protein arginine N-methyltransferase 8; heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4 (PRMT8, HRMT1L4)
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Function
- membrane-associated protein arginine N-methyltransferase
- catalyzes formation of omega-N monomethylarginine (MMA) & asymmetrical dimethylarginine (aDMA)
- able to mono- & dimethylate EWS protein;
- role toward EWS remains unclear as it still interacts with fully methylated EWS
- homodimers & heterodimers with PRMT1 or PRMT2, recruiting PRMT1 to the cell membrane
- interacts with PRMT2 & FYN (via the SH3 domain)
- interacts with EWS; independently of EWS methylation status
- KM=1.3 uM for GRGGFGGRGGFRGGRGG-NH2
Structure
- the SH3-binding motifs mediate the interaction with SH3 domain-containing proteins such as PRMT2 & FYN, possibly leading to displace the N-terminal domain & activate the protein the N-terminal region (1-60) inhibits the enzymatic activity
- belongs to the protein arginine N-methyltransferase family, PRMT8 subfamily
Compartment
- cell membrane; lipid-anchor; cytoplasmic side
Alternative splicing
named isoforms=2
Expression
brain-specific