Loading the page.
Proteins/UNIPROT:P36406
E3 ubiquitin ligase that harbors GTPase activity encoded by the C-terminal ARF domain. Plays an essential role in autophagy activation during viral infection. Mechanistically, activates TANK-binding kinase 1/TBK1 by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor SQSTM1. In order to achieve this function, TRIM23 mediates 'Lys-27'-linked auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to induce its GTPase activity and its recruitment to autophagosomes. Catalyzes 'Lys-63'-linked polyubiquitination of HAX1 that triggers its liquid-liquid phase separation (LLPS) and contributes to P-bodies assembly induced by energy stress..
(Microbial infection) Mediates TRAF6 auto-ubiquitination in the presence of human cytomegalovirus protein UL144, resulting in the virally controlled activation of NF-kappa-B stimulation at early times of HCMV infection..
Function from UniProtKB (P36406), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
51 statements
51 statements · 2 reference databases · Subject: TRIM23 · Sources: gene ontology, Hetionet
8 names
Resolves to: TRIM23