InterPro : IPR014644

Name  Protein arginine N-methyltransferase PRMT7 Short Name  MeTrfase_PRMT7
Type  Family Description  This entry represents protein arginine N-methyltransferase PRMT7 [].PRMT7 can catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. It mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. It also mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. It plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. It may also play a role in embryonic stem cell (ESC) pluripotency [, , , ].
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Proteins

InterPro protein domain ID --> Contigs

 

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1 Parent Features

Id Name Short Name Type
IPR025799 Protein arginine N-methyltransferase Arg_MeTrfase Family

4 Publications

First Author Title Year Journal Volume Pages
Miranda TB PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. 2004 J Biol Chem 279 22902-7
Lee JH PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine. 2005 J Biol Chem 280 3656-64
Gonsalvez GB Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins. 2007 J Cell Biol 178 733-40
Wang H Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry. 2009 J Am Soc Mass Spectrom 20 507-19



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)