PRMT3

From Wikipedia, the free encyclopedia

Protein arginine methyltransferase 3

PDB rendering based on 1f3l.

Available structures: 1f3l, 1wir, 2fyt

Identifiers

Symbol(s)

PRMT3; HRMT1L3

External IDs

OMIM: 603190 MGI: 1919224 HomoloGene: 24255

Gene ontology
Molecular Function:	• nucleic acid binding • methyltransferase activity • zinc ion binding • protein-arginine N-methyltransferase activity • transferase activity • metal ion binding
Cellular Component:	• intracellular • cytoplasm
Biological Process:	• biological_process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005788 (mRNA)
NP_005779 (protein)

NM_133740 (mRNA)
NP_598501 (protein)

Location

Chr 11: 20.37 - 20.49 Mb

Chr 7: 49.65 - 49.73 Mb

Pubmed search

[1]

[2]

Protein arginine methyltransferase 3, also known as PRMT3, is a human gene.^[1]

[edit] References

^ Entrez Gene: PRMT3 protein arginine methyltransferase 3.

[edit] 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. 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. 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. doi:10.1073/pnas.242603899. 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. PMID 10224081.
Tang J, Gary JD, Clarke S, Herschman HR (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. PMID 9642256.