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Q08649

- ESA1_YEAST

UniProt

Q08649 - ESA1_YEAST

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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.10 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei304 – 3041Important for catalytic activityCurated
Active sitei338 – 3381Proton donor/acceptor4 PublicationsCurated
Binding sitei342 – 3421Acetyl-CoA3 Publications

GO - Molecular functioni

  1. H4 histone acetyltransferase activity Source: SGD
  2. histone acetyltransferase activity Source: SGD
  3. peptide N-acetyltransferase activity Source: SGD

GO - Biological processi

  1. chromatin silencing at rDNA Source: SGD
  2. DNA repair Source: SGD
  3. DNA-templated transcription, elongation Source: SGD
  4. histone acetylation Source: SGD
  5. histone H4 acetylation Source: GOC
  6. peptidyl-lysine acetylation Source: SGD
  7. positive regulation of macroautophagy Source: SGD
  8. positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  9. regulation of cell cycle Source: SGD
  10. regulation of transcription by chromatin organization Source: SGD
  11. regulation of transcription from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-33738-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase ESA1 (EC:2.3.1.484 Publications)
Gene namesi
Name:ESA1
Ordered Locus Names:YOR244W
ORF Names:O5257
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XV

Organism-specific databases

CYGDiYOR244w.
SGDiS000005770. ESA1.

Subcellular locationi

GO - Cellular componenti

  1. NuA4 histone acetyltransferase complex Source: SGD
  2. nuclear chromatin Source: SGD
  3. Piccolo NuA4 histone acetyltransferase complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi247 – 2471W → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi250 – 2501N → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi251 – 2511L → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi252 – 2521C → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi253 – 2531L → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi254 – 2541L → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi256 – 2561K → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi259 – 2591L → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi260 – 2601D → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi262 – 2621K → A: Strongly reduces HAT activity. 1 Publication
Mutagenesisi262 – 2621K → R: Strongly reduces HAT activity. 1 Publication
Mutagenesisi304 – 3041C → A: Reduces HAT activity. 1 Publication
Mutagenesisi304 – 3041C → S: Strongly reduces HAT activity, but is not lethal (in vivo). Lethal, when associated with Q-338. 3 Publications
Mutagenesisi315 – 3151G → E: Loss of function. 1 Publication
Mutagenesisi338 – 3381E → Q: Strongly reduces HAT activity at pH 9.2. Nearly abolishes HAT activity at pH 8.0, but is not lethal (in vivo). Lethal; when associated with S-334. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Histone acetyltransferase ESA1PRO_0000051562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Phosphoserine1 Publication
Modified residuei262 – 2621N6-acetyllysine; by autocatalysis1 Publication

Post-translational modificationi

Autoacetylation at Lys-262 is required for proper function.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ08649.
PaxDbiQ08649.
PeptideAtlasiQ08649.

Expressioni

Gene expression databases

GenevestigatoriQ08649.

Interactioni

Subunit structurei

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).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP4P8042810EBI-6648,EBI-2939
EAF1Q063377EBI-6648,EBI-35867
EAF3Q1243212EBI-6648,EBI-6281
HHF2P023095EBI-6648,EBI-8113
RAP1P119386EBI-6648,EBI-14821
SWC4P532018EBI-6648,EBI-23061
TRA1P3881110EBI-6648,EBI-24638
YAF9P539306EBI-6648,EBI-28841

Protein-protein interaction databases

BioGridi34635. 635 interactions.
DIPiDIP-4115N.
IntActiQ08649. 37 interactions.
MINTiMINT-511080.
STRINGi4932.YOR244W.

Structurei

Secondary structure

1
445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133
Helixi18 – 203
Beta strandi25 – 306
Beta strandi35 – 4410
Beta strandi46 – 494
Beta strandi51 – 555
Beta strandi65 – 684
Turni69 – 713
Beta strandi74 – 763
Beta strandi78 – 803
Beta strandi169 – 1724
Beta strandi175 – 1773
Beta strandi194 – 1974
Turni199 – 2013
Beta strandi204 – 2074
Helixi208 – 2158
Beta strandi224 – 2307
Beta strandi232 – 2409
Helixi241 – 2433
Helixi245 – 25612
Beta strandi271 – 28010
Beta strandi283 – 29513
Beta strandi300 – 3034
Beta strandi305 – 3073
Helixi309 – 3113
Beta strandi313 – 3153
Helixi316 – 33015
Beta strandi335 – 3373
Helixi343 – 36321
Beta strandi366 – 3694
Helixi370 – 3778
Helixi381 – 39010
Beta strandi394 – 3974
Beta strandi400 – 4045
Helixi407 – 41812
Helixi426 – 4283

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FY7X-ray2.00A160-435[»]
1MJ9X-ray2.50A160-435[»]
1MJAX-ray2.26A160-435[»]
1MJBX-ray2.50A160-435[»]
2RNZNMR-A17-89[»]
2RO0NMR-A1-89[»]
3TO6X-ray2.10A160-435[»]
3TO7X-ray1.90A160-435[»]
3TO9X-ray2.00A160-435[»]
ProteinModelPortaliQ08649.
SMRiQ08649. Positions 1-89, 160-435.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08649.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 8654ChromoAdd
BLAST
Domaini162 – 433272MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni303 – 3075Acetyl-CoA binding3 Publications
Regioni312 – 3187Acetyl-CoA binding3 Publications

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi245 – 26622ESA1-RPD3 motifAdd
BLAST

Domaini

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.2 Publications

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 chromo domain.Curated

Phylogenomic databases

eggNOGiCOG5027.
GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
InParanoidiQ08649.
KOiK11304.
OMAiSQLRFAW.
OrthoDBiEOG7RFTRR.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08649-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSHDGKEEPG IAKKINSVDD IIIKCQCWVQ KNDEERLAEI LSINTRKAPP
60 70 80 90 100
KFYVHYVNYN KRLDEWITTD RINLDKEVLY PKLKATDEDN KKQKKKKATN
110 120 130 140 150
TSETPQDSLQ DGVDGFSREN TDVMDLDNLN VQGIKDENIS HEDEIKKLRT
160 170 180 190 200
SGSMTQNPHE VARVRNLNRI IMGKYEIEPW YFSPYPIELT DEDFIYIDDF
210 220 230 240 250
TLQYFGSKKQ YERYRKKCTL RHPPGNEIYR DDYVSFFEID GRKQRTWCRN
260 270 280 290 300
LCLLSKLFLD HKTLYYDVDP FLFYCMTRRD ELGHHLVGYF SKEKESADGY
310 320 330 340 350
NVACILTLPQ YQRMGYGKLL IEFSYELSKK ENKVGSPEKP LSDLGLLSYR
360 370 380 390 400
AYWSDTLITL LVEHQKEITI DEISSMTSMT TTDILHTAKT LNILRYYKGQ
410 420 430 440
HIIFLNEDIL DRYNRLKAKK RRTIDPNRLI WKPPVFTASQ LRFAW
Length:445
Mass (Da):52,613
Last modified:November 1, 1996 - v1
Checksum:i9E970F744D0B9E18
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z75152 Genomic DNA. Translation: CAA99465.1.
BK006948 Genomic DNA. Translation: DAA11012.1.
PIRiS67137.
RefSeqiNP_014887.3. NM_001183663.3.

Genome annotation databases

EnsemblFungiiYOR244W; YOR244W; YOR244W.
GeneIDi854418.
KEGGisce:YOR244W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z75152 Genomic DNA. Translation: CAA99465.1 .
BK006948 Genomic DNA. Translation: DAA11012.1 .
PIRi S67137.
RefSeqi NP_014887.3. NM_001183663.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q08649.
SMRi Q08649. Positions 1-89, 160-435.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 34635. 635 interactions.
DIPi DIP-4115N.
IntActi Q08649. 37 interactions.
MINTi MINT-511080.
STRINGi 4932.YOR244W.

Proteomic databases

MaxQBi Q08649.
PaxDbi Q08649.
PeptideAtlasi Q08649.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YOR244W ; YOR244W ; YOR244W .
GeneIDi 854418.
KEGGi sce:YOR244W.

Organism-specific databases

CYGDi YOR244w.
SGDi S000005770. ESA1.

Phylogenomic databases

eggNOGi COG5027.
GeneTreei ENSGT00550000074503.
HOGENOMi HOG000182457.
InParanoidi Q08649.
KOi K11304.
OMAi SQLRFAW.
OrthoDBi EOG7RFTRR.

Enzyme and pathway databases

BioCyci YEAST:G3O-33738-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q08649.
NextBioi 976622.
PROi Q08649.

Gene expression databases

Genevestigatori Q08649.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
[Graphical view ]
Pfami PF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view ]
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEi PS51726. MYST_HAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION OF HISTONE H4.
  15. 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] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE NUA4 COMPLEX.
  17. 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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  23. "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] [Europe PMC] [Abstract]
    Cited for: ACETYLATION OF HISTONE H2A VARIANT HTZ1.
  24. "Catalytic mechanism of a MYST family histone acetyltransferase."
    Berndsen C.E., Albaugh B.N., Tan S., Denu J.M.
    Biochemistry 46:623-629(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-304 AND GLU-338, ACTIVE SITE.
  25. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Catalytic-site mutations in the MYST family histone Acetyltransferase Esa1."
    Decker P.V., Yu D.Y., Iizuka M., Qiu Q., Smith M.M.
    Genetics 178:1209-1220(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-304 AND GLU-338, CATALYTIC ACTIVITY, ACTIVE SITE.
  27. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 160-435 IN COMPLEX WITH COENZYME A.
  28. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 162-435 OF MUTANTS GLN-338 AND CYS-304 IN COMPLEX WITH ACETYL-COA, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF CYS-304 AND GLU-338.
  29. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 160-435 IN COMPLEXES WITH ACETYL-COA ANALOGS, CATALYTIC ACTIVITY, ACTIVE SITE, ACETYLATION AT LYS-262, MUTAGENESIS OF LYS-262.

Entry informationi

Entry nameiESA1_YEAST
AccessioniPrimary (citable) accession number: Q08649
Secondary accession number(s): D6W2U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1170 molecules/cell in log phase SD medium.1 Publication

Caution

The catalytic mechanisms is still under debate. Cys-304 was proposed to function as a nucleophile that forms a covalent intermediate with acetyl-CoA during the reaction (PubMed:12368900), and indeed the residue can be acetylated (in vitro) (PubMed:12368900 and PubMed:17223684). Depending on the assay system, mutation of Cys-304 leads to reduced or undetectable activity, indicating that is plays an important role. Still, mutation of Cys-304 has only a minor effect on the catalytic activity of the NuA4 histone acetyltransferase (HAT) complex (PubMed:17223684), making it unlikely that this residue functions as the catalytic nucleophile.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3