| Post Translational Modifications | Phosphorylated at Thr-188 and Thr-315 by PKR in response to certain RNA viruses. This phosphorylation results in the dissociation of ILF2 from the ILF2-ILF3 complex resulting in a cytoplasmic sequestration of ILF3 where it can bind to viral RNAs and impede viral replication. Methylated by protein arginine N-methyltransferase 1. Ubiquitinated at Lys-297 in a TRIM47-dependent manner.this 'Lys-48'-linked ubiquitination promotes ILF3 degradation. |
| Function | RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. Plays thereby a role in the back-splicing of a subset of circRNAs. As a consequence, participates in a wide range of transcriptional and post-transcriptional processes. Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Upon viral infection, ILF3 accumulates in the cytoplasm and participates in the innate antiviral response. Mechanistically, ILF3 becomes phosphorylated and activated by the double-stranded RNA-activated protein kinase/PKR which releases ILF3 from cellular mature circRNAs. In turn, unbound ILF3 molecules are able to interact with and thus inhibit viral mRNAs. (Microbial infection) Plays a positive role in HIV-1 virus production by binding to and thereby stabilizing HIV-1 RNA, together with ILF3. |
| Protein Name | Interleukin Enhancer-Binding Factor 3Double-Stranded Rna-Binding Protein 76Drbp76M-Phase Phosphoprotein 4Mpp4Nuclear Factor Associated With DsrnaNfarNuclear Factor Of Activated T-Cells 90 KdaNf-At-90Translational Control Protein 80Tcp80 |
| Database Links | Reactome: R-HSA-9762293Reactome: R-HSA-9833482 |
| Cellular Localisation | NucleusNucleolusCytoplasmLocalizes In The Cytoplasm In Response To Viral InfectionThe Unphosphorylated Form Is Retained In The Nucleus By Ilf2Phosphorylation At Thr-188 And Thr-315 Causes The Dissociation Of Ilf2 From The Ilf2-Ilf3 Complex Resulting In A Cytoplasmic Sequestration Of Ilf3Localized In Cytoplasmic Mrnp Granules Containing Untranslated Mrnas |
| Alternative Protein Names | Interleukin Enhancer-Binding Factor 3 proteinDouble-Stranded Rna-Binding Protein 76 proteinDrbp76 proteinM-Phase Phosphoprotein 4 proteinMpp4 proteinNuclear Factor Associated With Dsrna proteinNfar proteinNuclear Factor Of Activated T-Cells 90 Kda proteinNf-At-90 proteinTranslational Control Protein 80 proteinTcp80 proteinILF3 proteinDRBF proteinMPHOSPH4 proteinNF90 protein |
Information sourced from Uniprot.org
