TRIM13
Description
The TRIM13 (tripartite motif containing 13) is a protein-coding gene located on chromosome 13.
TRIM13 is an E3 ubiquitin ligase anchored to the endoplasmic reticulum (ER) membrane. It plays a key role in ER-associated degradation (ERAD), a process that removes misfolded and correctly folded proteins from the ER. TRIM13 regulates ER stress-induced autophagy and may act as a tumor suppressor. It enhances ionizing radiation-induced p53/TP53 stability and apoptosis by targeting MDM2 and AKT1 for ubiquitination and proteasomal degradation, leading to decreased AKT1 kinase activity. TRIM13 also participates in innate immune responses by stimulating NF-kappa-B activity in the TLR2 signaling pathway. It ubiquitinates TRAF6 via Lys-29-linked polyubiquitination, leading to NF-kappa-B activation. Furthermore, TRIM13 contributes to T-cell receptor-mediated NF-kappa-B activation. In the presence of TNF, it modulates the IKK complex by regulating IKBKG/NEMO ubiquitination, resulting in NF-kappa-B repression.
TRIM13 is also known as CAR, DLEU5, LEU5, RFP2, RNF77.
