Target intelligence / Profile preview

THO complex subunit 7 (THOC7)

Target
THOC7
Molecular classification
Nuclear protein, THO complex subunit, Component of the TREX (transcription/export) complex, RNA-binding protein, Spliceosome-associated protein
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Overview

THO complex subunit 7 (THOC7) is a 23 kDa nuclear protein that forms part of the THO complex, itself a core component of the larger TREX complex critical for mRNA biogenesis. The THO complex couples mRNA transcription, processing, and export processes, mostly by associating with fully spliced mRNAs. THOC7 plays an essential structural role in oligomerizing the complex; for example, it forms a coiled coil with THOC5, necessary for the assembly and stability of larger TREX structures in human cells. THOC7 is also implicated in the regulation of immune signaling, by negatively regulating type I interferon production through promotion of TBK1 degradation. Disruption or mutation of THOC7 or associated THO complex members can result in genetic syndromes or affect mRNA export, with downstream effects on cellular fitness and disease, including roles in viral infection and rare syndromic developmental disorders. To date, THOC7 is not a direct drug target, nor is it used as a biomarker in clinical practice.

Other names
THOC7NIF3L1BP1Functional spliceosome-associated protein 24 (fSAP24)Ngg1-interacting factor 3-like protein 1-binding protein 1hTREX30NIF3L1-binding protein 1
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Mechanism of action

Not applicable (no known drugs)

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Biological functions

mRNA export from the nucleusCoupling of mRNA transcription, processing, and exportOligomerization within the THO-DDX39B complexRNA bindingRegulation of type I interferon (IFN) production by promoting TBK1 proteasomal degradation
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Disease associations

Genetic diseases: Ogden syndrome, Microphthalmia syndromic 1Involvement in infectious disease: TREX complex required for Kaposi's sarcoma-associated herpesvirus (KSHV) mRNA export and virus productionHuman THO maintains stability of repetitive DNA; dysregulation can affect genome integrity
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Safety considerations

None reported; not a direct therapeutic target. General challenges are related to the essential nature of THO complex proteins for cellular viability and genomic stability.

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