EC - Type II protein arginine methyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
type II protein arginine methyltransferase
Other names:
PRMT5 (gene name)
PRMT9 (gene name)
Systematic name:
S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nω,Nω'-dimethyl-L-arginine-forming)



The enzyme catalyses the methylation of one of the terminal guanidino nitrogen atoms in arginine residues within proteins, forming monomethylarginine, followed by the methylation of the second terminal nitrogen atom to form a symmetrical dimethylarginine. The mammalian enzyme is active in both the nucleus and the cytoplasm, and plays a role in the assembly of snRNP core particles by methylating certain small nuclear ribonucleoproteins. cf. EC, type I protein arginine methyltransferase, EC, type III protein arginine methyltransferase, and EC, type IV protein arginine methyltransferase.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0035243
UniProtKB/Swiss-Prot: (35) [show] [UniProt]


  1. Branscombe, T. L., Frankel, A., Lee, J. H., Cook, J. R., Yang , Z., Pestka, S., Clarke, S.
    PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins.
    J. Biol. Chem. 276 : 32971-32976 (2001). [PMID: 11413150]
  2. Wang, X., Zhang, Y., Ma, Q., Zhang, Z., Xue, Y., Bao, S., Chong, K.
    SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis.
    EMBO J. 26 : 1934-1941 (2007). [PMID: 17363895]
  3. Lacroix, M., El Messaoudi, S., Rodier, G., Le Cam, A., Sardet, C., Fabbrizio, E.
    The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5.
    EMBO Rep. 9 : 452-458 (2008). [PMID: 18404153]
  4. Chari, A., Golas, M. M., Klingenhager, M., Neuenkirchen, N., Sander, B., Englbrecht, C., Sickmann, A., Stark, H., Fischer, U.
    An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs.
    Cell 135 : 497-509 (2008). [PMID: 18984161]
  5. Antonysamy, S., Bonday, Z., Campbell, R. M., Doyle, B., Druzina, Z., Gheyi, T., Han, B., Jungheim, L. N., Qian, Y., Rauch, C., Russell, M., Sauder, J. M., Wasserman, S. R., Weichert, K., Willard, F. S., Zhang, A., Emtage, S.
    Crystal structure of the human PRMT5:MEP50 complex.
    Proc. Natl. Acad. Sci. U.S.A. 109 : 17960-17965 (2012). [PMID: 23071334]
  6. Hadjikyriacou, A., Yang, Y., Espejo, A., Bedford, M. T., Clarke, S. G.
    Unique Features of Human Protein Arginine Methyltransferase 9 (PRMT9) and Its Substrate RNA Splicing Factor SF3B2.
    J. Biol. Chem. 290 : 16723-16743 (2015). [PMID: 25979344]

[EC created 2015]