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Q04437

- KU80_YEAST

UniProt

Q04437 - KU80_YEAST

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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

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. RNA binding Source: SGD
  6. 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
Complete GO annotation...

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
Complete GO annotation...

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.
InParanoidiQ04437.
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

        10         20         30         40         50
MSSESTTFIV DVSPSMMKNN NVSKSMAYLE YTLLNKSKKS RKTDWISCYL
60 70 80 90 100
ANCPVSENSQ EIPNVFQIQS FLAPVTTTAT IGFIKRLKQY CDQHSHDSSN
110 120 130 140 150
EGLQSMIQCL LVVSLDIKQQ FQARKILKQI VVFTDNLDDL DITDEEIDLL
160 170 180 190 200
TEELSTRIIL IDCGKDTQEE RKKSNWLKLV EAIPNSRIYN MNELLVEITS
210 220 230 240 250
PATSVVKPVR VFSGELRLGA DILSTQTSNP SGSMQDENCL CIKVEAFPAT
260 270 280 290 300
KAVSGLNRKT AVEVEDSQKK ERYVGVKSII EYEIHNEGNK KNVSEDDQSG
310 320 330 340 350
SSYIPVTISK DSVTKAYRYG ADYVVLPSVL VDQTVYESFP GLDLRGFLNR
360 370 380 390 400
EALPRYFLTS ESSFITADTR LGCQSDLMAF SALVDVMLEN RKIAVARYVS
410 420 430 440 450
KKDSEVNMCA LCPVLIEHSN INSEKKFVKS LTLCRLPFAE DERVTDFPKL
460 470 480 490 500
LDRTTTSGVP LKKETDGHQI DELMEQFVDS MDTDELPEIP LGNYYQPIGE
510 520 530 540 550
VTTDTTLPLP SLNKDQEENK KDPLRIPTVF VYRQQQVLLE WIHQLMINDS
560 570 580 590 600
REFEIPELPD SLKNKISPYT HKKFDSTKLV EVLGIKKVDK LKLDSELKTE
610 620
LEREKIPDLE TLLKRGEQHS RGSPNNSNN
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.
InParanoidi Q04437.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 120 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