MIR4273 Gene

HGNC Family Non-coding RNAs
Name microRNA 4273
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": "\nSeveral studies have delineated intricate signaling pathways that regulate actin cytoskeletal dynamics in diverse cellular contexts. For instance, one investigation described how sphingosine 1‐phosphate activates RhoA, leading to phospholipase Cε and PKD1‐mediated phosphorylation events that prevent the mitochondrial translocation of proapoptotic factors, thereby promoting cardiomyocyte survival. In parallel, another study demonstrated that during Legionella infection, caspase‐11 and caspase‐1 orchestrate opposing cofilin phosphorylation states to control phagolysosomal fusion. Notably, however, none of these reports provided evidence regarding any role or mechanistic function for MIR4273."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional research has focused on the regulation of actin dynamics by phosphatases, such as Slingshot-1 (SSH1) and its modulation of cofilin activity. One study detailed PDGF-induced activation of SSH1 by Nox1-mediated reactive oxygen species, while another illustrated how EphA receptor signaling leads to transient dendritic spine elongation via SSH1 and calcineurin-dependent dephosphorylation of cofilin. A separate investigation further showed that SSH1 not only dephosphorylates cofilin but also exerts F-actin-stabilizing and -bundling activities. Despite these insights into the molecular control of actin reorganization, none of these studies addressed any functional implications of MIR4273."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFurthermore, investigations into vascular remodeling and hepatocellular carcinoma have revealed that SSH1 significantly modulates responses to angiotensin II and influences circadian rhythm and oncogenic pathways, respectively. These studies underscore the critical roles of actin-regulatory proteins in pathophysiological processes such as fibrosis and tumor invasiveness. Nonetheless, across these diverse contexts, no study has examined or reported any direct involvement or functional consequence of MIR4273 in these signaling cascades."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sunny Y Xiang, Kunfu Ouyang, Bryan S Yung, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PLCε, PKD1, and SSH1L transduce RhoA signaling to protect mitochondria from oxidative stress in the heart."}]}, {"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.2004405"}], "href": "https://doi.org/10.1126/scisignal.2004405"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24345679"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24345679"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Kyle Caution, Mikhail A Gavrilin, Mia Tazi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Caspase-11 and caspase-1 differentially modulate actin polymerization via RhoA and Slingshot proteins to promote bacterial clearance."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep18479"}], "href": "https://doi.org/10.1038/srep18479"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26686473"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26686473"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Mithunan Maheswaranathan, Hope K A Gole, Isabel Fernandez, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Platelet-derived growth factor (PDGF) regulates Slingshot phosphatase activity via Nox1-dependent auto-dephosphorylation of serine 834 in vascular smooth muscle cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.268284"}], "href": "https://doi.org/10.1074/jbc.M111.268284"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21857021"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21857021"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Lei Zhou, Emma V Jones, Keith K Murai "}, {"type": "b", "children": [{"type": "t", "text": "EphA signaling promotes actin-based dendritic spine remodeling through slingshot phosphatase."}]}, {"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.M111.302802"}], "href": "https://doi.org/10.1074/jbc.M111.302802"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22282498"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22282498"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Souichi Kurita, Emi Gunji, Kazumasa Ohashi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Actin filaments-stabilizing and -bundling activities of cofilin-phosphatase Slingshot-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genes Cells (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1365-2443.2007.01078.x"}], "href": "https://doi.org/10.1111/j.1365-2443.2007.01078.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17535256"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17535256"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Holly C Williams, Jing Ma, Daiana Weiss, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The cofilin phosphatase slingshot homolog 1 restrains angiotensin II-induced vascular hypertrophy and fibrosis in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Lab Invest (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41374-018-0116-6"}], "href": "https://doi.org/10.1038/s41374-018-0116-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30291325"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30291325"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Shiue-Wei Lai, Yi-Chiao Cheng, Wen-Chien Huang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Dysregulated expression of slingshot protein phosphatase 1 (SSH1) disrupts circadian rhythm and WNT signaling associated to hepatocellular carcinoma pathogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Aging (Albany NY) (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/aging.205064"}], "href": "https://doi.org/10.18632/aging.205064"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37837551"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37837551"}]}]}]}
NCBI Gene ID 100422955
API
Download Associations
Predicted Functions View MIR4273's ARCHS4 Predicted Functions.
Co-expressed Genes View MIR4273's ARCHS4 Predicted Functions.
Expression in Tissues and Cell Lines View MIR4273's ARCHS4 Predicted Functions.

Functional Associations

MIR4273 has 585 functional associations with biological entities spanning 5 categories (molecular profile, functional term, phrase or reference, disease, phenotype or trait, cell line, cell type or tissue, gene, protein or microRNA) extracted from 15 datasets.

Click the + buttons to view associations for MIR4273 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 MIR4273 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
COMPARTMENTS Curated Protein Localization Evidence Scores cellular components containing MIR4273 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
COMPARTMENTS Experimental Protein Localization Evidence Scores cellular components containing MIR4273 protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
COSMIC Cell Line Gene CNV Profiles cell lines with high or low copy number of MIR4273 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
DISEASES Text-mining Gene-Disease Association Evidence Scores diseases co-occuring with MIR4273 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
ENCODE Histone Modification Site Profiles histone modification site profiles with high histone modification abundance at MIR4273 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 MIR4273 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
ENCODE Transcription Factor Targets transcription factors binding the promoter of MIR4273 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
GTEx Tissue Gene Expression Profiles tissues with high or low expression of MIR4273 gene relative to other tissues from the GTEx Tissue Gene Expression Profiles dataset.
JASPAR Predicted Transcription Factor Targets transcription factors regulating expression of MIR4273 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 MIR4273 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 MIR4273 gene from the KnockTF Gene Expression Profiles with Transcription Factor Perturbations dataset.
Roadmap Epigenomics Histone Modification Site Profiles histone modification site profiles with high histone modification abundance at MIR4273 gene from the Roadmap Epigenomics Histone Modification Site Profiles dataset.
TISSUES Curated Tissue Protein Expression Evidence Scores tissues with high expression of MIR4273 protein from the TISSUES Curated Tissue Protein Expression Evidence Scores dataset.
TISSUES Experimental Tissue Protein Expression Evidence Scores tissues with high expression of MIR4273 protein in proteomics datasets from the TISSUES Experimental Tissue Protein Expression Evidence Scores dataset.