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Entry version 231 (13 Feb 2019)
Sequence version 3 (04 May 2001)
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Protein

DNA topoisomerase 2-alpha

Gene

TOP2A

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

Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (By similarity).By similarity3 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_section">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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+4 Publications, Mn2+4 Publications, Ca2+4 PublicationsNote: Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ or Ca2+.4 Publications

<p>This subsection of the ‘Function’ 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 the intercalating agent amsacrine.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei91ATP2 Publications1
Binding sitei120ATP2 Publications1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi461Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi541Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi541Magnesium 21 Publication1
Metal bindingi543Magnesium 21 Publication1
<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>Sitei804Transition state stabilizerBy similarity1
<p>This subsection of the ‘Function’ 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 sitei805O-(5'-phospho-DNA)-tyrosine intermediateBy similarity1
Sitei856Important for DNA bending; intercalates between base pairs of target DNABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi148 – 150ATP2 Publications3
Nucleotide bindingi161 – 168ATP2 Publications8
Nucleotide bindingi376 – 378ATP1 Publication1 Publication3

<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

GO - Biological processi

<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
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.99.1.3 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex
R-HSA-4615885 SUMOylation of DNA replication proteins

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P11388

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P11388

<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_and_taxonomy_section">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 2-alpha (EC:5.99.1.3)
Alternative name(s):
DNA topoisomerase II, alpha isozyme
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:TOP2A
Synonyms:TOP2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000131747.14

Human Gene Nomenclature Database

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HGNCi
HGNC:11989 TOP2A

Online Mendelian Inheritance in Man (OMIM)

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MIMi
126430 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P11388

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi342 – 344KKK → AAA: Reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. 1 Publication3
Mutagenesisi342 – 344KKK → EEE: Strongly reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. 1 Publication3
Mutagenesisi461E → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. 2 Publications1
Mutagenesisi541D → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. 2 Publications1
Mutagenesisi543D → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. 2 Publications1
Mutagenesisi545D → A or C: Strongly reduced DNA cleavage. 1 Publication1
Mutagenesisi1469S → A: Abolishes binding to the antibody MPM2. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
7153

MalaCards human disease database

More...
MalaCardsi
TOP2A

Open Targets

More...
OpenTargetsi
ENSG00000131747

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
635 Neuroblastoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA354

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1806

Drug and drug target database

More...
DrugBanki
DB05022 Amonafide
DB06263 Amrubicin
DB00276 Amsacrine
DB04975 Banoxantrone
DB00537 Ciprofloxacin
DB00970 Dactinomycin
DB00694 Daunorubicin
DB00380 Dexrazoxane
DB00997 Doxorubicin
DB05129 Elsamitrucin
DB00467 Enoxacin
DB00445 Epirubicin
DB00773 Etoposide
DB09047 Finafloxacin
DB04576 Fleroxacin
DB01645 Genistein
DB01177 Idarubicin
DB01137 Levofloxacin
DB00978 Lomefloxacin
DB04967 Lucanthone
DB01204 Mitoxantrone
DB00218 Moxifloxacin
DB01059 Norfloxacin
DB01165 Ofloxacin
DB00487 Pefloxacin
DB01179 Podofilox
DB05920 RTA 744
DB04978 SP1049C
DB01208 Sparfloxacin
DB00444 Teniposide
DB00685 Trovafloxacin
DB00385 Valrubicin
DB06042 ZEN-012

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2637

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
TOP2A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
13959709

<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 ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001453631 – 1531DNA topoisomerase 2-alphaAdd BLAST1531

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 residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei4PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-linki17Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki156Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki157Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki261Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei282PhosphothreonineCombined sources1
Cross-linki352Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki386Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki397Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki416Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki418Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki425Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki440Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki466Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki480Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki584Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki599Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki614Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki622Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki625Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki632Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki639Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki655Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki662Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki676Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1075Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1106Phosphoserine; by CK1Combined sources2 Publications1
Cross-linki1114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1205PhosphothreonineCombined sources1
Modified residuei1213PhosphoserineCombined sources1
Cross-linki1228Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki1240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei1244PhosphothreonineCombined sources1
Modified residuei1247PhosphoserineCombined sources1
Cross-linki1259Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1283Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1286Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1295PhosphoserineCombined sources1
Modified residuei1297PhosphoserineCombined sources1
Modified residuei1299PhosphoserineCombined sources1
Modified residuei1302PhosphoserineCombined sources1
Modified residuei1327PhosphothreonineBy similarity1
Modified residuei1332PhosphoserineCombined sources1
Modified residuei1337PhosphoserineCombined sources1
Modified residuei1343Phosphothreonine; by PLK3Combined sources1 Publication1
Modified residuei1351PhosphoserineCombined sources1
Modified residuei1354PhosphoserineCombined sources1
Cross-linki1363Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1367Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1373Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1374PhosphoserineCombined sources1
Modified residuei1377PhosphoserineCombined sources1
Cross-linki1385Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1387PhosphoserineCombined sources1
Modified residuei1391PhosphoserineCombined sources1
Modified residuei1392PhosphoserineCombined sources1
Modified residuei1393PhosphoserineCombined sources1
Modified residuei1422N6-acetyllysine; alternateBy similarity1
Cross-linki1422Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei1442N6-acetyllysine; alternateBy similarity1
Cross-linki1442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei1449PhosphoserineCombined sources1
Cross-linki1454Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1459Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1469Phosphoserine; by CK2Combined sources1 Publication1
Modified residuei1470PhosphothreonineCombined sources1
Modified residuei1471PhosphoserineCombined sources1
Modified residuei1474PhosphoserineCombined sources1
Modified residuei1476PhosphoserineCombined sources1
Cross-linki1484Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki1492Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1495PhosphoserineCombined sources1
Modified residuei1504PhosphoserineCombined sources1
Modified residuei1525PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable complex formation.4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P11388

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P11388

MaxQB - The MaxQuant DataBase

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MaxQBi
P11388

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

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PaxDbi
P11388

PeptideAtlas

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PeptideAtlasi
P11388

PRoteomics IDEntifications database

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PRIDEi
P11388

ProteomicsDB human proteome resource

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ProteomicsDBi
52767
52768 [P11388-2]
52769 [P11388-3]
52770 [P11388-4]

2D gel databases

University College Dublin 2-DE Proteome Database

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UCD-2DPAGEi
P11388

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P11388

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P11388

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

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PhosphoSitePlusi
P11388

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P11388

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000131747 Expressed in 158 organ(s), highest expression level in heart

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P11388 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P11388 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB002448
HPA006458
HPA026773

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Interacts with COPS5. Interacts with RECQL5; this stimulates DNA decatenation. Interacts with SETMAR; stimulates the topoisomerase activity (PubMed:18790802, PubMed:20457750). Interacts with DHX9; this interaction occurs in a E2 enzyme UBE2I- and RNA-dependent manner, negatively regulates DHX9-mediated double-stranded DNA and RNA duplex helicase activity and stimulates TOP2A-mediated supercoiled DNA relaxation activity (PubMed:12711669). Interacts with HNRNPU (via C-terminus); this interaction protects the topoisomerase TOP2A from degradation and positively regulates the relaxation of supercoiled DNA in a RNA-dependent manner (By similarity).By similarity6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei489Interaction with DNAPROSITE-ProRule annotation1
Sitei492Interaction with DNA1 Publication1
Sitei661Interaction with DNA1 Publication1
Sitei662Interaction with DNA1 Publication1
Sitei723Interaction with DNA1 Publication1
Sitei757Interaction with DNA1 Publication1
Sitei763Interaction with DNA1 Publication1
Sitei931Interaction with DNA1 Publication1

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113006, 138 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P11388

Database of interacting proteins

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DIPi
DIP-33887N

Protein interaction database and analysis system

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IntActi
P11388, 59 interactors

Molecular INTeraction database

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MINTi
P11388

STRING: functional protein association networks

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STRINGi
9606.ENSP00000411532

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P11388

<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

11531
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LWZmodel-A431-1200[»]
1ZXMX-ray1.87A/B29-428[»]
1ZXNX-ray2.51A/B/C/D29-428[»]
4FM9X-ray2.90A431-1193[»]
4R1FX-ray2.51A/B/C/D29-428[»]
5GWKX-ray3.15A/B429-1188[»]
5NNEX-ray1.15C1198-1207[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P11388

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

More...
SMRi
P11388

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P11388

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini455 – 572ToprimPROSITE-ProRule annotationAdd BLAST118

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>Regioni342 – 344Interaction with DNA1 Publication3
Regioni990 – 999Interaction with DNA1 Publication10

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1018 – 1028Nuclear export signalAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminus has several structural domains; the ATPase domain (about residues 1-265), the transducer domain (about 266-428) and the toprim domain (455-572) (PubMed:25202966). Comparing different structures shows ATP hydrolysis induces domain shifts in the N-terminus that are probably part of the mechanism of DNA cleavage and rejoining (PubMed:25202966).By similarity1 Publication

<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 II topoisomerase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0355 Eukaryota
COG0187 LUCA
COG0188 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157539

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG052998

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P11388

KEGG Orthology (KO)

More...
KOi
K03164

Identification of Orthologs from Complete Genome Data

More...
OMAi
GESDDFH

Database of Orthologous Groups

More...
OrthoDBi
1406210at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P11388

TreeFam database of animal gene trees

More...
TreeFami
TF105282

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00075 HATPase_c, 1 hit
cd00187 TOP4c, 1 hit
cd03365 TOPRIM_TopoIIA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.10, 1 hit
3.30.565.10, 1 hit
3.40.50.670, 1 hit
3.90.199.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012542 DTHCT
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR001241 Topo_IIA
IPR013760 Topo_IIA-like_dom_sf
IPR002205 Topo_IIA_A/C
IPR013758 Topo_IIA_A/C_ab
IPR013759 Topo_IIA_B_C
IPR013506 Topo_IIA_bsu_dom2
IPR018522 TopoIIA_CS
IPR031660 TOPRIM_C
IPR006171 TOPRIM_domain
IPR034157 TOPRIM_TopoII

The PANTHER Classification System

More...
PANTHERi
PTHR10169 PTHR10169, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00204 DNA_gyraseB, 1 hit
PF00521 DNA_topoisoIV, 1 hit
PF08070 DTHCT, 1 hit
PF02518 HATPase_c, 1 hit
PF01751 Toprim, 1 hit
PF16898 TOPRIM_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00433 TOP2c, 1 hit
SM00434 TOP4c, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
SSF56719 SSF56719, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00177 TOPOISOMERASE_II, 1 hit
PS50880 TOPRIM, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P11388-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEVSPLQPVN ENMQVNKIKK NEDAKKRLSV ERIYQKKTQL EHILLRPDTY
60 70 80 90 100
IGSVELVTQQ MWVYDEDVGI NYREVTFVPG LYKIFDEILV NAADNKQRDP
110 120 130 140 150
KMSCIRVTID PENNLISIWN NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN
160 170 180 190 200
YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE TASREYKKMF KQTWMDNMGR
210 220 230 240 250
AGEMELKPFN GEDYTCITFQ PDLSKFKMQS LDKDIVALMV RRAYDIAGST
260 270 280 290 300
KDVKVFLNGN KLPVKGFRSY VDMYLKDKLD ETGNSLKVIH EQVNHRWEVC
310 320 330 340 350
LTMSEKGFQQ ISFVNSIATS KGGRHVDYVA DQIVTKLVDV VKKKNKGGVA
360 370 380 390 400
VKAHQVKNHM WIFVNALIEN PTFDSQTKEN MTLQPKSFGS TCQLSEKFIK
410 420 430 440 450
AAIGCGIVES ILNWVKFKAQ VQLNKKCSAV KHNRIKGIPK LDDANDAGGR
460 470 480 490 500
NSTECTLILT EGDSAKTLAV SGLGVVGRDK YGVFPLRGKI LNVREASHKQ
510 520 530 540 550
IMENAEINNI IKIVGLQYKK NYEDEDSLKT LRYGKIMIMT DQDQDGSHIK
560 570 580 590 600
GLLINFIHHN WPSLLRHRFL EEFITPIVKV SKNKQEMAFY SLPEFEEWKS
610 620 630 640 650
STPNHKKWKV KYYKGLGTST SKEAKEYFAD MKRHRIQFKY SGPEDDAAIS
660 670 680 690 700
LAFSKKQIDD RKEWLTNFME DRRQRKLLGL PEDYLYGQTT TYLTYNDFIN
710 720 730 740 750
KELILFSNSD NERSIPSMVD GLKPGQRKVL FTCFKRNDKR EVKVAQLAGS
760 770 780 790 800
VAEMSSYHHG EMSLMMTIIN LAQNFVGSNN LNLLQPIGQF GTRLHGGKDS
810 820 830 840 850
ASPRYIFTML SSLARLLFPP KDDHTLKFLY DDNQRVEPEW YIPIIPMVLI
860 870 880 890 900
NGAEGIGTGW SCKIPNFDVR EIVNNIRRLM DGEEPLPMLP SYKNFKGTIE
910 920 930 940 950
ELAPNQYVIS GEVAILNSTT IEISELPVRT WTQTYKEQVL EPMLNGTEKT
960 970 980 990 1000
PPLITDYREY HTDTTVKFVV KMTEEKLAEA ERVGLHKVFK LQTSLTCNSM
1010 1020 1030 1040 1050
VLFDHVGCLK KYDTVLDILR DFFELRLKYY GLRKEWLLGM LGAESAKLNN
1060 1070 1080 1090 1100
QARFILEKID GKIIIENKPK KELIKVLIQR GYDSDPVKAW KEAQQKVPDE
1110 1120 1130 1140 1150
EENEESDNEK ETEKSDSVTD SGPTFNYLLD MPLWYLTKEK KDELCRLRNE
1160 1170 1180 1190 1200
KEQELDTLKR KSPSDLWKED LATFIEELEA VEAKEKQDEQ VGLPGKGGKA
1210 1220 1230 1240 1250
KGKKTQMAEV LPSPRGQRVI PRITIEMKAE AEKKNKKKIK NENTEGSPQE
1260 1270 1280 1290 1300
DGVELEGLKQ RLEKKQKREP GTKTKKQTTL AFKPIKKGKK RNPWSDSESD
1310 1320 1330 1340 1350
RSSDESNFDV PPRETEPRRA ATKTKFTMDL DSDEDFSDFD EKTDDEDFVP
1360 1370 1380 1390 1400
SDASPPKTKT SPKLSNKELK PQKSVVSDLE ADDVKGSVPL SSSPPATHFP
1410 1420 1430 1440 1450
DETEITNPVP KKNVTVKKTA AKSQSSTSTT GAKKRAAPKG TKRDPALNSG
1460 1470 1480 1490 1500
VSQKPDPAKT KNRRKRKPST SDDSDSNFEK IVSKAVTSKK SKGESDDFHM
1510 1520 1530
DFDSAVAPRA KSVRAKKPIK YLEESDEDDL F
Length:1,531
Mass (Da):174,385
Last modified:May 4, 2001 - v3
<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:i3DF40BC9E84789DC
GO
Isoform 2 (identifier: P11388-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     401-401: A → AHLYSRFLIDPFFPNMIPNMIFSFSKA

Show »
Length:1,557
Mass (Da):177,501
Checksum:i4DE312DFAEC443EA
GO
Isoform 3 (identifier: P11388-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: K → KSSKYWSSRKSKQHILLNFFVLFKFINDAFFGICPFK

Show »
Length:1,567
Mass (Da):178,712
Checksum:iE5322E9ED4DD7BF5
GO
Isoform 4 (identifier: P11388-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     355-355: Q → QRELCNGAIL...SQSSGITDVK

Show »
Length:1,612
Mass (Da):182,681
Checksum:iAB857EA93238BD4A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3KTB7J3KTB7_HUMAN
DNA topoisomerase 2-alpha
TOP2A
147Annotation score:

Annotation score:1 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>
J3QR57J3QR57_HUMAN
DNA topoisomerase 2-alpha
TOP2A
27Annotation score:

Annotation score:1 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 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 conflicti152D → H in CAA09762 (PubMed:10095062).Curated1
Sequence conflicti180E → Q in CAA09762 (PubMed:10095062).Curated1
Sequence conflicti327D → H in CAA09762 (PubMed:10095062).Curated1
Sequence conflicti1022F → L in CAA09762 (PubMed:10095062).Curated1
Sequence conflicti1274T → S in CAA09762 (PubMed:10095062).Curated1
Sequence conflicti1295S → P in AAA61209 (PubMed:2845399).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_007532450R → Q in teniposide (VM-26) resistant cells. 1 PublicationCorresponds to variant dbSNP:rs746765101Ensembl.1
Natural variantiVAR_007533487R → K in amsacrine resistant cells. 1 PublicationCorresponds to variant dbSNP:rs267607133EnsemblClinVar.1
Natural variantiVAR_0292451324T → K. Corresponds to variant dbSNP:rs28969502Ensembl.1
Natural variantiVAR_0525941386G → D. Corresponds to variant dbSNP:rs34300454Ensembl.1
Natural variantiVAR_0525951515A → S. Corresponds to variant dbSNP:rs11540720Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006529321K → KSSKYWSSRKSKQHILLNFF VLFKFINDAFFGICPFK in isoform 3. 1 Publication1
Alternative sequenceiVSP_006530355Q → QRELCNGAILAHCNLRLMGS SDSPASASRVAGIAGGCHHT QLIFVFLVETGFHHVGQAGL ERLTSGDPPASASQSSGITD VK in isoform 4. 1 Publication1
Alternative sequenceiVSP_006531401A → AHLYSRFLIDPFFPNMIPNM IFSFSKA in isoform 2. 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
J04088 mRNA Translation: AAA61209.1
AF071747
, AF071738, AF071739, AF071740, AF071741, AF071742, AF071743, AF071744, AF071745, AF071746 Genomic DNA Translation: AAC77388.1
AJ011741
, AJ011742, AJ011743, AJ011744, AJ011745, AJ011746, AJ011747, AJ011748, AJ011749, AJ011750, AJ011751, AJ011752, AJ011753, AJ011754, AJ011755, AJ011756, AJ011757, AJ011758 Genomic DNA Translation: CAA09762.1
AC080112 Genomic DNA No translation available.
AF285157 mRNA Translation: AAG13403.1
AF285158 mRNA Translation: AAG13404.1
CH471152 Genomic DNA Translation: EAW60663.1
BC140791 mRNA Translation: AAI40792.1
AF285159 mRNA Translation: AAG13405.1
AF069522 Genomic DNA Translation: AAC23518.1
AF064590 Genomic DNA Translation: AAC16736.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS45672.1 [P11388-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A40493

NCBI Reference Sequences

More...
RefSeqi
NP_001058.2, NM_001067.3 [P11388-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.156346

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000423485; ENSP00000411532; ENSG00000131747 [P11388-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7153

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7153

UCSC genome browser

More...
UCSCi
uc002huq.4 human [P11388-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04088 mRNA Translation: AAA61209.1
AF071747
, AF071738, AF071739, AF071740, AF071741, AF071742, AF071743, AF071744, AF071745, AF071746 Genomic DNA Translation: AAC77388.1
AJ011741
, AJ011742, AJ011743, AJ011744, AJ011745, AJ011746, AJ011747, AJ011748, AJ011749, AJ011750, AJ011751, AJ011752, AJ011753, AJ011754, AJ011755, AJ011756, AJ011757, AJ011758 Genomic DNA Translation: CAA09762.1
AC080112 Genomic DNA No translation available.
AF285157 mRNA Translation: AAG13403.1
AF285158 mRNA Translation: AAG13404.1
CH471152 Genomic DNA Translation: EAW60663.1
BC140791 mRNA Translation: AAI40792.1
AF285159 mRNA Translation: AAG13405.1
AF069522 Genomic DNA Translation: AAC23518.1
AF064590 Genomic DNA Translation: AAC16736.1
CCDSiCCDS45672.1 [P11388-1]
PIRiA40493
RefSeqiNP_001058.2, NM_001067.3 [P11388-1]
UniGeneiHs.156346

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LWZmodel-A431-1200[»]
1ZXMX-ray1.87A/B29-428[»]
1ZXNX-ray2.51A/B/C/D29-428[»]
4FM9X-ray2.90A431-1193[»]
4R1FX-ray2.51A/B/C/D29-428[»]
5GWKX-ray3.15A/B429-1188[»]
5NNEX-ray1.15C1198-1207[»]
ProteinModelPortaliP11388
SMRiP11388
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113006, 138 interactors
CORUMiP11388
DIPiDIP-33887N
IntActiP11388, 59 interactors
MINTiP11388
STRINGi9606.ENSP00000411532

Chemistry databases

BindingDBiP11388
ChEMBLiCHEMBL1806
DrugBankiDB05022 Amonafide
DB06263 Amrubicin
DB00276 Amsacrine
DB04975 Banoxantrone
DB00537 Ciprofloxacin
DB00970 Dactinomycin
DB00694 Daunorubicin
DB00380 Dexrazoxane
DB00997 Doxorubicin
DB05129 Elsamitrucin
DB00467 Enoxacin
DB00445 Epirubicin
DB00773 Etoposide
DB09047 Finafloxacin
DB04576 Fleroxacin
DB01645 Genistein
DB01177 Idarubicin
DB01137 Levofloxacin
DB00978 Lomefloxacin
DB04967 Lucanthone
DB01204 Mitoxantrone
DB00218 Moxifloxacin
DB01059 Norfloxacin
DB01165 Ofloxacin
DB00487 Pefloxacin
DB01179 Podofilox
DB05920 RTA 744
DB04978 SP1049C
DB01208 Sparfloxacin
DB00444 Teniposide
DB00685 Trovafloxacin
DB00385 Valrubicin
DB06042 ZEN-012
GuidetoPHARMACOLOGYi2637

PTM databases

CarbonylDBiP11388
iPTMnetiP11388
PhosphoSitePlusiP11388
SwissPalmiP11388

Polymorphism and mutation databases

BioMutaiTOP2A
DMDMi13959709

2D gel databases

UCD-2DPAGEiP11388

Proteomic databases

EPDiP11388
jPOSTiP11388
MaxQBiP11388
PaxDbiP11388
PeptideAtlasiP11388
PRIDEiP11388
ProteomicsDBi52767
52768 [P11388-2]
52769 [P11388-3]
52770 [P11388-4]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000423485; ENSP00000411532; ENSG00000131747 [P11388-1]
GeneIDi7153
KEGGihsa:7153
UCSCiuc002huq.4 human [P11388-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7153
DisGeNETi7153
EuPathDBiHostDB:ENSG00000131747.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TOP2A

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0013797
HGNCiHGNC:11989 TOP2A
HPAiCAB002448
HPA006458
HPA026773
MalaCardsiTOP2A
MIMi126430 gene
neXtProtiNX_P11388
OpenTargetsiENSG00000131747
Orphaneti635 Neuroblastoma
PharmGKBiPA354

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0355 Eukaryota
COG0187 LUCA
COG0188 LUCA
GeneTreeiENSGT00940000157539
HOVERGENiHBG052998
InParanoidiP11388
KOiK03164
OMAiGESDDFH
OrthoDBi1406210at2759
PhylomeDBiP11388
TreeFamiTF105282

Enzyme and pathway databases

BRENDAi5.99.1.3 2681
ReactomeiR-HSA-1362277 Transcription of E2F targets under negative control by DREAM complex
R-HSA-4615885 SUMOylation of DNA replication proteins
SignaLinkiP11388
SIGNORiP11388

Miscellaneous databases

EvolutionaryTraceiP11388

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TOP2A

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

More...
GenomeRNAii
7153

Protein Ontology

More...
PROi
PR:P11388

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000131747 Expressed in 158 organ(s), highest expression level in heart
ExpressionAtlasiP11388 baseline and differential
GenevisibleiP11388 HS

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
cd00187 TOP4c, 1 hit
cd03365 TOPRIM_TopoIIA, 1 hit
Gene3Di3.30.230.10, 1 hit
3.30.565.10, 1 hit
3.40.50.670, 1 hit
3.90.199.10, 1 hit
InterProiView protein in InterPro
IPR012542 DTHCT
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR020568 Ribosomal_S5_D2-typ_fold
IPR014721 Ribosomal_S5_D2-typ_fold_subgr
IPR001241 Topo_IIA
IPR013760 Topo_IIA-like_dom_sf
IPR002205 Topo_IIA_A/C
IPR013758 Topo_IIA_A/C_ab
IPR013759 Topo_IIA_B_C
IPR013506 Topo_IIA_bsu_dom2
IPR018522 TopoIIA_CS
IPR031660 TOPRIM_C
IPR006171 TOPRIM_domain
IPR034157 TOPRIM_TopoII
PANTHERiPTHR10169 PTHR10169, 1 hit
PfamiView protein in Pfam
PF00204 DNA_gyraseB, 1 hit
PF00521 DNA_topoisoIV, 1 hit
PF08070 DTHCT, 1 hit
PF02518 HATPase_c, 1 hit
PF01751 Toprim, 1 hit
PF16898 TOPRIM_C, 1 hit
SMARTiView protein in SMART
SM00433 TOP2c, 1 hit
SM00434 TOP4c, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
SSF56719 SSF56719, 1 hit
PROSITEiView protein in PROSITE
PS00177 TOPOISOMERASE_II, 1 hit
PS50880 TOPRIM, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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<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 nameiTOP2A_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: P11388
Secondary accession number(s): B2RTS1
, Q71UN1, Q71UQ5, Q9HB24, Q9HB25, Q9HB26, Q9UP44, Q9UQP9
<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_and_isoforms">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: May 4, 2001
Last modified: February 13, 2019
This is version 231 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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