PRMT3

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

PRMT3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPRMT3, HRMT1L3, protein arginine methyltransferase 3
External IDsOMIM: 603190 MGI: 1919224 HomoloGene: 24255 GeneCards: PRMT3
Gene location (Human)
Chr.Chromosome 11 (human)[1]
Band11p15.1Start20,387,558 bp[1]
End20,509,338 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

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. GRCh38: Ensembl release 89: ENSG00000185238 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000030505 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Tang J, Gary JD, Clarke S, Herschman HR (July 1998). "PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation". The Journal of Biological Chemistry. 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. 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 WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, et al. (June 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  18. Dolgin E (June 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 (January 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 (June 2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  21. Choi S, Jung CR, Kim JY, Im DS (September 2008). "PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex". Biochimica et Biophysica Acta (BBA) - General Subjects. 1780 (9): 1062–9. doi:10.1016/j.bbagen.2008.05.010. PMID 18573314.

Further reading

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