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Thioredoxin-like protein 4B (TXNL4B) is a member of a conserved family of small proteins characterized by a thioredoxin-like fold[1][3][5]. It is predominantly located in the cytosol and nucleoplasm and plays an essential role in pre-mRNA splicing, being an integral component of the spliceosome machinery[1][6]. TXNL4B interacts with Prp6 within the U4/U6·U5 tri-snRNP complex, which is central to intron excision from precursor mRNAs. Structurally, TXNL4B exists as a homodimer and its function depends on intact folding and interface domains[3][5]. TXNL4B is also implicated in cell cycle regulation, specifically the S/G2 transition, underscoring its dual role in RNA processing and cell division[1][6]. While there is some disease association (such as pituitary adenoma), there is no evidence that it is a therapeutic target for drugs or a clinical biomarker[6][7].
Not applicable (no known drugs or modulators)
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