MIR1282 Gene

HGNC Family Non-coding RNAs
Name microRNA 1282
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 collective findings indicate that MIR1282—associated with components of the transcription/export (TREX) complex, including FMIP and THOC5—plays a pivotal role in coupling transcription elongation to the export of a select subset of mRNAs. Early studies demonstrated that while the THO complex is not essential for bulk polyadenylated mRNA export in higher eukaryotes, it is crucial for the export of specific mRNAs, suggesting that MIR1282-associated factors may modulate RNA processing/export under defined developmental or environmental conditions (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAdditional work focusing on FMIP, a protein functionally linked to MIR1282, has shown that its regulation through tyrosine kinase and protein kinase C (PKC) phosphorylation governs its nucleocytoplasmic distribution. This dynamic localization is critical for influencing key signaling pathways; for instance, FMIP phosphorylation impacts cell survival and the balance between adipocytic and myogenic differentiation, with alterations in RNA splicing and processing observed for regulators such as C/EBPα. These studies underscore a mechanism whereby MIR1282-associated proteins affect lineage commitment and differentiation via modulation of mRNA export (see."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMore recent investigations have expanded our understanding of MIR1282’s functional network by revealing that THOC5, another key component of the TREX complex linked to MIR1282 activity, is essential for the export and processing of mRNAs that drive processes such as hematopoietic differentiation and stress response. THOC5-dependent regulation has been implicated not only in the proper expression of developmental transcription factors and immediate-early genes (including those activated by M-CSF) but also in the nuclear export of unspliced viral transcripts. Together, these studies emphasize that MIR1282-associated proteins facilitate a highly selective mRNA export process that directly influences cell differentiation, migration, and even viral gene expression (see."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Annalisa Mancini, Susanne C Niemann-Seyde, Rüdiger Pankow, et al. "}, {"type": "b", "children": [{"type": "t", "text": "THOC5/FMIP, an mRNA export TREX complex protein, is essential for hematopoietic primitive cell survival in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Biol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1741-7007-8-1"}], "href": "https://doi.org/10.1186/1741-7007-8-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20051105"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20051105"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Anuja Guria, Doan Duy Hai Tran, Sheetal Ramachandran, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of mRNAs that are spliced but not exported to the cytoplasm in the absence of THOC5 in mouse embryo fibroblasts."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "RNA (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1261/rna.2607011"}], "href": "https://doi.org/10.1261/rna.2607011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21525145"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21525145"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Annalisa Mancini, Alexandra Koch, Anthony D Whetton, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The M-CSF receptor substrate and interacting protein FMIP is governed in its subcellular localization by protein kinase C-mediated phosphorylation, and thereby potentiates M-CSF-mediated differentiation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1207841"}], "href": "https://doi.org/10.1038/sj.onc.1207841"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15221008"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15221008"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "A Mancini, O El Bounkari, A-F Norrenbrock, et al. "}, {"type": "b", "children": [{"type": "t", "text": "FMIP controls the adipocyte lineage commitment of C2C12 cells by downmodulation of C/EBP alpha."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1209853"}], "href": "https://doi.org/10.1038/sj.onc.1209853"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16909111"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16909111"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "D D H Tran, S Saran, O Dittrich-Breiholz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Transcriptional regulation of immediate-early gene response by THOC5, a member of mRNA export complex, contributes to the M-CSF-induced macrophage differentiation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Death Dis (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/cddis.2013.409"}], "href": "https://doi.org/10.1038/cddis.2013.409"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24157873"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24157873"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Shashank Saran, Doan D H Tran, Sabine Klebba-Färber, et al. "}, {"type": "b", "children": [{"type": "t", "text": "THOC5, a member of the mRNA export complex, contributes to processing of a subset of wingless/integrated (Wnt) target mRNAs and integrity of the gut epithelial barrier."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Cell Biol (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1471-2121-14-51"}], "href": "https://doi.org/10.1186/1471-2121-14-51"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24267292"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24267292"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Toshie Sakuma, Jason M Tonne, Yasuhiro Ikeda "}, {"type": "b", "children": [{"type": "t", "text": "Murine leukemia virus uses TREX components for efficient nuclear export of unspliced viral transcripts."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Viruses (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/v6031135"}], "href": "https://doi.org/10.3390/v6031135"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24618812"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24618812"}]}]}]}
Synonyms MIRN1282, HSA-MIR-1282
NCBI Gene ID 100302254
API
Download Associations
Predicted Functions View MIR1282's ARCHS4 Predicted Functions.
Co-expressed Genes View MIR1282's ARCHS4 Predicted Functions.
Expression in Tissues and Cell Lines View MIR1282's ARCHS4 Predicted Functions.

Functional Associations

MIR1282 has 1,859 functional associations with biological entities spanning 3 categories (molecular profile, cell line, cell type or tissue, gene, protein or microRNA) extracted from 13 datasets.

Click the + buttons to view associations for MIR1282 from the datasets below.

If available, associations are ranked by standardized value

Dataset Summary
Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq tissue samples with high or low expression of MIR1282 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
CCLE Cell Line Gene CNV Profiles cell lines with high or low copy number of MIR1282 gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
ChEA Transcription Factor Binding Site Profiles transcription factor binding site profiles with transcription factor binding evidence at the promoter of MIR1282 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
ChEA Transcription Factor Targets transcription factors binding the promoter of MIR1282 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
ENCODE Histone Modification Site Profiles histone modification site profiles with high histone modification abundance at MIR1282 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 MIR1282 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
ENCODE Transcription Factor Targets transcription factors binding the promoter of MIR1282 gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
GTEx Tissue Gene Expression Profiles tissues with high or low expression of MIR1282 gene relative to other tissues from the GTEx Tissue Gene Expression Profiles dataset.
GTEx Tissue Sample Gene Expression Profiles tissue samples with high or low expression of MIR1282 gene relative to other tissue samples from the GTEx Tissue Sample Gene Expression Profiles dataset.
Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles cell lines with high or low copy number of MIR1282 gene relative to other cell lines from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene CNV Profiles dataset.
Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene Expression Profiles cell lines with high or low expression of MIR1282 gene relative to other cell lines from the Klijn et al., Nat. Biotechnol., 2015 Cell Line Gene Expression Profiles dataset.
MotifMap Predicted Transcription Factor Targets transcription factors regulating expression of MIR1282 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 MIR1282 gene from the Roadmap Epigenomics Histone Modification Site Profiles dataset.