PRMT1

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Protein arginine methyltransferase 1

PDB rendering based on 1or8.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsPRMT1; ANM1; HCP1; HRMT1L2; IR1B4
External IDsOMIM: 602950 MGI: 107846 HomoloGene: 21477 ChEMBL: 5524 GeneCards: PRMT1 Gene
EC number2.1.1.125
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez327615469
EnsemblENSG00000126457ENSMUSG00000052429
UniProtQ99873Q9JIF0
RefSeq (mRNA)NM_001207042NM_001252476
RefSeq (protein)NP_001193971NP_001239405
Location (UCSC)Chr 19:
50.18 – 50.19 Mb		Chr 7:
44.98 – 44.99 Mb
PubMed search
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Protein arginine N-methyltransferase 1 is an enzyme that in humans is encoded by the PRMT1 gene.[1] The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone methyltransferase specific for H4 (see MIM 602822).[2]

Model organisms

Model organisms have been used in the study of PRMT1 function. A conditional knockout mouse line, called Prmt1tm1a(EUCOMM)Wtsi[6][7] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[8][9][10]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[4][11] Twenty three tests were carried out on mutant mice and three significant abnormalities were observed.[4] No homozygous mutant embryos were identified during gestation, and thus none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and females displayed increased circulating creatinine levels.[4]

Interactions

PRMT1 has been shown to interact with BTG2,[12][13] KHDRBS1,[14] ILF3,[15][16] HNRPK,[14][17] BTG1,[12][13] HNRNPR,[17][18] IFNAR1,[19] FUS,[16][17][18] DHX9[20] and SUPT5H.[21]

References

  1. ↑ Scott HS, Antonarakis SE, Lalioti MD, Rossier C, Silver PA, Henry MF (June 1998). "Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)". Genomics 48 (3): 330–40. doi:10.1006/geno.1997.5190. PMID 9545638. 
  2. ↑ "Entrez Gene: PRMT1 protein arginine methyltransferase 1". 
  3. ↑ "Clinical chemistry data for Prmt1". Wellcome Trust Sanger Institute. 
  4. ↑ 4.0 4.1 4.2 4.3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. 
  5. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  6. ↑ "International Knockout Mouse Consortium". 
  7. ↑ "Mouse Genome Informatics". 
  8. ↑ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750. 
  9. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  10. ↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. 
  11. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353. 
  12. ↑ 12.0 12.1 Lin, W J; Gary J D, Yang M C, Clarke S, Herschman H R (June 1996). "The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase". J. Biol. Chem. (UNITED STATES) 271 (25): 15034–44. doi:10.1074/jbc.271.25.15034. ISSN 0021-9258. PMID 8663146. 
  13. ↑ 13.0 13.1 Berthet, Cyril; Guéhenneux Fabienne, Revol Valérie, Samarut Christiane, Lukaszewicz Agnès, Dehay Colette, Dumontet Charles, Magaud Jean-Pierre, Rouault Jean-Pierre (January 2002). "Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects". Genes Cells (England) 7 (1): 29–39. doi:10.1046/j.1356-9597.2001.00497.x. ISSN 1356-9597. PMID 11856371. 
  14. ↑ 14.0 14.1 Côté, Jocelyn; Boisvert Francois-Michel, Boulanger Marie-Chloé, Bedford Mark T, Richard Stéphane (January 2003). "Sam68 RNA Binding Protein Is an In Vivo Substrate for Protein Arginine N-Methyltransferase 1". Mol. Biol. Cell (United States) 14 (1): 274–87. doi:10.1091/mbc.E02-08-0484. ISSN 1059-1524. PMC 140244. PMID 12529443. 
  15. ↑ Tang, J; Kao P N, Herschman H R (June 2000). "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3". J. Biol. Chem. (UNITED STATES) 275 (26): 19866–76. doi:10.1074/jbc.M000023200. ISSN 0021-9258. PMID 10749851. 
  16. ↑ 16.0 16.1 Lee, Jaeho; Bedford Mark T (March 2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Rep. (England) 3 (3): 268–73. doi:10.1093/embo-reports/kvf052. ISSN 1469-221X. PMC 1084016. PMID 11850402. 
  17. ↑ 17.0 17.1 17.2 Wada, Kazuhiro; Inoue Koichi, Hagiwara Masatoshi (August 2002). "Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy". Biochim. Biophys. Acta (Netherlands) 1591 (1–3): 1–10. doi:10.1016/S0167-4889(02)00202-1. ISSN 0006-3002. PMID 12183049. 
  18. ↑ 18.0 18.1 Stelzl, Ulrich; Worm Uwe, Lalowski Maciej, Haenig Christian, Brembeck Felix H, Goehler Heike, Stroedicke Martin, Zenkner Martina, Schoenherr Anke, Koeppen Susanne, Timm Jan, Mintzlaff Sascha, Abraham Claudia, Bock Nicole, Kietzmann Silvia, Goedde Astrid, Toksöz Engin, Droege Anja, Krobitsch Sylvia, Korn Bernhard, Birchmeier Walter, Lehrach Hans, Wanker Erich E (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell (United States) 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. ISSN 0092-8674. PMID 16169070. 
  19. ↑ Abramovich, C; Yakobson B, Chebath J, Revel M (January 1997). "A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor". EMBO J. (ENGLAND) 16 (2): 260–6. doi:10.1093/emboj/16.2.260. ISSN 0261-4189. PMC 1169633. PMID 9029147. 
  20. ↑ Smith, Wendell A; Schurter Brandon T, Wong-Staal Flossie, David Michael (May 2004). "Arginine methylation of RNA helicase a determines its subcellular localization". J. Biol. Chem. (United States) 279 (22): 22795–8. doi:10.1074/jbc.C300512200. ISSN 0021-9258. PMID 15084609. 
  21. ↑ Kwak, Youn Tae; Guo Jun, Prajapati Shashi, Park Kyu-Jin, Surabhi Rama M, Miller Brady, Gehrig Peter, Gaynor Richard B (April 2003). "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties". Mol. Cell (United States) 11 (4): 1055–66. doi:10.1016/S1097-2765(03)00101-1. ISSN 1097-2765. PMID 12718890. 

Further reading


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