PRMT3 Gene

HGNC Family	Protein arginine methyltransferases (PRMT)
Name	protein arginine methyltransferase 3
Description	This gene belongs to the protein arginine methyltransferase (PRMT) family. The encoded enzyme catalyzes the methylation of guanidino nitrogens of arginyl residues of proteins. The enzyme acts on 40S ribosomal protein S2 (rpS2), which is its major in-vivo substrate, and is involved in the proper maturation of the 80S ribosome. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2013]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProtein arginine methyltransferase 3 (PRMT3) is a type I enzyme that catalyzes the formation of asymmetric dimethylarginine marks on target proteins. Early studies revealed that PRMT3 associates with the translational apparatus and methylates ribosomal proteins—notably the 40S subunit protein S2—and that its activity modulates later stages of ribosome biogenesis without affecting pre‐rRNA processing. Detailed enzymological analyses further showed that PRMT3 transfers sequential methyl groups to its substrates in a distributive manner, and structural studies have underlined the importance of key residues (such as Tyr87) in facilitating the interaction with ribosomal protein partners. Moreover, application of engineered cofactor analogues has significantly expanded the known substrate scope of PRMT3, revealing numerous targets that hint at a broader role in regulating cytoskeletal and translational dynamics."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical roles in ribosome-associated methylation, PRMT3 interacts with a diverse array of regulatory proteins that impact cell signaling and disease processes. PRMT3 forms complexes with tumor suppressor partners such as DAL‑1/4.1B, modulating methylation of other substrates in a manner that can affect tumor cell growth, while it also engages with proteins like expanded polyalanine-containing PABPN1, where its altered associations correlate with inclusion formation in muscular dystrophy. In addition, PRMT3 has been implicated in the regulation of ion channels (e.g. methylation of NaV1.5 enhances cardiac sodium currents), in transcriptional and metabolic control through interactions with VHL and nuclear receptors such as LXRα in fatty liver disease, and even in modulating osteogenic commitment via regulation of histone arginine marks. Other studies have shown that while PRMT3 does not appear to be mutated in neurodegenerative conditions related to FUS, it also can interact with enzymes like ALDH1A1, and its aberrant expression in colorectal cancer has been linked to C‑MYC stabilization."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTherapeutically, PRMT3 has emerged as an attractive target in oncology and other diseases owing to its multifaceted roles in modulating cellular methylation and signal transduction. The discovery of small‐molecule inhibitors acting via an allosteric mechanism has provided the first tools to directly modulate PRMT3 activity. In several cancers—including hepatocellular, endometrial, and invasive subtypes of breast carcinoma—inhibition or depletion of PRMT3 sensitizes cells to conventional treatments by affecting pathways such as ferroptosis induction and drug resistance mechanisms (for example, via methylation-dependent modulation of IGF2BP1 and downstream effectors). These studies, together with comprehensive reviews covering PRMT3’s regulation of transcriptional, translational, and metabolic processes, underscore its potential as a novel target for therapeutic intervention."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "François Bachand, Pamela A Silver "}, {"type": "b", "children": [{"type": "t", "text": "PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.emboj.7600265"}], "href": "https://doi.org/10.1038/sj.emboj.7600265"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15175657"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15175657"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Knut Kölbel, Christian Ihling, Kathrin Bellmann-Sickert, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Type I Arginine Methyltransferases PRMT1 and PRMT-3 Act Distributively."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M809547200"}], "href": "https://doi.org/10.1074/jbc.M809547200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19158082"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19158082"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Helena Handrkova, Jiri Petrak, Petr Halada, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Tyrosine 87 is vital for the activity of human protein arginine methyltransferase 3 (PRMT3)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbapap.2010.10.011"}], "href": "https://doi.org/10.1016/j.bbapap.2010.10.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21059412"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21059412"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Han Guo, Rui Wang, Weihong Zheng, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Profiling substrates of protein arginine N-methyltransferase 3 with S-adenosyl-L-methionine analogues."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "ACS Chem Biol (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/cb4008259"}], "href": "https://doi.org/10.1021/cb4008259"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24320160"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24320160"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Anne-Marie Landry-Voyer, Sarah Bilodeau, Danny Bergeron, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human PDCD2L Is an Export Substrate of CRM1 That Associates with 40S Ribosomal Subunit Precursors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.00303-16"}], "href": "https://doi.org/10.1128/MCB.00303-16"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27697862"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27697862"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Kiersten L Dionne, Danny Bergeron, Anne-Marie Landry-Voyer, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The 40S ribosomal protein uS5 (RPS2) assembles into an extraribosomal complex with human ZNF277 that competes with the PRMT3-uS5 interaction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.RA118.004928"}], "href": "https://doi.org/10.1074/jbc.RA118.004928"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30530495"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30530495"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Vinita Singh, Tina Branscombe Miranda, Wei Jiang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "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."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1208057"}], "href": "https://doi.org/10.1038/sj.onc.1208057"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15334060"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15334060"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "João Paulo Tavanez, Rocio Bengoechea, Maria T Berciano, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hsp70 chaperones and type I PRMTs are sequestered at intranuclear inclusions caused by polyalanine expansions in PABPN1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0006418"}], "href": "https://doi.org/10.1371/journal.pone.0006418"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19641605"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19641605"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Yanlai Lai, Meihua Song, Kevin Hakala, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteomic dissection of the von Hippel-Lindau (VHL) interactome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Proteome Res (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/pr200642c"}], "href": "https://doi.org/10.1021/pr200642c"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21942715"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21942715"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Thomas A Ravenscroft, Matt C Baker, Nicola J Rutherford, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neurobiol Aging (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.neurobiolaging.2013.04.004"}], "href": "https://doi.org/10.1016/j.neurobiolaging.2013.04.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23635657"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23635657"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Pedro Beltran-Alvarez, Alexsandra Espejo, Ralf Schmauder, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein arginine methyl transferases-3 and -5 increase cell surface expression of cardiac sodium channel."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS Lett (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.febslet.2013.07.043"}], "href": "https://doi.org/10.1016/j.febslet.2013.07.043"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23912080"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23912080"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Dong-il Kim, Min-jung Park, Seul-ki Lim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRMT3 regulates hepatic lipogenesis through direct interaction with LXRα."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetes (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2337/db13-1394"}], "href": "https://doi.org/10.2337/db13-1394"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25187371"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25187371"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Zhang Min, Liu Xiaomeng, Li Zheng, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Asymmetrical methyltransferase PRMT3 regulates human mesenchymal stem cell osteogenesis via miR-3648."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Death Dis (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41419-019-1815-7"}], "href": "https://doi.org/10.1038/s41419-019-1815-7"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31378783"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31378783"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Mamta Verma, Mohd Imran K Khan, Rajashekar Varma Kadumuri, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRMT3 interacts with ALDH1A1 and regulates gene-expression by inhibiting retinoic acid signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Commun Biol (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s42003-020-01644-3"}], "href": "https://doi.org/10.1038/s42003-020-01644-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33495566"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33495566"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Yongbo Hu, Yu Su, Yiming He, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Arginine methyltransferase PRMT3 promote tumorigenesis through regulating c-MYC stabilization in colorectal cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gene (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.gene.2021.145718"}], "href": "https://doi.org/10.1016/j.gene.2021.145718"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33991650"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33991650"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Fan Hao, Lin-Chen Tang, Jia-Xue Sun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Decreased nitric oxide content mediated by asymmetrical dimethylarginine and protein l-arginine methyltransferase 3 in macrophages induces trophoblast apoptosis: a potential cause of recurrent miscarriage."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Reprod (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/humrep/deab225"}], "href": "https://doi.org/10.1093/humrep/deab225"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34647126"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34647126"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Alena Siarheyeva, Guillermo Senisterra, Abdellah Allali-Hassani, et al. "}, {"type": "b", "children": [{"type": "t", "text": "An allosteric inhibitor of protein arginine methyltransferase 3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Structure (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.str.2012.06.001"}], "href": "https://doi.org/10.1016/j.str.2012.06.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22795084"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22795084"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Shih-Han Hsu, Wen-Chun Hung "}, {"type": "b", "children": [{"type": "t", "text": "Protein arginine methyltransferase 3: A crucial regulator in metabolic reprogramming and gene expression in cancers."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Lett (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.canlet.2022.216008"}], "href": "https://doi.org/10.1016/j.canlet.2022.216008"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36400311"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36400311"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Renyong Zhi, Kailiang Wu, Jingyue Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRMT3 regulates the progression of invasive micropapillary carcinoma of the breast."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Sci (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/cas.15724"}], "href": "https://doi.org/10.1111/cas.15724"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36637351"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36637351"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Yunxing Shi, Yi Niu, Yichuan Yuan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRMT3-mediated arginine methylation of IGF2BP1 promotes oxaliplatin resistance in liver cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-023-37542-5"}], "href": "https://doi.org/10.1038/s41467-023-37542-5"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37024475"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37024475"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Yiru Wang, Can Wang, Xue Guan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRMT3-Mediated Arginine Methylation of METTL14 Promotes Malignant Progression and Treatment Resistance in Endometrial Carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Adv Sci (Weinh) (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/advs.202303812"}], "href": "https://doi.org/10.1002/advs.202303812"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37973560"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37973560"}]}]}]}
Synonyms	HRMT1L3
Proteins	ANM3_HUMAN
NCBI Gene ID	10196
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PRMT3 has 6,527 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 120 datasets.

Click the + buttons to view associations for PRMT3 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PRMT3 Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PRMT3 gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of PRMT3 gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles	tissue samples with high or low expression of PRMT3 gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of PRMT3 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of PRMT3 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PRMT3 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of PRMT3 gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of PRMT3 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of PRMT3 gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of PRMT3 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PRMT3 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of PRMT3 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PRMT3 protein from the CCLE Cell Line Proteomics dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PRMT3 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PRMT3 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of PRMT3 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PRMT3 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PRMT3 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PRMT3 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with PRMT3 protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of PRMT3 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PRMT3 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Disease Associations	diseases associated with PRMT3 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by PRMT3 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with PRMT3 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PRMT3 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with PRMT3 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
	DisGeNET Gene-Disease Associations	diseases associated with PRMT3 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PRMT3 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	DrugBank Drug Targets	interacting drugs for PRMT3 protein from the curated DrugBank Drug Targets dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PRMT3 gene from the ENCODE Histone Modification Site Profiles dataset.
	ENCODE Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PRMT3 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PRMT3 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
	ESCAPE Omics Signatures of Genes and Proteins for Stem Cells	PubMedIDs of publications reporting gene signatures containing PRMT3 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD High Level Gene-Disease Associations	diseases associated with PRMT3 gene in GWAS and other genetic association datasets from the GAD High Level Gene-Disease Associations dataset.
	GDSC Cell Line Gene Expression Profiles	cell lines with high or low expression of PRMT3 gene relative to other cell lines from the GDSC Cell Line Gene Expression Profiles dataset.
	GeneRIF Biological Term Annotations	biological terms co-occuring with PRMT3 gene in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.
	GeneSigDB Published Gene Signatures	PubMedIDs of publications reporting gene signatures containing PRMT3 from the GeneSigDB Published Gene Signatures dataset.
	GEO Signatures of Differentially Expressed Genes for Diseases	disease perturbations changing expression of PRMT3 gene from the GEO Signatures of Differentially Expressed Genes for Diseases dataset.
	GEO Signatures of Differentially Expressed Genes for Gene Perturbations	gene perturbations changing expression of PRMT3 gene from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.