RRAGB
From Wikipedia, the free encyclopedia
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Ras-related GTP binding B
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| Identifiers | ||||||||||||||
| Symbol(s) | RRAGB; RAGB; bA465E19.1 | |||||||||||||
| External IDs | MGI: 3038613 HomoloGene: 48396 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 10325 | 245670 | ||||||||||||
| Ensembl | ENSG00000083750 | ENSMUSG00000041658 | ||||||||||||
| Uniprot | Q5VZM2 | Q6NTA4 | ||||||||||||
| Refseq | NM_006064 (mRNA) NP_006055 (protein) |
NM_001004154 (mRNA) NP_001004154 (protein) |
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| Location | Chr X: 55.76 - 55.8 Mb | Chr X: 148.48 - 148.51 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Ras-related GTP binding B, also known as RRAGB, is a human gene.[1]
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.[1]
[edit] References
[edit] 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:. 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:. 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. 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:. 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:. PMID 11073942.
- Hirose E, Nakashima N, Sekiguchi T, Nishimoto T (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.
- Schürmann A, Brauers A, Massmann S, et al. (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. PMID 7499430.

