Information Resource

More...PIRi		A30887 ISHUT1

NCBI Reference Sequences

More...RefSeqi		NP_003277.1, NM_003286.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000361337; ENSP00000354522; ENSG00000198900

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7150

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7150

UCSC genome browser

More...UCSCi		uc002xjl.4 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
CCDSiCCDS13312.1
PIRiA30887 ISHUT1
RefSeqiNP_003277.1, NM_003286.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
SMRiP11387
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi113003, 217 interactors
CORUMiP11387
DIPiDIP-36356N
ELMiP11387
IntActiP11387, 100 interactors
MINTiP11387
STRINGi9606.ENSP00000354522

Chemistry databases

BindingDBiP11387
ChEMBLiCHEMBL1781
DrugBankiDB07354 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
DB14962 Trastuzumab deruxtecan
DB06069 XMT-1001
DrugCentraliP11387

PTM databases

iPTMnetiP11387
MetOSiteiP11387
PhosphoSitePlusiP11387
SwissPalmiP11387

Polymorphism and mutation databases

BioMutaiTOP1
DMDMi12644118

2D gel databases

SWISS-2DPAGEiP11387

Proteomic databases

EPDiP11387
jPOSTiP11387
MassIVEiP11387
MaxQBiP11387
PaxDbiP11387
PeptideAtlasiP11387
PRIDEiP11387
ProteomicsDBi52766

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3962 402 antibodies

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7150
DisGeNETi7150

GeneCards: human genes, protein and diseases

More...GeneCardsi		TOP1
HGNCiHGNC:11986 TOP1
HPAiENSG00000198900 Low tissue specificity
MIMi126420 gene
neXtProtiNX_P11387
OpenTargetsiENSG00000198900
PharmGKBiPA353

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0981 Eukaryota
COG3569 LUCA
GeneTreeiENSGT00940000155006
HOGENOMiCLU_009193_0_1_1
InParanoidiP11387
KOiK03163
OMAiCSLKYEH
OrthoDBi303947at2759
PhylomeDBiP11387
TreeFamiTF105281

Enzyme and pathway databases

BRENDAi5.99.1.2 2681
ReactomeiR-HSA-4615885 SUMOylation of DNA replication proteins
SIGNORiP11387

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		TOP1 human
EvolutionaryTraceiP11387

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		TOP1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		7150
PharosiP11387 Tclin

Protein Ontology

More...PROi		PR:P11387
RNActiP11387 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000198900 Expressed in trabecular bone tissue and 231 other tissues
GenevisibleiP11387 HS

Family and domain databases

CDDicd00659 Topo_IB_C, 1 hit
DisProtiDP00075
Gene3Di1.10.10.41, 1 hit
1.10.132.10, 1 hit
2.170.11.10, 1 hit
3.90.15.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF14370 Topo_C_assoc, 1 hit
PF01028 Topoisom_I, 1 hit
PF02919 Topoisom_I_N, 1 hit
PRINTSiPR00416 EUTPISMRASEI
SMARTiView protein in SMART
SM00435 TOPEUc, 1 hit
SUPFAMiSSF56349 SSF56349, 1 hit
SSF56741 SSF56741, 1 hit
PROSITEiView protein in PROSITE
PS00176 TOPOISOMERASE_I_EUK, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTOP1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P11387
Secondary accession number(s): A8KA78
, E1P5W3, O43256, Q12855, Q12856, Q15610, Q5TFY3, Q9UJN0
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: December 1, 2000
Last modified: April 22, 2020
This is version 226 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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