RRAGB

Ras-related GTP binding B, also known as RRAGB, is a human gene.cite web | title = Entrez Gene: RRAGB Ras-related GTP binding B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10325| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: RRAGB Ras-related GTP binding B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10325| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Ross MT, Grafham DV, Coffey AJ, "et al." |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
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |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
*cite journal | author=Tomarev SI, Wistow G, Raymond V, "et al." |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=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |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
*cite journal | author=Sekiguchi T, Hirose E, Nakashima N, "et al." |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
*cite journal | author=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. |journal=J. Cell. Sci. |volume=111 ( Pt 1) |issue= |pages= 11-21 |year= 1998 |pmid= 9394008 |doi=
*cite journal | author=Schürmann A, Brauers A, Massmann S, "et al." |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 |year= 1996 |pmid= 7499430 |doi=

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