ILF3 (interleukin enhancer binding factor 3) or TCP80 (translational control protein 80), is a ubiquitously expressed nuclear protein that exists in a heterodimer with NF45. NF90 contains two DRBM (double-stranded RNA (dsRNA-)-binding) domains and one DZF domain and, in association with NF45 primarily participates in the regulation of IL-2 expression by binding to the antigen receptor response element (ARRE) target sequence of the IL-2 enhancer. In neuronal cells, the NF45/NF90 heterodimer can repress human rhinovirus type 2 replication by binding to a 5' untranslated region of the viral RNA that encodes the internal ribosome entry site (IRES). NF45 and NF90 belong to the double-stranded RNA-binding protein family and both are substrates for the dsRNA-activated protein kinase, PKR. Due to alternative splicing events, six isoforms exist for NF90, namely NFAR-2 (or ILF3-E), NFAR-1 (or DRBP76), isoform 3, DRBP76α (or ILF3-A), DRBP76δ (also known as DRBP76γ or ILF3-C) and isoform 6.