P38806 · YNG2_YEAST
- ProteinChromatin modification-related protein YNG2
- GeneYNG2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids282 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 224 | Histone H3K4me3 binding | ||||
Sequence: Y | ||||||
Binding site | 225 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 227 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 235 | Histone H3K4me3 binding | ||||
Sequence: M | ||||||
Binding site | 238 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 239 | Histone H3K4me3 binding | ||||
Sequence: D | ||||||
Binding site | 243 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Site | 247 | Histone H3K4me3 binding | ||||
Sequence: W | ||||||
Binding site | 249 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 252 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 265 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 268 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | NuA4 histone acetyltransferase complex | |
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Cellular Component | piccolo histone acetyltransferase complex | |
Molecular Function | metal ion binding | |
Molecular Function | methylated histone binding | |
Biological Process | chromatin remodeling | |
Biological Process | DNA repair | |
Biological Process | DNA-templated transcription | |
Biological Process | meiotic cell cycle | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChromatin modification-related protein YNG2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP38806
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000212679 | 1-282 | Chromatin modification-related protein YNG2 | |||
Sequence: MDPSLVLEQTIQDVSNLPSEFRYLLEEIGSNDLKLIEEKKKYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQSLQREKCVLANTALFLIARHLNKLEKNIALLEEDGVLAPVEEDGDMDSAAEASRESSVVSNSSVKKRRAASSSGSVPPTLKKKKTSRTSKLQNEIDVSSREKSVTPVSPSIEKKIARTKEFKNSRNGKGQNGSPENEEEDKTLYCFCQRVSFGEMVACDGPNCKYEWFHYDCVNLKEPPKGTWYCPECKIEMEKNKLKRKRN | ||||||
Modified residue | 183 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 185 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 188 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P38806 | EPL1 P43572 | 11 | EBI-24622, EBI-22792 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 35-86 | |||||
Sequence: LIEEKKKYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQSLQREK | ||||||
Region | 123-217 | Disordered | ||||
Sequence: DGDMDSAAEASRESSVVSNSSVKKRRAASSSGSVPPTLKKKKTSRTSKLQNEIDVSSREKSVTPVSPSIEKKIARTKEFKNSRNGKGQNGSPENE | ||||||
Compositional bias | 133-162 | Polar residues | ||||
Sequence: SRESSVVSNSSVKKRRAASSSGSVPPTLKK | ||||||
Zinc finger | 222-271 | PHD-type | ||||
Sequence: TLYCFCQRVSFGEMVACDGPNCKYEWFHYDCVNLKEPPKGTWYCPECKIE |
Domain
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence similarities
Belongs to the ING family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length282
- Mass (Da)32,086
- Last updated1995-02-01 v1
- Checksum110E0A2536547D03
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 133-162 | Polar residues | ||||
Sequence: SRESSVVSNSSVKKRRAASSSGSVPPTLKK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00060 EMBL· GenBank· DDBJ | AAB68930.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006934 EMBL· GenBank· DDBJ | DAA06786.1 EMBL· GenBank· DDBJ | Genomic DNA |