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Q08649

- ESA1_YEAST

UniProt

Q08649 - ESA1_YEAST

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
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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.9 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei262 – 26211 Publication
    Active sitei304 – 3041NucleophileBy similarity
    Binding sitei307 – 3071Acetyl-CoA
    Binding sitei342 – 3421Acetyl-CoA

    GO - Molecular functioni

    1. H4 histone acetyltransferase activity Source: SGD
    2. histone acetyltransferase activity Source: SGD
    3. peptide N-acetyltransferase activity Source: SGD
    4. protein binding Source: IntAct

    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

    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:2.3.1.48)
    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi247 – 2471W → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi250 – 2501N → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi251 – 2511L → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi252 – 2521C → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi253 – 2531L → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi254 – 2541L → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi256 – 2561K → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi259 – 2591L → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi260 – 2601D → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi262 – 2621K → A: Reduces strongly HAT activity. 1 Publication
    Mutagenesisi304 – 3041C → S: Loss of function; abolishes the formation of acetyl intermediate.
    Mutagenesisi315 – 3151G → E: Loss of function. 1 Publication
    Mutagenesisi338 – 3381E → Q: Loss of function; abolishes transfer of acetyl to C-304.

    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.

    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
    ARP4P804289EBI-6648,EBI-2939
    EAF1Q063377EBI-6648,EBI-35867
    EAF3Q1243211EBI-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. 632 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
    Regioni312 – 3187Acetyl-CoA bindingBy similarity

    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.
    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

    MSHDGKEEPG IAKKINSVDD IIIKCQCWVQ KNDEERLAEI LSINTRKAPP    50
    KFYVHYVNYN KRLDEWITTD RINLDKEVLY PKLKATDEDN KKQKKKKATN 100
    TSETPQDSLQ DGVDGFSREN TDVMDLDNLN VQGIKDENIS HEDEIKKLRT 150
    SGSMTQNPHE VARVRNLNRI IMGKYEIEPW YFSPYPIELT DEDFIYIDDF 200
    TLQYFGSKKQ YERYRKKCTL RHPPGNEIYR DDYVSFFEID GRKQRTWCRN 250
    LCLLSKLFLD HKTLYYDVDP FLFYCMTRRD ELGHHLVGYF SKEKESADGY 300
    NVACILTLPQ YQRMGYGKLL IEFSYELSKK ENKVGSPEKP LSDLGLLSYR 350
    AYWSDTLITL LVEHQKEITI DEISSMTSMT TTDILHTAKT LNILRYYKGQ 400
    HIIFLNEDIL DRYNRLKAKK RRTIDPNRLI WKPPVFTASQ LRFAW 445
    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. 632 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.
    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

    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. "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].
    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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION OF HISTONE H2A VARIANT HTZ1.
    25. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 160-435, ACTIVE SITE, ACETYLATION AT LYS-262.
    26. "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 (2.0 ANGSTROMS) IN COMPLEX WITH COENZYME A.
    27. "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 (2.3 ANGSTROMS) OF 162-435 OF MUTANTS GLN-338 AND CYS-304 IN COMPLEX WITH COENZYME A.

    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 1, 2014
    This is version 146 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

    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