FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues

Biochem Biophys Res Commun. 2006 Apr 7;342(2):472-81. doi: 10.1016/j.bbrc.2006.01.167. Epub 2006 Feb 8.


We have identified a protein, FLJ12673 or FBXO11, that contains domains characteristically present in protein arginine methyltransferases (PRMTs). Immuno-purified protein expressed from one of the four splice variants in HeLa cells and in Escherichia coli exhibited methyltransferase activity. Monomethylarginine, symmetric, and asymmetric dimethylarginine (SDMA, ADMA) were formed on arginine residues. Accordingly, we have designated the protein PRMT9. PRMT9 is the third member of the PRMT family that forms SDMA modifications in proteins. Structurally, this protein is distinct from all other known PRMTs implying that convergent evolution allowed this protein to develop the ability to methylate arginine residues and evolved elements conserved in PRMTs to accomplish this.

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Arginine / metabolism*
  • Base Sequence
  • Evolution, Molecular
  • F-Box Proteins / genetics
  • F-Box Proteins / metabolism*
  • HeLa Cells
  • Humans
  • Isoenzymes / genetics
  • Isoenzymes / metabolism
  • Methylation
  • Mice
  • Molecular Sequence Data
  • Multigene Family
  • Protein-Arginine N-Methyltransferases / genetics
  • Protein-Arginine N-Methyltransferases / metabolism*
  • Rats
  • Sequence Alignment
  • Sequence Analysis, Protein


  • F-Box Proteins
  • Isoenzymes
  • Arginine
  • FBXO11 protein, human
  • Protein-Arginine N-Methyltransferases