Reviewed, UniProtKB/Swiss-Prot Q02880 (TOP2B_HUMAN)

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

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1626 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 ivolved 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.
Catalytic activity	ATP-dependent breakage, passage and rejoining of double-stranded DNA.
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.
Subcellular location	Cytoplasm. Nucleus › nucleolus.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
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.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	DNA topological change Inferred from electronic annotation. Source: InterPro
Cellular component	chromosome Inferred from electronic annotation. Source: InterPro cytosol Inferred from direct assay. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase (ATP-hydrolyzing) activity Inferred from electronic annotation. Source: EC chromatin binding Inferred from direct assay. Source: UniProtKB histone deacetylase binding Inferred from physical interaction. Source: UniProtKB protein C-terminus binding Inferred from physical interaction. Source: UniProtKB protein heterodimerization activity Inferred from physical interaction. Source: UniProtKB protein kinase C binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Beta-2 (identifier: Q02880-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Beta-1 (identifier: Q02880-2)

The sequence of this isoform differs from the canonical sequence as follows:
     24-28: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1626	1626	DNA topoisomerase 2-beta		PRO_0000145369
Regions
	Nucleotide binding	182 – 187	6	ATP Potential
	Motif	1034 – 1044	11	Nuclear export signal
Sites
	Active site	826	1	O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Amino acid modifications
	Modified residue	431	1	Phosphoserine By similarity
	Modified residue	639	1	Phosphothreonine Ref.11
	Modified residue	640	1	Phosphoserine Ref.11
	Modified residue	1236	1	Phosphoserine Ref.14 Ref.17
	Modified residue	1336	1	Phosphoserine Ref.11 Ref.17
	Modified residue	1340	1	Phosphoserine Ref.11 Ref.17
	Modified residue	1342	1	Phosphoserine Ref.11 Ref.17
	Modified residue	1344	1	Phosphoserine Ref.11 Ref.17
	Modified residue	1375	1	Phosphoserine Ref.17
	Modified residue	1400	1	Phosphoserine Ref.11 Ref.16 Ref.17
	Modified residue	1413	1	Phosphoserine Ref.11 Ref.16 Ref.17
	Modified residue	1421	1	Phosphotyrosine Ref.17
	Modified residue	1424	1	Phosphoserine Ref.16 Ref.17
	Modified residue	1454	1	Phosphoserine Ref.15
	Modified residue	1466	1	Phosphoserine Ref.10 Ref.17
	Modified residue	1471	1	Phosphoserine Ref.12
	Modified residue	1522	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13 Ref.17
	Modified residue	1524	1	Phosphoserine Ref.11 Ref.12 Ref.13 Ref.17
	Modified residue	1526	1	Phosphoserine Ref.17
	Modified residue	1550	1	Phosphoserine Ref.11 Ref.17
	Modified residue	1552	1	Phosphoserine Ref.17
	Modified residue	1575	1	Phosphothreonine Ref.16
	Modified residue	1576	1	Phosphoserine Ref.17
	Modified residue	1581	1	Phosphoserine Ref.16 Ref.17
	Modified residue	1592	1	Phosphothreonine Ref.17
	Modified residue	1596	1	Phosphoserine Ref.17
	Modified residue	1609	1	Phosphotyrosine Ref.17
	Modified residue	1613	1	Phosphoserine Ref.17
Natural variations
	Alternative sequence	24 – 28	5	Missing in isoform Beta-1.		VSP_006532
Experimental info
	Sequence conflict	1431	1	T → S in CAA78821. Ref.4
	Sequence conflict	1431	1	T → S in CAA09753. Ref.4
	Sequence conflict	1611	1	A → T in CAA48197. Ref.1
	Sequence conflict	1621	1	D → H in CAA09753. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform Beta-2 [UniParc]. Last modified January 31, 2002. Version 3. Checksum: E60E9262CC68B05D	FASTA	1,626	183,267
	10 20 30 40 50 60 MAKSGGCGAG AGVGGGNGAL TWVTLFDQNN AAKKEESETA NKNDSSKKLS VERVYQKKTQ 70 80 90 100 110 120 LEHILLRPDT YIGSVEPLTQ FMWVYDEDVG MNCREVTFVP GLYKIFDEIL VNAADNKQRD 130 140 150 160 170 180 KNMTCIKVSI DPESNIISIW NNGKGIPVVE HKVEKVYVPA LIFGQLLTSS NYDDDEKKVT 190 200 210 220 230 240 GGRNGYGAKL CNIFSTKFTV ETACKEYKHS FKQTWMNNMM KTSEAKIKHF DGEDYTCITF 250 260 270 280 290 300 QPDLSKFKME KLDKDIVALM TRRAYDLAGS CRGVKVMFNG KKLPVNGFRS YVDLYVKDKL 310 320 330 340 350 360 DETGVALKVI HELANERWDV CLTLSEKGFQ QISFVNSIAT TKGGRHVDYV VDQVVGKLIE 370 380 390 400 410 420 VVKKKNKAGV SVKPFQVKNH IWVFINCLIE NPTFDSQTKE NMTLQPKSFG SKCQLSEKFF 430 440 450 460 470 480 KAASNCGIVE SILNWVKFKA QTQLNKKCSS VKYSKIKGIP KLDDANDAGG KHSLECTLIL 490 500 510 520 530 540 TEGDSAKSLA VSGLGVIGRD RYGVFPLRGK ILNVREASHK QIMENAEINN IIKIVGLQYK 550 560 570 580 590 600 KSYDDAESLK TLRYGKIMIM TDQDQDGSHI KGLLINFIHH NWPSLLKHGF LEEFITPIVK 610 620 630 640 650 660 ASKNKQELSF YSIPEFDEWK KHIENQKAWK IKYYKGLGTS TAKEAKEYFA DMERHRILFR 670 680 690 700 710 720 YAGPEDDAAI TLAFSKKKID DRKEWLTNFM EDRRQRRLHG LPEQFLYGTA TKHLTYNDFI 730 740 750 760 770 780 NKELILFSNS DNERSIPSLV DGFKPGQRKV LFTCFKRNDK REVKVAQLAG SVAEMSAYHH 790 800 810 820 830 840 GEQALMMTIV NLAQNFVGSN NINLLQPIGQ FGTRLHGGKD AASPRYIFTM LSTLARLLFP 850 860 870 880 890 900 AVDDNLLKFL YDDNQRVEPE WYIPIIPMVL INGAEGIGTG WACKLPNYDA REIVNNVRRM 910 920 930 940 950 960 LDGLDPHPML PNYKNFKGTI QELGQNQYAV SGEIFVVDRN TVEITELPVR TWTQVYKEQV 970 980 990 1000 1010 1020 LEPMLNGTDK TPALISDYKE YHTDTTVKFV VKMTEEKLAQ AEAAGLHKVF KLQTTLTCNS 1030 1040 1050 1060 1070 1080 MVLFDHMGCL KKYETVQDIL KEFFDLRLSY YGLRKEWLVG MLGAESTKLN NQARFILEKI 1090 1100 1110 1120 1130 1140 QGKITIENRS KKDLIQMLVQ RGYESDPVKA WKEAQEKAAE EDETQNQHDD SSSDSGTPSG 1150 1160 1170 1180 1190 1200 PDFNYILNMS LWSLTKEKVE ELIKQRDAKG REVNDLKRKS PSDLWKEDLA AFVEELDKVE 1210 1220 1230 1240 1250 1260 SQEREDVLAG MSGKAIKGKV GKPKVKKLQL EETMPSPYGR RIIPEITAMK ADASKKLLKK 1270 1280 1290 1300 1310 1320 KKGDLDTAAV KVEFDEEFSG APVEGAGEEA LTPSVPINKG PKPKREKKEP GTRVRKTPTS 1330 1340 1350 1360 1370 1380 SGKPSAKKVK KRNPWSDDES KSESDLEETE PVVIPRDSLL RRAAAERPKY TFDFSEEEDD 1390 1400 1410 1420 1430 1440 DADDDDDDNN DLEELKVKAS PITNDGEDEF VPSDGLDKDE YTFSPGKSKA TPEKSLHDKK 1450 1460 1470 1480 1490 1500 SQDFGNLFSF PSYSQKSEDD SAKFDSNEED SASVFSPSFG LKQTDKVPSK TVAAKKGKPS 1510 1520 1530 1540 1550 1560 SDTVPKPKRA PKQKKVVEAV NSDSDSEFGI PKKTTTPKGK GRGAKKRKAS GSENEGDYNP 1570 1580 1590 1600 1610 1620 GRKTSKTTSK KPKKTSFDQD SDVDIFPSDF PTEPPSLPRT GRARKEVKYF AESDEEEDDV DFAMFN
	Isoform Beta-1. Checksum: B1C091BF539F2391	FASTA	1,621	182,663
	10 20 30 40 50 60 MAKSGGCGAG AGVGGGNGAL TWVNNAAKKE ESETANKNDS SKKLSVERVY QKKTQLEHIL 70 80 90 100 110 120 LRPDTYIGSV EPLTQFMWVY DEDVGMNCRE VTFVPGLYKI FDEILVNAAD NKQRDKNMTC 130 140 150 160 170 180 IKVSIDPESN IISIWNNGKG IPVVEHKVEK VYVPALIFGQ LLTSSNYDDD EKKVTGGRNG 190 200 210 220 230 240 YGAKLCNIFS TKFTVETACK EYKHSFKQTW MNNMMKTSEA KIKHFDGEDY TCITFQPDLS 250 260 270 280 290 300 KFKMEKLDKD IVALMTRRAY DLAGSCRGVK VMFNGKKLPV NGFRSYVDLY VKDKLDETGV 310 320 330 340 350 360 ALKVIHELAN ERWDVCLTLS EKGFQQISFV NSIATTKGGR HVDYVVDQVV GKLIEVVKKK 370 380 390 400 410 420 NKAGVSVKPF QVKNHIWVFI NCLIENPTFD SQTKENMTLQ PKSFGSKCQL SEKFFKAASN 430 440 450 460 470 480 CGIVESILNW VKFKAQTQLN KKCSSVKYSK IKGIPKLDDA NDAGGKHSLE CTLILTEGDS 490 500 510 520 530 540 AKSLAVSGLG VIGRDRYGVF PLRGKILNVR EASHKQIMEN AEINNIIKIV GLQYKKSYDD 550 560 570 580 590 600 AESLKTLRYG KIMIMTDQDQ DGSHIKGLLI NFIHHNWPSL LKHGFLEEFI TPIVKASKNK 610 620 630 640 650 660 QELSFYSIPE FDEWKKHIEN QKAWKIKYYK GLGTSTAKEA KEYFADMERH RILFRYAGPE 670 680 690 700 710 720 DDAAITLAFS KKKIDDRKEW LTNFMEDRRQ RRLHGLPEQF LYGTATKHLT YNDFINKELI 730 740 750 760 770 780 LFSNSDNERS IPSLVDGFKP GQRKVLFTCF KRNDKREVKV AQLAGSVAEM SAYHHGEQAL 790 800 810 820 830 840 MMTIVNLAQN FVGSNNINLL QPIGQFGTRL HGGKDAASPR YIFTMLSTLA RLLFPAVDDN 850 860 870 880 890 900 LLKFLYDDNQ RVEPEWYIPI IPMVLINGAE GIGTGWACKL PNYDAREIVN NVRRMLDGLD 910 920 930 940 950 960 PHPMLPNYKN FKGTIQELGQ NQYAVSGEIF VVDRNTVEIT ELPVRTWTQV YKEQVLEPML 970 980 990 1000 1010 1020 NGTDKTPALI SDYKEYHTDT TVKFVVKMTE EKLAQAEAAG LHKVFKLQTT LTCNSMVLFD 1030 1040 1050 1060 1070 1080 HMGCLKKYET VQDILKEFFD LRLSYYGLRK EWLVGMLGAE STKLNNQARF ILEKIQGKIT 1090 1100 1110 1120 1130 1140 IENRSKKDLI QMLVQRGYES DPVKAWKEAQ EKAAEEDETQ NQHDDSSSDS GTPSGPDFNY 1150 1160 1170 1180 1190 1200 ILNMSLWSLT KEKVEELIKQ RDAKGREVND LKRKSPSDLW KEDLAAFVEE LDKVESQERE 1210 1220 1230 1240 1250 1260 DVLAGMSGKA IKGKVGKPKV KKLQLEETMP SPYGRRIIPE ITAMKADASK KLLKKKKGDL 1270 1280 1290 1300 1310 1320 DTAAVKVEFD EEFSGAPVEG AGEEALTPSV PINKGPKPKR EKKEPGTRVR KTPTSSGKPS 1330 1340 1350 1360 1370 1380 AKKVKKRNPW SDDESKSESD LEETEPVVIP RDSLLRRAAA ERPKYTFDFS EEEDDDADDD 1390 1400 1410 1420 1430 1440 DDDNNDLEEL KVKASPITND GEDEFVPSDG LDKDEYTFSP GKSKATPEKS LHDKKSQDFG 1450 1460 1470 1480 1490 1500 NLFSFPSYSQ KSEDDSAKFD SNEEDSASVF SPSFGLKQTD KVPSKTVAAK KGKPSSDTVP 1510 1520 1530 1540 1550 1560 KPKRAPKQKK VVEAVNSDSD SEFGIPKKTT TPKGKGRGAK KRKASGSENE GDYNPGRKTS 1570 1580 1590 1600 1610 1620 KTTSKKPKKT SFDQDSDVDI FPSDFPTEPP SLPRTGRARK EVKYFAESDE EEDDVDFAMF N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of cDNA clones encoding the beta isozyme of human DNA topoisomerase II and localisation of the gene to chromosome 3p24." Jenkins J.R., Ayton P., Jones T., Davies S.L., Simmons D.L., Harris A.L., Sheer D., Hickson I.D. Nucleic Acids Res. 20:5587-5592(1992) [PubMed: 1333583] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Novel HeLa topoisomerase II is the II beta isoform: complete coding sequence and homology with other type II topoisomerases." Austin C.A., Sng J.H., Patel S., Fisher L.M. Biochim. Biophys. Acta 1172:283-291(1993) [PubMed: 8383537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Characterization and immunological identification of cDNA clones encoding two human DNA topoisomerase II isozymes." Chung T.D., Drake F.H., Tan K.B., Per S.R., Crooke S.T., Mirabelli C.K. Proc. Natl. Acad. Sci. U.S.A. 86:9431-9435(1989) [PubMed: 2556712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 149-1034.
[4]	"Molecular cloning and characterization of the human topoisomerase IIalpha and IIbeta genes: evidence for isoform evolution through gene duplication." Sng J.H., Heaton V.J., Bell M., Mani P., Austin C.A., Fisher L.M. Biochim. Biophys. Acta 1444:395-406(1999) [PubMed: 10095062] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 910-1626.
[5]	"Isolation and characterization of a human cDNA clone encoding a novel DNA topoisomerase II homologue from HeLa cells." Austin C.A., Fisher L.M. FEBS Lett. 266:115-117(1990) [PubMed: 2163884] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1038-1271.
[6]	"Binding of wild-type p53 by topoisomerase II and overexpression of topoisomerase II in human hepatocellular carcinoma." Yuwen H., Hsia C.C., Nakashima Y., Evangelista A., Tabor E. Biochem. Biophys. Res. Commun. 234:194-197(1997) [PubMed: 9168988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1277-1626.
[7]	"Human cells express two differentially spliced forms of topoisomerase II beta mRNA." Davies S.L., Jenkins J.R., Hickson I.D. Nucleic Acids Res. 21:3719-3723(1993) [PubMed: 8396237] [Abstract] Cited for: ALTERNATIVE SPLICING.
[8]	"Identification of functional nuclear export sequences in human topoisomerase IIalpha and beta." Mirski S.E., Bielawski J.C., Cole S.P. Biochem. Biophys. Res. Commun. 306:905-911(2003) [PubMed: 12821127] [Abstract] Cited for: NUCLEAR EXPORT SIGNAL.
[9]	"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome." Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S. Cell 113:905-917(2003) [PubMed: 12837248] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[10]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1466 AND SER-1522, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-639; SER-640; SER-1336; SER-1340; SER-1342; SER-1344; SER-1400; SER-1413; SER-1522; SER-1524 AND SER-1550, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1471; SER-1522 AND SER-1524, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1522 AND SER-1524, MASS SPECTROMETRY.
[14]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1236, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454, MASS SPECTROMETRY.
[16]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1413; SER-1424; THR-1575 AND SER-1581, MASS SPECTROMETRY.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1236; SER-1336; SER-1340; SER-1342; SER-1344; SER-1375; SER-1400; SER-1413; TYR-1421; SER-1424; SER-1466; SER-1522; SER-1524; SER-1526; SER-1550; SER-1552; SER-1576; SER-1581; THR-1592; SER-1596; TYR-1609 AND SER-1613, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X68060 mRNA. Translation: CAA48197.1. X71911 Genomic DNA. No translation available. Z15111 mRNA. Translation: CAA78815.1. Z15115 mRNA. Translation: CAA78821.1. M27504 mRNA. Translation: AAA61210.1. AJ011721 , AJ011722, AJ011723, AJ011724, AJ011725, AJ011726, AJ011727, AJ011728, AJ011729, AJ011730, AJ011731, AJ011732 Genomic DNA. Translation: CAA09753.1. X53662 mRNA. Translation: CAA37706.1. U54831 mRNA. Translation: AAB01982.1.
IPI	IPI00027280. IPI00217709.
PIR	A39242. S26730.
RefSeq	NP_001059.2.
UniGene	Hs.475733
3D structure databases
HSSP	HSSP built from PDB template 1BJT based on UniProtKB P06786.
SMR	Q02880. Positions 50-426.
ModBase	Search...
PTM databases
PhosphoSite	Q02880.
Proteomic databases
PRIDE	Q02880.
Genome annotation databases
Ensembl	ENSG00000077097. Homo sapiens. [Contig view]
GeneID	7155.
KEGG	hsa:7155.
NMPDR	fig|9606.3.peg.22225.
Organism-specific databases
GeneCards	GC03M025614.
H-InvDB	HIX0030807.
HGNC	HGNC:11990. TOP2B.
HPA	CAB004601.
MIM	126431. gene.
PharmGKB	PA36672.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q02880.
HOVERGEN	Q02880.
OMA	Q02880. GAESTKL.
Enzyme and pathway databases
BRENDA	5.99.1.3. 247.
Gene expression databases
ArrayExpress	Q02880.
Bgee	Q02880.
CleanEx	HS_TOP2B.
GermOnline	ENSG00000077097. Homo sapiens.
Family and domain databases
InterPro	IPR003594. ATP_bd_ATPase. IPR012542. DTHCT. IPR002205. Topo_IIA_A/C. IPR013758. Topo_IIA_A/C_ab. IPR013757. Topo_IIA_A_a. IPR001241. Topo_IIA_B/N. IPR013759. Topo_IIA_B/N_ab. IPR013506. Topo_IIA_B_2. IPR018522. TopoIIA_CS. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit. G3DSA:3.90.199.10. Topo_IIA_A/C_ab. 1 hit. G3DSA:1.10.268.10. Topo_IIA_A_a. 1 hit. G3DSA:3.40.50.670. Topo_IIA_B/N_ab. 1 hit.
Pfam	PF00204. DNA_gyraseB. 1 hit. PF00521. DNA_topoisoIV. 1 hit. PF08070. DTHCT. 1 hit. PF02518. HATPase_c. 1 hit. [Graphical view]
PRINTS	PR00418. TPI2FAMILY.
ProDom	PD149633. DNA_gyrase_B. 1 hit. PD000742. DNA_topoisoIV. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00387. HATPase_c. 1 hit. SM00433. TOP2c. 1 hit. SM00434. TOP4c. 1 hit. [Graphical view]
PROSITE	PS00177. TOPOISOMERASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	27998.
SOURCE	Search...

Entry information

Entry name

TOP2B_HUMAN

Accession

Primary (citable) accession number: Q02880
Secondary accession number(s): Q13600, Q9UMG8, Q9UQP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 31, 2002
Last modified:	June 16, 2009
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)