MIR3672 Gene

HGNC Family Non-coding RNAs
Name microRNA 3672
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": "\nEMILIN2 is a multifunctional extracellular matrix glycoprotein that plays key roles in maintaining tissue microenvironments and regulating cellular functions. Structurally, it contains an N‑terminal EMI domain and a C‑terminal gC1q domain that mediate its assembly into multimeric complexes – both through homotypic and heterotypic interactions with EMILIN1 – thereby contributing to the integrity of basement membranes. In the cochlea, EMILIN2 is a major component of the basilar membrane where it likely contributes to its assembly and elastic properties, while in the bone marrow stroma its abundant deposition suggests an important role in modulating the hematopoietic niche. Moreover, studies in animal models indicate that EMILIN2 is critical for proper platelet function, influencing aggregation, clot retraction, and overall thrombus stability, which highlights its contribution to hemostasis and thrombosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its structural functions, EMILIN2 exerts a powerful influence on vascular biology. By directly binding to the epidermal growth factor receptor (EGFR), it enhances the production of proangiogenic cytokines such as interleukin‑8, thereby promoting endothelial cell proliferation and migration that are essential for angiogenesis. Furthermore, EMILIN2 facilitates pericyte recruitment and vascular stabilization by serving as an adhesion substrate through its interaction with integrins, and by triggering the synthesis of pericyte‑attracting factors like PDGF‑BB and HB‑EGF. These actions not only enhance vessel maturation and perfusion but also improve drug delivery and chemotherapeutic efficacy in tumor models."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Lori L Amma, Richard Goodyear, Jonathan S Faris, et al. "}, {"type": "b", "children": [{"type": "t", "text": "An emilin family extracellular matrix protein identified in the cochlear basilar membrane."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Neurosci (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/s1044-7431(03)00075-7"}], "href": "https://doi.org/10.1016/s1044-7431(03"}, {"type": "t", "text": "00075-7) PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12837629"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12837629"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Simonetta Bot, Eva Andreuzzi, Alessandra Capuano, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Multiple-interactions among EMILIN1 and EMILIN2 N- and C-terminal domains."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Matrix Biol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.matbio.2014.10.001"}], "href": "https://doi.org/10.1016/j.matbio.2014.10.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25445627"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25445627"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Menggui Huang, Devaraja Sannaningaiah, Nan Zhao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "EMILIN2 regulates platelet activation, thrombus formation, and clot retraction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0115284"}], "href": "https://doi.org/10.1371/journal.pone.0115284"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25658937"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25658937"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Alice Paulitti, Eva Andreuzzi, Dario Bizzotto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The ablation of the matricellular protein EMILIN2 causes defective vascularization due to impaired EGFR-dependent IL-8 production affecting tumor growth."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41388-017-0107-x"}], "href": "https://doi.org/10.1038/s41388-017-0107-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29483644"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29483644"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Francesco Da Ros, Luca Persano, Dario Bizzotto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Emilin-2 is a component of bone marrow extracellular matrix regulating mesenchymal stem cell differentiation and hematopoietic progenitors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Stem Cell Res Ther (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s13287-021-02674-2"}], "href": "https://doi.org/10.1186/s13287-021-02674-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35012633"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35012633"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Albina Fejza, Lucrezia Camicia, Greta Carobolante, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Emilin2 fosters vascular stability by promoting pericyte recruitment."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Matrix Biol (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.matbio.2023.08.002"}], "href": "https://doi.org/10.1016/j.matbio.2023.08.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37579864"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37579864"}]}]}]}
NCBI Gene ID 100500869
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Predicted Functions View MIR3672's ARCHS4 Predicted Functions.
Co-expressed Genes View MIR3672's ARCHS4 Predicted Functions.
Expression in Tissues and Cell Lines View MIR3672's ARCHS4 Predicted Functions.

Functional Associations

MIR3672 has 77 functional associations with biological entities spanning 1 categories (cell line, cell type or tissue) extracted from 1 datasets.

Click the + buttons to view associations for MIR3672 from the datasets below.

If available, associations are ranked by standardized value

Dataset Summary
Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles cell lines with high or low copy number of MIR3672 gene relative to other cell lines from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles dataset.