Q02880 (TOP2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1626 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. Ref.8 Ref.10
Catalytic activity	ATP-dependent breakage, passage and rejoining of double-stranded DNA. Ref.8
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+. Ref.8 Ref.22
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. Ref.10 Ref.22
Subcellular location	Cytoplasm. 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	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding DNA-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA topological change Inferred from direct assay Ref.8. Source: UniProtKB DNA-dependent DNA replication Inferred from Biological aspect of Ancestor. Source: RefGenome axonogenesis Inferred from electronic annotation. Source: Compara forebrain development Inferred from electronic annotation. Source: Compara mitotic recombination Inferred from Biological aspect of Ancestor. Source: RefGenome neuron migration Inferred from electronic annotation. Source: Compara 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 direct assay Ref.10. Source: BHF-UCL cytosol Inferred from direct assay PubMed 9049244. Source: UniProtKB nucleoplasm Inferred from direct assay PubMed 9049244. Source: UniProtKB 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 direct assay Ref.8. Source: UniProtKB chromatin binding Inferred from direct assay PubMed 9049244. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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

Domain

476 – 593

118

Toprim

Nucleotide binding

169 – 171

3

ATP By similarity

Nucleotide binding

182 – 189

8

ATP By similarity

Nucleotide binding

397 – 399

3

ATP By similarity

Region

363 – 365

3

Interaction with DNA By similarity

Region

1011 – 1020

10

Interaction with DNA

Motif

1034 – 1044

11

Nuclear export signal

Sites

Active site

826

1

O-(5'-phospho-DNA)-tyrosine intermediate Ref.22

Metal binding

482

1

Magnesium 1; catalytic By similarity

Metal binding

562

1

Magnesium 1; catalytic By similarity

Metal binding

562

1

Magnesium 2

Metal binding

564

1

Magnesium 2

Binding site

112

1

ATP By similarity

Binding site

141

1

ATP By similarity

Site

510

1

Interaction with DNA

Site

513

1

Interaction with DNA

Site

682

1

Interaction with DNA

Site

683

1

Interaction with DNA

Site

744

1

Interaction with DNA

Site

778

1

Interaction with DNA By similarity

Site

825

1

Transition state stabilizer

Site

877

1

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

Site

952

1

Interaction with DNA

Amino acid modifications

Modified residue

431

1

Phosphoserine By similarity

Modified residue

639

1

Phosphothreonine By similarity

Modified residue

1236

1

Phosphoserine Ref.18 Ref.19

Modified residue

1292

1

Phosphothreonine Ref.18

Modified residue

1336

1

Phosphoserine Ref.11 Ref.17 Ref.19 Ref.21

Modified residue

1340

1

Phosphoserine Ref.11 Ref.17 Ref.19 Ref.21

Modified residue

1342

1

Phosphoserine Ref.17 Ref.18 Ref.19 Ref.21

Modified residue

1344

1

Phosphoserine Ref.17 Ref.18 Ref.19 Ref.21

Modified residue

1358

1

Phosphoserine Ref.21

Modified residue

1375

1

Phosphoserine Ref.17 Ref.18

Modified residue

1400

1

Phosphoserine Ref.11 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21

Modified residue

1403

1

Phosphothreonine Ref.18

Modified residue

1413

1

Phosphoserine Ref.11 Ref.15 Ref.17 Ref.18 Ref.19 Ref.21

Modified residue

1421

1

Phosphotyrosine Ref.17

Modified residue

1424

1

Phosphoserine Ref.17 Ref.18 Ref.19 Ref.21

Modified residue

1441

1

Phosphoserine Ref.19 Ref.21

Modified residue

1452

1

Phosphoserine Ref.19

Modified residue

1454

1

Phosphoserine Ref.14 Ref.19 Ref.21

Modified residue

1461

1

Phosphoserine Ref.18

Modified residue

1466

1

Phosphoserine Ref.17 Ref.18 Ref.19 Ref.21

Modified residue

1473

1

Phosphoserine Ref.18

Modified residue

1476

1

Phosphoserine Ref.18 Ref.19

Modified residue

1522

1

Phosphoserine Ref.18 Ref.19 Ref.21

Modified residue

1524

1

Phosphoserine Ref.18 Ref.19 Ref.21

Modified residue

1526

1

Phosphoserine Ref.18 Ref.19

Modified residue

1550

1

Phosphoserine Ref.17 Ref.21

Modified residue

1552

1

Phosphoserine Ref.17

Modified residue

1575

1

Phosphothreonine Ref.18

Modified residue

1581

1

Phosphoserine Ref.15 Ref.17 Ref.18 Ref.21

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 Ref.19 Ref.21

Natural variations

Alternative sequence

24 – 28

5

Missing in isoform Beta-1.

VSP_006532

Experimental info

Mutagenesis

482

1

E → Q: Strongly reduced enzyme activity. Ref.8

Mutagenesis

485

1

S → A: Slightly reduced enzyme activity. Ref.8

Mutagenesis

508

1

R → E: Slightly reduced enzyme activity. Ref.8

Mutagenesis

510

1

K → E: Strongly reduced enzyme activity. Ref.8

Mutagenesis

515

1

R → Q: Slightly reduced enzyme activity. Ref.8

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

Secondary structure

1

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1626

Helix Strand Turn

Details...

Turn

466 – 469

4

Helix

473 – 475

3

Beta strand

477 – 482

6

Helix

483 – 491

9

Helix

497 – 499

3

Beta strand

502 – 507

6

Helix

519 – 524

6

Helix

526 – 535

10

Helix

548 – 551

4

Beta strand

555 – 560

6

Helix

565 – 581

17

Helix

583 – 587

5

Beta strand

591 – 594

4

Helix

644 – 650

7

Helix

652 – 655

4

Beta strand

656 – 660

5

Helix

664 – 674

11

Helix

676 – 678

3

Helix

679 – 698

20

Beta strand

713 – 715

3

Helix

716 – 722

7

Helix

724 – 735

12

Turn

739 – 741

3

Helix

745 – 757

13

Helix

765 – 776

12

Helix

782 – 793

12

Turn

814 – 820

7

Helix

835 – 838

4

Helix

841 – 844

4

Beta strand

849 – 852

4

Beta strand

855 – 860

6

Helix

868 – 871

4

Beta strand

875 – 877

3

Beta strand

882 – 884

3

Helix

890 – 901

12

Beta strand

918 – 924

7

Beta strand

927 – 931

5

Beta strand

933 – 938

6

Beta strand

941 – 946

6

Helix

953 – 959

7

Helix

961 – 966

6

Beta strand

969 – 971

3

Beta strand

976 – 980

5

Beta strand

989 – 992

4

Helix

995 – 1004

10

Helix

1006 – 1009

4

Beta strand

1013 – 1017

5

Beta strand

1021 – 1024

4

Beta strand

1030 – 1034

5

Helix

1036 – 1080

45

Helix

1091 – 1100

10

Helix

1107 – 1114

8

Helix

1144 – 1147

4

Helix

1151 – 1154

4

Helix

1156 – 1177

22

Helix

1181 – 1205

25

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 [UniParc]. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[8]	"Mutagenesis of E477 or K505 in the B' domain of human topoisomerase II beta increases the requirement for magnesium ions during strand passage." West K.L., Meczes E.L., Thorn R., Turnbull R.M., Marshall R., Austin C.A. Biochemistry 39:1223-1233(2000) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-482; SER-485; ARG-508; LYS-510 AND ARG-515.
[9]	"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] [Europe PMC] [Abstract] Cited for: NUCLEAR EXPORT SIGNAL.
[10]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336; SER-1340; SER-1400 AND SER-1413, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Prostate cancer.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1400; SER-1413 AND SER-1581, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: T-cell.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336; SER-1340; SER-1342; SER-1344; SER-1375; SER-1400; SER-1413; TYR-1421; SER-1424; SER-1466; SER-1550; SER-1552; SER-1581; THR-1592; SER-1596; TYR-1609 AND SER-1613, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1236; THR-1292; SER-1342; SER-1344; SER-1375; SER-1400; THR-1403; SER-1413; SER-1424; SER-1461; SER-1466; SER-1473; SER-1476; SER-1522; SER-1524; SER-1526; THR-1575 AND SER-1581, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1236; SER-1336; SER-1340; SER-1342; SER-1344; SER-1400; SER-1413; SER-1424; SER-1441; SER-1452; SER-1454; SER-1466; SER-1476; SER-1522; SER-1524; SER-1526 AND SER-1613, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1336; SER-1340; SER-1342; SER-1344; SER-1358; SER-1400; SER-1413; SER-1424; SER-1441; SER-1454; SER-1466; SER-1522; SER-1524; SER-1550; SER-1581 AND SER-1613, MASS SPECTROMETRY.
[22]	"Structural basis of type II topoisomerase inhibition by the anticancer drug etoposide." Wu C.C., Li T.K., Farh L., Lin L.Y., Lin T.S., Yu Y.J., Yen T.J., Chiang C.W., Chan N.L. Science 333:459-462(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 450-1206 IN COMPLEX WITH DNA; MAGNESIUM AND ETOPOSIDE, ACTIVE SITE, COFACTOR, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_001068.3.

UniGene

Hs.475733.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QX3	X-ray	2.16	A/B	450-1206	[»]

ProteinModelPortal

Q02880.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q02880. 4 interactions.

STRING

9606.ENSP00000396704.

PTM databases

PhosphoSite

Q02880.

Polymorphism databases

DMDM

20141946.

Proteomic databases

PaxDb

Q02880.

PRIDE

Q02880.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264331; ENSP00000264331; ENSG00000077097.
ENST00000435706; ENSP00000396704; ENSG00000077097.

GeneID

7155.

KEGG

hsa:7155.

UCSC

uc003cdj.2. human.
uc011awn.1. human.

Organism-specific databases

CTD

7155.

GeneCards

GC03M025639.

H-InvDB

HIX0030807.

HGNC

HGNC:11990. TOP2B.

HPA

CAB004601.
HPA024120.

MIM

126431. gene.

neXtProt

NX_Q02880.

PharmGKB

PA36672.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0187.

HOGENOM

HOG000216693.

HOVERGEN

HBG052998.

InParanoid

Q02880.

KO

K03164.

OMA

AKEYFQD.

PhylomeDB

Q02880.

Gene expression databases

ArrayExpress

Q02880.

Bgee

Q02880.

CleanEx

HS_TOP2B.

Genevestigator

Q02880.

GermOnline

ENSG00000077097. Homo sapiens.

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

Q02880.

ChEMBL

CHEMBL3396.

ChiTaRS

TOP2B. human.

GenomeRNAi

7155.

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:	May 1, 2013
This is version 149 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.