8.A.133. The SIAH1 E3 ubiquitin-protein ligase (SIAH1) Family
E3 ubiquitin-protein ligase, Siah1, mediates ubiquitination and subsequent proteasomal degradation of many target proteins (Hu and Fearon 1999). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (Germani et al. 2003). It interacts with the intracellular region of polycystin-1 and affects its stability via the ubiquitin-proteasome pathway (Kim et al. 2004). It has some overlapping function with SIAH2 (Pérez et al. 2012; Malz et al. 2012). It also stabilizes or destabilizes various protein targets (Liu et al. 2012). A review focuses on potential multiprotein complexes involving calcium-insensitive S100A10, annexin A2 and several other proteins including AHNAK, dysferlin, NS3, TASK-1 and TRPV5/6 (Rezvanpour and Shaw 2009). The E3 ligase TRIM7 suppresses the tumorigenesis of gastric cancer by targeting the SLC7A11 cystine/glutamate amino acid transporter (TC# 2.A.3.8.18) (Chen et al. 2024).