UniProt Summary: 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). {ECO:0000269|PubMed:15684077, ECO:0000269|PubMed:28871090}.
Pfam DomainsGO Terms
Pfam Domains
Miro
Arf
SRPRB
Ras
G-alpha
zf-B box
Gtr1 RagA
GO Terms
enzyme activator activity
Golgi to plasma membrane transport
GDP binding
vesicle-mediated transport to the plasma membrane
post-Golgi vesicle-mediated transport
nucleic acid binding
ubiquitin-protein transferase activity
lysosomal membrane
GTPase activity
Golgi vesicle transport
GTP binding
Golgi membrane
protein ubiquitination
viral process
innate immune response
protein modification by small protein conjugation
symbiotic process
interspecies interaction between organisms
zinc ion binding
defense response to other organism
Golgi apparatus
protein modification by small protein conjugation or removal
intracellular protein transport
identical protein binding
response to other organism
response to external biotic stimulus
response to biotic stimulus
defense response
positive regulation of catalytic activity
protein transport
intracellular transport
peptide transport
amide transport
cellular protein localization
cellular macromolecule localization
establishment of protein localization
positive regulation of molecular function
establishment of localization in cell
nitrogen compound transport
immune response
vesicle-mediated transport
CRISPR Data
Compound HitMost Correlated Genes in ChemogenomicsTissues where Essential in the Avana Dataset (DepMap 20Q1)