ATP-dependent RNA helicase DDX1 (DDX1)

ATP-dependent RNA helicase DDX1 (DDX1) is a member of the DEAD-box family of RNA helicases defined by the conserved Asp-Glu-Ala-Asp (DEAD) motif[1]. It is an enzyme that hydrolyzes ATP to unwind and remodel RNA and is involved in most stages of RNA metabolism, including transcription, splicing, ribosome synthesis, and mRNA stability and decay[1][2][3][4]. DDX1 is distinct among DEAD-box proteins for containing both the Q motif (important for ATP binding and hydrolysis) and a unique SPRY domain (involved in protein-protein recognition)[1]. DDX1 localizes predominantly to the nucleus, often in nucleoplasmic foci associated with the cleavage and polyadenylation of pre-mRNAs, but can also be found in the cytoplasm of certain transformed or overexpressing cells[1][3][4]. It is a component of several ribonucleoprotein complexes, participates directly in the 3' end processing of mRNA through interactions with factors like CstF-64, and plays additional roles in DNA repair, immune sensing of viral RNA, and miRNA maturation[1][3][4]. DDX1 is implicated in cancer—both through overexpression (notably in retinoblastoma and others) and its broader involvement in RNA processing pathways essential for cell proliferation[4]. There are currently no well-established drugs that directly target DDX1, and clinical use is limited by its essential role in diverse cellular processes[4].

Other names

DEAD-box helicase 1DEAD box protein 1DEAD box protein retinoblastomaDEAD/H-box helicase 1DBP-RBUKVH5dDEAD (Asp-Glu-Ala-Asp) box helicase 1