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)[1]
End	151,954,939 bp[1]
RNA expression pattern
	n/a
	Top expressed in
	hypothalamus; ; hippocampus proper; ; cerebellum; ; cerebellar cortex; ; superior frontal gyrus; ; olfactory bulb; ; ganglionic eminence; ; mirror; ; mesencephalon; ; adrenal gland;
	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.[4][5][6]

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.[6]

References

GRCm38: Ensembl release 89: ENSMUSG00000041658 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Schurmann A, Brauers A, Massmann S, Becker W, Joost HG (Jan 1996). "Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases". J Biol Chem. 270 (48): 28982–8. doi:10.1074/jbc.270.48.28982. PMID 7499430.
Hirose E, Nakashima N, Sekiguchi T, Nishimoto T (Feb 1998). "RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway". J Cell Sci. 111. ( Pt 1): 11–21. doi:10.1242/jcs.111.1.11. PMID 9394008.
"Entrez Gene: RRAGB Ras-related GTP binding B".

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.

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[refGRCm38Ensembl-1] GRCm38: Ensembl release 89: ENSMUSG00000041658 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7499430-4] Schurmann A, Brauers A, Massmann S, Becker W, Joost HG (Jan 1996). "Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases". J Biol Chem. 270 (48): 28982–8. doi:10.1074/jbc.270.48.28982. PMID 7499430.

[pmid9394008-5] Hirose E, Nakashima N, Sekiguchi T, Nishimoto T (Feb 1998). "RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway". J Cell Sci. 111. ( Pt 1): 11–21. doi:10.1242/jcs.111.1.11. PMID 9394008.

[entrez-6] "Entrez Gene: RRAGB Ras-related GTP binding B".

RRAGB

References

Further reading