PRMT3

PRMT3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases PRMT3, HRMT1L3, protein arginine methyltransferase 3
External IDs MGI: 1919224 HomoloGene: 24255 GeneCards: PRMT3
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

10196

71974

Ensembl

ENSG00000185238

ENSMUSG00000030505

UniProt

O60678

Q922H1

RefSeq (mRNA)

NM_001145166
NM_001145167
NM_005788

NM_133740

RefSeq (protein)

NP_005779.1

NP_598501.1

Location (UCSC) Chr 11: 20.39 – 20.51 Mb Chr 7: 49.78 – 49.86 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Protein arginine N-methyltransferase 3 is an enzyme that in humans is encoded by the PRMT3 gene.[3][4]

Model organisms

Model organisms have been used in the study of PRMT3 function. A conditional knockout mouse line, called Prmt3tm1a(EUCOMM)Wtsi[13][14] 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.[15][16][17]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[11][18] Twenty seven tests were carried out on mutant mice and seven significant abnormalities were observed.[11] 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.[11]

Interactions

PRMT3 has been shown to interact with RPS2.[19]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. ↑ 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.
  4. ↑ "Entrez Gene: PRMT3 protein arginine methyltransferase 3".
  5. ↑ "Body weight data for Prmt3". Wellcome Trust Sanger Institute.
  6. ↑ "Indirect calorimetry data for Prmt3". Wellcome Trust Sanger Institute.
  7. ↑ "DEXA data for Prmt3". Wellcome Trust Sanger Institute.
  8. ↑ "Eye morphology data for Prmt3". Wellcome Trust Sanger Institute.
  9. ↑ "Salmonella infection data for Prmt3". Wellcome Trust Sanger Institute.
  10. ↑ "Citrobacter infection data for Prmt3". Wellcome Trust Sanger Institute.
  11. 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.
  12. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  13. ↑ "International Knockout Mouse Consortium".
  14. ↑ "Mouse Genome Informatics".
  15. ↑ 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 3572410Freely accessible. PMID 21677750.
  16. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  17. ↑ 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.
  18. ↑ 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 3218837Freely accessible. PMID 21722353.
  19. ↑ 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


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