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PRMT3

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}Protein arginine N-methyltransferase 3 is an enzyme that in humans is encoded by the PRMT3 gene.{{cite journal | vauthors = Tang J, Gary JD, Clarke S, Herschman HR | title = PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation | journal = The Journal of Biological Chemistry | volume = 273 | issue = 27 | pages = 16935–45 | date = July 1998 | pmid = 9642256 | doi = 10.1074/jbc.273.27.16935 | doi-access = free }}{{cite web | title = Entrez Gene: PRMT3 protein arginine methyltransferase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10196}}

Interactions

PRMT3 has been shown to interact with RPS2.{{cite journal | vauthors = Choi S, Jung CR, Kim JY, Im DS | title = PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex | journal = Biochimica et Biophysica Acta (BBA) - General Subjects | volume = 1780 | issue = 9 | pages = 1062–9 | date = September 2008 | pmid = 18573314 | doi = 10.1016/j.bbagen.2008.05.010 }}

References

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Further reading

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  • {{cite journal | vauthors = Singh V, Miranda TB, Jiang W, Frankel A, Roemer ME, Robb VA, Gutmann DH, Herschman HR, Clarke S, Newsham IF | display-authors = 6 | title = 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 | journal = Oncogene | volume = 23 | issue = 47 | pages = 7761–71 | date = October 2004 | pmid = 15334060 | doi = 10.1038/sj.onc.1208057 | doi-access = free }}
  • {{cite journal | vauthors = Bachand F, Silver PA | title = PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits | journal = The EMBO Journal | volume = 23 | issue = 13 | pages = 2641–50 | date = July 2004 | pmid = 15175657 | pmc = 449775 | doi = 10.1038/sj.emboj.7600265 }}
  • {{cite journal | vauthors = Smith JJ, Rücknagel KP, Schierhorn A, Tang J, Nemeth A, Linder M, Herschman HR, Wahle E | display-authors = 6 | title = Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3 | journal = The Journal of Biological Chemistry | volume = 274 | issue = 19 | pages = 13229–34 | date = May 1999 | pmid = 10224081 | doi = 10.1074/jbc.274.19.13229 | doi-access = free }}

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External links

  • {{UCSC genome browser|PRMT3}}
  • {{UCSC gene details|PRMT3}}

{{PDB Gallery|geneid=10196}}

Category:Genes mutated in mice

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