PRMT2

Protein arginine N-methyltransferase 2 is an enzyme that in humans is encoded by the PRMT2 gene.[5][6]

PRMT2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1X2P
Identifiers
Aliases	PRMT2, HRMT1L1, protein arginine methyltransferase 2
External IDs	OMIM: 601961 MGI: 1316652 HomoloGene: 55587 GeneCards: PRMT2
EC number	2.1.1.321
Gene location (Human) Chr. Chromosome 21 (human)[1] Band 21q22.3 Start 46,635,595 bp[1] End 46,665,124 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10 C1|10 38.74 cM Start 76,207,222 bp[2] End 76,237,865 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • methyltransferase activity • transferase activity • histone methyltransferase activity • protein homodimerization activity • progesterone receptor binding • GO:0001105 transcription coactivator activity • signal transducer activity • thyroid hormone receptor binding • GO:0001948 protein binding • androgen receptor binding • peroxisome proliferator activated receptor binding • retinoic acid receptor binding • estrogen receptor binding • protein-arginine N-methyltransferase activity • histone-arginine N-methyltransferase activity • protein-arginine omega-N asymmetric methyltransferase activity • GO:0032403 macromolecular complex binding Cellular component • cytoplasm • cytosol • Rb-E2F complex • nucleoplasm • nucleolus • cell nucleus Biological process • developmental cell growth • negative regulation of G1/S transition of mitotic cell cycle • positive regulation of transcription, DNA-templated • methylation • positive regulation of apoptotic process • regulation of androgen receptor signaling pathway • histone methylation • negative regulation of transcription, DNA-templated • negative regulation of NF-kappaB transcription factor activity • signal transduction • protein methylation • histone arginine methylation • peptidyl-arginine N-methylation • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine • regulation of transcription, DNA-templated Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	3275	15468
Ensembl	ENSG00000160310	ENSMUSG00000020230
UniProt	P55345	Q9R144
RefSeq (mRNA)	NM_001242864 NM_001242865 NM_001242866 NM_001286676 NM_001286677 NM_001286678 NM_001535 NM_206962	NM_001077638 NM_133182 NM_001302965
RefSeq (protein)	NP_001229793 NP_001229794 NP_001229795 NP_001273605 NP_001273606 NP_001273607 NP_001526 NP_996845	n/a
Location (UCSC)	Chr 21: 46.64 – 46.67 Mb	Chr 10: 76.21 – 76.24 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

PRMT2 has been shown to interact with Estrogen receptor alpha[7] and HNRPUL1.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000160310 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020230 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: PRMT2 protein arginine methyltransferase 2".
7. 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.
8. 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. Bibcode:2000Natur.405..311H. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.437.1173R. 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.