Protein arginine methyltransferase 5

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PRMT5
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PRMT5, HRMT1L5, IBP72, JBP1, SKB1, SKB1Hs, Protein arginine methyltransferase 5
External IDs MGI: 1351645 HomoloGene: 4454 GeneCards: PRMT5
EC number 2.1.1.125
RNA expression pattern
PBB GE PRMT5 217786 at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_013768
NM_001313906
NM_001313907

RefSeq (protein)
Location (UCSC) Chr 14: 22.92 – 22.93 Mb Chr 14: 54.51 – 54.52 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Protein arginine N-methyltransferase 5 is an enzyme that in humans is encoded by the PRMT5 gene.[3][4]

PRMT5 is a highly conserved arginine methyltransferase that translocated from the cytoplasm to the nucleus at embryonic day ~E8.5, and during preimplantation development at the ~4-cell stage.[5]

Model organisms[edit]

Model organisms have been used in the study of PRMT5 function. A conditional knockout mouse line, called Prmt5tm2a(EUCOMM)Wtsi[11][12] 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.[13][14][15]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[9][16] Twenty five tests were carried out on mutant mice and two significant abnormalities were observed.[9] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice but no further abnormalities were observed.[9]

A conditional allele of Prmt5 in the mouse limb shows that it is essential for maintaining a progenitor population, as conditional mutants have limb defects [17]

Interactions[edit]

Protein arginine methyltransferase 5 has been shown to interact with:

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Gilbreth M, Yang P, Bartholomeusz G, Pimental RA, Kansra S, Gadiraju R, Marcus S (Jan 1999). "Negative regulation of mitosis in fission yeast by the shk1 interacting protein skb1 and its human homolog, Skb1Hs". Proc Natl Acad Sci U S A. 95 (25): 14781–6. doi:10.1073/pnas.95.25.14781. PMC 24526Freely accessible. PMID 9843966. 
  4. ^ "Entrez Gene: PRMT5 protein arginine methyltransferase 5". 
  5. ^ Kim S, Gunesdogan, U, Zylicz JJ, Hackett, JA, Cougot, D, Bao, S, Lee, C, Dietmann, S, Allen, GE, Sngupta, R, Surani MA (Nov 2014). "PRMT5 Protects Genomic Integrity during Global DNA Demethylation in Primordial Germ Cells and Preimplantation Embryos". Molecular Cell. 56: 564–579. doi:10.1016/j.molcel.2014.10.003. 
  6. ^ "Haematology data for Prmt5". Wellcome Trust Sanger Institute. 
  7. ^ "Salmonella infection data for Prmt5". Wellcome Trust Sanger Institute. 
  8. ^ "Citrobacter infection data for Prmt5". Wellcome Trust Sanger Institute. 
  9. ^ a b c d 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. 
  10. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  11. ^ "International Knockout Mouse Consortium". 
  12. ^ "Mouse Genome Informatics". 
  13. ^ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, 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. 
  14. ^ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  15. ^ 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. 
  16. ^ 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. 
  17. ^ Jacqueline L. Norrie, Qiang Li, Swanie Co, Bau-Lin Huang, Ding Ding, Jann C. Uy, Zhicheng Ji, Susan Mackem, Mark T. Bedford, Antonella Galli, Hongkai Ji, Steven A. Vokes Development 2016 : doi: 10.1242/dev.140715
  18. ^ a b Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, Dreyfuss G (Mar 2002). "A novel WD repeat protein component of the methylosome binds Sm proteins". J. Biol. Chem. 277 (10): 8243–7. doi:10.1074/jbc.M109984200. PMID 11756452. 
  19. ^ Krapivinsky G, Pu W, Wickman K, Krapivinsky L, Clapham DE (May 1998). "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology". J. Biol. Chem. 273 (18): 10811–4. doi:10.1074/jbc.273.18.10811. PMID 9556550. 
  20. ^ a b Friesen WJ, Paushkin S, Wyce A, Massenet S, Pesiridis GS, Van Duyne G, Rappsilber J, Mann M, Dreyfuss G (Dec 2001). "The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins". Mol. Cell. Biol. 21 (24): 8289–300. doi:10.1128/MCB.21.24.8289-8300.2001. PMC 99994Freely accessible. PMID 11713266. 
  21. ^ Pollack BP, Kotenko SV, He W, Izotova LS, Barnoski BL, Pestka S (Oct 1999). "The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity". J. Biol. Chem. 274 (44): 31531–42. doi:10.1074/jbc.274.44.31531. PMID 10531356. 
  22. ^ Kwak YT, Guo J, Prajapati S, Park KJ, Surabhi RM, Miller B, Gehrig P, Gaynor RB (Apr 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[edit]