Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
433
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Region 3rib A 1-6 disorder
Region 3rib A 7-433 order
Region 3rib B 1-6 disorder
Region 3rib B 7-280 order
Region 3rib B 281-287 disorder
Region 3rib B 288-331 order
Region 3rib B 332-336 disorder
Region 3rib B 337-433 order
Region 3s7b A 1-4 disorder
Region 3s7b A 5-433 order
Region 3s7j A 1-5 disorder
Region 3s7j A 6-433 order
Region 3tg4 A 1-5 disorder
Region 3tg4 A 6-432 order
Region 3tg4 A 433-433 disorder
Region 4wuy A 1-4 disorder
Region 4wuy A 5-280 order
Region 4wuy A 281-286 disorder
Region 4wuy A 287-306 order
Region 4wuy A 307-315 disorder
Region 4wuy A 316-433 order
Region 4ynd A 1-2 disorder
Region 4ynd A 3-430 order
Region 4ynd A 431-433 disorder
Region 5arf A 2-5 disorder
Region 5arf A 6-430 order
Region 5arf A 431-433 disorder
Region 5arg A 2-5 disorder
Region 5arg A 6-431 order
Region 5arg A 432-433 disorder
Region 5kjk A 5-433 order
Region 5kjl A 5-5 disorder
Region 5kjl A 6-433 order
Region 5kjm A 5-433 order
Region 5kjn A 5-433 order
Region 5wcg A 1-1 disorder
Region 5wcg A 5-5 disorder
Region 5wcg A 6-432 order
Region 5wcg A 433-433 disorder
Region 6cbx A 1-4 disorder
Region 6cbx A 5-432 order
Region 6cbx A 433-433 disorder
Region 6cbx B 1-432 order
Region 6cbx B 433-433 disorder
Region 6cby A 1-4 disorder
Region 6cby A 5-432 order
Region 6cby A 433-433 disorder
Region 6cby B 1-4 disorder
Region 6cby B 5-279 order
Region 6cby B 280-286 disorder
Region 6cby B 287-433 order
Seq 1-433 Hetero dimer : IID00013 Complex
Region 4o6f A 1-2 disorder
Region 4o6f A 3-432 order
Region 4o6f A 433-433 disorder
Region 3s7f A 1-4 disorder
Region 3s7f A 5-433 order
Region 3s7d A 1-4 disorder
Region 3s7d A 5-433 order
Seq 1-433 Hetero dimer : IID00015 Complex
Region 3tg5 A 1-5 disorder
Region 3tg5 A 6-430 order
Region 3tg5 A 431-433 disorder
Function
Function in SwissProt
Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Biological Process
See also
Diagram with PDB data
ESR1/SMYD2 Structural Basis of Estrogen Receptor Alpha Methylation Mediated by Histone Methyltransferase SmyD2
TP53/SMYD2 Structure of SMYD2 in complex with p53 and SAH