Q4WHG1 · ESA1_ASPFU

Function

function

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 (By similarity).
Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity).
The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination (By similarity).
Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins (By similarity).
In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively (By similarity).

Catalytic activity

Features

Showing features for binding site, site, active site.

TypeIDPosition(s)Description
Binding site336-340acetyl-CoA (UniProtKB | ChEBI)
Site337Important for catalytic activity
Binding site345-351acetyl-CoA (UniProtKB | ChEBI)
Active site371Proton donor/acceptor
Binding site375acetyl-CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromatin
Cellular ComponentNuA4 histone acetyltransferase complex
Cellular Componentnucleus
Cellular Componentpericentric heterochromatin
Cellular Componentsite of double-strand break
Cellular ComponentSwr1 complex
Molecular Functionchromatin binding
Molecular Functionhistone H3K4 acetyltransferase activity
Molecular Functionhistone H4K16 acetyltransferase activity
Molecular Functionpeptide 2-hydroxyisobutyryltransferase activity
Molecular Functionpeptide butyryltransferase activity
Molecular Functionpeptide crotonyltransferase activity
Molecular Functiontranscription coregulator activity
Biological Processbiosynthetic process
Biological ProcessDNA repair
Biological ProcessDNA repair-dependent chromatin remodeling
Biological Processpositive regulation of heterochromatin formation
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone acetyltransferase esa1
  • EC number
  • Alternative names
    • Protein 2-hydroxyisobutyryltransferase esa1
      (EC:2.3.1.-
      ) . EC:2.3.1.- (UniProtKB | ENZYME | Rhea)
    • Protein acetyltransferase esa1
      (EC:2.3.1.-
      ) . EC:2.3.1.- (UniProtKB | ENZYME | Rhea)
    • Protein crotonyltransferase esa1
      (EC:2.3.1.-
      ) . EC:2.3.1.- (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      esa1
    • ORF names
      AFUA_2G05530

Organism names

Accessions

  • Primary accession
    Q4WHG1

Proteomes

Subcellular Location

Nucleus
Chromosome
Note: Following DNA damage, localizes to sites of DNA damage, such as double stand breaks (DSBs).

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000515521-483Histone acetyltransferase esa1
Modified residue295N6-acetyllysine; by autocatalysis

Post-translational modification

Autoacetylation at Lys-295 is required for proper function.

Keywords

Interaction

Subunit

Component of the NuA4 histone acetyltransferase complex.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region, zinc finger, motif.

TypeIDPosition(s)Description
Domain10-53Tudor-knot
Compositional bias57-73Basic and acidic residues
Region57-127Disordered
Domain195-471MYST-type HAT
Zinc finger228-253C2HC MYST-type; degenerate
Motif278-299ESA1-RPD3 motif

Domain

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 similarities

Belongs to the MYST (SAS/MOZ) family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    483
  • Mass (Da)
    55,969
  • Last updated
    2005-07-05 v1
  • Checksum
    8EBF3CDAE55CE6F8
MLLLMFALLQDGELRKAEILSIRQRKDGPSFYVHYVDFNKRLDEWIDASRLDLSHEVEWPQPEKPEKKKTGVGNKAPSKNAQKRARADSRDVSATPDLLTGKNVNVGKAQRPSKAGGKENRDGTPLSMPIVTAEAISTDGTPKAESDDVEMVDVSFTDGKSIKEEERALGLMSREEEIERLRTSGSMTQNPTEIHRVRNLNRLQMGKYDIEPWYFSPYPASFSDADIIYIDEFCLSYFDDKRAFERHRTKCTLVHPPGNEIYRDDYISFFEVDGRRQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMCTRDETGCHLVGYFSKEKDSAEGYNLACILTLPQYQRRGFGRLLISFSYELSKREGKLGSPEKPLSDLGLLGYRQYWRETLVEILMEPGRETVSENELALLTSMTEKDVHETLVVLNMLRYYKGNWVIVLTDYVVEQHKKRLEKEKLKGARKIDPARLQWKPPVFTASSRTWNW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias57-73Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAHF01000008
EMBL· GenBank· DDBJ
EAL87644.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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