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Entry version 192 (16 Oct 2019)
Sequence version 2 (14 Dec 2011)
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Protein

DNA topoisomerase 2-alpha

Gene

Top2a

Organism
Mus musculus (Mouse)
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 (PubMed:24321095).2 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

  • ATP-dependent breakage, passage and rejoining of double-stranded DNA.PROSITE-ProRule annotation1 Publication EC:5.6.2.2

<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+PROSITE-ProRule annotation, Mn2+PROSITE-ProRule annotation, Ca2+PROSITE-ProRule annotationNote: 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+.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei90ATPBy similarity1
Binding sitei119ATPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi460Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi540Magnesium 1; catalyticPROSITE-ProRule annotation1
Metal bindingi540Magnesium 2PROSITE-ProRule annotation1
Metal bindingi542Magnesium 2PROSITE-ProRule annotation1
<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>Sitei803Transition state stabilizerBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei804O-(5'-phospho-DNA)-tyrosine intermediateBy similarity1
Sitei855Important for DNA bending; intercalates between base pairs of target DNABy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi147 – 149ATPBy similarity3
Nucleotide bindingi160 – 167ATPBy similarity8
Nucleotide bindingi375 – 377ATPBy similarity3

<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

Reactome - a knowledgebase of biological pathways and processes

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

<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:5.6.2.2PROSITE-ProRule annotation1 Publication)
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:Top-2, 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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:98790 Top2a

<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

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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3586

<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_00001453641 – 1528DNA topoisomerase 2-alphaAdd BLAST1528

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-acetylmethionineBy similarity1
Modified residuei4PhosphoserineBy similarity1
<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)By similarity
Cross-linki155Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki156Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei281PhosphothreonineBy similarity1
Cross-linki351Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki385Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki396Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki415Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki417Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki424Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki439Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki479Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki528Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki583Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki598Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki613Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki621Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki624Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki631Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki638Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki654Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki661Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki675Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1074Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1105Phosphoserine; by CK1By similarity1
Cross-linki1193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1201Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1211PhosphoserineCombined sources1
Cross-linki1226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1238Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1238Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei1245PhosphothreonineCombined sources1
Cross-linki1272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1282Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1291PhosphoserineBy similarity1
Modified residuei1293PhosphoserineBy similarity1
Modified residuei1295PhosphoserineBy similarity1
Modified residuei1298PhosphoserineBy similarity1
Modified residuei1323PhosphothreonineCombined sources1
Modified residuei1328PhosphoserineCombined sources1
Modified residuei1333PhosphoserineCombined sources1
Modified residuei1350PhosphothreonineCombined sources1
Cross-linki1359Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1363Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1370PhosphoserineBy similarity1
Modified residuei1373PhosphoserineCombined sources1
Cross-linki1382Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1384PhosphoserineBy similarity1
Modified residuei1388PhosphoserineCombined sources1
Modified residuei1418N6-acetyllysine; alternateCombined sources1
Cross-linki1418Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei1438N6-acetyllysine; alternateCombined sources1
Cross-linki1438Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki1450Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1455Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1465PhosphoserineBy similarity1
Modified residuei1467PhosphoserineBy similarity1
Modified residuei1470PhosphoserineBy similarity1
Modified residuei1472PhosphoserineBy similarity1
Cross-linki1480Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1488Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1521PhosphoserineCombined 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 (By similarity). However, phosphorylation at Ser-1105 by CSNK1D/CK1 promotes DNA cleavable complex formation (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q01320

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q01320

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q01320

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

More...
PaxDbi
Q01320

PeptideAtlas

More...
PeptideAtlasi
Q01320

PRoteomics IDEntifications database

More...
PRIDEi
Q01320

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01320

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

More...
PhosphoSitePlusi
Q01320

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q01320

<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
ENSMUSG00000020914 Expressed in 258 organ(s), highest expression level in ganglionic eminence

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q01320 MM

<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 (By similarity).

Interacts with COPS5 (By similarity).

Interacts with RECQL5; this stimulates DNA decatenation (By similarity).

Interacts with SETMAR; stimulates the topoisomerase activity (By similarity).

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 (By similarity).

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).

Interacts with MCM3AP (By similarity).

Interacts with ERCC6 (By similarity).

By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei488Interaction with DNAPROSITE-ProRule annotation1
Sitei491Interaction with DNAPROSITE-ProRule annotation1
Sitei660Interaction with DNAPROSITE-ProRule annotation1
Sitei661Interaction with DNAPROSITE-ProRule annotation1
Sitei722Interaction with DNAPROSITE-ProRule annotation1
Sitei756Interaction with DNAPROSITE-ProRule annotation1
Sitei762Interaction with DNAPROSITE-ProRule annotation1
Sitei930Interaction with DNAPROSITE-ProRule annotation1

<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

WithEntry#Exp.IntActNotes
Smarca4Q3TKT43EBI-642809,EBI-1210244

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
204276, 14 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q01320

Database of interacting proteins

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DIPi
DIP-40621N

Protein interaction database and analysis system

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IntActi
Q01320, 23 interactors

Molecular INTeraction database

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MINTi
Q01320

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000068896

<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

3D structure databases

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

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SMRi
Q01320

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Domaini454 – 571ToprimPROSITE-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>Regioni341 – 343Interaction with DNABy similarity3
Regioni989 – 998Interaction with DNABy similarity10

<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 HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000216693

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q01320

KEGG Orthology (KO)

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KOi
K03164

Identification of Orthologs from Complete Genome Data

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OMAi
VNENMQI

Database of Orthologous Groups

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OrthoDBi
117851at2759

TreeFam database of animal gene trees

More...
TreeFami
TF105282

Family and domain databases

Conserved Domains Database

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CDDi
cd00187 TOP4c, 1 hit
cd03365 TOPRIM_TopoIIA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.268.10, 1 hit
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

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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
IPR013757 Topo_IIA_A_a_sf
IPR013759 Topo_IIA_B_C
IPR013506 Topo_IIA_bsu_dom2
IPR018522 TopoIIA_CS
IPR031660 TOPRIM_C
IPR006171 TOPRIM_domain
IPR034157 TOPRIM_TopoII

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

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

Superfamily database of structural and functional annotation

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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>. 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_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.

Q01320-1 [UniParc]FASTAAdd to basket
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MELSPLQPVN ENMLMNKKKN EDGKKRLSIE RIYQKKTQLE HILLRPDTYI
60 70 80 90 100
GSVELVTQQM WVYDEDVGIN YREVTFVPGL YKIFDEILVN AADNKQRDPK
110 120 130 140 150
MSCIRVTIDP ENNVISIWNN GKGIPVVEHK VEKIYVPALI FGQLLTSSNY
160 170 180 190 200
DDDEKKVTGG RNGYGAKLCN IFSTKFTVET ASREYKKMFK QTWMDNMGRA
210 220 230 240 250
GDMELKPFSG EDYTCITFQP DLSKFKMQSL DKDIVALMVR RAYDIAGSTK
260 270 280 290 300
DVKVFLNGNS LPVKGFRSYV DLYLKDKVDE TGNSLKVIHE QVNPRWEVCL
310 320 330 340 350
TMSERGFQQI SFVNSIATSK GGRHVDYVAD QIVSKLVDVV KKKNKGGVAV
360 370 380 390 400
KAHQVKNHMW IFVNALIENP TFDSQTKENM TLQAKSFGST CQLSEKFIKA
410 420 430 440 450
AIGCGIVESI LNWVKFKAQI QLNKKCSAVK HTKIKGIPKL DDANDAGSRN
460 470 480 490 500
STECTLILTE GDSAKTLAVS GLGVVGRDKY GVFPLRGKIL NVREASHKQI
510 520 530 540 550
MENAEINNII KIVGLQYKKN YEDEDSLKTL RYGKIMIMTD QDQDGSHIKG
560 570 580 590 600
LLINFIHHNW PSLLRHRFLE EFITPIVKVS KNKQEIAFYS LPEFEEWKSS
610 620 630 640 650
TPNHKKWKVK YYKGLGTSTS KEAKEYFADM KRHRIQFKYS GPEDDAAISL
660 670 680 690 700
AFSKKQVDDR KEWLTNFMED RRQRKLLGLP EDYLYGQSTS YLTYNDFINK
710 720 730 740 750
ELILFSNSDN ERSIPSMVDG LKPGQRKVLF TCFKRNDKRE VKVAQLAGSV
760 770 780 790 800
AEMSSYHHGE MSLMMTIINL AQNFVGSNNL NLLQPIGQFG TRLHGGKDSA
810 820 830 840 850
SPRYIFTMLS PLARLLFPPK DDHTLRFLYD DNQRVEPEWY IPIIPMVLIN
860 870 880 890 900
GAEGIGTGWS CKIPNFDVRE VVNNIRRLLD GEEPLPMLPS YKNFKGTIEE
910 920 930 940 950
LASNQYVING EVAILDSTTI EISELPIRTW TQTYKEQVLE PMLNGTEKTP
960 970 980 990 1000
SLITDYREYH TDTTVKFVIK MTEEKLAEAE RVGLHKVFKL QSSLTCNSMV
1010 1020 1030 1040 1050
LFDHVGCLKK YDTVLDILRD FFELRLKYYG LRKEWLLGML GAESSKLNNQ
1060 1070 1080 1090 1100
ARFILEKIDG KIVIENKPKK ELIKVLIQRG YDSDPVKAWK EAQQKVPDEE
1110 1120 1130 1140 1150
ENEESDTETS TSDSAAEAGP TFNYLLDMPL WYLTKEKKDE LCKQRNEKEQ
1160 1170 1180 1190 1200
ELNTLKQKSP SDLWKEDLAV FIEELEVVEA KEKQDEQVGL PGKAGKAKGK
1210 1220 1230 1240 1250
KAQMCADVLP SPRGKRVIPQ VTVEMKAEAE KKIRKKIKSE NVEGTPAEDG
1260 1270 1280 1290 1300
AEPGSLRQRI EKKQKKEPGA KKQTTLPFKP VKKGRKKNPW SDSESDVSSN
1310 1320 1330 1340 1350
ESNVDVPPRQ KEQRSAAAKA KFTVDLDSDE DFSGLDEKDE DEDFLPLDAT
1360 1370 1380 1390 1400
PPKAKIPPKN TKKALKTQGS SMSVVDLESD VKDSVPASPG VPAADFPAET
1410 1420 1430 1440 1450
EQSKPSKKTV GVKKTATKSQ SSVSTAGTKK RAAPKGTKSD SALSARVSEK
1460 1470 1480 1490 1500
PAPAKAKNSR KRKPSSSDSS DSDFERAISK GATSKKAKGE EQDFPVDLED
1510 1520
TIAPRAKSDR ARKPIKYLEE SDDDDDLF
Length:1,528
Mass (Da):172,790
Last modified:December 14, 2011 - 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:i63CBF8F649D103C7
GO

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 conflicti184E → A in BAA02076 (PubMed:1331984).Curated1
Sequence conflicti260S → M in BAA02076 (PubMed:1331984).Curated1
Sequence conflicti640S → P in BAA02076 (PubMed:1331984).Curated1
Sequence conflicti841I → N in BAA02076 (PubMed:1331984).Curated1
Sequence conflicti844 – 845IP → NT in BAA02076 (PubMed:1331984).Curated2
Sequence conflicti1316A → R in BAA02076 (PubMed:1331984).Curated1
Sequence conflicti1316A → R in AAC52135 (PubMed:8261398).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
D12513 mRNA Translation: BAA02076.1
AL591067 Genomic DNA No translation available.
U01915 mRNA Translation: AAC52135.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS25370.1

Protein sequence database of the Protein Information Resource

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PIRi
JS0703

NCBI Reference Sequences

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RefSeqi
NP_035753.2, NM_011623.2
XP_006533216.1, XM_006533153.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000068031; ENSMUSP00000068896; ENSMUSG00000020914

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
21973

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:21973

UCSC genome browser

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UCSCi
uc007lid.1 mouse

<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
D12513 mRNA Translation: BAA02076.1
AL591067 Genomic DNA No translation available.
U01915 mRNA Translation: AAC52135.1
CCDSiCCDS25370.1
PIRiJS0703
RefSeqiNP_035753.2, NM_011623.2
XP_006533216.1, XM_006533153.2

3D structure databases

SMRiQ01320
ModBaseiSearch...

Protein-protein interaction databases

BioGridi204276, 14 interactors
CORUMiQ01320
DIPiDIP-40621N
IntActiQ01320, 23 interactors
MINTiQ01320
STRINGi10090.ENSMUSP00000068896

Chemistry databases

ChEMBLiCHEMBL3586

PTM databases

iPTMnetiQ01320
PhosphoSitePlusiQ01320
SwissPalmiQ01320

Proteomic databases

EPDiQ01320
jPOSTiQ01320
MaxQBiQ01320
PaxDbiQ01320
PeptideAtlasiQ01320
PRIDEiQ01320

Genome annotation databases

EnsembliENSMUST00000068031; ENSMUSP00000068896; ENSMUSG00000020914
GeneIDi21973
KEGGimmu:21973
UCSCiuc007lid.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7153
MGIiMGI:98790 Top2a

Phylogenomic databases

eggNOGiKOG0355 Eukaryota
COG0187 LUCA
COG0188 LUCA
GeneTreeiENSGT00940000157539
HOGENOMiHOG000216693
InParanoidiQ01320
KOiK03164
OMAiVNENMQI
OrthoDBi117851at2759
TreeFamiTF105282

Enzyme and pathway databases

ReactomeiR-MMU-4615885 SUMOylation of DNA replication proteins

Miscellaneous databases

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

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ChiTaRSi
Top2a mouse

Protein Ontology

More...
PROi
PR:Q01320

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000020914 Expressed in 258 organ(s), highest expression level in ganglionic eminence
GenevisibleiQ01320 MM

Family and domain databases

CDDicd00187 TOP4c, 1 hit
cd03365 TOPRIM_TopoIIA, 1 hit
Gene3Di1.10.268.10, 1 hit
3.30.230.10, 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
IPR013757 Topo_IIA_A_a_sf
IPR013759 Topo_IIA_B_C
IPR013506 Topo_IIA_bsu_dom2
IPR018522 TopoIIA_CS
IPR031660 TOPRIM_C
IPR006171 TOPRIM_domain
IPR034157 TOPRIM_TopoII
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

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 nameiTOP2A_MOUSE
<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: Q01320
Secondary accession number(s): E9PX08
<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: April 1, 1993
Last sequence update: December 14, 2011
Last modified: October 16, 2019
This is version 192 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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