protein arginine N-methyltransferase 7; histone-arginine N-methyltransferase PRMT7, [myelin basic protein]-arginine N-methyltransferase PRMT7 (PRMT7, KIAA1933)
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Function
- protein arginine N-methyltransferase
- catalyzes formation of omega-N monomethylarginine (MMA) & symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA
- specifically mediates symmetrical dimethylation of Arg in the small nuclear ribonucleoproteins Sm-D1 (SNRPD1) & Sm-D3 (SNRPD3); methylation is required for assembly & biogenesis of snRNP core particles
- specifically mediates symmetric dimethylation of histone H4 Arg-3 to form H4R3me2s
- role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) & methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites
- may also play a role in pluripotent embryonic stem cells
- also able to mediate Arg methylation of histone H2A & myelin basic protein (MBP) in vitro (relevance uncertain)
- homodimer & heterodimer (putative)
- interacts with CTCFL (putative)
- interacts with PRMT5 & SNRPD3
S-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]
S-adenosyl-L-methionine + [[[A144869|myelin basic protein]]]-arginine = S-adenosyl-L-homocysteine + [[[A144869|myelin basic protein]]]-N(omega)- methyl-arginine
Structure
- belongs to the protein arginine N-methyltransferase family, PRMT7 subfamily
Compartment
Alternative splicing
named isoforms=4
Pharmacology
- may be involved in etoposide-induced cytotoxicity
- down-regulation of PRMT7 confers increased sensitivity of Top1 to inhibition by camptothecin