Protein arginine methylation in mammals: who, what, and why

Mol Cell. 2009 Jan 16;33(1):1-13. doi: 10.1016/j.molcel.2008.12.013.


The covalent marking of proteins by methyl group addition to arginine residues can promote their recognition by binding partners or can modulate their biological activity. A small family of gene products that catalyze such methylation reactions in eukaryotes (PRMTs) works in conjunction with a changing cast of associated subunits to recognize distinct cellular substrates. These reactions display many of the attributes of reversible covalent modifications such as protein phosphorylation or protein lysine methylation; however, it is unclear to what extent protein arginine demethylation occurs. Physiological roles for protein arginine methylation have been established in signal transduction, mRNA splicing, transcriptional control, DNA repair, and protein translocation.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arginine / metabolism*
  • Mammals / metabolism*
  • Methylation
  • Molecular Sequence Data
  • Protein-Arginine N-Methyltransferases / chemistry
  • Protein-Arginine N-Methyltransferases / metabolism
  • Proteins / chemistry
  • Proteins / metabolism*
  • Substrate Specificity


  • Proteins
  • Arginine
  • Protein-Arginine N-Methyltransferases