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Proteins/UNIPROT:Q9ULC3
The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. In conjunction with IFT57 and KIF17, it drives the localization of specific G protein-coupled receptors, such as the dopamime receptor DRD1, to primary cilia. Has a critical role in the formation and elongation of neuronal primary cilia, thereby impacting the activation of sonic hedgehog (Shh) signaling. Additionally, it is involved in the down-regulation of Shh signaling by cooperating with SUFU to prevent the nuclear import of GLI1 transcription factor, thus suppressing its transcriptional activity. Regulates GLI1 in differentiating chondrocytes. Likewise, regulates GLI3 proteolytic processing and modulates GLI2 and GLI3 transcription factor activity. Plays a role in autophagic vacuole assembly, and mediates defense against pathogens, such as S.aureus, by promoting their capture by autophagosomes that then merge with lysosomes..
Function from UniProtKB (Q9ULC3), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
2 rows
63 statements
63 statements · 5 reference databases · Subject: RAB23 · Sources: gene ontology, Hetionet, Reactome, UniProt, WikiPathways
1 reaction
1 name
Resolves to: RAB23
Rhea RHEA:19669CC BY 4.0Reference data