ESA1_YEAST
ID ESA1_YEAST Reviewed; 445 AA.
AC Q08649; D6W2U6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Histone acetyltransferase ESA1 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:17223684, ECO:0000269|PubMed:18245364, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:9520405};
DE AltName: Full=Protein 2-hydroxyisobutyryltransferase ESA1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:O94446};
DE AltName: Full=Protein acetyltransferase ESA1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:22539722, ECO:0000269|PubMed:29765047};
DE AltName: Full=Protein crotonyltransferase ESA1 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:31699900};
GN Name=ESA1 {ECO:0000303|PubMed:9520405, ECO:0000312|SGD:S000005770};
GN OrderedLocusNames=YOR244W; ORFNames=O5257;
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=8972580;
RX DOI=10.1002/(sici)1097-0061(199612)12:15<1575::aid-yea45>3.0.co;2-e;
RA Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.;
RT "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the
RT yeast Saccharomyces cerevisiae.";
RL Yeast 12:1575-1586(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
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 FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-315.
RX PubMed=9520405; DOI=10.1073/pnas.95.7.3561;
RA Smith E.R., Eisen A., Gu W., Sattah M., Pannuti A., Zhou J., Cook R.G.,
RA Lucchesi J.C., Allis C.D.;
RT "ESA1 is a histone acetyltransferase that is essential for growth in
RT yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:3561-3565(1998).
RN [5]
RP IDENTIFICATION IN A NUA4 COMPLEX WITH TRA1.
RX PubMed=10487762; DOI=10.1093/emboj/18.18.5108;
RA Allard S., Utley R.T., Savard J., Clarke A.S., Grant P.A., Brandl C.J.,
RA Pillus L., Workman J.L., Cote J.;
RT "NuA4, an essential transcription adaptor/histone H4 acetyltransferase
RT complex containing Esa1p and the ATM-related cofactor Tra1p.";
RL EMBO J. 18:5108-5119(1999).
RN [6]
RP FUNCTION OF THE NUA4 COMPLEX.
RX PubMed=9858608; DOI=10.1128/mcb.19.1.855;
RA Ikeda K., Steger D.J., Eberharter A., Workman J.L.;
RT "Activation domain-specific and general transcription stimulation by native
RT histone acetyltransferase complexes.";
RL Mol. Cell. Biol. 19:855-863(1999).
RN [7]
RP FUNCTION, AND ACETYLATION OF HISTONES H2A; H3 AND H4.
RX PubMed=10082517; DOI=10.1128/mcb.19.4.2515;
RA Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.;
RT "Esa1p is an essential histone acetyltransferase required for cell cycle
RT progression.";
RL Mol. Cell. Biol. 19:2515-2526(1999).
RN [8]
RP FUNCTION OF THE NUA4 COMPLEX.
RX PubMed=10835360; DOI=10.1093/emboj/19.11.2629;
RA Vignali M., Steger D.J., Neely K.E., Workman J.L.;
RT "Distribution of acetylated histones resulting from Gal4-VP16 recruitment
RT of SAGA and NuA4 complexes.";
RL EMBO J. 19:2629-2640(2000).
RN [9]
RP IDENTIFICATION IN THE NUA4 COMPLEX, FUNCTION OF THE NUA4 COMPLEX,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONES H2A; H3 AND H4.
RX PubMed=10911987; DOI=10.1016/s1097-2765(00)80258-0;
RA Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L., Allard S.,
RA Savard J., Lane W.S., Stillman D.J., Cote J.;
RT "Multiple links between the NuA4 histone acetyltransferase complex and
RT epigenetic control of transcription.";
RL Mol. Cell 5:927-937(2000).
RN [10]
RP ACETYLATION OF HISTONES H2A AND H4.
RX PubMed=11100734; DOI=10.1038/35044127;
RA Vogelauer M., Wu J., Suka N., Grunstein M.;
RT "Global histone acetylation and deacetylation in yeast.";
RL Nature 408:495-498(2000).
RN [11]
RP ACETYLATION OF HISTONES H2A; H2B AND H4.
RX PubMed=11545749; DOI=10.1016/s1097-2765(01)00301-x;
RA Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.;
RT "Highly specific antibodies determine histone acetylation site usage in
RT yeast heterochromatin and euchromatin.";
RL Mol. Cell 8:473-479(2001).
RN [12]
RP DOMAIN, AND MUTAGENESIS OF TRP-247; ASN-250; LEU-251; CYS-252; LEU-253;
RP LEU-254; LYS-256; LEU-259; ASP-260 AND LYS-262.
RX PubMed=12110674; DOI=10.1074/jbc.m204640200;
RA Adachi N., Kimura A., Horikoshi M.;
RT "A conserved motif common to the histone acetyltransferase Esa1 and the
RT histone deacetylase Rpd3.";
RL J. Biol. Chem. 277:35688-35695(2002).
RN [13]
RP FUNCTION.
RX PubMed=12353039; DOI=10.1038/nature01035;
RA Bird A.W., Yu D.Y., Pray-Grant M.G., Qiu Q., Harmon K.E., Megee P.C.,
RA Grant P.A., Smith M.M., Christman M.F.;
RT "Acetylation of histone H4 by Esa1 is required for DNA double-strand break
RT repair.";
RL Nature 419:411-415(2002).
RN [14]
RP FUNCTION IN ACETYLATION OF HISTONE H4.
RX PubMed=12379856; DOI=10.1038/ng1017;
RA Suka N., Luo K., Grunstein M.;
RT "Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine
RT 16 and spreading of heterochromatin.";
RL Nat. Genet. 32:378-383(2002).
RN [15]
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 [16]
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 [17]
RP FUNCTION OF THE NUA4 COMPLEX.
RX PubMed=15175650; DOI=10.1038/sj.emboj.7600230;
RA Nourani A., Utley R.T., Allard S., Cote J.;
RT "Recruitment of the NuA4 complex poises the PHO5 promoter for chromatin
RT remodeling and activation.";
RL EMBO J. 23:2597-2607(2004).
RN [18]
RP FUNCTION.
RX PubMed=15494307; DOI=10.1016/j.molcel.2004.09.021;
RA Robert F., Pokholok D.K., Hannett N.M., Rinaldi N.J., Chandy M., Rolfe A.,
RA Workman J.L., Gifford D.K., Young R.A.;
RT "Global position and recruitment of HATs and HDACs in the yeast genome.";
RL Mol. Cell 16:199-209(2004).
RN [19]
RP FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15045029; DOI=10.1371/journal.pbio.0020131;
RA Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W.,
RA Jennings J.L., Link A.J., Madhani H.D., Rine J.;
RT "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p
RT deposits histone variant H2A.Z into euchromatin.";
RL PLoS Biol. 2:587-599(2004).
RN [20]
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 [21]
RP REGULATION BY HISTONE H3 METHYLATION.
RX PubMed=15949446; DOI=10.1016/j.molcel.2005.05.009;
RA Morillon A., Karabetsou N., Nair A., Mellor J.;
RT "Dynamic lysine methylation on histone H3 defines the regulatory phase of
RT gene transcription.";
RL Mol. Cell 18:723-734(2005).
RN [22]
RP FUNCTION.
RX PubMed=15923609; DOI=10.1128/mcb.25.12.4903-4913.2005;
RA Tamburini B.A., Tyler J.K.;
RT "Localized histone acetylation and deacetylation triggered by the
RT homologous recombination pathway of double-strand DNA repair.";
RL Mol. Cell. Biol. 25:4903-4913(2005).
RN [23]
RP DOMAIN.
RX PubMed=15964809; DOI=10.1128/mcb.25.13.5535-5542.2005;
RA Selleck W., Fortin I., Sermwittayawong D., Cote J., Tan S.;
RT "The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase
RT complex requires the Enhancer of Polycomb A domain and chromodomain to
RT acetylate nucleosomes.";
RL Mol. Cell. Biol. 25:5535-5542(2005).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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).
RN [25]
RP FUNCTION IN ACETYLATION OF HISTONE H2A VARIANT HTZ1.
RX PubMed=16543223; DOI=10.1101/gad.1395506;
RA Millar C.B., Xu F., Zhang K., Grunstein M.;
RT "Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in
RT yeast.";
RL Genes Dev. 20:711-722(2006).
RN [26]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-304 AND GLU-338, AND ACTIVE SITE.
RX PubMed=17223684; DOI=10.1021/bi602513x;
RA Berndsen C.E., Albaugh B.N., Tan S., Denu J.M.;
RT "Catalytic mechanism of a MYST family histone acetyltransferase.";
RL Biochemistry 46:623-629(2007).
RN [27]
RP FUNCTION, MUTAGENESIS OF CYS-304 AND GLU-338, CATALYTIC ACTIVITY, AND
RP ACTIVE SITE.
RX PubMed=18245364; DOI=10.1534/genetics.107.080135;
RA Decker P.V., Yu D.Y., Iizuka M., Qiu Q., Smith M.M.;
RT "Catalytic-site mutations in the MYST family histone Acetyltransferase
RT Esa1.";
RL Genetics 178:1209-1220(2008).
RN [28]
RP FUNCTION.
RX PubMed=19822662; DOI=10.1128/mcb.01033-09;
RA Ginsburg D.S., Govind C.K., Hinnebusch A.G.;
RT "NuA4 lysine acetyltransferase Esa1 is targeted to coding regions and
RT stimulates transcription elongation with Gcn5.";
RL Mol. Cell. Biol. 29:6473-6487(2009).
RN [29]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22539722; DOI=10.1126/science.1216990;
RA Yi C., Ma M., Ran L., Zheng J., Tong J., Zhu J., Ma C., Sun Y., Zhang S.,
RA Feng W., Zhu L., Le Y., Gong X., Yan X., Hong B., Jiang F.J., Xie Z.,
RA Miao D., Deng H., Yu L.;
RT "Function and molecular mechanism of acetylation in autophagy regulation.";
RL Science 336:474-477(2012).
RN [30]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29765047; DOI=10.1038/s41467-018-04363-w;
RA Li T.Y., Song L., Sun Y., Li J., Yi C., Lam S.M., Xu D., Zhou L., Li X.,
RA Yang Y., Zhang C.S., Xie C., Huang X., Shui G., Lin S.Y., Reue K.,
RA Lin S.C.;
RT "Tip60-mediated lipin 1 acetylation and ER translocation determine
RT triacylglycerol synthesis rate.";
RL Nat. Commun. 9:1916-1916(2018).
RN [31]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31699900; DOI=10.1074/jbc.ra119.010302;
RA Kollenstart L., de Groot A.J.L., Janssen G.M.C., Cheng X., Vreeken K.,
RA Martino F., Cote J., van Veelen P.A., van Attikum H.;
RT "Gcn5 and Esa1 function as histone crotonyltransferases to regulate
RT crotonylation-dependent transcription.";
RL J. Biol. Chem. 294:20122-20134(2019).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 160-435 IN COMPLEX WITH COENZYME
RP A.
RX PubMed=11106757; DOI=10.1016/s1097-2765(00)00116-7;
RA Yan Y., Barlev N.A., Haley R.H., Berger S.L., Marmorstein R.;
RT "Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis
RT and substrate binding by histone acetyltransferases.";
RL Mol. Cell 6:1195-1205(2000).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 162-435 OF MUTANTS GLN-338 AND
RP CYS-304 IN COMPLEX WITH ACETYL-COA, CATALYTIC ACTIVITY, ACTIVE SITE, AND
RP MUTAGENESIS OF CYS-304 AND GLU-338.
RX PubMed=12368900; DOI=10.1038/nsb849;
RA Yan Y., Harper S., Speicher D.W., Marmorstein R.;
RT "The catalytic mechanism of the ESA1 histone acetyltransferase involves a
RT self-acetylated intermediate.";
RL Nat. Struct. Biol. 9:862-869(2002).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 160-435 IN COMPLEXES WITH
RP ACETYL-COA ANALOGS, CATALYTIC ACTIVITY, ACTIVE SITE, ACETYLATION AT
RP LYS-262, AND MUTAGENESIS OF LYS-262.
RX PubMed=22020126; DOI=10.1038/emboj.2011.382;
RA Yuan H., Rossetto D., Mellert H., Dang W., Srinivasan M., Johnson J.,
RA Hodawadekar S., Ding E.C., Speicher K., Abshiru N., Perry R., Wu J.,
RA Yang C., Zheng Y.G., Speicher D.W., Thibault P., Verreault A.,
RA Johnson F.B., Berger S.L., Sternglanz R., McMahon S.B., Cote J.,
RA Marmorstein R.;
RT "MYST protein acetyltransferase activity requires active site lysine
RT autoacetylation.";
RL EMBO J. 31:58-70(2012).
CC -!- FUNCTION: Catalytic component of the NuA4 histone acetyltransferase
CC (HAT), a multiprotein complex involved in epigenetic transcriptional
CC activation of selected genes principally by acetylation of nucleosomal
CC histones H4, H3, H2B, H2A and H2A variant H2A.Z (PubMed:9520405,
CC PubMed:12379856, PubMed:10082517, PubMed:10835360, PubMed:10911987,
CC PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307,
CC PubMed:15923609, PubMed:16543223, PubMed:18245364, PubMed:9858608).
CC Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac,
CC histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A
CC to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form
CC H2A.ZK14ac (PubMed:10082517, PubMed:10835360, PubMed:10911987,
CC PubMed:12353039, PubMed:15045029, PubMed:15175650, PubMed:15494307,
CC PubMed:15923609, PubMed:18245364, PubMed:9858608). Acetylation of
CC histones gives a specific tag for epigenetic transcription initiation
CC and elongation (PubMed:16543223, PubMed:19822662). Acetylation of
CC histone H4 is essential for DNA double-strand break repair through
CC homologous recombination (PubMed:10082517, PubMed:10835360,
CC PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650,
CC PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608).
CC Involved in cell cycle progression (PubMed:10082517, PubMed:10835360,
CC PubMed:10911987, PubMed:12353039, PubMed:15045029, PubMed:15175650,
CC PubMed:15494307, PubMed:15923609, PubMed:18245364, PubMed:9858608).
CC Recruitment to promoters depends on H3K4me (PubMed:10082517,
CC PubMed:10835360, PubMed:10911987, PubMed:12353039, PubMed:15045029,
CC PubMed:15175650, PubMed:15494307, PubMed:15923609, PubMed:18245364,
CC PubMed:9858608). Also acetylates non-histone proteins, such as ATG3 and
CC PAH1 (PubMed:22539722, PubMed:29765047). Regulates autophagy by
CC acetylating ATG3, controlling interaction the interaction between ATG3
CC and ATG8 and ATG8 lipidation (PubMed:22539722). Acts as a regulator of
CC fatty-acid-induced triacylglycerol synthesis by catalyzing acetylation
CC of PAH1, thereby promoting the synthesis of diacylglycerol
CC (PubMed:29765047). In addition to protein acetyltransferase, can use
CC different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-
CC hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able
CC to mediate protein 2-hydroxyisobutyrylation and crotonylation,
CC respectively (PubMed:31699900). Catalyzes histone crotonylation
CC (PubMed:31699900). {ECO:0000269|PubMed:10082517,
CC ECO:0000269|PubMed:10835360, ECO:0000269|PubMed:10911987,
CC ECO:0000269|PubMed:12353039, ECO:0000269|PubMed:12379856,
CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15175650,
CC ECO:0000269|PubMed:15494307, ECO:0000269|PubMed:15923609,
CC ECO:0000269|PubMed:16543223, ECO:0000269|PubMed:18245364,
CC ECO:0000269|PubMed:19822662, ECO:0000269|PubMed:22539722,
CC ECO:0000269|PubMed:29765047, ECO:0000269|PubMed:31699900,
CC ECO:0000269|PubMed:9520405, ECO:0000269|PubMed:9858608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:17223684,
CC ECO:0000269|PubMed:18245364, ECO:0000269|PubMed:22020126,
CC ECO:0000269|PubMed:9520405};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:17223684,
CC ECO:0000269|PubMed:18245364, ECO:0000269|PubMed:22020126,
CC ECO:0000269|PubMed:9520405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000269|PubMed:22539722, ECO:0000269|PubMed:29765047};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000269|PubMed:22539722, ECO:0000269|PubMed:29765047};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) +
CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780,
CC ChEBI:CHEBI:144968; Evidence={ECO:0000250|UniProtKB:O94446};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000250|UniProtKB:O94446};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
CC (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:137954; Evidence={ECO:0000269|PubMed:31699900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC Evidence={ECO:0000269|PubMed:31699900};
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
CC composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1,
CC SWC4, TRA1, VID21, YAF9 and YNG2. The complex interacts with histones
CC H4 (HHF1 and HHF2), H3 (HHT1 and HHT2) and H2A (HTA1 and HTA2).
CC {ECO:0000269|PubMed:10487762, ECO:0000269|PubMed:10911987,
CC ECO:0000269|PubMed:11106757, ECO:0000269|PubMed:12368900,
CC ECO:0000269|PubMed:15045029, ECO:0000269|PubMed:15353583}.
CC -!- INTERACTION:
CC Q08649; P80428: ARP4; NbExp=9; IntAct=EBI-6648, EBI-2939;
CC Q08649; Q12432: EAF3; NbExp=11; IntAct=EBI-6648, EBI-6281;
CC Q08649; P02309: HHF2; NbExp=5; IntAct=EBI-6648, EBI-8113;
CC Q08649; P11938: RAP1; NbExp=6; IntAct=EBI-6648, EBI-14821;
CC Q08649; P38811: TRA1; NbExp=10; IntAct=EBI-6648, EBI-24638;
CC -!- DOMAIN: The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required
CC for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone
CC deacetylase (HDAC) activity. {ECO:0000269|PubMed:12110674,
CC ECO:0000269|PubMed:15964809}.
CC -!- PTM: Autoacetylation at Lys-262 is required for proper function.
CC {ECO:0000269|PubMed:22020126}.
CC -!- MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
CC -!- CAUTION: The catalytic mechanisms is still under debate. Cys-304 was
CC proposed to function as a nucleophile that forms a covalent
CC intermediate with acetyl-CoA during the reaction (PubMed:12368900), and
CC indeed the residue can be acetylated (in vitro) (PubMed:12368900 and
CC PubMed:17223684). Depending on the assay system, mutation of Cys-304
CC leads to reduced or undetectable activity, indicating that is plays an
CC important role. Still, mutation of Cys-304 has only a minor effect on
CC the catalytic activity of the NuA4 histone acetyltransferase (HAT)
CC complex (PubMed:17223684), making it unlikely that this residue
CC functions as the catalytic nucleophile. {ECO:0000305}.
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DR EMBL; Z75152; CAA99465.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11012.1; -; Genomic_DNA.
DR PIR; S67137; S67137.
DR RefSeq; NP_014887.3; NM_001183663.3.
DR PDB; 1FY7; X-ray; 2.00 A; A=160-435.
DR PDB; 1MJ9; X-ray; 2.50 A; A=160-435.
DR PDB; 1MJA; X-ray; 2.26 A; A=160-435.
DR PDB; 1MJB; X-ray; 2.50 A; A=160-435.
DR PDB; 2RNZ; NMR; -; A=17-89.
DR PDB; 2RO0; NMR; -; A=1-89.
DR PDB; 3TO6; X-ray; 2.10 A; A=160-435.
DR PDB; 3TO7; X-ray; 1.90 A; A=160-435.
DR PDB; 3TO9; X-ray; 2.00 A; A=160-435.
DR PDB; 5J9Q; X-ray; 3.25 A; A/E/I=141-445.
DR PDB; 5J9T; X-ray; 2.70 A; A/E/I=141-445.
DR PDB; 5J9U; X-ray; 2.95 A; A/E/I=141-445.
DR PDB; 5J9W; X-ray; 2.80 A; A/E/I=141-445.
DR PDBsum; 1FY7; -.
DR PDBsum; 1MJ9; -.
DR PDBsum; 1MJA; -.
DR PDBsum; 1MJB; -.
DR PDBsum; 2RNZ; -.
DR PDBsum; 2RO0; -.
DR PDBsum; 3TO6; -.
DR PDBsum; 3TO7; -.
DR PDBsum; 3TO9; -.
DR PDBsum; 5J9Q; -.
DR PDBsum; 5J9T; -.
DR PDBsum; 5J9U; -.
DR PDBsum; 5J9W; -.
DR AlphaFoldDB; Q08649; -.
DR BMRB; Q08649; -.
DR SMR; Q08649; -.
DR BioGRID; 34635; 934.
DR ComplexPortal; CPX-3155; NuA4 histone acetyltransferase complex.
DR ComplexPortal; CPX-3185; Piccolo NuA4 histone acetyltransferase complex.
DR DIP; DIP-4115N; -.
DR IntAct; Q08649; 40.
DR MINT; Q08649; -.
DR STRING; 4932.YOR244W; -.
DR ChEMBL; CHEMBL3832954; -.
DR iPTMnet; Q08649; -.
DR MaxQB; Q08649; -.
DR PaxDb; Q08649; -.
DR PRIDE; Q08649; -.
DR EnsemblFungi; YOR244W_mRNA; YOR244W; YOR244W.
DR GeneID; 854418; -.
DR KEGG; sce:YOR244W; -.
DR SGD; S000005770; ESA1.
DR VEuPathDB; FungiDB:YOR244W; -.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000174488; -.
DR HOGENOM; CLU_011815_2_0_1; -.
DR InParanoid; Q08649; -.
DR OMA; MNMVKYW; -.
DR BioCyc; YEAST:G3O-33738-MON; -.
DR BRENDA; 2.3.1.48; 984.
DR Reactome; R-SCE-3214847; HATs acetylate histones.
DR Reactome; R-SCE-6804758; Regulation of TP53 Activity through Acetylation.
DR EvolutionaryTrace; Q08649; -.
DR PRO; PR:Q08649; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08649; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; IDA:SGD.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:SGD.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:SGD.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0140068; F:histone crotonyltransferase activity; IDA:SGD.
DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR GO; GO:0034212; F:peptide N-acetyltransferase activity; IMP:SGD.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; IMP:SGD.
DR GO; GO:0016239; P:positive regulation of macroautophagy; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:UniProtKB.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006351; P:transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Chromatin regulator; DNA damage;
KW DNA repair; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..445
FT /note="Histone acetyltransferase ESA1"
FT /id="PRO_0000051562"
FT DOMAIN 22..74
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 162..433
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 195..220
FT /note="C2HC MYST-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 88..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 245..266
FT /note="ESA1-RPD3 motif"
FT ACT_SITE 338
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000303|PubMed:12368900,
FT ECO:0000303|PubMed:17223684, ECO:0000303|PubMed:18245364,
FT ECO:0000303|PubMed:22020126, ECO:0000305"
FT BINDING 303..307
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:11106757,
FT ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:22020126"
FT BINDING 312..318
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:11106757,
FT ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:22020126"
FT BINDING 342
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000269|PubMed:11106757,
FT ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:22020126"
FT SITE 304
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 262
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:22020126"
FT MUTAGEN 247
FT /note="W->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 250
FT /note="N->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 251
FT /note="L->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 252
FT /note="C->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 253
FT /note="L->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 254
FT /note="L->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 256
FT /note="K->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 259
FT /note="L->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 260
FT /note="D->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 262
FT /note="K->A: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:12110674"
FT MUTAGEN 262
FT /note="K->R: Strongly reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:22020126"
FT MUTAGEN 304
FT /note="C->A: Reduces HAT activity."
FT /evidence="ECO:0000269|PubMed:17223684"
FT MUTAGEN 304
FT /note="C->S: Strongly reduces HAT activity, but is not
FT lethal (in vivo). Lethal, when associated with Q-338."
FT /evidence="ECO:0000269|PubMed:12368900,
FT ECO:0000269|PubMed:17223684, ECO:0000269|PubMed:18245364"
FT MUTAGEN 315
FT /note="G->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:9520405"
FT MUTAGEN 338
FT /note="E->Q: Strongly reduces HAT activity at pH 9.2.
FT Nearly abolishes HAT activity at pH 8.0, but is not lethal
FT (in vivo). Lethal; when associated with S-334."
FT /evidence="ECO:0000269|PubMed:12368900,
FT ECO:0000269|PubMed:17223684, ECO:0000269|PubMed:18245364"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2RO0"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2RNZ"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2RNZ"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:2RNZ"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2RNZ"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2RNZ"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2RNZ"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2RNZ"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2RNZ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:2RO0"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:5J9T"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:5J9T"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3TO7"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 208..215
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 245..256
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 271..280
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 283..295
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:1FY7"
FT HELIX 316..330
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 343..363
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 381..390
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:3TO7"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 407..418
FT /evidence="ECO:0007829|PDB:3TO7"
FT HELIX 426..428
FT /evidence="ECO:0007829|PDB:3TO7"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:5J9U"
SQ SEQUENCE 445 AA; 52613 MW; 9E970F744D0B9E18 CRC64;
MSHDGKEEPG IAKKINSVDD IIIKCQCWVQ KNDEERLAEI LSINTRKAPP KFYVHYVNYN
KRLDEWITTD RINLDKEVLY PKLKATDEDN KKQKKKKATN TSETPQDSLQ DGVDGFSREN
TDVMDLDNLN VQGIKDENIS HEDEIKKLRT SGSMTQNPHE VARVRNLNRI IMGKYEIEPW
YFSPYPIELT DEDFIYIDDF TLQYFGSKKQ YERYRKKCTL RHPPGNEIYR DDYVSFFEID
GRKQRTWCRN LCLLSKLFLD HKTLYYDVDP FLFYCMTRRD ELGHHLVGYF SKEKESADGY
NVACILTLPQ YQRMGYGKLL IEFSYELSKK ENKVGSPEKP LSDLGLLSYR AYWSDTLITL
LVEHQKEITI DEISSMTSMT TTDILHTAKT LNILRYYKGQ HIIFLNEDIL DRYNRLKAKK
RRTIDPNRLI WKPPVFTASQ LRFAW
