RRAGB

Ras-related GTP-binding protein B is a protein that in humans is encoded by the RRAGB gene.[4][5][6]

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] Band X|X F3 Start 153,139,981 bp[1] End 153,171,943 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GTP binding • GO:0001948 protein binding • guanyl ribonucleotide binding • GTPase activity • protein heterodimerization activity • GTPase binding Cellular component • cytoplasm • cytosol • lysosomal membrane • lysosome • cell nucleus • EGO complex • Gtr1-Gtr2 GTPase complex Biological process • regulation of TOR signaling • cellular response to amino acid starvation • cellular protein localization • cell cycle arrest • 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	n/a	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: 153.14 – 153.17 Mb
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

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

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.
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.
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. PMID 9394008.
6. "Entrez Gene: RRAGB Ras-related GTP binding B".

Further reading

• Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome". Nature. 434 (7031): 325–37. 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. 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.