CARM1 monoclonal antibody

Protein arginine N-methyltransferase 1 (PRMT1) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine. Though all PRMT proteins catalyze the formation of mono-methyl arginine, Type I PRMTs (PRMT1, 3, 4, and 6) add an additional methyl group to produce an asymmetric di-methyl arginine while Type II PRMTs (PRMT 5 and 7) produce symmetric di-methyl arginine. Mono-methyl arginine, but not di-methyl arginine, can be converted to citrulline through deimination catalyzed by enzymes such as PADI4 . Most PRMTs, including PRMT1, methylate arginine residues found within glycine-arginine rich (GAR) protein domains, such as RGG, RG, and RXR repeats. However, PRMT4/CARM1 and PRMT5 methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs. PRMT1 methylates Arg3 of histone H4 and cooperates synergistically with p300/CBP to enhance transcriptional activation by nuclear receptor proteins. In addition, PRMT1 methylates many non-histone proteins, including the orphan nuclear receptor HNF4, components of the heterogeneous nuclear ribonucleoprotein (hnRNP) particle, the RNA binding protein Sam68, interleukin enhancer-binding factor 3 (ILF3) and interferon-α and β receptors. These interactions suggest additional functions in transcriptional regulation, mRNA processing and signal transduction. Alternative mRNA splicing produces three enzymatically active PRMT1 isoforms that differ in their amino-terminal regions. PRMT1 is localized to the nucleus or cytoplasm, depending on cell type, and appears in many distinct protein complexes. ILF3, TIS21 and the leukemia-associated BTG1 proteins bind PRMT1 to regulate its methyltransferase activity.