A0A9P7EAS8 · A0A9P7EAS8_9AGAM

  • Protein
    Chromatin modification-related protein
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Component of an histone acetyltransferase complex.

Caution

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

Features

Showing features for site, binding site.

134450100150200250300
Type
IDPosition(s)Description
Site282Histone H3K4me3 binding
Binding site283Zn2+ 1 (UniProtKB | ChEBI)
Binding site285Zn2+ 1 (UniProtKB | ChEBI)
Site293Histone H3K4me3 binding
Binding site296Zn2+ 2 (UniProtKB | ChEBI)
Site297Histone H3K4me3 binding
Binding site301Zn2+ 2 (UniProtKB | ChEBI)
Site305Histone H3K4me3 binding
Binding site307Zn2+ 1 (UniProtKB | ChEBI)
Binding site310Zn2+ 1 (UniProtKB | ChEBI)
Binding site323Zn2+ 2 (UniProtKB | ChEBI)
Binding site326Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentchromatin
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionmethylated histone binding
Biological Processchromatin organization
Biological Processregulation of DNA-templated transcription

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Chromatin modification-related protein

Gene names

    • ORF names
      BJ212DRAFT_1358321

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MN1
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Boletales > Suillineae > Suillaceae > Suillus

Accessions

  • Primary accession
    A0A9P7EAS8

Proteomes

Subcellular Location

Keywords

  • Cellular component

Interaction

Subunit

Component of an histone acetyltransferase complex. Interacts with H3K4me3 and to a lesser extent with H3K4me2.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region64-84Disordered
Region221-276Disordered
Compositional bias250-276Acidic residues
Domain280-329PHD-type

Domain

The PHD-type zinc finger mediates the binding to H3K4me3.

Sequence similarities

Belongs to the ING family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    344
  • Mass (Da)
    36,840
  • Last updated
    2023-09-13 v1
  • Checksum
    B0DE6944583C5CD8
MSTASVQNLEEAVTIASEFIMTLDNLPSEVQFLLQELRSKETDSQDIQNDLAKDAHKYMRYSLRSDGTDPASKEKGGAPAPPIEKLRDAQEKLSALSDAKIALASRIVDLLSRKRARLEYDLGRVLVLQGEADPASVFAGAAASTPVSVSGLGSGTAGYVLGGRNPAAQINESLRNAFAGGTATPLAGGSGSMASVGGRASVTGEDNAFKKRRLMATQGSIKLPSPAPSAYVPSTRGRRRRRGASSEAEDFDFDYGDETQGAEEAEEGDGEEGEDGEDKELYCFCQKLSYGEMIACDNPDCPYQWFHLPCVSLKQPLPESWFCDDCLRKMGPPASGPGRKGRKK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias250-276Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABBWG010000018
EMBL· GenBank· DDBJ
KAG1815731.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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