2.1.1.- Protein arginine N-methyltransferases C

Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).

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Overview

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Protein arginine N-methyltransferases (PRMT, EC 2.1.1.-) encompass histone arginine N-methyltransferases (PRMT4, PRMT7, EC 2.1.1.125) and myelin basic protein N-methyltransferases (PRMT7, EC 2.1.1.126). They are dimeric or tetrameric enzymes which use S-adenosyl methionine as a methyl donor, generating S-adenosylhomocysteine as a by-product. They generate both mono-methylated and di-methylated products; these may be symmetric (SDMA) or asymmetric (NG,NG-dimethyl-L-arginine) versions, where both guanidine nitrogens are monomethylated or one of the two is dimethylated, respectively.

Enzymes

PRMT1 (protein arginine methyltransferase 1 ) Show summary » More detailed page

PRMT2 (protein arginine methyltransferase 2 ) Show summary »

PRMT3 (protein arginine methyltransferase 3) Show summary » More detailed page

PRMT4 (coactivator associated arginine methyltransferase 1) Show summary » More detailed page

PRMT5 (protein arginine methyltransferase 5 ) Show summary » More detailed page

PRMT6 (protein arginine methyltransferase 6) Show summary » More detailed page

PRMT7 (protein arginine methyltransferase 7 ) Show summary » More detailed page

PRMT8 (protein arginine methyltransferase 8) Show summary »

PRMT9 (F-box protein 11) Show summary »

PRMT10 (protein arginine methyltransferase 9) Show summary »

PRMT11 (F-box protein 10) Show summary »

References

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How to cite this family page

Database page citation:

2.1.1.- Protein arginine N-methyltransferases. Accessed on 11/12/2017. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/FamilyDisplayForward?familyId=254.

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Fabbro D, Kelly E, Marrion NV, Peters JA, Faccenda E, Harding SD, Pawson AJ, Sharman JL, Southan C, Davies JA; CGTP Collaborators. (2017) The Concise Guide to PHARMACOLOGY 2017/18: Enzymes. Br J Pharmacol. 174 Suppl 1: S272-S359.