A0A9P7EAS8 · A0A9P7EAS8_9AGAM
- ProteinChromatin modification-related protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids344 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Component of an histone acetyltransferase complex.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Site | 282 | Histone H3K4me3 binding | |||
Binding site | 283 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 285 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Site | 293 | Histone H3K4me3 binding | |||
Binding site | 296 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Site | 297 | Histone H3K4me3 binding | |||
Binding site | 301 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Site | 305 | Histone H3K4me3 binding | |||
Binding site | 307 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 310 | Zn2+ 1 (UniProtKB | ChEBI) | |||
Binding site | 323 | Zn2+ 2 (UniProtKB | ChEBI) | |||
Binding site | 326 | Zn2+ 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | methylated histone binding | |
Biological Process | chromatin organization | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameChromatin modification-related protein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Agaricomycetidae > Boletales > Suillineae > Suillaceae > Suillus
Accessions
- Primary accessionA0A9P7EAS8
Proteomes
Subcellular Location
Interaction
Subunit
Component of an histone acetyltransferase complex. Interacts with H3K4me3 and to a lesser extent with H3K4me2.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 64-84 | Disordered | |||
Region | 221-276 | Disordered | |||
Compositional bias | 250-276 | Acidic residues | |||
Domain | 280-329 | PHD-type | |||
Domain
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence similarities
Belongs to the ING family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length344
- Mass (Da)36,840
- Last updated2023-09-13 v1
- ChecksumB0DE6944583C5CD8
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 250-276 | Acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JABBWG010000018 EMBL· GenBank· DDBJ | KAG1815731.1 EMBL· GenBank· DDBJ | Genomic DNA |