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P32807

- KU70_YEAST

UniProt

P32807 - KU70_YEAST

Protein

ATP-dependent DNA helicase II subunit 1

Gene

YKU70

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    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.11 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent DNA helicase activity Source: InterPro
    3. damaged DNA binding Source: SGD
    4. protein binding Source: IntAct
    5. RNA binding Source: SGD
    6. telomeric DNA binding Source: InterPro

    GO - Biological processi

    1. chromatin assembly or disassembly Source: SGD
    2. chromatin silencing Source: SGD
    3. chromatin silencing at silent mating-type cassette Source: SGD
    4. double-strand break repair via break-induced replication Source: SGD
    5. double-strand break repair via homologous recombination Source: SGD
    6. double-strand break repair via nonhomologous end joining Source: SGD
    7. mitochondrial double-strand break repair via homologous recombination Source: SGD
    8. telomere maintenance Source: SGD

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32954-MONOMER.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:YKU70
    Synonyms:HDF1, NES24
    Ordered Locus Names:YMR284W
    ORF Names:YM8021.10
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR284w.
    SGDiS000004897. YKU70.

    Subcellular locationi

    Nucleus 1 Publication. Chromosometelomere 1 Publication

    GO - Cellular componenti

    1. Ku70:Ku80 complex Source: SGD
    2. nuclear chromatin Source: SGD
    3. nuclear envelope Source: SGD
    4. nuclear telomeric heterochromatin Source: SGD

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 602602ATP-dependent DNA helicase II subunit 1PRO_0000210184Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei370 – 3701Phosphoserine1 Publication
    Modified residuei371 – 3711Phosphoserine1 Publication
    Modified residuei372 – 3721Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated by MMS21.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP32807.
    PaxDbiP32807.
    PeptideAtlasiP32807.
    PRIDEiP32807.

    Expressioni

    Gene expression databases

    GenevestigatoriP32807.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    YKU80Q044373EBI-8214,EBI-8224

    Protein-protein interaction databases

    BioGridi35464. 323 interactions.
    DIPiDIP-2483N.
    IntActiP32807. 2 interactions.
    MINTiMINT-619653.

    Structurei

    3D structure databases

    ProteinModelPortaliP32807.
    SMRiP32807. Positions 30-518.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini268 – 483216KuAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ku70 family.Curated
    Contains 1 Ku domain.Curated

    Phylogenomic databases

    eggNOGiNOG305318.
    GeneTreeiENSGT00390000001422.
    KOiK10884.
    OMAiPPYLKLL.
    OrthoDBiEOG747PSQ.

    Family and domain databases

    Gene3Di1.10.1600.10. 1 hit.
    2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR006165. Ku70.
    IPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view]
    PANTHERiPTHR12604:SF2. PTHR12604:SF2. 1 hit.
    PfamiPF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF003033. Ku70. 1 hit.
    SMARTiSM00559. Ku78. 1 hit.
    [Graphical view]
    SUPFAMiSSF100939. SSF100939. 1 hit.
    SSF53300. SSF53300. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P32807-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRSVTNAFGN SGELNDQVDE TGYRKFDIHE GILFCIELSE TMFKESSDLE    50
    YKSPLLEILE SLDELMSQLV ITRPGTAIGC YFYYCNREDA KEGIYELFPL 100
    RDINATFMKK LNDLLEDLSS GRISLYDYFM FQQTGSEKQV RLSVLFTFML 150
    DTFLEEIPGQ KQLSNKRVFL FTDIDKPQEA QDIDERARLR RLTIDLFDNK 200
    VNFATFFIGY ADKPFDNEFY SDILQLGSHT NENTGLDSEF DGPSTKPIDA 250
    KYIKSRILRK KEVKRIMFQC PLILDEKTNF IVGVKGYTMY THEKAGVRYK 300
    LVYEHEDIRQ EAYSKRKFLN PITGEDVTGK TVKVYPYGDL DINLSDSQDQ 350
    IVMEAYTQKD AFLKIIGFRS SSKSIHYFNN IDKSSFIVPD EAKYEGSIRT 400
    LASLLKILRK KDKIAILWGK LKSNSHPSLY TLSPSSVKDY NEGFYLYRVP 450
    FLDEIRKFPS LLSYDDGSEH KLDYDNMKKV TQSIMGYFNL RDGYNPSDFK 500
    NPLLQKHYKV LHDYLLQIET TFDENETPNT KKDRMMREDD SLRKLYYIRN 550
    KILESEKSED PIIQRLNKYV KIWNMFYKKF NDDNISIKEE KKPFDKKPKF 600
    NI 602
    Length:602
    Mass (Da):70,647
    Last modified:February 1, 1996 - v2
    Checksum:iBD58160328EE6C6E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31S → P in CAA49840. (PubMed:8509423)Curated
    Sequence conflicti87 – 871R → T in AAT92882. (PubMed:9169872)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211T → K in strain: ABYS 60 and SK1.
    Natural varianti50 – 501E → D in strain: ABYS 60, DBVPG6044, SK1 and YPS128.
    Natural varianti230 – 2301T → A in strain: DBVPG6044.
    Natural varianti368 – 3681F → I in strain: YPS128.
    Natural varianti562 – 5621I → T in strain: ABYS 60, DBVPG6044, SK1 and YPS128.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS54591.
    RefSeqiNP_014011.1. NM_001182791.1.

    Genome annotation databases

    EnsemblFungiiYMR284W; YMR284W; YMR284W.
    GeneIDi855328.
    KEGGisce:YMR284W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S54591.
    RefSeqi NP_014011.1. NM_001182791.1.

    3D structure databases

    ProteinModelPortali P32807.
    SMRi P32807. Positions 30-518.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35464. 323 interactions.
    DIPi DIP-2483N.
    IntActi P32807. 2 interactions.
    MINTi MINT-619653.

    Proteomic databases

    MaxQBi P32807.
    PaxDbi P32807.
    PeptideAtlasi P32807.
    PRIDEi P32807.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR284W ; YMR284W ; YMR284W .
    GeneIDi 855328.
    KEGGi sce:YMR284W.

    Organism-specific databases

    CYGDi YMR284w.
    SGDi S000004897. YKU70.

    Phylogenomic databases

    eggNOGi NOG305318.
    GeneTreei ENSGT00390000001422.
    KOi K10884.
    OMAi PPYLKLL.
    OrthoDBi EOG747PSQ.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32954-MONOMER.

    Miscellaneous databases

    NextBioi 979046.
    PROi P32807.

    Gene expression databases

    Genevestigatori P32807.

    Family and domain databases

    Gene3Di 1.10.1600.10. 1 hit.
    2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR006165. Ku70.
    IPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view ]
    PANTHERi PTHR12604:SF2. PTHR12604:SF2. 1 hit.
    Pfami PF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF003033. Ku70. 1 hit.
    SMARTi SM00559. Ku78. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100939. SSF100939. 1 hit.
    SSF53300. SSF53300. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. 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. 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].

    Entry informationi

    Entry nameiKU70_YEAST
    AccessioniPrimary (citable) accession number: P32807
    Secondary accession number(s): D6W0B1
    , P32498, Q0P778, Q0P779, Q0P787, Q0P789, Q6B267
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 892 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3