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 27-MAR-2024, entry version 216. 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%3c1575::aid-yea45%3e3.0.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, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7VVU; EM; 3.40 A; P=1-445. DR PDB; 7VVZ; EM; 8.80 A; P=1-445. 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 PDBsum; 7VVU; -. DR PDBsum; 7VVZ; -. DR AlphaFoldDB; Q08649; -. DR BMRB; Q08649; -. DR EMDB; EMD-32150; -. DR SMR; Q08649; -. DR BioGRID; 34635; 944. 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 GlyGen; Q08649; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q08649; -. DR MaxQB; Q08649; -. DR PaxDb; 4932-YOR244W; -. DR PeptideAtlas; Q08649; -. DR EnsemblFungi; YOR244W_mRNA; YOR244W; YOR244W. DR GeneID; 854418; -. DR KEGG; sce:YOR244W; -. DR AGR; SGD:S000005770; -. 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; QYQRHGY; -. DR OrthoDB; 118560at2759; -. DR BioCyc; YEAST:G3O-33738-MONOMER; -. DR BRENDA; 2.3.1.48; 984. DR Reactome; R-SCE-2559586; DNA Damage/Telomere Stress Induced Senescence. DR Reactome; R-SCE-5693548; Sensing of DNA Double Strand Breaks. DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression. DR BioGRID-ORCS; 854418; 5 hits in 10 CRISPR screens. 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; NAS:ComplexPortal. DR GO; GO:0032777; C:piccolo histone acetyltransferase complex; IDA:SGD. DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:SGD. DR GO; GO:0140068; F:histone crotonyltransferase activity; IDA:SGD. DR GO; GO:0010485; F:histone H4 acetyltransferase activity; IDA:SGD. DR GO; GO:0046972; F:histone H4K16 acetyltransferase activity; IBA:GO_Central. 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:0006351; P:DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:0006354; P:DNA-templated transcription elongation; IDA:SGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central. 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 by RNA polymerase II; IMP:SGD. DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:UniProtKB. DR GO; GO:0000183; P:rDNA heterochromatin formation; 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 CDD; cd18986; CBD_ESA1_like; 1. DR CDD; cd04301; NAT_SF; 1. DR Gene3D; 2.30.30.140; -; 1. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1. DR PANTHER; PTHR10615:SF161; HISTONE ACETYLTRANSFERASE KAT5; 1. 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; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1. DR SUPFAM; SSF54160; Chromo domain-like; 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 //