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P11388

- TOP2A_HUMAN

UniProt

P11388 - TOP2A_HUMAN

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Protein

DNA topoisomerase 2-alpha

Gene
TOP2A, TOP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.2 Publications

Cofactori

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+ Inferred.4 Publications

Enzyme regulationi

Specifically inhibited by the intercalating agent amsacrine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911ATP
Binding sitei120 – 1201ATP
Metal bindingi461 – 4611Magnesium 1; catalytic By similarity
Sitei489 – 4891Interaction with DNA By similarity
Sitei492 – 4921Interaction with DNA
Metal bindingi541 – 5411Magnesium 1; catalytic By similarity
Metal bindingi541 – 5411Magnesium 2
Metal bindingi543 – 5431Magnesium 2
Sitei661 – 6611Interaction with DNA
Sitei662 – 6621Interaction with DNA
Sitei723 – 7231Interaction with DNA
Sitei757 – 7571Interaction with DNA
Sitei763 – 7631Interaction with DNA
Sitei804 – 8041Transition state stabilizer By similarity
Active sitei805 – 8051O-(5'-phospho-DNA)-tyrosine intermediate By similarity
Sitei856 – 8561Important for DNA bending; intercalates between base pairs of target DNA By similarity
Sitei931 – 9311Interaction with DNA

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi148 – 1503ATP
Nucleotide bindingi161 – 1688ATP
Nucleotide bindingi376 – 3783ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. chromatin binding Source: UniProtKB
  3. DNA binding Source: UniProtKB
  4. DNA binding, bending Source: UniProtKB
  5. DNA-dependent ATPase activity Source: UniProtKB
  6. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB
  7. drug binding Source: UniProtKB
  8. enzyme binding Source: UniProtKB
  9. histone deacetylase binding Source: UniProtKB
  10. magnesium ion binding Source: UniProtKB
  11. poly(A) RNA binding Source: UniProtKB
  12. protein binding Source: UniProtKB
  13. protein C-terminus binding Source: UniProtKB
  14. protein heterodimerization activity Source: UniProtKB
  15. protein homodimerization activity Source: UniProtKB
  16. protein kinase C binding Source: UniProtKB
  17. ubiquitin binding Source: UniProtKB

GO - Biological processi

  1. apoptotic chromosome condensation Source: UniProtKB
  2. ATP catabolic process Source: GOC
  3. cellular response to DNA damage stimulus Source: UniProtKB
  4. chromosome segregation Source: UniProtKB
  5. DNA ligation Source: UniProtKB
  6. DNA repair Source: UniProtKB
  7. DNA replication Source: UniProtKB
  8. DNA topological change Source: UniProtKB
  9. DNA unwinding involved in DNA replication Source: RefGenome
  10. embryonic cleavage Source: Ensembl
  11. mitotic cell cycle Source: Reactome
  12. mitotic DNA integrity checkpoint Source: RefGenome
  13. mitotic recombination Source: RefGenome
  14. phosphatidylinositol-mediated signaling Source: UniProtKB
  15. positive regulation of apoptotic process Source: UniProtKB
  16. positive regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
  17. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  18. positive regulation of viral genome replication Source: UniProtKB
  19. resolution of meiotic recombination intermediates Source: RefGenome
  20. sister chromatid segregation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Ligandi

ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi5.99.1.3. 2681.
ReactomeiREACT_111214. G0 and Early G1.
SignaLinkiP11388.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA topoisomerase 2-alpha (EC:5.99.1.3)
Alternative name(s):
DNA topoisomerase II, alpha isozyme
Gene namesi
Name:TOP2A
Synonyms:TOP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:11989. TOP2A.

Subcellular locationi

Cytoplasm. Nucleusnucleoplasm
Note: Generally located in the nucleoplasm.1 Publication

GO - Cellular componenti

  1. condensed chromosome Source: Ensembl
  2. cytoplasm Source: UniProtKB-SubCell
  3. DNA topoisomerase complex (ATP-hydrolyzing) Source: UniProtKB
  4. nucleolus Source: UniProtKB
  5. nucleoplasm Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi342 – 3443KKK → AAA: Reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. 1 Publication
Mutagenesisi342 – 3443KKK → EEE: Strongly reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. 1 Publication
Mutagenesisi461 – 4611E → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. 2 Publications
Mutagenesisi541 – 5411D → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. 2 Publications
Mutagenesisi543 – 5431D → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. 2 Publications
Mutagenesisi545 – 5451D → A or C: Strongly reduced DNA cleavage. 1 Publication
Mutagenesisi1469 – 14691S → A: Abolishes binding to the antibody MPM2. 1 Publication

Organism-specific databases

Orphaneti635. Neuroblastoma.
PharmGKBiPA354.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15311531DNA topoisomerase 2-alphaPRO_0000145363Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei4 – 41Phosphoserine4 Publications
Modified residuei282 – 2821Phosphothreonine1 Publication
Modified residuei1106 – 11061Phosphoserine; by CK16 Publications
Modified residuei1205 – 12051Phosphothreonine1 Publication
Modified residuei1213 – 12131Phosphoserine6 Publications
Modified residuei1247 – 12471Phosphoserine6 Publications
Modified residuei1295 – 12951Phosphoserine1 Publication
Modified residuei1297 – 12971Phosphoserine1 Publication
Modified residuei1299 – 12991Phosphoserine1 Publication
Modified residuei1302 – 13021Phosphoserine1 Publication
Modified residuei1332 – 13321Phosphoserine5 Publications
Modified residuei1337 – 13371Phosphoserine5 Publications
Modified residuei1343 – 13431Phosphothreonine; by PLK35 Publications
Modified residuei1351 – 13511Phosphoserine4 Publications
Modified residuei1354 – 13541Phosphoserine3 Publications
Modified residuei1374 – 13741Phosphoserine5 Publications
Modified residuei1377 – 13771Phosphoserine5 Publications
Modified residuei1387 – 13871Phosphoserine1 Publication
Modified residuei1392 – 13921Phosphoserine1 Publication
Modified residuei1393 – 13931Phosphoserine2 Publications
Modified residuei1422 – 14221N6-acetyllysine By similarity
Modified residuei1442 – 14421N6-acetyllysine By similarity
Modified residuei1449 – 14491Phosphoserine1 Publication
Modified residuei1469 – 14691Phosphoserine; by CK23 Publications
Modified residuei1470 – 14701Phosphothreonine2 Publications
Modified residuei1471 – 14711Phosphoserine3 Publications
Modified residuei1474 – 14741Phosphoserine3 Publications
Modified residuei1476 – 14761Phosphoserine1 Publication
Modified residuei1495 – 14951Phosphoserine1 Publication
Modified residuei1504 – 15041Phosphoserine3 Publications
Modified residuei1525 – 15251Phosphoserine6 Publications

Post-translational modificationi

Phosphorylation has no effect on catalytic activity. However, phosphorylation at Ser-1106 by CSNK1D/CK1 promotes DNA cleavable complex formation.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11388.
PaxDbiP11388.
PRIDEiP11388.

2D gel databases

UCD-2DPAGEP11388.

PTM databases

PhosphoSiteiP11388.

Expressioni

Gene expression databases

ArrayExpressiP11388.
BgeeiP11388.
CleanExiHS_TOP2A.
GenevestigatoriP11388.

Organism-specific databases

HPAiCAB002448.
HPA006458.
HPA026773.

Interactioni

Subunit structurei

Homodimer. Interacts with COPS5. Interacts with RECQL5; this stimulates DNA decatenation.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352225EBI-539628,EBI-491549

Protein-protein interaction databases

BioGridi113006. 60 interactions.
DIPiDIP-33887N.
IntActiP11388. 17 interactions.
MINTiMINT-98770.

Structurei

Secondary structure

1
1531
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 334
Beta strandi34 – 363
Helixi39 – 457
Helixi48 – 514
Beta strandi57 – 659
Turni66 – 683
Beta strandi69 – 779
Helixi79 – 9820
Beta strandi104 – 1107
Turni111 – 1144
Beta strandi115 – 1239
Beta strandi128 – 1303
Turni131 – 1344
Helixi137 – 1437
Beta strandi144 – 1496
Helixi153 – 1553
Helixi166 – 1727
Beta strandi174 – 18310
Turni184 – 1874
Beta strandi188 – 1958
Turni196 – 1994
Beta strandi205 – 2084
Beta strandi214 – 2218
Helixi223 – 2264
Helixi233 – 24917
Beta strandi250 – 2523
Beta strandi254 – 2574
Helixi267 – 2759
Beta strandi281 – 2855
Beta strandi289 – 2946
Beta strandi297 – 3037
Beta strandi305 – 3073
Beta strandi309 – 3146
Helixi324 – 34118
Helixi353 – 3575
Beta strandi360 – 3667
Beta strandi373 – 3753
Helixi385 – 3873
Beta strandi388 – 3903
Helixi396 – 4027
Helixi411 – 4155
Beta strandi419 – 4213
Turni445 – 4484
Helixi452 – 4543
Beta strandi456 – 4627
Helixi463 – 47614
Beta strandi478 – 4869
Helixi498 – 5036
Helixi505 – 51410
Beta strandi518 – 5203
Helixi525 – 5306
Beta strandi534 – 5396
Helixi544 – 56017
Helixi562 – 5665
Beta strandi570 – 5734
Beta strandi577 – 5815
Beta strandi586 – 5905
Helixi592 – 60110
Beta strandi607 – 6126
Helixi616 – 6183
Helixi621 – 6299
Helixi631 – 6344
Beta strandi635 – 6395
Helixi644 – 65310
Helixi658 – 67821
Beta strandi685 – 6884
Beta strandi691 – 6944
Helixi695 – 7017
Helixi703 – 71412
Turni718 – 7203
Helixi724 – 73512
Helixi744 – 75411
Helixi762 – 77211
Turni793 – 7997
Turni803 – 8053
Helixi812 – 8176
Helixi822 – 8243
Helixi831 – 8333
Turni848 – 8503
Beta strandi853 – 8564
Beta strandi861 – 8644
Helixi869 – 88113
Beta strandi897 – 9037
Beta strandi906 – 9105
Beta strandi921 – 9233
Helixi932 – 9387
Helixi940 – 9445
Beta strandi948 – 9503
Beta strandi955 – 9595
Beta strandi968 – 9714
Helixi974 – 98310
Helixi985 – 9884
Beta strandi992 – 9965
Beta strandi1000 – 10034
Beta strandi1009 – 10113
Helixi1015 – 105945
Helixi1070 – 108011
Helixi1086 – 10916
Helixi1126 – 11294
Helixi1138 – 116023
Helixi1163 – 118927

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LWZmodel-A431-1200[»]
1ZXMX-ray1.87A/B29-428[»]
1ZXNX-ray2.51A/B/C/D29-428[»]
4FM9X-ray2.90A431-1193[»]
ProteinModelPortaliP11388.
SMRiP11388. Positions 29-1190.

Miscellaneous databases

EvolutionaryTraceiP11388.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini455 – 572118ToprimAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni342 – 3443Interaction with DNA Inferred
Regioni990 – 99910Interaction with DNA

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1018 – 102811Nuclear export signalAdd
BLAST

Sequence similaritiesi

Contains 1 Toprim domain.

Phylogenomic databases

eggNOGiCOG0187.
HOVERGENiHBG052998.
KOiK03164.
OMAiSRWEVCL.
OrthoDBiEOG73JKTM.
PhylomeDBiP11388.
TreeFamiTF105282.

Family and domain databases

Gene3Di1.10.268.10. 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.
InterProiIPR024946. Arg_repress_C-like.
IPR012542. DTHCT.
IPR003594. HATPase_ATP-bd.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR028466. Top2a.
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]
PANTHERiPTHR10169:SF33. PTHR10169:SF33. 1 hit.
PfamiPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF08070. DTHCT. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSiPR00418. TPI2FAMILY.
SMARTiSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P11388-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MEVSPLQPVN ENMQVNKIKK NEDAKKRLSV ERIYQKKTQL EHILLRPDTY     50
IGSVELVTQQ MWVYDEDVGI NYREVTFVPG LYKIFDEILV NAADNKQRDP 100
KMSCIRVTID PENNLISIWN NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN 150
YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE TASREYKKMF KQTWMDNMGR 200
AGEMELKPFN GEDYTCITFQ PDLSKFKMQS LDKDIVALMV RRAYDIAGST 250
KDVKVFLNGN KLPVKGFRSY VDMYLKDKLD ETGNSLKVIH EQVNHRWEVC 300
LTMSEKGFQQ ISFVNSIATS KGGRHVDYVA DQIVTKLVDV VKKKNKGGVA 350
VKAHQVKNHM WIFVNALIEN PTFDSQTKEN MTLQPKSFGS TCQLSEKFIK 400
AAIGCGIVES ILNWVKFKAQ VQLNKKCSAV KHNRIKGIPK LDDANDAGGR 450
NSTECTLILT EGDSAKTLAV SGLGVVGRDK YGVFPLRGKI LNVREASHKQ 500
IMENAEINNI IKIVGLQYKK NYEDEDSLKT LRYGKIMIMT DQDQDGSHIK 550
GLLINFIHHN WPSLLRHRFL EEFITPIVKV SKNKQEMAFY SLPEFEEWKS 600
STPNHKKWKV KYYKGLGTST SKEAKEYFAD MKRHRIQFKY SGPEDDAAIS 650
LAFSKKQIDD RKEWLTNFME DRRQRKLLGL PEDYLYGQTT TYLTYNDFIN 700
KELILFSNSD NERSIPSMVD GLKPGQRKVL FTCFKRNDKR EVKVAQLAGS 750
VAEMSSYHHG EMSLMMTIIN LAQNFVGSNN LNLLQPIGQF GTRLHGGKDS 800
ASPRYIFTML SSLARLLFPP KDDHTLKFLY DDNQRVEPEW YIPIIPMVLI 850
NGAEGIGTGW SCKIPNFDVR EIVNNIRRLM DGEEPLPMLP SYKNFKGTIE 900
ELAPNQYVIS GEVAILNSTT IEISELPVRT WTQTYKEQVL EPMLNGTEKT 950
PPLITDYREY HTDTTVKFVV KMTEEKLAEA ERVGLHKVFK LQTSLTCNSM 1000
VLFDHVGCLK KYDTVLDILR DFFELRLKYY GLRKEWLLGM LGAESAKLNN 1050
QARFILEKID GKIIIENKPK KELIKVLIQR GYDSDPVKAW KEAQQKVPDE 1100
EENEESDNEK ETEKSDSVTD SGPTFNYLLD MPLWYLTKEK KDELCRLRNE 1150
KEQELDTLKR KSPSDLWKED LATFIEELEA VEAKEKQDEQ VGLPGKGGKA 1200
KGKKTQMAEV LPSPRGQRVI PRITIEMKAE AEKKNKKKIK NENTEGSPQE 1250
DGVELEGLKQ RLEKKQKREP GTKTKKQTTL AFKPIKKGKK RNPWSDSESD 1300
RSSDESNFDV PPRETEPRRA ATKTKFTMDL DSDEDFSDFD EKTDDEDFVP 1350
SDASPPKTKT SPKLSNKELK PQKSVVSDLE ADDVKGSVPL SSSPPATHFP 1400
DETEITNPVP KKNVTVKKTA AKSQSSTSTT GAKKRAAPKG TKRDPALNSG 1450
VSQKPDPAKT KNRRKRKPST SDDSDSNFEK IVSKAVTSKK SKGESDDFHM 1500
DFDSAVAPRA KSVRAKKPIK YLEESDEDDL F 1531
Length:1,531
Mass (Da):174,385
Last modified:May 4, 2001 - v3
Checksum:i3DF40BC9E84789DC
GO
Isoform 2 (identifier: P11388-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,557
Mass (Da):177,501
Checksum:i4DE312DFAEC443EA
GO
Isoform 3 (identifier: P11388-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,567
Mass (Da):178,712
Checksum:iE5322E9ED4DD7BF5
GO
Isoform 4 (identifier: P11388-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,612
Mass (Da):182,681
Checksum:iAB857EA93238BD4A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti450 – 4501R → Q in teniposide (VM-26) resistant cells. 1 Publication
VAR_007532
Natural varianti487 – 4871R → K in amsacrine resistant cells. 1 Publication
VAR_007533
Natural varianti1324 – 13241T → K.
Corresponds to variant rs28969502 [ dbSNP | Ensembl ].
VAR_029245
Natural varianti1386 – 13861G → D.
Corresponds to variant rs34300454 [ dbSNP | Ensembl ].
VAR_052594
Natural varianti1515 – 15151A → S.
Corresponds to variant rs11540720 [ dbSNP | Ensembl ].
VAR_052595

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei321 – 3211K → KSSKYWSSRKSKQHILLNFF VLFKFINDAFFGICPFK in isoform 3. VSP_006529
Alternative sequencei355 – 3551Q → QRELCNGAILAHCNLRLMGS SDSPASASRVAGIAGGCHHT QLIFVFLVETGFHHVGQAGL ERLTSGDPPASASQSSGITD VK in isoform 4. VSP_006530
Alternative sequencei401 – 4011A → AHLYSRFLIDPFFPNMIPNM IFSFSKA in isoform 2. VSP_006531

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521D → H in CAA09762. 1 Publication
Sequence conflicti180 – 1801E → Q in CAA09762. 1 Publication
Sequence conflicti327 – 3271D → H in CAA09762. 1 Publication
Sequence conflicti1022 – 10221F → L in CAA09762. 1 Publication
Sequence conflicti1274 – 12741T → S in CAA09762. 1 Publication
Sequence conflicti1295 – 12951S → P in AAA61209. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS45672.1. [P11388-1]
PIRiA40493.
RefSeqiNP_001058.2. NM_001067.3. [P11388-1]
UniGeneiHs.156346.

Genome annotation databases

EnsembliENST00000423485; ENSP00000411532; ENSG00000131747. [P11388-1]
GeneIDi7153.
KEGGihsa:7153.
UCSCiuc002huq.3. human. [P11388-1]

Polymorphism databases

DMDMi13959709.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS45672.1. [P11388-1 ]
PIRi A40493.
RefSeqi NP_001058.2. NM_001067.3. [P11388-1 ]
UniGenei Hs.156346.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P11388.
SMRi P11388. Positions 29-1190.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113006. 60 interactions.
DIPi DIP-33887N.
IntActi P11388. 17 interactions.
MINTi MINT-98770.

Chemistry

BindingDBi P11388.
ChEMBLi CHEMBL1806.
DrugBanki 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.
GuidetoPHARMACOLOGYi 2637.

PTM databases

PhosphoSitei P11388.

Polymorphism databases

DMDMi 13959709.

2D gel databases

UCD-2DPAGE P11388.

Proteomic databases

MaxQBi P11388.
PaxDbi P11388.
PRIDEi P11388.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000423485 ; ENSP00000411532 ; ENSG00000131747 . [P11388-1 ]
GeneIDi 7153.
KEGGi hsa:7153.
UCSCi uc002huq.3. human. [P11388-1 ]

Organism-specific databases

CTDi 7153.
GeneCardsi GC17M038544.
H-InvDB HIX0013797.
HGNCi HGNC:11989. TOP2A.
HPAi CAB002448.
HPA006458.
HPA026773.
MIMi 126430. gene.
neXtProti NX_P11388.
Orphaneti 635. Neuroblastoma.
PharmGKBi PA354.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0187.
HOVERGENi HBG052998.
KOi K03164.
OMAi SRWEVCL.
OrthoDBi EOG73JKTM.
PhylomeDBi P11388.
TreeFami TF105282.

Enzyme and pathway databases

BRENDAi 5.99.1.3. 2681.
Reactomei REACT_111214. G0 and Early G1.
SignaLinki P11388.

Miscellaneous databases

EvolutionaryTracei P11388.
GeneWikii TOP2A.
GenomeRNAii 7153.
NextBioi 27992.
PROi P11388.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11388.
Bgeei P11388.
CleanExi HS_TOP2A.
Genevestigatori P11388.

Family and domain databases

Gene3Di 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.
InterProi IPR024946. Arg_repress_C-like.
IPR012542. DTHCT.
IPR003594. HATPase_ATP-bd.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR028466. Top2a.
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 ]
PANTHERi PTHR10169:SF33. PTHR10169:SF33. 1 hit.
Pfami 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 ]
PRINTSi PR00418. TPI2FAMILY.
SMARTi SM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEi PS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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-1106; SER-1213; SER-1247; SER-1332; SER-1337; THR-1343; SER-1351; SER-1354; SER-1374; SER-1377 AND SER-1525, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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.
  24. "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.
  25. "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.
  26. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  27. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "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.
  31. "RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation and cell cycle progression."
    Ramamoorthy M., Tadokoro T., Rybanska I., Ghosh A.K., Wersto R., May A., Kulikowicz T., Sykora P., Croteau D.L., Bohr V.A.
    Nucleic Acids Res. 40:1621-1635(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RECQL5.
  32. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "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.
  34. "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.
  35. "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.
  36. "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.
  37. "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.

Entry informationi

Entry nameiTOP2A_HUMAN
AccessioniPrimary (citable) accession number: P11388
Secondary accession number(s): B2RTS1
, Q71UN1, Q71UQ5, Q9HB24, Q9HB25, Q9HB26, Q9UP44, Q9UQP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 4, 2001
Last modified: September 3, 2014
This is version 183 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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