RAB29

RAB29 (RAB29, Member RAS Oncogene Family) is a Protein Coding gene. Among its related pathways are Metabolism of proteins and RAB geranylgeranylation. Gene Ontology (GO) annotations related to this gene include GTP binding and GTPase activity. An important paralog of this gene is RAB32.

Full Name

RAB29, Member RAS Oncogene Family

Function

The small GTPases Rab are key regulators in vesicle trafficking (PubMed:24788816).
Essential for maintaining the integrity of the endosome-trans-Golgi network structure (By similarity).
Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (PubMed:24788816).
Recruits LRRK2 to the Golgi complex and stimulates LRRK2 kinase activity (PubMed:29212815).
Regulates neuronal process morphology in the intact central nervous system (CNS) (By similarity).
May play a role in the formation of typhoid toxin transport intermediates during Salmonella enterica serovar Typhi (S.Typhi) epithelial cell infection (PubMed:22042847).

Biological Process

Biological Process cell differentiationIEA:UniProtKB-KW
Biological Process Golgi organizationManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process intracellular protein transportManual Assertion Based On ExperimentIBA:GO_Central
Biological Process melanosome organizationManual Assertion Based On ExperimentIBA:GO_Central
Biological Process mitochondrion organizationManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process modulation by host of viral processManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process negative regulation of neuron projection developmentManual Assertion Based On ExperimentIDA:ParkinsonsUK-UCL
Biological Process positive regulation of intracellular protein transportManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process positive regulation of receptor recyclingManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process positive regulation of T cell receptor signaling pathwayManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process protein localization to ciliary membraneISS:ParkinsonsUK-UCL
Biological Process protein localization to membraneManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process regulation of neuron deathBy SimilarityISS:ParkinsonsUK-UCL
Biological Process regulation of retrograde transport, endosome to GolgiIEA:Ensembl
Biological Process response to bacteriumManual Assertion Based On ExperimentIDA:ParkinsonsUK-UCL
Biological Process retrograde transport, endosome to GolgiManual Assertion Based On ExperimentIMP:UniProtKB
Biological Process synapse assemblyManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process T cell activationManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL
Biological Process toxin transportManual Assertion Based On ExperimentIMP:ParkinsonsUK-UCL

Cellular Location

Cell membrane
Cytoplasm
Cytoplasm, perinuclear region
Golgi apparatus
Golgi apparatus, trans-Golgi network
Vacuole
Cytoplasm, cytoskeleton
Colocalizes with LRRK2 along tubular structures emerging from Golgi apparatus (PubMed:29212815).
Colocalizes with GM130 at the Golgi apparatus (PubMed:22042847).
Colocalizes with dynamic tubules emerging from and retracting to the Golgi apparatus (PubMed:22042847).
Colocalizes with TGN46 at the trans-Golgi network (TGN) (PubMed:24788816).
In Salmonella enterica serovar Typhi (S.Typhi) infected epithelial cells, is recruited and colocalized with both S.Typhi-containing vacuoles and dynamic tubules as well as those emerging from the vacuole toward the cell periphery (PubMed:22042847).

PTM

In case of Salmonella enterica serovar Typhimurium (S.Typhimurium) infection, is proteolytically cleaved between Gly-41 and Val-42 by the GtgE viral protease encoded on the Gifsy-2 lysogen bacteriophage, which therefore prevents the recruitment of RAB29 to S.Typhimurium-containing vacuoles. In contrast, no proteolytically cleavage is detected in S.Typhi-infected cells (PubMed:22042847).