IUBMB Enzyme Nomenclature


Accepted name: type IV protein arginine methyltransferase

Reaction: S-adenosyl-L-methionine + [protein]-L-arginine = S-adenosyl-L-homocysteine + [protein]-N5-methyl-L-arginine

Other name(s): RMT2 (gene name)

Systematic name: S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-N5-methyl-L-arginine-forming)

Comments: This enzyme, characterized from the yeast Saccharomyces cerevisiae, methylates the the δ-nitrogen atom of arginine residues within proteins. Among its substrates are Arg67 of the ribosomal protein L12. cf. EC, type I protein arginine methyltransferase, EC, type II protein arginine methyltransferase, and EC, type III protein arginine methyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:


1. Niewmierzycka, A. and Clarke, S. S-Adenosylmethionine-dependent methylation in Saccharomyces cerevisiae. Identification of a novel protein arginine methyltransferase. J. Biol. Chem. 274 (1999) 814-824. [PMID: 9873020]

2. Chern, M.K., Chang, K.N., Liu, L.F., Tam, T.C., Liu, Y.C., Liang, Y.L. and Tam, M.F. Yeast ribosomal protein L12 is a substrate of protein-arginine methyltransferase 2. J. Biol. Chem. 277 (2002) 15345-15353. [PMID: 11856739]

3. Olsson, I., Berrez, J.M., Leipus, A., Ostlund, C. and Mutvei, A. The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100. Exp Cell Res 313 (2007) 1778-1789. [PMID: 17448464]

[EC created 2015]

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