TRIM14: A Potential Drug Target and Biomarker (G9830)

Target Name: TRIM14

NCBI ID: G9830

TRIM14

TRIM14: A Potential Drug Target and Biomarker

TRIM14 (Tripartite Motif Containing 14) is a protein that is expressed in various tissues and cell types in the human body. Its unique structure, consisting of three parts connected to each other, has led to its identification as a potential drug target and biomarker. In this article, we will explore the TRIM14 protein, its potential drug target status, and its potential as a biomarker for various diseases.

Structure and Function

TRIM14 is a 14kDa protein that is expressed in various tissues, including muscle, heart, kidney, liver, and brain. It is characterized by three distinct parts, each of which has unique functions in regulating cellular processes. The N-terminus of TRIM14 contains a putative N-acyltransferase domain (NAT), which is involved in the transfer of acyl groups to other proteins. The middle region of TRIM14 contains a putative transmembrane domain (TMD), which is responsible for the protein's localization and stability. The C-terminus of TRIM14 contains a putative coiled-coil domain (CCD), which is involved in the regulation of protein stability and localization.

TRIM14 functions as a negative regulator of the nuclear factor of activated T cells (NFAT), a transcription factor that plays a crucial role in regulating cellular processes such as cell growth, differentiation, and survival. NFAT is activated by various factors, including DNA-binding proteins and chemokines. Once NFAT is activated, it translocates into the nucleus and enhances the expression of various genes involved in cell growth and survival.

TRIM14 is known to interact with the NFATC1 gene, which encodes the NFAT transcription factor. This interaction between TRIM14 and NFATC1 leads to the regulation of NFAT activity and the silencing of its downstream targets. This interaction between TRIM14 and NFATC1 also plays a role in the regulation of cellular processes such as cell growth, apoptosis, and inflammation.

Potential Drug Target

TRIM14 has been identified as a potential drug target due to its unique structure and its involvement in the regulation of cellular processes that are crucial for human health. One of the TRIM14-mediated pathways, the regulation of NFAT activity, has been targeted by various drugs, including inhibitors of the protein kinase B (PKB), which is a well-established TRIM14 inhibitor.

In addition to inhibitors of PKB, TRIM14 has also been targeted by inhibitors of the DNA-protein binding protein p53, which is a negative regulator of NFAT. p53 has been shown to play a role in the regulation of cellular processes such as cell growth, apoptosis, and DNA repair. TRIM14 has been shown to interact with p53 and to regulate its activity, suggesting a potential role for TRIM14 as a biomarker for p53-mediated diseases.

Potential Biomarker

TRIM14 has been shown to be involved in the regulation of cellular processes that are relevant to a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. In cancer, TRIM14 has been shown to play a role in the regulation of cell cycle progression, apoptosis, and angiogenesis. In neurodegenerative diseases, TRIM14 has been shown to contribute to the regulation of neuroinflammation and neuroprotection. In autoimmune diseases, TRIM14 has been shown to play a role in the regulation of immune cell function and the regulation of inflammation.

Conclusion

In conclusion, TRIM14 is a protein that is expressed in various tissues and cell types

Protein Name: Tripartite Motif Containing 14

Functions: Plays an essential role in the innate immune defense against viruses and bacteria (PubMed:30150992, PubMed:32404352). Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways (PubMed:24379373). Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation (PubMed:27666593). Acts as a scaffold between TBK1 and STAT3 to promote phosphorylation of STAT3 and resolve interferon-stimulated gene (ISG) expression (PubMed:32404352). Inhibits the transcriptional activity of SPI1 in a dose-dependent manner (By similarity)

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•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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•   pharmacochemistry experiments;
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The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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