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Protein

DNA topoisomerase 2-alpha

Gene

TOP2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. May play a role in regulating the period length of ARNTL/BMAL1 transcriptional oscillation (By similarity).By similarity3 Publications

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.PROSITE-ProRule annotation2 Publications

Cofactori

Mg2+4 Publications, Mn2+4 Publications, Ca2+4 PublicationsNote: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca2+.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; catalyticPROSITE-ProRule annotation
Sitei489 – 4891Interaction with DNAPROSITE-ProRule annotation
Sitei492 – 4921Interaction with DNA
Metal bindingi541 – 5411Magnesium 1; catalyticPROSITE-ProRule annotation
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 stabilizerBy similarity
Active sitei805 – 8051O-(5'-phospho-DNA)-tyrosine intermediateBy similarity
Sitei856 – 8561Important for DNA bending; intercalates between base pairs of target DNABy similarity
Sitei931 – 9311Interaction with DNA

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • chromatin binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA binding, bending Source: UniProtKB
  • DNA-dependent ATPase activity Source: UniProtKB
  • DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB
  • drug binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein C-terminus binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase C binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • apoptotic chromosome condensation Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • chromosome segregation Source: UniProtKB
  • DNA ligation Source: UniProtKB
  • DNA topological change Source: UniProtKB
  • DNA unwinding involved in DNA replication Source: GO_Central
  • embryonic cleavage Source: Ensembl
  • hematopoietic progenitor cell differentiation Source: Ensembl
  • mitotic cell cycle Source: Reactome
  • mitotic DNA integrity checkpoint Source: GO_Central
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of single stranded viral RNA replication via double stranded DNA intermediate Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • positive regulation of viral genome replication Source: UniProtKB
  • regulation of circadian rhythm Source: UniProtKB
  • resolution of meiotic recombination intermediates Source: GO_Central
  • rhythmic process Source: UniProtKB-KW
  • sister chromatid segregation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Topoisomerase

Keywords - Biological processi

Biological rhythms

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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11989. TOP2A.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome Source: Ensembl
  • cytoplasm Source: UniProtKB-SubCell
  • DNA topoisomerase complex (ATP-hydrolyzing) Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • 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.

Chemistry

DrugBankiDB00276. Amsacrine.
DB00537. Ciprofloxacin.
DB00970. Dactinomycin.
DB00694. Daunorubicin.
DB00380. Dexrazoxane.
DB00997. Doxorubicin.
DB00467. Enoxacin.
DB00445. Epirubicin.
DB00773. Etoposide.
DB04576. Fleroxacin.
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.

Polymorphism and mutation databases

BioMutaiTOP2A.
DMDMi13959709.

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-acetyllysineBy similarity
Modified residuei1442 – 14421N6-acetyllysineBy 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.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11388.
PaxDbiP11388.
PRIDEiP11388.

2D gel databases

UCD-2DPAGEP11388.

PTM databases

PhosphoSiteiP11388.

Expressioni

Gene expression databases

BgeeiP11388.
CleanExiHS_TOP2A.
ExpressionAtlasiP11388. baseline and differential.
GenevisibleiP11388. HS.

Organism-specific databases

HPAiCAB002448.
HPA006458.
HPA026773.

Interactioni

Subunit structurei

Homodimer. Interacts with COPS5. Interacts with RECQL5; this stimulates DNA decatenation. Interacts with SETMAR; stimulates the topoisomerase activity (PubMed:18790802, PubMed:20457750).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352225EBI-539628,EBI-491549
PRKCDQ0565510EBI-539628,EBI-704279

Protein-protein interaction databases

BioGridi113006. 66 interactions.
DIPiDIP-33887N.
IntActiP11388. 18 interactions.
MINTiMINT-98770.
STRINGi9606.ENSP00000411532.

Structurei

Secondary structure

1
1531
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 334Combined sources
Beta strandi34 – 363Combined sources
Helixi39 – 457Combined sources
Helixi48 – 514Combined sources
Beta strandi57 – 659Combined sources
Turni66 – 683Combined sources
Beta strandi69 – 779Combined sources
Helixi79 – 9820Combined sources
Beta strandi104 – 1107Combined sources
Turni111 – 1144Combined sources
Beta strandi115 – 1239Combined sources
Beta strandi128 – 1303Combined sources
Turni131 – 1344Combined sources
Helixi137 – 1437Combined sources
Beta strandi144 – 1496Combined sources
Helixi153 – 1553Combined sources
Helixi166 – 1727Combined sources
Beta strandi174 – 18310Combined sources
Turni184 – 1874Combined sources
Beta strandi188 – 1958Combined sources
Turni196 – 1994Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi214 – 2218Combined sources
Helixi223 – 2264Combined sources
Helixi233 – 24917Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi254 – 2574Combined sources
Helixi267 – 2759Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi289 – 2946Combined sources
Beta strandi297 – 3037Combined sources
Beta strandi305 – 3073Combined sources
Beta strandi309 – 3146Combined sources
Helixi324 – 34118Combined sources
Beta strandi346 – 3483Combined sources
Helixi353 – 3575Combined sources
Beta strandi360 – 3667Combined sources
Beta strandi373 – 3753Combined sources
Helixi385 – 3873Combined sources
Beta strandi388 – 3903Combined sources
Helixi396 – 4027Combined sources
Helixi407 – 4104Combined sources
Helixi411 – 4155Combined sources
Beta strandi419 – 4213Combined sources
Beta strandi423 – 4253Combined sources
Turni445 – 4484Combined sources
Helixi452 – 4543Combined sources
Beta strandi456 – 4627Combined sources
Helixi463 – 47614Combined sources
Beta strandi478 – 4869Combined sources
Helixi498 – 5036Combined sources
Helixi505 – 51410Combined sources
Beta strandi518 – 5203Combined sources
Helixi525 – 5306Combined sources
Beta strandi534 – 5396Combined sources
Helixi544 – 56017Combined sources
Helixi562 – 5665Combined sources
Beta strandi570 – 5734Combined sources
Beta strandi577 – 5815Combined sources
Beta strandi586 – 5905Combined sources
Helixi592 – 60110Combined sources
Beta strandi607 – 6126Combined sources
Helixi616 – 6183Combined sources
Helixi621 – 6299Combined sources
Helixi631 – 6344Combined sources
Beta strandi635 – 6395Combined sources
Helixi644 – 65310Combined sources
Helixi658 – 67821Combined sources
Beta strandi685 – 6884Combined sources
Beta strandi691 – 6944Combined sources
Helixi695 – 7017Combined sources
Helixi703 – 71412Combined sources
Turni718 – 7203Combined sources
Helixi724 – 73512Combined sources
Helixi744 – 75411Combined sources
Helixi762 – 77211Combined sources
Turni793 – 7997Combined sources
Turni803 – 8053Combined sources
Helixi812 – 8176Combined sources
Helixi822 – 8243Combined sources
Helixi831 – 8333Combined sources
Turni848 – 8503Combined sources
Beta strandi853 – 8564Combined sources
Beta strandi861 – 8644Combined sources
Helixi869 – 88113Combined sources
Beta strandi897 – 9037Combined sources
Beta strandi906 – 9105Combined sources
Beta strandi921 – 9233Combined sources
Helixi932 – 9387Combined sources
Helixi940 – 9445Combined sources
Beta strandi948 – 9503Combined sources
Beta strandi955 – 9595Combined sources
Beta strandi968 – 9714Combined sources
Helixi974 – 98310Combined sources
Helixi985 – 9884Combined sources
Beta strandi992 – 9965Combined sources
Beta strandi1000 – 10034Combined sources
Beta strandi1009 – 10113Combined sources
Helixi1015 – 105945Combined sources
Helixi1070 – 108011Combined sources
Helixi1086 – 10916Combined sources
Helixi1126 – 11294Combined sources
Helixi1138 – 116023Combined sources
Helixi1163 – 118927Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LWZmodel-A431-1200[»]
1ZXMX-ray1.87A/B29-428[»]
1ZXNX-ray2.51A/B/C/D29-428[»]
4FM9X-ray2.90A431-1193[»]
4R1FX-ray2.51A/B/C/D29-428[»]
ProteinModelPortaliP11388.
SMRiP11388. Positions 29-405, 433-1190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11388.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini455 – 572118ToprimPROSITE-ProRule annotationAdd
BLAST

Region

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

Motif

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

Sequence similaritiesi

Belongs to the type II topoisomerase family.Curated
Contains 1 Toprim domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0187.
GeneTreeiENSGT00390000016222.
HOVERGENiHBG052998.
InParanoidiP11388.
KOiK03164.
OMAiVKFIVKM.
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_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR028466. Top2a.
IPR001241. Topo_IIA.
IPR013760. Topo_IIA-like_dom.
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.
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. AlignAdd to basket

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

        10         20         30         40         50
MEVSPLQPVN ENMQVNKIKK NEDAKKRLSV ERIYQKKTQL EHILLRPDTY
60 70 80 90 100
IGSVELVTQQ MWVYDEDVGI NYREVTFVPG LYKIFDEILV NAADNKQRDP
110 120 130 140 150
KMSCIRVTID PENNLISIWN NGKGIPVVEH KVEKMYVPAL IFGQLLTSSN
160 170 180 190 200
YDDDEKKVTG GRNGYGAKLC NIFSTKFTVE TASREYKKMF KQTWMDNMGR
210 220 230 240 250
AGEMELKPFN GEDYTCITFQ PDLSKFKMQS LDKDIVALMV RRAYDIAGST
260 270 280 290 300
KDVKVFLNGN KLPVKGFRSY VDMYLKDKLD ETGNSLKVIH EQVNHRWEVC
310 320 330 340 350
LTMSEKGFQQ ISFVNSIATS KGGRHVDYVA DQIVTKLVDV VKKKNKGGVA
360 370 380 390 400
VKAHQVKNHM WIFVNALIEN PTFDSQTKEN MTLQPKSFGS TCQLSEKFIK
410 420 430 440 450
AAIGCGIVES ILNWVKFKAQ VQLNKKCSAV KHNRIKGIPK LDDANDAGGR
460 470 480 490 500
NSTECTLILT EGDSAKTLAV SGLGVVGRDK YGVFPLRGKI LNVREASHKQ
510 520 530 540 550
IMENAEINNI IKIVGLQYKK NYEDEDSLKT LRYGKIMIMT DQDQDGSHIK
560 570 580 590 600
GLLINFIHHN WPSLLRHRFL EEFITPIVKV SKNKQEMAFY SLPEFEEWKS
610 620 630 640 650
STPNHKKWKV KYYKGLGTST SKEAKEYFAD MKRHRIQFKY SGPEDDAAIS
660 670 680 690 700
LAFSKKQIDD RKEWLTNFME DRRQRKLLGL PEDYLYGQTT TYLTYNDFIN
710 720 730 740 750
KELILFSNSD NERSIPSMVD GLKPGQRKVL FTCFKRNDKR EVKVAQLAGS
760 770 780 790 800
VAEMSSYHHG EMSLMMTIIN LAQNFVGSNN LNLLQPIGQF GTRLHGGKDS
810 820 830 840 850
ASPRYIFTML SSLARLLFPP KDDHTLKFLY DDNQRVEPEW YIPIIPMVLI
860 870 880 890 900
NGAEGIGTGW SCKIPNFDVR EIVNNIRRLM DGEEPLPMLP SYKNFKGTIE
910 920 930 940 950
ELAPNQYVIS GEVAILNSTT IEISELPVRT WTQTYKEQVL EPMLNGTEKT
960 970 980 990 1000
PPLITDYREY HTDTTVKFVV KMTEEKLAEA ERVGLHKVFK LQTSLTCNSM
1010 1020 1030 1040 1050
VLFDHVGCLK KYDTVLDILR DFFELRLKYY GLRKEWLLGM LGAESAKLNN
1060 1070 1080 1090 1100
QARFILEKID GKIIIENKPK KELIKVLIQR GYDSDPVKAW KEAQQKVPDE
1110 1120 1130 1140 1150
EENEESDNEK ETEKSDSVTD SGPTFNYLLD MPLWYLTKEK KDELCRLRNE
1160 1170 1180 1190 1200
KEQELDTLKR KSPSDLWKED LATFIEELEA VEAKEKQDEQ VGLPGKGGKA
1210 1220 1230 1240 1250
KGKKTQMAEV LPSPRGQRVI PRITIEMKAE AEKKNKKKIK NENTEGSPQE
1260 1270 1280 1290 1300
DGVELEGLKQ RLEKKQKREP GTKTKKQTTL AFKPIKKGKK RNPWSDSESD
1310 1320 1330 1340 1350
RSSDESNFDV PPRETEPRRA ATKTKFTMDL DSDEDFSDFD EKTDDEDFVP
1360 1370 1380 1390 1400
SDASPPKTKT SPKLSNKELK PQKSVVSDLE ADDVKGSVPL SSSPPATHFP
1410 1420 1430 1440 1450
DETEITNPVP KKNVTVKKTA AKSQSSTSTT GAKKRAAPKG TKRDPALNSG
1460 1470 1480 1490 1500
VSQKPDPAKT KNRRKRKPST SDDSDSNFEK IVSKAVTSKK SKGESDDFHM
1510 1520 1530
DFDSAVAPRA KSVRAKKPIK YLEESDEDDL F
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521D → H in CAA09762 (PubMed:10095062).Curated
Sequence conflicti180 – 1801E → Q in CAA09762 (PubMed:10095062).Curated
Sequence conflicti327 – 3271D → H in CAA09762 (PubMed:10095062).Curated
Sequence conflicti1022 – 10221F → L in CAA09762 (PubMed:10095062).Curated
Sequence conflicti1274 – 12741T → S in CAA09762 (PubMed:10095062).Curated
Sequence conflicti1295 – 12951S → P in AAA61209 (PubMed:2845399).Curated

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. 1 PublicationVSP_006529
Alternative sequencei355 – 3551Q → QRELCNGAILAHCNLRLMGS SDSPASASRVAGIAGGCHHT QLIFVFLVETGFHHVGQAGL ERLTSGDPPASASQSSGITD VK in isoform 4. 1 PublicationVSP_006530
Alternative sequencei401 – 4011A → AHLYSRFLIDPFFPNMIPNM IFSFSKA in isoform 2. 1 PublicationVSP_006531

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
GeneIDi7153.
KEGGihsa:7153.
UCSCiuc002huq.3. human. [P11388-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LWZmodel-A431-1200[»]
1ZXMX-ray1.87A/B29-428[»]
1ZXNX-ray2.51A/B/C/D29-428[»]
4FM9X-ray2.90A431-1193[»]
4R1FX-ray2.51A/B/C/D29-428[»]
ProteinModelPortaliP11388.
SMRiP11388. Positions 29-405, 433-1190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113006. 66 interactions.
DIPiDIP-33887N.
IntActiP11388. 18 interactions.
MINTiMINT-98770.
STRINGi9606.ENSP00000411532.

Chemistry

BindingDBiP11388.
ChEMBLiCHEMBL2094255.
DrugBankiDB00276. Amsacrine.
DB00537. Ciprofloxacin.
DB00970. Dactinomycin.
DB00694. Daunorubicin.
DB00380. Dexrazoxane.
DB00997. Doxorubicin.
DB00467. Enoxacin.
DB00445. Epirubicin.
DB00773. Etoposide.
DB04576. Fleroxacin.
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.
GuidetoPHARMACOLOGYi2637.

PTM databases

PhosphoSiteiP11388.

Polymorphism and mutation databases

BioMutaiTOP2A.
DMDMi13959709.

2D gel databases

UCD-2DPAGEP11388.

Proteomic databases

MaxQBiP11388.
PaxDbiP11388.
PRIDEiP11388.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7153.
GeneCardsiGC17M038544.
H-InvDBHIX0013797.
HGNCiHGNC:11989. TOP2A.
HPAiCAB002448.
HPA006458.
HPA026773.
MIMi126430. gene.
neXtProtiNX_P11388.
Orphaneti635. Neuroblastoma.
PharmGKBiPA354.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0187.
GeneTreeiENSGT00390000016222.
HOVERGENiHBG052998.
InParanoidiP11388.
KOiK03164.
OMAiVKFIVKM.
OrthoDBiEOG73JKTM.
PhylomeDBiP11388.
TreeFamiTF105282.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP11388.
GeneWikiiTOP2A.
GenomeRNAii7153.
NextBioi27992.
PROiP11388.
SOURCEiSearch...

Gene expression databases

BgeeiP11388.
CleanExiHS_TOP2A.
ExpressionAtlasiP11388. baseline and differential.
GenevisibleiP11388. HS.

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_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR028466. Top2a.
IPR001241. Topo_IIA.
IPR013760. Topo_IIA-like_dom.
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.
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]
ProtoNetiSearch...

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. "The SET and transposase domain protein Metnase enhances chromosome decatenation: regulation by automethylation."
    Williamson E.A., Rasila K.K., Corwin L.K., Wray J., Beck B.D., Severns V., Mobarak C., Lee S.H., Nickoloff J.A., Hromas R.
    Nucleic Acids Res. 36:5822-5831(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SETMAR.
  22. 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.
  23. "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].
  24. "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.
  25. "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.
  26. "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.
  27. "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.
  28. Cited for: INTERACTION WITH SETMAR.
  29. "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.
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "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].
  32. "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.
  33. "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.
  34. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. "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.
  36. "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.
  37. "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.
  38. "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.
  39. "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: July 22, 2015
This is version 194 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.