Protein arginine methyltransferase 5

Protein arginine methyltransferase 5
Identifiers
Symbols	PRMT5 ; HRMT1L5; IBP72; JBP1; SKB1; SKB1Hs
External IDs	Template:OMIM5 Template:MGI HomoloGene: 4454
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE PRMT5 217786 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Protein arginine methyltransferase 5, also known as PRMT5, is a human gene.

Further reading

• Krapivinsky G, Pu W, Wickman K; et al. (1998). "pICln binds to a mammalian homolog of a yeast protein involved in regulation of cell morphology". J. Biol. Chem. 273 (18): 10811–4. PMID 9556550.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gilbreth M, Yang P, Bartholomeusz G; et al. (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. PMID 9843966.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pollack BP, Kotenko SV, He W; et al. (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. PMID 10531356.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Schwärzler A, Kreienkamp HJ, Richter D (2000). "Interaction of the somatostatin receptor subtype 1 with the human homolog of the Shk1 kinase-binding protein from yeast". J. Biol. Chem. 275 (13): 9557–62. PMID 10734105.CS1 maint: Multiple names: authors list (link)
• Rho J, Choi S, Seong YR; et al. (2001). "Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family". J. Biol. Chem. 276 (14): 11393–401. doi:10.1074/jbc.M008660200. PMID 11152681.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Friesen WJ, Paushkin S, Wyce A; et al. (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. PMID 11713266.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Brahms H, Meheus L, de Brabandere V; et al. (2001). "Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein". RNA. 7 (11): 1531–42. PMID 11720283.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Meister G, Eggert C, Bühler D; et al. (2002). "Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln". Curr. Biol. 11 (24): 1990–4. PMID 11747828.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Friesen WJ, Wyce A, Paushkin S; et al. (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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Fabbrizio E, El Messaoudi S, Polanowska J; et al. (2003). "Negative regulation of transcription by the type II arginine methyltransferase PRMT5". EMBO Rep. 3 (7): 641–5. doi:10.1093/embo-reports/kvf136. PMID 12101096.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Jiang LQ, Wen SJ, Wang HY, Chen LY (2003). "Screening the proteins that interact with calpain in a human heart cDNA library using a yeast two-hybrid system". Hypertens. Res. 25 (4): 647–52. PMID 12358155.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gevaert K, Goethals M, Martens L; et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kwak YT, Guo J, Prajapati S; et al. (2003). "Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties". Mol. Cell. 11 (4): 1055–66. PMID 12718890.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pal S, Yun R, Datta A; et al. (2003). "mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad". Mol. Cell. Biol. 23 (21): 7475–87. PMID 14559996.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yanagida M, Hayano T, Yamauchi Y; et al. (2004). "Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins alpha 3 and beta 1 that is independent of its association with preribosomal ribonucleoprotein complexes". J. Biol. Chem. 279 (3): 1607–14. doi:10.1074/jbc.M305604200. PMID 14583623.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Jin J, Smith FD, Stark C; et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Miranda TB, Khusial P, Cook JR; et al. (2004). "Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus". Biochem. Biophys. Res. Commun. 323 (2): 382–7. doi:10.1016/j.bbrc.2004.08.107. PMID 15369763.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pal S, Vishwanath SN, Erdjument-Bromage H; et al. (2004). "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes". Mol. Cell. Biol. 24 (21): 9630–45. doi:10.1128/MCB.24.21.9630-9645.2004. PMID 15485929.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)