CATH Classification

Domain Context

CATH Clusters

Superfamily Hnrnp arginine n-methyltransferase1
Functional Family Protein arginine N-methyltransferase 5

Enzyme Information

2.1.1.320
Type II protein arginine methyltransferase.
based on mapping to UniProt O14744
2 S-adenosyl-L-methionine + [protein]-L-arginine = 2 S-adenosyl-L- homocysteine + [protein]-N(omega),N(omega')-dimethyl-L-arginine.
-!- The enzyme catalyzes the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. -!- The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. -!- Cf. EC 2.1.1.319, 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)

Q9BQA1
MEP50_HUMAN
Homo sapiens
Methylosome protein 50

PDB Structure

PDB 4X61
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models.
Chan-Penebre, E., Kuplast, K.G., Majer, C.R., Boriack-Sjodin, P.A., Wigle, T.J., Johnston, L.D., Rioux, N., Munchhof, M.J., Jin, L., Jacques, S.L., West, K.A., Lingaraj, T., Stickland, K., Ribich, S.A., Raimondi, A., Scott, M.P., Waters, N.J., Pollock, R.M., Smith, J.J., Barbash, O., Pappalardi, M., Ho, T.F., Nurse, K., Oza, K.P., Gallagher, K.T., Kruger, R., Moyer, M.P., Copeland, R.A., Chesworth, R., Duncan, K.W.
Nat.Chem.Biol.