DNA topoisomerase 2-beta - Mus musculus (Mouse)

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Q64511 (TOP2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 122. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA topoisomerase 2-beta
EC=5.99.1.3

Alternative name(s):
DNA topoisomerase II, beta isozyme

Gene names

Name:

Top2b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1612 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Nucleus › nucleolus.
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 component	Nucleus
Ligand	ATP-binding DNA-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 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_component	WINAC complex Inferred from Biological aspect of Ancestor. Source: RefGenome cytosol Inferred from electronic annotation. Source: Compara nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: Compara synaptonemal complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW 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
Aicda	Q9WVE0	3	EBI-2325586,EBI-3835567

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1612

1612

DNA topoisomerase 2-beta

PRO_0000145370

Regions

Domain

464 – 581

118

Toprim

Nucleotide binding

157 – 159

ATP By similarity

Nucleotide binding

170 – 177

ATP By similarity

Nucleotide binding

385 – 387

ATP By similarity

Region

351 – 353

Interaction with DNA By similarity

Region

999 – 1008

Interaction with DNA By similarity

Sites

Active site

814

O-(5'-phospho-DNA)-tyrosine intermediate By similarity

Metal binding

470

Magnesium 1; catalytic By similarity

Metal binding

550

Magnesium 1; catalytic By similarity

Metal binding

550

Magnesium 2 By similarity

Metal binding

552

Magnesium 2 By similarity

Binding site

100

ATP By similarity

Binding site

129

ATP By similarity

Site

498

Interaction with DNA By similarity

Site

501

Interaction with DNA By similarity

Site

670

Interaction with DNA By similarity

Site

671

Interaction with DNA By similarity

Site

732

Interaction with DNA By similarity

Site

766

Interaction with DNA By similarity

Site

813

Transition state stabilizer By similarity

Site

865

Important for DNA bending; intercalates between base pairs of target DNA By similarity

Site

940

Interaction with DNA By similarity

Amino acid modifications

Modified residue

419

Phosphoserine Ref.3

Modified residue

627

Phosphothreonine Ref.3

Modified residue

1224

Phosphoserine By similarity

Modified residue

1280

Phosphothreonine By similarity

Modified residue

1324

Phosphoserine Ref.5

Modified residue

1328

Phosphoserine Ref.5

Modified residue

1330

Phosphoserine Ref.5

Modified residue

1332

Phosphoserine Ref.5

Modified residue

1346

Phosphoserine By similarity

Modified residue

1363

Phosphoserine By similarity

Modified residue

1387

Phosphoserine Ref.3 Ref.4 Ref.5

Modified residue

1390

Phosphothreonine By similarity

Modified residue

1400

Phosphoserine Ref.3

Modified residue

1408

Phosphotyrosine By similarity

Modified residue

1411

Phosphoserine By similarity

Modified residue

1428

Phosphoserine By similarity

Modified residue

1439

Phosphoserine By similarity

Modified residue

1441

Phosphoserine By similarity

Modified residue

1448

Phosphoserine By similarity

Modified residue

1453

Phosphoserine Ref.3 Ref.4 Ref.7

Modified residue

1458

Phosphothreonine Ref.3

Modified residue

1460

Phosphoserine By similarity

Modified residue

1509

Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7

Modified residue

1511

Phosphoserine Ref.4 Ref.5 Ref.7

Modified residue

1513

Phosphoserine Ref.4

Modified residue

1537

Phosphoserine Ref.4 Ref.5

Modified residue

1539

Phosphoserine Ref.4 Ref.5

Modified residue

1562

Phosphothreonine By similarity

Modified residue

1568

Phosphoserine By similarity

Modified residue

1596

Phosphotyrosine By similarity

Modified residue

1600

Phosphoserine By similarity

Experimental info

Sequence conflict

V → A in BAA07236. Ref.1

Sequence conflict

1434

L → P in BAA07236. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q64511 [UniParc].

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

1,612

181,909

        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' referencesShow '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]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; THR-627; SER-1387; SER-1400; SER-1453 AND THR-1458, MASS SPECTROMETRY. Tissue: Liver.
[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-1453; SER-1509; SER-1511; SER-1513; SER-1537 AND SER-1539, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1324; SER-1328; SER-1330; SER-1332; SER-1387; SER-1509; SER-1511; SER-1537 AND SER-1539, MASS SPECTROMETRY. Tissue: Melanoma.
[6]	"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-1509, MASS SPECTROMETRY. Tissue: Macrophage.
[7]	"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-1453; SER-1509 AND SER-1511, MASS SPECTROMETRY. 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.
IPI	IPI00135443.
RefSeq	NP_033435.2. NM_009409.2.
UniGene	Mm.130362.
3D structure databases
ProteinModelPortal	Q64511.
SMR	Q64511. Positions 38-414, 445-1194.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q64511. 5 interactions.
STRING	10090.ENSMUSP00000017629.
PTM databases
PhosphoSite	Q64511.
Proteomic databases
PaxDb	Q64511.
PRIDE	Q64511.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000017629; ENSMUSP00000017629; ENSMUSG00000017485.
GeneID	21974.
KEGG	mmu:21974.
UCSC	uc007shc.1. mouse.
Organism-specific databases
CTD	7155.
MGI	MGI:98791. Top2b.
Phylogenomic databases
eggNOG	COG0187.
GeneTree	ENSGT00390000016222.
HOGENOM	HOG000216693.
HOVERGEN	HBG052998.
InParanoid	Q64511.
KO	K03164.
OMA	AKEYFQD.
OrthoDB	EOG4640B2.
Gene expression databases
ArrayExpress	Q64511.
Bgee	Q64511.
CleanEx	MM_TOP2B.
Genevestigator	Q64511.
GermOnline	ENSMUSG00000017485. Mus musculus.
Family and domain databases
Gene3D	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.
InterPro	IPR024946. Arg_repress_C-like. IPR012542. DTHCT. IPR003594. HATPase_ATP-bd. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. 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]
Pfam	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]
PRINTS	PR00418. TPI2FAMILY.
SMART	SM00387. HATPase_c. 1 hit. SM00433. TOP2c. 1 hit. SM00434. TOP4c. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. SSF56719. Topo_IIA_cen. 1 hit.
PROSITE	PS00177. TOPOISOMERASE_II. 1 hit. PS50880. TOPRIM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q64511.
ChEMBL	CHEMBL5564.
NextBio	301674.
SOURCE	Search...

Entry information

Entry name

TOP2B_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents