E3 ubiquitin-protein ligase TRIM39 (TRIM39)

E3 ubiquitin-protein ligase TRIM39 (TRIM39) is a member of the tripartite motif (TRIM) protein family characterized by a RING domain, B-box type 1 and 2, and a coiled-coil region[4][5]. TRIM39 functions primarily as an E3 ubiquitin ligase that modulates protein stability and turnover, especially in cellular pathways regulating inflammation, apoptosis, autophagy, and cell cycle progression[1][2][3][4]. It stabilizes key cell cycle regulators (notably p21), promotes autophagosome–lysosome fusion via interactions with Rab7, and can regulate tumor suppressors such as p53. TRIM39 is upregulated in several cancers, where its activity facilitates tumor progression; it is also involved in immune signaling and may be relevant to autoimmune conditions. Elevated TRIM39 is linked to poor prognosis in colorectal and breast cancer, suggesting its utility as a biomarker and therapeutic target[1][3][5].

Other names

Tripartite motif-containing protein 39RING finger protein 23RNF23Testis-abundant finger proteinTFPTRIM39B

Targeting TRIM39 can potentially alter cell cycle arrest (via p21 stabilization), modulate apoptosis, or impede autophagic flux depending on cancer context[1][2][3].