| HGNC Family | Non-coding RNAs |
| Name | microRNA 548y |
| Description | microRNAs (miRNAs) are short (20-24 nt) non-coding RNAs that are involved in post-transcriptional regulation of gene expression in multicellular organisms by affecting both the stability and translation of mRNAs. miRNAs are transcribed by RNA polymerase II as part of capped and polyadenylated primary transcripts (pri-miRNAs) that can be either protein-coding or non-coding. The primary transcript is cleaved by the Drosha ribonuclease III enzyme to produce an approximately 70-nt stem-loop precursor miRNA (pre-miRNA), which is further cleaved by the cytoplasmic Dicer ribonuclease to generate the mature miRNA and antisense miRNA star (miRNA*) products. The mature miRNA is incorporated into a RNA-induced silencing complex (RISC), which recognizes target mRNAs through imperfect base pairing with the miRNA and most commonly results in translational inhibition or destabilization of the target mRNA. The RefSeq represents the predicted microRNA stem-loop. [provided by RefSeq, Sep 2009] |
| Summary |
{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe collection of studies provided reveals a wealth of information on the multifaceted functions of Vanin‑1, a membrane‐bound pantetheinase, in a broad range of pathological contexts. In liver disease models, hepatocyte‐derived microparticles—whose proangiogenic capacity in steatohepatitis is critically dependent on Vanin‑1—serve as intercellular signals contributing to pathological angiogenesis and liver injury."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOther investigations have demonstrated that Vanin‑1 plays a central role as an oxidative stress sensor and regulator of inflammation. Loss of Vanin‑1 leads to enhanced glutathione synthesis, conferring resistance to oxidative injury and dampening inflammatory responses in models of radiation, chemical toxicity, and colitis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "2", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn developmental biology, Vanin‑1 expression is tightly regulated in a sex‐specific manner in the fetal gonad where it is activated by key transcription factors such as SF‑1 and SOX9. This regulation is essential for establishing the proper microenvironment required for male germ cell development."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn liver metabolism, Vanin‑1 is upregulated in fasting and insulin resistant states. Its transcriptional activation by factors including PGC‑1α and HNF‑4α leads to increased gluconeogenic gene expression and hepatic glucose output, suggesting its potential as a therapeutic target in metabolic diseases."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nVanin‑1 also influences immune cell recruitment and activation; for instance, its presence modulates macrophage polarization and is required for proper granuloma formation during infections such as Q fever, thereby impacting bacterial clearance and tissue homeostasis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the tumorigenic context, Vanin‑1 has emerged as a modulator of neoplastic transformation. In adrenocortical cancer models driven by SF‑1 overexpression, genetic ablation of Vanin‑1 significantly alleviates neoplastic lesion severity, an effect that can be reversed by exogenous cysteamine."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMoreover, Vanin‑1 participates in cholesterol metabolism and inflammatory regulation within macrophage‐derived foam cells, thereby promoting atherosclerotic lesion development. Increased Vanin‑1 expression is associated with augmented cellular cholesterol accumulation and altered inflammatory mediator production."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn autoimmune fibrotic disorders such as systemic sclerosis, dysregulation of the Vanin‑1/pantetheinase pathway contributes to fibrosis, vasculopathy, and autoimmunity. Elevated Vanin‑1 activity and its metabolite pantothenic acid correlate with disease severity, and inhibition of Vanin‑1 confers protection in experimental models."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOn the analytical side, a highly sensitive bioluminogenic probe has been developed for in vivo detection of pantetheinase activity, facilitating real‑time monitoring of endogenous Vanin‑1 levels and advancing research into its diverse biological roles."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn pancreatic cancer, Vanin‑1 overexpression in malignant cells is implicated in paraneoplastic islet dysfunction. Cancer‑derived exosomes carrying Vanin‑1 disrupt normal islet function by inhibiting key metabolic regulators such as AMPK and Sirt1, leading to β‑cell dedifferentiation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFurther, in models of intrauterine growth retardation associated with asthma, upregulation of Vanin‑1 in bronchial epithelium activates the PI3K/Akt/NF‑κB signaling pathway, increasing oxidative stress and the production of inflammatory mediators that predispose to airway hyperresponsiveness."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the setting of cancer chemoresistance, visualizing Vanin‑1 with a fluorescent probe has provided evidence that its inhibition can modulate glutathione synthesis; when combined with cisplatin, Vanin‑1 inhibition alters tumor cell response, underscoring its role in drug resistance mechanisms."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditionally, recent work highlights a potential role for Vanin‑1 in brown adipose tissue mitochondrial function and energy expenditure during obesity, suggesting that it may contribute to systemic metabolic regulation under conditions of overnutrition."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond these functions, studies in erythrocyte biology have linked reduced serum pantetheinase activity to shortened red blood cell lifespan and increased susceptibility to hemolytic stress, a finding that also correlates with complications during malaria infection."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, aberrant Vanin‑1 expression has been implicated in processes of ectopic bone formation and calcification observed in skeletal disorders, further illustrating its influence on chondrogenesis and osteoblastic function."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIt is noteworthy that one study among the provided abstracts focused on a microRNA—miR‑203—in the modulation of lung injury in septic shock."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": " However, none of these reports address the function of MIR548Y. Instead, the collective evidence centers on Vanin‑1, underscoring its diverse roles in oxidative stress regulation, inflammation, metabolism, tissue remodeling, and disease pathogenesis.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Davide Povero, Akiko Eguchi, Ingrid R Niesman, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Lipid-induced toxicity stimulates hepatocytes to release angiogenic microparticles that require Vanin-1 for uptake by endothelial cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Signal (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/scisignal.2004512"}], "href": "https://doi.org/10.1126/scisignal.2004512"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24106341"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24106341"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Florent Martin, Marie-France Penet, Fabrice Malergue, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Vanin-1(-/-) mice show decreased NSAID- and Schistosoma-induced intestinal inflammation associated with higher glutathione stores."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI19557"}], "href": "https://doi.org/10.1172/JCI19557"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14966568"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14966568"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "C Berruyer, F M Martin, R Castellano, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Vanin-1-/- mice exhibit a glutathione-mediated tissue resistance to oxidative stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.24.16.7214-7224.2004"}], "href": "https://doi.org/10.1128/MCB.24.16.7214-7224.2004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15282320"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15282320"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Carole Berruyer, Laurent Pouyet, Virginie Millet, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Vanin-1 licenses inflammatory mediator production by gut epithelial cells and controls colitis by antagonizing peroxisome proliferator-activated receptor gamma activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Exp Med (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1084/jem.20061640"}], "href": "https://doi.org/10.1084/jem.20061640"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17145956"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17145956"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Luana Di Leandro, Bruno Maras, M Eugenia Schininà, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cystamine restores GSTA3 levels in Vanin-1 null mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Free Radic Biol Med (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.freeradbiomed.2007.12.015"}], "href": "https://doi.org/10.1016/j.freeradbiomed.2007.12.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18206125"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18206125"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Megan J Wilson, Pancharatnam Jeyasuria, Keith L Parker, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The transcription factors steroidogenic factor-1 and SOX9 regulate expression of Vanin-1 during mouse testis development."}]}, {"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.M412806200"}], "href": "https://doi.org/10.1074/jbc.M412806200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15590666"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15590666"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Siyu Chen, Wenxiang Zhang, Chunqi Tang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Vanin-1 is a key activator for hepatic gluconeogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetes (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2337/db13-0788"}], "href": "https://doi.org/10.2337/db13-0788"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24550194"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24550194"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Daniel W Ferreira, Michael J Goedken, Samuel Rommelaere, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Enhanced hepatotoxicity by acetaminophen in Vanin-1 knockout mice is associated with deficient proliferative and immune responses."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbadis.2016.02.001"}], "href": "https://doi.org/10.1016/j.bbadis.2016.02.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26850476"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26850476"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Janna A van Diepen, Patrick A Jansen, Dov B Ballak, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Genetic and pharmacological inhibition of vanin-1 activity in animal models of type 2 diabetes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep21906"}], "href": "https://doi.org/10.1038/srep21906"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26932716"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26932716"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Soraya Meghari, Carole Berruyer, Hubert Lepidi, et al. 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| NCBI Gene ID | 100500919 |
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| Download Associations | |
| Predicted Functions |
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| Co-expressed Genes |
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| Expression in Tissues and Cell Lines |
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MIR548Y has 182 functional associations with biological entities spanning 3 categories (molecular profile, cell line, cell type or tissue, gene, protein or microRNA) extracted from 10 datasets.
Click the + buttons to view associations for MIR548Y from the datasets below.
If available, associations are ranked by standardized value
| Dataset | Summary | |
|---|---|---|
| CCLE Cell Line Gene CNV Profiles | cell lines with high or low copy number of MIR548Y gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset. | |
| COSMIC Cell Line Gene CNV Profiles | cell lines with high or low copy number of MIR548Y gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset. | |
| ENCODE Histone Modification Site Profiles | histone modification site profiles with high histone modification abundance at MIR548Y 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 MIR548Y gene from the ENCODE Transcription Factor Binding Site Profiles dataset. | |
| ENCODE Transcription Factor Targets | transcription factors binding the promoter of MIR548Y gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset. | |
| JASPAR Predicted Transcription Factor Targets | transcription factors regulating expression of MIR548Y gene predicted using known transcription factor binding site motifs from the JASPAR Predicted Transcription Factor Targets dataset. | |
| Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles | cell lines with high or low copy number of MIR548Y gene relative to other cell lines from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles dataset. | |
| KnockTF Gene Expression Profiles with Transcription Factor Perturbations | transcription factor perturbations changing expression of MIR548Y gene from the KnockTF Gene Expression Profiles with Transcription Factor Perturbations dataset. | |
| MotifMap Predicted Transcription Factor Targets | transcription factors regulating expression of MIR548Y gene predicted using known transcription factor binding site motifs from the MotifMap Predicted Transcription Factor Targets dataset. | |
| Roadmap Epigenomics Histone Modification Site Profiles | histone modification site profiles with high histone modification abundance at MIR548Y gene from the Roadmap Epigenomics Histone Modification Site Profiles dataset. | |