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P06786

- TOP2_YEAST

UniProt

P06786 - TOP2_YEAST

Protein

DNA topoisomerase 2

Gene

TOP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      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.3 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+.2 PublicationsPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei70 – 701ATP
    Binding sitei99 – 991ATP
    Metal bindingi449 – 4491Magnesium 1; catalytic1 PublicationPROSITE-ProRule annotation
    Sitei477 – 4771Interaction with DNAPROSITE-ProRule annotation
    Sitei480 – 4801Interaction with DNA
    Metal bindingi526 – 5261Magnesium 1; catalytic1 PublicationPROSITE-ProRule annotation
    Metal bindingi526 – 5261Magnesium 21 PublicationPROSITE-ProRule annotation
    Metal bindingi528 – 5281Magnesium 21 PublicationPROSITE-ProRule annotation
    Sitei650 – 6501Interaction with DNA
    Sitei651 – 6511Interaction with DNA
    Sitei700 – 7001Interaction with DNA
    Sitei734 – 7341Interaction with DNAPROSITE-ProRule annotation
    Sitei740 – 7401Interaction with DNAPROSITE-ProRule annotation
    Sitei781 – 7811Transition state stabilizer
    Active sitei782 – 7821O-(5'-phospho-DNA)-tyrosine intermediate2 Publications
    Sitei833 – 8331Important for DNA bending; intercalates between base pairs of target DNA
    Sitei908 – 9081Interaction with DNAPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi127 – 1293ATP
    Nucleotide bindingi140 – 1478ATP
    Nucleotide bindingi365 – 3673ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: SGD
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. chromatin assembly or disassembly Source: SGD
    3. chromatin remodeling at centromere Source: SGD
    4. DNA strand elongation involved in DNA replication Source: SGD
    5. DNA topological change Source: SGD
    6. DNA unwinding involved in DNA replication Source: SGD
    7. mitotic DNA integrity checkpoint Source: SGD
    8. reciprocal meiotic recombination Source: SGD
    9. regulation of mitotic recombination Source: SGD
    10. replication fork progression beyond termination site Source: SGD

    Keywords - Molecular functioni

    Isomerase, Topoisomerase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33117-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA topoisomerase 2 (EC:5.99.1.3)
    Alternative name(s):
    DNA topoisomerase II
    Gene namesi
    Name:TOP2
    Synonyms:TOR3
    Ordered Locus Names:YNL088W
    ORF Names:N2244
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIV

    Organism-specific databases

    CYGDiYNL088w.
    SGDiS000005032. TOP2.

    Subcellular locationi

    GO - Cellular componenti

    1. DNA replication termination region Source: SGD
    2. nucleus Source: SGD
    3. synaptonemal complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi333 – 3364KKKK → AAAA: Reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding.
    Mutagenesisi333 – 3364KKKK → AEEA: Strongly reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding.
    Mutagenesisi690 – 6901R → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi697 – 6971D → A: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi700 – 7001K → A: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi704 – 7041R → A: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi736 – 7361H → A: No effect. 1 Publication
    Mutagenesisi781 – 7811R → A: Strongly reduced enzyme activity. 1 Publication
    Mutagenesisi782 – 7821Y → F: Loss of enzyme activity. 1 Publication
    Mutagenesisi828 – 8281N → A: Strongly reduced enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14281428DNA topoisomerase 2PRO_0000145387Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1086 – 10861Phosphothreonine; by CK21 Publication
    Modified residuei1087 – 10871Phosphoserine; by CK21 Publication
    Modified residuei1252 – 12521Phosphoserine1 Publication
    Modified residuei1258 – 12581Phosphothreonine; by CK21 Publication
    Modified residuei1266 – 12661Phosphoserine; by CK21 Publication
    Modified residuei1269 – 12691Phosphoserine; by CK21 Publication
    Modified residuei1272 – 12721Phosphoserine; by CK21 Publication
    Modified residuei1353 – 13531Phosphoserine; by CK21 Publication
    Modified residuei1356 – 13561Phosphoserine; by CK21 Publication
    Modified residuei1408 – 14081Phosphoserine; by CK21 Publication
    Modified residuei1423 – 14231Phosphoserine; by CK21 Publication

    Post-translational modificationi

    Phosphorylation enhances the activity. Stimulates decatenation activity.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP06786.
    PaxDbiP06786.
    PeptideAtlasiP06786.

    Expressioni

    Gene expression databases

    GenevestigatoriP06786.

    Interactioni

    Subunit structurei

    Homodimer.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PKC1P245832EBI-19352,EBI-9860

    Protein-protein interaction databases

    BioGridi35735. 76 interactions.
    DIPiDIP-2300N.
    IntActiP06786. 19 interactions.
    MINTiMINT-495862.

    Structurei

    Secondary structure

    1
    1428
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 114
    Beta strandi12 – 143
    Helixi17 – 237
    Helixi26 – 294
    Beta strandi35 – 439
    Turni44 – 474
    Beta strandi48 – 569
    Helixi58 – 7720
    Beta strandi83 – 897
    Turni90 – 934
    Beta strandi94 – 1029
    Turni110 – 1123
    Helixi116 – 1227
    Beta strandi123 – 1286
    Helixi145 – 1517
    Beta strandi153 – 16210
    Turni163 – 1664
    Beta strandi167 – 1748
    Turni175 – 1784
    Beta strandi184 – 1874
    Beta strandi194 – 2018
    Helixi203 – 2064
    Helixi213 – 22917
    Beta strandi234 – 2374
    Helixi247 – 2526
    Turni253 – 2575
    Beta strandi280 – 2856
    Beta strandi288 – 2947
    Beta strandi296 – 2983
    Beta strandi300 – 3056
    Helixi315 – 33218
    Helixi342 – 3465
    Beta strandi349 – 3557
    Beta strandi362 – 3643
    Helixi374 – 3763
    Beta strandi377 – 3793
    Helixi385 – 3917
    Helixi395 – 40511
    Turni433 – 4364
    Helixi438 – 4425
    Beta strandi444 – 4507
    Helixi451 – 46414
    Beta strandi466 – 47510
    Beta strandi479 – 4813
    Helixi486 – 4916
    Helixi492 – 50211
    Turni503 – 5053
    Beta strandi506 – 5083
    Beta strandi513 – 5175
    Beta strandi519 – 5257
    Beta strandi527 – 5304
    Helixi534 – 54512
    Helixi547 – 5504
    Beta strandi555 – 5584
    Beta strandi563 – 5686
    Beta strandi574 – 5807
    Helixi581 – 59010
    Turni591 – 5944
    Beta strandi597 – 5993
    Helixi609 – 62921
    Helixi634 – 6429
    Helixi647 – 65610
    Beta strandi668 – 6703
    Helixi678 – 69114
    Turni695 – 6973
    Helixi701 – 71313
    Helixi721 – 73212
    Beta strandi736 – 7383
    Helixi741 – 7499
    Turni753 – 7553
    Beta strandi760 – 7656
    Turni770 – 7734
    Turni780 – 7823
    Beta strandi784 – 7874
    Helixi791 – 7944
    Helixi797 – 8026
    Beta strandi805 – 8084
    Beta strandi811 – 8166
    Helixi824 – 8274
    Beta strandi830 – 8334
    Beta strandi838 – 8414
    Helixi846 – 85712
    Beta strandi874 – 8807
    Beta strandi883 – 8875
    Beta strandi889 – 8946
    Beta strandi897 – 9026
    Helixi909 – 92012
    Beta strandi924 – 9263
    Beta strandi932 – 9354
    Beta strandi938 – 9403
    Beta strandi943 – 9464
    Helixi949 – 95810
    Helixi960 – 9634
    Beta strandi967 – 9715
    Beta strandi975 – 9784
    Beta strandi984 – 9896
    Helixi990 – 103445
    Beta strandi1041 – 10433
    Helixi1045 – 105410
    Turni1108 – 11103
    Helixi1114 – 11174
    Helixi1121 – 11244
    Helixi1126 – 114722
    Helixi1151 – 117626

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BGWX-ray2.70A409-1201[»]
    1BJTX-ray2.50A409-1201[»]
    1PVGX-ray1.80A/B1-413[»]
    1QZRX-ray1.90A/B1-413[»]
    2RGRX-ray3.00A419-1177[»]
    3L4JX-ray2.48A421-1177[»]
    3L4KX-ray2.98A421-1177[»]
    4GFHX-ray4.41A/F1-1177[»]
    DisProtiDP00076.
    ProteinModelPortaliP06786.
    SMRiP06786. Positions 8-405, 419-1177.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06786.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini443 – 557115ToprimPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni333 – 3364Interaction with DNA
    Regioni965 – 97410Interaction with DNA

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0187.
    GeneTreeiENSGT00390000016222.
    HOGENOMiHOG000216693.
    KOiK03164.
    OMAiKXKGRGA.
    OrthoDBiEOG7CCC0D.

    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. 2 hits.
    InterProiIPR024946. Arg_repress_C-like.
    IPR003594. HATPase_ATP-bd.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR001241. Topo_IIA.
    IPR002205. Topo_IIA_A/C.
    IPR013758. Topo_IIA_A/C_ab.
    IPR013757. Topo_IIA_A_a.
    IPR013506. Topo_IIA_bsu_dom2.
    IPR013759. Topo_IIA_cen_dom.
    IPR013760. Topo_IIA_like_dom.
    IPR018522. TopoIIA_CS.
    IPR006171. Toprim_domain.
    [Graphical view]
    PfamiPF00204. DNA_gyraseB. 1 hit.
    PF00521. DNA_topoisoIV. 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]

    Sequencei

    Sequence statusi: Complete.

    P06786-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTEPVSASD KYQKISQLEH ILKRPDTYIG SVETQEQLQW IYDEETDCMI     50
    EKNVTIVPGL FKIFDEILVN AADNKVRDPS MKRIDVNIHA EEHTIEVKND 100
    GKGIPIEIHN KENIYIPEMI FGHLLTSSNY DDDEKKVTGG RNGYGAKLCN 150
    IFSTEFILET ADLNVGQKYV QKWENNMSIC HPPKITSYKK GPSYTKVTFK 200
    PDLTRFGMKE LDNDILGVMR RRVYDINGSV RDINVYLNGK SLKIRNFKNY 250
    VELYLKSLEK KRQLDNGEDG AAKSDIPTIL YERINNRWEV AFAVSDISFQ 300
    QISFVNSIAT TMGGTHVNYI TDQIVKKISE ILKKKKKKSV KSFQIKNNMF 350
    IFINCLIENP AFTSQTKEQL TTRVKDFGSR CEIPLEYINK IMKTDLATRM 400
    FEIADANEEN ALKKSDGTRK SRITNYPKLE DANKAGTKEG YKCTLVLTEG 450
    DSALSLAVAG LAVVGRDYYG CYPLRGKMLN VREASADQIL KNAEIQAIKK 500
    IMGLQHRKKY EDTKSLRYGH LMIMTDQDHD GSHIKGLIIN FLESSFPGLL 550
    DIQGFLLEFI TPIIKVSITK PTKNTIAFYN MPDYEKWREE ESHKFTWKQK 600
    YYKGLGTSLA QEVREYFSNL DRHLKIFHSL QGNDKDYIDL AFSKKKADDR 650
    KEWLRQYEPG TVLDPTLKEI PISDFINKEL ILFSLADNIR SIPNVLDGFK 700
    PGQRKVLYGC FKKNLKSELK VAQLAPYVSE CTAYHHGEQS LAQTIIGLAQ 750
    NFVGSNNIYL LLPNGAFGTR ATGGKDAAAA RYIYTELNKL TRKIFHPADD 800
    PLYKYIQEDE KTVEPEWYLP ILPMILVNGA EGIGTGWSTY IPPFNPLEII 850
    KNIRHLMNDE ELEQMHPWFR GWTGTIEEIE PLRYRMYGRI EQIGDNVLEI 900
    TELPARTWTS TIKEYLLLGL SGNDKIKPWI KDMEEQHDDN IKFIITLSPE 950
    EMAKTRKIGF YERFKLISPI SLMNMVAFDP HGKIKKYNSV NEILSEFYYV 1000
    RLEYYQKRKD HMSERLQWEV EKYSFQVKFI KMIIEKELTV TNKPRNAIIQ 1050
    ELENLGFPRF NKEGKPYYGS PNDEIAEQIN DVKGATSDEE DEESSHEDTE 1100
    NVINGPEELY GTYEYLLGMR IWSLTKERYQ KLLKQKQEKE TELENLLKLS 1150
    AKDIWNTDLK AFEVGYQEFL QRDAEARGGN VPNKGSKTKG KGKRKLVDDE 1200
    DYDPSKKNKK STARKGKKIK LEDKNFERIL LEQKLVTKSK APTKIKKEKT 1250
    PSVSETKTEE EENAPSSTSS SSIFDIKKED KDEGELSKIS NKFKKISTIF 1300
    DKMGSTSATS KENTPEQDDV ATKKNQTTAK KTAVKPKLAK KPVRKQQKVV 1350
    ELSGESDLEI LDSYTDREDS NKDEDDAIPQ RSRRQRSSRA ASVPKKSYVE 1400
    TLELSDDSFI EDDEEENQGS DVSFNEED 1428
    Length:1,428
    Mass (Da):164,215
    Last modified:February 1, 1996 - v2
    Checksum:i0E29EB8B89AA1387
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741N → NN in AAB36610. (PubMed:3017975)Curated
    Sequence conflicti547 – 5471P → L in AAB36610. (PubMed:3017975)Curated
    Sequence conflicti837 – 8371W → R in AAB36610. (PubMed:3017975)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13814 Genomic DNA. Translation: AAB36610.1.
    AF458969 Genomic DNA. Translation: AAM00518.1.
    AF458971 Genomic DNA. Translation: AAM00530.1.
    AF458972 Genomic DNA. Translation: AAM00536.1.
    X89016 Genomic DNA. Translation: CAA61422.1.
    Z71364 Genomic DNA. Translation: CAA95964.1.
    BK006947 Genomic DNA. Translation: DAA10457.1.
    PIRiS57534. ISBYT2.
    RefSeqiNP_014311.3. NM_001182926.3.

    Genome annotation databases

    EnsemblFungiiYNL088W; YNL088W; YNL088W.
    GeneIDi855636.
    KEGGisce:YNL088W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13814 Genomic DNA. Translation: AAB36610.1 .
    AF458969 Genomic DNA. Translation: AAM00518.1 .
    AF458971 Genomic DNA. Translation: AAM00530.1 .
    AF458972 Genomic DNA. Translation: AAM00536.1 .
    X89016 Genomic DNA. Translation: CAA61422.1 .
    Z71364 Genomic DNA. Translation: CAA95964.1 .
    BK006947 Genomic DNA. Translation: DAA10457.1 .
    PIRi S57534. ISBYT2.
    RefSeqi NP_014311.3. NM_001182926.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BGW X-ray 2.70 A 409-1201 [» ]
    1BJT X-ray 2.50 A 409-1201 [» ]
    1PVG X-ray 1.80 A/B 1-413 [» ]
    1QZR X-ray 1.90 A/B 1-413 [» ]
    2RGR X-ray 3.00 A 419-1177 [» ]
    3L4J X-ray 2.48 A 421-1177 [» ]
    3L4K X-ray 2.98 A 421-1177 [» ]
    4GFH X-ray 4.41 A/F 1-1177 [» ]
    DisProti DP00076.
    ProteinModelPortali P06786.
    SMRi P06786. Positions 8-405, 419-1177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35735. 76 interactions.
    DIPi DIP-2300N.
    IntActi P06786. 19 interactions.
    MINTi MINT-495862.

    Chemistry

    ChEMBLi CHEMBL5290.

    Proteomic databases

    MaxQBi P06786.
    PaxDbi P06786.
    PeptideAtlasi P06786.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YNL088W ; YNL088W ; YNL088W .
    GeneIDi 855636.
    KEGGi sce:YNL088W.

    Organism-specific databases

    CYGDi YNL088w.
    SGDi S000005032. TOP2.

    Phylogenomic databases

    eggNOGi COG0187.
    GeneTreei ENSGT00390000016222.
    HOGENOMi HOG000216693.
    KOi K03164.
    OMAi KXKGRGA.
    OrthoDBi EOG7CCC0D.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33117-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06786.
    NextBioi 979854.

    Gene expression databases

    Genevestigatori P06786.

    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. 2 hits.
    InterProi IPR024946. Arg_repress_C-like.
    IPR003594. HATPase_ATP-bd.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR001241. Topo_IIA.
    IPR002205. Topo_IIA_A/C.
    IPR013758. Topo_IIA_A/C_ab.
    IPR013757. Topo_IIA_A_a.
    IPR013506. Topo_IIA_bsu_dom2.
    IPR013759. Topo_IIA_cen_dom.
    IPR013760. Topo_IIA_like_dom.
    IPR018522. TopoIIA_CS.
    IPR006171. Toprim_domain.
    [Graphical view ]
    Pfami PF00204. DNA_gyraseB. 1 hit.
    PF00521. DNA_topoisoIV. 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. "The complete nucleotide sequence of the structural gene TOP2 of yeast DNA topoisomerase II."
      Giaever F., Lynn R., Goto T., Wang J.C.
      J. Biol. Chem. 261:12448-12454(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Dissecting the architecture of a quantitative trait locus in yeast."
      Steinmetz L.M., Sinha H., Richards D.R., Spiegelman J.I., Oefner P.J., McCusker J.H., Davis R.W.
      Nature 416:326-330(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: S96, YJM 320 and YJM 326.
    3. "The sequence of a 17,933 bp segment of Saccharomyces cerevisiae chromosome XIV contains the RHO2, TOP2, MKT1 and END3 genes and five new open reading frames."
      Soler-Mira A., Saiz J.E., Ballesta J.P.G., Remacha M.A.
      Yeast 12:485-491(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
      Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
      , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
      Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "Topoisomerase II: its functions and phosphorylation."
      Gasser S.M., Walter R., Dang Q., Cardenas M.E.
      Antonie Van Leeuwenhoek 62:15-24(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON PHOSPHORYLATION.
    7. "Casein kinase II phosphorylates the eukaryote-specific C-terminal domain of topoisomerase II in vivo."
      Cardenas M.E., Dang Q., Glover C.V., Gasser S.M.
      EMBO J. 11:1785-1796(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-1086; SER-1087; THR-1258; SER-1266; SER-1269; SER-1272; SER-1353; SER-1356; SER-1408 AND SER-1423.
    8. "Identification of active site residues in the 'GyrA' half of yeast DNA topoisomerase II."
      Liu Q., Wang J.C.
      J. Biol. Chem. 273:20252-20260(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, ACTIVE SITE, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF ARG-690; ASP-697; LYS-700; ARG-704; HIS-736; ARG-781; TYR-782 AND ASN-828.
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1252, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structure and mechanism of DNA topoisomerase II."
      Berger J.M., Gamblin S.J., Harrison S.C., Wang J.C.
      Nature 379:225-232(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 410-1202.
    14. "Quaternary changes in topoisomerase II may direct orthogonal movement of two DNA strands."
      Fass D., Bogden C.E., Berger J.M.
      Nat. Struct. Biol. 6:322-326(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 409-1201.
    15. "Structure of the topoisomerase II ATPase region and its mechanism of inhibition by the chemotherapeutic agent ICRF-187."
      Classen S., Olland S., Berger J.M.
      Proc. Natl. Acad. Sci. U.S.A. 100:10629-10634(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-413 IN COMPLEX WITH ATP ANALOG, SUBUNIT.
    16. "Structural basis for gate-DNA recognition and bending by type IIA topoisomerases."
      Dong K.C., Berger J.M.
      Nature 450:1201-1205(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 419-1177 IN COMPLEX WITH DNA AND MAGNESIUM, CATALYTIC ACTIVITY, COFACTOR.
    17. "A novel and unified two-metal mechanism for DNA cleavage by type II and IA topoisomerases."
      Schmidt B.H., Burgin A.B., Deweese J.E., Osheroff N., Berger J.M.
      Nature 465:641-644(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 421-1177 IN COMPLEX WITH DNA AND ZINC IONS, ACTIVE SITE, ENZYME MECHANISM, COFACTOR.
    18. "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: X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS) OF 1-1177 IN COMPLEX WITH DNA AND ATP ANALOG, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT.

    Entry informationi

    Entry nameiTOP2_YEAST
    AccessioniPrimary (citable) accession number: P06786
    Secondary accession number(s): D6W191
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 173 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In yeast topoisomerase II can substitute topoisomerase I for the relaxing activity.
    Eukaryotic topoisomerase I and II can relax both negative and positive supercoils, whereas prokaryotic enzymes relax only negative supercoils.
    Present with 5730 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

    External Data

    Dasty 3