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P11388

- TOP2A_HUMAN

UniProt

P11388 - TOP2A_HUMAN

Protein

DNA topoisomerase 2-alpha

Gene

TOP2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 3 (04 May 2001)
      Previous versions | rss
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    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 PublicationsPROSITE-ProRule annotation

    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+ Probable.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

    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

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

    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

    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. 3 Publications
    Mutagenesisi541 – 5411D → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. 3 Publications
    Mutagenesisi543 – 5431D → A or C: Impairs bending of target DNA. Strongly reduced DNA cleavage. 3 Publications
    Mutagenesisi545 – 5451D → A or C: Strongly reduced DNA cleavage. 2 Publications
    Mutagenesisi1469 – 14691S → A: Abolishes binding to the antibody MPM2. 2 Publications

    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-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.13 Publications

    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.4 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.
    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.
    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

    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:
    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

    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: October 1, 2014
    This is version 184 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

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