InterPro domain: IPR007857

This entry represents a group of arginine N-methyltransferases, including Skb1 from S. pombe [ 1 ], Hsl7 from S. cerevisiae [ 2 ] and their homologues PRMT5 from animals [ 3 , 4 , 5 ] and plants [ 6 ]. Skb1 is a mediator of hyperosmotic stress response in Schizosaccharomyces pombe [ 7 ]. Plant PMRT15 is involved in the post-transcriptional regulation of the circadian clock [ 7 ]. Human PRMT5 is a component of multiple protein complexes and contributes to essential cellular processes, such as RNA transport and splicing, cell cycle regulation, tumour growth, and chromatin remodelling, leading to either gene silencing or activation [ 8 ].

1. The highly conserved protein methyltransferase, Skb1, is a mediator of hyperosmotic stress response in the fission yeast Schizosaccharomyces pombe. J. Biol. Chem. 276, 14549-52
2. Hsl7p, the yeast homologue of human JBP1, is a protein methyltransferase. Biochem. Biophys. Res. Commun. 274, 105-11
3. The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. J. Biol. Chem. 274, 31531-42
4. Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. J. Biol. Chem. 276, 11393-401
5. Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. J. Cell Biol. 178, 733-40
6. SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis. EMBO J. 26, 1934-41
7. A methyl transferase links the circadian clock to the regulation of alternative splicing. Nature 468, 112-6
8. HOXA9 methylation by PRMT5 is essential for endothelial cell expression of leukocyte adhesion molecules. Mol. Cell. Biol. 32, 1202-13