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P06786

- TOP2_YEAST

UniProt

P06786 - TOP2_YEAST

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Protein
DNA topoisomerase 2
Gene
TOP2, TOR3, YNL088W, N2244
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes.2 Publications

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.3 Publications

Cofactori

Magnesium. Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ and Ca2+.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei70 – 701ATP
Binding sitei99 – 991ATP
Metal bindingi449 – 4491Magnesium 1; catalytic
Sitei477 – 4771Interaction with DNA By similarity
Sitei480 – 4801Interaction with DNA
Metal bindingi526 – 5261Magnesium 1; catalytic
Metal bindingi526 – 5261Magnesium 2
Metal bindingi528 – 5281Magnesium 2
Sitei650 – 6501Interaction with DNA
Sitei651 – 6511Interaction with DNA
Sitei700 – 7001Interaction with DNA
Sitei734 – 7341Interaction with DNA By similarity
Sitei740 – 7401Interaction with DNA By similarity
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 DNA By similarity

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. DNA strand elongation involved in DNA replication Source: SGD
  3. DNA topological change Source: SGD
  4. DNA unwinding involved in DNA replication Source: SGD
  5. chromatin assembly or disassembly Source: SGD
  6. chromatin remodeling at centromere 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
Complete GO annotation...

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
Complete GO annotation...

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 2
PRO_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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP06786.
PaxDbiP06786.
PeptideAtlasiP06786.

Expressioni

Gene expression databases

GenevestigatoriP06786.

Interactioni

Subunit structurei

Homodimer.3 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

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.

Miscellaneous databases

EvolutionaryTraceiP06786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini443 – 557115Toprim
Add
BLAST

Region

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

Sequence similaritiesi

Contains 1 Toprim domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741N → NN in AAB36610. 1 Publication
Sequence conflicti547 – 5471P → L in AAB36610. 1 Publication
Sequence conflicti837 – 8371W → R in AAB36610. 1 Publication

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

« Hide 'large scale' publications
  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: June 11, 2014
This is version 172 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.

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

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