Protein arginine N-methyltransferase domain

Definition

This entry represents a domain found C-terminal in Protein arginine N-methyltransferase 1 and twice in Protein arginine N-methyltransferase 7. This domain is also found in histone-arginine methyltransferases CARM1 and CARMER. CARM1 methylates (mono- and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in several proteins involved in DNA packaging, transcription regulation, pre-mRNA splicing, and mRNA stability [[cite:PMID:12237300], [cite:PMID:16497732], [cite:PMID:19405910]]. This domain shows a β-barrel structure PMID:12737817 and is involved in oligomerization. Protein arginine methyltransferases (PRMTs) are enzymes that transfer methyl groups to the arginine residues of histones and other proteins. Arginine methylation is an important posttranslational modification process that plays functional roles in transcriptional control, splicing, DNA repair, and signaling [[cite:PMID:17010682], [cite:PMID:19300908], [cite:PMID:18057026]].

8 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (8 proteins: gene, accession, name)

• CARM1
• PRMT1
• PRMT2
• PRMT3
• PRMT6
• PRMT7
• PRMT8
• PRMT9