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P06786

- TOP2_YEAST

UniProt

P06786 - TOP2_YEAST

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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

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

Mg2+2 PublicationsPROSITE-ProRule annotation, Mn2+2 PublicationsPROSITE-ProRule annotation, Ca2+2 PublicationsPROSITE-ProRule annotationNote: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP06786.
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_C.
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

        10         20         30         40         50
MSTEPVSASD KYQKISQLEH ILKRPDTYIG SVETQEQLQW IYDEETDCMI
60 70 80 90 100
EKNVTIVPGL FKIFDEILVN AADNKVRDPS MKRIDVNIHA EEHTIEVKND
110 120 130 140 150
GKGIPIEIHN KENIYIPEMI FGHLLTSSNY DDDEKKVTGG RNGYGAKLCN
160 170 180 190 200
IFSTEFILET ADLNVGQKYV QKWENNMSIC HPPKITSYKK GPSYTKVTFK
210 220 230 240 250
PDLTRFGMKE LDNDILGVMR RRVYDINGSV RDINVYLNGK SLKIRNFKNY
260 270 280 290 300
VELYLKSLEK KRQLDNGEDG AAKSDIPTIL YERINNRWEV AFAVSDISFQ
310 320 330 340 350
QISFVNSIAT TMGGTHVNYI TDQIVKKISE ILKKKKKKSV KSFQIKNNMF
360 370 380 390 400
IFINCLIENP AFTSQTKEQL TTRVKDFGSR CEIPLEYINK IMKTDLATRM
410 420 430 440 450
FEIADANEEN ALKKSDGTRK SRITNYPKLE DANKAGTKEG YKCTLVLTEG
460 470 480 490 500
DSALSLAVAG LAVVGRDYYG CYPLRGKMLN VREASADQIL KNAEIQAIKK
510 520 530 540 550
IMGLQHRKKY EDTKSLRYGH LMIMTDQDHD GSHIKGLIIN FLESSFPGLL
560 570 580 590 600
DIQGFLLEFI TPIIKVSITK PTKNTIAFYN MPDYEKWREE ESHKFTWKQK
610 620 630 640 650
YYKGLGTSLA QEVREYFSNL DRHLKIFHSL QGNDKDYIDL AFSKKKADDR
660 670 680 690 700
KEWLRQYEPG TVLDPTLKEI PISDFINKEL ILFSLADNIR SIPNVLDGFK
710 720 730 740 750
PGQRKVLYGC FKKNLKSELK VAQLAPYVSE CTAYHHGEQS LAQTIIGLAQ
760 770 780 790 800
NFVGSNNIYL LLPNGAFGTR ATGGKDAAAA RYIYTELNKL TRKIFHPADD
810 820 830 840 850
PLYKYIQEDE KTVEPEWYLP ILPMILVNGA EGIGTGWSTY IPPFNPLEII
860 870 880 890 900
KNIRHLMNDE ELEQMHPWFR GWTGTIEEIE PLRYRMYGRI EQIGDNVLEI
910 920 930 940 950
TELPARTWTS TIKEYLLLGL SGNDKIKPWI KDMEEQHDDN IKFIITLSPE
960 970 980 990 1000
EMAKTRKIGF YERFKLISPI SLMNMVAFDP HGKIKKYNSV NEILSEFYYV
1010 1020 1030 1040 1050
RLEYYQKRKD HMSERLQWEV EKYSFQVKFI KMIIEKELTV TNKPRNAIIQ
1060 1070 1080 1090 1100
ELENLGFPRF NKEGKPYYGS PNDEIAEQIN DVKGATSDEE DEESSHEDTE
1110 1120 1130 1140 1150
NVINGPEELY GTYEYLLGMR IWSLTKERYQ KLLKQKQEKE TELENLLKLS
1160 1170 1180 1190 1200
AKDIWNTDLK AFEVGYQEFL QRDAEARGGN VPNKGSKTKG KGKRKLVDDE
1210 1220 1230 1240 1250
DYDPSKKNKK STARKGKKIK LEDKNFERIL LEQKLVTKSK APTKIKKEKT
1260 1270 1280 1290 1300
PSVSETKTEE EENAPSSTSS SSIFDIKKED KDEGELSKIS NKFKKISTIF
1310 1320 1330 1340 1350
DKMGSTSATS KENTPEQDDV ATKKNQTTAK KTAVKPKLAK KPVRKQQKVV
1360 1370 1380 1390 1400
ELSGESDLEI LDSYTDREDS NKDEDDAIPQ RSRRQRSSRA ASVPKKSYVE
1410 1420
TLELSDDSFI EDDEEENQGS DVSFNEED
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
InParanoidi P06786.
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_C.
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: November 26, 2014
This is version 175 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