title: The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans.
abstract: Information about the family of protein arginine methyltransferases (PRMTs) has been growing rapidly over the last few years and the emerging role of arginine methylation involved in cellular processes like signaling, RNA processing, gene transcription, and cellular transport function has been investigated. To date, 11 PRMTs gene transcripts have been identified in humans. Almost all PRMTs have been shown to have enzymatic activity and to catalyze arginine methylation. This review will summarize the overall function of human PRMTs and include novel highlights on each family member.
authors.affiliation: Bayer Schering Pharma AG, Global Drug Discovery, TRG Women's Healthcare, Muellerstr 178, 13353, Berlin, Germany. siegmund.wolf@bayerhealthcare.com
authors.forename: S S
authors.initials: SS
authors.lastname: Wolf
mesh_terms: D000818:Animals; D001120:Arginine / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism*; D008745:Methylation; D015394:Molecular Structure; D010802:Phylogeny; D011499:Protein Processing, Post-Translational; D011484:Protein-Arginine N-Methyltransferases / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology
chemical_list: D007527:Isoenzymes; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases