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P32807 (KU70_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 132. 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 1

EC=3.6.4.12
Alternative name(s):
ATP-dependent DNA helicase II subunit Ku70
High affinity DNA-binding factor subunit 1
Gene names
Name:YKU70
Synonyms:HDF1, NES24
Ordered Locus Names:YMR284W
ORF Names:YM8021.10
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length602 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.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Heterodimer of YKU70/HDF1 and YKU80/HDF2. Ref.1

Subcellular location

Nucleus. Chromosometelomere Ref.10.

Post-translational modification

Sumoylated by MMS21. Ref.19

Miscellaneous

Present with 892 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ku70 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
   PTMPhosphoprotein
Ubl conjugation
   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

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype PubMed 18791224. Source: SGD

double-strand break repair via break-induced replication

Inferred from mutant phenotype PubMed 17321803. 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 mutant phenotype PubMed 10908335. Source: SGD

mitochondrial double-strand break repair via homologous recombination

Inferred from mutant phenotype PubMed 22214610. 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 envelope

Inferred from direct assay PubMed 10638763. 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

RNA binding

Inferred from direct assay Ref.16. Source: SGD

damaged DNA binding

Traceable author statement PubMed 10367891. Source: SGD

protein binding

Inferred from physical interaction PubMed 11805826PubMed 16429126. Source: IntAct

telomeric DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YKU80Q044373EBI-8214,EBI-8224

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 602602ATP-dependent DNA helicase II subunit 1
PRO_0000210184

Regions

Domain268 – 483216Ku

Amino acid modifications

Modified residue3701Phosphoserine Ref.20
Modified residue3711Phosphoserine Ref.20
Modified residue3721Phosphoserine Ref.20

Natural variations

Natural variant211T → K in strain: ABYS 60 and SK1.
Natural variant501E → D in strain: ABYS 60, DBVPG6044, SK1 and YPS128.
Natural variant2301T → A in strain: DBVPG6044.
Natural variant3681F → I in strain: YPS128.
Natural variant5621I → T in strain: ABYS 60, DBVPG6044, SK1 and YPS128.

Experimental info

Sequence conflict31S → P in CAA49840. Ref.1
Sequence conflict871R → T in AAT92882. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P32807 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: BD58160328EE6C6E

FASTA60270,647
        10         20         30         40         50         60 
MRSVTNAFGN SGELNDQVDE TGYRKFDIHE GILFCIELSE TMFKESSDLE YKSPLLEILE 

        70         80         90        100        110        120 
SLDELMSQLV ITRPGTAIGC YFYYCNREDA KEGIYELFPL RDINATFMKK LNDLLEDLSS 

       130        140        150        160        170        180 
GRISLYDYFM FQQTGSEKQV RLSVLFTFML DTFLEEIPGQ KQLSNKRVFL FTDIDKPQEA 

       190        200        210        220        230        240 
QDIDERARLR RLTIDLFDNK VNFATFFIGY ADKPFDNEFY SDILQLGSHT NENTGLDSEF 

       250        260        270        280        290        300 
DGPSTKPIDA KYIKSRILRK KEVKRIMFQC PLILDEKTNF IVGVKGYTMY THEKAGVRYK 

       310        320        330        340        350        360 
LVYEHEDIRQ EAYSKRKFLN PITGEDVTGK TVKVYPYGDL DINLSDSQDQ IVMEAYTQKD 

       370        380        390        400        410        420 
AFLKIIGFRS SSKSIHYFNN IDKSSFIVPD EAKYEGSIRT LASLLKILRK KDKIAILWGK 

       430        440        450        460        470        480 
LKSNSHPSLY TLSPSSVKDY NEGFYLYRVP FLDEIRKFPS LLSYDDGSEH KLDYDNMKKV 

       490        500        510        520        530        540 
TQSIMGYFNL RDGYNPSDFK NPLLQKHYKV LHDYLLQIET TFDENETPNT KKDRMMREDD 

       550        560        570        580        590        600 
SLRKLYYIRN KILESEKSED PIIQRLNKYV KIWNMFYKKF NDDNISIKEE KKPFDKKPKF 


NI 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 4-20, SUBUNIT.
Strain: ABYS 60.
[2]"Cloning and sequencing of the NES24 gene of Saccharomyces cerevisiae."
Yoshida M., Shimma Y., Uno I., Toh-e A.
Yeast 10:371-376(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"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, DBVPG3051, DBVPG6044, DBVPG6763, DBVPG6765, SK1 and Y55.
[4]"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.
[5]"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.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"Involvement of the Saccharomyces cerevisiae HDF1 gene in DNA double-strand break repair and recombination."
Mages G.J., Feldmann H.M., Winnacker E.-L.
J. Biol. Chem. 271:7910-7915(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TELOMERE MAINTENANCE AND MATING-TYPE SWITCHING.
[8]"Hdf1, a yeast Ku-protein homologue, is involved in illegitimate recombination, but not in homologous recombination."
Tsukamoto Y., Kato J., Ideka H.
Nucleic Acids Res. 24:2067-2072(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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].
[19]"A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization."
Zhao X., Blobel G.
Proc. Natl. Acad. Sci. U.S.A. 102:4777-4782(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION BY MMS21.
[20]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 AND SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70379 Genomic DNA. Translation: CAA49840.1.
D15052 Genomic DNA. Translation: BAA03648.1.
AM296304 Genomic DNA. Translation: CAL36013.1.
AM296302 Genomic DNA. Translation: CAL36015.1.
AM296301 Genomic DNA. Translation: CAL36016.1.
AM296299 Genomic DNA. Translation: CAL36018.1.
AM296298 Genomic DNA. Translation: CAL36019.1.
AM296297 Genomic DNA. Translation: CAL36020.1.
AM296296 Genomic DNA. Translation: CAL36021.1.
AM296294 Genomic DNA. Translation: CAL36023.1.
AM296292 Genomic DNA. Translation: CAL36025.1.
AM296295 Genomic DNA. Translation: CAL36022.1.
AM296303 Genomic DNA. Translation: CAL36014.1.
AM296293 Genomic DNA. Translation: CAL36024.1.
Z49704 Genomic DNA. Translation: CAA89782.1.
AY692863 Genomic DNA. Translation: AAT92882.1.
BK006946 Genomic DNA. Translation: DAA10185.1.
PIRS54591.
RefSeqNP_014011.1. NM_001182791.1.

3D structure databases

ProteinModelPortalP32807.
SMRP32807. Positions 30-518.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35464. 323 interactions.
DIPDIP-2483N.
IntActP32807. 2 interactions.
MINTMINT-619653.

Proteomic databases

MaxQBP32807.
PaxDbP32807.
PeptideAtlasP32807.
PRIDEP32807.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR284W; YMR284W; YMR284W.
GeneID855328.
KEGGsce:YMR284W.

Organism-specific databases

CYGDYMR284w.
SGDS000004897. YKU70.

Phylogenomic databases

eggNOGNOG305318.
GeneTreeENSGT00390000001422.
KOK10884.
OMAPPYLKLL.
OrthoDBEOG747PSQ.

Enzyme and pathway databases

BioCycYEAST:G3O-32954-MONOMER.

Gene expression databases

GenevestigatorP32807.

Family and domain databases

Gene3D1.10.1600.10. 1 hit.
2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
InterProIPR006165. Ku70.
IPR006164. Ku70/Ku80_beta-barrel_dom.
IPR005160. Ku_C.
IPR005161. Ku_N.
IPR016194. SPOC_like_C_dom.
IPR002035. VWF_A.
[Graphical view]
PANTHERPTHR12604:SF2. PTHR12604:SF2. 1 hit.
PfamPF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
[Graphical view]
PIRSFPIRSF003033. Ku70. 1 hit.
SMARTSM00559. Ku78. 1 hit.
[Graphical view]
SUPFAMSSF100939. SSF100939. 1 hit.
SSF53300. SSF53300. 1 hit.
ProtoNetSearch...

Other

NextBio979046.
PROP32807.

Entry information

Entry nameKU70_YEAST
AccessionPrimary (citable) accession number: P32807
Secondary accession number(s): D6W0B1 expand/collapse secondary AC list , P32498, Q0P778, Q0P779, Q0P787, Q0P789, Q6B267
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 132 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 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