ILF3, also known as NF90, DRBP76, and NFAR, is a double-stranded RNA-binding protein. It has 2 conserved dsRNA-binding domains and 1 RGG motif related to RNA binding. The cellular activity of ILF3 may be regulated by interferon-induced protein kinase PRKR mediated phospholylation. ILF3 binds to the AU-rich elements (AREs) of 3'-UTR and slows down the degradation of IL-2 mRNA. A nuclear localization signal (NLS) and a nuclear export signal (NES) are contained in NF90; in nonstimulated cells, this protein was shown to be localized in the nucleus, whereas in activated T cells, it is accumulated in the cytoplasm. The phosphorylation of NF90 by AKT is reported to mediate nuclear export and increase the stability of IL-2 mRNA. ILF3 is also known to be involved in the localization of transcripts in the nucleus, the transportation of mRNA to the cytoplasm, and the export of ribonucleoprotein.