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Q04437 (KU80_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
ATP-dependent DNA helicase II subunit 2

EC=3.6.4.12
Alternative name(s):
ATP-dependent DNA helicase II subunit Ku80
High affinity DNA-binding factor subunit 2
Yeast Ku80
Gene names
Name:YKU80
Synonyms:HDF2
Ordered Locus Names:YMR106C
ORF Names:YM9718.05C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length629 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Heterodimer of YKU70/HDF1 and YKU80/HDF2. Interacts with SIR4. Ref.4 Ref.5 Ref.18

Subcellular location

Nucleus. Chromosometelomere Ref.8.

Miscellaneous

Present with 358 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ku80 family.

Contains 1 Ku domain.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   Cellular componentChromosome
Nucleus
Telomere
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin assembly or disassembly

Inferred from direct assay PubMed 11553718. Source: SGD

chromatin silencing

Inferred from direct assay PubMed 9501103. Source: SGD

donor selection

Inferred from direct assay Ref.19. Source: SGD

double-strand break repair via homologous recombination

Inferred from mutant phenotype PubMed 11016833. Source: SGD

double-strand break repair via nonhomologous end joining

Inferred from electronic annotation. Source: InterPro

protein localization to chromosome

Inferred from genetic interaction PubMed 18716325. Source: SGD

telomere maintenance

Inferred from mutant phenotype PubMed 10818099. Source: SGD

   Cellular_componentKu70:Ku80 complex

Inferred from direct assay PubMed 8754818. Source: SGD

nuclear chromatin

Traceable author statement PubMed 10367891. Source: SGD

nuclear telomeric heterochromatin

Traceable author statement PubMed 12080091. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from direct assay Ref.19. Source: SGD

RNA binding

Inferred from direct assay Ref.15. Source: SGD

damaged DNA binding

Traceable author statement PubMed 10367891. Source: SGD

protein binding

Inferred from physical interaction PubMed 11805826Ref.18PubMed 16429126PubMed 22354040. Source: IntAct

telomeric DNA binding

Inferred from direct assay PubMed 17656141. Source: SGD

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 629629ATP-dependent DNA helicase II subunit 2
PRO_0000084339

Regions

Domain254 – 476223Ku

Natural variations

Natural variant1491L → V in strain: DBVPG6044, SK1 and YPS128.
Natural variant3011S → L in strain: DBVPG1853.
Natural variant3491N → D in strain: DBVPG6044, SK1 and YPS128.
Natural variant4991G → D in strain: DBVPG1853.
Natural variant5181E → A in strain: DBVPG6044, SK1 and YPS128.
Natural variant5281T → A in strain: DBVPG1853.
Natural variant5851I → S in strain: DBVPG6763.

Sequences

Sequence LengthMass (Da)Tools
Q04437 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 58126164EE375643

FASTA62971,241
        10         20         30         40         50         60 
MSSESTTFIV DVSPSMMKNN NVSKSMAYLE YTLLNKSKKS RKTDWISCYL ANCPVSENSQ 

        70         80         90        100        110        120 
EIPNVFQIQS FLAPVTTTAT IGFIKRLKQY CDQHSHDSSN EGLQSMIQCL LVVSLDIKQQ 

       130        140        150        160        170        180 
FQARKILKQI VVFTDNLDDL DITDEEIDLL TEELSTRIIL IDCGKDTQEE RKKSNWLKLV 

       190        200        210        220        230        240 
EAIPNSRIYN MNELLVEITS PATSVVKPVR VFSGELRLGA DILSTQTSNP SGSMQDENCL 

       250        260        270        280        290        300 
CIKVEAFPAT KAVSGLNRKT AVEVEDSQKK ERYVGVKSII EYEIHNEGNK KNVSEDDQSG 

       310        320        330        340        350        360 
SSYIPVTISK DSVTKAYRYG ADYVVLPSVL VDQTVYESFP GLDLRGFLNR EALPRYFLTS 

       370        380        390        400        410        420 
ESSFITADTR LGCQSDLMAF SALVDVMLEN RKIAVARYVS KKDSEVNMCA LCPVLIEHSN 

       430        440        450        460        470        480 
INSEKKFVKS LTLCRLPFAE DERVTDFPKL LDRTTTSGVP LKKETDGHQI DELMEQFVDS 

       490        500        510        520        530        540 
MDTDELPEIP LGNYYQPIGE VTTDTTLPLP SLNKDQEENK KDPLRIPTVF VYRQQQVLLE 

       550        560        570        580        590        600 
WIHQLMINDS REFEIPELPD SLKNKISPYT HKKFDSTKLV EVLGIKKVDK LKLDSELKTE 

       610        620 
LEREKIPDLE TLLKRGEQHS RGSPNNSNN 

« Hide

References

« Hide 'large scale' references
[1]"Sequence diversity, reproductive isolation and species concepts in Saccharomyces."
Liti G., Barton D.B., Louis E.J.
Genetics 174:839-850(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794, DBVPG1853, DBVPG3051, DBVPG6044, DBVPG6763, DBVPG6765, SK1, Y55 and YPS128.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"HDF2, the second subunit of the Ku homologue from Saccharomyces cerevisiae."
Feldmann H., Driller L., Meier B., Mages G., Kellermann J., Winnacker E.-L.
J. Biol. Chem. 271:27765-27769(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION IN TELOMERE MAINTENANCE, SUBUNIT.
[5]"A putative homologue of the human autoantigen Ku from Saccharomyces cerevisiae."
Feldmann H., Winnacker E.L.
J. Biol. Chem. 268:12895-12900(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[6]"Identification of a Saccharomyces cerevisiae Ku80 homologue: roles in DNA double strand break rejoining and in telomeric maintenance."
Boulton S.J., Jackson S.P.
Nucleic Acids Res. 24:4639-4648(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TELOMERE MAINTENANCE.
[7]"Telomerase, Ku, and telomeric silencing in Saccharomyces cerevisiae."
Evans S.K., Sistrunk M.L., Nugent C.I., Lundblad V.
Chromosoma 107:352-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TELOMERIC GENE SILENCING.
[8]"Mutation of yeast Ku genes disrupts the subnuclear organization of telomeres."
Laroche T., Martin S.G., Gotta M., Gorham H.C., Pryde F.E., Louis E.J., Gasser S.M.
Curr. Biol. 8:653-656(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TELOMERE MAINTENANCE, SUBCELLULAR LOCATION.
[9]"Telomere maintenance is dependent on activities required for end repair of double-strand breaks."
Nugent C.I., Bosco G., Ross L.O., Evans S.K., Salinger A.P., Moore J.K., Haber J.E., Lundblad V.
Curr. Biol. 8:657-660(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DOUBLE-STRAND DNA REPAIR AND TELOMERE MAINTENANCE.
[10]"The yeast Ku heterodimer is essential for protection of the telomere against nucleolytic and recombinational activities."
Polotnianka R.M., Li J., Lustig A.J.
Curr. Biol. 8:831-834(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TELOMERE MAINTENANCE.
[11]"Yeast Ku as a regulator of chromosomal DNA end structure."
Gravel S., Larrivee M., Labrecque P., Wellinger R.J.
Science 280:741-744(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CHROMOSOME END PROTECTION AND TELOMERE MAINTENANCE.
[12]"The Saccharomyces cerevisiae DNA damage checkpoint is required for efficient repair of double strand breaks by non-homologous end joining."
de la Torre-Ruiz M., Lowndes N.F.
FEBS Lett. 467:311-315(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NON-HOMOLOGOUS END JOINING DNA REPAIR.
[13]"Cdc13 cooperates with the yeast Ku proteins and Stn1 to regulate telomerase recruitment."
Grandin N., Damon C., Charbonneau M.
Mol. Cell. Biol. 20:8397-8408(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TELOMERASE AND CDC13 TELOMERE RECRUITMENT.
[14]"Involvement of replicative polymerases, Tel1p, Mec1p, Cdc13p, and the Ku complex in telomere-telomere recombination."
Tsai Y.-L., Tseng S.-F., Chang S.-H., Lin C.-C., Teng S.-C.
Mol. Cell. Biol. 22:5679-5687(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TELOMERE RECOMBINATION.
[15]"Ku interacts with telomerase RNA to promote telomere addition at native and broken chromosome ends."
Stellwagen A.E., Haimberger Z.W., Veatch J.R., Gottschling D.E.
Genes Dev. 17:2384-2395(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TELOMERIC REPAIR AND BINDING TO TLC1 STEM LOOP.
[16]"The Ku heterodimer performs separable activities at double-strand breaks and chromosome termini."
Bertuch A.A., Lundblad V.
Mol. Cell. Biol. 23:8202-8215(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DOUBLE-STRAND DNA REPAIR AND TELOMERE MAINTENANCE.
[17]"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].
[18]"Separation-of-function mutants of yeast Ku80 reveal a Yku80p-Sir4p interaction involved in telomeric silencing."
Roy R., Meier B., McAinsh A.D., Feldmann H.M., Jackson S.P.
J. Biol. Chem. 279:86-94(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TELOMERIC SILENCING, INTERACTION WITH SIR4.
[19]"The DNA repair protein yKu80 regulates the function of recombination enhancer during yeast mating type switching."
Ruan C., Workman J.L., Simpson R.T.
Mol. Cell. Biol. 25:8476-8485(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MATING-TYPE SWITCHING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM296333 Genomic DNA. Translation: CAL35984.1.
AM296334 Genomic DNA. Translation: CAL35983.1.
AM296335 Genomic DNA. Translation: CAL35982.1.
AM296336 Genomic DNA. Translation: CAL35981.1.
AM296337 Genomic DNA. Translation: CAL35980.1.
AM296338 Genomic DNA. Translation: CAL35979.1.
AM296339 Genomic DNA. Translation: CAL35978.1.
AM296340 Genomic DNA. Translation: CAL35977.1.
AM296341 Genomic DNA. Translation: CAL35976.1.
AM296342 Genomic DNA. Translation: CAL35975.1.
AM296343 Genomic DNA. Translation: CAL35974.1.
AM296344 Genomic DNA. Translation: CAL35973.1.
AM296345 Genomic DNA. Translation: CAL35972.1.
Z49702 Genomic DNA. Translation: CAA89742.1.
BK006946 Genomic DNA. Translation: DAA10003.1.
PIRS54567.
RefSeqNP_013824.1. NM_001182606.1.

3D structure databases

ProteinModelPortalQ04437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35281. 142 interactions.
DIPDIP-2757N.
IntActQ04437. 6 interactions.
MINTMINT-619682.
STRING4932.YMR106C.

Proteomic databases

MaxQBQ04437.
PaxDbQ04437.
PeptideAtlasQ04437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR106C; YMR106C; YMR106C.
GeneID855132.
KEGGsce:YMR106C.

Organism-specific databases

CYGDYMR106c.
SGDS000004712. YKU80.

Phylogenomic databases

eggNOGNOG238452.
HOGENOMHOG000066046.
KOK10885.
OMAYRYGADY.
OrthoDBEOG7TJ3SF.

Enzyme and pathway databases

BioCycYEAST:G3O-32803-MONOMER.

Gene expression databases

GenevestigatorQ04437.

Family and domain databases

Gene3D2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
InterProIPR006164. Ku70/Ku80_beta-barrel_dom.
IPR024193. Ku80.
IPR005160. Ku_C.
IPR005161. Ku_N.
IPR016194. SPOC_like_C_dom.
IPR002035. VWF_A.
[Graphical view]
PANTHERPTHR12604:SF3. PTHR12604:SF3. 1 hit.
PfamPF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
[Graphical view]
PIRSFPIRSF016570. Ku80. 1 hit.
SMARTSM00559. Ku78. 1 hit.
[Graphical view]
SUPFAMSSF100939. SSF100939. 2 hits.
SSF53300. SSF53300. 1 hit.
ProtoNetSearch...

Other

NextBio978505.
PROQ04437.

Entry information

Entry nameKU80_YEAST
AccessionPrimary (citable) accession number: Q04437
Secondary accession number(s): D6VZS9 expand/collapse secondary AC list , Q0P737, Q0P738, Q0P741, Q0P749
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families