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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Sitei304Important for catalytic activityCurated1
Active sitei338Proton donor/acceptor4 PublicationsCurated1
Binding sitei342Acetyl-CoA3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri195 – 220C2HC MYST-type; degeneratePROSITE-ProRule annotationAdd BLAST26

GO - Molecular functioni

  • H4 histone acetyltransferase activity Source: SGD
  • histone acetyltransferase activity Source: SGD
  • peptide N-acetyltransferase activity Source: SGD

GO - Biological processi

  • chromatin silencing at rDNA Source: SGD
  • DNA repair Source: SGD
  • DNA-templated transcription, elongation Source: SGD
  • histone acetylation Source: SGD
  • histone displacement Source: SGD
  • peptidyl-lysine acetylation Source: SGD
  • positive regulation of macroautophagy Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  • regulation of cell cycle Source: SGD
  • 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.
BRENDAi2.3.1.48. 984.
ReactomeiR-SCE-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-SCE-3214847. HATs acetylate histones.
R-SCE-5693548. Sensing of DNA Double Strand Breaks.
R-SCE-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-SCE-6804758. Regulation of TP53 Activity through Acetylation.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR244W.
SGDiS000005770. ESA1.

Subcellular locationi

GO - Cellular componenti

  • NuA4 histone acetyltransferase complex Source: SGD
  • nuclear chromatin Source: SGD
  • Piccolo NuA4 histone acetyltransferase complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi247W → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi250N → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi251L → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi252C → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi253L → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi254L → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi256K → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi259L → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi260D → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi262K → A: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi262K → R: Strongly reduces HAT activity. 1 Publication1
Mutagenesisi304C → A: Reduces HAT activity. 1 Publication1
Mutagenesisi304C → S: Strongly reduces HAT activity, but is not lethal (in vivo). Lethal, when associated with Q-338. 3 Publications1
Mutagenesisi315G → E: Loss of function. 1 Publication1
Mutagenesisi338E → 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 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000515621 – 445Histone acetyltransferase ESA1Add BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphoserineCombined sources1
Modified residuei262N6-acetyllysine; by autocatalysis1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ08649.
PRIDEiQ08649.

PTM databases

iPTMnetiQ08649.

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. 642 interactors.
DIPiDIP-4115N.
IntActiQ08649. 38 interactors.
MINTiMINT-511080.

Structurei

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Helixi18 – 20Combined sources3
Beta strandi25 – 30Combined sources6
Beta strandi35 – 44Combined sources10
Beta strandi46 – 49Combined sources4
Beta strandi51 – 55Combined sources5
Beta strandi65 – 68Combined sources4
Turni69 – 71Combined sources3
Beta strandi74 – 76Combined sources3
Beta strandi78 – 80Combined sources3
Beta strandi169 – 172Combined sources4
Beta strandi175 – 177Combined sources3
Beta strandi194 – 197Combined sources4
Turni199 – 201Combined sources3
Beta strandi204 – 207Combined sources4
Helixi208 – 215Combined sources8
Beta strandi224 – 230Combined sources7
Beta strandi232 – 240Combined sources9
Helixi241 – 243Combined sources3
Helixi245 – 256Combined sources12
Beta strandi271 – 280Combined sources10
Beta strandi283 – 295Combined sources13
Beta strandi300 – 303Combined sources4
Beta strandi305 – 307Combined sources3
Helixi309 – 311Combined sources3
Beta strandi313 – 315Combined sources3
Helixi316 – 330Combined sources15
Beta strandi335 – 337Combined sources3
Helixi343 – 363Combined sources21
Beta strandi366 – 369Combined sources4
Helixi370 – 377Combined sources8
Helixi381 – 390Combined sources10
Beta strandi394 – 397Combined sources4
Beta strandi400 – 404Combined sources5
Helixi407 – 418Combined sources12
Helixi426 – 428Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ08649.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 86ChromoAdd BLAST54
Domaini162 – 433MYST-type HATPROSITE-ProRule annotationAdd BLAST272

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni303 – 307Acetyl-CoA binding3 Publications5
Regioni312 – 318Acetyl-CoA binding3 Publications7

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi245 – 266ESA1-RPD3 motifAdd BLAST22

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 C2HC MYST-type zinc finger.PROSITE-ProRule annotation
Contains 1 chromo domain.Curated
Contains 1 MYST-type HAT (histone acetyltransferase) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri195 – 220C2HC MYST-type; degeneratePROSITE-ProRule annotationAdd BLAST26

Phylogenomic databases

GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
InParanoidiQ08649.
KOiK11304.
OMAiRAYWSDT.
OrthoDBiEOG092C043Q.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
Z75152 Genomic DNA. Translation: CAA99465.1.
BK006948 Genomic DNA. Translation: DAA11012.1.
PIRiS67137.
RefSeqiNP_014887.3. NM_001183663.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34635. 642 interactors.
DIPiDIP-4115N.
IntActiQ08649. 38 interactors.
MINTiMINT-511080.

PTM databases

iPTMnetiQ08649.

Proteomic databases

MaxQBiQ08649.
PRIDEiQ08649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YOR244W.
SGDiS000005770. ESA1.

Phylogenomic databases

GeneTreeiENSGT00550000074503.
HOGENOMiHOG000182457.
InParanoidiQ08649.
KOiK11304.
OMAiRAYWSDT.
OrthoDBiEOG092C043Q.

Enzyme and pathway databases

BioCyciYEAST:G3O-33738-MONOMER.
BRENDAi2.3.1.48. 984.
ReactomeiR-SCE-2559586. DNA Damage/Telomere Stress Induced Senescence.
R-SCE-3214847. HATs acetylate histones.
R-SCE-5693548. Sensing of DNA Double Strand Breaks.
R-SCE-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-SCE-6804758. Regulation of TP53 Activity through Acetylation.

Miscellaneous databases

EvolutionaryTraceiQ08649.
PROiQ08649.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. HAT_MYST-type.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 168 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.