Q08649 (ESA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase ESA1
EC=2.3.1.48

Gene names

Name:	ESA1
Ordered Locus Names:	YOR244W
ORF Names:	O5257

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me. Ref.6 Ref.7 Ref.8 Ref.9 Ref.13 Ref.16 Ref.17 Ref.18 Ref.21
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, SWC4, TRA1, VID21, YAF9 and YNG2. The complex interacts with histones H4 (HHF1 and HHF2), H3 (HHT1 and HHT2) and H2A (HTA1 and HTA2). Ref.9
Domain	The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity. Ref.12 Ref.22
Miscellaneous	Present with 1170 molecules/cell in log phase SD medium. Ref.15
Sequence similarities	Belongs to the MYST (SAS/MOZ) family. Contains 1 chromo domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Molecular function	Activator Chromatin regulator Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from direct assay. Source: SGD chromatin silencing at rDNA Inferred from mutant phenotype. Source: SGD positive regulation of transcription elongation from RNA polymerase II promoter Inferred from mutant phenotype. Source: SGD regulation of cell cycle Inferred from mutant phenotype Ref.7. Source: SGD regulation of transcription by chromatin organization Inferred from mutant phenotype. Source: SGD transcription elongation, DNA-dependent Inferred from direct assay Ref.20. Source: SGD
Cellular component	NuA4 histone acetyltransferase complex Inferred from physical interaction Ref.5. Source: SGD Piccolo NuA4 histone acetyltransferase complex Inferred from direct assay. Source: SGD
Molecular function	H4 histone acetyltransferase activity Inferred from direct assay Ref.12. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARP4	P80428	9	EBI-6648,EBI-2939
EAF1	Q06337	7	EBI-6648,EBI-35867
EAF3	Q12432	11	EBI-6648,EBI-6281
SWC4	P53201	8	EBI-6648,EBI-23061
TRA1	P38811	10	EBI-6648,EBI-24638
YAF9	P53930	6	EBI-6648,EBI-28841

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 445

445

Histone acetyltransferase ESA1

PRO_0000051562

Regions

Domain

33 – 86

54

Chromo

Region

312 – 318

7

Acetyl-CoA binding By similarity

Motif

245 – 266

22

ESA1-RPD3 motif

Sites

Active site

304

1

Nucleophile By similarity

Binding site

307

1

Acetyl-CoA

Binding site

342

1

Acetyl-CoA

Amino acid modifications

Modified residue

17

1

Phosphoserine Ref.23

Experimental info

Mutagenesis

247

1

W → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

250

1

N → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

251

1

L → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

252

1

C → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

253

1

L → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

254

1

L → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

256

1

K → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

259

1

L → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

260

1

D → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

262

1

K → A: Reduces strongly HAT activity. Ref.12

Mutagenesis

304

1

C → S: Loss of function; abolishes the formation of acetyl intermediate.

Mutagenesis

315

1

G → E: Loss of function. Ref.4

Mutagenesis

338

1

E → Q: Loss of function; abolishes transfer of acetyl to C-304.

Secondary structure

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445

Helix Strand Turn

Details...

Beta strand

11 – 13

3

Helix

18 – 20

3

Beta strand

25 – 30

6

Beta strand

35 – 44

10

Beta strand

46 – 49

4

Beta strand

51 – 55

5

Beta strand

65 – 68

4

Turn

69 – 71

3

Beta strand

74 – 76

3

Beta strand

169 – 172

4

Beta strand

175 – 177

3

Beta strand

194 – 197

4

Turn

199 – 201

3

Beta strand

204 – 207

4

Helix

208 – 215

8

Beta strand

224 – 230

7

Beta strand

232 – 240

9

Helix

241 – 243

3

Helix

245 – 256

12

Beta strand

271 – 280

10

Beta strand

283 – 295

13

Beta strand

300 – 303

4

Beta strand

305 – 307

3

Helix

309 – 311

3

Beta strand

313 – 315

3

Helix

316 – 330

15

Beta strand

335 – 337

3

Helix

343 – 363

21

Beta strand

366 – 369

4

Helix

370 – 377

8

Helix

381 – 391

11

Beta strand

394 – 397

4

Beta strand

400 – 404

5

Helix

407 – 418

12

Helix

426 – 428

3

Sequences

	Sequence		Length	Mass (Da)
	Q08649 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 9E970F744D0B9E18	FASTA	445	52,613
	10 20 30 40 50 60 MSHDGKEEPG IAKKINSVDD IIIKCQCWVQ KNDEERLAEI LSINTRKAPP KFYVHYVNYN 70 80 90 100 110 120 KRLDEWITTD RINLDKEVLY PKLKATDEDN KKQKKKKATN TSETPQDSLQ DGVDGFSREN 130 140 150 160 170 180 TDVMDLDNLN VQGIKDENIS HEDEIKKLRT SGSMTQNPHE VARVRNLNRI IMGKYEIEPW 190 200 210 220 230 240 YFSPYPIELT DEDFIYIDDF TLQYFGSKKQ YERYRKKCTL RHPPGNEIYR DDYVSFFEID 250 260 270 280 290 300 GRKQRTWCRN LCLLSKLFLD HKTLYYDVDP FLFYCMTRRD ELGHHLVGYF SKEKESADGY 310 320 330 340 350 360 NVACILTLPQ YQRMGYGKLL IEFSYELSKK ENKVGSPEKP LSDLGLLSYR AYWSDTLITL 370 380 390 400 410 420 LVEHQKEITI DEISSMTSMT TTDILHTAKT LNILRYYKGQ HIIFLNEDIL DRYNRLKAKK 430 440 RRTIDPNRLI WKPPVFTASQ LRFAW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of a 26.9 kb fragment from chromosome XV of the yeast Saccharomyces cerevisiae." Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B. Yeast 12:1575-1586(1996) [PubMed: 8972580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"ESA1 is a histone acetyltransferase that is essential for growth in yeast." Smith E.R., Eisen A., Gu W., Sattah M., Pannuti A., Zhou J., Cook R.G., Lucchesi J.C., Allis C.D. Proc. Natl. Acad. Sci. U.S.A. 95:3561-3565(1998) [PubMed: 9520405] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF GLY-315.
[5]	"NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p." Allard S., Utley R.T., Savard J., Clarke A.S., Grant P.A., Brandl C.J., Pillus L., Workman J.L., Cote J. EMBO J. 18:5108-5119(1999) [PubMed: 10487762] [Abstract] Cited for: IDENTIFICATION IN A NUA4 COMPLEX WITH TRA1.
[6]	"Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes." Ikeda K., Steger D.J., Eberharter A., Workman J.L. Mol. Cell. Biol. 19:855-863(1999) [PubMed: 9858608] [Abstract] Cited for: FUNCTION OF THE NUA4 COMPLEX.
[7]	"Esa1p is an essential histone acetyltransferase required for cell cycle progression." Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L. Mol. Cell. Biol. 19:2515-2526(1999) [PubMed: 10082517] [Abstract] Cited for: FUNCTION, ACETYLATION OF HISTONES H2A; H3 AND H4.
[8]	"Distribution of acetylated histones resulting from Gal4-VP16 recruitment of SAGA and NuA4 complexes." Vignali M., Steger D.J., Neely K.E., Workman J.L. EMBO J. 19:2629-2640(2000) [PubMed: 10835360] [Abstract] Cited for: FUNCTION OF THE NUA4 COMPLEX.
[9]	"Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription." Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L., Allard S., Savard J., Lane W.S., Stillman D.J., Cote J. Mol. Cell 5:927-937(2000) [PubMed: 10911987] [Abstract] Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, FUNCTION OF THE NUA4 COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH HISTONES H2A; H3 AND H4.
[10]	"Global histone acetylation and deacetylation in yeast." Vogelauer M., Wu J., Suka N., Grunstein M. Nature 408:495-498(2000) [PubMed: 11100734] [Abstract] Cited for: ACETYLATION OF HISTONES H2A AND H4.
[11]	"Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin." Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M. Mol. Cell 8:473-479(2001) [PubMed: 11545749] [Abstract] Cited for: ACETYLATION OF HISTONES H2A; H2B AND H4.
[12]	"A conserved motif common to the histone acetyltransferase Esa1 and the histone deacetylase Rpd3." Adachi N., Kimura A., Horikoshi M. J. Biol. Chem. 277:35688-35695(2002) [PubMed: 12110674] [Abstract] Cited for: DOMAIN, MUTAGENESIS OF TRP-247; ASN-250; LEU-251; CYS-252; LEU-253; LEU-254; LYS-256; LEU-259; ASP-260 AND LYS-262.
[13]	"Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair." Bird A.W., Yu D.Y., Pray-Grant M.G., Qiu Q., Harmon K.E., Megee P.C., Grant P.A., Smith M.M., Christman M.F. Nature 419:411-415(2002) [PubMed: 12353039] [Abstract] Cited for: FUNCTION.
[14]	"Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine 16 and spreading of heterochromatin." Suka N., Luo K., Grunstein M. Nat. Genet. 32:378-383(2002) [PubMed: 12379856] [Abstract] Cited for: ACETYLATION OF HISTONE H4.
[15]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[16]	"Recruitment of the NuA4 complex poises the PHO5 promoter for chromatin remodeling and activation." Nourani A., Utley R.T., Allard S., Cote J. EMBO J. 23:2597-2607(2004) [PubMed: 15175650] [Abstract] Cited for: FUNCTION OF THE NUA4 COMPLEX.
[17]	"Global position and recruitment of HATs and HDACs in the yeast genome." Robert F., Pokholok D.K., Hannett N.M., Rinaldi N.J., Chandy M., Rolfe A., Workman J.L., Gifford D.K., Young R.A. Mol. Cell 16:199-209(2004) [PubMed: 15494307] [Abstract] Cited for: FUNCTION.
[18]	"A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin." Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J. PLoS Biol. 2:587-599(2004) [PubMed: 15045029] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[19]	"Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4." Krogan N.J., Baetz K., Keogh M.-C., Datta N., Sawa C., Kwok T.C.Y., Thompson N.J., Davey M.G., Pootoolal J., Hughes T.R., Emili A., Buratowski S., Hieter P., Greenblatt J.F. Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004) [PubMed: 15353583] [Abstract] Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, MASS SPECTROMETRY.
[20]	"Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription." Morillon A., Karabetsou N., Nair A., Mellor J. Mol. Cell 18:723-734(2005) [PubMed: 15949446] [Abstract] Cited for: REGULATION BY HISTONE H3 METHYLATION.
[21]	"Localized histone acetylation and deacetylation triggered by the homologous recombination pathway of double-strand DNA repair." Tamburini B.A., Tyler J.K. Mol. Cell. Biol. 25:4903-4913(2005) [PubMed: 15923609] [Abstract] Cited for: FUNCTION.
[22]	"The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes." Selleck W., Fortin I., Sermwittayawong D., Cote J., Tan S. Mol. Cell. Biol. 25:5535-5542(2005) [PubMed: 15964809] [Abstract] Cited for: DOMAIN.
[23]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, MASS SPECTROMETRY.
[24]	"Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast." Millar C.B., Xu F., Zhang K., Grunstein M. Genes Dev. 20:711-722(2006) [PubMed: 16543223] [Abstract] Cited for: ACETYLATION OF HISTONE H2A VARIANT HTZ1.
[25]	"Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases." Yan Y., Barlev N.A., Haley R.H., Berger S.L., Marmorstein R. Mol. Cell 6:1195-1205(2000) [PubMed: 11106757] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH COENZYME A.
[26]	"The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate." Yan Y., Harper S., Speicher D.W., Marmorstein R. Nat. Struct. Biol. 9:862-869(2002) [PubMed: 12368900] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 162-435 OF MUTANTS GLN-338 AND CYS-304 IN COMPLEX WITH COENZYME A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z75152 Genomic DNA. Translation: CAA99465.1.
BK006948 Genomic DNA. Translation: DAA11012.1.

PIR

S67137.

RefSeq

NP_014887.1. NM_001183663.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FY7	X-ray	2.00	A	160-435	[»]
1MJ9	X-ray	2.50	A	160-435	[»]
1MJA	X-ray	2.26	A	160-435	[»]
1MJB	X-ray	2.50	A	160-435	[»]
2RNZ	NMR	-	A	17-89	[»]
2RO0	NMR	-	A	1-89	[»]
3TO6	X-ray	2.10	A	160-435	[»]
3TO7	X-ray	1.90	A	160-435	[»]
3TO9	X-ray	2.00	A	160-435	[»]

ProteinModelPortal

Q08649.

SMR

Q08649. Positions 1-89, 162-434.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4115N.

IntAct

Q08649. 38 interactions.

MINT

MINT-511080.

STRING

Q08649.

Proteomic databases

PeptideAtlas

Q08649.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR244W; YOR244W; YOR244W.

GeneID

854418.

KEGG

sce:YOR244W.

NMPDR

fig|4932.3.peg.5999.

Organism-specific databases

CYGD

YOR244w.

SGD

S000005770. ESA1.

Phylogenomic databases

eggNOG

fuNOG04749.

GeneTree

EFGT00050000002010.

HOGENOM

HBG631736.

OMA

EEDEKGH.

OrthoDB

EOG4R7ZKC.

Gene expression databases

ArrayExpress

Q08649.

Genevestigator

Q08649.

GermOnline

YOR244W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.

KO

K11304.

Pfam

PF01853. MOZ_SAS. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
[Graphical view]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF54160. Chromodomain-like. 1 hit.

PROSITE

PS00598. CHROMO_1. False negative.
PS50013. CHROMO_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

NextBio

976622.

Entry information

Entry name

ESA1_YEAST

Accession

Primary (citable) accession number: Q08649
Secondary accession number(s): D6W2U6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program