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Gene Review

PRMT5  -  protein arginine methyltransferase 5

Homo sapiens

Synonyms: 72 kDa ICln-binding protein, HRMT1L5, Histone-arginine N-methyltransferase PRMT5, IBP72, JBP1, ...
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Disease relevance of PRMT5


High impact information on PRMT5

  • We have now identified a homolog of JBP1, JBP2, containing a domain related to the SWI2/SNF2 family of chromatin remodeling proteins that is upregulated in bloodstream form cells and interacts with nuclear chromatin [4].
  • We have previously identified a J binding protein (JBP1) involved in propagating J synthesis [4].
  • The PRMT5 complex, previously implicated in methylation and storage of Sm proteins, interacts with the SMN complex and enhances its activity in an ATP-dependent manner [5].
  • These phenotypes suggest a possible role for Skb1 as a mitotic inhibitor [6].
  • Homologs of Skb1 are encoded by open reading frames in the genomes of S. cerevisiae and Caenorhabditis elegans and by an uncharacterized human cDNA sequence [7].

Biological context of PRMT5


Anatomical context of PRMT5


Associations of PRMT5 with chemical compounds


Physical interactions of PRMT5

  • This implies that the PRMT5 complex is involved in an early stage of U7 snRNP assembly and hence may have a second snRNP assembly function unrelated to sDMA modification [8].
  • Protein-protein interaction studies indicate that PRMT5 and mSin3A interact with the same hSWI/SNF subunits as those targeted by c-Myc [15].
  • We show that MEP50 is important for methylosome activity and binds to JBP1 and to a subset of Sm proteins [16].
  • Markedly, recombinant COPR5 binds to the amino terminus of histone H4 and is required to recruit PRMT5 to reconstituted nucleosomes in vitro [17].

Other interactions of PRMT5


Analytical, diagnostic and therapeutic context of PRMT5


  1. Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. Rho, J., Choi, S., Seong, Y.R., Cho, W.K., Kim, S.H., Im, D.S. J. Biol. Chem. (2001) [Pubmed]
  2. Phosphorylation regulates the activity of the SMN complex during assembly of spliceosomal U snRNPs. Grimmler, M., Bauer, L., Nousiainen, M., Körner, R., Meister, G., Fischer, U. EMBO Rep. (2005) [Pubmed]
  3. Identification of gastric cancer-related genes using a cDNA microarray containing novel expressed sequence tags expressed in gastric cancer cells. Kim, J.M., Sohn, H.Y., Yoon, S.Y., Oh, J.H., Yang, J.O., Kim, J.H., Song, K.S., Rho, S.M., Yoo, H.S., Yoo, H.S., Kim, Y.S., Kim, J.G., Kim, N.S. Clin. Cancer Res. (2005) [Pubmed]
  4. Regulation of trypanosome DNA glycosylation by a SWI2/SNF2-like protein. DiPaolo, C., Kieft, R., Cross, M., Sabatini, R. Mol. Cell (2005) [Pubmed]
  5. Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs. Meister, G., Fischer, U. EMBO J. (2002) [Pubmed]
  6. Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs. Gilbreth, M., Yang, P., Bartholomeusz, G., Pimental, R.A., Kansra, S., Gadiraju, R., Marcus, S. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  7. The highly conserved skb1 gene encodes a protein that interacts with Shk1, a fission yeast Ste20/PAK homolog. Gilbreth, M., Yang, P., Wang, D., Frost, J., Polverino, A., Cobb, M.H., Marcus, S. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  8. Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes. Azzouz, T.N., Pillai, R.S., Däpp, C., Chari, A., Meister, G., Kambach, C., Fischer, U., Schümperli, D. J. Biol. Chem. (2005) [Pubmed]
  9. Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Pal, S., Vishwanath, S.N., Erdjument-Bromage, H., Tempst, P., Sif, S. Mol. Cell. Biol. (2004) [Pubmed]
  10. MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties. Le Guezennec, X., Vermeulen, M., Brinkman, A.B., Hoeijmakers, W.A., Cohen, A., Lasonder, E., Stunnenberg, H.G. Mol. Cell. Biol. (2006) [Pubmed]
  11. Histone methyltransferases in Aspergillus nidulans: evidence for a novel enzyme with a unique substrate specificity. Trojer, P., Dangl, M., Bauer, I., Graessle, S., Loidl, P., Brosch, G. Biochemistry (2004) [Pubmed]
  12. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. Branscombe, T.L., Frankel, A., Lee, J.H., Cook, J.R., Yang , Z., Pestka, S., Clarke, S. J. Biol. Chem. (2001) [Pubmed]
  13. Human PRMT5 expression is enhanced during in vitro tubule formation and after in vivo ischemic injury in renal epithelial cells. Braun, M.C., Kelly, C.N., Prada, A.E., Mishra, J., Chand, D., Devarajan, P., Zahedi, K. American journal of nephrology. (2004) [Pubmed]
  14. Formation of linear inverted repeat amplicons following targeting of an essential gene in Leishmania. Genest, P.A., ter Riet, B., Dumas, C., Papadopoulou, B., van Luenen, H.G., Borst, P. Nucleic Acids Res. (2005) [Pubmed]
  15. mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad. Pal, S., Yun, R., Datta, A., Lacomis, L., Erdjument-Bromage, H., Kumar, J., Tempst, P., Sif, S. Mol. Cell. Biol. (2003) [Pubmed]
  16. A novel WD repeat protein component of the methylosome binds Sm proteins. Friesen, W.J., Wyce, A., Paushkin, S., Abel, L., Rappsilber, J., Mann, M., Dreyfuss, G. J. Biol. Chem. (2002) [Pubmed]
  17. The histone-binding protein COPR5 is required for nuclear functions of the protein arginine methyltransferase PRMT5. Lacroix, M., El Messaoudi, S., Rodier, G., Le Cam, A., Sardet, C., Fabbrizio, E. EMBO Rep. (2008) [Pubmed]
  18. PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine. Lee, J.H., Cook, J.R., Yang, Z.H., Mirochnitchenko, O., Gunderson, S.I., Felix, A.M., Herth, N., Hoffmann, R., Pestka, S. J. Biol. Chem. (2005) [Pubmed]
  19. Identification of proteins interacting with the RNAPII FCP1 phosphatase: FCP1 forms a complex with arginine methyltransferase PRMT5 and it is a substrate for PRMT5-mediated methylation. Amente, S., Napolitano, G., Licciardo, P., Monti, M., Pucci, P., Lania, L., Majello, B. FEBS Lett. (2005) [Pubmed]
  20. The tumor suppressor DAL-1/4.1B modulates protein arginine N-methyltransferase 5 activity in a substrate-specific manner. Jiang, W., Roemer, M.E., Newsham, I.F. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
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