PRMT8
Domain
The SH3-binding motifs mediate the interaction with SH3 domain-containing proteins such as PRMT2 and FYN, possibly leading to displace the N-terminal domain and activate the protein.
The N-terminal region (1-60) inhibits the arginine N-methyltransferase activity.
Function
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:26529540, PubMed:26876602). 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).
Sequence Similarities
Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. PRMT8 subfamily.
Tissue Specificity
Brain-specific.
Cellular localization
- Cell membrane
- Lipid-anchor
- Cytoplasmic side
Alternative names
HRMT1L3, HRMT1L4, PRMT8, Protein arginine N-methyltransferase 8, Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4