Function and Biology Details
Reaction catalysed:
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Interferon regulatory factor-3
- Nucleolar pre-ribosomal-associated protein 1, N-terminal
- Nuclear receptor coactivator, CREB-bp-like, interlocking domain superfamily
- Nuclear receptor coactivator, CREB-bp-like, interlocking
- Nuclear receptor coactivator, interlocking
- SMAD/FHA domain superfamily
- SMAD-like domain superfamily
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159751 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Interferon regulatory factor 3
Molecule details ›
Chains: A, B
Length: 210 amino acids
Theoretical weight: 23.65 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Interferon-regulatory factor 3
Length: 210 amino acids
Theoretical weight: 23.65 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P70671 (Residues: 184-390; Coverage: 49%)
Sequence domains: Interferon-regulatory factor 3
CREB-binding protein
Molecule details ›
Chains: C, D
Length: 47 amino acids
Theoretical weight: 5.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Creb binding
Length: 47 amino acids
Theoretical weight: 5.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q92793 (Residues: 2065-2111; Coverage: 2%)
Sequence domains: Creb binding
