P11388 (TOP2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA topoisomerase 2-alpha
EC=5.99.1.3

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

Gene names

Name:	TOP2A
Synonyms:	TOP2

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	1531 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. Essential during mitosis and meiosis for proper segregation of daughter chromosomes. Ref.30
Catalytic activity	ATP-dependent breakage, passage and rejoining of double-stranded DNA. Ref.22 Ref.23
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+ Probable. Ref.22 Ref.23 Ref.30 Ref.32
Enzyme regulation	Specifically inhibited by the intercalating agent amsacrine.
Subunit structure	Homodimer. Interacts with COPS5. Ref.14 Ref.32
Subcellular location	Cytoplasm. Nucleus › nucleoplasm. Note: Generally located in the nucleoplasm.
Post-translational modification	Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable complex formation.
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 Polymorphism
Ligand	ATP-binding DNA-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA ligation Inferred from direct assay PubMed 15491148. Source: UniProtKB DNA repair Non-traceable author statement PubMed 15504738. Source: UniProtKB DNA topological change Inferred from direct assay Ref.30. Source: UniProtKB DNA-dependent DNA replication Inferred from Biological aspect of Ancestor. Source: RefGenome apoptotic chromosome condensation Inferred from direct assay PubMed 10959840. Source: UniProtKB embryonic cleavage Inferred from electronic annotation. Source: Compara mitotic cell cycle Traceable author statement. Source: Reactome mitotic recombination Inferred from Biological aspect of Ancestor. Source: RefGenome phosphatidylinositol-mediated signaling Non-traceable author statement PubMed 15504738. Source: UniProtKB positive regulation of apoptotic process Inferred from direct assay PubMed 16611985. Source: UniProtKB positive regulation of retroviral genome replication Inferred from mutant phenotype PubMed 16712776. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter 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	DNA topoisomerase complex (ATP-hydrolyzing) Inferred from direct assay PubMed 10473615. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from direct assay PubMed 17567603. 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 binding, bending Inferred from direct assay Ref.30. Source: UniProtKB DNA topoisomerase type II (ATP-hydrolyzing) activity Inferred from direct assay PubMed 16611985. Source: UniProtKB chromatin binding Inferred from direct assay PubMed 9049244. Source: UniProtKB drug binding Inferred from direct assay PubMed 16914642. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.30. Source: UniProtKB ubiquitin binding Inferred from mutant phenotype PubMed 15965487. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CTNNB1	P35222	5	EBI-539628,EBI-491549

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P11388-1)

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 2 (identifier: P11388-2)

The sequence of this isoform differs from the canonical sequence as follows:
     401-401: A → AHLYSRFLIDPFFPNMIPNMIFSFSKA

Isoform 3 (identifier: P11388-3)

The sequence of this isoform differs from the canonical sequence as follows:
     321-321: K → KSSKYWSSRKSKQHILLNFFVLFKFINDAFFGICPFK

Isoform 4 (identifier: P11388-4)

The sequence of this isoform differs from the canonical sequence as follows:
     355-355: Q → QRELCNGAIL...SQSSGITDVK

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1531

1531

DNA topoisomerase 2-alpha

PRO_0000145363

Regions

Domain

455 – 572

118

Toprim

Nucleotide binding

148 – 150

3

ATP

Nucleotide binding

161 – 168

8

ATP

Nucleotide binding

376 – 378

3

ATP

Region

342 – 344

3

Interaction with DNA Probable

Region

990 – 999

10

Interaction with DNA

Motif

1018 – 1028

11

Nuclear export signal

Sites

Active site

805

1

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

Metal binding

461

1

Magnesium 1; catalytic By similarity

Metal binding

541

1

Magnesium 1; catalytic By similarity

Metal binding

541

1

Magnesium 2

Metal binding

543

1

Magnesium 2

Binding site

91

1

ATP

Binding site

120

1

ATP

Site

489

1

Interaction with DNA By similarity

Site

492

1

Interaction with DNA

Site

661

1

Interaction with DNA

Site

662

1

Interaction with DNA

Site

723

1

Interaction with DNA

Site

757

1

Interaction with DNA

Site

763

1

Interaction with DNA

Site

804

1

Transition state stabilizer By similarity

Site

856

1

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

Site

931

1

Interaction with DNA

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.10 Ref.26 Ref.28

Modified residue

4

1

Phosphoserine Ref.15 Ref.20 Ref.26 Ref.28

Modified residue

29

1

Phosphoserine Ref.15

Modified residue

282

1

Phosphothreonine Ref.26

Modified residue

1106

1

Phosphoserine; by CK1 Ref.11 Ref.15 Ref.21 Ref.24 Ref.26 Ref.28

Modified residue

1205

1

Phosphothreonine Ref.26

Modified residue

1213

1

Phosphoserine Ref.15 Ref.16 Ref.20 Ref.21 Ref.26 Ref.28

Modified residue

1247

1

Phosphoserine Ref.15 Ref.17 Ref.20 Ref.25 Ref.26 Ref.28

Modified residue

1295

1

Phosphoserine Ref.28

Modified residue

1297

1

Phosphoserine Ref.28

Modified residue

1299

1

Phosphoserine Ref.28

Modified residue

1302

1

Phosphoserine Ref.28

Modified residue

1332

1

Phosphoserine Ref.15 Ref.20 Ref.21 Ref.26 Ref.28

Modified residue

1337

1

Phosphoserine Ref.15 Ref.20 Ref.21 Ref.26 Ref.28

Modified residue

1343

1

Phosphothreonine; by PLK3 Ref.15 Ref.18 Ref.21 Ref.26 Ref.28

Modified residue

1351

1

Phosphoserine Ref.15 Ref.21 Ref.26 Ref.28

Modified residue

1354

1

Phosphoserine Ref.15 Ref.26 Ref.28

Modified residue

1374

1

Phosphoserine Ref.15 Ref.16 Ref.25 Ref.26 Ref.28

Modified residue

1377

1

Phosphoserine Ref.15 Ref.16 Ref.20 Ref.26 Ref.28

Modified residue

1387

1

Phosphoserine Ref.25

Modified residue

1392

1

Phosphoserine Ref.21

Modified residue

1393

1

Phosphoserine Ref.21 Ref.25

Modified residue

1449

1

Phosphoserine Ref.21

Modified residue

1469

1

Phosphoserine; by CK2 Ref.12 Ref.21 Ref.28

Modified residue

1470

1

Phosphothreonine Ref.21 Ref.28

Modified residue

1471

1

Phosphoserine Ref.21 Ref.26 Ref.28

Modified residue

1474

1

Phosphoserine Ref.21 Ref.26 Ref.28

Modified residue

1476

1

Phosphoserine Ref.28

Modified residue

1495

1

Phosphoserine Ref.26

Modified residue

1504

1

Phosphoserine Ref.19 Ref.25 Ref.26

Modified residue

1525

1

Phosphoserine Ref.15 Ref.16 Ref.21 Ref.25 Ref.26 Ref.28

Natural variations

Alternative sequence

321

1

K → KSSKYWSSRKSKQHILLNFF VLFKFINDAFFGICPFK in isoform 3.

VSP_006529

Alternative sequence

355

1

Q → QRELCNGAILAHCNLRLMGS SDSPASASRVAGIAGGCHHT QLIFVFLVETGFHHVGQAGL ERLTSGDPPASASQSSGITD VK in isoform 4.

VSP_006530

Alternative sequence

401

1

A → AHLYSRFLIDPFFPNMIPNM IFSFSKA in isoform 2.

VSP_006531

Natural variant

450

1

R → Q in teniposide (VM-26) resistant cells. Ref.34

VAR_007532

Natural variant

487

1

R → K in amsacrine resistant cells. Ref.33

VAR_007533

Natural variant

1324

1

T → K.
Corresponds to variant rs28969502 [ dbSNP | Ensembl ].

VAR_029245

Natural variant

1386

1

G → D.
Corresponds to variant rs34300454 [ dbSNP | Ensembl ].

VAR_052594

Natural variant

1515

1

A → S.
Corresponds to variant rs11540720 [ dbSNP | Ensembl ].

VAR_052595

Experimental info

Mutagenesis

342 – 344

3

KKK → AAA: Reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. Ref.29

Mutagenesis

342 – 344

3

KKK → EEE: Strongly reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. Ref.29

Mutagenesis

461

1

E → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. Ref.23 Ref.30

Mutagenesis

541

1

D → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. Ref.23 Ref.30

Mutagenesis

543

1

D → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. Ref.23 Ref.30

Mutagenesis

545

1

D → A or C: Strongly reduced DNA cleavage. Ref.23

Mutagenesis

1469

1

S → A: Abolishes binding to the antibody MPM2. Ref.12

Sequence conflict

152

1

D → H in CAA09762. Ref.4

Sequence conflict

180

1

E → Q in CAA09762. Ref.4

Sequence conflict

327

1

D → H in CAA09762. Ref.4

Sequence conflict

1022

1

F → L in CAA09762. Ref.4

Sequence conflict

1274

1

T → S in CAA09762. Ref.4

Sequence conflict

1295

1

S → P in AAA61209. Ref.1

Secondary structure

1

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1531

Helix Strand Turn

Details...

Helix

30 – 33

4

Beta strand

34 – 36

3

Helix

39 – 45

7

Helix

48 – 51

4

Beta strand

57 – 65

9

Turn

66 – 68

3

Beta strand

69 – 77

9

Helix

79 – 98

20

Beta strand

104 – 110

7

Turn

111 – 114

4

Beta strand

115 – 123

9

Beta strand

128 – 130

3

Turn

131 – 134

4

Helix

137 – 143

7

Beta strand

144 – 149

6

Helix

153 – 155

3

Helix

166 – 172

7

Beta strand

174 – 183

10

Turn

184 – 187

4

Beta strand

188 – 195

8

Turn

196 – 199

4

Beta strand

205 – 208

4

Beta strand

214 – 221

8

Helix

223 – 226

4

Helix

233 – 249

17

Beta strand

250 – 252

3

Beta strand

254 – 257

4

Helix

267 – 275

9

Beta strand

281 – 285

5

Beta strand

289 – 294

6

Beta strand

297 – 303

7

Beta strand

305 – 307

3

Beta strand

309 – 314

6

Helix

324 – 341

18

Helix

353 – 357

5

Beta strand

360 – 366

7

Beta strand

373 – 375

3

Helix

385 – 387

3

Beta strand

388 – 390

3

Helix

396 – 402

7

Helix

411 – 415

5

Beta strand

419 – 421

3

Turn

445 – 448

4

Helix

452 – 454

3

Beta strand

456 – 462

7

Helix

463 – 476

14

Beta strand

478 – 486

9

Helix

498 – 503

6

Helix

505 – 514

10

Beta strand

518 – 520

3

Helix

525 – 530

6

Beta strand

534 – 539

6

Helix

544 – 560

17

Helix

562 – 566

5

Beta strand

570 – 573

4

Beta strand

577 – 581

5

Beta strand

586 – 590

5

Helix

592 – 601

10

Beta strand

607 – 612

6

Helix

616 – 618

3

Helix

621 – 629

9

Helix

631 – 634

4

Beta strand

635 – 639

5

Helix

644 – 653

10

Helix

658 – 678

21

Beta strand

685 – 688

4

Beta strand

691 – 694

4

Helix

695 – 701

7

Helix

703 – 714

12

Turn

718 – 720

3

Helix

724 – 735

12

Helix

744 – 754

11

Helix

762 – 772

11

Turn

793 – 799

7

Turn

803 – 805

3

Helix

812 – 817

6

Helix

822 – 824

3

Helix

831 – 833

3

Turn

848 – 850

3

Beta strand

853 – 856

4

Beta strand

861 – 864

4

Helix

869 – 881

13

Beta strand

897 – 903

7

Beta strand

906 – 910

5

Beta strand

921 – 923

3

Helix

932 – 938

7

Helix

940 – 944

5

Beta strand

948 – 950

3

Beta strand

955 – 959

5

Beta strand

968 – 971

4

Helix

974 – 983

10

Helix

985 – 988

4

Beta strand

992 – 996

5

Beta strand

1000 – 1003

4

Beta strand

1009 – 1011

3

Helix

1015 – 1059

45

Helix

1070 – 1080

11

Helix

1086 – 1091

6

Helix

1126 – 1129

4

Helix

1138 – 1160

23

Helix

1163 – 1189

27

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 4, 2001. Version 3. Checksum: 3DF40BC9E84789DC	FASTA	1,531	174,385
	10 20 30 40 50 60 MEVSPLQPVN ENMQVNKIKK NEDAKKRLSV ERIYQKKTQL EHILLRPDTY IGSVELVTQQ 70 80 90 100 110 120 MWVYDEDVGI NYREVTFVPG LYKIFDEILV NAADNKQRDP KMSCIRVTID PENNLISIWN 130 140 150 160 170 180 NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE 190 200 210 220 230 240 TASREYKKMF KQTWMDNMGR AGEMELKPFN GEDYTCITFQ PDLSKFKMQS LDKDIVALMV 250 260 270 280 290 300 RRAYDIAGST KDVKVFLNGN KLPVKGFRSY VDMYLKDKLD ETGNSLKVIH EQVNHRWEVC 310 320 330 340 350 360 LTMSEKGFQQ ISFVNSIATS KGGRHVDYVA DQIVTKLVDV VKKKNKGGVA VKAHQVKNHM 370 380 390 400 410 420 WIFVNALIEN PTFDSQTKEN MTLQPKSFGS TCQLSEKFIK AAIGCGIVES ILNWVKFKAQ 430 440 450 460 470 480 VQLNKKCSAV KHNRIKGIPK LDDANDAGGR NSTECTLILT EGDSAKTLAV SGLGVVGRDK 490 500 510 520 530 540 YGVFPLRGKI LNVREASHKQ IMENAEINNI IKIVGLQYKK NYEDEDSLKT LRYGKIMIMT 550 560 570 580 590 600 DQDQDGSHIK GLLINFIHHN WPSLLRHRFL EEFITPIVKV SKNKQEMAFY SLPEFEEWKS 610 620 630 640 650 660 STPNHKKWKV KYYKGLGTST SKEAKEYFAD MKRHRIQFKY SGPEDDAAIS LAFSKKQIDD 670 680 690 700 710 720 RKEWLTNFME DRRQRKLLGL PEDYLYGQTT TYLTYNDFIN KELILFSNSD NERSIPSMVD 730 740 750 760 770 780 GLKPGQRKVL FTCFKRNDKR EVKVAQLAGS VAEMSSYHHG EMSLMMTIIN LAQNFVGSNN 790 800 810 820 830 840 LNLLQPIGQF GTRLHGGKDS ASPRYIFTML SSLARLLFPP KDDHTLKFLY DDNQRVEPEW 850 860 870 880 890 900 YIPIIPMVLI NGAEGIGTGW SCKIPNFDVR EIVNNIRRLM DGEEPLPMLP SYKNFKGTIE 910 920 930 940 950 960 ELAPNQYVIS GEVAILNSTT IEISELPVRT WTQTYKEQVL EPMLNGTEKT PPLITDYREY 970 980 990 1000 1010 1020 HTDTTVKFVV KMTEEKLAEA ERVGLHKVFK LQTSLTCNSM VLFDHVGCLK KYDTVLDILR 1030 1040 1050 1060 1070 1080 DFFELRLKYY GLRKEWLLGM LGAESAKLNN QARFILEKID GKIIIENKPK KELIKVLIQR 1090 1100 1110 1120 1130 1140 GYDSDPVKAW KEAQQKVPDE EENEESDNEK ETEKSDSVTD SGPTFNYLLD MPLWYLTKEK 1150 1160 1170 1180 1190 1200 KDELCRLRNE KEQELDTLKR KSPSDLWKED LATFIEELEA VEAKEKQDEQ VGLPGKGGKA 1210 1220 1230 1240 1250 1260 KGKKTQMAEV LPSPRGQRVI PRITIEMKAE AEKKNKKKIK NENTEGSPQE DGVELEGLKQ 1270 1280 1290 1300 1310 1320 RLEKKQKREP GTKTKKQTTL AFKPIKKGKK RNPWSDSESD RSSDESNFDV PPRETEPRRA 1330 1340 1350 1360 1370 1380 ATKTKFTMDL DSDEDFSDFD EKTDDEDFVP SDASPPKTKT SPKLSNKELK PQKSVVSDLE 1390 1400 1410 1420 1430 1440 ADDVKGSVPL SSSPPATHFP DETEITNPVP KKNVTVKKTA AKSQSSTSTT GAKKRAAPKG 1450 1460 1470 1480 1490 1500 TKRDPALNSG VSQKPDPAKT KNRRKRKPST SDDSDSNFEK IVSKAVTSKK SKGESDDFHM 1510 1520 1530 DFDSAVAPRA KSVRAKKPIK YLEESDEDDL F
	Isoform 2 [UniParc]. Checksum: 4DE312DFAEC443EA	FASTA	1,557	177,501
	10 20 30 40 50 60 MEVSPLQPVN ENMQVNKIKK NEDAKKRLSV ERIYQKKTQL EHILLRPDTY IGSVELVTQQ 70 80 90 100 110 120 MWVYDEDVGI NYREVTFVPG LYKIFDEILV NAADNKQRDP KMSCIRVTID PENNLISIWN 130 140 150 160 170 180 NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE 190 200 210 220 230 240 TASREYKKMF KQTWMDNMGR AGEMELKPFN GEDYTCITFQ PDLSKFKMQS LDKDIVALMV 250 260 270 280 290 300 RRAYDIAGST KDVKVFLNGN KLPVKGFRSY VDMYLKDKLD ETGNSLKVIH EQVNHRWEVC 310 320 330 340 350 360 LTMSEKGFQQ ISFVNSIATS KGGRHVDYVA DQIVTKLVDV VKKKNKGGVA VKAHQVKNHM 370 380 390 400 410 420 WIFVNALIEN PTFDSQTKEN MTLQPKSFGS TCQLSEKFIK AHLYSRFLID PFFPNMIPNM 430 440 450 460 470 480 IFSFSKAAIG CGIVESILNW VKFKAQVQLN KKCSAVKHNR IKGIPKLDDA NDAGGRNSTE 490 500 510 520 530 540 CTLILTEGDS AKTLAVSGLG VVGRDKYGVF PLRGKILNVR EASHKQIMEN AEINNIIKIV 550 560 570 580 590 600 GLQYKKNYED EDSLKTLRYG KIMIMTDQDQ DGSHIKGLLI NFIHHNWPSL LRHRFLEEFI 610 620 630 640 650 660 TPIVKVSKNK QEMAFYSLPE FEEWKSSTPN HKKWKVKYYK GLGTSTSKEA KEYFADMKRH 670 680 690 700 710 720 RIQFKYSGPE DDAAISLAFS KKQIDDRKEW LTNFMEDRRQ RKLLGLPEDY LYGQTTTYLT 730 740 750 760 770 780 YNDFINKELI LFSNSDNERS IPSMVDGLKP GQRKVLFTCF KRNDKREVKV AQLAGSVAEM 790 800 810 820 830 840 SSYHHGEMSL MMTIINLAQN FVGSNNLNLL QPIGQFGTRL HGGKDSASPR YIFTMLSSLA 850 860 870 880 890 900 RLLFPPKDDH TLKFLYDDNQ RVEPEWYIPI IPMVLINGAE GIGTGWSCKI PNFDVREIVN 910 920 930 940 950 960 NIRRLMDGEE PLPMLPSYKN FKGTIEELAP NQYVISGEVA ILNSTTIEIS ELPVRTWTQT 970 980 990 1000 1010 1020 YKEQVLEPML NGTEKTPPLI TDYREYHTDT TVKFVVKMTE EKLAEAERVG LHKVFKLQTS 1030 1040 1050 1060 1070 1080 LTCNSMVLFD HVGCLKKYDT VLDILRDFFE LRLKYYGLRK EWLLGMLGAE SAKLNNQARF 1090 1100 1110 1120 1130 1140 ILEKIDGKII IENKPKKELI KVLIQRGYDS DPVKAWKEAQ QKVPDEEENE ESDNEKETEK 1150 1160 1170 1180 1190 1200 SDSVTDSGPT FNYLLDMPLW YLTKEKKDEL CRLRNEKEQE LDTLKRKSPS DLWKEDLATF 1210 1220 1230 1240 1250 1260 IEELEAVEAK EKQDEQVGLP GKGGKAKGKK TQMAEVLPSP RGQRVIPRIT IEMKAEAEKK 1270 1280 1290 1300 1310 1320 NKKKIKNENT EGSPQEDGVE LEGLKQRLEK KQKREPGTKT KKQTTLAFKP IKKGKKRNPW 1330 1340 1350 1360 1370 1380 SDSESDRSSD ESNFDVPPRE TEPRRAATKT KFTMDLDSDE DFSDFDEKTD DEDFVPSDAS 1390 1400 1410 1420 1430 1440 PPKTKTSPKL SNKELKPQKS VVSDLEADDV KGSVPLSSSP PATHFPDETE ITNPVPKKNV 1450 1460 1470 1480 1490 1500 TVKKTAAKSQ SSTSTTGAKK RAAPKGTKRD PALNSGVSQK PDPAKTKNRR KRKPSTSDDS 1510 1520 1530 1540 1550 DSNFEKIVSK AVTSKKSKGE SDDFHMDFDS AVAPRAKSVR AKKPIKYLEE SDEDDLF
	Isoform 3 [UniParc]. Checksum: E5322E9ED4DD7BF5	FASTA	1,567	178,712
	10 20 30 40 50 60 MEVSPLQPVN ENMQVNKIKK NEDAKKRLSV ERIYQKKTQL EHILLRPDTY IGSVELVTQQ 70 80 90 100 110 120 MWVYDEDVGI NYREVTFVPG LYKIFDEILV NAADNKQRDP KMSCIRVTID PENNLISIWN 130 140 150 160 170 180 NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE 190 200 210 220 230 240 TASREYKKMF KQTWMDNMGR AGEMELKPFN GEDYTCITFQ PDLSKFKMQS LDKDIVALMV 250 260 270 280 290 300 RRAYDIAGST KDVKVFLNGN KLPVKGFRSY VDMYLKDKLD ETGNSLKVIH EQVNHRWEVC 310 320 330 340 350 360 LTMSEKGFQQ ISFVNSIATS KSSKYWSSRK SKQHILLNFF VLFKFINDAF FGICPFKGGR 370 380 390 400 410 420 HVDYVADQIV TKLVDVVKKK NKGGVAVKAH QVKNHMWIFV NALIENPTFD SQTKENMTLQ 430 440 450 460 470 480 PKSFGSTCQL SEKFIKAAIG CGIVESILNW VKFKAQVQLN KKCSAVKHNR IKGIPKLDDA 490 500 510 520 530 540 NDAGGRNSTE CTLILTEGDS AKTLAVSGLG VVGRDKYGVF PLRGKILNVR EASHKQIMEN 550 560 570 580 590 600 AEINNIIKIV GLQYKKNYED EDSLKTLRYG KIMIMTDQDQ DGSHIKGLLI NFIHHNWPSL 610 620 630 640 650 660 LRHRFLEEFI TPIVKVSKNK QEMAFYSLPE FEEWKSSTPN HKKWKVKYYK GLGTSTSKEA 670 680 690 700 710 720 KEYFADMKRH RIQFKYSGPE DDAAISLAFS KKQIDDRKEW LTNFMEDRRQ RKLLGLPEDY 730 740 750 760 770 780 LYGQTTTYLT YNDFINKELI LFSNSDNERS IPSMVDGLKP GQRKVLFTCF KRNDKREVKV 790 800 810 820 830 840 AQLAGSVAEM SSYHHGEMSL MMTIINLAQN FVGSNNLNLL QPIGQFGTRL HGGKDSASPR 850 860 870 880 890 900 YIFTMLSSLA RLLFPPKDDH TLKFLYDDNQ RVEPEWYIPI IPMVLINGAE GIGTGWSCKI 910 920 930 940 950 960 PNFDVREIVN NIRRLMDGEE PLPMLPSYKN FKGTIEELAP NQYVISGEVA ILNSTTIEIS 970 980 990 1000 1010 1020 ELPVRTWTQT YKEQVLEPML NGTEKTPPLI TDYREYHTDT TVKFVVKMTE EKLAEAERVG 1030 1040 1050 1060 1070 1080 LHKVFKLQTS LTCNSMVLFD HVGCLKKYDT VLDILRDFFE LRLKYYGLRK EWLLGMLGAE 1090 1100 1110 1120 1130 1140 SAKLNNQARF ILEKIDGKII IENKPKKELI KVLIQRGYDS DPVKAWKEAQ QKVPDEEENE 1150 1160 1170 1180 1190 1200 ESDNEKETEK SDSVTDSGPT FNYLLDMPLW YLTKEKKDEL CRLRNEKEQE LDTLKRKSPS 1210 1220 1230 1240 1250 1260 DLWKEDLATF IEELEAVEAK EKQDEQVGLP GKGGKAKGKK TQMAEVLPSP RGQRVIPRIT 1270 1280 1290 1300 1310 1320 IEMKAEAEKK NKKKIKNENT EGSPQEDGVE LEGLKQRLEK KQKREPGTKT KKQTTLAFKP 1330 1340 1350 1360 1370 1380 IKKGKKRNPW SDSESDRSSD ESNFDVPPRE TEPRRAATKT KFTMDLDSDE DFSDFDEKTD 1390 1400 1410 1420 1430 1440 DEDFVPSDAS PPKTKTSPKL SNKELKPQKS VVSDLEADDV KGSVPLSSSP PATHFPDETE 1450 1460 1470 1480 1490 1500 ITNPVPKKNV TVKKTAAKSQ SSTSTTGAKK RAAPKGTKRD PALNSGVSQK PDPAKTKNRR 1510 1520 1530 1540 1550 1560 KRKPSTSDDS DSNFEKIVSK AVTSKKSKGE SDDFHMDFDS AVAPRAKSVR AKKPIKYLEE SDEDDLF
	Isoform 4 [UniParc]. Checksum: AB857EA93238BD4A	FASTA	1,612	182,681
	10 20 30 40 50 60 MEVSPLQPVN ENMQVNKIKK NEDAKKRLSV ERIYQKKTQL EHILLRPDTY IGSVELVTQQ 70 80 90 100 110 120 MWVYDEDVGI NYREVTFVPG LYKIFDEILV NAADNKQRDP KMSCIRVTID PENNLISIWN 130 140 150 160 170 180 NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE 190 200 210 220 230 240 TASREYKKMF KQTWMDNMGR AGEMELKPFN GEDYTCITFQ PDLSKFKMQS LDKDIVALMV 250 260 270 280 290 300 RRAYDIAGST KDVKVFLNGN KLPVKGFRSY VDMYLKDKLD ETGNSLKVIH EQVNHRWEVC 310 320 330 340 350 360 LTMSEKGFQQ ISFVNSIATS KGGRHVDYVA DQIVTKLVDV VKKKNKGGVA VKAHQRELCN 370 380 390 400 410 420 GAILAHCNLR LMGSSDSPAS ASRVAGIAGG CHHTQLIFVF LVETGFHHVG QAGLERLTSG 430 440 450 460 470 480 DPPASASQSS GITDVKVKNH MWIFVNALIE NPTFDSQTKE NMTLQPKSFG STCQLSEKFI 490 500 510 520 530 540 KAAIGCGIVE SILNWVKFKA QVQLNKKCSA VKHNRIKGIP KLDDANDAGG RNSTECTLIL 550 560 570 580 590 600 TEGDSAKTLA VSGLGVVGRD KYGVFPLRGK ILNVREASHK QIMENAEINN IIKIVGLQYK 610 620 630 640 650 660 KNYEDEDSLK TLRYGKIMIM TDQDQDGSHI KGLLINFIHH NWPSLLRHRF LEEFITPIVK 670 680 690 700 710 720 VSKNKQEMAF YSLPEFEEWK SSTPNHKKWK VKYYKGLGTS TSKEAKEYFA DMKRHRIQFK 730 740 750 760 770 780 YSGPEDDAAI SLAFSKKQID DRKEWLTNFM EDRRQRKLLG LPEDYLYGQT TTYLTYNDFI 790 800 810 820 830 840 NKELILFSNS DNERSIPSMV DGLKPGQRKV LFTCFKRNDK REVKVAQLAG SVAEMSSYHH 850 860 870 880 890 900 GEMSLMMTII NLAQNFVGSN NLNLLQPIGQ FGTRLHGGKD SASPRYIFTM LSSLARLLFP 910 920 930 940 950 960 PKDDHTLKFL YDDNQRVEPE WYIPIIPMVL INGAEGIGTG WSCKIPNFDV REIVNNIRRL 970 980 990 1000 1010 1020 MDGEEPLPML PSYKNFKGTI EELAPNQYVI SGEVAILNST TIEISELPVR TWTQTYKEQV 1030 1040 1050 1060 1070 1080 LEPMLNGTEK TPPLITDYRE YHTDTTVKFV VKMTEEKLAE AERVGLHKVF KLQTSLTCNS 1090 1100 1110 1120 1130 1140 MVLFDHVGCL KKYDTVLDIL RDFFELRLKY YGLRKEWLLG MLGAESAKLN NQARFILEKI 1150 1160 1170 1180 1190 1200 DGKIIIENKP KKELIKVLIQ RGYDSDPVKA WKEAQQKVPD EEENEESDNE KETEKSDSVT 1210 1220 1230 1240 1250 1260 DSGPTFNYLL DMPLWYLTKE KKDELCRLRN EKEQELDTLK RKSPSDLWKE DLATFIEELE 1270 1280 1290 1300 1310 1320 AVEAKEKQDE QVGLPGKGGK AKGKKTQMAE VLPSPRGQRV IPRITIEMKA EAEKKNKKKI 1330 1340 1350 1360 1370 1380 KNENTEGSPQ EDGVELEGLK QRLEKKQKRE PGTKTKKQTT LAFKPIKKGK KRNPWSDSES 1390 1400 1410 1420 1430 1440 DRSSDESNFD VPPRETEPRR AATKTKFTMD LDSDEDFSDF DEKTDDEDFV PSDASPPKTK 1450 1460 1470 1480 1490 1500 TSPKLSNKEL KPQKSVVSDL EADDVKGSVP LSSSPPATHF PDETEITNPV PKKNVTVKKT 1510 1520 1530 1540 1550 1560 AAKSQSSTST TGAKKRAAPK GTKRDPALNS GVSQKPDPAK TKNRRKRKPS TSDDSDSNFE 1570 1580 1590 1600 1610 KIVSKAVTSK KSKGESDDFH MDFDSAVAPR AKSVRAKKPI KYLEESDEDD LF

References

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[1]	"Cloning and sequencing of cDNA encoding human DNA topoisomerase II and localization of the gene to chromosome region 17q21-22." Tsai-Pflugfelder M., Liu L.F., Liu A.A., Tewey K.M., Whang-Peng J., Knutsen T., Huebner K., Croce C.M., Wang J.C. Proc. Natl. Acad. Sci. U.S.A. 85:7177-7181(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Use of yeast in the study of anticancer drugs targeting DNA topoisomerases: expression of a functional recombinant human DNA topoisomerase II alpha in yeast." Wasserman R.A., Austin C.A., Fisher L.M., Wang J.C. Cancer Res. 53:3591-3596(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 109-114.
[3]	"Structural organization of the human TOP2A and TOP2B genes." Lang A.J., Mirski S.E., Cummings H.J., Yu Q., Gerlach J.H., Cole S.P. Gene 221:255-266(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[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] (ISOFORM 1).
[5]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORM 1).
[8]	"Two differentially spliced forms of topoisomerase II alpha and beta mRNAs are conserved between birds and humans." Petruti-Mot A.S., Earnshaw W.C. Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-500 (ISOFORMS 2; 3 AND 4).
[9]	Neri S., Govoni M., Perrotta L., Pozzi S., Pession A. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21 AND 48-72.
[10]	Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-17; 74-96; 124-131; 169-184; 243-251; 277-287; 325-336; 387-397; 467-478; 481-487; 500-519; 569-579; 702-713; 805-815; 828-835; 864-877; 937-958; 1021-1026 AND 1185-1196, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[11]	Bienvenut W.V., Waridel P., Quadroni M. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 135-157; 228-241; 307-321; 325-336; 387-397; 401-416; 467-478; 536-550; 569-579; 640-655; 702-713; 805-815; 1011-1020; 1097-1114; 1169-1184; 1239-1259 AND 1374-1411, PHOSPHORYLATION AT SER-1106, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Mitotic phosphorylation of DNA topoisomerase II alpha by protein kinase CK2 creates the MPM-2 phosphoepitope on Ser-1469." Escargueil A.E., Plisov S.Y., Filhol O., Cochet C., Larsen A.K. J. Biol. Chem. 275:34710-34718(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-1469, MUTAGENESIS OF SER-1469.
[13]	"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.
[14]	"Interaction between glucose-regulated destruction domain of DNA topoisomerase IIalpha and MPN domain of Jab1/CSN5." Yun J., Tomida A., Andoh T., Tsuruo T. J. Biol. Chem. 279:31296-31303(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH COPS5.
[15]	"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-4; SER-29; SER-1106; SER-1213; SER-1247; SER-1332; SER-1337; THR-1343; SER-1351; SER-1354; SER-1374; SER-1377 AND SER-1525, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1213; SER-1374; SER-1377 AND SER-1525, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Plk3 phosphorylates topoisomerase IIalpha at Thr(1342), a site that is not recognized by Plk1." Iida M., Matsuda M., Komatani H. Biochem. J. 411:27-32(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-1343.
[19]	"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-1504, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-1213; SER-1247; SER-1332; SER-1337 AND SER-1377, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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-1106; SER-1213; SER-1332; SER-1337; THR-1343; SER-1351; SER-1392; SER-1393; SER-1449; SER-1469; THR-1470; SER-1471; SER-1474 AND SER-1525, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"Use of divalent metal ions in the DNA cleavage reaction of human type II topoisomerases." Deweese J.E., Burch A.M., Burgin A.B., Osheroff N. Biochemistry 48:1862-1869(2009) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR.
[23]	"Metal ion interactions in the DNA cleavage/ligation active site of human topoisomerase IIalpha." Deweese J.E., Guengerich F.P., Burgin A.B., Osheroff N. Biochemistry 48:8940-8947(2009) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF GLU-461; ASP-541; ASP-543 AND ASP-545, PUTATIVE METAL-BINDING SITES, CATALYTIC ACTIVITY, COFACTOR.
[24]	"Casein kinase I delta/epsilon phosphorylates topoisomerase IIalpha at serine-1106 and modulates DNA cleavage activity." Grozav A.G., Chikamori K., Kozuki T., Grabowski D.R., Bukowski R.M., Willard B., Kinter M., Andersen A.H., Ganapathi R., Ganapathi M.K. Nucleic Acids Res. 37:382-392(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-1106 BY CSNK1D/CK1.
[25]	"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-1247; SER-1374; SER-1387; SER-1393; SER-1504 AND SER-1525, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; THR-282; SER-1106; THR-1205; SER-1213; SER-1247; SER-1332; SER-1337; THR-1343; SER-1351; SER-1354; SER-1374; SER-1377; SER-1471; SER-1474; SER-1495; SER-1504 AND SER-1525, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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].
[28]	"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-1106; SER-1213; SER-1247; SER-1295; SER-1297; SER-1299; SER-1302; SER-1332; SER-1337; THR-1343; SER-1351; SER-1354; SER-1374; SER-1377; SER-1469; THR-1470; SER-1471; SER-1474; SER-1476 AND SER-1525, MASS SPECTROMETRY.
[29]	"Structure of a topoisomerase II-DNA-nucleotide complex reveals a new control mechanism for ATPase activity." Schmidt B.H., Osheroff N., Berger J.M. Nat. Struct. Mol. Biol. 19:1147-1154(2012) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF 342-LYS--LYS-344.
[30]	"DNA cleavage and opening reactions of human topoisomerase IIalpha are regulated via Mg2+-mediated dynamic bending of gate-DNA." Lee S., Jung S.R., Heo K., Byl J.A., Deweese J.E., Osheroff N., Hohng S. Proc. Natl. Acad. Sci. U.S.A. 109:2925-2930(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLU-461; ASP-541 AND ASP-543, COFACTOR.
[31]	"Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase." Wei H., Ruthenburg A.J., Bechis S.K., Verdine G.L. J. Biol. Chem. 280:37041-37047(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 29-428 IN COMPLEX WITH ADP, X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 29-428 IN COMPLEX WITH AMPPNP.
[32]	"The structure of DNA-bound human topoisomerase II alpha: conformational mechanisms for coordinating inter-subunit interactions with DNA cleavage." Wendorff T.J., Schmidt B.H., Heslop P., Austin C.A., Berger J.M. J. Mol. Biol. 424:109-124(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 431-1193 IN COMPLEX WITH DNA AND MAGNESIUM ION, SUBUNIT, COFACTOR.
[33]	"Identification of a point mutation in the topoisomerase II gene from a human leukemia cell line containing an amsacrine-resistant form of topoisomerase II." Hinds M., Deisseroth K., Mayes J., Altschuler E., Jansen R., Ledley F.D., Zwelling L.A. Cancer Res. 51:4729-4731(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT AMSACRINE-RESISTANT LYS-487.
[34]	"Expression of a mutant DNA topoisomerase II in CCRF-CEM human leukemic cells selected for resistance to teniposide." Bugg B.Y., Danks M.K., Beck W.T., Suttle D.P. Proc. Natl. Acad. Sci. U.S.A. 88:7654-7658(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TENIPOSIDE-RESISTANT GLN-450.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04088 mRNA. Translation: AAA61209.1.
AF071747 , AF071738, AF071739, AF071740, AF071741, AF071742, AF071743, AF071744, AF071745, AF071746 Genomic DNA. Translation: AAC77388.1.
AJ011741 , AJ011742, AJ011743, AJ011744, AJ011745, AJ011746, AJ011747, AJ011748, AJ011749, AJ011750, AJ011751, AJ011752, AJ011753, AJ011754, AJ011755, AJ011756, AJ011757, AJ011758 Genomic DNA. Translation: CAA09762.1.
AC080112 Genomic DNA. No translation available.
AF285157 mRNA. Translation: AAG13403.1.
AF285158 mRNA. Translation: AAG13404.1.
CH471152 Genomic DNA. Translation: EAW60663.1.
BC140791 mRNA. Translation: AAI40792.1.
AF285159 mRNA. Translation: AAG13405.1.
AF069522 Genomic DNA. Translation: AAC23518.1.
AF064590 Genomic DNA. Translation: AAC16736.1.

IPI

IPI00414101.
IPI00478232.
IPI00879004.
IPI01011132.

PIR

A40493.

RefSeq

NP_001058.2. NM_001067.3.

UniGene

Hs.156346.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LWZ	model	-	A	431-1200	[»]
1ZXM	X-ray	1.87	A/B	29-428	[»]
1ZXN	X-ray	2.51	A/B/C/D	29-428	[»]
4FM9	X-ray	2.90	A	431-1193	[»]

ProteinModelPortal

P11388.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33887N.

IntAct

P11388. 16 interactions.

MINT

MINT-98770.

PTM databases

PhosphoSite

P11388.

Polymorphism databases

DMDM

13959709.

2D gel databases

UCD-2DPAGE

P11388.

Proteomic databases

PaxDb

P11388.

PRIDE

P11388.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000423485; ENSP00000411532; ENSG00000131747.

GeneID

7153.

KEGG

hsa:7153.

UCSC

uc002huq.3. human.

Organism-specific databases

CTD

7153.

GeneCards

GC17M038544.

H-InvDB

HIX0013797.

HGNC

HGNC:11989. TOP2A.

HPA

CAB002448.
HPA006458.
HPA026773.

MIM

126430. gene.

neXtProt

NX_P11388.

PharmGKB

PA354.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0187.

HOVERGEN

HBG052998.

KO

K03164.

OrthoDB

EOG4KWJS0.

Enzyme and pathway databases

BRENDA

5.99.1.3. 2681.

Reactome

REACT_115566. Cell Cycle.

SignaLink

P11388.

Gene expression databases

Bgee

P11388.

CleanEx

HS_TOP2A.

Genevestigator

P11388.

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

P11388.

ChEMBL

CHEMBL1806.

DrugBank

DB00276. Amsacrine.
DB00537. Ciprofloxacin.
DB00380. Dexrazoxane.
DB00997. Doxorubicin.
DB00467. Enoxacin.
DB00445. Epirubicin.
DB00773. Etoposide.
DB04576. Fleroxacin.
DB01044. Gatifloxacin.
DB01177. Idarubicin.
DB01137. Levofloxacin.
DB00978. Lomefloxacin.
DB04967. Lucanthone.
DB01204. Mitoxantrone.
DB00218. Moxifloxacin.
DB01059. Norfloxacin.
DB01165. Ofloxacin.
DB00487. Pefloxacin.
DB01179. Podofilox.
DB01208. Sparfloxacin.
DB00444. Teniposide.
DB00685. Trovafloxacin.
DB00385. Valrubicin.

EvolutionaryTrace

P11388.

GenomeRNAi

7153.

NextBio

27992.

SOURCE

Search...

Entry information

Entry name

TOP2A_HUMAN

Accession

Primary (citable) accession number: P11388
Secondary accession number(s): B2RTS1 , Q71UN1, Q71UQ5, Q9HB24, Q9HB25, Q9HB26, Q9UP44, Q9UQP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	May 4, 2001
Last modified:	May 29, 2013
This is version 170 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.