InterPro : IPR025799

Name  Protein arginine N-methyltransferase Short Name  Arg_MeTrfase
Type  Family Description  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 [, , ]. PRMTs use S-adenosylmethionine(SAM or AdoMet)-dependent methylation to modify the guanidino nitrogens of the arginine side chain by adding one or two methyl groups []. According to their methylation status, the PRMT enzymes are classified into different group types. While the type-I PRMT enzymes catalyse the formation of monomethylarginine (MMA) and asymmetric dimethylarginine (aDMA), the type-II PRMT enzymes form MMA and symmetric dimethylarginine (sDMA). The enzymes PRMT1, PRMT3, PRMT4, PRMT6 and PRMT8 belong to the type-I and PRMT5, PRMT7 and PRMT9 to type-II.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

2 Child Features

Id Name Short Name Type
IPR007857 Protein arginine N-methyltransferase PRMT5 Arg_MeTrfase_PRMT5 Family
IPR014644 Protein arginine N-methyltransferase PRMT7 MeTrfase_PRMT7 Family

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0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Pahlich S Protein arginine methylation: Cellular functions and methods of analysis. 2006 Biochim Biophys Acta 1764 1890-903
Wolf SS The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans. 2009 Cell Mol Life Sci 66 2109-21
Bedford MT Arginine methylation an emerging regulator of protein function. 2005 Mol Cell 18 263-72
Bedford MT Arginine methylation at a glance. 2007 J Cell Sci 120 4243-6



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)