PRMT2

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; OMA:PRMT2 - orthologs
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 76,043,056 bp [2] End 76,073,699 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in C1 segment right coronary artery ganglionic eminence tibial nerve popliteal artery tibial arteries granulocyte thoracic aorta ascending aorta ventricular zone Top expressed in hypothalamus neural tube mesencephalon rhombencephalon dentate gyrus of hippocampal formation granule cell ganglionic eminence hippocampus proper placenta olfactory bulb lung More reference expression data BioGPS More reference expression data
Gene ontology Molecular function methyltransferase activity transferase activity histone methyltransferase activity protein homodimerization activity progesterone receptor binding transcription coactivator activity signal transducer activity thyroid hormone receptor binding 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 protein-containing complex binding Cellular component cytoplasm cytosol Rb-E2F complex nucleoplasm nucleolus 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: 76.04 – 76.07 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

Functions

The enzyme methylates final nitrogen atom of arginine residue in some proteins. It transfers two methyl groups from S-adenosyl-L-methionine.

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. 277 (32). United States: 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. 358 (Pt 2). England: 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. S2CID   32074112.
• 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. S2CID   4427026.
• 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.