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ATP-dependent DNA helicase II subunit 2 (EC 3.6.4.12) (ATP-dependent DNA helicase II subunit Ku80) (High affinity DNA-binding factor subunit 2) (Yeast Ku80)

 KU80_YEAST              Reviewed;         629 AA.
Q04437; D6VZS9; Q0P737; Q0P738; Q0P741; Q0P749;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 145.
RecName: Full=ATP-dependent DNA helicase II subunit 2;
EC=3.6.4.12;
AltName: Full=ATP-dependent DNA helicase II subunit Ku80;
AltName: Full=High affinity DNA-binding factor subunit 2;
AltName: Full=Yeast Ku80;
Name=YKU80; Synonyms=HDF2; OrderedLocusNames=YMR106C;
ORFNames=YM9718.05C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DBVPG1135, DBVPG1373, DBVPG1378, DBVPG1788, DBVPG1794,
DBVPG1853, DBVPG3051, DBVPG6044, DBVPG6763, DBVPG6765, SK1, Y55, and
YPS128;
PubMed=16951060; DOI=10.1534/genetics.106.062166;
Liti G., Barton D.B., Louis E.J.;
"Sequence diversity, reproductive isolation and species concepts in
Saccharomyces.";
Genetics 174:839-850(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PARTIAL PROTEIN SEQUENCE, FUNCTION IN TELOMERE MAINTENANCE, AND
SUBUNIT.
PubMed=8910371; DOI=10.1074/jbc.271.44.27765;
Feldmann H., Driller L., Meier B., Mages G., Kellermann J.,
Winnacker E.-L.;
"HDF2, the second subunit of the Ku homologue from Saccharomyces
cerevisiae.";
J. Biol. Chem. 271:27765-27769(1996).
[5]
SUBUNIT.
PubMed=8509423;
Feldmann H., Winnacker E.L.;
"A putative homologue of the human autoantigen Ku from Saccharomyces
cerevisiae.";
J. Biol. Chem. 268:12895-12900(1993).
[6]
FUNCTION IN TELOMERE MAINTENANCE.
PubMed=8972848; DOI=10.1093/nar/24.23.4639;
Boulton S.J., Jackson S.P.;
"Identification of a Saccharomyces cerevisiae Ku80 homologue: roles in
DNA double strand break rejoining and in telomeric maintenance.";
Nucleic Acids Res. 24:4639-4648(1996).
[7]
FUNCTION IN TELOMERIC GENE SILENCING.
PubMed=9914366; DOI=10.1007/s004120050318;
Evans S.K., Sistrunk M.L., Nugent C.I., Lundblad V.;
"Telomerase, Ku, and telomeric silencing in Saccharomyces
cerevisiae.";
Chromosoma 107:352-358(1998).
[8]
FUNCTION IN TELOMERE MAINTENANCE, AND SUBCELLULAR LOCATION.
PubMed=9635192; DOI=10.1016/S0960-9822(98)70252-0;
Laroche T., Martin S.G., Gotta M., Gorham H.C., Pryde F.E.,
Louis E.J., Gasser S.M.;
"Mutation of yeast Ku genes disrupts the subnuclear organization of
telomeres.";
Curr. Biol. 8:653-656(1998).
[9]
FUNCTION IN DOUBLE-STRAND DNA REPAIR AND TELOMERE MAINTENANCE.
PubMed=9635193; DOI=10.1016/S0960-9822(98)70253-2;
Nugent C.I., Bosco G., Ross L.O., Evans S.K., Salinger A.P.,
Moore J.K., Haber J.E., Lundblad V.;
"Telomere maintenance is dependent on activities required for end
repair of double-strand breaks.";
Curr. Biol. 8:657-660(1998).
[10]
FUNCTION IN TELOMERE MAINTENANCE.
PubMed=9663392; DOI=10.1016/S0960-9822(98)70325-2;
Polotnianka R.M., Li J., Lustig A.J.;
"The yeast Ku heterodimer is essential for protection of the telomere
against nucleolytic and recombinational activities.";
Curr. Biol. 8:831-834(1998).
[11]
FUNCTION IN CHROMOSOME END PROTECTION AND TELOMERE MAINTENANCE.
PubMed=9563951; DOI=10.1126/science.280.5364.741;
Gravel S., Larrivee M., Labrecque P., Wellinger R.J.;
"Yeast Ku as a regulator of chromosomal DNA end structure.";
Science 280:741-744(1998).
[12]
FUNCTION IN NON-HOMOLOGOUS END JOINING DNA REPAIR.
PubMed=10675560; DOI=10.1016/S0014-5793(00)01180-7;
de la Torre-Ruiz M., Lowndes N.F.;
"The Saccharomyces cerevisiae DNA damage checkpoint is required for
efficient repair of double strand breaks by non-homologous end
joining.";
FEBS Lett. 467:311-315(2000).
[13]
FUNCTION IN TELOMERASE AND CDC13 TELOMERE RECRUITMENT.
PubMed=11046137; DOI=10.1128/MCB.20.22.8397-8408.2000;
Grandin N., Damon C., Charbonneau M.;
"Cdc13 cooperates with the yeast Ku proteins and Stn1 to regulate
telomerase recruitment.";
Mol. Cell. Biol. 20:8397-8408(2000).
[14]
FUNCTION IN TELOMERE RECOMBINATION.
PubMed=12138180; DOI=10.1128/MCB.22.16.5679-5687.2002;
Tsai Y.-L., Tseng S.-F., Chang S.-H., Lin C.-C., Teng S.-C.;
"Involvement of replicative polymerases, Tel1p, Mec1p, Cdc13p, and the
Ku complex in telomere-telomere recombination.";
Mol. Cell. Biol. 22:5679-5687(2002).
[15]
FUNCTION IN TELOMERIC REPAIR AND BINDING TO TLC1 STEM LOOP.
PubMed=12975323; DOI=10.1101/gad.1125903;
Stellwagen A.E., Haimberger Z.W., Veatch J.R., Gottschling D.E.;
"Ku interacts with telomerase RNA to promote telomere addition at
native and broken chromosome ends.";
Genes Dev. 17:2384-2395(2003).
[16]
FUNCTION IN DOUBLE-STRAND DNA REPAIR AND TELOMERE MAINTENANCE.
PubMed=14585978; DOI=10.1128/MCB.23.22.8202-8215.2003;
Bertuch A.A., Lundblad V.;
"The Ku heterodimer performs separable activities at double-strand
breaks and chromosome termini.";
Mol. Cell. Biol. 23:8202-8215(2003).
[17]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[18]
FUNCTION IN TELOMERIC SILENCING, AND INTERACTION WITH SIR4.
PubMed=14551211; DOI=10.1074/jbc.M306841200;
Roy R., Meier B., McAinsh A.D., Feldmann H.M., Jackson S.P.;
"Separation-of-function mutants of yeast Ku80 reveal a Yku80p-Sir4p
interaction involved in telomeric silencing.";
J. Biol. Chem. 279:86-94(2004).
[19]
FUNCTION IN MATING-TYPE SWITCHING.
PubMed=16166630; DOI=10.1128/MCB.25.19.8476-8485.2005;
Ruan C., Workman J.L., Simpson R.T.;
"The DNA repair protein yKu80 regulates the function of recombination
enhancer during yeast mating type switching.";
Mol. Cell. Biol. 25:8476-8485(2005).
-!- 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.
{ECO:0000269|PubMed:10675560, ECO:0000269|PubMed:11046137,
ECO:0000269|PubMed:12138180, ECO:0000269|PubMed:12975323,
ECO:0000269|PubMed:14551211, ECO:0000269|PubMed:14585978,
ECO:0000269|PubMed:16166630, ECO:0000269|PubMed:8910371,
ECO:0000269|PubMed:8972848, ECO:0000269|PubMed:9563951,
ECO:0000269|PubMed:9635192, ECO:0000269|PubMed:9635193,
ECO:0000269|PubMed:9663392, ECO:0000269|PubMed:9914366}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Heterodimer of YKU70/HDF1 and YKU80/HDF2. Interacts with
SIR4. {ECO:0000269|PubMed:14551211, ECO:0000269|PubMed:8509423,
ECO:0000269|PubMed:8910371}.
-!- INTERACTION:
P22336:RFA1; NbExp=2; IntAct=EBI-8224, EBI-14971;
P11978:SIR4; NbExp=2; IntAct=EBI-8224, EBI-17237;
Q12306:SMT3; NbExp=2; IntAct=EBI-8224, EBI-17490;
P32807:YKU70; NbExp=2; IntAct=EBI-8224, EBI-8214;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9635192}.
Chromosome, telomere {ECO:0000269|PubMed:9635192}.
-!- MISCELLANEOUS: Present with 358 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the ku80 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AM296333; CAL35984.1; -; Genomic_DNA.
EMBL; AM296334; CAL35983.1; -; Genomic_DNA.
EMBL; AM296335; CAL35982.1; -; Genomic_DNA.
EMBL; AM296336; CAL35981.1; -; Genomic_DNA.
EMBL; AM296337; CAL35980.1; -; Genomic_DNA.
EMBL; AM296338; CAL35979.1; -; Genomic_DNA.
EMBL; AM296339; CAL35978.1; -; Genomic_DNA.
EMBL; AM296340; CAL35977.1; -; Genomic_DNA.
EMBL; AM296341; CAL35976.1; -; Genomic_DNA.
EMBL; AM296342; CAL35975.1; -; Genomic_DNA.
EMBL; AM296343; CAL35974.1; -; Genomic_DNA.
EMBL; AM296344; CAL35973.1; -; Genomic_DNA.
EMBL; AM296345; CAL35972.1; -; Genomic_DNA.
EMBL; Z49702; CAA89742.1; -; Genomic_DNA.
EMBL; BK006946; DAA10003.1; -; Genomic_DNA.
PIR; S54567; S54567.
RefSeq; NP_013824.1; NM_001182606.1.
ProteinModelPortal; Q04437; -.
BioGrid; 35281; 162.
DIP; DIP-2757N; -.
IntAct; Q04437; 115.
MINT; MINT-619682; -.
STRING; 4932.YMR106C; -.
MaxQB; Q04437; -.
PRIDE; Q04437; -.
EnsemblFungi; YMR106C; YMR106C; YMR106C.
GeneID; 855132; -.
KEGG; sce:YMR106C; -.
EuPathDB; FungiDB:YMR106C; -.
SGD; S000004712; YKU80.
HOGENOM; HOG000066046; -.
InParanoid; Q04437; -.
KO; K10885; -.
OMA; YRYGADY; -.
OrthoDB; EOG092C1B2W; -.
BioCyc; YEAST:G3O-32803-MONOMER; -.
PRO; PR:Q04437; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0043564; C:Ku70:Ku80 complex; IDA:SGD.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IMP:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IDA:SGD.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:SGD.
GO; GO:0042162; F:telomeric DNA binding; IDA:SGD.
GO; GO:0006333; P:chromatin assembly or disassembly; IDA:SGD.
GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
GO; GO:0007535; P:donor selection; IDA:SGD.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
GO; GO:0097695; P:establishment of macromolecular complex localization to telomere; IMP:SGD.
GO; GO:0034502; P:protein localization to chromosome; IGI:SGD.
GO; GO:0000723; P:telomere maintenance; IMP:SGD.
Gene3D; 2.40.290.10; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
InterPro; IPR024193; Ku80.
InterPro; IPR005161; Ku_N.
InterPro; IPR016194; SPOC-like_C_dom_sf.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR12604:SF4; PTHR12604:SF4; 1.
Pfam; PF02735; Ku; 1.
Pfam; PF03731; Ku_N; 1.
PIRSF; PIRSF016570; Ku80; 1.
SMART; SM00559; Ku78; 1.
SUPFAM; SSF100939; SSF100939; 2.
SUPFAM; SSF53300; SSF53300; 1.
1: Evidence at protein level;
ATP-binding; Chromosome; Complete proteome; Direct protein sequencing;
DNA damage; DNA recombination; DNA repair; DNA-binding; Helicase;
Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; Telomere.
CHAIN 1 629 ATP-dependent DNA helicase II subunit 2.
/FTId=PRO_0000084339.
DOMAIN 254 476 Ku.
VARIANT 149 149 L -> V (in strain: DBVPG6044, SK1 and
YPS128).
VARIANT 301 301 S -> L (in strain: DBVPG1853).
VARIANT 349 349 N -> D (in strain: DBVPG6044, SK1 and
YPS128).
VARIANT 499 499 G -> D (in strain: DBVPG1853).
VARIANT 518 518 E -> A (in strain: DBVPG6044, SK1 and
YPS128).
VARIANT 528 528 T -> A (in strain: DBVPG1853).
VARIANT 585 585 I -> S (in strain: DBVPG6763).
SEQUENCE 629 AA; 71241 MW; 58126164EE375643 CRC64;
MSSESTTFIV DVSPSMMKNN NVSKSMAYLE YTLLNKSKKS RKTDWISCYL ANCPVSENSQ
EIPNVFQIQS FLAPVTTTAT IGFIKRLKQY CDQHSHDSSN EGLQSMIQCL LVVSLDIKQQ
FQARKILKQI VVFTDNLDDL DITDEEIDLL TEELSTRIIL IDCGKDTQEE RKKSNWLKLV
EAIPNSRIYN MNELLVEITS PATSVVKPVR VFSGELRLGA DILSTQTSNP SGSMQDENCL
CIKVEAFPAT KAVSGLNRKT AVEVEDSQKK ERYVGVKSII EYEIHNEGNK KNVSEDDQSG
SSYIPVTISK DSVTKAYRYG ADYVVLPSVL VDQTVYESFP GLDLRGFLNR EALPRYFLTS
ESSFITADTR LGCQSDLMAF SALVDVMLEN RKIAVARYVS KKDSEVNMCA LCPVLIEHSN
INSEKKFVKS LTLCRLPFAE DERVTDFPKL LDRTTTSGVP LKKETDGHQI DELMEQFVDS
MDTDELPEIP LGNYYQPIGE VTTDTTLPLP SLNKDQEENK KDPLRIPTVF VYRQQQVLLE
WIHQLMINDS REFEIPELPD SLKNKISPYT HKKFDSTKLV EVLGIKKVDK LKLDSELKTE
LEREKIPDLE TLLKRGEQHS RGSPNNSNN


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