EAF6_YEAST
ID EAF6_YEAST Reviewed; 113 AA.
AC P47128; D6VWQ1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Chromatin modification-related protein EAF6;
DE AltName: Full=ESA1-associated factor 6;
GN Name=EAF6; OrderedLocusNames=YJR082C; ORFNames=J1854;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15485911; DOI=10.1128/mcb.24.21.9424-9436.2004;
RA Zhang H., Richardson D.O., Roberts D.N., Utley R.T., Erdjument-Bromage H.,
RA Tempst P., Cote J., Cairns B.R.;
RT "The Yaf9 component of the SWR1 and NuA4 complexes is required for proper
RT gene expression, histone H4 acetylation, and Htz1 replacement near
RT telomeres.";
RL Mol. Cell. Biol. 24:9424-9436(2004).
RN [8]
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15353583; DOI=10.1073/pnas.0405753101;
RA Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y.,
RA Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A.,
RA Buratowski S., Hieter P., Greenblatt J.F.;
RT "Regulation of chromosome stability by the histone H2A variant Htz1, the
RT Swr1 chromatin remodeling complex, and the histone acetyltransferase
RT NuA4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004).
RN [9]
RP FUNCTION OF THE NUA3 COMPLEX, IDENTIFICATION IN THE NUA3 COMPLEX, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17157260; DOI=10.1016/j.molcel.2006.10.026;
RA Taverna S.D., Ilin S., Rogers R.S., Tanny J.C., Lavender H., Li H.,
RA Baker L., Boyle J., Blair L.P., Chait B.T., Patel D.J., Aitchison J.D.,
RA Tackett A.J., Allis C.D.;
RT "Yng1 PHD finger binding to H3 trimethylated at K4 promotes NuA3 HAT
RT activity at K14 of H3 and transcription at a subset of targeted ORFs.";
RL Mol. Cell 24:785-796(2006).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of selected genes principally
CC by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is
CC also involved in DNA repair. Component of the NuA3 histone
CC acetyltransferase complex, that acetylates Lys-14 of histone H3.
CC Recruitment of NuA3 to nucleosomes requires methylated histone H3. In
CC conjunction with the FACT complex, NuA3 may be involved in
CC transcriptional regulation. {ECO:0000269|PubMed:17157260}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
CC composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6,
CC EAF7, EPL1, ESA1, TRA1 and YNG2. Component of the NuA3 complex,
CC composed of at least NTO1, SAS3, TAF14, YNG1 and EAF6.
CC {ECO:0000269|PubMed:15353583, ECO:0000269|PubMed:15485911,
CC ECO:0000269|PubMed:17157260}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 504 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EAF6 family. {ECO:0000305}.
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DR EMBL; Z49581; CAA89609.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39305.1; -; Genomic_DNA.
DR EMBL; AY557889; AAS56215.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08867.1; -; Genomic_DNA.
DR PIR; S57101; S57101.
DR RefSeq; NP_012615.3; NM_001181739.3.
DR PDB; 5J9Q; X-ray; 3.25 A; B/F/J=1-113.
DR PDB; 5J9T; X-ray; 2.70 A; B/F/J=1-113.
DR PDB; 5J9U; X-ray; 2.95 A; B/F/J=1-113.
DR PDB; 5J9W; X-ray; 2.80 A; B/F/J=1-113.
DR PDBsum; 5J9Q; -.
DR PDBsum; 5J9T; -.
DR PDBsum; 5J9U; -.
DR PDBsum; 5J9W; -.
DR AlphaFoldDB; P47128; -.
DR SMR; P47128; -.
DR BioGRID; 33837; 263.
DR ComplexPortal; CPX-1810; NuA3 histone acetyltransferase complex.
DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR DIP; DIP-4058N; -.
DR IntAct; P47128; 21.
DR MINT; P47128; -.
DR STRING; 4932.YJR082C; -.
DR MaxQB; P47128; -.
DR PaxDb; P47128; -.
DR PRIDE; P47128; -.
DR DNASU; 853544; -.
DR EnsemblFungi; YJR082C_mRNA; YJR082C; YJR082C.
DR GeneID; 853544; -.
DR KEGG; sce:YJR082C; -.
DR SGD; S000003842; EAF6.
DR VEuPathDB; FungiDB:YJR082C; -.
DR eggNOG; KOG3856; Eukaryota.
DR HOGENOM; CLU_093901_2_1_1; -.
DR InParanoid; P47128; -.
DR OMA; FVKQQEG; -.
DR BioCyc; YEAST:G3O-31710-MON; -.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-6804758; Regulation of TP53 Activity through Acetylation.
DR PRO; PR:P47128; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47128; protein.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0033100; C:NuA3 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:1990467; C:NuA3a histone acetyltransferase complex; IDA:SGD.
DR GO; GO:1990468; C:NuA3b histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR015418; Eaf6.
DR PANTHER; PTHR13476; PTHR13476; 1.
DR Pfam; PF09340; NuA4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; Coiled coil; DNA damage; DNA repair;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..113
FT /note="Chromatin modification-related protein EAF6"
FT /id="PRO_0000086901"
FT REGION 36..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..43
FT /evidence="ECO:0000255"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:5J9T"
FT HELIX 8..43
FT /evidence="ECO:0007829|PDB:5J9T"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:5J9T"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:5J9T"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:5J9T"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:5J9T"
SQ SEQUENCE 113 AA; 12895 MW; 396029BD06F31E6C CRC64;
MTDELKSYEA LKAELKKSLQ DRREQEDTFD NLQQEIYDKE TEYFSHNSNN NHSGHGGAHG
SKSHYSGNII KGFDTFSKSH HSHADSAFNN NDRIFSLSSA TYVKQQHGQS QND
