Complex: NuA4 histone acetyltransferase complex
Macromolecular complex annotations are imported from the Complex Portal. These annotations have been derived from physical molecular interaction evidence extracted from the literature and cross-referenced in the entry, or by curator inference from information on homologs in closely related species or by inference from scientific background.
- Curated by
- MINT
- ComplexAc
- CPX-3155
- Systematic Name
- ACT1:ARP4:EAF1:EAF3:EAF5:EAF6:EAF7:EPL1:ESA1:SWC4:TRA1:VID21:YAF9:YNG2
- SGD ID
- SGD:S000218218
- Description
- Essential gene regulatory acetyltransferase with ATPase, DNA helicase and structural DNA binding activities. NuA4 histone acetyltransferase (HAT) complex 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, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression.
Complex Diagram
This diagram displays the protein subunits (blue) of the complex and how they interact with each other. Interactions with other relevant participants such as small molecules (purple), sub-complexes (yellow), and other subunits (red) are also shown. If a participant appears in the diagram with no lines connected to it, then its specific interactions with other participants are currently unknown.
PDB Structure
When available from the Protein Data Bank (PDB), the physical structure of the macromolecular complex is displayed. Click on the image or link for further information about the physical structure.
| 5Y81 |
Subunits
This table lists all participants of the complex (proteins, small molecules, nucleic acids, etc.) and their respective stoichiometry. A brief description is also provided for each participant in the table.
Increase the total number of rows showing on this page by using the pull-down located below the table, or use the page scroll at the table's top right to browse through its pages; use the arrows to the right of a column header to sort by that column; filter the table using the "Filter" box at the top of the table.
| Subunit | Description | Stoichiometry |
|---|
Gene Ontology
Gene Ontology (GO) terms that describe the function of a complex, the biological process in which it participates, or its cellular location. Click on a term for its definition and other objects annotated to that term.
- Molecular Function
-
- enables histone acetyltransferase activity (IDA)
- Biological Process
-
- involved in DNA-templated transcription (BSR)
- acts upstream of or within nucleotide-excision repair (IMP)
Shared Annotations
This diagram displays Gene Ontology terms (green) and subunits (blue) that are shared between the given macromolecular complex (black) and other yeast complexes (yellow). The shared GO terms or subunits can be visualized separately using the radio button at the bottom of the graph. Note: No diagram is shown ("No shared annotations") if there are less than 2 shared annotations (either GO terms or subunits of other complexes) between this complex and any other complexes.
References
List of references used specifically to curate the information on this page.
- Wang X, et al. (2018) Architecture of the Saccharomyces cerevisiae NuA4/TIP60 complex. Nat Commun 9(1):1147 PMID: 29559617
- Rossetto D, et al. (2014) Eaf5/7/3 form a functionally independent NuA4 submodule linked to RNA polymerase II-coupled nucleosome recycling. EMBO J 33(12):1397-415 PMID: 24843044
- Chittuluru JR, et al. (2011) Structure and nucleosome interaction of the yeast NuA4 and Piccolo-NuA4 histone acetyltransferase complexes. Nat Struct Mol Biol 18(11):1196-203 PMID: 21984211
- Doyon Y and Côté J (2004) The highly conserved and multifunctional NuA4 HAT complex. Curr Opin Genet Dev 14(2):147-54 PMID: 15196461
Resources
IntAct | ModelArchive | PDB:5Y81 ... Show all Show fewer