PRMT3

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; OMA:PRMT3 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	20,509,338 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	49,508,013 bp
RNA expression pattern
	Top expressed in
	ventricular zone; ; Achilles tendon; ; gonad; ; gingival epithelium; ; gastrocnemius muscle; ; left lobe of thyroid gland; ; germinal epithelium; ; right lobe of thyroid gland; ; islet of Langerhans; ; C1 segment;
	Top expressed in
	genital tubercle; ; tail of embryo; ; condyle; ; cumulus cell; ; fossa; ; substantia nigra; ; Paneth cell; ; primitive streak; ; endothelial cell of lymphatic vessel; ; epiblast;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	metal ion binding; methyltransferase activity; transferase activity; 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; 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
	10196
	71974
	ENSG00000185238
	ENSMUSG00000030505
	O60678
	Q922H1
	NM_001145166; NM_001145167; NM_005788
	NM_133740
	NP_001138638; NP_001138639; NP_005779
	NP_598501
	Wikidata
View/Edit Human	View/Edit Mouse

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

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

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000185238 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000030505 – 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.
^ Tang J, Gary JD, Clarke S, Herschman HR (Aug 1998). "PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation". J Biol Chem. 273 (27): 16935–45. doi:10.1074/jbc.273.27.16935. PMID 9642256.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ "Entrez Gene: PRMT3 protein arginine methyltransferase 3".
^ "Body weight data for Prmt3". Wellcome Trust Sanger Institute.
^ "Indirect calorimetry data for Prmt3". Wellcome Trust Sanger Institute.
^ "DEXA data for Prmt3". Wellcome Trust Sanger Institute.
^ "Eye morphology data for Prmt3". Wellcome Trust Sanger Institute.
^ "Salmonella infection data for Prmt3". Wellcome Trust Sanger Institute.
^ "Citrobacter infection data for Prmt3". Wellcome Trust Sanger Institute.
^ ^a ^b ^c ^d 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.
^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
^ "International Knockout Mouse Consortium".
^ "Mouse Genome Informatics".
^ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
^ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ Choi, Seeyoung; Jung Cho-Rok; Kim Jin-Young; Im Dong-Soo (Sep 2008). "PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex". Biochim. Biophys. Acta. 1780 (9). Netherlands: 1062–9. doi:10.1016/j.bbagen.2008.05.010. ISSN 0006-3002. PMID 18573314. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)

External links

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

Template:PBB Controls

This article on a gene on human chromosome 11 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000185238 – Ensembl, May 2017

[refGRCm38Ensembl-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.

[pmid9642256-5] Tang J, Gary JD, Clarke S, Herschman HR (Aug 1998). "PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation". J Biol Chem. 273 (27): 16935–45. doi:10.1074/jbc.273.27.16935. PMID 9642256.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[entrez-6] "Entrez Gene: PRMT3 protein arginine methyltransferase 3".

[Body_weight-7] "Body weight data for Prmt3". Wellcome Trust Sanger Institute.

[Indirect_calorimetry-8] "Indirect calorimetry data for Prmt3". Wellcome Trust Sanger Institute.

[DEXA-9] "DEXA data for Prmt3". Wellcome Trust Sanger Institute.

[Eye_morphology-10] "Eye morphology data for Prmt3". Wellcome Trust Sanger Institute.

[''Salmonella''_infection-11] "Salmonella infection data for Prmt3". Wellcome Trust Sanger Institute.

[''Citrobacter''_infection-12] "Citrobacter infection data for Prmt3". Wellcome Trust Sanger Institute.

[mgp_reference-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.

[allele_ref-15] "International Knockout Mouse Consortium".

[mgi_allele_ref-16] "Mouse Genome Informatics".

[pmid21677750-17] Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.

[mouse_library-18] Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.

[mouse_for_all_reasons-19] Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.

[pmid21722353-20] van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[pmid18573314-21] Choi, Seeyoung; Jung Cho-Rok; Kim Jin-Young; Im Dong-Soo (Sep 2008). "PRMT3 inhibits ubiquitination of ribosomal protein S2 and together forms an active enzyme complex". Biochim. Biophys. Acta. 1780 (9). Netherlands: 1062–9. doi:10.1016/j.bbagen.2008.05.010. ISSN 0006-3002. PMID 18573314. {{cite journal}}: Cite has empty unknown parameters: |laydate=, |laysource=, and |laysummary= (help)

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Model organisms

Interactions

References

Further reading

External links