Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P41515 (TOP2A_CRIGR)

Entry version 152 (10 Feb 2021)
Sequence version 1 (01 Nov 1995)
Previous versions | rss
Add a publicationFeedback
Protein

DNA topoisomerase 2-alpha

Gene

TOP2A

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
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 transcript 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

Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand (By similarity). May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (By similarity).By similarity

Miscellaneous

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

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

  • ATP-dependent breakage, passage and rejoining of double-stranded DNA.PROSITE-ProRule annotation 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%5Fsection">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%5Fsection">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%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active 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%5Fsection">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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionDNA-binding, Isomerase, Topoisomerase
Biological processBiological rhythms
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA topoisomerase 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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TOP2A
Synonyms:TOP-2, TOP2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10029 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Cricetidae › Cricetinae › Cricetulus

<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 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001453621 – 1526DNA topoisomerase 2-alphaAdd BLAST1526

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%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-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
Cross-linki260Glycyl 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-linki1191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1208PhosphoserineBy similarity1
Cross-linki1223Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1235Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1235Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei1242PhosphothreonineBy similarity1
Cross-linki1254Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1271Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1281Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1290PhosphoserineBy similarity1
Modified residuei1292PhosphoserineBy similarity1
Modified residuei1294PhosphoserineBy similarity1
Modified residuei1297PhosphoserineBy similarity1
Modified residuei1322PhosphothreonineBy similarity1
Modified residuei1327PhosphoserineBy similarity1
Modified residuei1332PhosphoserineBy similarity1
Modified residuei1349PhosphothreonineBy similarity1
Cross-linki1358Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1362Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1369PhosphoserineBy similarity1
Modified residuei1372PhosphoserineBy similarity1
Cross-linki1380Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1382PhosphoserineBy similarity1
Modified residuei1386PhosphoserineBy similarity1
Modified residuei1417N6-acetyllysine; alternateBy similarity1
Cross-linki1417Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei1437N6-acetyllysine; alternateBy similarity1
Cross-linki1437Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki1449Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1454Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1464PhosphoserineBy similarity1
Modified residuei1466PhosphoserineBy similarity1
Modified residuei1469PhosphoserineBy similarity1
Modified residuei1471PhosphoserineBy similarity1
Cross-linki1479Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1487Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1520PhosphoserineBy similarity1

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

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

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

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

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).

Interacts with PLSCR1 (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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

STRING: functional protein association networks

More...STRINGi		10029.NP_001233667.1

<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

More...SMRi		P41515

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%5Fand%5Fdomains%5Fsection">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
Regioni1428 – 1434Interaction with PLSCR1By similarity7

<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

Identification of Orthologs from Complete Genome Data

More...OMAi		VNENMQI

Database of Orthologous Groups

More...OrthoDBi		117851at2759

Family and domain databases

Conserved Domains Database

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

Gene3D Structural and Functional Annotation of Protein Families

More...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

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
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

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

P41515-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELSPLQPVN ENMQMNKKKN EDAKKRLSIE RIYQKKTQLE HILLRPDTYI 
        60         70         80         90        100
GSVELVTQQM WVYDEDVGIN YREVTFVPGL YKIFDEILVN AADNKQRDPK 
       110        120        130        140        150
MSCIRVTIDP ENNLISIWNN GKGIPVVEHK VEKMYVPALI FGQLLTSSNY 
       160        170        180        190        200
DDDEKKVTGG RNGYGAKLCN IFSTRFTVET ASKEYKKMFK QTWMDNMGRA 
       210        220        230        240        250
GDMELKPFNG EDYTCITFQP DLSKFKMQSL DKDIVALMVR RAYDIAGSTK 
       260        270        280        290        300
DVKVFLNGNK LPVKGFRSYV DMYLKDKLDE TGNALKVVHE QVNPRWEVCL 
       310        320        330        340        350
TMSEKGFQQI SFVNSIATSK GGRHVDYVAD QIVSKLVDVV KKKNKGGVAV 
       360        370        380        390        400
KAHQVKNHMW IFVNALIENP TFDSQTKENM TLQAKSFGST CQLSEKFIKA 
       410        420        430        440        450
AIGCGIVESI LNWVKFKAQI QLNKKCSAVK HNRIKGIPKL 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 KNKQELAFYS LPEFEEWKSS 
       610        620        630        640        650
TPNHKKWKVK YYKGLGTSTS KEAKEYFADM KRHRIQFKYS GPEDDAAISL 
       660        670        680        690        700
AFSKKQVDDR KEWLTHFMED RRQRKLLGLP EDYLYGQTTT 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 PLTRLLFPPK DDHTLKFLYD DNQRVEPEWY IPIIPMVLIN 
       860        870        880        890        900
GAEGIGTGWS CKIPNFDIRE VVNNIRRLLD GEEPLPMLPS YKNFKGTIEE 
       910        920        930        940        950
LASNQYVING EVAILNSTTI EISELPIRTW TQTYKEQVLE PMLNGTEKTP 
       960        970        980        990       1000
PLITDYREYH TDTTVKFVIK MTEEKLAEAE RVGLHKVFKL QTSLTCNSMV 
      1010       1020       1030       1040       1050
LFDHVGCLKK YDTVLDILKD FFELRLKYYG LRKEWLLGML GAESAKLNNQ 
      1060       1070       1080       1090       1100
ARFILEKIDG KIIIENKPKK ELIKVLIQRG YDSDPVKAWK EAQQKVPDEE 
      1110       1120       1130       1140       1150
ENEESDNENS DSVAESGPTF NYLLDMPLWY LTKEKKDELC KQRNEKEQEL 
      1160       1170       1180       1190       1200
NTLKNKSPSD LWKEDLAVFI EELEVVEAKE KQDEQVGLPG KGGKAKGKKA 
      1210       1220       1230       1240       1250
QMSEVLPSPH GKRVIPQVTM EMKAEAEKKI RKKIKSENVE GTPTENGLEL 
      1260       1270       1280       1290       1300
GSLKQRIEKK QKKEPGAMTK KQTTLAFKPI KKGKKRNPWS DSESDMSSNE 
      1310       1320       1330       1340       1350
SNVDVPPREK DPRRAATKAK FTMDLDSDED FSGSDGKDED EDFFPLDTTP 
      1360       1370       1380       1390       1400
PKTKIPQKNT KKALKPQKSA MSGDPESDEK DSVPASPGPP AADLPADTEQ 
      1410       1420       1430       1440       1450
LKPSSKQTVA VKKTATKSQS STSTAGTKKR AVPKGSKSDS ALNAHGPEKP 
      1460       1470       1480       1490       1500
VPAKAKNSRK RKQSSSDDSD SDFEKVVSKV AASKKSKGEN QDFRVDLDET 
      1510       1520 
MVPRAKSGRA KKPIKYLEES DDDDLF
Length:1,526
Mass (Da):173,197
Last modified:November 1, 1995 - v1
<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:i5FB2D8FBF1C02929
GO

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 varianti493R → Q in cells resistant to the antineoplastic agents VP-16 and VM-26. 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
L04607 mRNA Translation: AAA37023.1

Protein sequence database of the Protein Information Resource

More...PIRi		A44406

NCBI Reference Sequences

More...RefSeqi		NP_001233667.1, NM_001246738.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSCGRT00001026641; ENSCGRP00001022396; ENSCGRG00001020913

Database of genes from NCBI RefSeq genomes

More...GeneIDi		100689304

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		cge:100689304

<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
L04607 mRNA Translation: AAA37023.1
PIRiA44406
RefSeqiNP_001233667.1, NM_001246738.1

3D structure databases

SMRiP41515
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10029.NP_001233667.1

Genome annotation databases

EnsembliENSCGRT00001026641; ENSCGRP00001022396; ENSCGRG00001020913
GeneIDi100689304
KEGGicge:100689304

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7153

Phylogenomic databases

eggNOGiKOG0355, Eukaryota
OMAiVNENMQI
OrthoDBi117851at2759

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_CRIGR
<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: P41515
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 10, 2021
This is version 152 of the entry and version 1 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again