Plays an essential role in the innate immune defense against viruses and bacteria (PubMed:30150992, PubMed:32404352). Promotes the 'Lys-48'-linked ubiquitination and subsequent degradation of hepatitis C virus NS5A leading to the inhibition of viral replication (PubMed:27578425). Also plays a role in the inhibition of ebolavirus infection by enhancing IFN-beta and NF-kappa-B activation after binding to the viral protein NP (PubMed:37562033). Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways (PubMed:24379373). Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation (PubMed:27666593). Acts as a scaffold between TBK1 and STAT3 to promote phosphorylation of STAT3 and resolve interferon-stimulated gene (ISG) expression (PubMed:32404352). Inhibits the transcriptional activity of SPI1 in a dose-dependent manner (By similarity). Also inhibits OPTN- mediated selective autophagic degradation of KDM4D and thereby negatively regulates H3K9me2 and H3K9me3. Mechanistically, recruits USP14 to remove the 'Lys-63'-linked ubiquitination of KDM4D, preventing its recognition by OPTN and subsequent degradation (PubMed:35145029). {ECO:0000250|UniProtKB:Q8BVW3, ECO:0000269|PubMed:24379373, ECO:0000269|PubMed:27578425, ECO:0000269|PubMed:27666593, ECO:0000269|PubMed:29053956, ECO:0000269|PubMed:30150992, ECO:0000269|PubMed:32404352, ECO:0000269|PubMed:35145029, ECO:0000269|PubMed:37562033}. This is the function of TRIM14 (tripartite motif containing 14, ENSG00000106785).