[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 96604 / S288c / FY1679; DOI=10.1002/(SICI)1097-0061(199612)12:15<1575::AID-YEA45>3.3.CO;2-5; PubMed=8972580 [NCBI, ExPASy, EBI, Israel, Japan] Boyer J., Michaux G., Fairhead C., Gaillon L., Dujon B.; "Sequence and analysis of a 26.9 kb fragment from chromosome XV of the yeast Saccharomyces cerevisiae."; Yeast 12:1575-1586(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 96604 / S288c / FY1679; PubMed=9169874 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; Nature 387:98-102(1997).
[3]	CHARACTERIZATION, AND MUTAGENESIS OF GLY-315. DOI=10.1073/pnas.95.7.3561; PubMed=9520405 [NCBI, ExPASy, EBI, Israel, Japan] Smith E.R., Eisen A., Gu W., Sattah M., Pannuti A., Zhou J., Cook R.G., Lucchesi J.C., Allis C.D.; "ESA1 is a histone acetyltransferase that is essential for growth in yeast."; Proc. Natl. Acad. Sci. U.S.A. 95:3561-3565(1998).
[4]	IDENTIFICATION IN A NUA4 COMPLEX WITH TRA1. DOI=10.1093/emboj/18.18.5108; PubMed=10487762 [NCBI, ExPASy, EBI, Israel, Japan] Allard S., Utley R.T., Savard J., Clarke A.S., Grant P.A., Brandl C.J., Pillus L., Workman J.L., Cote J.; "NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p."; EMBO J. 18:5108-5119(1999).
[5]	FUNCTION OF THE NUA4 COMPLEX. PubMed=9858608 [NCBI, ExPASy, EBI, Israel, Japan] Ikeda K., Steger D.J., Eberharter A., Workman J.L.; "Activation domain-specific and general transcription stimulation by native histone acetyltransferase complexes."; Mol. Cell. Biol. 19:855-863(1999).
[6]	FUNCTION, AND ACETYLATION OF HISTONES H2A; H3 AND H4. PubMed=10082517 [NCBI, ExPASy, EBI, Israel, Japan] Clarke A.S., Lowell J.E., Jacobson S.J., Pillus L.; "Esa1p is an essential histone acetyltransferase required for cell cycle progression."; Mol. Cell. Biol. 19:2515-2526(1999).
[7]	FUNCTION OF THE NUA4 COMPLEX. DOI=10.1093/emboj/19.11.2629; PubMed=10835360 [NCBI, ExPASy, EBI, Israel, Japan] Vignali M., Steger D.J., Neely K.E., Workman J.L.; "Distribution of acetylated histones resulting from Gal4-VP16 recruitment of SAGA and NuA4 complexes."; EMBO J. 19:2629-2640(2000).
[8]	IDENTIFICATION IN THE NUA4 COMPLEX, FUNCTION OF THE NUA4 COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONES H2A; H3 AND H4. DOI=10.1016/S1097-2765(00)80258-0; PubMed=10911987 [NCBI, ExPASy, EBI, Israel, Japan] Galarneau L., Nourani A., Boudreault A.A., Zhang Y., Heliot L., Allard S., Savard J., Lane W.S., Stillman D.J., Cote J.; "Multiple links between the NuA4 histone acetyltransferase complex and epigenetic control of transcription."; Mol. Cell 5:927-937(2000).
[9]	ACETYLATION OF HISTONES H2A AND H4. DOI=10.1038/35044127; PubMed=11100734 [NCBI, ExPASy, EBI, Israel, Japan] Vogelauer M., Wu J., Suka N., Grunstein M.; "Global histone acetylation and deacetylation in yeast."; Nature 408:495-498(2000).
[10]	ACETYLATION OF HISTONES H2A; H2B AND H4. DOI=10.1016/S1097-2765(01)00301-X; PubMed=11545749 [NCBI, ExPASy, EBI, Israel, Japan] Suka N., Suka Y., Carmen A.A., Wu J., Grunstein M.; "Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin."; Mol. Cell 8:473-479(2001).
[11]	DOMAIN, AND MUTAGENESIS OF TRP-247; ASN-250; LEU-251; CYS-252; LEU-253; LEU-254; LYS-256; LEU-259; ASP-260 AND LYS-262. DOI=10.1074/jbc.M204640200; PubMed=12110674 [NCBI, ExPASy, EBI, Israel, Japan] Adachi N., Kimura A., Horikoshi M.; "A conserved motif common to the histone acetyltransferase Esa1 and the histone deacetylase Rpd3."; J. Biol. Chem. 277:35688-35695(2002).
[12]	FUNCTION. DOI=10.1038/nature01035; PubMed=12353039 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair."; Nature 419:411-415(2002).
[13]	ACETYLATION OF HISTONE H4. DOI=10.1038/ng1017; PubMed=12379856 [NCBI, ExPASy, EBI, Israel, Japan] Suka N., Luo K., Grunstein M.; "Sir2p and Sas2p opposingly regulate acetylation of yeast histone H4 lysine 16 and spreading of heterochromatin."; Nat. Genet. 32:378-383(2002).
[14]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[15]	FUNCTION OF THE NUA4 COMPLEX. DOI=10.1038/sj.emboj.7600230; PubMed=15175650 [NCBI, ExPASy, EBI, Israel, Japan] Nourani A., Utley R.T., Allard S., Cote J.; "Recruitment of the NuA4 complex poises the PHO5 promoter for chromatin remodeling and activation."; EMBO J. 23:2597-2607(2004).
[16]	FUNCTION. DOI=10.1016/j.molcel.2004.09.021; PubMed=15494307 [NCBI, ExPASy, EBI, Israel, Japan] Robert F., Pokholok D.K., Hannett N.M., Rinaldi N.J., Chandy M., Rolfe A., Workman J.L., Gifford D.K., Young R.A.; "Global position and recruitment of HATs and HDACs in the yeast genome."; Mol. Cell 16:199-209(2004).
[17]	FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY. DOI=10.1371/journal.pbio.0020131; PubMed=15045029 [NCBI, ExPASy, EBI, Israel, Japan] Kobor M.S., Venkatasubrahmanyam S., Meneghini M.D., Gin J.W., Jennings J.L., Link A.J., Madhani H.D., Rine J.; "A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin."; PLoS Biol. 2:587-599(2004).
[18]	IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0405753101; PubMed=15353583 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4."; Proc. Natl. Acad. Sci. U.S.A. 101:13513-13518(2004).
[19]	REGULATION BY HISTONE H3 METHYLATION. DOI=10.1016/j.molcel.2005.05.009; PubMed=15949446 [NCBI, ExPASy, EBI, Israel, Japan] Morillon A., Karabetsou N., Nair A., Mellor J.; "Dynamic lysine methylation on histone H3 defines the regulatory phase of gene transcription."; Mol. Cell 18:723-734(2005).
[20]	FUNCTION. DOI=10.1128/MCB.25.12.4903-4913.2005; PubMed=15923609 [NCBI, ExPASy, EBI, Israel, Japan] Tamburini B.A., Tyler J.K.; "Localized histone acetylation and deacetylation triggered by the homologous recombination pathway of double-strand DNA repair."; Mol. Cell. Biol. 25:4903-4913(2005).
[21]	DOMAIN. DOI=10.1128/MCB.25.13.5535-5542.2005; PubMed=15964809 [NCBI, ExPASy, EBI, Israel, Japan] Selleck W., Fortin I., Sermwittayawong D., Cote J., Tan S.; "The Saccharomyces cerevisiae Piccolo NuA4 histone acetyltransferase complex requires the Enhancer of Polycomb A domain and chromodomain to acetylate nucleosomes."; Mol. Cell. Biol. 25:5535-5542(2005).
[22]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).
[23]	ACETYLATION OF HISTONE H2A VARIANT HTZ1. DOI=10.1101/gad.1395506; PubMed=16543223 [NCBI, ExPASy, EBI, Israel, Japan] Millar C.B., Xu F., Zhang K., Grunstein M.; "Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast."; Genes Dev. 20:711-722(2006).
[24]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH COENZYME A. DOI=10.1016/S1097-2765(00)00116-7; PubMed=11106757 [NCBI, ExPASy, EBI, Israel, Japan] Yan Y., Barlev N.A., Haley R.H., Berger S.L., Marmorstein R.; "Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases."; Mol. Cell 6:1195-1205(2000).
[25]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 162-435 OF MUTANTS GLN-338 AND CYS-304 IN COMPLEX WITH COENZYME A. DOI=10.1038/nsb849; PubMed=12368900 [NCBI, ExPASy, EBI, Israel, Japan] Yan Y., Harper S., Speicher D.W., Marmorstein R.; "The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate."; Nat. Struct. Biol. 9:862-869(2002).

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.
CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
SUBUNIT: 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).
INTERACTION:
P80428:ARP4; NbExp=1; IntAct=EBI-6648, EBI-2939;
Q12432:EAF3; NbExp=2; IntAct=EBI-6648, EBI-6281;
P53201:SWC4; NbExp=1; IntAct=EBI-6648, EBI-23061;
P38811:TRA1; NbExp=2; IntAct=EBI-6648, EBI-24638;
Q06337:VID21; NbExp=1; IntAct=EBI-6648, EBI-35867;
P53930:YAF9; NbExp=1; IntAct=EBI-6648, EBI-28841;
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.
MISCELLANEOUS: Present with 1170 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
SIMILARITY: Contains 1 chromo domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z75152; CAA99465.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S67137; S67137.

RefSeq

NP_014887.1; -.

3D structure databases

PDB

1FY7; X-ray; 2.00 A; A=160-435.	[ExPASy / RCSB / EBI]
1MJ9; X-ray; 2.50 A; A=160-435.	[ExPASy / RCSB / EBI]
1MJA; X-ray; 2.26 A; A=160-435.	[ExPASy / RCSB / EBI]
1MJB; X-ray; 2.50 A; A=160-435.	[ExPASy / RCSB / EBI]
2RNZ; NMR; -; A=17-89.	[ExPASy / RCSB / EBI]
2RO0; NMR; -; A=1-89.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1FY7; -.
1MJ9; -.
1MJA; -.
1MJB; -.
2RNZ; -.
2RO0; -.

ModBase

Q08649.

Protein-protein interaction databases

DIP

DIP:4115N; -.

IntAct

Q08649; 36.

Organism-specific databases

YOR244w; -.

S000005770; ESA1.

Gene expression databases

ArrayExpress

Q08649; -.

GermOnline

YOR244W; Saccharomyces cerevisiae.

Ontologies

GO:0000785;	Cellular component: chromatin (inferred from electronic annotation from InterPro).
GO:0035267;	Cellular component: NuA4 histone acetyltransferase complex (inferred from physical interaction from SGD).
GO:0032777;	Cellular component: Piccolo NuA4 histone acetyltransferase complex (inferred from direct assay from SGD).
GO:0003682;	Molecular function: chromatin binding (inferred from electronic annotation from InterPro).
GO:0043166;	Molecular function: H4/H2A histone acetyltransferase activity (inferred from mutant phenotype from SGD).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006333;	Biological process: chromatin assembly or disassembly (inferred from electronic annotation from InterPro).
GO:0006281;	Biological process: DNA repair (inferred from direct assay from SGD).
GO:0016573;	Biological process: histone acetylation (inferred from direct assay from SGD).
GO:0051726;	Biological process: regulation of cell cycle (inferred from mutant phenotype from SGD).
GO:0006357;	Biological process: regulation of transcription from RNA polymerase II promoter (inferred from mutant phenotype from SGD).
GO:0006354;	Biological process: RNA elongation (inferred from direct assay from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR016181; Acyl_CoA_acyltransferase.
IPR000953; Chromodomain.
IPR002717; MOZ_SAS.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.

Pfam

PF01853; MOZ_SAS; 1.
Pfam graphical view of domain structure.

SMART

SM00298; CHROMO; 1.
SMART graphical view of domain structure.

PROSITE

PS00598; CHROMO_1; FALSE_NEG.
PS50013; CHROMO_2; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

Q08649; -.

Genome annotation databases

Ensembl

YOR244W; Saccharomyces cerevisiae. [Contig view]

854418; -.

Y13140_GR; YOR244W.

sce:YOR244W; -.

fig|4932.3.peg.5999; -.

Phylogenomic databases

HOGENOM

Q08649; -.

Other

Q08649; -.

976622; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Activator; Chromatin regulator; Complete proteome; Phosphoprotein; Transcription; Transcription regulation; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 445`	`445`	`Histone acetyltransferase ESA1.`	`PRO_0000051562`
`DOMAIN`	`33 86`	`54`	`Chromo.`
`MOTIF`	`245 266`	`22`	`ESA1-RPD3 motif.`
`ACT_SITE`	`304 304`
`BINDING`	`307 307`		`Coenzyme A.`
`BINDING`	`342 342`		`Coenzyme A.`
`MOD_RES`	`17 17`		`Phosphoserine.`
`MUTAGEN`	`247 247`		`W->A: Reduces strongly HAT activity.`
`MUTAGEN`	`250 250`		`N->A: Reduces strongly HAT activity.`
`MUTAGEN`	`251 251`		`L->A: Reduces strongly HAT activity.`
`MUTAGEN`	`252 252`		`C->A: Reduces strongly HAT activity.`
`MUTAGEN`	`253 253`		`L->A: Reduces strongly HAT activity.`
`MUTAGEN`	`254 254`		`L->A: Reduces strongly HAT activity.`
`MUTAGEN`	`256 256`		`K->A: Reduces strongly HAT activity.`
`MUTAGEN`	`259 259`		`L->A: Reduces strongly HAT activity.`
`MUTAGEN`	`260 260`		`D->A: Reduces strongly HAT activity.`
`MUTAGEN`	`262 262`		`K->A: Reduces strongly HAT activity.`
`MUTAGEN`	`304 304`		`C->S: Loss of function; abolishes the formation of acetyl intermediate.`
`MUTAGEN`	`315 315`		`G->E: Loss of function.`
`MUTAGEN`	`338 338`		`E->Q: Loss of function; abolishes transfer of acetyl to C-304.`
`STRAND`	`11 13`	`3`
`HELIX`	`18 20`	`3`
`STRAND`	`25 30`	`6`
`STRAND`	`35 44`	`10`
`STRAND`	`46 49`	`4`
`STRAND`	`51 55`	`5`
`STRAND`	`65 68`	`4`
`TURN`	`69 71`	`3`
`STRAND`	`74 76`	`3`
`STRAND`	`169 172`	`4`
`STRAND`	`175 177`	`3`
`STRAND`	`194 197`	`4`
`TURN`	`199 201`	`3`
`STRAND`	`204 207`	`4`
`HELIX`	`208 215`	`8`
`STRAND`	`224 230`	`7`
`STRAND`	`232 240`	`9`
`HELIX`	`241 243`	`3`
`HELIX`	`245 256`	`12`
`STRAND`	`271 280`	`10`
`STRAND`	`283 295`	`13`
`STRAND`	`300 303`	`4`
`STRAND`	`305 307`	`3`
`HELIX`	`309 311`	`3`
`STRAND`	`313 315`	`3`
`HELIX`	`316 330`	`15`
`STRAND`	`335 337`	`3`
`HELIX`	`343 363`	`21`
`STRAND`	`366 369`	`4`
`HELIX`	`370 377`	`8`
`HELIX`	`381 391`	`11`
`STRAND`	`394 397`	`4`
`STRAND`	`400 404`	`5`
`HELIX`	`407 418`	`12`
`HELIX`	`426 428`	`3`

Sequence information

Length: 445 AA [This is the length of the unprocessed precursor]

Molecular weight: 52613 Da [This is the MW of the unprocessed precursor]

CRC64: 9E970F744D0B9E18 [This is a checksum on the sequence]

        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

Q08649 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools