G9NAG4 · G9NAG4_HYPVG

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. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. 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. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins. 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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site392Proton donor/acceptor

GO annotations

AspectTerm
Cellular ComponentNuA4 histone acetyltransferase complex
Cellular Componentnucleosome
Cellular Componentnucleus
Cellular Componentpiccolo histone acetyltransferase complex
Molecular Functionhistone crotonyltransferase activity
Molecular Functionhistone H4K16 acetyltransferase activity
Molecular Functionpeptide 2-hydroxyisobutyryltransferase activity
Molecular Functiontranscription coregulator activity
Biological ProcessDNA repair
Biological ProcessDNA-templated transcription elongation
Biological Processnegative regulation of DNA-templated transcription
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

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone acetyltransferase
  • EC number

Gene names

    • ORF names
      TRIVIDRAFT_40290

Organism names

Accessions

  • Primary accession
    G9NAG4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

PTM/Processing

Keywords

Interaction

Subunit

Component of the NuA4 histone acetyltransferase complex.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-35Disordered
Compositional bias85-104Basic and acidic residues
Region85-211Disordered
Compositional bias144-166Polar residues
Compositional bias176-203Basic and acidic residues
Domain216-490MYST-type HAT

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    502
  • Mass (Da)
    57,838
  • Last updated
    2012-02-22 v1
  • Checksum
    ED1109B642DC0280
MAGGTPHGEPSVGSDTPRQKGKATPETLKTGCIAWVEKDGQPRRAEILSIKETKSGKHYYCNFDNFNKRLDEWVPVARIDFTQDVEWPNPEKDKPKDSKTKKVPSNQPKKSQVSKKAQKRPGKREQSVNSEATTPHPWADFVESQGQRKSSSVGPEAESQAGVTFEASATPGAGDDLLADEKEDEGKKDEHGFSREEEIEKLRTSGSMTQNPAEISRIRNISKVQFGKNDLFPWYFSPYPEIFALEDVIYICEFCLSYYGDEFAFTRHRKKCTLQHPPGNEIYRDDYVSFFEIDGRRQRTWCRNLCLLSKMFLDHKTLYYDVDPFLFYVMTMRTDKGCHIVGYFSKEKESADAYNVACILTLPQYQRKGYGRLLIQFSYELSKIEGKLGSPEKPLSDLGLLSYRQYWSENILDLLLGYNERDEKVTIEAISSALAMTTQDVEHTLQAMKMQVYHKSDHKIVIPERLIEQREKQKLKRKRVLDPLKIQWKPPVFTASSRTWGW

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias85-104Basic and acidic residues
Compositional bias144-166Polar residues
Compositional bias176-203Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ABDF02000091
EMBL· GenBank· DDBJ
EHK15825.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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