EAF5_YEAST
ID EAF5_YEAST Reviewed; 279 AA.
AC P39995; D3DLN1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Chromatin modification-related protein EAF5;
DE AltName: Full=ESA1-associated factor 5;
GN Name=EAF5; OrderedLocusNames=YEL018W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [4]
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 [5]
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 [6]
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 [7]
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).
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.
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. {ECO:0000269|PubMed:15353583,
CC ECO:0000269|PubMed:15485911}.
CC -!- INTERACTION:
CC P39995; Q12432: EAF3; NbExp=11; IntAct=EBI-22312, EBI-6281;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EAF5 family. {ECO:0000305}.
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DR EMBL; U18530; AAB64495.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07635.1; -; Genomic_DNA.
DR PIR; S50441; S50441.
DR RefSeq; NP_010897.1; NM_001178833.1.
DR PDB; 5Y81; EM; 4.70 A; H=1-279.
DR PDBsum; 5Y81; -.
DR AlphaFoldDB; P39995; -.
DR SMR; P39995; -.
DR BioGRID; 36712; 347.
DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-3184; EAF5-7-3 nucleosome disassembly/reassembly complex.
DR DIP; DIP-5280N; -.
DR IntAct; P39995; 23.
DR MINT; P39995; -.
DR STRING; 4932.YEL018W; -.
DR MaxQB; P39995; -.
DR PaxDb; P39995; -.
DR PRIDE; P39995; -.
DR EnsemblFungi; YEL018W_mRNA; YEL018W; YEL018W.
DR GeneID; 856696; -.
DR KEGG; sce:YEL018W; -.
DR SGD; S000000744; EAF5.
DR VEuPathDB; FungiDB:YEL018W; -.
DR eggNOG; ENOG502S0AH; Eukaryota.
DR HOGENOM; CLU_071344_0_0_1; -.
DR InParanoid; P39995; -.
DR OMA; DFDDTVQ; -.
DR BioCyc; YEAST:G3O-30143-MON; -.
DR PRO; PR:P39995; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39995; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:1990453; C:nucleosome disassembly/reassembly complex; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IMP:ComplexPortal.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0006337; P:nucleosome disassembly; IMP:ComplexPortal.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR026226; EAF5.
DR PRINTS; PR02067; PROTEINEAF5.
PE 1: Evidence at protein level;
KW 3D-structure; Chromatin regulator; DNA damage; DNA repair; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..279
FT /note="Chromatin modification-related protein EAF5"
FT /id="PRO_0000086892"
FT REGION 147..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 31644 MW; 679658AB395EE16A CRC64;
MDKEVSELVV LQLIHTLISN KNEELVRNGG GINMIGNNLR ISLVKLTNEI QNNLLINELT
NLRRQSNVAN GNRKLGINDI LTIVKNLFPE YRTTLNDGQL SLHGLEMHDI EKLLDEKYDR
FKKTQVEQIR MMEDEILKNG IKTGASQLQP HANAGKSGSA GTSATITTTT PHMAHSMDPK
REKLLKLYRD TVLNKLESKT GNFQKLFKSP DGSIIKNEIN YEDIKNETPG SVHELQLILQ
KSITDGVMRK VIGTDDWKLA RQVQFELDDT VQFMRRALE
