GNAI2

Identifiers

GNAI2, GIP, GNAI2B, H_LUCA15.1, H_LUCA16.1, G protein subunit alpha i2

External IDs

MGI: 95772 HomoloGene: 55539 GeneCards: GNAI2

Gene ontology
Molecular function	• nucleotide binding • G-protein beta/gamma-subunit complex binding • signal transducer activity • metal ion binding • protein binding • GTPase activity • guanyl nucleotide binding • G-protein coupled receptor binding • GTP binding
Cellular component	• cytoplasm • cell body • extracellular vesicle • cytosol • centrosome • membrane • plasma membrane • nucleoplasm • microtubule organizing center • dendrite • midbody • heterotrimeric G-protein complex • membrane raft • extracellular exosome • cytoskeleton • nucleus
Biological process	• gamma-aminobutyric acid signaling pathway • G-protein coupled acetylcholine receptor signaling pathway • G-protein coupled receptor signaling pathway • adenosine receptor signaling pathway • negative regulation of adenylate cyclase activity • intracellular signal transduction • regulation of calcium ion transport • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway • response to nutrient • activation of MAPKK activity • adenylate cyclase-modulating G-protein coupled receptor signaling pathway • negative regulation of synaptic transmission • cell division • positive regulation of cell proliferation • cell cycle • cell proliferation • signal transduction • protein folding
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


2771


14678

Ensembl


ENSG00000114353


ENSMUSG00000032562

UniProt


P04899


P08752

RefSeq (mRNA)

NM_002070 NM_001166425 NM_001282617 NM_001282618 NM_001282619
NM_001282620


NM_008138

RefSeq (protein)

NP_001159897.1 NP_001269546.1 NP_001269547.1 NP_001269548.1 NP_001269549.1
NP_002061.1


NP_032164.2

Location (UCSC)

Chr 3: 50.23 – 50.26 Mb

Chr 9: 107.61 – 107.64 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Guanine nucleotide-binding protein G(i), alpha-2 subunit is a protein that in humans is encoded by the GNAI2 gene.^[3]^[4]^[5]

Interactions

GNAI2 has been shown to interact with:

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Didsbury JR, Ho YS, Snyderman R (Jan 1987). "Human Gi protein alpha-subunit: deduction of amino acid structure from a cloned cDNA". FEBS Letters. 211 (2): 160–4. doi:10.1016/0014-5793(87)81428-X. PMID 3100330.
↑ Magovcevic I, Ang SL, Seidman JG, Tolman CJ, Neer EJ, Morton CC (Jan 1992). "Regional localization of the human G protein alpha i2 (GNAI2) gene: assignment to 3p21 and a related sequence (GNAI2L) to 12p12-p13". Genomics. 12 (1): 125–9. doi:10.1016/0888-7543(92)90414-N. PMID 1733849.
↑ "Entrez Gene: GNAI2 Guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 2".
↑ Fan X, Brass LF, Poncz M, Spitz F, Maire P, Manning DR (Oct 2000). "The alpha subunits of Gz and Gi interact with the eyes absent transcription cofactor Eya2, preventing its interaction with the six class of homeodomain-containing proteins". The Journal of Biological Chemistry. 275 (41): 32129–34. doi:10.1074/jbc.M004577200. PMID 10906137.
↑ Marty C, Browning DD, Ye RD (Jun 2003). "Identification of tetratricopeptide repeat 1 as an adaptor protein that interacts with heterotrimeric G proteins and the small GTPase Ras". Molecular and Cellular Biology. 23 (11): 3847–58. doi:10.1128/mcb.23.11.3847-3858.2003. PMC 155206. PMID 12748287.
↑ Mochizuki N, Cho G, Wen B, Insel PA (Nov 1996). "Identification and cDNA cloning of a novel human mosaic protein, LGN, based on interaction with G alpha i2". Gene. 181 (1-2): 39–43. doi:10.1016/s0378-1119(96)00456-8. PMID 8973305.
↑ Damaj BB, McColl SR, Neote K, Songqing N, Ogborn KT, Hébert CA, Naccache PH (Oct 1996). "Identification of G-protein binding sites of the human interleukin-8 receptors by functional mapping of the intracellular loops". FASEB Journal. 10 (12): 1426–34. PMID 8903513.
↑ Damaj BB, McColl SR, Mahana W, Crouch MF, Naccache PH (May 1996). "Physical association of Gi2alpha with interleukin-8 receptors". The Journal of Biological Chemistry. 271 (22): 12783–9. doi:10.1074/jbc.271.22.12783. PMID 8662698.
↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
↑ Chen C, Zheng B, Han J, Lin SC (Mar 1997). "Characterization of a novel mammalian RGS protein that binds to Galpha proteins and inhibits pheromone signaling in yeast". The Journal of Biological Chemistry. 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 (Feb 2001). "Characterization of RGS5 in regulation of G protein-coupled receptor signaling". Life Sciences. 68 (13): 1457–69. doi:10.1016/s0024-3205(01)00939-0. PMID 11253162.
↑ Tall GG, Krumins AM, Gilman AG (Mar 2003). "Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor". The Journal of Biological Chemistry. 278 (10): 8356–62. doi:10.1074/jbc.M211862200. PMID 12509430.

Sidhu A, Niznik HB (Nov 2000). "Coupling of dopamine receptor subtypes to multiple and diverse G proteins". International Journal of Developmental Neuroscience. 18 (7): 669–77. doi:10.1016/S0736-5748(00)00033-2. PMID 10978845.
Offermanns S, Schultz G, Rosenthal W (Feb 1991). "Evidence for opioid receptor-mediated activation of the G-proteins, Go and Gi2, in membranes of neuroblastoma x glioma (NG108-15) hybrid cells". The Journal of Biological Chemistry. 266 (6): 3365–8. PMID 1671672.
Cormont M, Le Marchand-Brustel Y, Van Obberghen E, Spiegel AM, Sharp GW (Sep 1991). "Identification of G protein alpha-subunits in RINm5F cells and their selective interaction with galanin receptor". Diabetes. 40 (9): 1170–6. doi:10.2337/diabetes.40.9.1170. PMID 1718802.
Bushfield M, Murphy GJ, Lavan BE, Parker PJ, Hruby VJ, Milligan G, Houslay MD (Jun 1990). "Hormonal regulation of Gi2 alpha-subunit phosphorylation in intact hepatocytes". The Biochemical Journal. 268 (2): 449–57. PMC 1131453. PMID 2114093.
Lyons J, Landis CA, Harsh G, Vallar L, Grünewald K, Feichtinger H, Duh QY, Clark OH, Kawasaki E, Bourne HR (Aug 1990). "Two G protein oncogenes in human endocrine tumors". Science. 249 (4969): 655–9. doi:10.1126/science.2116665. PMID 2116665.
Osawa S, Dhanasekaran N, Woon CW, Johnson GL (Nov 1990). "G alpha i-G alpha s chimeras define the function of alpha chain domains in control of G protein activation and beta gamma subunit complex interactions". Cell. 63 (4): 697–706. doi:10.1016/0092-8674(90)90136-3. PMID 2121366.
McClue SJ, Milligan G (Sep 1990). "The alpha 2B adrenergic receptor of undifferentiated neuroblastoma x glioma hybrid NG108-15 cells, interacts directly with the guanine nucleotide binding protein, Gi2". FEBS Letters. 269 (2): 430–4. doi:10.1016/0014-5793(90)81209-7. PMID 2169434.
Rudolph U, Koesling D, Hinsch KD, Seifert R, Bigalke M, Schultz G, Rosenthal W (May 1989). "G-protein alpha-subunits in cytosolic and membranous fractions of human neutrophils". Molecular and Cellular Endocrinology. 63 (1-2): 143–53. doi:10.1016/0303-7207(89)90090-7. PMID 2502457.
Lang JC, Costa T (1990). "Distribution of the alpha-subunit of the guanine nucleotide-binding protein Gi2 and its comparison to G alpha o". Journal of Receptor Research. 9 (4-5): 313–29. PMID 2512386.
Itoh H, Toyama R, Kozasa T, Tsukamoto T, Matsuoka M, Kaziro Y (May 1988). "Presence of three distinct molecular species of Gi protein alpha subunit. Structure of rat cDNAs and human genomic DNAs". The Journal of Biological Chemistry. 263 (14): 6656–64. PMID 2834384.
Weinstein LS, Spiegel AM, Carter AD (May 1988). "Cloning and characterization of the human gene for the alpha-subunit of Gi2, a GTP-binding signal transduction protein". FEBS Letters. 232 (2): 333–40. doi:10.1016/0014-5793(88)80764-6. PMID 2837412.
Beals CR, Wilson CB, Perlmutter RM (Nov 1987). "A small multigene family encodes Gi signal-transduction proteins". Proceedings of the National Academy of Sciences of the United States of America. 84 (22): 7886–90. doi:10.1073/pnas.84.22.7886. PMC 299440. PMID 3120178.
Williamson EA, Ince PG, Harrison D, Kendall-Taylor P, Harris PE (Feb 1995). "G-protein mutations in human pituitary adrenocorticotrophic hormone-secreting adenomas". European Journal of Clinical Investigation. 25 (2): 128–31. doi:10.1111/j.1365-2362.1995.tb01537.x. PMID 7737262.
Takigawa M, Sakurai T, Kasuya Y, Abe Y, Masaki T, Goto K (Feb 1995). "Molecular identification of guanine-nucleotide-binding regulatory proteins which couple to endothelin receptors". European Journal of Biochemistry / FEBS. 228 (1): 102–8. doi:10.1111/j.1432-1033.1995.tb20236.x. PMID 7882989.
Grassie MA, Milligan G (Mar 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". The Biochemical Journal. 306 (2): 525–30. doi:10.1042/bj3060525. PMC 1136549. PMID 7887906.
Migeon JC, Thomas SL, Nathanson NM (Nov 1994). "Regulation of cAMP-mediated gene transcription by wild type and mutated G-protein alpha subunits. Inhibition of adenylyl cyclase activity by muscarinic receptor-activated and constitutively activated G(o) alpha". The Journal of Biological Chemistry. 269 (46): 29146–52. PMID 7961880.
Wennogle LP, Conder L, Winter C, Braunwalder A, Vlattas S, Kramer R, Cioffi C, Hu SI (Jul 1994). "Stabilization of C5a receptor--G-protein interactions through ligand binding". Journal of Cellular Biochemistry. 55 (3): 380–8. doi:10.1002/jcb.240550316. PMID 7962171.
Valet P, Senard JM, Devedjian JC, Planat V, Salomon R, Voisin T, Drean G, Couvineau A, Daviaud D, Denis C (May 1993). "Characterization and distribution of alpha 2-adrenergic receptors in the human intestinal mucosa". The Journal of Clinical Investigation. 91 (5): 2049–57. doi:10.1172/JCI116427. PMC 288203. PMID 8098045.

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

both	Dual-specificity kinase

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

Hydrolases: acid anhydride hydrolases (EC 3.6)

3.6.1

3.6.2

3.6.3-4: ATPase

3.6.3

Cu++ (3.6.3.4)	Menkes/ATP7A Wilson/ATP7B

Ca+ (3.6.3.8)	SERCA ATP2A1 ATP2A2 ATP2A3 Plasma membrane ATP2B1 ATP2B2 ATP2B3 ATP2B4 SPCA ATP2C1 ATP2C2

Na+/K+ (3.6.3.9)	ATP1A1 ATP1A2 ATP1A3 ATP1A4 ATP1B1 ATP1B2 ATP1B3 ATP1B4

H+/K+ (3.6.3.10)	ATP4A

Other P-type ATPase	ATP8B1 ATP10A ATP11B ATP12A ATP13A2 ATP13A3

3.6.4

3.6.5: GTPase

3.6.5.1: Heterotrimeric G protein	G_αs G_αi GNAI1 GNAI2 GNAI3 G_αq/11 GNAQ GNA11 G_α12/13 GNA12 GNA13 Transducin GNAT1 GNAT2 Gustducin GNAT3

3.6.5.2: Small GTPase > Ras superfamily	Rho family of GTPases: Cdc42 CDC42 TC10 TCL RhoUV RhoU RhoV Rac Rac1 2 3 RhoG RhoBTB 1 2 RhoH Rho A B C Rnd 1 2 3 RhoDF RhoF RhoD other: Ras HRAS KRAS NRAS Rab RAB23 RAB27 Arf ARF6 SAR1B ARL13B ARL6 Ran Rheb Rap RGK

3.6.5.3: Protein-synthesizing GTPase	Prokaryotic IF-2 EF-Tu EF-G Eukaryotic

3.6.5.5-6: Polymerization motors	Dynamin Tubulin

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GNAI2

Interactions

References

Further reading