GNAO1

GNAO1

Available structures

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, DEE17, HG1G

External IDs

OMIM: 139311 MGI: 95775 HomoloGene: 39203 GeneCards: GNAO1

Gene location (Human)

Chr.	Chromosome 16 (human)^[1]

Band	16q13	Start	56,191,390 bp^[1]
Band	16q13	End	56,357,444 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 8 (mouse)^[2]

Band	8 C5\|8 45.94 cM	Start	94,536,594 bp^[2]
Band	8 C5\|8 45.94 cM	End	94,696,016 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

superficial temporal artery

entorhinal cortex

superior frontal gyrus

prefrontal cortex

putamen

postcentral gyrus

caudate nucleus

nucleus accumbens

Brodmann area 9

amygdala

Top expressed in

entorhinal cortex

superior frontal gyrus

habenula

cerebellar cortex

subiculum

olfactory tubercle

primary motor cortex

superior colliculus

inferior colliculus

dorsomedial hypothalamic nucleus

More reference expression data

BioGPS


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 signaling receptor binding G protein-coupled serotonin receptor binding mu-type opioid receptor binding GTPase activating protein binding protein-containing complex binding corticotropin-releasing hormone receptor 1 binding G protein-coupled receptor binding
Cellular component	cell body membrane myelin sheath plasma membrane dendrite heterotrimeric G-protein complex neuron projection protein-containing 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 human ageing dopamine receptor signaling pathway response to morphine positive regulation of GTPase activity response to organonitrogen compound negative regulation of calcium ion transport forebrain development neuron projection development response to hydrogen peroxide 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: 94.54 – 94.7 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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

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

YouTube Encyclopedic

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Transcription

Interactions

GNAO1 has been shown to interact with:

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000087258 - Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000031748 - 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.
^ 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.
^ 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.
^ "Entrez Gene: GNAO1 guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O".
^ 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.
^ 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.
^ 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.
^ 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. Bibcode:1996PNAS...9315203D. doi:10.1073/pnas.93.26.15203. PMC 26381. PMID 8986788.
^ 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.
^ 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.
^ 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.

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. doi:10.1016/S0021-9258(19)50172-7. 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. doi:10.1016/S0021-9258(18)42691-9. 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. doi:10.1016/S0021-9258(19)67879-8. 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. Bibcode:1991PNAS...88.2974T. 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. Bibcode:1996PNAS...93..116L. 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. S2CID 35816963.
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. Bibcode:1996PNAS...9315203D. 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. Bibcode:1997PNAS...94.1727V. 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.

Intracellular signaling peptides and proteins

MAP

see MAP kinase pathway

Calcium

G protein

Heterotrimeric

cAMP:	Heterotrimeric G protein Gs/Gi Adenylate cyclase cAMP 3',5'-cyclic-AMP phosphodiesterase Protein kinase A
cGMP:	Transducin Gustducin Guanylate cyclase cGMP 3',5'-cyclic-GMP phosphodiesterase Protein kinase G
G alpha subunit G_α GNAO1 GNAI1 GNAI2 GNAI3 GNAT1 GNAT2 GNAT3 GNAZ GNAS GNAL GNAQ GNA11 GNA12 GNA13 GNA14 GNA15/GNA16
G beta-gamma complex G_β GNB1 GNB2 GNB3 GNB4 GNB5 G_γ GNGT1 GNGT2 GNG2 GNG3 GNG4 GNG5 GNG7 GNG8 GNG10 GNG11 GNG12 GNG13 BSCL2
G protein-coupled receptor kinase AMP-activated protein kinase

Monomeric

Cyclin

Lipid

Other protein kinase

Serine/threonine:	Casein kinase 1 2 eIF-2 kinase EIF2AK3 Glycogen synthase kinase GSK1 GSK2 GSK-3 GSK3A GSK3B IκB kinase CHUK IKK2 IKBKG Interleukin-1 receptor associated kinase IRAK1 IRAK2 IRAK3 IRAK4 Lim kinase LIMK1 LIMK2 p21-activated kinases PAK1 PAK2 PAK3 PAK4 Rho-associated protein kinase ROCK1 ROCK2 Ribosomal s6 kinase RPS6KA1
Tyrosine:	ZAP70 Focal adhesion protein-tyrosine kinase PTK2 PTK2B BTK
Serine/threonine/tyrosine	Dual-specificity kinase DYRK1A DYRK1B DYRK2 DYRK3 DYRK4
Arginine	Arginine kinase McsB

Other protein phosphatase

Serine/threonine:	Protein phosphatase 2
Tyrosine:	protein tyrosine phosphatase: Receptor-like protein tyrosine phosphatase Sh2 domain-containing protein tyrosine phosphatase
both:	Dual-specificity phosphatase

Apoptosis

see apoptosis signaling pathway

GTP-binding protein regulators

see GTP-binding protein regulators

Other

see also deficiencies of intracellular signaling peptides and proteins

This article on a gene on human chromosome 16 is a stub. You can help Wikipedia by expanding it.

This page was last edited on 8 November 2023, at 23:29

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Transcription

Interactions

References

Further reading