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P06786 (TOP2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA topoisomerase 2

EC=5.99.1.3
Alternative name(s):
DNA topoisomerase II
Gene names
Name:TOP2
Synonyms:TOR3
Ordered Locus Names:YNL088W
ORF Names:N2244
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1428 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.18

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. Ref.8 Ref.16 Ref.18

Cofactor

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+. Ref.16 Ref.17

Subunit structure

Homodimer. Ref.8 Ref.15 Ref.18

Subcellular location

Nucleus.

Post-translational modification

Phosphorylation enhances the activity. Stimulates decatenation activity.

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.

Sequence similarities

Belongs to the type II topoisomerase family.

Contains 1 Toprim domain.

Ontologies

Keywords
   Cellular componentNucleus
   LigandATP-binding
DNA-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionIsomerase
Topoisomerase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 6088500PubMed 6323017. Source: GOC

DNA strand elongation involved in DNA replication

Inferred from mutant phenotype PubMed 2549254. Source: SGD

DNA topological change

Inferred from direct assay PubMed 6088500. Source: SGD

DNA unwinding involved in DNA replication

Inferred from mutant phenotype PubMed 24062159. Source: SGD

chromatin assembly or disassembly

Inferred from mutant phenotype PubMed 9199287. Source: SGD

chromatin remodeling at centromere

Inferred from mutant phenotype PubMed 18701701. Source: SGD

mitotic DNA integrity checkpoint

Inferred from mutant phenotype PubMed 16651657. Source: SGD

reciprocal meiotic recombination

Inferred from mutant phenotype PubMed 2156624. Source: SGD

regulation of mitotic recombination

Inferred from mutant phenotype PubMed 2902925. Source: SGD

replication fork progression beyond termination site

Inferred from mutant phenotype PubMed 20797631. Source: SGD

   Cellular_componentDNA replication termination region

Inferred from physical interaction PubMed 20797631. Source: SGD

nucleus

Inferred from direct assay PubMed 6088500. Source: SGD

synaptonemal complex

Inferred from direct assay PubMed 1315786. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase type II (ATP-hydrolyzing) activity

Inferred from direct assay PubMed 6088500PubMed 6323017. Source: SGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PKC1P245832EBI-19352,EBI-9860

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14281428DNA topoisomerase 2
PRO_0000145387

Regions

Domain443 – 557115Toprim
Nucleotide binding127 – 1293ATP
Nucleotide binding140 – 1478ATP
Nucleotide binding365 – 3673ATP
Region333 – 3364Interaction with DNA
Region965 – 97410Interaction with DNA

Sites

Active site7821O-(5'-phospho-DNA)-tyrosine intermediate Ref.8 Ref.17
Metal binding4491Magnesium 1; catalytic
Metal binding5261Magnesium 1; catalytic
Metal binding5261Magnesium 2
Metal binding5281Magnesium 2
Binding site701ATP
Binding site991ATP
Site4771Interaction with DNA By similarity
Site4801Interaction with DNA
Site6501Interaction with DNA
Site6511Interaction with DNA
Site7001Interaction with DNA
Site7341Interaction with DNA By similarity
Site7401Interaction with DNA By similarity
Site7811Transition state stabilizer
Site8331Important for DNA bending; intercalates between base pairs of target DNA
Site9081Interaction with DNA By similarity

Amino acid modifications

Modified residue10861Phosphothreonine; by CK2 Ref.7
Modified residue10871Phosphoserine; by CK2 Ref.7
Modified residue12521Phosphoserine Ref.12
Modified residue12581Phosphothreonine; by CK2 Ref.7
Modified residue12661Phosphoserine; by CK2 Ref.7
Modified residue12691Phosphoserine; by CK2 Ref.7
Modified residue12721Phosphoserine; by CK2 Ref.7
Modified residue13531Phosphoserine; by CK2 Ref.7
Modified residue13561Phosphoserine; by CK2 Ref.7
Modified residue14081Phosphoserine; by CK2 Ref.7
Modified residue14231Phosphoserine; by CK2 Ref.7

Experimental info

Mutagenesis333 – 3364KKKK → AAAA: Reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding.
Mutagenesis333 – 3364KKKK → AEEA: Strongly reduced enzyme activity; abolishes stimulation of ATPase activity upon DNA binding.
Mutagenesis6901R → A: Loss of enzyme activity. Ref.8
Mutagenesis6971D → A: Strongly reduced enzyme activity. Ref.8
Mutagenesis7001K → A: Strongly reduced enzyme activity. Ref.8
Mutagenesis7041R → A: Strongly reduced enzyme activity. Ref.8
Mutagenesis7361H → A: No effect. Ref.8
Mutagenesis7811R → A: Strongly reduced enzyme activity. Ref.8
Mutagenesis7821Y → F: Loss of enzyme activity. Ref.8
Mutagenesis8281N → A: Strongly reduced enzyme activity. Ref.8
Sequence conflict741N → NN in AAB36610. Ref.1
Sequence conflict5471P → L in AAB36610. Ref.1
Sequence conflict8371W → R in AAB36610. Ref.1

Secondary structure

............................................................................................................................................................................................... 1428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06786 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 0E29EB8B89AA1387

FASTA1,428164,215
        10         20         30         40         50         60 
MSTEPVSASD KYQKISQLEH ILKRPDTYIG SVETQEQLQW IYDEETDCMI EKNVTIVPGL 

        70         80         90        100        110        120 
FKIFDEILVN AADNKVRDPS MKRIDVNIHA EEHTIEVKND GKGIPIEIHN KENIYIPEMI 

       130        140        150        160        170        180 
FGHLLTSSNY DDDEKKVTGG RNGYGAKLCN IFSTEFILET ADLNVGQKYV QKWENNMSIC 

       190        200        210        220        230        240 
HPPKITSYKK GPSYTKVTFK PDLTRFGMKE LDNDILGVMR RRVYDINGSV RDINVYLNGK 

       250        260        270        280        290        300 
SLKIRNFKNY VELYLKSLEK KRQLDNGEDG AAKSDIPTIL YERINNRWEV AFAVSDISFQ 

       310        320        330        340        350        360 
QISFVNSIAT TMGGTHVNYI TDQIVKKISE ILKKKKKKSV KSFQIKNNMF IFINCLIENP 

       370        380        390        400        410        420 
AFTSQTKEQL TTRVKDFGSR CEIPLEYINK IMKTDLATRM FEIADANEEN ALKKSDGTRK 

       430        440        450        460        470        480 
SRITNYPKLE DANKAGTKEG YKCTLVLTEG DSALSLAVAG LAVVGRDYYG CYPLRGKMLN 

       490        500        510        520        530        540 
VREASADQIL KNAEIQAIKK IMGLQHRKKY EDTKSLRYGH LMIMTDQDHD GSHIKGLIIN 

       550        560        570        580        590        600 
FLESSFPGLL DIQGFLLEFI TPIIKVSITK PTKNTIAFYN MPDYEKWREE ESHKFTWKQK 

       610        620        630        640        650        660 
YYKGLGTSLA QEVREYFSNL DRHLKIFHSL QGNDKDYIDL AFSKKKADDR KEWLRQYEPG 

       670        680        690        700        710        720 
TVLDPTLKEI PISDFINKEL ILFSLADNIR SIPNVLDGFK PGQRKVLYGC FKKNLKSELK 

       730        740        750        760        770        780 
VAQLAPYVSE CTAYHHGEQS LAQTIIGLAQ NFVGSNNIYL LLPNGAFGTR ATGGKDAAAA 

       790        800        810        820        830        840 
RYIYTELNKL TRKIFHPADD PLYKYIQEDE KTVEPEWYLP ILPMILVNGA EGIGTGWSTY 

       850        860        870        880        890        900 
IPPFNPLEII KNIRHLMNDE ELEQMHPWFR GWTGTIEEIE PLRYRMYGRI EQIGDNVLEI 

       910        920        930        940        950        960 
TELPARTWTS TIKEYLLLGL SGNDKIKPWI KDMEEQHDDN IKFIITLSPE EMAKTRKIGF 

       970        980        990       1000       1010       1020 
YERFKLISPI SLMNMVAFDP HGKIKKYNSV NEILSEFYYV RLEYYQKRKD HMSERLQWEV 

      1030       1040       1050       1060       1070       1080 
EKYSFQVKFI KMIIEKELTV TNKPRNAIIQ ELENLGFPRF NKEGKPYYGS PNDEIAEQIN 

      1090       1100       1110       1120       1130       1140 
DVKGATSDEE DEESSHEDTE NVINGPEELY GTYEYLLGMR IWSLTKERYQ KLLKQKQEKE 

      1150       1160       1170       1180       1190       1200 
TELENLLKLS AKDIWNTDLK AFEVGYQEFL QRDAEARGGN VPNKGSKTKG KGKRKLVDDE 

      1210       1220       1230       1240       1250       1260 
DYDPSKKNKK STARKGKKIK LEDKNFERIL LEQKLVTKSK APTKIKKEKT PSVSETKTEE 

      1270       1280       1290       1300       1310       1320 
EENAPSSTSS SSIFDIKKED KDEGELSKIS NKFKKISTIF DKMGSTSATS KENTPEQDDV 

      1330       1340       1350       1360       1370       1380 
ATKKNQTTAK KTAVKPKLAK KPVRKQQKVV ELSGESDLEI LDSYTDREDS NKDEDDAIPQ 

      1390       1400       1410       1420 
RSRRQRSSRA ASVPKKSYVE TLELSDDSFI EDDEEENQGS DVSFNEED 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRISBYT2. S57534.
RefSeqNP_014311.3. NM_001182926.3.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00076.
ProteinModelPortalP06786.
SMRP06786. Positions 8-1177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35735. 76 interactions.
DIPDIP-2300N.
IntActP06786. 19 interactions.
MINTMINT-495862.

Chemistry

ChEMBLCHEMBL5290.

Proteomic databases

PaxDbP06786.
PeptideAtlasP06786.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL088W; YNL088W; YNL088W.
GeneID855636.
KEGGsce:YNL088W.

Organism-specific databases

CYGDYNL088w.
SGDS000005032. TOP2.

Phylogenomic databases

eggNOGCOG0187.
GeneTreeENSGT00390000016222.
HOGENOMHOG000216693.
KOK03164.
OMARHIDYVV.
OrthoDBEOG7CCC0D.

Enzyme and pathway databases

BioCycYEAST:G3O-33117-MONOMER.

Gene expression databases

GenevestigatorP06786.

Family and domain databases

Gene3D1.10.268.10. 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.
InterProIPR024946. 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]
PfamPF00204. DNA_gyraseB. 1 hit.
PF00521. DNA_topoisoIV. 1 hit.
PF02518. HATPase_c. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00418. TPI2FAMILY.
SMARTSM00387. HATPase_c. 1 hit.
SM00433. TOP2c. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
SSF56719. SSF56719. 1 hit.
PROSITEPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06786.
NextBio979854.

Entry information

Entry nameTOP2_YEAST
AccessionPrimary (citable) accession number: P06786
Secondary accession number(s): D6W191
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references