Q7S9B6 · ESA1_NEUCR

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 site361-365acetyl-CoA (UniProtKB | ChEBI)
Site362Important for catalytic activity
Binding site370-376acetyl-CoA (UniProtKB | ChEBI)
Active site396Proton donor/acceptor
Binding site400acetyl-CoA (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromatin
Cellular ComponentNuA4 histone acetyltransferase complex
Cellular Componentnucleosome
Cellular Componentnucleus
Cellular Componentpiccolo histone acetyltransferase complex
Molecular Functionchromatin binding
Molecular Functionhistone crotonyltransferase activity
Molecular Functionhistone H4K16 acetyltransferase activity
Molecular Functionmetal ion binding
Molecular Functionpeptide 2-hydroxyisobutyryltransferase activity
Molecular Functiontranscription coregulator activity
Biological ProcessDNA repair
Biological ProcessDNA-templated transcription elongation
Biological Processpositive regulation of macroautophagy
Biological Processpositive regulation of transcription elongation by RNA polymerase II
Biological Processpositive regulation of triglyceride biosynthetic process
Biological ProcessrDNA heterochromatin formation
Biological Processregulation of cell cycle
Biological Processregulation of transcription by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone acetyltransferase esa-1
  • EC number
  • Alternative names
    • Histone acetyltransferase hat-4
    • Protein 2-hydroxyisobutyryltransferase esa-1
      (EC:2.3.1.-
      ) . EC:2.3.1.- (UniProtKB | ENZYME | Rhea)
    • Protein acetyltransferase esa-1
      (EC:2.3.1.-
      ) . EC:2.3.1.- (UniProtKB | ENZYME | Rhea)
    • Protein crotonyltransferase esa-1
      (EC:2.3.1.-
      ) . EC:2.3.1.- (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      esa-1
    • Synonyms
      hat-4
    • ORF names
      NCU05218

Organism names

Accessions

  • Primary accession
    Q7S9B6

Proteomes

    • Identifier
    • Component
      Chromosome 4, Linkage Group IV

Organism-specific databases

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_00000515591-506Histone acetyltransferase esa-1
Modified residue320N6-acetyllysine; by autocatalysis

Post-translational modification

Autoacetylation at Lys-320 is required for proper function.

Keywords

Proteomic databases

Interaction

Subunit

Component of the NuA4 histone acetyltransferase complex.

Protein-protein interaction databases

Structure

Family & Domains

Features

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

TypeIDPosition(s)Description
Region1-24Disordered
Domain26-78Tudor-knot
Compositional bias82-102Basic and acidic residues
Region82-215Disordered
Compositional bias125-147Polar residues
Compositional bias168-206Basic and acidic residues
Domain220-494MYST-type HAT
Zinc finger253-278C2HC MYST-type
Motif303-324ESA1-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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    506
  • Mass (Da)
    58,807
  • Last updated
    2003-12-15 v1
  • Checksum
    53A62414D139674A
MSPPGGDATVGSDEKRQKGKATPDTIKMGCIAMVMKEGQLRRAEILSIKDTKSGRQFYCNFDNFNKRLDEWVPAARIDFEQDVEWPNPDKDKQKDAKTKKNNSTVSKKQPSKKNNQKKASKREQSVASDGQTPHPWTEFVESQPGKNNRQRGKTEDGTDVNASLEVGGDKGVKRKADEIDMDEDEIPAAKKQRQPSFSREQEIEKLRTSGSMTQNPTEISRIRNISKVEFGRYVLFPWYFSPYPQIFDQEDCIYICEFCLSYYGELKSFVRHRQKCTLHHPPGNEIYRDDYVSFFEIDGRRQRTWCRNLCLLSKMFLDHKTLYYDVDPFLFYVMTTRDDRGCHIIGYFSKEKESTDGYNVACILTLPQYQRKGYGRLLIQFSYELSKIEGKLGSPEKPLSDLGLLSYRQYWSENIIDILLGYNERKEACTIENIAVALAMTTQDVEHTLQALKMQVYHKGEHKIVVPEKLIKQREKSKAKQKRLIDPERIQWKPPVFTALNRTWGW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias82-102Basic and acidic residues
Compositional bias125-147Polar residues
Compositional bias168-206Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM002239
EMBL· GenBank· DDBJ
EAA32981.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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