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Q64511

- TOP2B_MOUSE

UniProt

Q64511 - TOP2B_MOUSE

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Protein
DNA topoisomerase 2-beta
Gene
Top2b
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. Indirectly involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene By similarity.

Catalytic activityi

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

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 sitei100 – 1001ATP By similarity
Binding sitei129 – 1291ATP By similarity
Metal bindingi470 – 4701Magnesium 1; catalytic By similarity
Sitei498 – 4981Interaction with DNA By similarity
Sitei501 – 5011Interaction with DNA By similarity
Metal bindingi550 – 5501Magnesium 1; catalytic By similarity
Metal bindingi550 – 5501Magnesium 2 By similarity
Metal bindingi552 – 5521Magnesium 2 By similarity
Sitei670 – 6701Interaction with DNA By similarity
Sitei671 – 6711Interaction with DNA By similarity
Sitei732 – 7321Interaction with DNA By similarity
Sitei766 – 7661Interaction with DNA By similarity
Sitei813 – 8131Transition state stabilizer By similarity
Active sitei814 – 8141O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Sitei865 – 8651Important for DNA bending; intercalates between base pairs of target DNA By similarity
Sitei940 – 9401Interaction with DNA By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi157 – 1593ATP By similarity
Nucleotide bindingi170 – 1778ATP By similarity
Nucleotide bindingi385 – 3873ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. DNA topological change Source: UniProtKB
  3. DNA unwinding involved in DNA replication Source: RefGenome
  4. axonogenesis Source: MGI
  5. forebrain development Source: MGI
  6. mitotic DNA integrity checkpoint Source: RefGenome
  7. mitotic recombination Source: RefGenome
  8. neuron migration Source: MGI
  9. resolution of meiotic recombination intermediates Source: RefGenome
  10. sister chromatid segregation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 2-beta (EC:5.99.1.3)
Alternative name(s):
DNA topoisomerase II, beta isozyme
Gene namesi
Name:Top2b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:98791. Top2b.

Subcellular locationi

GO - Cellular componenti

  1. DNA topoisomerase complex (ATP-hydrolyzing) Source: RefGenome
  2. cytosol Source: Ensembl
  3. nucleolus Source: UniProtKB-SubCell
  4. nucleoplasm Source: Ensembl
  5. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 16121611DNA topoisomerase 2-beta
PRO_0000145370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei3 – 31N6-acetyllysine1 Publication
Modified residuei1224 – 12241Phosphoserine By similarity
Modified residuei1280 – 12801Phosphothreonine By similarity
Modified residuei1324 – 13241Phosphoserine By similarity
Modified residuei1328 – 13281Phosphoserine By similarity
Modified residuei1330 – 13301Phosphoserine By similarity
Modified residuei1332 – 13321Phosphoserine By similarity
Modified residuei1346 – 13461Phosphoserine By similarity
Modified residuei1363 – 13631Phosphoserine By similarity
Modified residuei1387 – 13871Phosphoserine1 Publication
Modified residuei1390 – 13901Phosphothreonine By similarity
Modified residuei1400 – 14001Phosphoserine1 Publication
Modified residuei1408 – 14081Phosphotyrosine By similarity
Modified residuei1411 – 14111Phosphoserine By similarity
Modified residuei1428 – 14281Phosphoserine By similarity
Modified residuei1439 – 14391Phosphoserine By similarity
Modified residuei1441 – 14411Phosphoserine By similarity
Modified residuei1448 – 14481Phosphoserine By similarity
Modified residuei1453 – 14531Phosphoserine By similarity
Modified residuei1460 – 14601Phosphoserine By similarity
Modified residuei1509 – 15091Phosphoserine3 Publications
Modified residuei1511 – 15111Phosphoserine3 Publications
Modified residuei1513 – 15131Phosphoserine1 Publication
Modified residuei1537 – 15371Phosphoserine1 Publication
Modified residuei1539 – 15391Phosphoserine1 Publication
Modified residuei1562 – 15621Phosphothreonine By similarity
Modified residuei1568 – 15681Phosphoserine By similarity
Modified residuei1596 – 15961Phosphotyrosine By similarity
Modified residuei1600 – 16001Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ64511.
PaxDbiQ64511.
PRIDEiQ64511.

PTM databases

PhosphoSiteiQ64511.

Expressioni

Gene expression databases

ArrayExpressiQ64511.
BgeeiQ64511.
CleanExiMM_TOP2B.
GenevestigatoriQ64511.

Interactioni

Subunit structurei

Homodimer. Component of the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
AicdaQ9WVE03EBI-2325586,EBI-3835567

Protein-protein interaction databases

BioGridi204277. 5 interactions.
IntActiQ64511. 6 interactions.
MINTiMINT-4138251.
STRINGi10090.ENSMUSP00000017629.

Structurei

3D structure databases

ProteinModelPortaliQ64511.
SMRiQ64511. Positions 38-1194.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini464 – 581118Toprim
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni351 – 3533Interaction with DNA By similarity
Regioni999 – 100810Interaction with DNA By similarity

Sequence similaritiesi

Contains 1 Toprim domain.

Phylogenomic databases

eggNOGiCOG0187.
GeneTreeiENSGT00390000016222.
HOGENOMiHOG000216693.
HOVERGENiHBG052998.
InParanoidiQ64511.
KOiK03164.
OMAiEPLTQFM.
OrthoDBiEOG73JKTM.
PhylomeDBiQ64511.
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.
IPR028467. Top2b.
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:SF36. PTHR10169:SF36. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q64511-1 [UniParc]FASTAAdd to Basket

« Hide

MAKSSLAGSD GALTWVNNAT KKEELETANK NDSTKKLSVE RVYQKKTQLE     50
HILLRPDTYI GSVEPLTQLM WVYDEDVGMN CREVTFVPGL YKIFDEILVN 100
AADNKQRDKN MTCIKVSIDP ESNIISIWNN GKGIPVVEHK VEKVYVPALI 150
FGQLLTSSNY DDDEKKVTGG RNGYGAKLCN IFSTKFTVET ACKEYKHSFK 200
QTWMNNMMKT SEAKIKHFDG EDYTCITFQP DLSKFKMEKL DKDIVALMTR 250
RAYDLAGSCK GVKVMFNGKK LPVNGFRSYV DLYVKDKLDE TGVALKVIHE 300
LANERWDVCL TLSEKGFQQI SFVNSIATTK GGRHVDYVVD QVVSKLIEVV 350
KKKNKAGVSV KPFQVKNHIW VFINCLIENP TFDSQTKENM TLQPKSFGSK 400
CQLSEKFFKA ASNCGIVESI LNWVKFKAQT QLNKKCSSVK YSKIKGIPKL 450
DDANDAGGKH SLECTLILTE GDSAKSLAVS GLGVIGRDRY GVFPLRGKIL 500
NVREASHKQI MENAEINNII KIVGLQYKKS YDDAESLKTL RYGKIMIMTD 550
QDQDGSHIKG LLINFIHHNW PSLLKHGFLE EFITPIVKAS KNKQELSFYS 600
IPEFDEWKKH IENQKAWKIK YYKGLGTSTA KEAKEYFADM ERHRILFRYA 650
GPEDDAAITL AFSKKKIDDR KEWLTNFMED RRQRRLHGLP EQFLYGTATK 700
HLTYNDFINK ELILFSNSDN ERSIPSLVDG FKPGQRKVLF TCFKRNDKRE 750
VKVAQLAGSV AEMSAYHHGE QALMMTIVNL AQNFVGSNNI NLLQPIGQFG 800
TRLHGGKDAA SPRYIFTMLS SLARLLFPAV DDNLLKFLYD DNQRVEPEWY 850
IPIIPMVLIN GAEGIGTGWA CKLPNYDARE IVNNVRRMLE GLDPHPMLPN 900
YKNFKGTIQE LGQNQYAVSG EIFVVDRNTV EITELPVRTW TQVYKEQVLE 950
PMLNGTDKTP ALISDYKEYH TDTTVKFVVK MTEEKLAQAE AAGLHKVFKL 1000
QTTLTCNSMV LFDHMGCLKK YETVQDILKE FFDLRLSYYG LRKEWLVGML 1050
GAESTKLNNQ ARFILEKIQG KITIENRSKK DLIQMLVQRG YESDPVKAWK 1100
EAQEKAAEEE DSQNQHDDSS SDSGTPSGPD FNYILNMSLW SLTKEKVEEL 1150
IKQRDTKGRE VNDLKRKSPS DLWKEDLAAF VEELDKVEAQ EREDILAGMS 1200
GKAIKGKVGK PKVKKLQLEE TMPSPYGRRI VPEITAMKAD ASRKLLKKKK 1250
GDPDTTVVKV EFDEEFSGTP AEGTGEETLT PSAPVNKGPK PKREKKEPGT 1300
RVRKTPTSTG KTNAKKVKKR NPWSDDESKS ESDLEEAEPV VIPRDSLLRR 1350
AAAERPKYTF DFSEEEDDDA AAADDSNDLE ELKVKASPIT NDGEDEFVPS 1400
DGLDKDEYAF SSGKSKATPE KSSNDKKSQD FGNLFSFPSY SQKSEDDSAK 1450
FDSNEEDTAS VFAPSFGLKQ TDKLPSKTVA AKKGKPPSDT APKAKRAPKQ 1500
KKIVETINSD SDSEFGIPKK TTTPKGKGRG AKKRKASGSE NEGDYNPGRK 1550
PSKTASKKPK KTSFDQDSDV DIFPSDFTSE PPALPRTGRA RKEVKYFAES 1600
DEEEDVDFAM FN 1612
Length:1,612
Mass (Da):181,909
Last modified:September 27, 2005 - v2
Checksum:i974D9D5DAD0DB96A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161V → A in BAA07236. 1 Publication
Sequence conflicti1434 – 14341L → P in BAA07236. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38046 mRNA. Translation: BAA07236.1.
BC041106 mRNA. Translation: AAH41106.1.
BC054541 mRNA. Translation: AAH54541.1.
CCDSiCCDS26833.1.
RefSeqiNP_033435.2. NM_009409.2.
UniGeneiMm.130362.

Genome annotation databases

EnsembliENSMUST00000017629; ENSMUSP00000017629; ENSMUSG00000017485.
GeneIDi21974.
KEGGimmu:21974.
UCSCiuc007shc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D38046 mRNA. Translation: BAA07236.1 .
BC041106 mRNA. Translation: AAH41106.1 .
BC054541 mRNA. Translation: AAH54541.1 .
CCDSi CCDS26833.1.
RefSeqi NP_033435.2. NM_009409.2.
UniGenei Mm.130362.

3D structure databases

ProteinModelPortali Q64511.
SMRi Q64511. Positions 38-1194.
ModBasei Search...

Protein-protein interaction databases

BioGridi 204277. 5 interactions.
IntActi Q64511. 6 interactions.
MINTi MINT-4138251.
STRINGi 10090.ENSMUSP00000017629.

Chemistry

BindingDBi Q64511.
ChEMBLi CHEMBL5564.

PTM databases

PhosphoSitei Q64511.

Proteomic databases

MaxQBi Q64511.
PaxDbi Q64511.
PRIDEi Q64511.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000017629 ; ENSMUSP00000017629 ; ENSMUSG00000017485 .
GeneIDi 21974.
KEGGi mmu:21974.
UCSCi uc007shc.1. mouse.

Organism-specific databases

CTDi 7155.
MGIi MGI:98791. Top2b.

Phylogenomic databases

eggNOGi COG0187.
GeneTreei ENSGT00390000016222.
HOGENOMi HOG000216693.
HOVERGENi HBG052998.
InParanoidi Q64511.
KOi K03164.
OMAi EPLTQFM.
OrthoDBi EOG73JKTM.
PhylomeDBi Q64511.
TreeFami TF105282.

Miscellaneous databases

NextBioi 301674.
PROi Q64511.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q64511.
Bgeei Q64511.
CleanExi MM_TOP2B.
Genevestigatori Q64511.

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.
IPR028467. Top2b.
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:SF36. PTHR10169:SF36. 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. Miyaike M., Adachi N., Kikuchi A.
    Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Brain and Eye.
  3. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; SER-1509; SER-1511; SER-1513; SER-1537 AND SER-1539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1509 AND SER-1511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509 AND SER-1511, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. "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 ALA-2 AND LYS-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTOP2B_MOUSE
AccessioniPrimary (citable) accession number: Q64511
Secondary accession number(s): Q7TQG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 27, 2005
Last modified: September 3, 2014
This is version 136 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