Protein arginine methyltransferase 5

From Wikipedia, the free encyclopedia

Identifiers

PRMT5; HRMT1L5; IBP72; JBP1; SKB1; SKB1Hs

External IDs

OMIM: 604045 MGI: 1351645 HomoloGene: 4454

Gene ontology
Molecular Function:	• methyltransferase activity • histone-arginine N-methyltransferase activity • transferase activity
Cellular Component:	• cytoplasm
Biological Process:	• transcription • regulation of transcription, DNA-dependent • regulation of mitosis • cell proliferation • chromatin modification • peptidyl-arginine N-methylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001039619 (mRNA)
NP_001034708 (protein)

NM_013768 (mRNA)
NP_038796 (protein)

Location

Chr 14: 22.46 - 22.47 Mb

Chr 14: 53.46 - 53.47 Mb

Pubmed search

[1]

[2]

Protein arginine methyltransferase 5, also known as PRMT5, is a human gene.^[1]

[edit] References

^ Entrez Gene: PRMT5 protein arginine methyltransferase 5.

[edit] 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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.