Protein arginine N-methyltransferase 5 is an enzyme that in humans is encoded by the PRMT5 gene.^[5][6] PRMT5 symmetrically dimethylates H2AR3, H4R3, H3R2, and H3R8 in vivo, all of which are linked to a range of transcriptional regulatory events.^[7]

Quick Facts PRMT5, Available structures ...

PRMT5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4GQB, 4X60, 4X61, 4X63, 5EML, 5FA5, 5EMJ, 5EMK, 5EMM, 5C9Z
Identifiers
Aliases	PRMT5, HRMT1L5, IBP72, JBP1, SKB1, SKB1Hs, Protein arginine methyltransferase 5, HSL7
External IDs	OMIM: 604045 MGI: 1351645 HomoloGene: 4454 GeneCards: PRMT5
EC number	2.1.1.321
Gene location (Human) Chr. Chromosome 14 (human)[1] Band 14q11.2 Start 22,920,525 bp[1] End 22,929,408 bp[1]
Gene location (Mouse) Chr. Chromosome 14 (mouse)[2] Band 14|14 C2 Start 54,744,644 bp[2] End 54,754,982 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in amniotic fluid ganglionic eminence right uterine tube gastrocnemius muscle islet of Langerhans left uterine tube stromal cell of endometrium right lobe of thyroid gland left lobe of thyroid gland rectum Top expressed in yolk sac maxillary prominence somite primitive streak otic placode abdominal wall morula triceps brachii muscle sternocleidomastoid muscle lens More reference expression data BioGPS More reference expression data
Gene ontology Molecular function methyltransferase activity transferase activity histone methyltransferase activity (H4-R3 specific) transcription corepressor activity methyl-CpG binding core promoter sequence-specific DNA binding protein binding protein heterodimerization activity ribonucleoprotein complex binding histone-arginine N-methyltransferase activity protein-arginine N-methyltransferase activity protein-arginine omega-N symmetric methyltransferase activity identical protein binding protein-containing complex binding E-box binding Cellular component cytoplasm cytosol Golgi apparatus nucleoplasm methylosome nucleus histone methyltransferase complex protein-containing complex Biological process regulation of mitotic nuclear division positive regulation of oligodendrocyte differentiation regulation of transcription, DNA-templated histone H4-R3 methylation rhythmic process DNA-templated transcription, termination negative regulation of cell differentiation peptidyl-arginine N-methylation endothelial cell activation circadian regulation of gene expression transcription, DNA-templated spliceosomal snRNP assembly liver regeneration methylation peptidyl-arginine methylation regulation of ERK1 and ERK2 cascade regulation of DNA methylation cell population proliferation Golgi ribbon formation protein methylation negative regulation of nucleic acid-templated transcription positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway regulation of signal transduction by p53 class mediator peptidyl-arginine methylation, to symmetrical-dimethyl arginine chromatin organization histone arginine methylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10419 27374 Ensembl ENSG00000100462 ENSMUSG00000023110 UniProt O14744 Q8CIG8 RefSeq (mRNA) NM_001039619 NM_001282953 NM_001282954 NM_001282955 NM_001282956 NM_006109 NM_013768 NM_001313906 NM_001313907 RefSeq (protein) NP_001034708 NP_001269882 NP_001269883 NP_001269884 NP_001269885 NP_006100 NP_001300835 NP_001300836 NP_038796 Location (UCSC) Chr 14: 22.92 – 22.93 Mb Chr 14: 54.74 – 54.75 Mb PubMed search [3] [4]
Wikidata
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PRMT5 is a highly conserved arginine methyltransferase that translocated from the cytoplasm to the nucleus at embryonic day ~E8.5, and during preimplantation development at the ~4-cell stage.^[8]

Protein arginine methyltransferase 5 has been shown to interact with:

• CLNS1A,^{[9][10][11][12]}
• Janus kinase 2,^[13]
• SNRPD3,^[11]
• SUPT5H,^[14]
• MEP50,^[9]
• RIOK1, ^[15][12]
• COPR5.^[12]

PRMT5 has been shown to interact with CLNS1A, RIOK1 and COPR5 through an interface created by a shallow groove located on the TIM barrel domain of PRMT5 and the consensus sequence GQF[D/E]DA[E/D] located in the terminal regions of the adaptor proteins.^[12][16] The characterisation of the interactions occurring in the binding groove between PRMT5 and peptides derived from the adaptor proteins lead to development of protein-protein interaction (PPI) inhibitors, modulating binding between PRMT5 and the adaptor proteins.^[17][18] Furthermore, Asberry and co-workers synthesised the first-in-class small molecule inhibitor of the PPI between PRMT5 and MEP50.^[19] The PPI inhibitors complement a plethora of compounds directly suppressing the enzymatic activity of PRMT5.^[20]