Spliceosome RNA helicase DDX39B (DDX39B)

Spliceosome RNA helicase DDX39B (commonly abbreviated as DDX39B, also known as UAP56 or BAT1), is a member of the DEAD-box RNA helicase family. It is a key enzyme involved in multiple aspects of RNA metabolism, primarily mRNA splicing and nucleocytoplasmic mRNA export via the TREX complex, and has additional roles in the regulation of pre-ribosomal RNA synthesis and stability[1][2][3][5]. DDX39B catalyzes ATP-dependent unwinding of RNA, facilitates assembly of spliceosomal complexes, and bridges interactions between RNA-binding proteins and splicing/exon-junction complexes[1][4]. Beyond its vital housekeeping roles, DDX39B expression is found to be elevated in several cancer types and has been associated with increased cell proliferation[2]. Genetic and functional studies link DDX39B to immune function by regulating the splicing of FOXP3 and IL7R, among others, implicating it in autoimmune and inflammatory processes[5]. DDX39B is also required for the export of specific viral RNAs and participates in the cellular response to viral infection[1][3]. As a fundamental regulator of gene expression at the RNA level, DDX39B is considered a potential therapeutic target in oncology, immunology, and virology, but no drugs directly targeting DDX39B are currently in clinical use[2][5].

Other names

BAT1UAP56D6S81E56 kDa U2AF65-associated proteinATP-dependent RNA helicase p47DEAD box protein UAP56HLA-B-associated transcript 1 proteinU2AF65-associated protein 56spliceosome RNA helicase BAT1DEAD (Asp-Glu-Ala-Asp) box polypeptide 39Bnuclear RNA helicase (DEAD family)

Inhibitors or modifiers would theoretically act by altering ATPase or helicase activity, potentially disrupting mRNA export and splicing