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Q64511 (TOP2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 2-beta

EC=5.99.1.3
Alternative name(s):
DNA topoisomerase II, beta isozyme
Gene names
Name:Top2b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1612 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

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.

Subunit structure

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.

Subcellular location

Nucleusnucleolus.

Miscellaneous

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

Sequence similarities

Belongs to the type II topoisomerase family.

Contains 1 Toprim domain.

Ontologies

Keywords
   Cellular componentNucleus
   LigandATP-binding
DNA-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionIsomerase
Topoisomerase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from Biological aspect of Ancestor. Source: GOC

DNA topological change

Inferred from sequence or structural similarity. Source: UniProtKB

DNA-dependent DNA replication

Inferred from Biological aspect of Ancestor. Source: RefGenome

axonogenesis

Inferred from mutant phenotype PubMed 10615047. Source: MGI

chromosome segregation

Inferred from Biological aspect of Ancestor. Source: RefGenome

forebrain development

Inferred from mutant phenotype PubMed 12773624. Source: MGI

mitotic DNA integrity checkpoint

Inferred from Biological aspect of Ancestor. Source: RefGenome

mitotic recombination

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuron migration

Inferred from mutant phenotype PubMed 12773624. Source: MGI

resolution of meiotic recombination intermediates

Inferred from Biological aspect of Ancestor. Source: RefGenome

sister chromatid segregation

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentWINAC complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

cytosol

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 11835579PubMed 9224616. Source: MGI

synaptonemal complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding, bending

Inferred from electronic annotation. Source: InterPro

DNA topoisomerase type II (ATP-hydrolyzing) activity

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

histone deacetylase binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase C binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AicdaQ9WVE03EBI-2325586,EBI-3835567

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 16121611DNA topoisomerase 2-beta
PRO_0000145370

Regions

Domain464 – 581118Toprim
Nucleotide binding157 – 1593ATP By similarity
Nucleotide binding170 – 1778ATP By similarity
Nucleotide binding385 – 3873ATP By similarity
Region351 – 3533Interaction with DNA By similarity
Region999 – 100810Interaction with DNA By similarity

Sites

Active site8141O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Metal binding4701Magnesium 1; catalytic By similarity
Metal binding5501Magnesium 1; catalytic By similarity
Metal binding5501Magnesium 2 By similarity
Metal binding5521Magnesium 2 By similarity
Binding site1001ATP By similarity
Binding site1291ATP By similarity
Site4981Interaction with DNA By similarity
Site5011Interaction with DNA By similarity
Site6701Interaction with DNA By similarity
Site6711Interaction with DNA By similarity
Site7321Interaction with DNA By similarity
Site7661Interaction with DNA By similarity
Site8131Transition state stabilizer By similarity
Site8651Important for DNA bending; intercalates between base pairs of target DNA By similarity
Site9401Interaction with DNA By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Modified residue31N6-acetyllysine Ref.7
Modified residue12241Phosphoserine By similarity
Modified residue12801Phosphothreonine By similarity
Modified residue13241Phosphoserine By similarity
Modified residue13281Phosphoserine By similarity
Modified residue13301Phosphoserine By similarity
Modified residue13321Phosphoserine By similarity
Modified residue13461Phosphoserine By similarity
Modified residue13631Phosphoserine By similarity
Modified residue13871Phosphoserine Ref.4
Modified residue13901Phosphothreonine By similarity
Modified residue14001Phosphoserine Ref.5
Modified residue14081Phosphotyrosine By similarity
Modified residue14111Phosphoserine By similarity
Modified residue14281Phosphoserine By similarity
Modified residue14391Phosphoserine By similarity
Modified residue14411Phosphoserine By similarity
Modified residue14481Phosphoserine By similarity
Modified residue14531Phosphoserine By similarity
Modified residue14601Phosphoserine By similarity
Modified residue15091Phosphoserine Ref.4 Ref.5 Ref.6
Modified residue15111Phosphoserine Ref.4 Ref.5 Ref.6
Modified residue15131Phosphoserine Ref.4
Modified residue15371Phosphoserine Ref.4
Modified residue15391Phosphoserine Ref.4
Modified residue15621Phosphothreonine By similarity
Modified residue15681Phosphoserine By similarity
Modified residue15961Phosphotyrosine By similarity
Modified residue16001Phosphoserine By similarity

Experimental info

Sequence conflict161V → A in BAA07236. Ref.1
Sequence conflict14341L → P in BAA07236. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q64511 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: 974D9D5DAD0DB96A

FASTA1,612181,909
        10         20         30         40         50         60 
MAKSSLAGSD GALTWVNNAT KKEELETANK NDSTKKLSVE RVYQKKTQLE HILLRPDTYI 

        70         80         90        100        110        120 
GSVEPLTQLM WVYDEDVGMN CREVTFVPGL YKIFDEILVN AADNKQRDKN MTCIKVSIDP 

       130        140        150        160        170        180 
ESNIISIWNN GKGIPVVEHK VEKVYVPALI FGQLLTSSNY DDDEKKVTGG RNGYGAKLCN 

       190        200        210        220        230        240 
IFSTKFTVET ACKEYKHSFK QTWMNNMMKT SEAKIKHFDG EDYTCITFQP DLSKFKMEKL 

       250        260        270        280        290        300 
DKDIVALMTR RAYDLAGSCK GVKVMFNGKK LPVNGFRSYV DLYVKDKLDE TGVALKVIHE 

       310        320        330        340        350        360 
LANERWDVCL TLSEKGFQQI SFVNSIATTK GGRHVDYVVD QVVSKLIEVV KKKNKAGVSV 

       370        380        390        400        410        420 
KPFQVKNHIW VFINCLIENP TFDSQTKENM TLQPKSFGSK CQLSEKFFKA ASNCGIVESI 

       430        440        450        460        470        480 
LNWVKFKAQT QLNKKCSSVK YSKIKGIPKL DDANDAGGKH SLECTLILTE GDSAKSLAVS 

       490        500        510        520        530        540 
GLGVIGRDRY GVFPLRGKIL NVREASHKQI MENAEINNII KIVGLQYKKS YDDAESLKTL 

       550        560        570        580        590        600 
RYGKIMIMTD QDQDGSHIKG LLINFIHHNW PSLLKHGFLE EFITPIVKAS KNKQELSFYS 

       610        620        630        640        650        660 
IPEFDEWKKH IENQKAWKIK YYKGLGTSTA KEAKEYFADM ERHRILFRYA GPEDDAAITL 

       670        680        690        700        710        720 
AFSKKKIDDR KEWLTNFMED RRQRRLHGLP EQFLYGTATK HLTYNDFINK ELILFSNSDN 

       730        740        750        760        770        780 
ERSIPSLVDG FKPGQRKVLF TCFKRNDKRE VKVAQLAGSV AEMSAYHHGE QALMMTIVNL 

       790        800        810        820        830        840 
AQNFVGSNNI NLLQPIGQFG TRLHGGKDAA SPRYIFTMLS SLARLLFPAV DDNLLKFLYD 

       850        860        870        880        890        900 
DNQRVEPEWY IPIIPMVLIN GAEGIGTGWA CKLPNYDARE IVNNVRRMLE GLDPHPMLPN 

       910        920        930        940        950        960 
YKNFKGTIQE LGQNQYAVSG EIFVVDRNTV EITELPVRTW TQVYKEQVLE PMLNGTDKTP 

       970        980        990       1000       1010       1020 
ALISDYKEYH TDTTVKFVVK MTEEKLAQAE AAGLHKVFKL QTTLTCNSMV LFDHMGCLKK 

      1030       1040       1050       1060       1070       1080 
YETVQDILKE FFDLRLSYYG LRKEWLVGML GAESTKLNNQ ARFILEKIQG KITIENRSKK 

      1090       1100       1110       1120       1130       1140 
DLIQMLVQRG YESDPVKAWK EAQEKAAEEE DSQNQHDDSS SDSGTPSGPD FNYILNMSLW 

      1150       1160       1170       1180       1190       1200 
SLTKEKVEEL IKQRDTKGRE VNDLKRKSPS DLWKEDLAAF VEELDKVEAQ EREDILAGMS 

      1210       1220       1230       1240       1250       1260 
GKAIKGKVGK PKVKKLQLEE TMPSPYGRRI VPEITAMKAD ASRKLLKKKK GDPDTTVVKV 

      1270       1280       1290       1300       1310       1320 
EFDEEFSGTP AEGTGEETLT PSAPVNKGPK PKREKKEPGT RVRKTPTSTG KTNAKKVKKR 

      1330       1340       1350       1360       1370       1380 
NPWSDDESKS ESDLEEAEPV VIPRDSLLRR AAAERPKYTF DFSEEEDDDA AAADDSNDLE 

      1390       1400       1410       1420       1430       1440 
ELKVKASPIT NDGEDEFVPS DGLDKDEYAF SSGKSKATPE KSSNDKKSQD FGNLFSFPSY 

      1450       1460       1470       1480       1490       1500 
SQKSEDDSAK FDSNEEDTAS VFAPSFGLKQ TDKLPSKTVA AKKGKPPSDT APKAKRAPKQ 

      1510       1520       1530       1540       1550       1560 
KKIVETINSD SDSEFGIPKK TTTPKGKGRG AKKRKASGSE NEGDYNPGRK PSKTASKKPK 

      1570       1580       1590       1600       1610 
KTSFDQDSDV DIFPSDFTSE PPALPRTGRA RKEVKYFAES DEEEDVDFAM FN 

« Hide

References

« Hide 'large scale' references
[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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D38046 mRNA. Translation: BAA07236.1.
BC041106 mRNA. Translation: AAH41106.1.
BC054541 mRNA. Translation: AAH54541.1.
RefSeqNP_033435.2. NM_009409.2.
UniGeneMm.130362.

3D structure databases

ProteinModelPortalQ64511.
SMRQ64511. Positions 38-1194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204277. 5 interactions.
IntActQ64511. 6 interactions.
MINTMINT-4138251.
STRING10090.ENSMUSP00000017629.

Chemistry

BindingDBQ64511.
ChEMBLCHEMBL5564.

PTM databases

PhosphoSiteQ64511.

Proteomic databases

PaxDbQ64511.
PRIDEQ64511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017629; ENSMUSP00000017629; ENSMUSG00000017485.
GeneID21974.
KEGGmmu:21974.
UCSCuc007shc.1. mouse.

Organism-specific databases

CTD7155.
MGIMGI:98791. Top2b.

Phylogenomic databases

eggNOGCOG0187.
GeneTreeENSGT00390000016222.
HOGENOMHOG000216693.
HOVERGENHBG052998.
InParanoidQ64511.
KOK03164.
OMARHIDYVV.
OrthoDBEOG73JKTM.
PhylomeDBQ64511.
TreeFamTF105282.

Gene expression databases

ArrayExpressQ64511.
BgeeQ64511.
CleanExMM_TOP2B.
GenevestigatorQ64511.

Family and domain databases

Gene3D1.10.268.10. 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.
InterProIPR024946. 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]
PANTHERPTHR10169:SF18. PTHR10169:SF18. 1 hit.
PfamPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF08070. DTHCT. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00418. TPI2FAMILY.
SMARTSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301674.
PROQ64511.
SOURCESearch...

Entry information

Entry nameTOP2B_MOUSE
AccessionPrimary (citable) accession number: Q64511
Secondary accession number(s): Q7TQG4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 27, 2005
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot