PRMT2

Protein arginine methyltransferase 2
PDB rendering based on 1x2p.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1X2P​
Identifiers
Symbols	PRMT2 ; HRMT1L1
External IDs	OMIM: 601961 MGI: 1316652 HomoloGene: 55587 GeneCards: PRMT2 Gene
EC number	2.1.1.125
Gene ontology Molecular function • transcription coactivator activity • signal transducer activity • protein binding • histone-arginine N-methyltransferase activity • protein-arginine N-methyltransferase activity • estrogen receptor binding • progesterone receptor binding • protein-arginine omega-N asymmetric methyltransferase activity • histone methyltransferase activity • protein homodimerization activity • retinoic acid receptor binding • peroxisome proliferator activated receptor binding • thyroid hormone receptor binding • androgen receptor binding Cellular component • nucleus • nucleoplasm • nucleolus • cytoplasm • cytosol • Rb-E2F complex Biological process • protein methylation • signal transduction • histone methylation • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine • negative regulation of NF-kappaB transcription factor activity • histone arginine methylation • positive regulation of apoptotic process • negative regulation of transcription, DNA-templated • positive regulation of transcription, DNA-templated • developmental cell growth • regulation of androgen receptor signaling pathway • negative regulation of G1/S transition of mitotic cell cycle Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3275	15468
Ensembl	ENSG00000160310	ENSMUSG00000020230
UniProt	P55345	E9QP78
RefSeq (mRNA)	NM_001242864	NM_001077638
RefSeq (protein)	NP_001229793	NP_001071106
Location (UCSC)	Chr 21: 46.64 – 46.67 Mb	Chr 10: 76.21 – 76.24 Mb
PubMed search

Protein arginine N-methyltransferase 2 is an enzyme that in humans is encoded by the PRMT2 gene.^[1][2]

Interactions

PRMT2 has been shown to interact with Estrogen receptor alpha^[3] and HNRPUL1.^[4]

References

1. Scott HS, Antonarakis SE, Lalioti MD, Rossier C, Silver PA, Henry MF (Jun 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.
2. "Entrez Gene: PRMT2 protein arginine methyltransferase 2".
3. Qi, Chao; Chang Jeffrey; Zhu Yiwei; Yeldandi Anjana V; Rao Sambasiva M; Zhu Yi-Jun (Aug 2002). "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha". J. Biol. Chem. (United States) 277 (32): 28624–30. doi:10.1074/jbc.M201053200. ISSN 0021-9258. PMID 12039952.
4. Kzhyshkowska, J; Schütt H; Liss M; Kremmer E; Stauber R; Wolf H; Dobner T (Sep 2001). "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1". Biochem. J. (England) 358 (Pt 2): 305–14. doi:10.1042/0264-6021:3580305. ISSN 0264-6021. PMC 1222062. PMID 11513728.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Katsanis N, Yaspo ML, Fisher EM (1997). "Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene". Mamm. Genome 8 (7): 526–9. doi:10.1007/s003359900491. PMID 9196002.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
• Kzhyshkowska J, Schütt H, Liss M, et al. (2001). "Heterogeneous nuclear ribonucleoprotein E1B-AP5 is methylated in its Arg-Gly-Gly (RGG) box and interacts with human arginine methyltransferase HRMT1L1". Biochem. J. 358 (Pt 2): 305–14. doi:10.1042/0264-6021:3580305. PMC 1222062. PMID 11513728.
• Qi C, Chang J, Zhu Y, et al. (2002). "Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha". J. Biol. Chem. 277 (32): 28624–30. doi:10.1074/jbc.M201053200. PMID 12039952.
• 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. PMC 139241. PMID 12477932.
• Lehner B, Semple JI, Brown SE, et al. (2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region". Genomics 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• 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.
• 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. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Ganesh L, Yoshimoto T, Moorthy NC, et al. (2006). "Protein Methyltransferase 2 Inhibits NF-κB Function and Promotes Apoptosis". Mol. Cell. Biol. 26 (10): 3864–74. doi:10.1128/MCB.26.10.3864-3874.2006. PMC 1488990. PMID 16648481.