GNAO1

Guanine nucleotide-binding protein G(o) subunit alpha is a protein that in humans is encoded by the GNAO1 gene.[5][6][7]

GNAO1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3C7K
Identifiers
Aliases	GNAO1, EIEE17, G-ALPHA-o, GNAO, G protein subunit alpha o1, HLA-DQB1, NEDIM
External IDs	OMIM: 139311 MGI: 95775 HomoloGene: 39203 GeneCards: GNAO1
Gene location (Human) Chr. Chromosome 16 (human)[1] Band 16q13 Start 56,191,489 bp[1] End 56,357,444 bp[1]
Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8 C5|8 45.94 cM Start 93,809,966 bp[2] End 93,969,388 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • G-protein beta/gamma-subunit complex binding • signal transducer activity • metal ion binding • guanyl nucleotide binding • GTP binding • GTPase activity • receptor binding • G-protein coupled serotonin receptor binding • mu-type opioid receptor binding • GTPase activating protein binding • GO:0032403 macromolecular complex binding • corticotropin-releasing hormone receptor 1 binding • G-protein coupled receptor binding Cellular component • cell body • membrane • myelin • cell membrane • dendrite • heterotrimeric G-protein complex • neuron projection • macromolecular complex Biological process • G-protein coupled receptor signaling pathway • response to cytokine • muscle contraction • regulation of heart contraction • response to organic cyclic compound • locomotory behavior • adenylate cyclase-modulating G-protein coupled receptor signaling pathway • aging • dopamine receptor signaling pathway • response to morphine • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation of GTPase activity • response to organonitrogen compound • negative regulation of calcium ion transport • forebrain development • neuron projection development • response to hydrogen peroxide • response to drug • cellular process • signal transduction • protein folding • Wnt signaling pathway, calcium modulating pathway • odontogenesis of dentin-containing tooth Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	2775	14681
Ensembl	ENSG00000087258	ENSMUSG00000031748
UniProt	P09471 Q8N6I9	P18872
RefSeq (mRNA)	NM_020988 NM_138736	NM_001113384 NM_010308
RefSeq (protein)	NP_066268 NP_620073 NP_066268.1 NP_620073.2	NP_001106855 NP_034438
Location (UCSC)	Chr 16: 56.19 – 56.36 Mb	Chr 8: 93.81 – 93.97 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Mutations in this gene have been shown to cause epileptic encephalopathy.[8]

Interactions

GNAO1 has been shown to interact with:

• RGS5,[9][10]
• RGS19,[11][12]
• RGS20,[13] and
• RIC8A[14]

References

1. GRCh38: Ensembl release 89: ENSG00000087258 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031748 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Murtagh JJ Jr; Eddy R; Shows TB; Moss J; Vaughan M (Mar 1991). "Different forms of Go alpha mRNA arise by alternative splicing of transcripts from a single gene on human chromosome 16". Mol Cell Biol. 11 (2): 1146–55. doi:10.1128/MCB.11.2.1146. PMC 359797. PMID 1899283.
6. Kinoshita M, Nukada T, Asano T, Mori Y, Akaike A, Satoh M, Kaneko S (Jul 2001). "Binding of G alpha(o) N terminus is responsible for the voltage-resistant inhibition of alpha(1A) (P/Q-type, Ca(v)2.1) Ca(2+) channels". J Biol Chem. 276 (31): 28731–8. doi:10.1074/jbc.M104806200. PMID 11395521.
7. "Entrez Gene: GNAO1 guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O".
8. Nakamura K, Kodera H, Akita T, Shiina M, Kato M, Hoshino H, Terashima H, Osaka H, Nakamura S, Tohyama J, Kumada T, Furukawa T, Iwata S, Shiihara T, Kubota M, Miyatake S, Koshimizu E, Nishiyama K, Nakashima M, Tsurusaki Y, Miyake N, Hayasaka K, Ogata K, Fukuda A, Matsumoto N, Saitsu H (September 2013). "De Novo mutations in GNAO1, encoding a Gαo subunit of heterotrimeric G proteins, cause epileptic encephalopathy". Am. J. Hum. Genet. 93 (3): 496–505. doi:10.1016/j.ajhg.2013.07.014. PMC 3769919. PMID 23993195.
9. Chen C, Zheng B, Han J, Lin SC (1997). "Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast". J. Biol. Chem. 272 (13): 8679–85. doi:10.1074/jbc.272.13.8679. PMID 9079700.
10. Zhou J, Moroi K, Nishiyama M, Usui H, Seki N, Ishida J, Fukamizu A, Kimura S (2001). "Characterization of RGS5 in regulation of G protein-coupled receptor signaling". Life Sci. 68 (13): 1457–69. doi:10.1016/S0024-3205(01)00939-0. PMID 11253162.
11. De Vries L, Elenko E, Hubler L, Jones TL, Farquhar MG (1996). "GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits". Proc. Natl. Acad. Sci. U.S.A. 93 (26): 15203–8. doi:10.1073/pnas.93.26.15203. PMC 26381. PMID 8986788.
12. Woulfe DS, Stadel JM (1999). "Structural basis for the selectivity of the RGS protein, GAIP, for Galphai family members. Identification of a single amino acid determinant for selective interaction of Galphai subunits with GAIP". J. Biol. Chem. 274 (25): 17718–24. doi:10.1074/jbc.274.25.17718. PMID 10364213.
13. Pagano M, Jordan JD, Neves SR, Nguyen T, Iyengar R (2008). "Galphao/i-stimulated proteosomal degradation of RGS20: a mechanism for temporal integration of Gs and Gi pathways". Cell. Signal. 20 (6): 1190–7. doi:10.1016/j.cellsig.2008.02.008. PMC 3107604. PMID 18407463.
14. Tall GG, Krumins AM, Gilman AG (2003). "Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor". J. Biol. Chem. 278 (10): 8356–62. doi:10.1074/jbc.M211862200. PMID 12509430.

Further reading

• Raymond JR, Mukhin YV, Gelasco A, et al. (2002). "Multiplicity of mechanisms of serotonin receptor signal transduction". Pharmacol. Ther. 92 (2–3): 179–212. doi:10.1016/S0163-7258(01)00169-3. PMID 11916537.
• Coupry I, Duzic E, Lanier SM (1992). "Factors determining the specificity of signal transduction by guanine nucleotide-binding protein-coupled receptors. II. Preferential coupling of the alpha 2C-adrenergic receptor to the guanine nucleotide-binding protein, Go". J. Biol. Chem. 267 (14): 9852–7. PMID 1349607.
• Denker BM, Neer EJ, Schmidt CJ (1992). "Mutagenesis of the amino terminus of the alpha subunit of the G protein Go. In vitro characterization of alpha o beta gamma interactions". J. Biol. Chem. 267 (9): 6272–7. PMID 1556134.
• Yi F, Denker BM, Neer EJ (1991). "Structural and functional studies of cross-linked Go protein subunits". J. Biol. Chem. 266 (6): 3900–6. PMID 1899868.
• Tsukamoto T, Toyama R, Itoh H, et al. (1991). "Structure of the human gene and two rat cDNAs encoding the alpha chain of GTP-binding regulatory protein Go: two different mRNAs are generated by alternative splicing". Proc. Natl. Acad. Sci. U.S.A. 88 (8): 2974–8. doi:10.1073/pnas.88.8.2974. PMC 51366. PMID 1901650.
• Gabrion J, Brabet P, Nguyen Than Dao B, et al. (1990). "Ultrastructural localization of the GTP-binding protein Go in neurons". Cell. Signal. 1 (1): 107–23. doi:10.1016/0898-6568(89)90025-9. PMID 2518353.
• Lavu S, Clark J, Swarup R, et al. (1988). "Molecular cloning and DNA sequence analysis of the human guanine nucleotide-binding protein Go alpha". Biochem. Biophys. Res. Commun. 150 (2): 811–5. doi:10.1016/0006-291X(88)90463-9. PMID 3124840.
• Zumbihl R, Breuiller-Fouché M, Carrette J, et al. (1995). "Up-regulation in late pregnancy of both Go1 alpha and Go2 alpha isoforms in human myometrium". Eur. J. Pharmacol. 288 (1): 9–15. doi:10.1016/0922-4106(94)90004-3. PMID 7705473.
• Grassie MA, Milligan G (1995). "Analysis of the relative interactions between the alpha 2C10 adrenoceptor and the guanine-nucleotide-binding proteins G(o)1 alpha and Gi 2 alpha following co-expression of these polypeptides in rat 1 fibroblasts". Biochem. J. 306 (2): 525–30. doi:10.1042/bj3060525. PMC 1136549. PMID 7887906.
• Wu HC, Lin CT (1994). "Association of heterotrimeric GTP binding regulatory protein (Go) with mitosis". Lab. Invest. 71 (2): 175–81. PMID 8078296.
• Nitta K, Uchida K, Kawashima A, et al. (1994). "Identification of GTP-binding proteins in human glomeruli". Nippon Jinzo Gakkai Shi. 36 (1): 9–12. PMID 8107314.
• Georgoussi Z, Carr C, Milligan G (1993). "Direct measurements of in situ interactions of rat brain opioid receptors with the guanine nucleotide-binding protein Go". Mol. Pharmacol. 44 (1): 62–9. PMID 8393523.
• Laugwitz KL, Allgeier A, Offermanns S, et al. (1996). "The human thyrotropin receptor: a heptahelical receptor capable of stimulating members of all four G protein families". Proc. Natl. Acad. Sci. U.S.A. 93 (1): 116–20. doi:10.1073/pnas.93.1.116. PMC 40189. PMID 8552586.
• Kawano N, Ito T, Kitamura H, et al. (1997). "Immunoexpression of the alpha subunit of a guanine nucleotide-binding protein (Go) in pulmonary neuroendocrine cells and neoplasms". Pathol. Int. 46 (6): 393–8. doi:10.1111/j.1440-1827.1996.tb03629.x. PMID 8869990.
• De Vries L, Elenko E, Hubler L, et al. (1997). "GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits". Proc. Natl. Acad. Sci. U.S.A. 93 (26): 15203–8. doi:10.1073/pnas.93.26.15203. PMC 26381. PMID 8986788.
• Valenzuela D, Han X, Mende U, et al. (1997). "G alpha(o) is necessary for muscarinic regulation of Ca2+ channels in mouse heart". Proc. Natl. Acad. Sci. U.S.A. 94 (5): 1727–32. doi:10.1073/pnas.94.5.1727. PMC 19984. PMID 9050846.
• Chen C, Zheng B, Han J, Lin SC (1997). "Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast". J. Biol. Chem. 272 (13): 8679–85. doi:10.1074/jbc.272.13.8679. PMID 9079700.
• Natochin M, Lipkin VM, Artemyev NO (1997). "Interaction of human retinal RGS with G-protein alpha-subunits". FEBS Lett. 411 (2–3): 179–82. doi:10.1016/S0014-5793(97)00687-X. PMID 9271201. S2CID 84269212.
• Busconi L, Denker BM (1998). "Analysis of the N-terminal binding domain of Go alpha". Biochem. J. 328 (1): 23–31. doi:10.1042/bj3280023. PMC 1218882. PMID 9359829.