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Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

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

Catalytic activityi

Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine.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 by RNA polymerase II Source: SGD

Keywordsi

Molecular functionActivator, Chromatin regulator, Transferase
Biological processTranscription, 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
R-SCE-9018519 Estrogen-dependent gene expression

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Chemistry databases

ChEMBLiCHEMBL3832954

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
PaxDbiQ08649
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

Show more details

Protein-protein interaction databases

BioGridi34635, 914 interactors
DIPiDIP-4115N
IntActiQ08649, 40 interactors
MINTiQ08649
STRINGi4932.YOR244W

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
Helixi161 – 163Combined sources3
Beta strandi169 – 172Combined sources4
Beta strandi175 – 177Combined sources3
Helixi187 – 191Combined sources5
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
Turni438 – 440Combined 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[»]
5J9QX-ray3.25A/E/I141-445[»]
5J9TX-ray2.70A/E/I141-445[»]
5J9UX-ray2.95A/E/I141-445[»]
5J9WX-ray2.80A/E/I141-445[»]
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

Zinc finger

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

Phylogenomic databases

GeneTreeiENSGT00910000144012
HOGENOMiHOG000182457
InParanoidiQ08649
KOiK11304
OMAiMNMVKYW
OrthoDBiEOG092C043Q

Family and domain databases

CDDicd00024 CHROMO, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016181 Acyl_CoA_acyltransferase
IPR016197 Chromo-like_dom_sf
IPR000953 Chromo/chromo_shadow_dom
IPR037995 Esa1/KAT5/Tip60
IPR002717 HAT_MYST-type
IPR025995 Tudor-knot
IPR036388 WH-like_DNA-bd_sf
PANTHERiPTHR10615:SF124 PTHR10615:SF124, 1 hit
PfamiView protein in Pfam
PF01853 MOZ_SAS, 1 hit
PF11717 Tudor-knot, 1 hit
SMARTiView protein in SMART
SM00298 CHROMO, 1 hit
SUPFAMiSSF54160 SSF54160, 1 hit
SSF55729 SSF55729, 1 hit
PROSITEiView protein in PROSITE
PS51726 MYST_HAT, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiESA1_YEAST
AccessioniPrimary (citable) accession number: Q08649
Secondary accession number(s): D6W2U6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 182 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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