| HGNC Family | Non-coding RNAs |
| Name | microRNA 4798 |
| 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 here offers a comprehensive view of the mitochondrial apoptotic pathway, highlighting the pivotal roles of pro‐ and antiapoptotic Bcl‑2 family members—such as Bax, Bak, and their upstream regulators like p53 and Akt—in orchestrating mitochondrial outer membrane permeabilization, cytochrome c release, and caspase activation. These reports detail step‐by‐step mechanisms including conformational changes in Bax/Bak, BH3–domain interactions, phosphorylation events, and coordinated contributions from other modulators that together define the cell’s decision to initiate apoptosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "45"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDespite the impressive breadth of mechanistic insights into apoptosis and mitochondrial dynamics these studies provide, none of the abstracts explicitly discuss or characterize the function of MIR4798. In the absence of direct experimental data linking this microRNA to apoptotic regulation, one can only speculate by analogy that MIR4798 might participate in the fine modulation of these processes—for example, by post‐transcriptionally regulating mRNAs encoding key apoptotic proteins such as Bax, Bak, or other modulators within the mitochondrial stress response pathways. Such a role would be consistent with the extensive network of regulatory controls revealed by these reports."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "45"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn summary, while these reports collectively elaborate on the multifaceted control of mitochondrial apoptosis—from Bax/ Bak activation and mitochondrial dynamics to the modulation by growth and stress signals—they do not currently attribute a defined functional role to MIR4798. Given the regulatory complexity evident in these studies, it remains an attractive possibility that MIR4798 could serve as a microRNA regulator modulating the expression or activity of apoptosis‐related factors. Nonetheless, dedicated research is required to uncover whether MIR4798 intervenes in these signaling cascades and to determine its precise impact on mitochondrial integrity and cell fate."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "45"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kurt Degenhardt, Ramya Sundararajan, Tullia Lindsten, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Bax and Bak independently promote cytochrome C release from mitochondria."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109939200"}], "href": "https://doi.org/10.1074/jbc.M109939200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11836241"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11836241"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Fuminori Tsuruta, Norihisa Masuyama, Yukiko Gotoh "}, {"type": "b", "children": [{"type": "t", "text": "The phosphatidylinositol 3-kinase (PI3K)-Akt pathway suppresses Bax translocation to mitochondria."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M108975200"}], "href": "https://doi.org/10.1074/jbc.M108975200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11842081"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11842081"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Lonnie D Russell, Helio Chiarini-Garcia, Stanley J Korsmeyer, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Akt-directed glucose metabolism can prevent Bax conformation change and promote growth factor-independent survival."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.23.20.7315-7328.2003"}], "href": "https://doi.org/10.1128/MCB.23.20.7315-7328.2003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14517300"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14517300"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Shyra J Gardai, David A Hildeman, Steve K Frankel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phosphorylation of Bax Ser184 by Akt regulates its activity and apoptosis in neutrophils."}]}, {"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.M400063200"}], "href": "https://doi.org/10.1074/jbc.M400063200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14766748"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14766748"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Jerry E Chipuk, Tomomi Kuwana, Lisa Bouchier-Hayes, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Science (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1126/science.1092734"}], "href": "https://doi.org/10.1126/science.1092734"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14963330"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14963330"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Nancy G Forger, Greta J Rosen, Elizabeth M Waters, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deletion of Bax eliminates sex differences in the mouse forebrain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0404644101"}], "href": "https://doi.org/10.1073/pnas.0404644101"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15342910"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15342910"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Hisashi Harada, Bonnie Quearry, Antonio Ruiz-Vela, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Survival factor-induced extracellular signal-regulated kinase phosphorylates BIM, inhibiting its association with BAX and proapoptotic activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0406837101"}], "href": "https://doi.org/10.1073/pnas.0406837101"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15486085"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15486085"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Nathan Majewski, Veronique Nogueira, Prashanth Bhaskar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hexokinase-mitochondria interaction mediated by Akt is required to inhibit apoptosis in the presence or absence of Bax and Bak."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2004.11.014"}], "href": "https://doi.org/10.1016/j.molcel.2004.11.014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15574336"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15574336"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Woong Sun, Adam Winseck, Sharon Vinsant, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Programmed cell death of adult-generated hippocampal neurons is mediated by the proapoptotic gene Bax."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1523/JNEUROSCI.1436-04.2004"}], "href": "https://doi.org/10.1523/JNEUROSCI.1436-04.2004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15590937"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15590937"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Osamu Takeuchi, Jill Fisher, Heikyung Suh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Essential role of BAX,BAK in B cell homeostasis and prevention of autoimmune disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0504783102"}], "href": "https://doi.org/10.1073/pnas.0504783102"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16055554"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16055554"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Lisa J Pagliari, Tomomi Kuwana, Christine Bonzon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The multidomain proapoptotic molecules Bax and Bak are directly activated by heat."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0506712102"}], "href": "https://doi.org/10.1073/pnas.0506712102"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16330765"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16330765"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Ariel E Feldstein, Nathan W Werneburg, Zhengzheng Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Bax inhibition protects against free fatty acid-induced lysosomal permeabilization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Gastrointest Liver Physiol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpgi.00509.2005"}], "href": "https://doi.org/10.1152/ajpgi.00509.2005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16484678"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16484678"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Mariusz Karbowski, Kristi L Norris, Megan M Cleland, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of Bax and Bak in mitochondrial morphogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/nature05111"}], "href": "https://doi.org/10.1038/nature05111"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17035996"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17035996"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Dieter A Kubli, John E Ycaza, Asa B Gustafsson "}, {"type": "b", "children": [{"type": "t", "text": "Bnip3 mediates mitochondrial dysfunction and cell death through Bax and Bak."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20070319"}], "href": "https://doi.org/10.1042/BJ20070319"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17447897"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17447897"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Rana S Moubarak, Victor J Yuste, Cédric Artus, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.02141-06"}], "href": "https://doi.org/10.1128/MCB.02141-06"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17470554"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17470554"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Diana Steckley, Meera Karajgikar, Lianne B Dale, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Puma is a dominant regulator of oxidative stress induced Bax activation and neuronal apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1523/JNEUROSCI.3400-07.2007"}], "href": "https://doi.org/10.1523/JNEUROSCI.3400-07.2007"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18032672"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18032672"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Ryuji Yamaguchi, Lydia Lartigue, Guy Perkins, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Opa1-mediated cristae opening is Bax/Bak and BH3 dependent, required for apoptosis, and independent of Bak oligomerization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2008.07.010"}], "href": "https://doi.org/10.1016/j.molcel.2008.07.010"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18691924"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18691924"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Ildikò Szabó, Jürgen Bock, Heike Grassmé, et al. 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| NCBI Gene ID | 100616471 |
| API | |
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| Predicted Functions |
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| Co-expressed Genes |
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| Expression in Tissues and Cell Lines |
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MIR4798 has 210 functional associations with biological entities spanning 3 categories (molecular profile, cell line, cell type or tissue, gene, protein or microRNA) extracted from 8 datasets.
Click the + buttons to view associations for MIR4798 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 MIR4798 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 MIR4798 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 MIR4798 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 MIR4798 gene from the ENCODE Transcription Factor Binding Site Profiles dataset. | |
| ENCODE Transcription Factor Targets | transcription factors binding the promoter of MIR4798 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset. | |
| Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles | cell lines with high or low copy number of MIR4798 gene relative to other cell lines from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles dataset. | |
| MotifMap Predicted Transcription Factor Targets | transcription factors regulating expression of MIR4798 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 MIR4798 gene from the Roadmap Epigenomics Histone Modification Site Profiles dataset. | |