function:May facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. Can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. Can regulate protein arginine N-methyltransferase 1 activity. May regulate transcription of the IL2 gene during T-cell activation. Can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA.,PTM:Arg-609 is dimethylated, probably to asymmetric dimethylarginine.,PTM:Methylated by protein arginine N-methyltransferase 1.,PTM:Phosphorylated by RNA-dependent protein kinase (EIF2AK2).,sequence caution:Contaminating sequence. Potential poly-A sequence.,sequence caution:Sequencing errors.,similarity:Contains 1 DZF domain.,similarity:Contains 2 DRBM (double-stranded RNA-binding) domains.,subunit:Interacts with FUS and SMN proteins and with PRMT1. Forms a complex with ILF2. Can also bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7 and the heterodimeric complex of G22P1/KU70 and XRCC5/KU80. Forms a heteromeric complex with ZNF346 and ILF3. Found in a nuclear export complex with XPO5, ILF3, Ran and double-stranded RNA or double-stranded minihelix VA1 RNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346.,tissue specificity:Ubiquitous.,
Nucleus, nucleolus . Cytoplasm . Nucleus . Localizes in the cytoplasm in response to viral infection. The unphosphorylated form is retained in the nucleus by ILF2. Phosphorylation at Thr-188 and Thr-315 causes the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. .
Ubiquitous.