ID GNAI1_HUMAN Reviewed; 354 AA. AC P63096; A8KA88; B4E2V1; C9J3A4; P04898; P11015; P31871; Q5U074; Q8TAN5; AC Q9UGA4; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 195. DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-1; DE AltName: Full=Adenylate cyclase-inhibiting G alpha protein; GN Name=GNAI1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101. RX PubMed=2834384; DOI=10.1016/s0021-9258(18)68692-2; RA Itoh H., Toyama R., Kozasa T., Tsukamoto T., Matsuoka M., Kaziro Y.; RT "Presence of three distinct molecular species of Gi protein alpha subunit. RT Structure of rat cDNAs and human genomic DNAs."; RL J. Biol. Chem. 263:6656-6664(1988). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-354. RX PubMed=3110783; DOI=10.1073/pnas.84.15.5115; RA Bray P., Carter A., Guo V., Puckett C., Kamholz J., Spiegel A., RA Nirenberg M.; RT "Human cDNA clones for an alpha subunit of Gi signal-transduction RT protein."; RL Proc. Natl. Acad. Sci. U.S.A. 84:5115-5119(1987). RN [11] RP PROTEIN SEQUENCE OF 91-100 AND 162-176. RC TISSUE=Adipocyte; RX PubMed=15242332; DOI=10.1042/bj20040647; RA Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.; RT "Vectorial proteomics reveal targeting, phosphorylation and specific RT fragmentation of polymerase I and transcript release factor (PTRF) at the RT surface of caveolae in human adipocytes."; RL Biochem. J. 383:237-248(2004). RN [12] RP FUNCTION, AND INTERACTION WITH RGS10. RX PubMed=8774883; DOI=10.1038/383175a0; RA Hunt T.W., Fields T.A., Casey P.J., Peralta E.G.; RT "RGS10 is a selective activator of G alpha i GTPase activity."; RL Nature 383:175-177(1996). RN [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17635935; DOI=10.1083/jcb.200604114; RA Cho H., Kehrl J.H.; RT "Localization of Gi alpha proteins in the centrosomes and at the midbody: RT implication for their role in cell division."; RL J. Cell Biol. 178:245-255(2007). RN [14] RP INTERACTION WITH CCDC88A. RX PubMed=19211784; DOI=10.1073/pnas.0900294106; RA Garcia-Marcos M., Ghosh P., Farquhar M.G.; RT "GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates RT Akt signaling."; RL Proc. Natl. Acad. Sci. U.S.A. 106:3178-3183(2009). RN [15] RP MYRISTOYLATION AT GLY-2. RX PubMed=20213681; DOI=10.1002/pmic.200900783; RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., RA Tsunasawa S., Utsumi T.; RT "Strategy for comprehensive identification of human N-myristoylated RT proteins using an insect cell-free protein synthesis system."; RL Proteomics 10:1780-1793(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22327364; DOI=10.1038/ncb2440; RA Kiyomitsu T., Cheeseman I.M.; RT "Chromosome- and spindle-pole-derived signals generate an intrinsic code RT for spindle position and orientation."; RL Nat. Cell Biol. 14:311-317(2012). RN [18] RP DEAMIDATION AT GLN-204 (MICROBIAL INFECTION). RX PubMed=24141704; DOI=10.1038/nsmb.2688; RA Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E., RA Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C., RA Aktories K.; RT "A bacterial toxin catalyzing tyrosine glycosylation of Rho and deamidation RT of Gq and Gi proteins."; RL Nat. Struct. Mol. Biol. 20:1273-1280(2013). RN [19] RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=25255805; DOI=10.1038/ncomms5919; RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H., RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.; RT "Global profiling of co- and post-translationally N-myristoylated proteomes RT in human cells."; RL Nat. Commun. 5:4919-4919(2014). RN [20] RP INTERACTION WITH CCDC88C. RX PubMed=26126266; DOI=10.7554/elife.07091; RA Aznar N., Midde K.K., Dunkel Y., Lopez-Sanchez I., Pavlova Y., Marivin A., RA Barbazan J., Murray F., Nitsche U., Janssen K.P., Willert K., Goel A., RA Abal M., Garcia-Marcos M., Ghosh P.; RT "Daple is a novel non-receptor GEF required for trimeric G protein RT activation in Wnt signaling."; RL Elife 4:E07091-E07091(2015). RN [21] RP IDENTIFICATION IN A SPINDLE ORIENTATION COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=26766442; DOI=10.1016/j.devcel.2015.12.016; RA Chiu C.W., Monat C., Robitaille M., Lacomme M., Daulat A.M., Macleod G., RA McNeill H., Cayouette M., Angers S.; RT "SAPCD2 controls spindle orientation and asymmetric divisions by negatively RT regulating the Galphai-LGN-NuMA ternary complex."; RL Dev. Cell 36:50-62(2016). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-349 IN COMPLEX WITH RGS14 AND RP GDP, AND INTERACTION WITH RGS14. RX PubMed=11976690; DOI=10.1038/416878a; RA Kimple R.J., Kimple M.E., Betts L., Sondek J., Siderovski D.P.; RT "Structural determinants for GoLoco-induced inhibition of nucleotide RT release by Galpha subunits."; RL Nature 416:878-881(2002). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 26-354 IN COMPLEX WITH GDP. RX PubMed=16004878; DOI=10.1016/j.str.2005.04.007; RA Johnston C.A., Willard F.S., Jezyk M.R., Fredericks Z., Bodor E.T., RA Jones M.B., Blaesius R., Watts V.J., Harden T.K., Sondek J., Ramer J.K., RA Siderovski D.P.; RT "Structure of Galpha(i1) bound to a GDP-selective peptide provides insight RT into guanine nucleotide exchange."; RL Structure 13:1069-1080(2005). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 31-354, AND MUTAGENESIS OF GLU-116 RP AND GLN-147. RX PubMed=17603074; DOI=10.1016/j.jmb.2007.05.096; RA Sammond D.W., Eletr Z.M., Purbeck C., Kimple R.J., Siderovski D.P., RA Kuhlman B.; RT "Structure-based protocol for identifying mutations that enhance protein- RT protein binding affinities."; RL J. Mol. Biol. 371:1392-1404(2007). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND RETRACTED PAPER. RX PubMed=17264214; DOI=10.1073/pnas.0608599104; RA Johnston C.A., Siderovski D.P.; RT "Structural basis for nucleotide exchange on G alpha i subunits and RT receptor coupling specificity."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2001-2006(2007). RN [26] RP ERRATUM OF PUBMED:17264214, AND RETRACTION NOTICE OF PUBMED:17264214. RX PubMed=22408789; DOI=10.1073/pnas.1200173109; RA Johnston C.A., Siderovski D.P.; RL Proc. Natl. Acad. Sci. U.S.A. 109:1808-1808(2012). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 32-354 IN COMPLEX WITH RGS1; RP RGS16; GDP; MAGNESIUM AND TRANSITION STATE ANALOG, FUNCTION, INTERACTION RP WITH GNB1; GNG2; RGS1; RGS3; RGS4; RGS6; RGS7; RGS8; RGS10; RGS12; RGS14; RP RGS16; RGS17; RGS18 AND RGS20, AND SUBUNIT. RX PubMed=18434541; DOI=10.1073/pnas.0801508105; RA Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J., RA Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A., RA Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P.; RT "Structural diversity in the RGS domain and its interaction with RT heterotrimeric G protein alpha-subunits."; RL Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 31-354 IN COMPLEX WITH RGS14 AND RP GDP, AND MUTAGENESIS OF GLU-116; GLN-147 AND GLU-245. RX PubMed=21115486; DOI=10.1074/jbc.m110.190496; RA Bosch D.E., Kimple A.J., Sammond D.W., Muller R.E., Miley M.J., Machius M., RA Kuhlman B., Willard F.S., Siderovski D.P.; RT "Structural determinants of affinity enhancement between GoLoco motifs and RT G-protein alpha subunit mutants."; RL J. Biol. Chem. 286:3351-3358(2011). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 25-354 IN COMPLEX WITH GPSM2 AND RP GDP, AND INTERACTION WITH GPSM2. RX PubMed=22952234; DOI=10.1074/jbc.m112.391607; RA Jia M., Li J., Zhu J., Wen W., Zhang M., Wang W.; RT "Crystal structures of the scaffolding protein LGN reveal the general RT mechanism by which GoLoco binding motifs inhibit the release of GDP from RT Galphai."; RL J. Biol. Chem. 287:36766-36776(2012). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 31-354 IN COMPLEX WITH GDP AND RP MAGNESIUM, SUBUNIT, INTERACTION WITH GNB1; GNG1 AND RGS14, AND MUTAGENESIS RP OF GLY-42. RX PubMed=22383884; DOI=10.1371/journal.ppat.1002553; RA Bosch D.E., Willard F.S., Ramanujam R., Kimple A.J., Willard M.D., RA Naqvi N.I., Siderovski D.P.; RT "A P-loop mutation in Galpha subunits prevents transition to the active RT state: implications for G-protein signaling in fungal pathogenesis."; RL PLoS Pathog. 8:E1002553-E1002553(2012). RN [31] RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 2-354 IN COMPLEX WITH RP GNB1; GNG2 AND HHV-5 US27, INTERACTION WITH HHV-5 US27 (MICROBIAL RP INFECTION), STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) IN COMPLEX RP WITH HOST GNB1; CX3CL1; GNG2 AND HHV-5 US28, AND INTERACTION WITH HHV-5 RP US28 (MICROBIAL INFECTION). RX PubMed=35061538; DOI=10.1126/sciadv.abl5442; RA Tsutsumi N., Maeda S., Qu Q., Voegele M., Jude K.M., Suomivuori C.M., RA Panova O., Waghray D., Kato H.E., Velasco A., Dror R.O., Skiniotis G., RA Kobilka B.K., Garcia K.C.; RT "Atypical structural snapshots of human cytomegalovirus GPCR interactions RT with host G proteins."; RL Sci. Adv. 8:eabl5442-eabl5442(2022). RN [32] {ECO:0007744|PDB:7EJX, ECO:0007744|PDB:7WZ4} RP STRUCTURE BY ELECTRON MICROSCOPY (2.40 ANGSTROMS) IN COMPLEX WITH GPR88; RP GNB1; GNG2; GI-STABILIZING ANTIBODY SCFV16 AND SYNTHETIC AGONIST 2-PCCA. RX PubMed=35501348; DOI=10.1038/s41467-022-30081-5; RA Chen G., Xu J., Inoue A., Schmidt M.F., Bai C., Lu Q., Gmeiner P., Liu Z., RA Du Y.; RT "Activation and allosteric regulation of the orphan GPR88-Gi1 signaling RT complex."; RL Nat. Commun. 13:2375-2375(2022). RN [33] RP CHARACTERIZATION OF VARIANT NEDHISB PRO-52. RX PubMed=34685729; DOI=10.3390/cells10102749; RA Solis G.P., Kozhanova T.V., Koval A., Zhilina S.S., Mescheryakova T.I., RA Abramov A.A., Ishmuratov E.V., Bolshakova E.S., Osipova K.V., RA Ayvazyan S.O., Lebon S., Kanivets I.V., Pyankov D.V., Troccaz S., RA Silachev D.N., Zavadenko N.N., Prityko A.G., Katanaev V.L.; RT "Pediatric Encephalopathy: Clinical, Biochemical and Cellular Insights into RT the Role of Gln52 of GNAO1 and GNAI1 for the Dominant Disease."; RL Cells 10:0-0(2021). RN [34] RP VARIANTS NEDHISB ARG-40; CYS-40; ASP-45; ILE-48; LYS-48; PRO-52; SER-75 RP DEL; GLN-172 DEL; VAL-173; 186-GLU--PHE-189 DEL; TYR-224; ARG-270; ASN-270; RP PRO-326 AND GLU-332, AND INVOLVEMENT IN NEDHISB. RX PubMed=33473207; DOI=10.1038/s41436-020-01076-8; RA Muir A.M., Gardner J.F., van Jaarsveld R.H., de Lange I.M., RA van der Smagt J.J., Wilson G.N., Dubbs H., Goldberg E.M., Zitano L., RA Bupp C., Martinez J., Srour M., Accogli A., Alhakeem A., Meltzer M., RA Gropman A., Brewer C., Caswell R.C., Montgomery T., McKenna C., McKee S., RA Powell C., Vasudevan P.C., Brady A.F., Joss S., Tysoe C., Noh G., RA Tarnopolsky M., Brady L., Zafar M., Schrier Vergano S.A., Murray B., RA Sawyer L., Hainline B.E., Sapp K., DeMarzo D., Huismann D.J., RA Wentzensen I.M., Schnur R.E., Monaghan K.G., Juusola J., Rhodes L., RA Dobyns W.B., Lecoquierre F., Goldenberg A., Polster T., Axer-Schaefer S., RA Platzer K., Kloeckner C., Hoffman T.L., MacArthur D.G., O'Leary M.C., RA VanNoy G.E., England E., Varghese V.C., Mefford H.C.; RT "Variants in GNAI1 cause a syndrome associated with variable features RT including developmental delay, seizures, and hypotonia."; RL Genet. Med. 23:881-887(2021). RN [35] RP VARIANT NEDHISB GLY-272, AND INVOLVEMENT IN NEDHISB. RX PubMed=34819662; DOI=10.1038/s10038-021-00988-w; RA Wayhelova M., Vallova V., Broz P., Mikulasova A., Loubalova D., Filkova H., RA Smetana J., Drabova K., Gaillyova R., Kuglik P.; RT "Novel de novo pathogenic variant in the GNAI1 gene as a cause of severe RT disorders of intellectual development."; RL J. Hum. Genet. 67:209-214(2022). CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as CC transducers downstream of G protein-coupled receptors (GPCRs) in CC numerous signaling cascades. The alpha chain contains the guanine CC nucleotide binding site and alternates between an active, GTP-bound CC state and an inactive, GDP-bound state. Signaling by an activated GPCR CC promotes GDP release and GTP binding. The alpha subunit has a low CC GTPase activity that converts bound GTP to GDP, thereby terminating the CC signal. Both GDP release and GTP hydrolysis are modulated by numerous CC regulatory proteins (PubMed:8774883, PubMed:18434541). Signaling is CC mediated via effector proteins, such as adenylate cyclase. Inhibits CC adenylate cyclase activity, leading to decreased intracellular cAMP CC levels (By similarity). The inactive GDP-bound form prevents the CC association of RGS14 with centrosomes and is required for the CC translocation of RGS14 from the cytoplasm to the plasma membrane. CC Required for normal cytokinesis during mitosis (PubMed:17635935). CC Required for cortical dynein-dynactin complex recruitment during CC metaphase (PubMed:22327364). {ECO:0000250|UniProtKB:P10824, CC ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:18434541, CC ECO:0000269|PubMed:22327364, ECO:0000269|PubMed:8774883}. CC -!- SUBUNIT: Heterotrimeric G proteins are composed of 3 units; alpha, beta CC and gamma. Part of a spindle orientation complex at least composed of CC GNAI1, GPSM2 and NUMA1 (PubMed:26766442). The alpha chain contains the CC guanine nucleotide binding site. Identified in complex with the beta CC subunit GNB1 and the gamma subunit GNG1 (PubMed:22383884). Identified CC in complex with the beta subunit GNB1 and the gamma subunit GNG2 CC (PubMed:18434541). GTP binding causes dissociation of the heterotrimer, CC liberating the individual subunits so that they can interact with CC downstream effector proteins (PubMed:22383884). Interacts (GDP-bound CC form) with GPSM1; this inhibits guanine nucleotide exchange and GTP CC binding (By similarity). Interacts (GDP-bound form) with GPSM2 (via CC GoLoco domains); this inhibits guanine nucleotide exchange CC (PubMed:22952234). Interacts with RGS10; this strongly enhances GTP CC hydrolysis (PubMed:8774883, PubMed:18434541). Interacts with RGS1 and CC RGS16; this strongly enhances GTPase activity (PubMed:18434541). CC Interacts with RGS4 (PubMed:18434541). Interacts with RGS12 CC (PubMed:18434541). Interacts (via active GTP- or inactive GDP-bound CC forms) with RGS14 (via RGS and GoLoco domains) (PubMed:11976690, CC PubMed:18434541, PubMed:21115486, PubMed:22383884). Interacts with CC RGS3, RGS6, RGS7, RGS8, RGS17, RGS18 and RGS20 (in vitro) CC (PubMed:18434541). Interacts (GDP-bound form) with RIC8A (via C- CC terminus) (By similarity). Interacts (inactive GDP-bound form) with CC NUCB1 (via GBA motif); the interaction leads to activation of GNAI1 (By CC similarity). Interacts (inactive GDP-bound form) with CCDC88C/DAPLE CC (via GBA motif); the interaction leads to activation of GNAI1 CC (PubMed:26126266). Interacts (inactive GDP-bound form) with CCDC8A/GIV CC (via GBA motif) (PubMed:19211784). {ECO:0000250|UniProtKB:P10824, CC ECO:0000269|PubMed:11976690, ECO:0000269|PubMed:16004878, CC ECO:0000269|PubMed:17264214, ECO:0000269|PubMed:18434541, CC ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:21115486, CC ECO:0000269|PubMed:22383884, ECO:0000269|PubMed:22952234, CC ECO:0000269|PubMed:26126266, ECO:0000269|PubMed:26766442, CC ECO:0000269|PubMed:8774883}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC (HHV-5) US27; this interaction this interaction does not lead to the CC catalytic activation of Gi complex and probably interferes with the CC chemokine-Gi signaling. {ECO:0000269|PubMed:35061538}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC (HHV-5) US28; this interaction does not lead to the catalytic CC activation of Gi complex and probably interferes with the chemokine-Gi CC signaling. {ECO:0000269|PubMed:35061538}. CC -!- INTERACTION: CC P63096; P81274: GPSM2; NbExp=3; IntAct=EBI-618639, EBI-618655; CC P63096; Q9Y4H4: GPSM3; NbExp=8; IntAct=EBI-618639, EBI-347538; CC P63096; Q14980: NUMA1; NbExp=4; IntAct=EBI-618639, EBI-521611; CC P63096; Q8IVA1: PCP2; NbExp=6; IntAct=EBI-618639, EBI-12250122; CC P63096; Q9UGC6: RGS17; NbExp=3; IntAct=EBI-618639, EBI-3918154; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10824}. Cytoplasm CC {ECO:0000269|PubMed:17635935}. Cell membrane CC {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:26766442}; Peripheral CC membrane protein {ECO:0000250|UniProtKB:P10824}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P10824}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:17635935}. Cytoplasm, CC cell cortex {ECO:0000269|PubMed:22327364}. Membrane CC {ECO:0000250|UniProtKB:P10824}; Lipid-anchor CC {ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805}. CC Note=Localizes in the centrosomes of interphase and mitotic cells, but CC not in centrosomes during cytokinesis. Detected at the cleavage furrow CC or the midbody (PubMed:17635935). Localized at the plasma membrane CC throughout mitosis. Colocalizes with RIC8A and RGS14 at the plasma CC membrane. {ECO:0000250|UniProtKB:P10824, ECO:0000269|PubMed:17635935}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P63096-1; Sequence=Displayed; CC Name=2; CC IsoId=P63096-2; Sequence=VSP_045215; CC -!- PTM: Myristoylation at Gly-2 is required for membrane anchoring before CC palmitoylation. {ECO:0000250|UniProtKB:P10824}. CC -!- PTM: Palmitoylation at Cys-3 varies with membrane lipid composition. CC {ECO:0000250|UniProtKB:P10824}. CC -!- PTM: (Microbial infection) Deamidated at Gln-204 by Photorhabdus CC asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric CC GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby CC activating RhoA. {ECO:0000269|PubMed:24141704}. CC -!- DISEASE: Neurodevelopmental disorder with hypotonia, impaired speech, CC and behavioral abnormalities (NEDHISB) [MIM:619854]: An autosomal CC dominant disorder characterized by global developmental delay, impaired CC intellectual development, delayed or absent speech, hypotonia, CC behavioral abnormalities, and epilepsy that ranges from self-limiting CC to intractable. More variable features include non-specific dysmorphic CC facial features, distal skeletal anomalies, and brain imaging CC abnormalities. {ECO:0000269|PubMed:33473207, CC ECO:0000269|PubMed:34685729, ECO:0000269|PubMed:34819662}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF493905; AAM12619.1; -; mRNA. DR EMBL; AF055013; AAC09361.1; -; mRNA. DR EMBL; AL049933; CAB43212.2; -; mRNA. DR EMBL; BT019775; AAV38580.1; -; mRNA. DR EMBL; AK292953; BAF85642.1; -; mRNA. DR EMBL; AK304442; BAG65263.1; -; mRNA. DR EMBL; AC004159; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC080066; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471091; EAW77011.1; -; Genomic_DNA. DR EMBL; BC026326; AAH26326.1; -; mRNA. DR EMBL; M20596; AAA35893.1; -; Genomic_DNA. DR EMBL; M20594; AAA35893.1; JOINED; Genomic_DNA. DR EMBL; M20595; AAA35893.1; JOINED; Genomic_DNA. DR EMBL; M17219; AAA52581.1; -; mRNA. DR CCDS; CCDS5595.1; -. [P63096-1] DR CCDS; CCDS59061.1; -. [P63096-2] DR PIR; A28318; RGHUI1. DR RefSeq; NP_001243343.1; NM_001256414.1. [P63096-2] DR RefSeq; NP_002060.4; NM_002069.5. [P63096-1] DR PDB; 1KJY; X-ray; 2.70 A; A/C=30-354. DR PDB; 1Y3A; X-ray; 2.50 A; A/B/C/D=26-354. DR PDB; 2G83; X-ray; 2.80 A; A/B=33-345. DR PDB; 2GTP; X-ray; 2.55 A; A/B=32-354. DR PDB; 2IK8; X-ray; 2.71 A; A/C=31-354. DR PDB; 2OM2; X-ray; 2.20 A; A/C=31-354. DR PDB; 2XNS; X-ray; 3.41 A; A/B=30-354. DR PDB; 3ONW; X-ray; 2.38 A; A/B=31-354. DR PDB; 3QE0; X-ray; 3.00 A; A/B/C=33-354. DR PDB; 3QI2; X-ray; 2.80 A; A/B=31-354. DR PDB; 3UMR; X-ray; 2.24 A; A=1-354. DR PDB; 3UMS; X-ray; 2.60 A; A=1-354. DR PDB; 4G5Q; X-ray; 2.90 A; A/B/C/D=25-354. DR PDB; 5JS7; NMR; -; A=30-354. DR PDB; 5JS8; NMR; -; A=30-354. DR PDB; 5TDH; X-ray; 3.00 A; A/H=1-354. DR PDB; 6CMO; EM; 4.50 A; A=1-354. DR PDB; 6CRK; X-ray; 2.00 A; A=2-354. DR PDB; 6DDE; EM; 3.50 A; A=1-354. DR PDB; 6DDF; EM; 3.50 A; A=1-354. DR PDB; 6KPF; EM; 2.90 A; A=1-354. DR PDB; 6KPG; EM; 3.00 A; A=2-354. DR PDB; 6LFM; EM; 3.50 A; A=2-354. DR PDB; 6LFO; EM; 3.40 A; A=2-354. DR PDB; 6LML; EM; 3.90 A; A=1-354. DR PDB; 6N4B; EM; 3.00 A; A=1-354. DR PDB; 6OMM; EM; 3.17 A; A=2-354. DR PDB; 6OS9; EM; 3.00 A; A=1-354. DR PDB; 6OSA; EM; 3.00 A; A=1-354. DR PDB; 6OT0; EM; 3.90 A; A=1-354. DR PDB; 6PB0; EM; 3.00 A; A=61-184. DR PDB; 6PB1; EM; 2.80 A; A=61-184. DR PDB; 6PT0; EM; 3.20 A; A=1-354. DR PDB; 6QNO; EM; 4.38 A; A=1-354. DR PDB; 6VU8; EM; 4.14 A; B=2-354. DR PDB; 6XBJ; EM; 3.88 A; A=1-354. DR PDB; 6XBK; EM; 3.24 A; A=1-354. DR PDB; 6XBL; EM; 3.90 A; A=1-354. DR PDB; 6XBM; EM; 3.15 A; A=1-354. DR PDB; 7CMU; EM; 3.00 A; A=1-354. DR PDB; 7CMV; EM; 2.70 A; A=1-354. DR PDB; 7DB6; EM; 3.30 A; A=1-354. DR PDB; 7DW9; EM; 2.60 A; A=1-19, A=61-181, A=229-242. DR PDB; 7E2X; EM; 3.00 A; A=1-354. DR PDB; 7E2Y; EM; 3.00 A; A=1-354. DR PDB; 7E2Z; EM; 3.10 A; A=1-354. DR PDB; 7E32; EM; 2.90 A; A=1-354. DR PDB; 7E33; EM; 2.90 A; A=1-354. DR PDB; 7E9G; EM; 3.50 A; A=1-354. DR PDB; 7EB2; EM; 3.50 A; A=1-354. DR PDB; 7EJX; EM; 2.40 A; A=1-354. DR PDB; 7EO2; EM; 2.89 A; B=1-354. DR PDB; 7EO4; EM; 2.86 A; B=1-354. DR PDB; 7EUO; EM; 2.90 A; A=1-354. DR PDB; 7EVY; EM; 2.98 A; A=1-354. DR PDB; 7EVZ; EM; 3.07 A; A=1-354. DR PDB; 7EW0; EM; 3.42 A; A=1-354. DR PDB; 7EW1; EM; 3.40 A; D=1-354. DR PDB; 7EW2; EM; 3.10 A; A=1-354. DR PDB; 7EW3; EM; 3.10 A; A=1-354. DR PDB; 7EW4; EM; 3.20 A; A=1-354. DR PDB; 7EW7; EM; 3.27 A; A=1-354. DR PDB; 7EXD; EM; 3.40 A; A=1-354. DR PDB; 7EZH; EM; 3.20 A; A=1-354. DR PDB; 7EZK; EM; 3.10 A; A=4-19, A=61-181, A=229-242. DR PDB; 7EZM; EM; 2.90 A; A=2-30. DR PDB; 7F1Q; EM; 2.90 A; A=1-354. DR PDB; 7F1R; EM; 3.00 A; A=1-354. DR PDB; 7F1S; EM; 2.80 A; A=1-354. DR PDB; 7F4D; EM; 3.00 A; A=4-19, A=61-181, A=229-242. DR PDB; 7F4F; EM; 2.90 A; A=1-19, A=61-181, A=229-242. DR PDB; 7F4H; EM; 2.70 A; A=4-19, A=61-181, A=229-242. DR PDB; 7F4I; EM; 3.10 A; A=1-19, A=61-181, A=229-242. DR PDB; 7JHJ; EM; 3.20 A; A=2-354. DR PDB; 7JVR; EM; 2.80 A; A=1-354. DR PDB; 7L0P; EM; 4.10 A; A=1-354. DR PDB; 7L0Q; EM; 4.30 A; A=1-354. DR PDB; 7L0R; EM; 4.20 A; A=1-354. DR PDB; 7L0S; EM; 4.50 A; A=1-354. DR PDB; 7MTS; EM; 3.20 A; C=1-354. DR PDB; 7NA7; EM; 2.70 A; A=1-354. DR PDB; 7NA8; EM; 2.70 A; A=1-354. DR PDB; 7O7F; EM; 3.15 A; A=1-354. DR PDB; 7P02; EM; 2.87 A; A=229-242. DR PDB; 7RKM; EM; 3.50 A; A=2-354. DR PDB; 7RKN; EM; 3.60 A; A=2-354. DR PDB; 7RKX; EM; 3.10 A; A=2-354. DR PDB; 7RKY; EM; 3.80 A; A=2-354. DR PDB; 7S8M; EM; 2.54 A; B=1-354. DR PDB; 7S8O; EM; 2.58 A; B=1-354. DR PDB; 7SBF; EM; 2.90 A; A=1-354. DR PDB; 7SCG; EM; 3.00 A; A=1-354. DR PDB; 7SQO; EM; 3.17 A; A=1-354. DR PDB; 7T2G; EM; 2.50 A; A=1-354. DR PDB; 7T2H; EM; 3.20 A; A=1-354. DR PDB; 7T6B; EM; 3.19 A; A=1-32. DR PDB; 7T6S; EM; 3.00 A; A=2-354. DR PDB; 7T6T; EM; 3.20 A; A=2-354. DR PDB; 7T6U; EM; 2.90 A; A=2-354. DR PDB; 7T6V; EM; 3.10 A; A=2-354. DR PDB; 7TRK; EM; 2.80 A; A=1-354. DR PDB; 7TRP; EM; 2.40 A; A=1-354. DR PDB; 7TRQ; EM; 2.50 A; A=1-354. DR PDB; 7TRS; EM; 2.80 A; A=1-354. DR PDB; 7TUZ; EM; 3.12 A; A=1-354. DR PDB; 7U2K; EM; 3.30 A; A=1-354. DR PDB; 7U2L; EM; 3.20 A; A=1-354. DR PDB; 7V68; EM; 3.40 A; A=1-354. DR PDB; 7V69; EM; 3.40 A; A=1-354. DR PDB; 7V6A; EM; 3.60 A; A=1-354. DR PDB; 7V9L; EM; 2.60 A; A=4-19, A=61-181, A=229-242. DR PDB; 7VAB; EM; 3.20 A; A=1-19, A=61-181, A=229-242. DR PDB; 7VDH; EM; 2.90 A; A=1-354. DR PDB; 7VDL; EM; 3.22 A; A=1-354. DR PDB; 7VDM; EM; 2.98 A; A=1-354. DR PDB; 7VFX; EM; 2.80 A; A=1-354. DR PDB; 7VGX; EM; 3.20 A; A=2-354. DR PDB; 7VGY; EM; 3.10 A; B=2-354. DR PDB; 7VGZ; EM; 3.30 A; C=2-354. DR PDB; 7VH0; EM; 3.46 A; B=2-354. DR PDB; 7VIE; EM; 2.86 A; D=1-354. DR PDB; 7VIF; EM; 2.83 A; D=1-354. DR PDB; 7VIG; EM; 2.89 A; D=1-354. DR PDB; 7VIH; EM; 2.98 A; D=1-354. DR PDB; 7VKT; EM; 2.90 A; B=1-354. DR PDB; 7VL8; EM; 2.90 A; A=1-354. DR PDB; 7VL9; EM; 2.60 A; A=1-354. DR PDB; 7VLA; EM; 2.70 A; A=1-354. DR PDB; 7VUG; EM; 3.20 A; A=2-354. DR PDB; 7VUY; EM; 2.84 A; A=1-354. DR PDB; 7VUZ; EM; 2.89 A; A=1-354. DR PDB; 7VV3; EM; 2.97 A; A=1-354. DR PDB; 7VV5; EM; 2.76 A; A=1-354. DR PDB; 7W0L; EM; 3.57 A; A=1-354. DR PDB; 7W0M; EM; 3.71 A; A=1-354. DR PDB; 7W0N; EM; 4.21 A; A=1-354. DR PDB; 7W0O; EM; 3.78 A; A=1-354. DR PDB; 7W0P; EM; 3.16 A; A=1-354. DR PDB; 7WF7; EM; 3.40 A; B=1-354. DR PDB; 7WIC; EM; 2.80 A; A=1-354. DR PDB; 7WIG; EM; 2.70 A; A=1-354. DR PDB; 7WJ5; EM; 3.72 A; A=1-354. DR PDB; 7WQ3; EM; 2.70 A; A=1-354. DR PDB; 7WU4; EM; 3.40 A; A=181-354. DR PDB; 7WU5; EM; 3.00 A; A=4-57, A=181-354. DR PDB; 7WU9; EM; 3.38 A; A=2-354. DR PDB; 7WUI; EM; 3.10 A; A=1-19, A=61-181, A=229-242. DR PDB; 7WUJ; EM; 3.30 A; A=4-19, A=61-181, A=229-242. DR PDB; 7WVU; EM; 3.30 A; A=1-354. DR PDB; 7WYB; EM; 2.97 A; B=1-354. DR PDB; 7WZ4; EM; 3.00 A; A=1-354. DR PDB; 7X2V; EM; 3.09 A; B=1-354. DR PDB; 7X5H; EM; 3.10 A; A=1-354. DR PDB; 7X9A; EM; 3.20 A; A=1-354. DR PDB; 7X9B; EM; 3.40 A; A=1-354. DR PDB; 7X9C; EM; 3.00 A; A=1-354. DR PDB; 7X9Y; EM; 3.10 A; A=1-354. DR PDB; 7XA3; EM; 2.90 A; A=1-354. DR PDB; 7XAT; EM; 2.85 A; B=1-354. DR PDB; 7XAU; EM; 2.97 A; B=1-354. DR PDB; 7XAV; EM; 2.87 A; B=1-354. DR PDB; 7XBW; EM; 2.80 A; C=1-354. DR PDB; 7XBX; EM; 3.40 A; C=1-354. DR PDB; 7XK2; EM; 3.10 A; A=1-354. DR PDB; 7XK8; EM; 3.30 A; A=1-354. DR PDB; 7XMR; EM; 3.10 A; A=1-354. DR PDB; 7XMS; EM; 2.90 A; A=1-354. DR PDB; 7XMT; EM; 2.80 A; A=1-354. DR PDB; 7XTA; EM; 3.20 A; A=1-354. DR PDB; 7XXH; EM; 2.90 A; A=2-24. DR PDB; 7Y12; EM; 3.10 A; A=1-354. DR PDB; 7Y15; EM; 2.90 A; A=1-354. DR PDB; 7Y1F; EM; 3.30 A; A=1-354. DR PDB; 7Y64; EM; 2.90 A; A=1-354. DR PDB; 7Y65; EM; 3.20 A; A=1-354. DR PDB; 7Y66; EM; 2.90 A; A=1-354. DR PDB; 7Y67; EM; 2.80 A; A=1-354. DR PDB; 7Y89; EM; 3.02 A; C=4-354. DR PDB; 7YAC; EM; 3.24 A; A=1-354. DR PDB; 7YAE; EM; 3.37 A; A=1-354. DR PDB; 7YDJ; EM; 3.03 A; A=1-20, A=60-181, A=229-242. DR PDB; 7YDP; EM; 3.10 A; A=4-19, A=61-181, A=229-242. DR PDB; 7YKD; EM; 2.81 A; C=4-354. DR PDB; 7YON; EM; 2.95 A; A=1-354. DR PDB; 7YOO; EM; 3.11 A; A=1-354. DR PDB; 7YU3; EM; 3.40 A; A=1-354. DR PDB; 7YU5; EM; 3.30 A; A=1-354. DR PDB; 7YU6; EM; 3.50 A; A=1-354. DR PDB; 7YU7; EM; 3.80 A; A=1-354. DR PDB; 7YU8; EM; 4.50 A; A=1-354. DR PDB; 8DZP; EM; 2.71 A; B=1-354. DR PDB; 8EF5; EM; 3.30 A; A/F=1-354. DR PDB; 8EF6; EM; 3.20 A; A/F=1-354. DR PDB; 8EFB; EM; 3.20 A; A=1-354. DR PDB; 8EFL; EM; 3.20 A; A/F=1-354. DR PDB; 8EFO; EM; 2.80 A; A/F=1-354. DR PDB; 8EFQ; EM; 3.30 A; A=1-354. DR PDB; 8F7Q; EM; 3.22 A; A/F=1-354. DR PDB; 8F7R; EM; 3.28 A; A/F=1-354. DR PDB; 8F7S; EM; 3.00 A; A/F=1-354. DR PDB; 8F7W; EM; 3.19 A; A=1-354. DR PDB; 8F7X; EM; 3.28 A; A=1-354. DR PDB; 8FEG; EM; 2.54 A; C=1-354. DR PDB; 8G05; EM; 3.00 A; A=1-354. DR PDB; 8G59; EM; 2.64 A; A=1-329. DR PDB; 8G94; EM; 3.15 A; B=1-354. DR PDB; 8GHV; EM; 2.80 A; A=1-354. DR PDB; 8GUQ; EM; 3.08 A; A=1-354. DR PDB; 8GUR; EM; 2.84 A; A=1-354. DR PDB; 8GUS; EM; 2.97 A; A=1-354. DR PDB; 8GUT; EM; 2.98 A; A=1-354. DR PDB; 8H2G; EM; 3.01 A; B=1-354. DR PDB; 8H4I; EM; 3.06 A; A=4-19, A=61-181, A=229-242. DR PDB; 8HBD; EM; 2.99 A; A=1-354. DR PDB; 8HK2; EM; 2.90 A; B=2-354. DR PDB; 8HK3; EM; 3.20 A; A=2-354. DR PDB; 8HK5; EM; 3.00 A; C=2-354. DR PDB; 8HNK; EM; 3.01 A; A=1-354. DR PDB; 8HNL; EM; 2.98 A; A=1-354. DR PDB; 8HNM; EM; 2.94 A; A=1-354. DR PDB; 8HQE; EM; 2.97 A; A=1-354. DR PDB; 8HQM; EM; 2.95 A; A=1-354. DR PDB; 8HQN; EM; 3.00 A; A=1-354. DR PDB; 8HS3; EM; 3.14 A; A=1-354. DR PDB; 8HSC; EM; 3.22 A; A=1-354. DR PDB; 8HVI; EM; 3.04 A; B=1-354. DR PDB; 8IA8; EM; 2.86 A; C=4-354. DR PDB; 8IC0; EM; 3.41 A; B=1-354. DR PDB; 8ID3; EM; 3.10 A; A=1-354. DR PDB; 8ID4; EM; 3.10 A; A=1-354. DR PDB; 8ID6; EM; 2.80 A; A=1-354. DR PDB; 8ID8; EM; 3.00 A; A=1-354. DR PDB; 8ID9; EM; 3.00 A; A=1-354. DR PDB; 8IHB; EM; 2.85 A; A=1-354. DR PDB; 8IHF; EM; 2.97 A; A=1-354. DR PDB; 8IHH; EM; 3.06 A; A=1-354. DR PDB; 8IHI; EM; 3.11 A; A=1-354. DR PDB; 8IHJ; EM; 3.07 A; A=1-354. DR PDB; 8INR; EM; 2.73 A; A=1-19, A=61-181, A=229-242. DR PDB; 8IOC; EM; 2.86 A; A=1-19, A=61-181, A=229-242. DR PDB; 8IOD; EM; 2.59 A; A=4-19, A=61-181, A=229-242. DR PDB; 8IRS; EM; 3.00 A; A=1-354. DR PDB; 8IRT; EM; 2.70 A; A=1-354. DR PDB; 8IRV; EM; 3.10 A; A=2-19, A=61-181, A=229-242. DR PDB; 8IW4; EM; 3.49 A; A=4-19, A=61-181, A=229-242. DR PDB; 8IW7; EM; 2.97 A; A=1-19, A=61-181, A=229-242. DR PDB; 8IW9; EM; 3.08 A; A=1-19, A=61-181, A=229-242. DR PDB; 8IY5; EM; 2.80 A; A=1-354. DR PDB; 8J18; EM; 2.89 A; A=1-354. DR PDB; 8J19; EM; 3.23 A; A=1-354. DR PDB; 8J1A; EM; 3.24 A; A=1-354. DR PDB; 8J6P; EM; 2.55 A; A=3-354. DR PDB; 8J6Q; EM; 2.60 A; A=3-354. DR PDB; 8J6R; EM; 2.76 A; A=3-354. DR PDB; 8JD3; EM; 3.30 A; A=1-354. DR PDB; 8JD5; EM; 3.60 A; A=1-354. DR PDB; 8JHY; EM; 2.87 A; D=1-354. DR PDB; 8JII; EM; 3.17 A; D=1-354. DR PDB; 8JIL; EM; 3.50 A; D=1-354. DR PDB; 8JIM; EM; 2.98 A; D=1-354. DR PDB; 8JR9; EM; 2.57 A; A=4-19, A=61-181, A=229-242. DR PDB; 8JSP; EM; 3.65 A; A=4-354. DR PDB; 8JZ7; EM; 2.60 A; D=1-354. DR PDB; 8K2X; EM; 3.20 A; A=1-354. DR PDB; 8K4N; EM; 2.83 A; A=1-354. DR PDB; 8SAI; EM; 3.27 A; D=1-354. DR PDB; 8SG1; EM; 2.94 A; A=4-354. DR PDB; 8W8B; EM; 3.00 A; A=1-354. DR PDB; 8WRB; EM; 2.91 A; A=1-354. DR PDBsum; 1KJY; -. DR PDBsum; 1Y3A; -. DR PDBsum; 2G83; -. DR PDBsum; 2GTP; -. DR PDBsum; 2IK8; -. DR PDBsum; 2OM2; -. DR PDBsum; 2XNS; -. DR PDBsum; 3ONW; -. DR PDBsum; 3QE0; -. DR PDBsum; 3QI2; -. DR PDBsum; 3UMR; -. DR PDBsum; 3UMS; -. DR PDBsum; 4G5Q; -. DR PDBsum; 5JS7; -. DR PDBsum; 5JS8; -. DR PDBsum; 5TDH; -. DR PDBsum; 6CMO; -. DR PDBsum; 6CRK; -. DR PDBsum; 6DDE; -. DR PDBsum; 6DDF; -. DR PDBsum; 6KPF; -. DR PDBsum; 6KPG; -. DR PDBsum; 6LFM; -. DR PDBsum; 6LFO; -. DR PDBsum; 6LML; -. DR PDBsum; 6N4B; -. DR PDBsum; 6OMM; -. DR PDBsum; 6OS9; -. DR PDBsum; 6OSA; -. DR PDBsum; 6OT0; -. DR PDBsum; 6PB0; -. DR PDBsum; 6PB1; -. DR PDBsum; 6PT0; -. DR PDBsum; 6QNO; -. DR PDBsum; 6VU8; -. DR PDBsum; 6XBJ; -. DR PDBsum; 6XBK; -. DR PDBsum; 6XBL; -. DR PDBsum; 6XBM; -. DR PDBsum; 7CMU; -. DR PDBsum; 7CMV; -. DR PDBsum; 7DB6; -. DR PDBsum; 7DW9; -. DR PDBsum; 7E2X; -. DR PDBsum; 7E2Y; -. DR PDBsum; 7E2Z; -. DR PDBsum; 7E32; -. DR PDBsum; 7E33; -. DR PDBsum; 7E9G; -. DR PDBsum; 7EB2; -. DR PDBsum; 7EJX; -. DR PDBsum; 7EO2; -. DR PDBsum; 7EO4; -. DR PDBsum; 7EUO; -. DR PDBsum; 7EVY; -. DR PDBsum; 7EVZ; -. DR PDBsum; 7EW0; -. DR PDBsum; 7EW1; -. DR PDBsum; 7EW2; -. DR PDBsum; 7EW3; -. DR PDBsum; 7EW4; -. DR PDBsum; 7EW7; -. DR PDBsum; 7EXD; -. DR PDBsum; 7EZH; -. DR PDBsum; 7EZK; -. DR PDBsum; 7EZM; -. DR PDBsum; 7F1Q; -. DR PDBsum; 7F1R; -. DR PDBsum; 7F1S; -. DR PDBsum; 7F4D; -. DR PDBsum; 7F4F; -. DR PDBsum; 7F4H; -. DR PDBsum; 7F4I; -. DR PDBsum; 7JHJ; -. DR PDBsum; 7JVR; -. DR PDBsum; 7L0P; -. DR PDBsum; 7L0Q; -. DR PDBsum; 7L0R; -. DR PDBsum; 7L0S; -. DR PDBsum; 7MTS; -. DR PDBsum; 7NA7; -. DR PDBsum; 7NA8; -. DR PDBsum; 7O7F; -. DR PDBsum; 7P02; -. DR PDBsum; 7RKM; -. DR PDBsum; 7RKN; -. DR PDBsum; 7RKX; -. DR PDBsum; 7RKY; -. DR PDBsum; 7S8M; -. DR PDBsum; 7S8O; -. DR PDBsum; 7SBF; -. DR PDBsum; 7SCG; -. DR PDBsum; 7SQO; -. DR PDBsum; 7T2G; -. DR PDBsum; 7T2H; -. DR PDBsum; 7T6B; -. DR PDBsum; 7T6S; -. DR PDBsum; 7T6T; -. DR PDBsum; 7T6U; -. DR PDBsum; 7T6V; -. DR PDBsum; 7TRK; -. DR PDBsum; 7TRP; -. DR PDBsum; 7TRQ; -. DR PDBsum; 7TRS; -. DR PDBsum; 7TUZ; -. DR PDBsum; 7U2K; -. DR PDBsum; 7U2L; -. DR PDBsum; 7V68; -. DR PDBsum; 7V69; -. DR PDBsum; 7V6A; -. DR PDBsum; 7V9L; -. DR PDBsum; 7VAB; -. DR PDBsum; 7VDH; -. DR PDBsum; 7VDL; -. DR PDBsum; 7VDM; -. DR PDBsum; 7VFX; -. DR PDBsum; 7VGX; -. DR PDBsum; 7VGY; -. DR PDBsum; 7VGZ; -. DR PDBsum; 7VH0; -. DR PDBsum; 7VIE; -. DR PDBsum; 7VIF; -. DR PDBsum; 7VIG; -. DR PDBsum; 7VIH; -. DR PDBsum; 7VKT; -. DR PDBsum; 7VL8; -. DR PDBsum; 7VL9; -. DR PDBsum; 7VLA; -. DR PDBsum; 7VUG; -. DR PDBsum; 7VUY; -. DR PDBsum; 7VUZ; -. DR PDBsum; 7VV3; -. DR PDBsum; 7VV5; -. DR PDBsum; 7W0L; -. DR PDBsum; 7W0M; -. DR PDBsum; 7W0N; -. DR PDBsum; 7W0O; -. DR PDBsum; 7W0P; -. DR PDBsum; 7WF7; -. DR PDBsum; 7WIC; -. DR PDBsum; 7WIG; -. DR PDBsum; 7WJ5; -. DR PDBsum; 7WQ3; -. DR PDBsum; 7WU4; -. DR PDBsum; 7WU5; -. DR PDBsum; 7WU9; -. DR PDBsum; 7WUI; -. DR PDBsum; 7WUJ; -. DR PDBsum; 7WVU; -. DR PDBsum; 7WYB; -. DR PDBsum; 7WZ4; -. DR PDBsum; 7X2V; -. DR PDBsum; 7X5H; -. DR PDBsum; 7X9A; -. DR PDBsum; 7X9B; -. DR PDBsum; 7X9C; -. DR PDBsum; 7X9Y; -. DR PDBsum; 7XA3; -. DR PDBsum; 7XAT; -. DR PDBsum; 7XAU; -. DR PDBsum; 7XAV; -. DR PDBsum; 7XBW; -. DR PDBsum; 7XBX; -. DR PDBsum; 7XK2; -. DR PDBsum; 7XK8; -. DR PDBsum; 7XMR; -. DR PDBsum; 7XMS; -. DR PDBsum; 7XMT; -. DR PDBsum; 7XTA; -. DR PDBsum; 7XXH; -. DR PDBsum; 7Y12; -. DR PDBsum; 7Y15; -. DR PDBsum; 7Y1F; -. DR PDBsum; 7Y64; -. DR PDBsum; 7Y65; -. DR PDBsum; 7Y66; -. DR PDBsum; 7Y67; -. DR PDBsum; 7Y89; -. DR PDBsum; 7YAC; -. DR PDBsum; 7YAE; -. DR PDBsum; 7YDJ; -. DR PDBsum; 7YDP; -. DR PDBsum; 7YKD; -. DR PDBsum; 7YON; -. DR PDBsum; 7YOO; -. DR PDBsum; 7YU3; -. DR PDBsum; 7YU5; -. DR PDBsum; 7YU6; -. DR PDBsum; 7YU7; -. DR PDBsum; 7YU8; -. DR PDBsum; 8DZP; -. DR PDBsum; 8EF5; -. DR PDBsum; 8EF6; -. DR PDBsum; 8EFB; -. DR PDBsum; 8EFL; -. DR PDBsum; 8EFO; -. DR PDBsum; 8EFQ; -. DR PDBsum; 8F7Q; -. DR PDBsum; 8F7R; -. DR PDBsum; 8F7S; -. DR PDBsum; 8F7W; -. DR PDBsum; 8F7X; -. DR PDBsum; 8FEG; -. DR PDBsum; 8G05; -. DR PDBsum; 8G59; -. DR PDBsum; 8G94; -. DR PDBsum; 8GHV; -. DR PDBsum; 8GUQ; -. DR PDBsum; 8GUR; -. DR PDBsum; 8GUS; -. DR PDBsum; 8GUT; -. DR PDBsum; 8H2G; -. DR PDBsum; 8H4I; -. DR PDBsum; 8HBD; -. DR PDBsum; 8HK2; -. DR PDBsum; 8HK3; -. DR PDBsum; 8HK5; -. DR PDBsum; 8HNK; -. DR PDBsum; 8HNL; -. DR PDBsum; 8HNM; -. DR PDBsum; 8HQE; -. DR PDBsum; 8HQM; -. DR PDBsum; 8HQN; -. DR PDBsum; 8HS3; -. DR PDBsum; 8HSC; -. DR PDBsum; 8HVI; -. DR PDBsum; 8IA8; -. DR PDBsum; 8IC0; -. DR PDBsum; 8ID3; -. DR PDBsum; 8ID4; -. DR PDBsum; 8ID6; -. DR PDBsum; 8ID8; -. DR PDBsum; 8ID9; -. DR PDBsum; 8IHB; -. DR PDBsum; 8IHF; -. DR PDBsum; 8IHH; -. DR PDBsum; 8IHI; -. DR PDBsum; 8IHJ; -. DR PDBsum; 8INR; -. DR PDBsum; 8IOC; -. DR PDBsum; 8IOD; -. DR PDBsum; 8IRS; -. DR PDBsum; 8IRT; -. DR PDBsum; 8IRV; -. DR PDBsum; 8IW4; -. DR PDBsum; 8IW7; -. DR PDBsum; 8IW9; -. DR PDBsum; 8IY5; -. DR PDBsum; 8J18; -. DR PDBsum; 8J19; -. DR PDBsum; 8J1A; -. DR PDBsum; 8J6P; -. DR PDBsum; 8J6Q; -. DR PDBsum; 8J6R; -. DR PDBsum; 8JD3; -. DR PDBsum; 8JD5; -. DR PDBsum; 8JHY; -. DR PDBsum; 8JII; -. DR PDBsum; 8JIL; -. DR PDBsum; 8JIM; -. DR PDBsum; 8JR9; -. DR PDBsum; 8JSP; -. DR PDBsum; 8JZ7; -. DR PDBsum; 8K2X; -. DR PDBsum; 8K4N; -. DR PDBsum; 8SAI; -. DR PDBsum; 8SG1; -. DR PDBsum; 8W8B; -. DR PDBsum; 8WRB; -. DR AlphaFoldDB; P63096; -. DR EMDB; EMD-0339; -. DR EMDB; EMD-0744; -. DR EMDB; EMD-0745; -. DR EMDB; EMD-0877; -. DR EMDB; EMD-0879; -. DR EMDB; EMD-0918; -. DR EMDB; EMD-12746; -. DR EMDB; EMD-20126; -. DR EMDB; EMD-20180; -. DR EMDB; EMD-20181; -. DR EMDB; EMD-20190; -. DR EMDB; EMD-20470; -. DR EMDB; EMD-21388; -. DR EMDB; EMD-22117; -. DR EMDB; EMD-22118; -. DR EMDB; EMD-22119; -. DR EMDB; EMD-22120; -. DR EMDB; EMD-22338; -. DR EMDB; EMD-22511; -. DR EMDB; EMD-23099; -. DR EMDB; EMD-23100; -. DR EMDB; EMD-23101; -. DR EMDB; EMD-23102; -. DR EMDB; EMD-23996; -. DR EMDB; EMD-24267; -. DR EMDB; EMD-24268; -. DR EMDB; EMD-24500; -. DR EMDB; EMD-24501; -. DR EMDB; EMD-24506; -. DR EMDB; EMD-24507; -. DR EMDB; EMD-24897; -. DR EMDB; EMD-24899; -. DR EMDB; EMD-24978; -. DR EMDB; EMD-25034; -. DR EMDB; EMD-25389; -. DR EMDB; EMD-25612; -. DR EMDB; EMD-25613; -. DR EMDB; EMD-25726; -. DR EMDB; EMD-25727; -. DR EMDB; EMD-25728; -. DR EMDB; EMD-25729; -. DR EMDB; EMD-26099; -. DR EMDB; EMD-26100; -. DR EMDB; EMD-26101; -. DR EMDB; EMD-26102; -. DR EMDB; EMD-26104; -. DR EMDB; EMD-26136; -. DR EMDB; EMD-26313; -. DR EMDB; EMD-26314; -. DR EMDB; EMD-27804; -. DR EMDB; EMD-28066; -. DR EMDB; EMD-28069; -. DR EMDB; EMD-28077; -. DR EMDB; EMD-28085; -. DR EMDB; EMD-28086; -. DR EMDB; EMD-28088; -. DR EMDB; EMD-28907; -. DR EMDB; EMD-28908; -. DR EMDB; EMD-28909; -. DR EMDB; EMD-28911; -. DR EMDB; EMD-28912; -. DR EMDB; EMD-29645; -. DR EMDB; EMD-29736; -. DR EMDB; EMD-29861; -. DR EMDB; EMD-30410; -. DR EMDB; EMD-30411; -. DR EMDB; EMD-30627; -. DR EMDB; EMD-30971; -. DR EMDB; EMD-30972; -. DR EMDB; EMD-30973; -. DR EMDB; EMD-30974; -. DR EMDB; EMD-30975; -. DR EMDB; EMD-31031; -. DR EMDB; EMD-31049; -. DR EMDB; EMD-31164; -. DR EMDB; EMD-31225; -. DR EMDB; EMD-31226; -. DR EMDB; EMD-31323; -. DR EMDB; EMD-31341; -. DR EMDB; EMD-31342; -. DR EMDB; EMD-31343; -. DR EMDB; EMD-31344; -. DR EMDB; EMD-31345; -. DR EMDB; EMD-31346; -. DR EMDB; EMD-31347; -. DR EMDB; EMD-31349; -. DR EMDB; EMD-31371; -. DR EMDB; EMD-31387; -. DR EMDB; EMD-31422; -. DR EMDB; EMD-31423; -. DR EMDB; EMD-31424; -. DR EMDB; EMD-31448; -. DR EMDB; EMD-31449; -. DR EMDB; EMD-31452; -. DR EMDB; EMD-31453; -. DR EMDB; EMD-31738; -. DR EMDB; EMD-31739; -. DR EMDB; EMD-31740; -. DR EMDB; EMD-31918; -. DR EMDB; EMD-31922; -. DR EMDB; EMD-31923; -. DR EMDB; EMD-31962; -. DR EMDB; EMD-31979; -. DR EMDB; EMD-31980; -. DR EMDB; EMD-31981; -. DR EMDB; EMD-31982; -. DR EMDB; EMD-32006; -. DR EMDB; EMD-32007; -. DR EMDB; EMD-32008; -. DR EMDB; EMD-32009; -. DR EMDB; EMD-32018; -. DR EMDB; EMD-32020; -. DR EMDB; EMD-32021; -. DR EMDB; EMD-32022; -. DR EMDB; EMD-32127; -. DR EMDB; EMD-32131; -. DR EMDB; EMD-32132; -. DR EMDB; EMD-32136; -. DR EMDB; EMD-32138; -. DR EMDB; EMD-32243; -. DR EMDB; EMD-32244; -. DR EMDB; EMD-32245; -. DR EMDB; EMD-32246; -. DR EMDB; EMD-32247; -. DR EMDB; EMD-32461; -. DR EMDB; EMD-32528; -. DR EMDB; EMD-32529; -. DR EMDB; EMD-32543; -. DR EMDB; EMD-32698; -. DR EMDB; EMD-32819; -. DR EMDB; EMD-32820; -. DR EMDB; EMD-32824; -. DR EMDB; EMD-32858; -. DR EMDB; EMD-32890; -. DR EMDB; EMD-32904; -. DR EMDB; EMD-32905; -. DR EMDB; EMD-32932; -. DR EMDB; EMD-32972; -. DR EMDB; EMD-33014; -. DR EMDB; EMD-33069; -. DR EMDB; EMD-33070; -. DR EMDB; EMD-33071; -. DR EMDB; EMD-33085; -. DR EMDB; EMD-33086; -. DR EMDB; EMD-33098; -. DR EMDB; EMD-33099; -. DR EMDB; EMD-33100; -. DR EMDB; EMD-33107; -. DR EMDB; EMD-33108; -. DR EMDB; EMD-33247; -. DR EMDB; EMD-33302; -. DR EMDB; EMD-33303; -. DR EMDB; EMD-33304; -. DR EMDB; EMD-33444; -. DR EMDB; EMD-33554; -. DR EMDB; EMD-33557; -. DR EMDB; EMD-33562; -. DR EMDB; EMD-33633; -. DR EMDB; EMD-33634; -. DR EMDB; EMD-33635; -. DR EMDB; EMD-33636; -. DR EMDB; EMD-33682; -. DR EMDB; EMD-33708; -. DR EMDB; EMD-33710; -. DR EMDB; EMD-33749; -. DR EMDB; EMD-33891; -. DR EMDB; EMD-33984; -. DR EMDB; EMD-33985; -. DR EMDB; EMD-34097; -. DR EMDB; EMD-34099; -. DR EMDB; EMD-34100; -. DR EMDB; EMD-34101; -. DR EMDB; EMD-34102; -. DR EMDB; EMD-34276; -. DR EMDB; EMD-34277; -. DR EMDB; EMD-34278; -. DR EMDB; EMD-34279; -. DR EMDB; EMD-34437; -. DR EMDB; EMD-34619; -. DR EMDB; EMD-34842; -. DR EMDB; EMD-34843; -. DR EMDB; EMD-34846; -. DR EMDB; EMD-34914; -. DR EMDB; EMD-34915; -. DR EMDB; EMD-34916; -. DR EMDB; EMD-34948; -. DR EMDB; EMD-34950; -. DR EMDB; EMD-34951; -. DR EMDB; EMD-34984; -. DR EMDB; EMD-34993; -. DR EMDB; EMD-35044; -. DR EMDB; EMD-35298; -. DR EMDB; EMD-35351; -. DR EMDB; EMD-35356; -. DR EMDB; EMD-35357; -. DR EMDB; EMD-35358; -. DR EMDB; EMD-35359; -. DR EMDB; EMD-35360; -. DR EMDB; EMD-35442; -. DR EMDB; EMD-35443; -. DR EMDB; EMD-35444; -. DR EMDB; EMD-35445; -. DR EMDB; EMD-35446; -. DR EMDB; EMD-35684; -. DR EMDB; EMD-35685; -. DR EMDB; EMD-35814; -. DR EMDB; EMD-35913; -. DR EMDB; EMD-35914; -. DR EMDB; EMD-35915; -. DR EMDB; EMD-36174; -. DR EMDB; EMD-36176; -. DR EMDB; EMD-36300; -. DR EMDB; EMD-36312; -. DR EMDB; EMD-36317; -. DR EMDB; EMD-36318; -. DR EMDB; EMD-36626; -. DR EMDB; EMD-36736; -. DR EMDB; EMD-36842; -. DR EMDB; EMD-36887; -. DR EMDB; EMD-37351; -. DR EMDB; EMD-37771; -. DR EMDB; EMD-40052; -. DR EMDB; EMD-40270; -. DR EMDB; EMD-40450; -. DR EMDB; EMD-4598; -. DR EMDB; EMD-7517; -. DR EMDB; EMD-7868; -. DR EMDB; EMD-7869; -. DR SMR; P63096; -. DR BioGRID; 109032; 151. DR CORUM; P63096; -. DR ELM; P63096; -. DR IntAct; P63096; 68. DR MINT; P63096; -. DR STRING; 9606.ENSP00000497260; -. DR BindingDB; P63096; -. DR ChEMBL; CHEMBL4741; -. DR DrugBank; DB04315; Guanosine-5'-Diphosphate. DR DrugBank; DB04444; Tetrafluoroaluminate Ion. DR GlyGen; P63096; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P63096; -. DR PhosphoSitePlus; P63096; -. DR SwissPalm; P63096; -. DR BioMuta; GNAI1; -. DR DMDM; 52000964; -. DR CPTAC; CPTAC-1243; -. DR CPTAC; CPTAC-1244; -. DR EPD; P63096; -. DR jPOST; P63096; -. DR MassIVE; P63096; -. DR MaxQB; P63096; -. DR PaxDb; 9606-ENSP00000343027; -. DR PeptideAtlas; P63096; -. DR PRIDE; P63096; -. DR ProteomicsDB; 57475; -. [P63096-1] DR ProteomicsDB; 5853; -. DR Pumba; P63096; -. DR ABCD; P63096; 2 sequenced antibodies. DR Antibodypedia; 15099; 337 antibodies from 37 providers. DR DNASU; 2770; -. DR Ensembl; ENST00000351004.8; ENSP00000343027.3; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000442586.2; ENSP00000391439.2; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000457358.7; ENSP00000410572.2; ENSG00000127955.17. [P63096-2] DR Ensembl; ENST00000648098.1; ENSP00000497717.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000648306.1; ENSP00000497773.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000648412.1; ENSP00000497051.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000648476.1; ENSP00000497179.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000648663.1; ENSP00000497379.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000648832.1; ENSP00000497765.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000648877.1; ENSP00000497760.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000648953.1; ENSP00000496800.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000649225.1; ENSP00000496829.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000649267.1; ENSP00000497315.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000649487.1; ENSP00000498091.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000649796.2; ENSP00000497260.1; ENSG00000127955.17. [P63096-1] DR Ensembl; ENST00000649855.1; ENSP00000497754.1; ENSG00000127955.17. [P63096-1] DR GeneID; 2770; -. DR KEGG; hsa:2770; -. DR MANE-Select; ENST00000649796.2; ENSP00000497260.1; NM_002069.6; NP_002060.4. DR UCSC; uc003uhb.2; human. [P63096-1] DR AGR; HGNC:4384; -. DR CTD; 2770; -. DR DisGeNET; 2770; -. DR GeneCards; GNAI1; -. DR HGNC; HGNC:4384; GNAI1. DR HPA; ENSG00000127955; Tissue enhanced (brain). DR MalaCards; GNAI1; -. DR MIM; 139310; gene. DR MIM; 619854; phenotype. DR neXtProt; NX_P63096; -. DR OpenTargets; ENSG00000127955; -. DR PharmGKB; PA172; -. DR VEuPathDB; HostDB:ENSG00000127955; -. DR eggNOG; KOG0082; Eukaryota. DR GeneTree; ENSGT00940000153567; -. DR HOGENOM; CLU_014184_6_0_1; -. DR InParanoid; P63096; -. DR OMA; CSELEMF; -. DR OrthoDB; 2897309at2759; -. DR PhylomeDB; P63096; -. DR TreeFam; TF300673; -. DR PathwayCommons; P63096; -. DR Reactome; R-HSA-170670; Adenylate cyclase inhibitory pathway. DR Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12. DR Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-418597; G alpha (z) signalling events. DR Reactome; R-HSA-422356; Regulation of insulin secretion. DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling. DR Reactome; R-HSA-9634597; GPER1 signaling. DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production. DR SignaLink; P63096; -. DR SIGNOR; P63096; -. DR BioGRID-ORCS; 2770; 10 hits in 1152 CRISPR screens. DR ChiTaRS; GNAI1; human. DR EvolutionaryTrace; P63096; -. DR GeneWiki; GNAI1; -. DR GenomeRNAi; 2770; -. DR Pharos; P63096; Tbio. DR PRO; PR:P63096; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P63096; Protein. DR Bgee; ENSG00000127955; Expressed in corpus callosum and 200 other cell types or tissues. DR ExpressionAtlas; P63096; baseline and differential. DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0031749; F:D2 dopamine receptor binding; IPI:ARUK-UCL. DR GO; GO:0001664; F:G protein-coupled receptor binding; ISS:UniProtKB. DR GO; GO:0031821; F:G protein-coupled serotonin receptor binding; IBA:GO_Central. DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central. DR GO; GO:0019003; F:GDP binding; ISS:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; TAS:Reactome. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IMP:UniProtKB. DR GO; GO:1904322; P:cellular response to forskolin; ISS:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB. DR GO; GO:1904778; P:positive regulation of protein localization to cell cortex; IMP:UniProtKB. DR GO; GO:0043949; P:regulation of cAMP-mediated signaling; ISS:UniProtKB. DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB. DR GO; GO:0043434; P:response to peptide hormone; ISS:BHF-UCL. DR CDD; cd00066; G-alpha; 1. DR Gene3D; 1.10.400.10; GI Alpha 1, domain 2-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR IDEAL; IID00608; -. DR InterPro; IPR001408; Gprotein_alpha_I. DR InterPro; IPR001019; Gprotein_alpha_su. DR InterPro; IPR011025; GproteinA_insert. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10218; GTP-BINDING PROTEIN ALPHA SUBUNIT; 1. DR PANTHER; PTHR10218:SF359; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; 1. DR Pfam; PF00503; G-alpha; 1. DR PRINTS; PR00318; GPROTEINA. DR PRINTS; PR00441; GPROTEINAI. DR SMART; SM00275; G_alpha; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF47895; Transducin (alpha subunit), insertion domain; 1. DR PROSITE; PS51882; G_ALPHA; 1. DR Genevisible; P63096; HS. PE 1: Evidence at protein level; KW 3D-structure; ADP-ribosylation; Alternative splicing; Cell cycle; KW Cell division; Cell membrane; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Disease variant; Epilepsy; GTP-binding; KW Host-virus interaction; Intellectual disability; Lipoprotein; Magnesium; KW Membrane; Metal-binding; Mitosis; Myristate; Nucleotide-binding; Nucleus; KW Palmitate; Reference proteome; Transducer; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:20213681, FT ECO:0000269|PubMed:25255805" FT CHAIN 2..354 FT /note="Guanine nucleotide-binding protein G(i) subunit FT alpha-1" FT /id="PRO_0000203671" FT DOMAIN 32..354 FT /note="G-alpha" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 35..48 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 173..181 FT /note="G2 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 196..205 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 265..272 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT REGION 324..329 FT /note="G5 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230" FT BINDING 43..48 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:21115486, FT ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, FT ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, FT ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, FT ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, FT ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, FT ECO:0007744|PDB:4G5Q" FT BINDING 47 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:18434541, FT ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0" FT BINDING 151 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:1KJY, ECO:0007744|PDB:2OM2, FT ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, FT ECO:0007744|PDB:4G5Q" FT BINDING 175..181 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, FT ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, FT ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, FT ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, FT ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, FT ECO:0007744|PDB:4G5Q" FT BINDING 181 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:18434541, FT ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0" FT BINDING 200..204 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:21115486" FT BINDING 269..272 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:21115486, FT ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, FT ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, FT ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, FT ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, FT ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, FT ECO:0007744|PDB:4G5Q" FT BINDING 326 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, FT ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, FT ECO:0007744|PDB:2OM2, ECO:0007744|PDB:3ONW, FT ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, FT ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, FT ECO:0007744|PDB:4G5Q" FT MOD_RES 178 FT /note="ADP-ribosylarginine; by cholera toxin" FT /evidence="ECO:0000250" FT MOD_RES 204 FT /note="Deamidated glutamine; by Photorhabdus PAU_02230" FT /evidence="ECO:0000269|PubMed:24141704" FT MOD_RES 351 FT /note="ADP-ribosylcysteine; by pertussis toxin" FT /evidence="ECO:0000250" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:20213681, FT ECO:0000269|PubMed:25255805" FT LIPID 3 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P10824" FT VAR_SEQ 1..52 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045215" FT VARIANT 40 FT /note="G -> C (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087204" FT VARIANT 40 FT /note="G -> R (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087205" FT VARIANT 45 FT /note="G -> D (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087206" FT VARIANT 48 FT /note="T -> I (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087207" FT VARIANT 48 FT /note="T -> K (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087208" FT VARIANT 52 FT /note="Q -> P (in NEDHISB; loss of GTP binding)" FT /evidence="ECO:0000269|PubMed:33473207, FT ECO:0000269|PubMed:34685729" FT /id="VAR_087209" FT VARIANT 75 FT /note="Missing (in NEDHISB; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087210" FT VARIANT 172 FT /note="Missing (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087211" FT VARIANT 173 FT /note="D -> V (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087212" FT VARIANT 186..189 FT /note="Missing (in NEDHISB; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087213" FT VARIANT 224 FT /note="C -> Y (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087214" FT VARIANT 270 FT /note="K -> N (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087215" FT VARIANT 270 FT /note="K -> R (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087216" FT VARIANT 272 FT /note="D -> G (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:34819662" FT /id="VAR_087217" FT VARIANT 326 FT /note="A -> P (in NEDHISB)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087218" FT VARIANT 332 FT /note="V -> E (in NEDHISB; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33473207" FT /id="VAR_087219" FT MUTAGEN 42 FT /note="G->R: Abolishes switch to an activated conformation FT and dissociation from beta and gamma subunits upon GTP FT binding. Abolishes interaction with RGS family members." FT /evidence="ECO:0000269|PubMed:22383884" FT MUTAGEN 116 FT /note="E->L: Enhances interaction (inactive GDP-bound) with FT RGS14." FT /evidence="ECO:0000269|PubMed:17603074, FT ECO:0000269|PubMed:21115486" FT MUTAGEN 147 FT /note="Q->L: Enhances interaction (inactive GDP-bound) with FT RGS14." FT /evidence="ECO:0000269|PubMed:17603074, FT ECO:0000269|PubMed:21115486" FT MUTAGEN 245 FT /note="E->L: Enhances interaction (inactive GDP-bound) with FT RGS14." FT /evidence="ECO:0000269|PubMed:21115486" FT CONFLICT 138 FT /note="A -> G (in Ref. 3; CAB43212)" FT /evidence="ECO:0000305" FT CONFLICT 219 FT /note="T -> A (in Ref. 8; AAH26326)" FT /evidence="ECO:0000305" FT CONFLICT 244 FT /note="H -> Y (in Ref. 4; AAV38580)" FT /evidence="ECO:0000305" FT CONFLICT 249 FT /note="L -> M (in Ref. 4; AAV38580)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="P -> Q (in Ref. 8; AAH26326)" FT /evidence="ECO:0000305" FT HELIX 7..31 FT /evidence="ECO:0007829|PDB:6CRK" FT STRAND 33..41 FT /evidence="ECO:0007829|PDB:6CRK" FT TURN 42..44 FT /evidence="ECO:0007829|PDB:7S8M" FT HELIX 46..57 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 63..67 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 70..91 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 100..110 FT /evidence="ECO:0007829|PDB:6CRK" FT TURN 111..114 FT /evidence="ECO:0007829|PDB:4G5Q" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 134..140 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 141..145 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 152..156 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 159..163 FT /evidence="ECO:0007829|PDB:6CRK" FT STRAND 164..166 FT /evidence="ECO:0007829|PDB:2G83" FT HELIX 171..175 FT /evidence="ECO:0007829|PDB:6CRK" FT STRAND 183..191 FT /evidence="ECO:0007829|PDB:6CRK" FT STRAND 194..203 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 208..211 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 212..215 FT /evidence="ECO:0007829|PDB:6CRK" FT STRAND 219..226 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 227..231 FT /evidence="ECO:0007829|PDB:6CRK" FT TURN 235..237 FT /evidence="ECO:0007829|PDB:7JVR" FT STRAND 238..241 FT /evidence="ECO:0007829|PDB:3UMS" FT HELIX 242..254 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 257..259 FT /evidence="ECO:0007829|PDB:6CRK" FT STRAND 262..269 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 271..277 FT /evidence="ECO:0007829|PDB:6CRK" FT TURN 278..280 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 283..285 FT /evidence="ECO:0007829|PDB:6CRK" FT STRAND 287..289 FT /evidence="ECO:0007829|PDB:8J18" FT TURN 292..294 FT /evidence="ECO:0007829|PDB:7F1S" FT HELIX 296..308 FT /evidence="ECO:0007829|PDB:6CRK" FT TURN 312..316 FT /evidence="ECO:0007829|PDB:6CRK" FT STRAND 319..323 FT /evidence="ECO:0007829|PDB:6CRK" FT STRAND 326..328 FT /evidence="ECO:0007829|PDB:7SCG" FT HELIX 329..346 FT /evidence="ECO:0007829|PDB:6CRK" FT HELIX 348..350 FT /evidence="ECO:0007829|PDB:3UMR" SQ SEQUENCE 354 AA; 40361 MW; 9F88311B46E62DE3 CRC64; MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR ADDARQLFVL AGAAEEGFMT AELAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF //