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RRAGB

{{Short description|Protein-coding gene in the species Homo sapiens}}

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Ras-related GTP-binding protein B is a protein that in humans is encoded by the RRAGB gene.{{cite journal | vauthors = Schurmann A, Brauers A, Massmann S, Becker W, Joost HG | title = Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagB1) with remote similarity to the Ras-related GTPases | journal = J Biol Chem | volume = 270 | issue = 48 | pages = 28982–8 |date=Jan 1996 | pmid = 7499430 | doi =10.1074/jbc.270.48.28982 | doi-access = free}}{{cite journal | vauthors = Hirose E, Nakashima N, Sekiguchi T, Nishimoto T | title = RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway | series = 111 | journal = J Cell Sci | volume = ( Pt 1) | pages = 11–21 |date=Feb 1998 | doi = 10.1242/jcs.111.1.11 | pmid = 9394008 }}{{cite web | title = Entrez Gene: RRAGB Ras-related GTP binding B| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10325}}

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.

References

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Further reading

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

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