Ras-related GTP-binding protein A Recombinant Protein | RRAGA recombinant protein

Recombinant Human Ras-related GTP-binding protein A

Cat. Num. AAA717268

• Gene Names: RRAGA; FIP1; RAGA; FIP-1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Ras-related GTP-binding protein A; Recombinant Human Ras-related GTP-binding protein A; Adenovirus E3 14.7 kDa-interacting protein 1FIP-1; RRAGA recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 1-247aa; Partial
• Sequence: MPNTAMKKKVLLMGKSGSGKTSMRSIIFANYIARDTRRLGATIDVEHSHVRFLGNLVLNLWDCGGQDTFMENYFTSQRDNIFRNVEVLIYVFDVESRELEKDMHYYQSCLEAILQNSPDAKIFCLVHKMDLVQEDQRDLIFKEREEDLRRLSRPLECACFRTSIWDETLYKAWSSIVYQLIPNVQQLEMNLRNFAQIIEADEVLLFERATFLVISHYQCKEQRDVHRFEKISNIIKQFKLSCSKLAA
• Sequence Length: 313

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for RRAGA recombinant protein

Guanine nucleotide-binding protein forming heterodimeric Rag complexes required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF-alpha signaling pathway leading to induction of cell death. May alternatively act as a cellular target for adenovirus E3-14. 7K, an inhibitor of TNF-alpha functions, thereby affecting cell death.

Product Categories/Family for RRAGA recombinant protein

Apoptosis

References

Cloning of a novel family of mammalian GTP-binding proteins (RagA, RagBs, RagBl) with remote similarity to the Ras-related GTPases.Schuermann A., Brauers A., Massmann S., Becker W., Joost H.-G.J. Biol. Chem. 270:28982-28988(1995) Interaction of an adenovirus 14.7-kilodalton protein inhibitor of tumor necrosis factor alpha cytolysis with a new member of the GTPase superfamily of signal transducers.Li Y., Kang J., Horwitz M.S.J. Virol. 71:1576-1582(1997) RagA is a functional homologue of S. cerevisiae Gtr1p involved in the Ran/Gsp1-GTPase pathway.Hirose E., Nakashima N., Sekiguchi T., Nishimoto T.J. Cell Sci. 111:11-21(1998) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) DNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004)

NCBI and Uniprot Product Information

• NCBI GI #: 5729999
• NCBI GeneID: 10670
• NCBI Accession #: NP_006561.1
• NCBI GenBank Nucleotide #: NM_006570.4
• UniProt Accession #: Q7L523; O00290; Q15347; B2R7L1
• Molecular Weight: 56.1 kDa
• NCBI Official Full Name: ras-related GTP-binding protein A
• NCBI Official Synonym Full Names: Ras-related GTP binding A
• NCBI Official Symbol: RRAGA
• NCBI Official Synonym Symbols: FIP1; RAGA; FIP-1
• NCBI Protein Information: ras-related GTP-binding protein A
• UniProt Protein Name: Ras-related GTP-binding protein A
• Protein Family: Ras-related GTP-binding protein
• UniProt Gene Name: RRAGA
• UniProt Synonym Gene Names: RagA
• UniProt Entry Name: RRAGA_HUMAN

Uniprot Description

RRAGA: Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity. Required for the amino acid-induced relocalization of mTORC1 to the lysosomes and its subsequent activation by the GTPase RHEB. This is a crucial step in the activation of the TOR signaling cascade by amino acids. Involved in the RCC1/Ran-GTPase pathway. May play a direct role in a TNF- alpha signaling pathway leading to induction of cell death. May alternatively act as a cellular target for adenovirus E3-14.7K, an inhibitor of TNF-alpha functions, thereby affecting cell death. Can occur as a homodimer, or form a heterodimer with RRAGC or RRAGD in a sequence-independent manner. Binds GTP. The GTP-bound form of RRAGA interacts with NOL8. Interacts with adenovirus E3 14.7 kDa protein. Ubiquitously expressed with highest levels of expression in skeletal muscle, heart, and brain. Belongs to the GTR/RAG GTP-binding protein family.

Protein type: G protein regulator, misc.

Chromosomal Location of Human Ortholog: 9p22.1

Cellular Component: cytoplasm; cytosol; Golgi apparatus; intracellular membrane-bound organelle; lysosomal membrane; lysosome; nucleus

Molecular Function: GTP binding; GTPase activity; phosphoprotein binding; protein binding; protein heterodimerization activity; protein homodimerization activity; ubiquitin protein ligase binding

Biological Process: apoptosis; cell cycle arrest; cell death; cellular response to amino acid starvation; gene expression; insulin receptor signaling pathway; macroautophagy; negative regulation of autophagy; positive regulation of cytolysis; positive regulation of TOR signaling pathway; transcription initiation from RNA polymerase II promoter; virus-host interaction