ATP-dependent DNA helicase II subunit 1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P32807 (KU70_YEAST)

Last modified June 16, 2009. Version 86. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    ATP-dependent DNA helicase II subunit 1
    EC=3.6.1.-
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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	602 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.
Subunit structure	Heterodimer of YKU70/HDF1 and YKU80/HDF2. Ref.1
Subcellular location	Nucleus. Telomere. Ref.9
Post-translational modification	Sumoylated by MMS21. Ref.18
Miscellaneous	Present with 892 molecules/cell in log phase SD medium. Ref.17
Sequence similarities	Belongs to the ku70 family. Contains 1 Ku domain.

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Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Cellular component	Chromosomal protein Nucleus Telomere
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	chromatin assembly or disassembly Inferred from direct assay. Source: SGD chromatin silencing at silent mating-type cassette Inferred from genetic interaction. Source: SGD double-strand break repair via break-induced replication Inferred from genetic interaction. Source: SGD double-strand break repair via nonhomologous end joining Inferred from direct assay. Source: SGD telomere maintenance Inferred from mutant phenotype. Source: SGD
Cellular component	DNA-dependent protein kinase-DNA ligase 4 complex Inferred from electronic annotation. Source: InterPro Ku70:Ku80 complex Inferred from direct assay. Source: SGD nuclear envelope Inferred from direct assay. Source: SGD nuclear telomeric heterochromatin Traceable author statement. Source: SGD
Molecular function	ATP-dependent DNA helicase activity Inferred from electronic annotation. Source: InterPro RNA binding Ref.15 Inferred from direct assay. Source: SGD damaged DNA binding Traceable author statement. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
YKU80	Q04437	1	EBI-8214,EBI-8224

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 602

602

ATP-dependent DNA helicase II subunit 1

PRO_0000210184

Regions

Domain

268 – 483

216

Amino acid modifications

Modified residue

370

Phosphoserine Ref.19

Modified residue

371

Phosphoserine Ref.19

Modified residue

372

Phosphoserine Ref.19

Natural variations

Natural variant

T → K in strain: ABYS 60 and SK1.

Natural variant

E → D in strain: ABYS 60, DBVPG6044, SK1 and YPS128.

Natural variant

230

T → A in strain: DBVPG6044.

Natural variant

368

F → I in strain: YPS128.

Natural variant

562

I → T in strain: ABYS 60, DBVPG6044, SK1 and YPS128.

Experimental info

Sequence conflict

S → P in CAA49840. Ref.1

Sequence conflict

R → T in AAT92882. Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

P32807-1 [UniParc].

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

602

70,647

        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

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References

	« Hide 'large scale' referencesShow '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: 8509423] [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: 8017106] [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: 16951060] [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. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	"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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"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: 8626469] [Abstract] Cited for: FUNCTION IN TELOMERE MAINTENANCE AND MATING-TYPE SWITCHING.
[7]	"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: 8668537] [Abstract] Cited for: FUNCTION.
[8]	"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: 9914366] [Abstract] Cited for: FUNCTION IN TELOMERIC GENE SILENCING.
[9]	"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: 9635192] [Abstract] Cited for: FUNCTION IN TELOMERE MAINTENANCE, SUBCELLULAR LOCATION.
[10]	"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: 9635193] [Abstract] Cited for: FUNCTION IN DOUBLE-STRAND DNA REPAIR AND TELOMERE MAINTENANCE.
[11]	"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: 9663392] [Abstract] Cited for: FUNCTION IN 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: 10675560] [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: 11046137] [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: 12138180] [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: 12975323] [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: 14585978] [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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[18]	"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: 15738391] [Abstract] Cited for: SUMOYLATION BY MMS21.
[19]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 AND SER-372, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	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.
PIR	S54591.
RefSeq	NP_014011.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2483N.
IntAct	P32807. 12 interactions.
Proteomic databases
PeptideAtlas	P32807.
PRIDE	P32807.
Genome annotation databases
Ensembl	YMR284W. Saccharomyces cerevisiae. [Contig view]
GeneID	855328.
GenomeReviews	Gene locus YMR284W in contig Z71257_GR.
KEGG	sce:YMR284W.
NMPDR	fig\|4932.3.peg.5069.
Organism-specific databases
CYGD	YMR284w.
SGD	S000004897. YKU70.
Yeast-GFP	Search...
Phylogenomic databases
OMA	P32807. LKLIGFR.
Gene expression databases
GermOnline	YMR284W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006164. DNA_helicase_ATP-dep_Ku. IPR006165. DNA_helicase_ATP-dep_Ku70. IPR005160. Ku_C. IPR005161. Ku_N. [Graphical view]
Pfam	PF02735. Ku. 1 hit. PF03730. Ku_C. 1 hit. PF03731. Ku_N. 1 hit. [Graphical view]
PIRSF	PIRSF003033. Ku70. 1 hit.
SMART	SM00559. Ku78. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	979046.

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Entry information

Entry name

KU70_YEAST

Accession

Primary (citable) accession number: P32807
Secondary accession number(s): P32498

Q6B267

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 1996
Last modified:	June 16, 2009
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents