P32807 (KU70_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	602 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Chromosome › telomere 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 process	DNA damage DNA recombination DNA repair
Cellular component	Chromosome Nucleus Telomere
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chromatin assembly or disassembly Inferred from direct assay PubMed 11553718. 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 nonhomologous end joining Inferred from direct assay PubMed 10908335. Source: SGD telomere maintenance Inferred from mutant phenotype PubMed 10818099. Source: SGD
Cellular_component	Ku70:Ku80 complex Inferred from direct assay PubMed 8754818. Source: SGD nuclear envelope Inferred from direct assay PubMed 10638763. Source: SGD nuclear telomeric heterochromatin Traceable author statement PubMed 12080091. Source: SGD
Molecular_function	ATP 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 telomeric DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
YKU80	Q04437	3	EBI-8214,EBI-8224

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	Ku
Amino acid modifications
	Modified residue	370	1	Phosphoserine Ref.20
	Modified residue	371	1	Phosphoserine Ref.20
	Modified residue	372	1	Phosphoserine Ref.20
Natural variations
	Natural variant	21	1	T → K in strain: ABYS 60 and SK1.
	Natural variant	50	1	E → D in strain: ABYS 60, DBVPG6044, SK1 and YPS128.
	Natural variant	230	1	T → A in strain: DBVPG6044.
	Natural variant	368	1	F → I in strain: YPS128.
	Natural variant	562	1	I → T in strain: ABYS 60, DBVPG6044, SK1 and YPS128.
Experimental info
	Sequence conflict	3	1	S → P in CAA49840. Ref.1
	Sequence conflict	87	1	R → T in AAT92882. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P32807 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: BD58160328EE6C6E	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

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] [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. , 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 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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. , 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, MASS SPECTROMETRY.
+	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.
PIR	S54591.
RefSeq	NP_014011.1. NM_001182791.1.
3D structure databases
ProteinModelPortal	P32807.
SMR	P32807. Positions 30-518.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2483N.
IntAct	P32807. 8 interactions.
MINT	MINT-619653.
Proteomic databases
PaxDb	P32807.
PeptideAtlas	P32807.
PRIDE	P32807.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR284W; YMR284W; YMR284W.
GeneID	855328.
KEGG	sce:YMR284W.
Organism-specific databases
CYGD	YMR284w.
SGD	S000004897. YKU70.
Phylogenomic databases
eggNOG	NOG305318.
GeneTree	ENSGT00390000001422.
KO	K10884.
OMA	KPPYLKL.
OrthoDB	EOG46DQBC.
Gene expression databases
ArrayExpress	P32807.
Genevestigator	P32807.
GermOnline	YMR284W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.10.1600.10. 1 hit. 2.40.290.10. 1 hit.
InterPro	IPR006165. Ku70. IPR006164. Ku70/Ku80_beta-barrel_dom. IPR005160. Ku_C. IPR005161. Ku_N. IPR016194. SPOC_like_C_dom. [Graphical view]
PANTHER	PTHR12604:SF2. PTHR12604:SF2. 1 hit.
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]
SUPFAM	SSF100939. SPOC-like. 1 hit.
ProtoNet	Search...
Other
NextBio	979046.

Entry information

Entry name

KU70_YEAST

Accession

Primary (citable) accession number: P32807
Secondary accession number(s): D6W0B1 , P32498, Q0P778, Q0P779, Q0P787, Q0P789, Q6B267

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program