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Q6CKE9

- ESA1_KLULA

UniProt

Q6CKE9 - ESA1_KLULA

Protein

Histone acetyltransferase ESA1

Gene

ESA1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      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 By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei256 – 2561By similarity
    Active sitei298 – 2981NucleophileBy similarity
    Binding sitei301 – 3011Acetyl-CoABy similarity
    Binding sitei336 – 3361Acetyl-CoABy similarity

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: UniProtKB-EC

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase ESA1 (EC:2.3.1.48)
    Gene namesi
    Name:ESA1
    Ordered Locus Names:KLLA0F11209g
    OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
    Taxonomic identifieri284590 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
    ProteomesiUP000000598: Chromosome F

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 439439Histone acetyltransferase ESA1PRO_0000051558Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei256 – 2561N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

    Autoacetylation at Lys-256 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation

    Interactioni

    Subunit structurei

    Component of the NuA4 histone acetyltransferase complex.By similarity

    Protein-protein interaction databases

    STRINGi28985.Q6CKE9.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6CKE9.
    SMRiQ6CKE9. Positions 16-88, 156-428.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini156 – 427272MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni306 – 3127Acetyl-CoA bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi239 – 26022ESA1-RPD3 motifBy similarityAdd
    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.

    Sequence similaritiesi

    Belongs to the MYST (SAS/MOZ) family.Curated

    Phylogenomic databases

    eggNOGiCOG5027.
    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.

    Q6CKE9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHGEEKEPG IPQKVDSIDE IFVGCKSWVL KDGQDRLAEI LSINSRRDPP    50
    KFYVHYEDFN KRLDEWITAD RLQIDKEVIF PRPKELEEKK DSKKKKQQQN 100
    KSATPQAASA TPDGGDVMDL DNLNVQGIPN EDISREDEIK KLRTSGSMTQ 150
    NQNEVARVRN LNKVIMGKYE IEPWYFSPYP IELTDEDVVY IDDFSLQYFG 200
    SKKQYERYRK KCTLRHPPGN EIYRDDYVSF FEIDGRKQRT WCRNLCLLSK 250
    LFLDHKTLYY DVDPFLFYCM TRRDELGHHI VGYFSKEKES ADAYNVACIL 300
    TLPQYQRMGY GRLLIEFSYE LSKKEGKVGS PEKPLSDLGL LSYRAYWADT 350
    LIKLLVEHGQ EITIDEVSSI SSMTTTDILH TAKALEILRF YRGQHVLYLN 400
    SDVMKRYKKL KNNKRRSIDP QKLIWTPPVF TASQLRFAW 439
    Length:439
    Mass (Da):51,474
    Last modified:August 16, 2004 - v1
    Checksum:i20E81CA743A33F81
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382126 Genomic DNA. Translation: CAG98298.1.
    RefSeqiXP_455590.1. XM_455590.1.

    Genome annotation databases

    GeneIDi2895129.
    KEGGikla:KLLA0F11209g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382126 Genomic DNA. Translation: CAG98298.1 .
    RefSeqi XP_455590.1. XM_455590.1.

    3D structure databases

    ProteinModelPortali Q6CKE9.
    SMRi Q6CKE9. Positions 16-88, 156-428.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 28985.Q6CKE9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2895129.
    KEGGi kla:KLLA0F11209g.

    Phylogenomic databases

    eggNOGi COG5027.
    HOGENOMi HOG000182457.
    KOi K11304.
    OMAi SQLRFAW.
    OrthoDBi EOG7RFTRR.

    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...

    Entry informationi

    Entry nameiESA1_KLULA
    AccessioniPrimary (citable) accession number: Q6CKE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 20, 2005
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3