Ankyrin repeat and KH domain-containing protein 1-eIF4E-binding protein 3 readthrough (ANKHD1-EIF4EBP3)

ANKHD1-EIF4EBP3 is a fusion protein product of a readthrough transcript between the ANKHD1 and EIF4EBP3 genes. The resulting protein is dominated by ankyrin repeat and KH domains from ANKHD1, with a unique C-terminal region translated in an alternate reading frame from EIF4EBP3. The canonical fusion (sometimes referred to as MASK-BP3) is expressed in various mammalian tissues and cancer cells, but its biological function is not well understood. Both parent proteins are involved in cellular processes including RNA binding, translation regulation, and signal transduction (notably Ras/MAPK signaling pathways). Experimentally, the fusion protein has been detected and may be a substrate for protein arginine methyltransferase 1 (PRMT1), which could modify its interaction properties. The fusion is described as evolutionarily conserved and potentially relevant to stress responses and differentiation, but there is no definitive evidence supporting a therapeutic or disease-related role at this time[1][2][5][6].\n\nFurther context: This readthrough event produces a chimeric protein distinct from both the ANKHD1 and EIF4EBP3 canonical proteins[1][5]. The frequency and impact of this fusion, as well as its conditions of expression, are not fully known[2]. Related, but distinct, proteins (ANKHD1 and EIF4EBP3) have documented roles in cell survival, proliferation, and translation repression; the fusion may integrate such signaling or regulatory functions[2][1].\n\nSummary: While ANKHD1-EIF4EBP3 exists as a valid transcript and protein, its functional significance, therapeutic targeting, and disease associations remain speculative and largely undetermined in the literature to date[1][5][6].

Other names

MASK-BP3MASK-BP3ARFMASK-4E-BP3 alternate reading frameANKHD1-EIF4EBP3 protein