Tripartite motif-containing protein 27 (TRIM27)

Tripartite motif-containing protein 27 (TRIM27) is a 58 kDa intracellular protein encoded by the *TRIM27* gene and belongs to the tripartite motif (TRIM) family of proteins, specifically the C-IV subfamily[1]. It contains a RING finger domain, two B-box domains, a coiled-coil domain, and a PRYSPRY domain, and is classified as a RING-type E3 ubiquitin ligase[1]. TRIM27 is involved in diverse cellular processes such as ubiquitination, regulation of transcription, and signal transduction. Functionally, TRIM27 modulates several key pathways, including PI3K/AKT (by inhibiting PTEN), Wnt/β-catenin (by degrading SIX3), and IL-6/JAK/STAT3 (by recruiting and promoting phosphorylation of JAK1 and STAT3), which contribute to cell proliferation, apoptosis regulation, and immune response modulation[1][3]. TRIM27 plays a crucial role in cancer progression and is often upregulated in various malignancies, promoting proliferation, epithelial-mesenchymal transition, invasion, and metastasis[2][3]. Its function in inflammation, immune signaling, and response to viral infection has also been documented, making it a potential therapeutic target and biomarker in cancer and inflammatory diseases[1][2][3].

Other names

Zinc finger protein RFPRFPRNF76RING finger protein 76Ret finger proteinTripartite motif-containing protein 27RFP transforming proteinRING-type E3 ubiquitin transferase TRIM27tripartite motif protein TRIM27

Modulation of PI3K/AKT signaling via inhibition of PTEN phosphatase activity. Promotion of Wnt/β-catenin signaling via degradation of SIX3. Promotion of STAT3 phosphorylation and downstream signaling (IL-6/JAK/STAT pathway). Regulation of immune responses by modulating TBK1 degradation and IFN production.