PRMT7 Gene

HGNC Family	Protein arginine methyltransferases (PRMT)
Name	protein arginine methyltransferase 7
Description	This gene encodes a member of the protein arginine N-methyltransferase family of proteins. The encoded enzyme transfers single methyl groups to arginine residues to generate monomethylarginines on histone proteins as well as other protein substrates. This enzyme plays a role in a wide range of biological processes, including neuronal differentiation, male germ line imprinting, small nuclear ribonucleoprotein biogenesis, and regulation of the Wnt signaling pathway. Mutations in this gene underlie multiple related syndromes in human patients characterized by intellectual disability, short stature and other features. The encoded protein may promote breast cancer cell invasion and metastasis in human patients. [provided by RefSeq, May 2017]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nProtein arginine methyltransferase 7 (PRMT7) is a distinctive member of the PRMT family that exhibits unique catalytic properties and substrate specificity. Biochemical studies using recombinant full‐length PRMT7 have shown that the enzyme predominantly catalyzes the formation of ω‑NG‐monomethylated arginine residues on substrates enriched for RXR and glycine/arginine motifs. Critical analyses have demonstrated that its activity relies on dual S‑adenosylmethionine–binding domains and essential acidic residues that modulate substrate recognition and turnover. Although many in vitro characterizations describe PRMT7 as a type III enzyme producing only monomethylarginine, subtle differences in experimental conditions and substrate context have also implicated PRMT7 in the formation of symmetric dimethylarginine marks on specific histone tails, indicating a context‐dependent catalytic versatility."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cellular contexts, PRMT7 plays multifaceted roles in epigenetic regulation and the control of diverse cellular processes. It methylates key arginine residues on histone H3, H2A, and H4, thereby affecting chromatin architecture and the recruitment of regulatory proteins such as WDR5, while also modulating the activity of PRMT5. This enzyme is essential for proper RNA splicing by influencing hnRNPA1 binding dynamics and is involved in the regulation of genes that govern DNA repair and cell cycle progression. In addition, PRMT7 contributes to the induction of epithelial-to-mesenchymal transition and the upregulation of oncogenes by altering the methylation landscape—an effect further exacerbated by enhancer variants that boost its expression in cancers including breast, renal, and hepatocellular carcinoma."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinically, dysregulation or genetic alterations in PRMT7 have been associated with a broad spectrum of human disorders and pathophysiological processes. Mutations in PRMT7 have been linked to syndromic phenotypes characterized by short stature, brachydactyly, intellectual developmental disability, and seizures—now recognized as part of the SBIDDS spectrum. In addition, aberrant PRMT7 activity contributes to altered stress responses by modulating key substrates such as HSP70 and components of antiviral signaling pathways, and it plays critical roles in embryonic development, where its overexpression can arrest early embryogenesis—a defect that can be partially rescued by its knockdown. These insights into PRMT7 function not only underscore its importance in gene regulation and cellular homeostasis but also suggest that targeted modulation of its activity may offer promising therapeutic avenues in cancer, developmental disorders, and other diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Tina Branscombe Miranda, Mark Miranda, Adam Frankel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M312904200"}], "href": "https://doi.org/10.1074/jbc.M312904200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15044439"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15044439"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Jin-Hyung Lee, Jeffry R Cook, Zhi-Hong Yang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRMT7, a new protein arginine methyltransferase that synthesizes symmetric dimethylarginine."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M405295200"}], "href": "https://doi.org/10.1074/jbc.M405295200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15494416"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15494416"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Cecilia I Zurita-Lopez, Troy Sandberg, Ryan Kelly, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human protein arginine methyltransferase 7 (PRMT7) is a type III enzyme forming ω-NG-monomethylated arginine residues."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.336271"}], "href": "https://doi.org/10.1074/jbc.M111.336271"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22241471"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22241471"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "R Mitchell Baldwin, Nasim Haghandish, Manijeh Daneshmand, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.3072"}], "href": "https://doi.org/10.18632/oncotarget.3072"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25605249"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25605249"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Timothy J Bondoc, Troy L Lowe, Steven G Clarke "}, {"type": "b", "children": [{"type": "t", "text": "The exquisite specificity of human protein arginine methyltransferase 7 (PRMT7) toward Arg-X-Arg sites."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0285812"}], "href": "https://doi.org/10.1371/journal.pone.0285812"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37216364"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37216364"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Graydon B Gonsalvez, Liping Tian, Jason K Ospina, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Two distinct arginine methyltransferases are required for biogenesis of Sm-class ribonucleoproteins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.200702147"}], "href": "https://doi.org/10.1083/jcb.200702147"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17709427"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17709427"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Valentina Migliori, Julius Müller, Sameer Phalke, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase δ catalytic subunit gene, POLD1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.378281"}], "href": "https://doi.org/10.1074/jbc.M112.378281"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22761421"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22761421"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Ruosi Yao, Hao Jiang, Yuhui Ma, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRMT7 induces epithelial-to-mesenchymal transition and promotes metastasis in breast cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-14-0800"}], "href": "https://doi.org/10.1158/0008-5472.CAN-14-0800"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25136067"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25136067"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "K D Kernohan, A McBride, Y Xi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss of the arginine methyltranserase PRMT7 causes syndromic intellectual disability with microcephaly and brachydactyly."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Genet (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/cge.12884"}], "href": "https://doi.org/10.1111/cge.12884"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27718516"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27718516"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Mamta Verma, Ramya Chandar M Charles, Baskar Chakrapani, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "PRMT7 promotes the growth of renal cell carcinoma through modulating the β-catenin/C-MYC axis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Biochem Cell Biol (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.biocel.2020.105686"}], "href": "https://doi.org/10.1016/j.biocel.2020.105686"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31926310"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31926310"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Wen-Juan Li, Yao-Hui He, Jing-Jing Yang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Profiling PRMT methylome reveals roles of hnRNPA1 arginine methylation in RNA splicing and cell growth."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-021-21963-1"}], "href": "https://doi.org/10.1038/s41467-021-21963-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33782401"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33782401"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Junji Zhu, Xiong Li, Xiaolian Cai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Arginine monomethylation by PRMT7 controls MAVS-mediated antiviral innate immunity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2021.06.004"}], "href": "https://doi.org/10.1016/j.molcel.2021.06.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34171297"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34171297"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Ting Shen, Ting Ni, Jiaxuan Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "An enhancer variant at 16q22.1 predisposes to hepatocellular carcinoma via regulating PRMT7 expression."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-022-28861-0"}], "href": "https://doi.org/10.1038/s41467-022-28861-0"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35264579"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35264579"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "E Agolini, M L Dentici, E Bellacchio, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expanding the clinical and molecular spectrum of PRMT7 mutations: 3 additional patients and review."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Genet (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/cge.13137"}], "href": "https://doi.org/10.1111/cge.13137"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28902392"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28902392"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Roee Birnbaum, Naama Yosha-Orpaz, Miri Yanoov-Sharav, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Short stature in PRMT7 Mutations: first evidence of response to growth hormone treatment."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Hum Genet (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41431-022-01220-9"}], "href": "https://doi.org/10.1038/s41431-022-01220-9"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36348013"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36348013"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Elisa Cali, Mohnish Suri, Marcello Scala, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Biallelic PRMT7 pathogenic variants are associated with a recognizable syndromic neurodevelopmental disorder with short stature, obesity, and craniofacial and digital abnormalities."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genet Med (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.gim.2022.09.016"}], "href": "https://doi.org/10.1016/j.gim.2022.09.016"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36399134"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36399134"}]}]}]}
Synonyms	SBIDDS
Proteins	ANM7_HUMAN
NCBI Gene ID	54496
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PRMT7 has 6,551 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, disease, phenotype or trait, functional term, phrase or reference, 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 PRMT7 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PRMT7 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 PRMT7 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 PRMT7 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 PRMT7 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 PRMT7 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 PRMT7 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 PRMT7 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 PRMT7 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 PRMT7 gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of PRMT7 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PRMT7 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 PRMT7 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PRMT7 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PRMT7 gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PRMT7 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PRMT7 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 PRMT7 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with PRMT7 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI KOLF21J CRISPRi Gene Perturbation Atlas	gene perturbations changing expression of PRMT7 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PRMT7 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PRMT7 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PRMT7 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing PRMT7 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing PRMT7 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PRMT7 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 PRMT7 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 PRMT7 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PRMT7 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PRMT7 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PRMT7 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with PRMT7 gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of PRMT7 protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by PRMT7 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DGIdb Drug Targets 2026	interacting drugs for PRMT7 protein from the DGIdb Drug Targets 2026 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PRMT7 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 PRMT7 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 PRMT7 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PRMT7 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PRMT7 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 PRMT7 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PRMT7 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.