ID   EAF7_YEAST              Reviewed;         425 AA.
AC   P53911; D6W146;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Chromatin modification-related protein EAF7;
DE   AltName: Full=ESA1-associated factor 7;
GN   Name=EAF7; OrderedLocusNames=YNL136W; ORFNames=N1212, N1843;
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=8619318; DOI=10.1002/yea.320111210;
RA   Mallet L., Bussereau F., Jacquet M.;
RT   "A 43.5 kb segment of yeast chromosome XIV, which contains MFA2, MEP2,
RT   CAP/SRV2, NAM9, FKB1/FPR1/RBP1, MOM22 and CPT1, predicts an adenosine
RT   deaminase gene and 14 new open reading frames.";
RL   Yeast 11:1195-1209(1995).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
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=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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 300 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the EAF7 family. {ECO:0000305}.
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DR   EMBL; Z46843; CAA86889.1; -; Genomic_DNA.
DR   EMBL; Z71412; CAA96018.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10412.1; -; Genomic_DNA.
DR   PIR; S55147; S55147.
DR   RefSeq; NP_014263.1; NM_001182974.1.
DR   AlphaFoldDB; P53911; -.
DR   SMR; P53911; -.
DR   BioGRID; 35690; 735.
DR   ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR   ComplexPortal; CPX-3184; EAF5-7-3 nucleosome disassembly/reassembly complex.
DR   IntAct; P53911; 15.
DR   MINT; P53911; -.
DR   STRING; 4932.YNL136W; -.
DR   iPTMnet; P53911; -.
DR   MaxQB; P53911; -.
DR   PaxDb; 4932-YNL136W; -.
DR   PeptideAtlas; P53911; -.
DR   EnsemblFungi; YNL136W_mRNA; YNL136W; YNL136W.
DR   GeneID; 855586; -.
DR   KEGG; sce:YNL136W; -.
DR   AGR; SGD:S000005080; -.
DR   SGD; S000005080; EAF7.
DR   VEuPathDB; FungiDB:YNL136W; -.
DR   eggNOG; KOG4051; Eukaryota.
DR   HOGENOM; CLU_053191_0_0_1; -.
DR   InParanoid; P53911; -.
DR   OMA; PEYHTEE; -.
DR   OrthoDB; 1700511at2759; -.
DR   BioCyc; YEAST:G3O-33155-MONOMER; -.
DR   BioGRID-ORCS; 855586; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53911; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53911; Protein.
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:ComplexPortal.
DR   GO; GO:0006281; P:DNA repair; IDA:SGD.
DR   GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IMP:ComplexPortal.
DR   GO; GO:0006351; P:DNA-templated transcription; NAS:ComplexPortal.
DR   GO; GO:0006337; P:nucleosome disassembly; IMP:ComplexPortal.
DR   GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IMP:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR   InterPro; IPR012423; Eaf7/MRGBP.
DR   PANTHER; PTHR13581; MRG-BINDING PROTEIN; 1.
DR   PANTHER; PTHR13581:SF5; MRG_MORF4L-BINDING PROTEIN; 1.
DR   Pfam; PF07904; Eaf7; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Coiled coil; DNA damage; DNA repair; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..425
FT                   /note="Chromatin modification-related protein EAF7"
FT                   /id="PRO_0000215882"
FT   REGION          143..425
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          209..310
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        145..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..311
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         225
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
SQ   SEQUENCE   425 AA;  49391 MW;  4C99805F529B4CF1 CRC64;
     MVVHWTIVDE IRLLRWASEF KPAGIHKHFH MFCIVERMNS PDKYPVTLLQ KETMKLGKVF
     TAKDIWDKLS QSYNLEKIDE MENTYSLEAT TESSRNGNGN GDDAEIHEET LLELNNRIRV
     RKQDFTLPWE EYGELILENA RKSPNSNEEY PRVEDMNEKD STIPKESPST DLKNDNNKQE
     KNATIKVKEL PEYHTEENDS PIDVQKEPIK EVQSDEKELQ REHMSEEEQK MKSTNKTAAP
     VRKSQRLKRS KEVKFEDEEK EEIEEDNTKD EEQKEKKEEI QEPKITHNEE VDKEKNENEE
     GDDEREKSTS YENTNGSESE GVDEGVDEEL GYESEREAEG KGKQIESEGG NLKKKTENKK
     GDDQQDDTKK DSKDKNEPLA KRTRHSSSTG NTSNETSPKR KRRKAGSRKN SPPATRVSSR
     LRNKK
//