PRMT3

Protein arginine N-methyltransferase 3 is an enzyme that in humans is encoded by the PRMT3 gene.[5][6]

PRMT3
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2FYT, 3SMQ, 4HSG, 4QQN, 4RYL
Identifiers
Aliases	PRMT3, HRMT1L3, protein arginine methyltransferase 3
External IDs	OMIM: 603190 MGI: 1919224 HomoloGene: 24255 GeneCards: PRMT3
Gene location (Human) Chr. Chromosome 11 (human)[1] Band 11p15.1 Start 20,387,558 bp[1] End 20,509,338 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 B4 Start 49,778,346 bp[2] End 49,858,265 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • metal ion binding • methyltransferase activity • transferase activity • GO:0001948 protein binding • protein-arginine N-methyltransferase activity • nucleic acid binding • histone-arginine N-methyltransferase activity • protein-arginine omega-N asymmetric methyltransferase activity • ribosome binding Cellular component • ribosome • cytoplasm • cytosol • cell nucleus Biological process • methylation • negative regulation of protein ubiquitination • peptidyl-arginine N-methylation • protein methylation • regulation of transcription, DNA-templated • peptidyl-arginine methylation, to asymmetrical-dimethyl arginine • histone arginine methylation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	10196	71974
Ensembl	ENSG00000185238	ENSMUSG00000030505
UniProt	O60678	Q922H1
RefSeq (mRNA)	NM_001145166 NM_001145167 NM_005788	NM_133740
RefSeq (protein)	NP_001138638 NP_001138639 NP_005779	NP_598501
Location (UCSC)	Chr 11: 20.39 – 20.51 Mb	Chr 7: 49.78 – 49.86 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Model organisms

Prmt3 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Normal
Fertility	Normal
General Observations	Abnormal
Body weight	Abnormal[7]
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Abnormal[8]
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Abnormal[9]
Radiography	Normal
Body temperature	Normal
Eye morphology	Abnormal[10]
Clinical chemistry	Normal
Haematology	Normal
Peripheral blood lymphocytes	Abnormal
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal[11]
Citrobacter infection	Normal[12]
All tests and analysis from[13][14]

Model organisms have been used in the study of PRMT3 function. A conditional knockout mouse line, called Prmt3^{tm1a(EUCOMM)Wtsi}[15][16] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[17][18][19]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[13][20] Twenty seven tests were carried out on mutant mice and seven significant abnormalities were observed.[13] Fewer than predicted homozygous mutant mice survived until weaning due to hydrocephaly. The remaining tests were carried out on both heterozygous and homozygous mutant adult mice. Male heterzygous mice had a decreased respiratory quotient. Homozygous females had decreased body weight, length and bone mineral density. Homozygous males had abnormal peripheral blood lymphocyte counts and homozygotes of both sex had eye abnormalities.[13]

Interactions

PRMT3 has been shown to interact with RPS2.[21]

References

1. GRCh38: Ensembl release 89: ENSG00000185238 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000030505 - 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. Tang J, Gary JD, Clarke S, Herschman HR (July 1998). "PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation". The Journal of Biological Chemistry. 273 (27): 16935–45. doi:10.1074/jbc.273.27.16935. PMID 9642256.
6. "Entrez Gene: PRMT3 protein arginine methyltransferase 3".
7. "Body weight data for Prmt3". Wellcome Trust Sanger Institute.
8. "Indirect calorimetry data for Prmt3". Wellcome Trust Sanger Institute.
9. "DEXA data for Prmt3". Wellcome Trust Sanger Institute.
10. "Eye morphology data for Prmt3". Wellcome Trust Sanger Institute.
11. "Salmonella infection data for Prmt3". Wellcome Trust Sanger Institute.
12. "Citrobacter infection data for Prmt3". Wellcome Trust Sanger Institute.
13. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
14. Mouse Resources Portal, Wellcome Trust Sanger Institute.
15. "International Knockout Mouse Consortium".
16. "Mouse Genome Informatics".
17. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, et al. (June 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
18. Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
19. Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
20. van der Weyden L, White JK, Adams DJ, Logan DW (June 2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biology. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
21. Choi S, Jung CR, Kim JY, Im DS (September 2008). "PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex". Biochimica et Biophysica Acta (BBA) - General Subjects. 1780 (9): 1062–9. doi:10.1016/j.bbagen.2008.05.010. PMID 18573314.

Further reading

• Singh V, Miranda TB, Jiang W, Frankel A, Roemer ME, Robb VA, et al. (October 2004). "DAL-1/4.1B tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo". Oncogene. 23 (47): 7761–71. doi:10.1038/sj.onc.1208057. PMID 15334060.
• Bachand F, Silver PA (July 2004). "PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits". The EMBO Journal. 23 (13): 2641–50. doi:10.1038/sj.emboj.7600265. PMC 449775. PMID 15175657.
• Smith JJ, Rücknagel KP, Schierhorn A, Tang J, Nemeth A, Linder M, et al. (May 1999). "Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3". The Journal of Biological Chemistry. 274 (19): 13229–34. doi:10.1074/jbc.274.19.13229. PMID 10224081.

External links

• PRMT3 human gene location in the UCSC Genome Browser.
• PRMT3 human gene details in the UCSC Genome Browser.