Q4WHG1 · ESA1_ASPFU
- ProteinHistone acetyltransferase esa1
- Geneesa1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids483 (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 | 336-340 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: ACILT | ||||||
Site | 337 | Important for catalytic activity | ||||
Sequence: C | ||||||
Binding site | 345-351 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: QRRGFGR | ||||||
Active site | 371 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 375 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | NuA4 histone acetyltransferase complex | |
Cellular Component | nucleus | |
Cellular Component | pericentric heterochromatin | |
Cellular Component | site of double-strand break | |
Cellular Component | Swr1 complex | |
Molecular Function | chromatin binding | |
Molecular Function | histone H3K4 acetyltransferase activity | |
Molecular Function | histone H4K16 acetyltransferase activity | |
Molecular Function | peptide 2-hydroxyisobutyryltransferase activity | |
Molecular Function | peptide butyryltransferase activity | |
Molecular Function | peptide crotonyltransferase activity | |
Molecular Function | transcription coregulator activity | |
Biological Process | biosynthetic process | |
Biological Process | DNA repair | |
Biological Process | DNA repair-dependent chromatin remodeling | |
Biological Process | positive regulation of heterochromatin formation | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone acetyltransferase esa1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionQ4WHG1
Proteomes
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_0000051552 | 1-483 | Histone acetyltransferase esa1 | |||
Sequence: MLLLMFALLQDGELRKAEILSIRQRKDGPSFYVHYVDFNKRLDEWIDASRLDLSHEVEWPQPEKPEKKKTGVGNKAPSKNAQKRARADSRDVSATPDLLTGKNVNVGKAQRPSKAGGKENRDGTPLSMPIVTAEAISTDGTPKAESDDVEMVDVSFTDGKSIKEEERALGLMSREEEIERLRTSGSMTQNPTEIHRVRNLNRLQMGKYDIEPWYFSPYPASFSDADIIYIDEFCLSYFDDKRAFERHRTKCTLVHPPGNEIYRDDYISFFEVDGRRQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMCTRDETGCHLVGYFSKEKDSAEGYNLACILTLPQYQRRGFGRLLISFSYELSKREGKLGSPEKPLSDLGLLGYRQYWRETLVEILMEPGRETVSENELALLTSMTEKDVHETLVVLNMLRYYKGNWVIVLTDYVVEQHKKRLEKEKLKGARKIDPARLQWKPPVFTASSRTWNW | ||||||
Modified residue | 295 | N6-acetyllysine; by autocatalysis | ||||
Sequence: K |
Post-translational modification
Autoacetylation at Lys-295 is required for proper function.
Keywords
- PTM
Interaction
Subunit
Component of the NuA4 histone acetyltransferase complex.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, zinc finger, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 10-53 | Tudor-knot | ||||
Sequence: QDGELRKAEILSIRQRKDGPSFYVHYVDFNKRLDEWIDASRLDL | ||||||
Compositional bias | 57-73 | Basic and acidic residues | ||||
Sequence: VEWPQPEKPEKKKTGVG | ||||||
Region | 57-127 | Disordered | ||||
Sequence: VEWPQPEKPEKKKTGVGNKAPSKNAQKRARADSRDVSATPDLLTGKNVNVGKAQRPSKAGGKENRDGTPLS | ||||||
Domain | 195-471 | MYST-type HAT | ||||
Sequence: HRVRNLNRLQMGKYDIEPWYFSPYPASFSDADIIYIDEFCLSYFDDKRAFERHRTKCTLVHPPGNEIYRDDYISFFEVDGRRQRTWCRNLCLLSKLFLDHKTLYYDVDPFLFYCMCTRDETGCHLVGYFSKEKDSAEGYNLACILTLPQYQRRGFGRLLISFSYELSKREGKLGSPEKPLSDLGLLGYRQYWRETLVEILMEPGRETVSENELALLTSMTEKDVHETLVVLNMLRYYKGNWVIVLTDYVVEQHKKRLEKEKLKGARKIDPARLQWKP | ||||||
Zinc finger | 228-253 | C2HC MYST-type; degenerate | ||||
Sequence: IYIDEFCLSYFDDKRAFERHRTKCTL | ||||||
Motif | 278-299 | ESA1-RPD3 motif | ||||
Sequence: RTWCRNLCLLSKLFLDHKTLYY |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length483
- Mass (Da)55,969
- Last updated2005-07-05 v1
- Checksum8EBF3CDAE55CE6F8
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 57-73 | Basic and acidic residues | ||||
Sequence: VEWPQPEKPEKKKTGVG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAHF01000008 EMBL· GenBank· DDBJ | EAL87644.1 EMBL· GenBank· DDBJ | Genomic DNA |