KU70_ARATH
ID KU70_ARATH Reviewed; 621 AA.
AC Q9FQ08; Q9FZ56;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=ATP-dependent DNA helicase 2 subunit KU70;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent DNA helicase 2 subunit 1;
DE AltName: Full=ATP-dependent DNA helicase II 70 kDa subunit;
GN Name=KU70; OrderedLocusNames=At1g16970; ORFNames=F6I1.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH KU80.
RC STRAIN=cv. Columbia;
RX PubMed=12148535; DOI=10.1046/j.1365-313x.2002.01258.x;
RA Tamura K., Adachi Y., Chiba K., Oguchi K., Takahashi H.;
RT "Identification of Ku70 and Ku80 homologues in Arabidopsis thaliana:
RT evidence for a role in the repair of DNA double-strand breaks.";
RL Plant J. 29:771-781(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH KU80, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12032094; DOI=10.1093/emboj/21.11.2819;
RA Riha K., Watson J.M., Parkey J., Shippen D.E.;
RT "Telomere length deregulation and enhanced sensitivity to genotoxic stress
RT in Arabidopsis mutants deficient in Ku70.";
RL EMBO J. 21:2819-2826(2002).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=12140324; DOI=10.1093/nar/gkf445;
RA Bundock P., van Attikum H., Hooykaas P.;
RT "Increased telomere length and hypersensitivity to DNA damaging agents in
RT an Arabidopsis KU70 mutant.";
RL Nucleic Acids Res. 30:3395-3400(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH KU80.
RX PubMed=12182708; DOI=10.1046/j.1365-313x.2002.01370.x;
RA West C.E., Waterworth W.M., Story G.W., Sunderland P.A., Jiang Q.,
RA Bray C.M.;
RT "Disruption of the Arabidopsis AtKu80 gene demonstrates an essential role
RT for AtKu80 protein in efficient repair of DNA double-strand breaks in
RT vivo.";
RL Plant J. 31:517-528(2002).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12511598; DOI=10.1073/pnas.0236128100;
RA Riha K., Shippen D.E.;
RT "Ku is required for telomeric C-rich strand maintenance but not for end-to-
RT end chromosome fusions in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:611-615(2003).
RN [9]
RP INTERACTION WITH TRP1 AND KU80, AND MUTAGENESIS OF ARG-117 AND GLY-319.
RX PubMed=15589838; DOI=10.1016/j.febslet.2004.11.021;
RA Kuchar M., Fajkus J.;
RT "Interactions of putative telomere-binding proteins in Arabidopsis
RT thaliana: identification of functional TRF2 homolog in plants.";
RL FEBS Lett. 578:311-315(2004).
RN [10]
RP INTERACTION WITH WEX.
RX PubMed=16396834; DOI=10.1093/nar/gki984;
RA Li B., Conway N., Navarro S., Comai L., Comai L.;
RT "A conserved and species-specific functional interaction between the Werner
RT syndrome-like exonuclease atWEX and the Ku heterodimer in Arabidopsis.";
RL Nucleic Acids Res. 33:6861-6867(2005).
RN [11]
RP INDUCTION BY HEAT SHOCK.
RX PubMed=18515112; DOI=10.1016/j.bbagrm.2008.05.002;
RA Liu P.F., Wang Y.K., Chang W.C., Chang H.Y., Pan R.L.;
RT "Regulation of Arabidopsis thaliana Ku genes at different developmental
RT stages under heat stress.";
RL Biochim. Biophys. Acta 1779:402-407(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH OFP1.
RX PubMed=20844935; DOI=10.1007/s11103-010-9685-5;
RA Wang Y.K., Chang W.C., Liu P.F., Hsiao M.K., Lin C.T., Lin S.M., Pan R.L.;
RT "Ovate family protein 1 as a plant Ku70 interacting protein involving in
RT DNA double-strand break repair.";
RL Plant Mol. Biol. 74:453-466(2010).
CC -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase.
CC Involved in DNA non-homologous end joining (NHEJ) required for double-
CC strand break repair. When associated with KU80, binds to double-
CC stranded telomeric and non-telomeric DNA sequences, but not to single-
CC stranded DNA. Plays a role in maintaining telomere length. Acts as a
CC negative regulator of telomerase. Required for maintenance of the
CC telomeric C-rich strand. {ECO:0000269|PubMed:12032094,
CC ECO:0000269|PubMed:12148535, ECO:0000269|PubMed:12182708,
CC ECO:0000269|PubMed:12511598, ECO:0000269|PubMed:20844935}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Heterodimer with KU80. Interacts with TRP1. Interacts with
CC WEX. Interacts with OFP1. {ECO:0000269|PubMed:12032094,
CC ECO:0000269|PubMed:12148535, ECO:0000269|PubMed:12182708,
CC ECO:0000269|PubMed:15589838, ECO:0000269|PubMed:16396834,
CC ECO:0000269|PubMed:20844935}.
CC -!- INTERACTION:
CC Q9FQ08; Q8L7L8: TRP1; NbExp=2; IntAct=EBI-476083, EBI-476071;
CC Q9FQ08; Q84LH3: WEX; NbExp=2; IntAct=EBI-476083, EBI-926580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12148535}. Cytoplasm
CC {ECO:0000269|PubMed:12148535}. Note=Predominantly in the nucleus.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC {ECO:0000269|PubMed:12032094, ECO:0000269|PubMed:12148535}.
CC -!- INDUCTION: Up-regulated in response to induction of double-strand
CC breaks. Down-regulated by heat shock. {ECO:0000269|PubMed:12148535,
CC ECO:0000269|PubMed:18515112}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype when grown under normal
CC conditions. Hypersensitivity to ionising radiation (IR) and to
CC methylmethane sulfonate (MMS). Longer telomeres.
CC {ECO:0000269|PubMed:12032094, ECO:0000269|PubMed:12140324,
CC ECO:0000269|PubMed:12511598}.
CC -!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99835.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF283759; AAG44852.1; -; mRNA.
DR EMBL; AC051629; AAF99835.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29527.1; -; Genomic_DNA.
DR EMBL; AK221642; BAD95294.1; -; mRNA.
DR PIR; D86305; D86305.
DR RefSeq; NP_564012.1; NM_101558.4.
DR AlphaFoldDB; Q9FQ08; -.
DR SMR; Q9FQ08; -.
DR BioGRID; 23508; 8.
DR IntAct; Q9FQ08; 3.
DR STRING; 3702.AT1G16970.1; -.
DR iPTMnet; Q9FQ08; -.
DR PaxDb; Q9FQ08; -.
DR PRIDE; Q9FQ08; -.
DR ProteomicsDB; 237118; -.
DR EnsemblPlants; AT1G16970.1; AT1G16970.1; AT1G16970.
DR GeneID; 838268; -.
DR Gramene; AT1G16970.1; AT1G16970.1; AT1G16970.
DR KEGG; ath:AT1G16970; -.
DR Araport; AT1G16970; -.
DR TAIR; locus:2035495; AT1G16970.
DR eggNOG; KOG2327; Eukaryota.
DR HOGENOM; CLU_014815_2_0_1; -.
DR InParanoid; Q9FQ08; -.
DR OMA; PNDMMGI; -.
DR OrthoDB; 402798at2759; -.
DR PhylomeDB; Q9FQ08; -.
DR PRO; PR:Q9FQ08; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FQ08; baseline and differential.
DR Genevisible; Q9FQ08; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043564; C:Ku70:Ku80 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; IBA:GO_Central.
DR GO; GO:0071481; P:cellular response to X-ray; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; TAS:TAIR.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR GO; GO:0000723; P:telomere maintenance; IDA:TAIR.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR Gene3D; 4.10.970.10; -; 1.
DR InterPro; IPR006165; Ku70.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR027388; Ku70_bridge/pillars_dom_sf.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12604:SF2; PTHR12604:SF2; 1.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF02037; SAP; 1.
DR PIRSF; PIRSF003033; Ku70; 1.
DR SMART; SM00559; Ku78; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR TIGRFAMs; TIGR00578; ku70; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..621
FT /note="ATP-dependent DNA helicase 2 subunit KU70"
FT /id="PRO_0000394130"
FT DOMAIN 273..471
FT /note="Ku"
FT DOMAIN 585..619
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 117
FT /note="R->K: Loss of interactions with TRP1 and KU80; when
FT associated with R-319."
FT /evidence="ECO:0000269|PubMed:15589838"
FT MUTAGEN 319
FT /note="G->R: Loss of interactions with TRP1 and KU80; when
FT associated with K-117."
FT /evidence="ECO:0000269|PubMed:15589838"
SQ SEQUENCE 621 AA; 70291 MW; AF1173E3DE189396 CRC64;
MELDPDDVFR DEDEDPENDF FQEKEASKEF VVYLIDASPK MFCSTCPSEE EDKQESHFHI
AVSCIAQSLK AHIINRSNDE IAICFFNTRE KKNLQDLNGV YVFNVPERDS IDRPTARLIK
EFDLIEESFD KEIGSQTGIV SDSRENSLYS ALWVAQALLR KGSLKTADKR MFLFTNEDDP
FGSMRISVKE DMTRTTLQRA KDAQDLGISI ELLPLSQPDK QFNITLFYKD LIGLNSDELT
EFMPSVGQKL EDMKDQLKKR VLAKRIAKRI TFVICDGLSI ELNGYALLRP AIPGSITWLD
STTNLPVKVE RSYICTDTGA IMQDPIQRIQ PYKNQNIMFT VEELSQVKRI STGHLRLLGF
KPLSCLKDYH NLKPSTFLYP SDKEVIGSTR AFIALHRSMI QLERFAVAFY GGTTPPRLVA
LVAQDEIESD GGQVEPPGIN MIYLPYANDI RDIDELHSKP GVAAPRASDD QLKKASALMR
RLELKDFSVC QFANPALQRH YAILQAIALD ENELRETRDE TLPDEEGMNR PAVVKAIEQF
KQSIYGDDPD EESDSGAKEK SKKRKAGDAD DGKYDYIELA KTGKLKDLTV VELKTYLTAN
NLLVSGKKEV LINRILTHIG K
