P38806 · YNG2_YEAST

Function

function

Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. Involved in cell cycle progression and meiosis.

Features

Showing features for site, binding site.

128220406080100120140160180200220240260280
TypeIDPosition(s)Description
Site224Histone H3K4me3 binding
Binding site225Zn2+ 1 (UniProtKB | ChEBI)
Binding site227Zn2+ 1 (UniProtKB | ChEBI)
Site235Histone H3K4me3 binding
Binding site238Zn2+ 2 (UniProtKB | ChEBI)
Site239Histone H3K4me3 binding
Binding site243Zn2+ 2 (UniProtKB | ChEBI)
Site247Histone H3K4me3 binding
Binding site249Zn2+ 1 (UniProtKB | ChEBI)
Binding site252Zn2+ 1 (UniProtKB | ChEBI)
Binding site265Zn2+ 2 (UniProtKB | ChEBI)
Binding site268Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular ComponentNuA4 histone acetyltransferase complex
Cellular Componentnucleosome
Cellular Componentnucleus
Cellular Componentpiccolo histone acetyltransferase complex
Molecular Functionmetal ion binding
Molecular Functionmethylated histone binding
Biological Processchromatin remodeling
Biological ProcessDNA repair
Biological ProcessDNA-templated transcription
Biological Processmeiotic cell cycle
Biological Processregulation of DNA-templated transcription

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Chromatin modification-related protein YNG2
  • Alternative names
    • ESA1-associated factor 4
    • ING1 homolog 2

Gene names

    • Name
      YNG2
    • Synonyms
      EAF4, NBN1
    • Ordered locus names
      YHR090C

Organism names

Accessions

  • Primary accession
    P38806
  • Secondary accessions
    • D3DL42

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002126791-282
Modified residue183Phosphoserine
Modified residue185Phosphothreonine
Modified residue188Phosphoserine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with H3K4me3 and to a lesser extent with H3K4me2. Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P38806EPL1 P4357211EBI-24622, EBI-22792
View interactors in UniProtKB
View CPX-3155 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for coiled coil, region, compositional bias, zinc finger.

TypeIDPosition(s)Description
Coiled coil35-86
Region123-217Disordered
Compositional bias133-162Polar residues
Zinc finger222-271PHD-type

Domain

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

Sequence similarities

Belongs to the ING family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    282
  • Mass (Da)
    32,086
  • Last updated
    1995-02-01 v1
  • Checksum
    110E0A2536547D03
MDPSLVLEQTIQDVSNLPSEFRYLLEEIGSNDLKLIEEKKKYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQSLQREKCVLANTALFLIARHLNKLEKNIALLEEDGVLAPVEEDGDMDSAAEASRESSVVSNSSVKKRRAASSSGSVPPTLKKKKTSRTSKLQNEIDVSSREKSVTPVSPSIEKKIARTKEFKNSRNGKGQNGSPENEEEDKTLYCFCQRVSFGEMVACDGPNCKYEWFHYDCVNLKEPPKGTWYCPECKIEMEKNKLKRKRN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias133-162Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U00060
EMBL· GenBank· DDBJ
AAB68930.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006934
EMBL· GenBank· DDBJ
DAA06786.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp