FEATURES

FAMILY

Protein arginine N-methyltransferase family

DESCRIPTION

Also known as ANM8_HUMAN, PRMT8, HRMT1L3, HRMT1L4. S-adenosyl-L-methionine-dependent and membrane-associated arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA) in proteins such as NIFK, myelin basic protein, histone H4, H2A and H2A/H2B dimer (PubMed:16051612, PubMed:17925405, PubMed:26876602, PubMed:26529540). Able to mono- and dimethylate EWS protein; however its precise role toward EWS remains unclear as it still interacts with fully methylated EWS (PubMed:18320585). Homodimer (PubMed:16051612, PubMed:26876602, PubMed:26529540). Tetramer; individual homodimers associates to form a homotetramer (PubMed:26529540). Homooctamer; individual homodimers associates to form a homooctamer and homooligomerization is required for proper localization to the cell membrane (PubMed:26876602). Heterodimer with PRMT1; heterodimerization may recruit PRMT1 activity to the plasma membrane (PubMed:16051612). Interacts with PRMT2 (via the SH3 domain) (PubMed:17925405). Interacts with FYN (via the SH3 domain) (PubMed:17925405). Interacts with EWS; independently of EWS methylation status (PubMed:18320585).

EXTERNAL LINKS

PRMT8

Mutations

Mutation(s) distribution

Mutations table