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	MGI: 1316652 HomoloGene: 55587 GeneCards: PRMT2
EC number	2.1.1.125
Gene location (Human)
Chr.	Chromosome 21 (human)[1]
End	46,665,124 bp[1]
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)[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; • 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; • 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
	3275
	15468
	ENSG00000160310
	ENSMUSG00000020230
	P55345
	Q9R144
NM_001242864; NM_001242865; NM_001242866; NM_001286676; NM_001286677;
	NM_001286678; NM_001535; NM_206962
	NM_001077638; NM_133182; NM_001302965
NP_001229793; NP_001229794; NP_001229795; NP_001273605; NP_001273606;
	NP_001273607; NP_001526; NP_996845
	n/a
	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]

Interactions

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

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000160310 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020230 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
↑ "Entrez Gene: PRMT2 protein arginine methyltransferase 2".
↑ 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.
↑ 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.

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. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000160310 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020230 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid9545638-5] 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.

[entrez-6] "Entrez Gene: PRMT2 protein arginine methyltransferase 2".

[pmid12039952-7] 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.

[pmid11513728-8] 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.

PRMT2

Interactions

References

Further reading