Overview:

PRMT7 (protein arginine methyltransferase 7), an arginine methyltransferase that exhibited type III enzymatic activity, catalyzing the formation of ω-NG-monomethylarginine residues. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency.

Gene Aliases:

FLJ10640, KIAA1933

Genbank Number:

BC000146

References:

1. Miranda TB, et al: PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J Biol Chem. 279(22):22902-7, 2004.

2. Lee JH, et al: PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine. J Biol Chem. 280(5):3656-64, 2005.

3. http://www.uniprot.org/uniprot/Q9NVM4