RRAGB

RRAGB
Identifiers
Aliases	RRAGB, RAGB, bA465E19.1, Ras related GTP binding B
External IDs	OMIM: 300725 MGI: 3038613 HomoloGene: 48396 GeneCards: RRAGB
Gene location (Mouse) Chr. X chromosome (mouse) Band X|X F3 Start 151,922,977 bp End 151,954,939 bp
RNA expression pattern Bgee Human Mouse (ortholog) n/a Top expressed in hypothalamus hippocampus proper cerebellum cerebellar cortex superior frontal gyrus olfactory bulb ganglionic eminence lens mesencephalon adrenal gland BioGPS 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 Species Human Mouse Entrez 10325 245670 Ensembl ENSG00000083750 ENSMUSG00000041658 UniProt Q5VZM2 Q6NTA4 RefSeq (mRNA) NM_006064 NM_016656 NM_001004154 RefSeq (protein) NP_006055 NP_057740 NP_001340940 NP_001340942 NP_001004154 Location (UCSC) n/a Chr X: 151.92 – 151.95 Mb PubMed search
Wikidata
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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.

Further reading

• Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. Bibcode:2005Natur.434..325R. doi:10.1038/nature03440. PMC 2665286. PMID 15772651.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Tomarev SI, Wistow G, Raymond V, et al. (2003). "Gene expression profile of the human trabecular meshwork: NEIBank sequence tag analysis". Invest. Ophthalmol. Vis. Sci. 44 (6): 2588–96. doi:10.1167/iovs.02-1099. PMID 12766061.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Sekiguchi T, Hirose E, Nakashima N, et al. (2001). "Novel G proteins, Rag C and Rag D, interact with GTP-binding proteins, Rag A and Rag B." J. Biol. Chem. 276 (10): 7246–57. doi:10.1074/jbc.M004389200. PMID 11073942.