Probable E3 ubiquitin-protein ligase MID2 (MID2)

Probable E3 ubiquitin-protein ligase MID2 (commonly known as MID2) is an **enzyme** belonging to the tripartite motif (TRIM) family, characterized by RING, B-box zinc finger, coiled-coil, COS, FN3, and PRY-SPRY domains[1][3][5][7][10]. MID2 is a cytoplasmic protein that localizes to microtubular structures and mediates *ubiquitination*—specifically, Lys-48-linked polyubiquitination of substrates such as LRRK2 (implicated in Parkinson's disease) and astrin (important for proper cytokinesis)[1][9][10]. It plays critical roles in cell division, microtubule stabilization, innate immunity (stimulating JAK-STAT and NF-κB signaling), and has developmental functions, with mutations causing X-linked developmental disorders and its overexpression implicated in breast cancer, where it may serve as a prognostic biomarker[3][5][10]. MID2 interacts with several proteins, including LRRK2 (targeted for degradation), MID1 (paralog), and BRCA1 (breast cancer gene)[1][3][5]. As an E3 ubiquitin ligase involved in essential cell regulation and disease, MID2 represents a potential but unexploited therapeutic target[3][7][10].

Other names

Midline-2TRIM1FXY2RNF60MRX101XLID101RING finger protein 60RING-type E3 ubiquitin transferase MID2tripartite motif-containing protein 1midin 2midline defect 2tripartite motif protein 1

Targeting by drugs (none currently approved) would likely involve inhibition or modulation of E3 ligase activity, affecting protein degradation or signaling pathways