Q7S9B6 · ESA1_NEUCR
- ProteinHistone acetyltransferase esa-1
- Geneesa-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids506 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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 (By similarity).
Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity).
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 (By similarity).
Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins (By similarity).
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 (By similarity).
Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity).
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 (By similarity).
Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins (By similarity).
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 (By similarity).
Catalytic activity
- acetyl-CoA + L-lysyl-[histone] = CoA + H+ + N6-acetyl-L-lysyl-[histone]This reaction proceeds in the forward direction.
- acetyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-acetyl-L-lysyl-[protein]This reaction proceeds in the forward direction.
- 2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-(2-hydroxyisobutanoyl)-L-lysyl-[protein]This reaction proceeds in the forward direction.
- (2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H+ + N6-(2E)-butenoyl-L-lysyl-[protein]This reaction proceeds in the forward direction.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 361-365 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: ACILT | ||||||
Site | 362 | Important for catalytic activity | ||||
Sequence: C | ||||||
Binding site | 370-376 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: QRKGYGR | ||||||
Active site | 396 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 400 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | NuA4 histone acetyltransferase complex | |
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Cellular Component | piccolo histone acetyltransferase complex | |
Molecular Function | chromatin binding | |
Molecular Function | histone crotonyltransferase activity | |
Molecular Function | histone H4K16 acetyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | peptide 2-hydroxyisobutyryltransferase activity | |
Molecular Function | transcription coregulator activity | |
Biological Process | DNA repair | |
Biological Process | DNA-templated transcription elongation | |
Biological Process | positive regulation of macroautophagy | |
Biological Process | positive regulation of transcription elongation by RNA polymerase II | |
Biological Process | positive regulation of triglyceride biosynthetic process | |
Biological Process | rDNA heterochromatin formation | |
Biological Process | regulation of cell cycle | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone acetyltransferase esa-1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Sordariaceae > Neurospora
Accessions
- Primary accessionQ7S9B6
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Following DNA damage, localizes to sites of DNA damage, such as double stand breaks (DSBs).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000051559 | 1-506 | Histone acetyltransferase esa-1 | |||
Sequence: MSPPGGDATVGSDEKRQKGKATPDTIKMGCIAMVMKEGQLRRAEILSIKDTKSGRQFYCNFDNFNKRLDEWVPAARIDFEQDVEWPNPDKDKQKDAKTKKNNSTVSKKQPSKKNNQKKASKREQSVASDGQTPHPWTEFVESQPGKNNRQRGKTEDGTDVNASLEVGGDKGVKRKADEIDMDEDEIPAAKKQRQPSFSREQEIEKLRTSGSMTQNPTEISRIRNISKVEFGRYVLFPWYFSPYPQIFDQEDCIYICEFCLSYYGELKSFVRHRQKCTLHHPPGNEIYRDDYVSFFEIDGRRQRTWCRNLCLLSKMFLDHKTLYYDVDPFLFYVMTTRDDRGCHIIGYFSKEKESTDGYNVACILTLPQYQRKGYGRLLIQFSYELSKIEGKLGSPEKPLSDLGLLSYRQYWSENIIDILLGYNERKEACTIENIAVALAMTTQDVEHTLQALKMQVYHKGEHKIVVPEKLIKQREKSKAKQKRLIDPERIQWKPPVFTALNRTWGW | ||||||
Modified residue | 320 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K |
Post-translational modification
Autoacetylation at Lys-320 is required for proper function.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Component of the NuA4 histone acetyltransferase complex.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, zinc finger, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MSPPGGDATVGSDEKRQKGKATPD | ||||||
Domain | 26-78 | Tudor-knot | ||||
Sequence: IKMGCIAMVMKEGQLRRAEILSIKDTKSGRQFYCNFDNFNKRLDEWVPAARID | ||||||
Compositional bias | 82-102 | Basic and acidic residues | ||||
Sequence: DVEWPNPDKDKQKDAKTKKNN | ||||||
Region | 82-215 | Disordered | ||||
Sequence: DVEWPNPDKDKQKDAKTKKNNSTVSKKQPSKKNNQKKASKREQSVASDGQTPHPWTEFVESQPGKNNRQRGKTEDGTDVNASLEVGGDKGVKRKADEIDMDEDEIPAAKKQRQPSFSREQEIEKLRTSGSMTQN | ||||||
Compositional bias | 125-147 | Polar residues | ||||
Sequence: SVASDGQTPHPWTEFVESQPGKN | ||||||
Compositional bias | 168-206 | Basic and acidic residues | ||||
Sequence: GDKGVKRKADEIDMDEDEIPAAKKQRQPSFSREQEIEKL | ||||||
Domain | 220-494 | MYST-type HAT | ||||
Sequence: SRIRNISKVEFGRYVLFPWYFSPYPQIFDQEDCIYICEFCLSYYGELKSFVRHRQKCTLHHPPGNEIYRDDYVSFFEIDGRRQRTWCRNLCLLSKMFLDHKTLYYDVDPFLFYVMTTRDDRGCHIIGYFSKEKESTDGYNVACILTLPQYQRKGYGRLLIQFSYELSKIEGKLGSPEKPLSDLGLLSYRQYWSENIIDILLGYNERKEACTIENIAVALAMTTQDVEHTLQALKMQVYHKGEHKIVVPEKLIKQREKSKAKQKRLIDPERIQWKP | ||||||
Zinc finger | 253-278 | C2HC MYST-type | ||||
Sequence: IYICEFCLSYYGELKSFVRHRQKCTL | ||||||
Motif | 303-324 | ESA1-RPD3 motif | ||||
Sequence: RTWCRNLCLLSKMFLDHKTLYY |
Domain
The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.
Sequence similarities
Belongs to the MYST (SAS/MOZ) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length506
- Mass (Da)58,807
- Last updated2003-12-15 v1
- Checksum53A62414D139674A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 82-102 | Basic and acidic residues | ||||
Sequence: DVEWPNPDKDKQKDAKTKKNN | ||||||
Compositional bias | 125-147 | Polar residues | ||||
Sequence: SVASDGQTPHPWTEFVESQPGKN | ||||||
Compositional bias | 168-206 | Basic and acidic residues | ||||
Sequence: GDKGVKRKADEIDMDEDEIPAAKKQRQPSFSREQEIEKL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM002239 EMBL· GenBank· DDBJ | EAA32981.1 EMBL· GenBank· DDBJ | Genomic DNA |