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Protein

DNA topoisomerase 2

Gene

TOP2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP-dependent breakage, passage and rejoining of double-stranded DNA.PROSITE-ProRule annotation3 Publications

Cofactori

Mg2+PROSITE-ProRule annotation2 Publications, Mn2+PROSITE-ProRule annotation2 Publications, Ca2+PROSITE-ProRule annotation2 PublicationsNote: 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+ or Ca2+.PROSITE-ProRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei70ATP1 Publication1
Binding sitei99ATP1 Publication1
Metal bindingi449Magnesium 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi526Magnesium 1; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi526Magnesium 2PROSITE-ProRule annotation1 Publication1
Metal bindingi528Magnesium 2PROSITE-ProRule annotation1 Publication1
Sitei781Transition state stabilizer1
Active sitei782O-(5'-phospho-DNA)-tyrosine intermediate2 Publications1
Sitei833Important for DNA bending; intercalates between base pairs of target DNA1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi127 – 129ATP1 Publication3
Nucleotide bindingi140 – 147ATP1 Publication8
Nucleotide bindingi365 – 367ATP1 Publication3

GO - Molecular functioni

GO - Biological processi

  • chromatin assembly or disassembly Source: SGD
  • chromatin remodeling at centromere Source: SGD
  • DNA strand elongation involved in DNA replication Source: SGD
  • DNA topological change Source: SGD
  • DNA unwinding involved in DNA replication Source: SGD
  • mitotic DNA integrity checkpoint Source: SGD
  • reciprocal meiotic recombination Source: SGD
  • regulation of mitotic recombination Source: SGD
  • replication fork progression beyond termination site Source: SGD
  • resolution of meiotic recombination intermediates Source: GO_Central
  • sister chromatid segregation Source: GO_Central
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.
BRENDAi5.99.1.3. 984.
ReactomeiR-SCE-4615885. SUMOylation of DNA replication proteins.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL088W.
SGDiS000005032. TOP2.

Subcellular locationi

GO - Cellular componenti

  • DNA replication termination region Source: SGD
  • DNA topoisomerase complex (ATP-hydrolyzing) Source: GO_Central
  • nucleus Source: SGD
  • synaptonemal complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi333 – 336KKKK → AAAA: Reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. 4
Mutagenesisi333 – 336KKKK → AEEA: Strongly reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding. 4
Mutagenesisi690R → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi697D → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi700K → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi704R → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi736H → A: No effect. 1 Publication1
Mutagenesisi781R → A: Strongly reduced enzyme activity. 1 Publication1
Mutagenesisi782Y → F: Loss of enzyme activity. 1 Publication1
Mutagenesisi828N → A: Strongly reduced enzyme activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5290.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001453871 – 1428DNA topoisomerase 2Add BLAST1428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1086Phosphothreonine; by CK21 Publication1
Modified residuei1087Phosphoserine; by CK21 Publication1
Modified residuei1252PhosphoserineCombined sources1
Modified residuei1258Phosphothreonine; by CK21 Publication1
Modified residuei1266Phosphoserine; by CK21 Publication1
Modified residuei1269Phosphoserine; by CK21 Publication1
Modified residuei1272Phosphoserine; by CK21 Publication1
Modified residuei1353Phosphoserine; by CK21 Publication1
Modified residuei1356Phosphoserine; by CK21 Publication1
Modified residuei1408Phosphoserine; by CK21 Publication1
Modified residuei1423Phosphoserine; by CK21 Publication1

Post-translational modificationi

Phosphorylation enhances the activity. Stimulates decatenation activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP06786.
PRIDEiP06786.

PTM databases

iPTMnetiP06786.

Interactioni

Subunit structurei

Homodimer.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei477Interaction with DNAPROSITE-ProRule annotation1
Sitei480Interaction with DNA1 Publication1
Sitei650Interaction with DNA1 Publication1
Sitei651Interaction with DNA1 Publication1
Sitei700Interaction with DNA1 Publication1
Sitei734Interaction with DNAPROSITE-ProRule annotation1
Sitei740Interaction with DNAPROSITE-ProRule annotation1
Sitei908Interaction with DNAPROSITE-ProRule annotation1

Binary interactionsi

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

Protein-protein interaction databases

BioGridi35735. 82 interactors.
DIPiDIP-2300N.
IntActiP06786. 19 interactors.
MINTiMINT-495862.

Structurei

Secondary structure

11428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 11Combined sources4
Beta strandi12 – 14Combined sources3
Helixi17 – 23Combined sources7
Helixi26 – 29Combined sources4
Beta strandi35 – 43Combined sources9
Turni44 – 47Combined sources4
Beta strandi48 – 56Combined sources9
Helixi58 – 77Combined sources20
Beta strandi83 – 89Combined sources7
Turni90 – 93Combined sources4
Beta strandi94 – 102Combined sources9
Turni110 – 112Combined sources3
Helixi116 – 122Combined sources7
Beta strandi123 – 128Combined sources6
Helixi145 – 151Combined sources7
Beta strandi153 – 162Combined sources10
Turni163 – 166Combined sources4
Beta strandi167 – 174Combined sources8
Turni175 – 178Combined sources4
Beta strandi184 – 187Combined sources4
Beta strandi194 – 201Combined sources8
Helixi203 – 206Combined sources4
Helixi213 – 229Combined sources17
Beta strandi234 – 237Combined sources4
Helixi247 – 252Combined sources6
Turni253 – 257Combined sources5
Beta strandi280 – 285Combined sources6
Beta strandi288 – 294Combined sources7
Beta strandi296 – 298Combined sources3
Beta strandi300 – 305Combined sources6
Helixi315 – 332Combined sources18
Helixi342 – 346Combined sources5
Beta strandi349 – 355Combined sources7
Beta strandi362 – 364Combined sources3
Helixi374 – 376Combined sources3
Beta strandi377 – 379Combined sources3
Helixi385 – 391Combined sources7
Helixi395 – 405Combined sources11
Turni433 – 436Combined sources4
Helixi438 – 442Combined sources5
Beta strandi444 – 450Combined sources7
Helixi451 – 464Combined sources14
Beta strandi466 – 475Combined sources10
Beta strandi479 – 481Combined sources3
Helixi486 – 491Combined sources6
Helixi492 – 502Combined sources11
Turni503 – 505Combined sources3
Beta strandi506 – 508Combined sources3
Beta strandi513 – 517Combined sources5
Beta strandi519 – 525Combined sources7
Beta strandi527 – 530Combined sources4
Helixi534 – 545Combined sources12
Helixi547 – 550Combined sources4
Beta strandi555 – 558Combined sources4
Beta strandi563 – 568Combined sources6
Beta strandi574 – 580Combined sources7
Helixi581 – 590Combined sources10
Turni591 – 594Combined sources4
Beta strandi597 – 599Combined sources3
Helixi609 – 629Combined sources21
Helixi634 – 642Combined sources9
Helixi647 – 656Combined sources10
Beta strandi668 – 670Combined sources3
Helixi678 – 691Combined sources14
Turni695 – 697Combined sources3
Helixi701 – 713Combined sources13
Helixi721 – 732Combined sources12
Beta strandi736 – 738Combined sources3
Helixi741 – 749Combined sources9
Turni753 – 755Combined sources3
Beta strandi760 – 765Combined sources6
Turni770 – 773Combined sources4
Turni780 – 782Combined sources3
Beta strandi784 – 787Combined sources4
Helixi791 – 794Combined sources4
Helixi797 – 802Combined sources6
Beta strandi805 – 808Combined sources4
Beta strandi811 – 816Combined sources6
Helixi824 – 827Combined sources4
Beta strandi830 – 833Combined sources4
Beta strandi838 – 841Combined sources4
Helixi846 – 857Combined sources12
Beta strandi874 – 880Combined sources7
Beta strandi883 – 887Combined sources5
Beta strandi889 – 894Combined sources6
Beta strandi897 – 902Combined sources6
Helixi909 – 920Combined sources12
Beta strandi924 – 926Combined sources3
Beta strandi932 – 935Combined sources4
Beta strandi938 – 940Combined sources3
Beta strandi943 – 946Combined sources4
Helixi949 – 958Combined sources10
Helixi960 – 963Combined sources4
Beta strandi967 – 971Combined sources5
Beta strandi975 – 978Combined sources4
Beta strandi984 – 989Combined sources6
Helixi990 – 1034Combined sources45
Beta strandi1041 – 1043Combined sources3
Helixi1045 – 1054Combined sources10
Turni1108 – 1110Combined sources3
Helixi1114 – 1117Combined sources4
Helixi1121 – 1124Combined sources4
Helixi1126 – 1147Combined sources22
Helixi1151 – 1176Combined sources26

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06786.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini443 – 557ToprimPROSITE-ProRule annotationAdd BLAST115

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni333 – 336Interaction with DNA1 Publication4
Regioni965 – 974Interaction with DNA1 Publication10

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00390000016222.
HOGENOMiHOG000216693.
InParanoidiP06786.
KOiK03164.
OMAiTCSPDPR.
OrthoDBiEOG092C08KH.

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.
IPR013760. Topo_IIA-like_dom.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_dom.
IPR018522. TopoIIA_CS.
IPR031660. TOPRIM_C.
IPR006171. Toprim_domain.
[Graphical view]
PfamiPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
PF16898. TOPRIM_C. 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)DescriptionActionsGraphical viewLength
Sequence conflicti74N → NN in AAB36610 (PubMed:3017975).Curated1
Sequence conflicti547P → L in AAB36610 (PubMed:3017975).Curated1
Sequence conflicti837W → R in AAB36610 (PubMed:3017975).Curated1

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.
PIRiS57534. ISBYT2.
RefSeqiNP_014311.3. NM_001182926.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35735. 82 interactors.
DIPiDIP-2300N.
IntActiP06786. 19 interactors.
MINTiMINT-495862.

Chemistry databases

ChEMBLiCHEMBL5290.

PTM databases

iPTMnetiP06786.

Proteomic databases

MaxQBiP06786.
PRIDEiP06786.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YNL088W.
SGDiS000005032. TOP2.

Phylogenomic databases

GeneTreeiENSGT00390000016222.
HOGENOMiHOG000216693.
InParanoidiP06786.
KOiK03164.
OMAiTCSPDPR.
OrthoDBiEOG092C08KH.

Enzyme and pathway databases

BioCyciYEAST:G3O-33117-MONOMER.
BRENDAi5.99.1.3. 984.
ReactomeiR-SCE-4615885. SUMOylation of DNA replication proteins.

Miscellaneous databases

EvolutionaryTraceiP06786.
PROiP06786.

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.
IPR013760. Topo_IIA-like_dom.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013757. Topo_IIA_A_a.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_dom.
IPR018522. TopoIIA_CS.
IPR031660. TOPRIM_C.
IPR006171. Toprim_domain.
[Graphical view]
PfamiPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
PF16898. TOPRIM_C. 1 hit.
[Graphical view]
PRINTSiPR00418. TPI2FAMILY.
SMARTiSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEiPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 194 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

Similar proteinsi

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