CATH Classification

Domain Context

CATH Clusters

Superfamily Hnrnp arginine n-methyltransferase1
Functional Family Probable histone-arginine methyltransferase CARM1

Enzyme Information

2.1.1.319
Type I protein arginine methyltransferase.
based on mapping to UniProt Q86X55
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega)-dimethyl-L-arginine.
-!- This eukaryotic enzyme catalyzes the sequential dimethylation of one of the terminal guanidino nitrogen atoms in arginine residues, resulting in formation of asymmetric dimethylarginine residues. -!- Some forms (e.g. PRMT1) have a very wide substrate specificity, while others (e.g. PRMT4 and PRMT6) are rather specific. -!- The enzyme has a preference for methylating arginine residues that are flanked by one or more glycine residues. -!- PRMT1 is responsible for the bulk (about 85%) of total protein arginine methylation activity in mammalian cells. -!- Cf. EC 2.1.1.320, EC 2.1.1.321 and EC 2.1.1.322. -!- Formerly EC 2.1.1.23, EC 2.1.1.124, EC 2.1.1.125 and EC 2.1.1.126.

UniProtKB Entries (1)

Q86X55
CARM1_HUMAN
Homo sapiens
Histone-arginine methyltransferase CARM1

PDB Structure

PDB 2Y1W
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Basis for Carm1 Inhibition by Indole and Pyrazole Inhibitors
Sack, J.S., Thieffine, S., Bandiera, T., Fasolini, M., Duke, G.J., Jayaraman, L., Kish, K.F., Klei, H.E., Purandare, A.V., Rosettani, P., Troiani, S., Xie, D., Bertrand, J.A.
Biochem.J.