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tRNA-uridine aminocarboxypropyltransferase 2 (DTWD2) is a cytoplasmic and nuclear enzyme responsible for the post-transcriptional modification of specific uridine residues in tRNA molecules, namely the formation of 3-(3-amino-3-carboxypropyl)uridine (acp^3^U) at position 20a of the D-loop in select cytoplasmic tRNAs[1][2][3]. This modification is thought to stabilize tRNA structure and promote efficient protein translation, with DTWD2 showing specificity distinct from its paralog DTWD1. While not currently established as a therapeutic drug target, recent research demonstrates that loss or downregulation of DTWD2 is associated with impaired cell growth and poor prognosis in colon adenocarcinoma, indicating a putative tumor suppressor function. DTWD2 does not appear to be directly targeted by any drugs as of current knowledge[2][3]. **Key details:** - DTWD2 acts as an aminocarboxypropyltransferase, catalyzing acp^3^U modification critical for translation fidelity and cell proliferation[1][3]. - DTWD2 expression is downregulated in colon cancer, and its low levels predict negative clinical outcomes, suggesting potential utility as a biomarker[2]. - There is no evidence for direct drug interaction or established mechanism-based safety concerns at present. *Note*: All information is consistently grounded in primary literature and gene/protein databases as of 2025, and there is no indication of problems with the spelling, identity, or target validity of DTWD2[1][2][3].
Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine (acp^3^U) at position 20a in the D-loop of several cytoplasmic tRNAs, which can impact protein synthesis and cell proliferation[1][2][3].
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