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]

Interactions

PRMT3 has been shown to interact with RPS2.^[7]

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 (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.
^ "Entrez Gene: PRMT3 protein arginine methyltransferase 3".
^ 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.

External links

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

[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 (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.

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

[pmid18573314-7] 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.

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Interactions

References

Further reading

External links