B2ASN1 · B2ASN1_PODAN
- ProteinHistone acetyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids513 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which 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, and histone H2A to form H2AK4ac and H2AK7ac. The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively.
Catalytic activity
- (2E)-butenoyl-CoA + L-lysyl-[protein] = N6-(2E)-butenoyl-L-lysyl-[protein] + CoA + H+This reaction proceeds in the forward direction.
- 2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N6-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H+This reaction proceeds in the forward direction.
- L-lysyl-[protein] + acetyl-CoA = N6-acetyl-L-lysyl-[protein] + CoA + H+This reaction proceeds in the forward direction.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 403 | Proton donor/acceptor | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | histone H4K16 acetyltransferase activity | |
Molecular Function | peptide 2-hydroxyisobutyryltransferase activity | |
Molecular Function | peptide crotonyltransferase activity | |
Molecular Function | transcription coregulator activity | |
Biological Process | DNA repair | |
Biological Process | negative regulation of DNA-templated transcription | |
Biological Process | positive regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone acetyltransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Podosporaceae > Podospora > Podospora anserina
Accessions
- Primary accessionB2ASN1
Organism-specific databases
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Component of the NuA4 histone acetyltransferase complex.
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 92-112 | Basic and acidic residues | ||||
Sequence: EVEWPNPEKDKPKDPKSKKTT | ||||||
Region | 92-200 | Disordered | ||||
Sequence: EVEWPNPEKDKPKDPKSKKTTAATSKKSQPSKKNQKRVSKREQSVASEGQTPHPWTEYVENGQHKDKNQETEEKSMGSLEVGGTPGVLGPDEMEIDEDETPAGAAKKDS | ||||||
Compositional bias | 150-165 | Basic and acidic residues | ||||
Sequence: VENGQHKDKNQETEEK | ||||||
Domain | 227-501 | MYST-type HAT | ||||
Sequence: SRIRNISQVEFGRYVLFPWYFSPYPEVFSQEESIFICEFCLSYYADMKSFSRHRQKCTLQHPPGNEIYRDDFVSFFEIDGRRQRTWCRNLCLLSKMFLDHKTLYYDVDPFLFYVMTTRDERGCHLIGYFSKEKESTDGYNVACILTLPQYQRKGYGRLLIQFSYELSKIEGKLGSPEKPLSDLGLLSYRQYWSENIIDLLLGFSERDEKCTIETIAQHLAMTATDVEHTLQALKMQVYHKGEHKIVLSDKLVEQRAKSRAKQKRLIDPERIQWKP |
Sequence similarities
Belongs to the MYST (SAS/MOZ) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length513
- Mass (Da)59,390
- Last updated2008-05-20 v1
- ChecksumE082CAA5C52D7478
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 92-112 | Basic and acidic residues | ||||
Sequence: EVEWPNPEKDKPKDPKSKKTT | ||||||
Compositional bias | 150-165 | Basic and acidic residues | ||||
Sequence: VENGQHKDKNQETEEK |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU633897 EMBL· GenBank· DDBJ | CAP67404.1 EMBL· GenBank· DDBJ | Genomic DNA |