Function | Acts as an E3 ubiquitin-protein ligase. 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. (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. |
Protein Name | E3 Ubiquitin-Protein Ligase Trim23Adp-Ribosylation Factor Domain-Containing Protein 1Gtp-Binding Protein Ard-1Ring Finger Protein 46Ring-Type E3 Ubiquitin Transferase Trim23Tripartite Motif-Containing Protein 23 |
Cellular Localisation | CytoplasmEndomembrane SystemGolgi Apparatus MembraneLysosome MembraneMembrane-Associated With The Golgi Complex And Lysosomal Structures |
Alternative Antibody Names | Anti-E3 Ubiquitin-Protein Ligase Trim23 antibodyAnti-Adp-Ribosylation Factor Domain-Containing Protein 1 antibodyAnti-Gtp-Binding Protein Ard-1 antibodyAnti-Ring Finger Protein 46 antibodyAnti-Ring-Type E3 Ubiquitin Transferase Trim23 antibodyAnti-Tripartite Motif-Containing Protein 23 antibodyAnti-TRIM23 antibodyAnti-ARD1 antibodyAnti-ARFD1 antibodyAnti-RNF46 antibody |
Information sourced from Uniprot.org