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PRMT2

Available structures

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]
Band	21q22.3	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]
Band	10 C1\|10 38.74 cM	End	76,073,699 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right coronary artery

ganglionic eminence

tibial nerve

popliteal artery

thoracic aorta

ascending aorta

gallbladder

canal of the cervix

left coronary artery

hypothalamus

Top expressed in

hypothalamus

neural tube

mesencephalon

rhombencephalon

ganglionic eminence

hippocampus proper

placenta

olfactory bulb

lung

urinary bladder

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000160310 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020230 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. 277 (32). United States: 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. 358 (Pt 2). England: 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. 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.

v t e PDB gallery
1x2p: Solution structure of the SH3 domain of the Protein arginine N-methyltransferase 2

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This page was last edited on 15 October 2023, at 19:15

PRMT2

From Wikipedia, the free encyclopedia

Functions

Interactions

References

Further reading