Function and Biology Details
Reaction catalysed:
S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-169858 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Retinoblastoma-binding protein 5
Molecule details ›
Chain: J
Length: 27 amino acids
Theoretical weight: 3.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Length: 27 amino acids
Theoretical weight: 3.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q15291 (Residues: 330-356; Coverage: 5%)
Set1/Ash2 histone methyltransferase complex subunit ASH2
Molecule details ›
Chain: B
Length: 184 amino acids
Theoretical weight: 20.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: SPRY domain
Structure domains: Jelly Rolls
Length: 184 amino acids
Theoretical weight: 20.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q9UBL3 (Residues: 380-496, 516-598; Coverage: 28%)
Sequence domains: SPRY domain
Structure domains: Jelly Rolls
MLL cleavage product C180
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 18.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: SET domain
Structure domains: SET domain
Length: 158 amino acids
Theoretical weight: 18.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q03164 (Residues: 3813-3969; Coverage: 4%)
Sequence domains: SET domain
Structure domains: SET domain
