PRMT3

PRMT3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPRMT3, HRMT1L3, protein arginine methyltransferase 3
External IDsMGI: 1919224 HomoloGene: 24255 GeneCards: PRMT3
Gene location (Human)
Chr.Chromosome 11 (human)[1]
Band11p15.1Start20,387,530 bp[1]
End20,509,294 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

10196

71974

Ensembl

ENSG00000185238

ENSMUSG00000030505

UniProt

O60678

Q922H1

RefSeq (mRNA)

NM_001145166
NM_001145167
NM_005788

NM_133740

RefSeq (protein)

NP_001138638
NP_001138639
NP_005779

NP_598501

Location (UCSC)Chr 11: 20.39 – 20.51 MbChr 7: 49.78 – 49.86 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein arginine N-methyltransferase 3 is an enzyme that in humans is encoded by the PRMT3 gene.[5][6]

Model organisms

Model organisms have been used in the study of PRMT3 function. A conditional knockout mouse line, called Prmt3tm1a(EUCOMM)Wtsi[15][16] 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.[17][18][19]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[13][20] Twenty seven tests were carried out on mutant mice and seven significant abnormalities were observed.[13] Fewer than predicted homozygous mutant mice survived until weaning due to hydrocephaly. The remaining tests were carried out on both heterozygous and homozygous mutant adult mice. Male heterzygous mice had a decreased respiratory quotient. Homozygous females had decreased body weight, length and bone mineral density. Homozygous males had abnormal peripheral blood lymphocyte counts and homozygotes of both sex had eye abnormalities.[13]

Interactions

PRMT3 has been shown to interact with RPS2.[21]

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000185238 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030505 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. ↑ Tang J, Gary JD, Clarke S, Herschman HR (Aug 1998). "PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation". J Biol Chem. 273 (27): 16935–45. doi:10.1074/jbc.273.27.16935. PMID 9642256.
  6. ↑ "Entrez Gene: PRMT3 protein arginine methyltransferase 3".
  7. ↑ "Body weight data for Prmt3". Wellcome Trust Sanger Institute.
  8. ↑ "Indirect calorimetry data for Prmt3". Wellcome Trust Sanger Institute.
  9. ↑ "DEXA data for Prmt3". Wellcome Trust Sanger Institute.
  10. ↑ "Eye morphology data for Prmt3". Wellcome Trust Sanger Institute.
  11. ↑ "Salmonella infection data for Prmt3". Wellcome Trust Sanger Institute.
  12. ↑ "Citrobacter infection data for Prmt3". Wellcome Trust Sanger Institute.
  13. 1 2 3 4 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.
  14. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  15. ↑ "International Knockout Mouse Consortium".
  16. ↑ "Mouse Genome Informatics".
  17. ↑ 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.
  18. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  19. ↑ 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.
  20. ↑ 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.
  21. ↑ Choi, Seeyoung; Jung Cho-Rok; Kim Jin-Young; Im Dong-Soo (Sep 2008). "PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex". Biochim. Biophys. Acta. Netherlands. 1780 (9): 1062–9. doi:10.1016/j.bbagen.2008.05.010. ISSN 0006-3002. PMID 18573314.

Further reading

  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Singh V, Miranda TB, Jiang W, et al. (2004). "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". Oncogene. 23 (47): 7761–71. doi:10.1038/sj.onc.1208057. PMID 15334060.
  • Bachand F, Silver PA (2005). "PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits". EMBO J. 23 (13): 2641–50. doi:10.1038/sj.emboj.7600265. PMC 449775. PMID 15175657.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Smith JJ, Rücknagel KP, Schierhorn A, et al. (1999). "Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3". J. Biol. Chem. 274 (19): 13229–34. doi:10.1074/jbc.274.19.13229. PMID 10224081.


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