PRMT1

From Wikipedia, the free encyclopedia

Protein arginine methyltransferase 1

PDB rendering based on 1or8.

Available structures: 1or8, 1orh, 1ori

Identifiers

Symbol(s)

PRMT1; ANM1; HCP1; HRMT1L2; IR1B4

External IDs

OMIM: 602950 MGI: 107846 HomoloGene: 21477

Gene ontology
Molecular Function:	• protein binding • N-methyltransferase activity • protein methyltransferase activity • transferase activity
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• in utero embryonic development • protein amino acid methylation • defense response • cell surface receptor linked signal transduction

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001536 (mRNA)
NP_001527 (protein)

NM_019830 (mRNA)
NP_062804 (protein)

Location

Chr 19: 54.87 - 54.88 Mb

Chr 7: 44.84 - 44.85 Mb

Pubmed search

[1]

[2]

Protein arginine methyltransferase 1, also known as PRMT1, is a human gene.

The HRMT1L2 gene encodes a protein arginine methyltransferase that functions as a histone methyltransferase specific for H4 (see MIM 602822).[supplied by OMIM]^[1]

[edit] References

^ Entrez Gene: PRMT1 protein arginine methyltransferase 1.

[edit] Further reading

Kim S, Park GH, Paik WK (1999). "Recent advances in protein methylation: enzymatic methylation of nucleic acid binding proteins.". Amino Acids 15 (4): 291-306. PMID 9891755.
Baldwin GS, Carnegie PR (1971). "Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin.". Science 171 (971): 579-81. PMID 4924231.
Rajpurohit R, Lee SO, Park JO, et al. (1994). "Enzymatic methylation of recombinant heterogeneous nuclear RNP protein A1. Dual substrate specificity for S-adenosylmethionine:histone-arginine N-methyltransferase.". J. Biol. Chem. 269 (2): 1075-82. PMID 8288564.
Lin WJ, Gary JD, Yang MC, et al. (1996). "The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase.". J. Biol. Chem. 271 (25): 15034-44. PMID 8663146.
Nikawa J, Nakano H, Ohi N (1996). "Structural and functional conservation of human and yeast HCP1 genes which can suppress the growth defect of the Saccharomyces cerevisiae ire15 mutant.". Gene 171 (1): 107-11. PMID 8675017.
Abramovich C, Yakobson B, Chebath J, Revel M (1997). "A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor.". EMBO J. 16 (2): 260-6. doi:10.1093/emboj/16.2.260. PMID 9029147.
Scott HS, Antonarakis SE, Lalioti MD, et al. (1998). "Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2).". Genomics 48 (3): 330-40. doi:10.1006/geno.1997.5190. PMID 9545638.
Klein S, Carroll JA, Chen Y, et al. (2000). "Biochemical analysis of the arginine methylation of high molecular weight fibroblast growth factor-2.". J. Biol. Chem. 275 (5): 3150-7. PMID 10652299.
Tang J, Kao PN, Herschman HR (2000). "Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3.". J. Biol. Chem. 275 (26): 19866-76. doi:10.1074/jbc.M000023200. PMID 10749851.
Nichols RC, Wang XW, Tang J, et al. (2000). "The RGG domain in hnRNP A2 affects subcellular localization.". Exp. Cell Res. 256 (2): 522-32. doi:10.1006/excr.2000.4827. PMID 10772824.
Zhang X, Zhou L, Cheng X (2000). "Crystal structure of the conserved core of protein arginine methyltransferase PRMT3.". EMBO J. 19 (14): 3509-19. doi:10.1093/emboj/19.14.3509. PMID 10899106.
Koh SS, Chen D, Lee YH, Stallcup MR (2001). "Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities.". J. Biol. Chem. 276 (2): 1089-98. doi:10.1074/jbc.M004228200. PMID 11050077.
Scorilas A, Black MH, Talieri M, Diamandis EP (2001). "Genomic organization, physical mapping, and expression analysis of the human protein arginine methyltransferase 1 gene.". Biochem. Biophys. Res. Commun. 278 (2): 349-59. doi:10.1006/bbrc.2000.3807. PMID 11097842.
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.
Mowen KA, Tang J, Zhu W, et al. (2001). "Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription.". Cell 104 (5): 731-41. PMID 11257227.
Wang H, Huang ZQ, Xia L, et al. (2001). "Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor.". Science 293 (5531): 853-7. doi:10.1126/science.1060781. PMID 11387442.
Strahl BD, Briggs SD, Brame CJ, et al. (2001). "Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1.". Curr. Biol. 11 (12): 996-1000. PMID 11448779.
Rho J, Choi S, Seong YR, et al. (2001). "The arginine-1493 residue in QRRGRTGR1493G motif IV of the hepatitis C virus NS3 helicase domain is essential for NS3 protein methylation by the protein arginine methyltransferase 1.". J. Virol. 75 (17): 8031-44. PMID 11483748.
Lee J, Bedford MT (2002). "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays.". EMBO Rep. 3 (3): 268-73. doi:10.1093/embo-reports/kvf052. PMID 11850402.