PRMT1

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 IUPHAR: 1252 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

Protein arginine N-methyltransferase 1 is an enzyme that in humans is encoded by the PRMT1 gene.[1]

Function

The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone methyltransferase specific for histone H4.[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:

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 WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V et al. (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 WJ, Gary JD, Yang MC, Clarke S, Herschman HR (June 1996). "The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase". J. Biol. Chem. 271 (25): 15034–44. doi:10.1074/jbc.271.25.15034. PMID 8663146.
  13. ↑ 13.0 13.1 Berthet C, Guéhenneux F, Revol V, Samarut C, Lukaszewicz A, Dehay C et al. (January 2002). "Interaction of PRMT1 with BTG/TOB proteins in cell signalling: molecular analysis and functional aspects". Genes Cells 7 (1): 29–39. doi:10.1046/j.1356-9597.2001.00497.x. PMID 11856371. Vancouver style error (help)
  14. ↑ Smith WA, Schurter BT, Wong-Staal F, David M (May 2004). "Arginine methylation of RNA helicase a determines its subcellular localization". J. Biol. Chem. 279 (22): 22795–8. doi:10.1074/jbc.C300512200. PMID 15084609.
  15. ↑ 15.0 15.1 Lee J, Bedford MT (March 2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays". EMBO Rep. 3 (3): 268–73. doi:10.1093/embo-reports/kvf052. PMC 1084016. PMID 11850402.
  16. ↑ 16.0 16.1 16.2 Wada K, Inoue K, Hagiwara M (August 2002). "Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy". Biochim. Biophys. Acta 1591 (1-3): 1–10. doi:10.1016/s0167-4889(02)00202-1. PMID 12183049.
  17. ↑ 17.0 17.1 Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H et al. (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
  18. ↑ 18.0 18.1 Côté J, Boisvert FM, Boulanger MC, Bedford MT, Richard S (January 2003). "Sam68 RNA binding protein is an in vivo substrate for protein arginine N-methyltransferase 1". Mol. Biol. Cell 14 (1): 274–87. doi:10.1091/mbc.E02-08-0484. PMC 140244. PMID 12529443. Vancouver style error (help)
  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. 16 (2): 260–6. doi:10.1093/emboj/16.2.260. PMC 1169633. PMID 9029147.
  20. ↑ Tang J, Kao PN, Herschman HR (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. 275 (26): 19866–76. doi:10.1074/jbc.M000023200. PMID 10749851.
  21. ↑ Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B et al. (April 2003). "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties". Mol. Cell 11 (4): 1055–66. doi:10.1016/s1097-2765(03)00101-1. PMID 12718890.

Further reading