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Q01320

- TOP2A_MOUSE

UniProt

Q01320 - TOP2A_MOUSE

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Protein
DNA topoisomerase 2-alpha
Gene
Top2a, Top-2, Top2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.1 Publication

Cofactori

Magnesium. 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+ and Ca2+ By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei90 – 901ATP By similarity
Binding sitei119 – 1191ATP By similarity
Metal bindingi460 – 4601Magnesium 1; catalytic By similarity
Sitei488 – 4881Interaction with DNA By similarity
Sitei491 – 4911Interaction with DNA By similarity
Metal bindingi540 – 5401Magnesium 1; catalytic By similarity
Metal bindingi540 – 5401Magnesium 2 By similarity
Metal bindingi542 – 5421Magnesium 2 By similarity
Sitei660 – 6601Interaction with DNA By similarity
Sitei661 – 6611Interaction with DNA By similarity
Sitei722 – 7221Interaction with DNA By similarity
Sitei756 – 7561Interaction with DNA By similarity
Sitei762 – 7621Interaction with DNA By similarity
Sitei803 – 8031Transition state stabilizer By similarity
Active sitei804 – 8041O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Sitei855 – 8551Important for DNA bending; intercalates between base pairs of target DNA By similarity
Sitei930 – 9301Interaction with DNA By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi147 – 1493ATP By similarity
Nucleotide bindingi160 – 1678ATP By similarity
Nucleotide bindingi375 – 3773ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding, bending Source: UniProtKB
  3. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: MGI
  4. chromatin binding Source: Ensembl
  5. drug binding Source: Ensembl
  6. magnesium ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA ligation Source: Ensembl
  3. DNA topological change Source: MGI
  4. DNA unwinding involved in DNA replication Source: RefGenome
  5. apoptotic chromosome condensation Source: RefGenome
  6. cellular response to DNA damage stimulus Source: Ensembl
  7. chromosome condensation Source: MGI
  8. chromosome segregation Source: MGI
  9. embryonic cleavage Source: MGI
  10. hematopoietic progenitor cell differentiation Source: MGI
  11. mitotic DNA integrity checkpoint Source: RefGenome
  12. mitotic recombination Source: RefGenome
  13. positive regulation of apoptotic process Source: Ensembl
  14. positive regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: Ensembl
  15. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  16. resolution of meiotic recombination intermediates Source: RefGenome
  17. sister chromatid segregation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Ligandi

ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_199110. G0 and Early G1.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 2-alpha (EC:5.99.1.3)
Alternative name(s):
DNA topoisomerase II, alpha isozyme
Gene namesi
Name:Top2a
Synonyms:Top-2, Top2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:98790. Top2a.

Subcellular locationi

GO - Cellular componenti

  1. DNA topoisomerase complex (ATP-hydrolyzing) Source: RefGenome
  2. centriole Source: Ensembl
  3. condensed chromosome Source: MGI
  4. nuclear chromosome Source: Ensembl
  5. nucleolus Source: MGI
  6. nucleoplasm Source: Ensembl
  7. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15281528DNA topoisomerase 2-alpha
PRO_0000145364Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei4 – 41Phosphoserine By similarity
Modified residuei281 – 2811Phosphothreonine By similarity
Modified residuei1105 – 11051Phosphoserine; by CK1 By similarity
Modified residuei1211 – 12111Phosphoserine By similarity
Modified residuei1291 – 12911Phosphoserine By similarity
Modified residuei1293 – 12931Phosphoserine By similarity
Modified residuei1295 – 12951Phosphoserine By similarity
Modified residuei1298 – 12981Phosphoserine By similarity
Modified residuei1328 – 13281Phosphoserine By similarity
Modified residuei1333 – 13331Phosphoserine By similarity
Modified residuei1370 – 13701Phosphoserine By similarity
Modified residuei1373 – 13731Phosphoserine By similarity
Modified residuei1384 – 13841Phosphoserine By similarity
Modified residuei1418 – 14181N6-acetyllysine1 Publication
Modified residuei1438 – 14381N6-acetyllysine1 Publication
Modified residuei1465 – 14651Phosphoserine By similarity
Modified residuei1467 – 14671Phosphoserine By similarity
Modified residuei1470 – 14701Phosphoserine By similarity
Modified residuei1472 – 14721Phosphoserine By similarity
Modified residuei1521 – 15211Phosphoserine By similarity

Post-translational modificationi

Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1105 by CSNK1D/CK1 promotes DNA cleavable complex formation By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ01320.
PRIDEiQ01320.

PTM databases

PhosphoSiteiQ01320.

Expressioni

Gene expression databases

ArrayExpressiQ01320.
BgeeiQ01320.
CleanExiMM_TOP2A.
GenevestigatoriQ01320.

Interactioni

Subunit structurei

Homodimer. Interacts with COPS5. Interacts with RECQL5; this stimulates DNA decatenation By similarity.

Protein-protein interaction databases

DIPiDIP-40621N.
IntActiQ01320. 8 interactions.
MINTiMINT-1712967.

Structurei

3D structure databases

ProteinModelPortaliQ01320.
SMRiQ01320. Positions 28-404, 433-1187.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini454 – 571118Toprim
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni341 – 3433Interaction with DNA By similarity
Regioni989 – 99810Interaction with DNA By similarity

Sequence similaritiesi

Contains 1 Toprim domain.

Phylogenomic databases

eggNOGiCOG0187.
GeneTreeiENSGT00390000016222.
HOGENOMiHOG000216693.
HOVERGENiHBG052998.
InParanoidiQ01320.
KOiK03164.
OMAiSRWEVCL.
OrthoDBiEOG73JKTM.
TreeFamiTF105282.

Family and domain databases

Gene3Di1.10.268.10. 1 hit.
3.30.1360.40. 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.
InterProiIPR024946. Arg_repress_C-like.
IPR012542. DTHCT.
IPR003594. HATPase_ATP-bd.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR028466. Top2a.
IPR001241. Topo_IIA.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_dom.
IPR013760. Topo_IIA_like_dom.
IPR018522. TopoIIA_CS.
IPR006171. Toprim_domain.
[Graphical view]
PANTHERiPTHR10169:SF33. PTHR10169:SF33. 1 hit.
PfamiPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF08070. DTHCT. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSiPR00418. TPI2FAMILY.
SMARTiSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01320-1 [UniParc]FASTAAdd to Basket

« Hide

MELSPLQPVN ENMLMNKKKN EDGKKRLSIE RIYQKKTQLE HILLRPDTYI     50
GSVELVTQQM WVYDEDVGIN YREVTFVPGL YKIFDEILVN AADNKQRDPK 100
MSCIRVTIDP ENNVISIWNN GKGIPVVEHK VEKIYVPALI FGQLLTSSNY 150
DDDEKKVTGG RNGYGAKLCN IFSTKFTVET ASREYKKMFK QTWMDNMGRA 200
GDMELKPFSG EDYTCITFQP DLSKFKMQSL DKDIVALMVR RAYDIAGSTK 250
DVKVFLNGNS LPVKGFRSYV DLYLKDKVDE TGNSLKVIHE QVNPRWEVCL 300
TMSERGFQQI SFVNSIATSK GGRHVDYVAD QIVSKLVDVV KKKNKGGVAV 350
KAHQVKNHMW IFVNALIENP TFDSQTKENM TLQAKSFGST CQLSEKFIKA 400
AIGCGIVESI LNWVKFKAQI QLNKKCSAVK HTKIKGIPKL DDANDAGSRN 450
STECTLILTE GDSAKTLAVS GLGVVGRDKY GVFPLRGKIL NVREASHKQI 500
MENAEINNII KIVGLQYKKN YEDEDSLKTL RYGKIMIMTD QDQDGSHIKG 550
LLINFIHHNW PSLLRHRFLE EFITPIVKVS KNKQEIAFYS LPEFEEWKSS 600
TPNHKKWKVK YYKGLGTSTS KEAKEYFADM KRHRIQFKYS GPEDDAAISL 650
AFSKKQVDDR KEWLTNFMED RRQRKLLGLP EDYLYGQSTS YLTYNDFINK 700
ELILFSNSDN ERSIPSMVDG LKPGQRKVLF TCFKRNDKRE VKVAQLAGSV 750
AEMSSYHHGE MSLMMTIINL AQNFVGSNNL NLLQPIGQFG TRLHGGKDSA 800
SPRYIFTMLS PLARLLFPPK DDHTLRFLYD DNQRVEPEWY IPIIPMVLIN 850
GAEGIGTGWS CKIPNFDVRE VVNNIRRLLD GEEPLPMLPS YKNFKGTIEE 900
LASNQYVING EVAILDSTTI EISELPIRTW TQTYKEQVLE PMLNGTEKTP 950
SLITDYREYH TDTTVKFVIK MTEEKLAEAE RVGLHKVFKL QSSLTCNSMV 1000
LFDHVGCLKK YDTVLDILRD FFELRLKYYG LRKEWLLGML GAESSKLNNQ 1050
ARFILEKIDG KIVIENKPKK ELIKVLIQRG YDSDPVKAWK EAQQKVPDEE 1100
ENEESDTETS TSDSAAEAGP TFNYLLDMPL WYLTKEKKDE LCKQRNEKEQ 1150
ELNTLKQKSP SDLWKEDLAV FIEELEVVEA KEKQDEQVGL PGKAGKAKGK 1200
KAQMCADVLP SPRGKRVIPQ VTVEMKAEAE KKIRKKIKSE NVEGTPAEDG 1250
AEPGSLRQRI EKKQKKEPGA KKQTTLPFKP VKKGRKKNPW SDSESDVSSN 1300
ESNVDVPPRQ KEQRSAAAKA KFTVDLDSDE DFSGLDEKDE DEDFLPLDAT 1350
PPKAKIPPKN TKKALKTQGS SMSVVDLESD VKDSVPASPG VPAADFPAET 1400
EQSKPSKKTV GVKKTATKSQ SSVSTAGTKK RAAPKGTKSD SALSARVSEK 1450
PAPAKAKNSR KRKPSSSDSS DSDFERAISK GATSKKAKGE EQDFPVDLED 1500
TIAPRAKSDR ARKPIKYLEE SDDDDDLF 1528
Length:1,528
Mass (Da):172,790
Last modified:December 14, 2011 - v2
Checksum:i63CBF8F649D103C7
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti184 – 1841E → A in BAA02076. 1 Publication
Sequence conflicti260 – 2601S → M in BAA02076. 1 Publication
Sequence conflicti640 – 6401S → P in BAA02076. 1 Publication
Sequence conflicti841 – 8411I → N in BAA02076. 1 Publication
Sequence conflicti844 – 8452IP → NT in BAA02076. 1 Publication
Sequence conflicti1316 – 13161A → R in BAA02076. 1 Publication
Sequence conflicti1316 – 13161A → R in AAC52135. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006533153.1.
UniGeneiMm.4237.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D12513 mRNA. Translation: BAA02076.1 .
AL591067 Genomic DNA. No translation available.
U01915 mRNA. Translation: AAC52135.1 .
CCDSi CCDS25370.1.
PIRi JS0703.
RefSeqi NP_035753.2. NM_011623.2.
XP_006533216.1. XM_006533153.1.
UniGenei Mm.4237.

3D structure databases

ProteinModelPortali Q01320.
SMRi Q01320. Positions 28-404, 433-1187.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-40621N.
IntActi Q01320. 8 interactions.
MINTi MINT-1712967.

Chemistry

BindingDBi Q01320.
ChEMBLi CHEMBL3586.
GuidetoPHARMACOLOGYi 2637.

PTM databases

PhosphoSitei Q01320.

Proteomic databases

PaxDbi Q01320.
PRIDEi Q01320.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000068031 ; ENSMUSP00000068896 ; ENSMUSG00000020914 .
GeneIDi 21973.
KEGGi mmu:21973.
UCSCi uc007lid.1. mouse.

Organism-specific databases

CTDi 7153.
MGIi MGI:98790. Top2a.

Phylogenomic databases

eggNOGi COG0187.
GeneTreei ENSGT00390000016222.
HOGENOMi HOG000216693.
HOVERGENi HBG052998.
InParanoidi Q01320.
KOi K03164.
OMAi SRWEVCL.
OrthoDBi EOG73JKTM.
TreeFami TF105282.

Enzyme and pathway databases

Reactomei REACT_199110. G0 and Early G1.

Miscellaneous databases

ChiTaRSi TOP2A. mouse.
NextBioi 301670.
PROi Q01320.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q01320.
Bgeei Q01320.
CleanExi MM_TOP2A.
Genevestigatori Q01320.

Family and domain databases

Gene3Di 1.10.268.10. 1 hit.
3.30.1360.40. 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.
InterProi IPR024946. Arg_repress_C-like.
IPR012542. DTHCT.
IPR003594. HATPase_ATP-bd.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR028466. Top2a.
IPR001241. Topo_IIA.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_dom.
IPR013760. Topo_IIA_like_dom.
IPR018522. TopoIIA_CS.
IPR006171. Toprim_domain.
[Graphical view ]
PANTHERi PTHR10169:SF33. PTHR10169:SF33. 1 hit.
Pfami PF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF08070. DTHCT. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view ]
PRINTSi PR00418. TPI2FAMILY.
SMARTi SM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEi PS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of cDNA encoding the mouse DNA topoisomerase II that can complement the budding yeast top2 mutation."
    Adachi N., Miyaike M., Ikeda H., Kikuchi A.
    Nucleic Acids Res. 20:5297-5303(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, FUNCTION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Characterization of a DNA topoisomerase IIalpha gene rearrangement in adriamycin-resistant P388 leukemia: expression of a fusion messenger RNA transcript encoding topoisomerase IIalpha and the retinoic acid receptor alpha locus."
    McPherson J., Brown G.A., Goldenberg G.J.
    Cancer Res. 53:5885-5889(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1254-1528.
    Tissue: Lymphoma.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1418 AND LYS-1438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTOP2A_MOUSE
AccessioniPrimary (citable) accession number: Q01320
Secondary accession number(s): E9PX08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 14, 2011
Last modified: September 3, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi