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]
Referencesedit
^ abcGRCm38: 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.
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. PMC2665286. 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. PMC528928. 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. PMC139241. 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.
This article on a gene on the human X chromosome and/or its associated protein is a stub. You can help Wikipedia by expanding it.
rragb, related, binding, protein, protein, that, humans, encoded, gene, identifiersaliases, ragb, ba465e19, related, binding, bexternal, idsomim, 300725, 3038613, homologene, 48396, genecards, gene, location, mouse, chromosome, mouse, bandx, f3start151, end151. Ras related GTP binding protein B is a protein that in humans is encoded by the RRAGB gene 4 5 6 RRAGBIdentifiersAliasesRRAGB RAGB bA465E19 1 Ras related GTP binding BExternal IDsOMIM 300725 MGI 3038613 HomoloGene 48396 GeneCards RRAGBGene location Mouse Chr X chromosome mouse 1 BandX X F3Start151 922 977 bp 1 End151 954 939 bp 1 RNA expression patternBgeeHumanMouse ortholog n aTop expressed inhypothalamushippocampus propercerebellumcerebellar cortexsuperior frontal gyrusolfactory bulbganglionic eminencelensmesencephalonadrenal glandBioGPSMore reference expression dataGene ontologyMolecular functionnucleotide binding GTP binding protein binding guanyl ribonucleotide binding GTPase activity protein heterodimerization activity GTPase bindingCellular componentcytoplasm cytosol lysosomal membrane lysosome nucleus Gtr1 Gtr2 GTPase complexBiological processregulation 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 starvationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez10325245670EnsemblENSG00000083750ENSMUSG00000041658UniProtQ5VZM2Q6NTA4RefSeq mRNA NM 006064NM 016656NM 001004154RefSeq protein NP 006055NP 057740NP 001340940NP 001340942NP 001004154Location UCSC n aChr X 151 92 151 95 MbPubMed search 2 3 WikidataView Edit HumanView 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 edit a b c 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 a b Entrez Gene RRAGB Ras related GTP binding B Further reading editRoss 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 nbsp This article on a gene on the human X chromosome and or its associated protein is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title RRAGB amp oldid 1196126601, wikipedia, wiki, book, books, library,
