The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

PRMT3  -  protein arginine methyltransferase 3

Homo sapiens

Synonyms: HRMT1L3, Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3, Protein arginine N-methyltransferase 3
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PRMT3


High impact information on PRMT3


Biological context of PRMT3

  • In vitro binding assays demonstrated that this was an interaction occurring via the C-terminal catalytic core domain of PRMT3 [4].
  • PRMT3 is unique in that its N-terminus harbours a C2H2 zinc-finger domain that is proposed to confer substrate specificity [5].
  • With GST-PRMT3, however, only nine dimethylated arginines, located mainly in the C-terminal region of EWS protein, could be assigned, indicating that structural determinants prevent complete methylation [6].

Associations of PRMT3 with chemical compounds

  • Using purified recombinant protein arginine methyltransferases (PRMTs), we showed that the C-terminal domain could be methylated by PRMT1, PRMT3, and PRMT4 in vitro and that both the R(544)-K mutant and the R(546)-K mutant were refractory toward these enzymes [7].

Other interactions of PRMT3


Analytical, diagnostic and therapeutic context of PRMT3


  1. Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3. Smith, J.J., Rücknagel, K.P., Schierhorn, A., Tang, J., Nemeth, A., Linder, M., Herschman, H.R., Wahle, E. J. Biol. Chem. (1999) [Pubmed]
  2. PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits. Bachand, F., Silver, P.A. EMBO J. (2004) [Pubmed]
  3. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. Tang, J., Gary, J.D., Clarke, S., Herschman, H.R. J. Biol. Chem. (1998) [Pubmed]
  4. DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo. Singh, V., Miranda, T.B., Jiang, W., Frankel, A., Roemer, M.E., Robb, V.A., Gutmann, D.H., Herschman, H.R., Clarke, S., Newsham, I.F. Oncogene (2004) [Pubmed]
  5. Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3). Swiercz, R., Person, M.D., Bedford, M.T. Biochem. J. (2005) [Pubmed]
  6. Different methylation characteristics of protein arginine methyltransferase 1 and 3 toward the Ewing Sarcoma protein and a peptide. Pahlich, S., Bschir, K., Chiavi, C., Belyanskaya, L., Gehring, H. Proteins (2005) [Pubmed]
  7. Alternative splicing modulates protein arginine methyltransferase-dependent methylation of fragile X syndrome mental retardation protein. Dolzhanskaya, N., Merz, G., Denman, R.B. Biochemistry (2006) [Pubmed]
  8. Effects of ADMA upon gene expression: an insight into the pathophysiological significance of raised plasma ADMA. Smith, C.L., Anthony, S., Hubank, M., Leiper, J.M., Vallance, P. PLoS Med. (2005) [Pubmed]
WikiGenes - Universities