Tripartite motif-containing protein 26 (TRIM26)

Tripartite motif-containing protein 26 (TRIM26) is an E3 ubiquitin-protein ligase and a member of the TRIM family, characterized by a RING domain, one or two B-Box domains, a coiled-coil region, and a C-terminal PRY/SPRY domain[1][2][5]. TRIM26 regulates multiple cellular processes, including antiviral innate immunity through modulation of interferon pathways, type I interferon response, and NF-κB/MAPK signaling[1][2][3][5]. It mediates ubiquitination and proteasomal degradation of key immune regulators (such as IRF3, TAB1) and tissue-specific transcription factors (e.g., C/EBPδ), thereby influencing responses to viral infections and inflammation[1][2][3][4][5]. TRIM26 displays both protective and pathogenic roles during infection, inflammation, tumorigenesis, and metabolic disease—actions contextually dependent on cell type and tissue[1][2][3]. It is considered a putative therapeutic target in antiviral, anti-inflammatory, and antifibrotic strategies, but its dual regulatory roles pose challenges for clinical exploitation[1][3][5].

Other names

RNF95ZNF173Acid finger proteinRING finger protein 95Zinc finger protein 173Widely expressed acid zinc finger protein

Ubiquitination and proteasomal degradation of target proteins (e.g., IRF3, C/EBPδ, PHF20, SLC7A11, TAB1) Modulation of viral protein stability (e.g., HCV NS5B, HBV HBx) Regulation of signaling complexes (e.g., bridging TBK1 and NEMO)