Aliases for TRIM23 Gene
- Tripartite Motif Containing 23 2 3 5
- ADP-Ribosylation Factor Domain-Containing Protein 1 3 4
- ADP-Ribosylation Factor Domain Protein 1, 64kDa 2 3
- RING-Type E3 Ubiquitin Transferase TRIM23 3 4
- Tripartite Motif-Containing Protein 23 3 4
- GTP-Binding Protein ARD-1 3 4
- RING Finger Protein 46 3 4
- ARFD1 3 4
External Ids for TRIM23 Gene
Previous HGNC Symbols for TRIM23 Gene
Previous GeneCards Identifiers for TRIM23 Gene
The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein is also a member of the ADP ribosylation factor family of guanine nucleotide-binding family of proteins. Its carboxy terminus contains an ADP-ribosylation factor domain and a guanine nucleotide binding site, while the amino terminus contains a GTPase activating protein domain which acts on the guanine nucleotide binding site. The protein localizes to lysosomes and the Golgi apparatus. It plays a role in the formation of intracellular transport vesicles, their movement from one compartment to another, and phopholipase D activation. Three alternatively spliced transcript variants for this gene have been described. [provided by RefSeq, Jul 2008]
GeneCards Summary for TRIM23 Gene
TRIM23 (Tripartite Motif Containing 23) is a Protein Coding gene. Gene Ontology (GO) annotations related to this gene include identical protein binding and ligase activity. An important paralog of this gene is ARF1.
UniProtKB/Swiss-Prot for TRIM23 Gene
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 (PubMed:28871090).
(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.