RRAGB

RRAGB
Identifiers
Aliases	RRAGB, RAGB, bA465E19.1, Ras related GTP binding B
External IDs	OMIM: 300725; MGI: 3038613; HomoloGene: 48396; GeneCards: RRAGB; OMA:RRAGB - orthologs
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	151,954,939 bp
RNA expression pattern
	n/a
	Top expressed in
	Hypothalamus; ; hippocampus proper; ; Cerebellum; ; epiblast; ; cerebellar cortex; ; dentate gyrus of hippocampal formation granule cell; ; primary visual cortex; ; Cortex of frontal lobe; ; superior frontal gyrus; ; olfactory bulb;
	More reference expression data
Gene ontology
Molecular function	nucleotide binding; GTP binding; protein binding; guanyl ribonucleotide binding; GTPase activity; protein heterodimerization activity; GTPase binding;
Cellular component	cytoplasm; cytosol; lysosomal membrane; lysosome; nucleus; Gtr1-Gtr2 GTPase complex;
Biological process	regulation of TOR signaling; cellular response to amino acid starvation; cellular response to amino acid stimulus; positive regulation of TOR signaling; regulation of autophagy; regulation of macroautophagy; positive regulation of TORC1 signaling; cellular response to leucine starvation; cellular response to starvation;
	Sources:Amigo / QuickGO
Orthologs
	10325
	245670
	ENSG00000083750
	ENSMUSG00000041658
	Q5VZM2
	Q6NTA4
	NM_006064; NM_016656
	NM_001004154
	NP_006055; NP_057740; NP_001340940; NP_001340942
	NP_001004154
	Wikidata
View/Edit Human	View/Edit Mouse

Ras-related GTP-binding protein B is a protein that in humans is encoded by the RRAGB gene.

Ras-homologous GTPases constitute a large family of signal transducers that alternate between an activated, GTP-binding state and an inactivated, GDP-binding state. These proteins represent cellular switches that are operated by GTP-exchange factors and factors that stimulate their intrinsic GTPase activity. All GTPases of the Ras superfamily have in common the presence of six conserved motifs involved in GTP/GDP binding, three of which are phosphate-/magnesium-binding sites (PM1-PM3) and three of which are guanine nucleotide-binding sites (G1-G3). Transcript variants encoding distinct isoforms have been identified. MTORC1 responds to amino acids via interaction with RAGB.