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Q04437

- KU80_YEAST

UniProt

Q04437 - KU80_YEAST

Protein

ATP-dependent DNA helicase II subunit 2

Gene

YKU80

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 119 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      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.14 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. DNA binding Source: SGD
    5. protein binding Source: IntAct
    6. RNA binding Source: SGD
    7. telomeric DNA binding Source: SGD

    GO - Biological processi

    1. chromatin assembly or disassembly Source: SGD
    2. chromatin silencing Source: SGD
    3. donor selection Source: SGD
    4. double-strand break repair via homologous recombination Source: SGD
    5. double-strand break repair via nonhomologous end joining Source: InterPro
    6. protein localization to chromosome Source: SGD
    7. 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-32803-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:YKU80
    Synonyms:HDF2
    Ordered Locus Names:YMR106C
    ORF Names:YM9718.05C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    CYGDiYMR106c.
    SGDiS000004712. YKU80.

    Subcellular locationi

    Nucleus 1 Publication. Chromosometelomere 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Chromosome, Nucleus, Telomere

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 629629ATP-dependent DNA helicase II subunit 2PRO_0000084339Add
    BLAST

    Proteomic databases

    MaxQBiQ04437.
    PaxDbiQ04437.
    PeptideAtlasiQ04437.

    Expressioni

    Gene expression databases

    GenevestigatoriQ04437.

    Interactioni

    Subunit structurei

    Heterodimer of YKU70/HDF1 and YKU80/HDF2. Interacts with SIR4.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RFA1P223362EBI-8224,EBI-14971
    SIR4P119782EBI-8224,EBI-17237
    YKU70P328073EBI-8224,EBI-8214

    Protein-protein interaction databases

    BioGridi35281. 142 interactions.
    DIPiDIP-2757N.
    IntActiQ04437. 6 interactions.
    MINTiMINT-619682.
    STRINGi4932.YMR106C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ04437.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini254 – 476223KuAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ku80 family.Curated
    Contains 1 Ku domain.Curated

    Phylogenomic databases

    eggNOGiNOG238452.
    HOGENOMiHOG000066046.
    KOiK10885.
    OMAiYRYGADY.
    OrthoDBiEOG7TJ3SF.

    Family and domain databases

    Gene3Di2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR024193. Ku80.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view]
    PANTHERiPTHR12604:SF3. PTHR12604:SF3. 1 hit.
    PfamiPF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF016570. Ku80. 1 hit.
    SMARTiSM00559. Ku78. 1 hit.
    [Graphical view]
    SUPFAMiSSF100939. SSF100939. 2 hits.
    SSF53300. SSF53300. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q04437-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSESTTFIV DVSPSMMKNN NVSKSMAYLE YTLLNKSKKS RKTDWISCYL    50
    ANCPVSENSQ EIPNVFQIQS FLAPVTTTAT IGFIKRLKQY CDQHSHDSSN 100
    EGLQSMIQCL LVVSLDIKQQ FQARKILKQI VVFTDNLDDL DITDEEIDLL 150
    TEELSTRIIL IDCGKDTQEE RKKSNWLKLV EAIPNSRIYN MNELLVEITS 200
    PATSVVKPVR VFSGELRLGA DILSTQTSNP SGSMQDENCL CIKVEAFPAT 250
    KAVSGLNRKT AVEVEDSQKK ERYVGVKSII EYEIHNEGNK KNVSEDDQSG 300
    SSYIPVTISK DSVTKAYRYG ADYVVLPSVL VDQTVYESFP GLDLRGFLNR 350
    EALPRYFLTS ESSFITADTR LGCQSDLMAF SALVDVMLEN RKIAVARYVS 400
    KKDSEVNMCA LCPVLIEHSN INSEKKFVKS LTLCRLPFAE DERVTDFPKL 450
    LDRTTTSGVP LKKETDGHQI DELMEQFVDS MDTDELPEIP LGNYYQPIGE 500
    VTTDTTLPLP SLNKDQEENK KDPLRIPTVF VYRQQQVLLE WIHQLMINDS 550
    REFEIPELPD SLKNKISPYT HKKFDSTKLV EVLGIKKVDK LKLDSELKTE 600
    LEREKIPDLE TLLKRGEQHS RGSPNNSNN 629
    Length:629
    Mass (Da):71,241
    Last modified:November 1, 1997 - v1
    Checksum:i58126164EE375643
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti149 – 1491L → V in strain: DBVPG6044, SK1 and YPS128.
    Natural varianti301 – 3011S → L in strain: DBVPG1853.
    Natural varianti349 – 3491N → D in strain: DBVPG6044, SK1 and YPS128.
    Natural varianti499 – 4991G → D in strain: DBVPG1853.
    Natural varianti518 – 5181E → A in strain: DBVPG6044, SK1 and YPS128.
    Natural varianti528 – 5281T → A in strain: DBVPG1853.
    Natural varianti585 – 5851I → S in strain: DBVPG6763.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiS54567.
    RefSeqiNP_013824.1. NM_001182606.1.

    Genome annotation databases

    EnsemblFungiiYMR106C; YMR106C; YMR106C.
    GeneIDi855132.
    KEGGisce:YMR106C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi S54567.
    RefSeqi NP_013824.1. NM_001182606.1.

    3D structure databases

    ProteinModelPortali Q04437.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35281. 142 interactions.
    DIPi DIP-2757N.
    IntActi Q04437. 6 interactions.
    MINTi MINT-619682.
    STRINGi 4932.YMR106C.

    Proteomic databases

    MaxQBi Q04437.
    PaxDbi Q04437.
    PeptideAtlasi Q04437.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR106C ; YMR106C ; YMR106C .
    GeneIDi 855132.
    KEGGi sce:YMR106C.

    Organism-specific databases

    CYGDi YMR106c.
    SGDi S000004712. YKU80.

    Phylogenomic databases

    eggNOGi NOG238452.
    HOGENOMi HOG000066046.
    KOi K10885.
    OMAi YRYGADY.
    OrthoDBi EOG7TJ3SF.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32803-MONOMER.

    Miscellaneous databases

    NextBioi 978505.
    PROi Q04437.

    Gene expression databases

    Genevestigatori Q04437.

    Family and domain databases

    Gene3Di 2.40.290.10. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR006164. Ku70/Ku80_beta-barrel_dom.
    IPR024193. Ku80.
    IPR005160. Ku_C.
    IPR005161. Ku_N.
    IPR016194. SPOC_like_C_dom.
    IPR002035. VWF_A.
    [Graphical view ]
    PANTHERi PTHR12604:SF3. PTHR12604:SF3. 1 hit.
    Pfami PF02735. Ku. 1 hit.
    PF03730. Ku_C. 1 hit.
    PF03731. Ku_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF016570. Ku80. 1 hit.
    SMARTi SM00559. Ku78. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100939. SSF100939. 2 hits.
    SSF53300. SSF53300. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. 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. 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.

    Entry informationi

    Entry nameiKU80_YEAST
    AccessioniPrimary (citable) accession number: Q04437
    Secondary accession number(s): D6VZS9
    , Q0P737, Q0P738, Q0P741, Q0P749
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 358 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