GNAI2_HUMAN
ID GNAI2_HUMAN Reviewed; 355 AA.
AC P04899; B3KTZ0; B4DYA0; B4E2X5; Q6B6N3; Q8IZ71;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Guanine nucleotide-binding protein G(i) subunit alpha-2;
DE AltName: Full=Adenylate cyclase-inhibiting G alpha protein;
GN Name=GNAI2; Synonyms=GNAI2B;
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 [MRNA] (ISOFORM 1).
RX PubMed=3100330; DOI=10.1016/0014-5793(87)81428-x;
RA Didsbury J.R., Ho Y.-S., Snyderman R.;
RT "Human Gi protein alpha-subunit: deduction of amino acid structure from a
RT cloned cDNA.";
RL FEBS Lett. 211:160-164(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3120178; DOI=10.1073/pnas.84.22.7886;
RA Beals C.R., Wilson C.B., Perlmutter R.M.;
RT "A small multigene family encodes Gi signal-transduction proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7886-7890(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SGI2), AND FUNCTION (ISOFORM SGI2).
RC TISSUE=Brain;
RX PubMed=17550964; DOI=10.1242/jcs.005611;
RA Lopez-Aranda M.F., Acevedo M.J., Gutierrez A., Koulen P., Khan Z.U.;
RT "Role of a Galphai2 protein splice variant in the formation of an
RT intracellular dopamine D2 receptor pool.";
RL J. Cell Sci. 120:2171-2178(2007).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5 AND 6).
RC TISSUE=Brain, Teratocarcinoma, Testis, and Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Mammary gland;
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RX PubMed=2837412; DOI=10.1016/0014-5793(88)80764-6;
RA Weinstein L.S., Spiegel A.M., Carter A.D.;
RT "Cloning and characterization of the human gene for the alpha-subunit of
RT Gi2, a GTP-binding signal transduction protein.";
RL FEBS Lett. 232:333-340(1988).
RN [11]
RP INTERACTION WITH CXCR1 AND CXCR2.
RX PubMed=8662698; DOI=10.1074/jbc.271.22.12783;
RA Damaj B.B., McColl S.R., Mahana W., Crouch M.F., Naccache P.H.;
RT "Physical association of Gi2alpha with interleukin-8 receptors.";
RL J. Biol. Chem. 271:12783-12789(1996).
RN [12]
RP INTERACTION WITH UNC5B.
RX PubMed=12359238; DOI=10.1016/s0006-291x(02)02277-5;
RA Komatsuzaki K., Dalvin S., Kinane T.B.;
RT "Modulation of G(ialpha(2)) signaling by the axonal guidance molecule
RT UNC5H2.";
RL Biochem. Biophys. Res. Commun. 297:898-905(2002).
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 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 [16]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP DEAMIDATION AT GLN-205 (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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
RN [21]
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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP INTERACTION WITH GNB2.
RX PubMed=28219978; DOI=10.1161/circresaha.116.310112;
RA Stallmeyer B., Kuss J., Kotthoff S., Zumhagen S., Vowinkel K., Rinne S.,
RA Matschke L.A., Friedrich C., Schulze-Bahr E., Rust S., Seebohm G.,
RA Decher N., Schulze-Bahr E.;
RT "A Mutation in the G-Protein Gene GNB2 Causes Familial Sinus Node and
RT Atrioventricular Conduction Dysfunction.";
RL Circ. Res. 120:e33-e44(2017).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as modulators or transducers in various transmembrane signaling
CC systems. The G(i) proteins are involved in hormonal regulation of
CC adenylate cyclase: they inhibit the cyclase in response to beta-
CC adrenergic stimuli. May play a role in cell division.
CC {ECO:0000269|PubMed:17635935}.
CC -!- FUNCTION: [Isoform sGi2]: Regulates the cell surface density of
CC dopamine receptors DRD2 by sequestrating them as an intracellular pool.
CC {ECO:0000269|PubMed:17550964}.
CC -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC alpha chain contains the guanine nucleotide binding site. In this
CC context, interacts with GNB2 (PubMed:28219978). Interacts with GPSM1
CC (By similarity). Interacts with RGS12 and RGS14 (By similarity).
CC Interacts with UNC5B (PubMed:12359238). Interacts (inactive GDP-bound
CC form) with NUCB1 (via GBA motif); the interaction leads to activation
CC of GNAI3 (By similarity). Interacts (inactive GDP-bound form) with
CC CCDC88C/DAPLE (via GBA motif) (PubMed:26126266). Interacts (inactive
CC GDP-bound form) with CCDC8A/GIV (via GBA motif) (PubMed:19211784).
CC Interacts with CXCR1 and CXCR2 (PubMed:8662698).
CC {ECO:0000250|UniProtKB:P04897, ECO:0000269|PubMed:12359238,
CC ECO:0000269|PubMed:19211784, ECO:0000269|PubMed:26126266,
CC ECO:0000269|PubMed:28219978, ECO:0000269|PubMed:8662698}.
CC -!- INTERACTION:
CC P04899; P32302: CXCR5; NbExp=5; IntAct=EBI-353997, EBI-2835269;
CC P04899; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-353997, EBI-347538;
CC P04899; Q15323: KRT31; NbExp=3; IntAct=EBI-353997, EBI-948001;
CC P04899; Q6A162: KRT40; NbExp=3; IntAct=EBI-353997, EBI-10171697;
CC P04899; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-353997, EBI-10171774;
CC P04899; Q99750: MDFI; NbExp=5; IntAct=EBI-353997, EBI-724076;
CC P04899; P14598: NCF1; NbExp=2; IntAct=EBI-353997, EBI-395044;
CC P04899; P19878: NCF2; NbExp=4; IntAct=EBI-353997, EBI-489611;
CC P04899; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-353997, EBI-945833;
CC P04899; Q8IVA1: PCP2; NbExp=3; IntAct=EBI-353997, EBI-12250122;
CC P04899; O76081-6: RGS20; NbExp=3; IntAct=EBI-353997, EBI-10178530;
CC P04899; Q15654: TRIP6; NbExp=3; IntAct=EBI-353997, EBI-742327;
CC P04899; P42866: Oprm1; Xeno; NbExp=2; IntAct=EBI-353997, EBI-5282656;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17635935}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:17635935}. Cell membrane
CC {ECO:0000269|PubMed:17635935}. Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Note=Localizes in the centrosomes of interphase and
CC mitotic cells. Detected at the cleavage furrow and/or the midbody.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=P04899-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04899-2; Sequence=VSP_017497;
CC Name=3;
CC IsoId=P04899-3; Sequence=VSP_043473;
CC Name=sGi2; Synonyms=sGalphai2;
CC IsoId=P04899-4; Sequence=VSP_043903;
CC Name=5;
CC IsoId=P04899-5; Sequence=VSP_054789;
CC Name=6;
CC IsoId=P04899-6; Sequence=VSP_054788;
CC -!- PTM: (Microbial infection) Deamidated at Gln-205 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 -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC {ECO:0000305}.
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DR EMBL; X04828; CAA28512.1; -; mRNA.
DR EMBL; J03004; AAA52556.1; ALT_SEQ; mRNA.
DR EMBL; M20593; AAA35894.1; -; Genomic_DNA.
DR EMBL; M20586; AAA35894.1; JOINED; Genomic_DNA.
DR EMBL; M20587; AAA35894.1; JOINED; Genomic_DNA.
DR EMBL; M20588; AAA35894.1; JOINED; Genomic_DNA.
DR EMBL; M20589; AAA35894.1; JOINED; Genomic_DNA.
DR EMBL; M20590; AAA35894.1; JOINED; Genomic_DNA.
DR EMBL; M20591; AAA35894.1; JOINED; Genomic_DNA.
DR EMBL; M20592; AAA35894.1; JOINED; Genomic_DNA.
DR EMBL; AY677118; AAT78421.1; -; mRNA.
DR EMBL; AF493906; AAM12620.1; -; mRNA.
DR EMBL; AK096299; BAG53252.1; -; mRNA.
DR EMBL; AK096595; BAG53334.1; -; mRNA.
DR EMBL; AK302330; BAG63662.1; -; mRNA.
DR EMBL; AK304473; BAG65287.1; -; mRNA.
DR EMBL; AC002077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U73166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U73169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65053.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW65055.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW65056.1; -; Genomic_DNA.
DR EMBL; BC012138; AAH12138.1; -; mRNA.
DR EMBL; BC016995; AAH16995.1; -; mRNA.
DR EMBL; X07854; CAA30703.1; -; Genomic_DNA.
DR CCDS; CCDS2813.1; -. [P04899-1]
DR CCDS; CCDS54587.1; -. [P04899-3]
DR CCDS; CCDS63642.1; -. [P04899-5]
DR CCDS; CCDS63644.1; -. [P04899-6]
DR PIR; S02319; RGHUI2.
DR RefSeq; NP_001159897.1; NM_001166425.1. [P04899-3]
DR RefSeq; NP_001269546.1; NM_001282617.1. [P04899-6]
DR RefSeq; NP_001269547.1; NM_001282618.1.
DR RefSeq; NP_001269548.1; NM_001282619.1. [P04899-2]
DR RefSeq; NP_001269549.1; NM_001282620.1. [P04899-5]
DR RefSeq; NP_002061.1; NM_002070.3. [P04899-1]
DR PDB; 6D9H; EM; 3.60 A; A=1-355.
DR PDB; 7F8V; EM; 3.30 A; A=1-355.
DR PDB; 7LD3; EM; 3.20 A; A=1-355.
DR PDB; 7LD4; EM; 3.30 A; A=1-355.
DR PDB; 7WVV; EM; 2.90 A; A=1-355.
DR PDB; 7WVW; EM; 3.10 A; A=1-355.
DR PDB; 7WVX; EM; 2.80 A; A=1-355.
DR PDB; 7WVY; EM; 3.00 A; A=1-355.
DR PDBsum; 6D9H; -.
DR PDBsum; 7F8V; -.
DR PDBsum; 7LD3; -.
DR PDBsum; 7LD4; -.
DR PDBsum; 7WVV; -.
DR PDBsum; 7WVW; -.
DR PDBsum; 7WVX; -.
DR PDBsum; 7WVY; -.
DR AlphaFoldDB; P04899; -.
DR SMR; P04899; -.
DR BioGRID; 109033; 207.
DR CORUM; P04899; -.
DR DIP; DIP-602N; -.
DR IntAct; P04899; 87.
DR MINT; P04899; -.
DR STRING; 9606.ENSP00000312999; -.
DR ChEMBL; CHEMBL4105887; -.
DR GlyGen; P04899; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; P04899; -.
DR MetOSite; P04899; -.
DR PhosphoSitePlus; P04899; -.
DR SwissPalm; P04899; -.
DR BioMuta; GNAI2; -.
DR DMDM; 121023; -.
DR CPTAC; CPTAC-1530; -.
DR CPTAC; CPTAC-1531; -.
DR EPD; P04899; -.
DR jPOST; P04899; -.
DR MassIVE; P04899; -.
DR MaxQB; P04899; -.
DR PaxDb; P04899; -.
DR PeptideAtlas; P04899; -.
DR PRIDE; P04899; -.
DR ProteomicsDB; 3695; -.
DR ProteomicsDB; 51752; -. [P04899-1]
DR ProteomicsDB; 51753; -. [P04899-2]
DR ProteomicsDB; 51754; -. [P04899-3]
DR ProteomicsDB; 51755; -. [P04899-4]
DR ProteomicsDB; 5863; -.
DR Antibodypedia; 2180; 297 antibodies from 35 providers.
DR DNASU; 2771; -.
DR Ensembl; ENST00000266027.9; ENSP00000266027.6; ENSG00000114353.17. [P04899-6]
DR Ensembl; ENST00000313601.11; ENSP00000312999.6; ENSG00000114353.17. [P04899-1]
DR Ensembl; ENST00000422163.5; ENSP00000406871.1; ENSG00000114353.17. [P04899-5]
DR Ensembl; ENST00000440628.5; ENSP00000395736.1; ENSG00000114353.17. [P04899-6]
DR Ensembl; ENST00000451956.1; ENSP00000406369.1; ENSG00000114353.17. [P04899-3]
DR GeneID; 2771; -.
DR KEGG; hsa:2771; -.
DR MANE-Select; ENST00000313601.11; ENSP00000312999.6; NM_002070.4; NP_002061.1.
DR UCSC; uc003cyp.3; human. [P04899-1]
DR CTD; 2771; -.
DR DisGeNET; 2771; -.
DR GeneCards; GNAI2; -.
DR HGNC; HGNC:4385; GNAI2.
DR HPA; ENSG00000114353; Low tissue specificity.
DR MalaCards; GNAI2; -.
DR MIM; 139360; gene.
DR neXtProt; NX_P04899; -.
DR OpenTargets; ENSG00000114353; -.
DR PharmGKB; PA24347; -.
DR VEuPathDB; HostDB:ENSG00000114353; -.
DR eggNOG; KOG0082; Eukaryota.
DR GeneTree; ENSGT00940000155125; -.
DR HOGENOM; CLU_014184_6_0_1; -.
DR InParanoid; P04899; -.
DR OMA; XYLNDER; -.
DR PhylomeDB; P04899; -.
DR TreeFam; TF300673; -.
DR PathwayCommons; P04899; -.
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; P04899; -.
DR SIGNOR; P04899; -.
DR BioGRID-ORCS; 2771; 34 hits in 1080 CRISPR screens.
DR ChiTaRS; GNAI2; human.
DR GeneWiki; GNAI2; -.
DR GenomeRNAi; 2771; -.
DR Pharos; P04899; Tchem.
DR PRO; PR:P04899; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P04899; protein.
DR Bgee; ENSG00000114353; Expressed in granulocyte and 201 other tissues.
DR ExpressionAtlas; P04899; baseline and differential.
DR Genevisible; P04899; HS.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IBA:GO_Central.
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:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0140199; P:negative regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; IEA:Ensembl.
DR GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
DR GO; GO:1903614; P:negative regulation of protein tyrosine phosphatase activity; IEA:Ensembl.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; IEA:Ensembl.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR GO; GO:0035810; P:positive regulation of urine volume; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0051924; P:regulation of calcium ion transport; IEA:Ensembl.
DR GO; GO:0007584; P:response to nutrient; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00066; G-alpha; 1.
DR Gene3D; 1.10.400.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; PTHR10218; 1.
DR Pfam; PF00503; G-alpha; 1.
DR PRINTS; PR00318; GPROTEINA.
DR PRINTS; PR00441; GPROTEINAI.
DR SMART; SM00275; G_alpha; 1.
DR SUPFAM; SSF47895; SSF47895; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51882; G_ALPHA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Alternative splicing; Cell cycle;
KW Cell division; Cell membrane; Cytoplasm; Cytoskeleton; GTP-binding;
KW Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate;
KW Nucleotide-binding; Palmitate; Reference proteome; Transducer.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:22223895,
FT ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..355
FT /note="Guanine nucleotide-binding protein G(i) subunit
FT alpha-2"
FT /id="PRO_0000203679"
FT DOMAIN 32..355
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 174..182
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 197..206
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 266..273
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT REGION 325..330
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63096"
FT BINDING 47
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 176..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 201..205
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63096"
FT BINDING 270..273
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P63096"
FT BINDING 327
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 179
FT /note="ADP-ribosylarginine; by cholera toxin"
FT /evidence="ECO:0000250"
FT MOD_RES 205
FT /note="Deamidated glutamine; by Photorhabdus PAU_02230"
FT /evidence="ECO:0000269|PubMed:24141704"
FT MOD_RES 352
FT /note="ADP-ribosylcysteine; by pertussis toxin"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:22223895,
FT ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..52
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054788"
FT VAR_SEQ 1..39
FT /note="MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLL -> MEYAGHLPA
FT SSAQGTILACTSCT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017497"
FT VAR_SEQ 1..39
FT /note="MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLL -> MR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043473"
FT VAR_SEQ 1..39
FT /note="MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLL -> MTEGVKTLG
FT WTKQKGGCHWGRSE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054789"
FT VAR_SEQ 332..355
FT /note="NVQFVFDAVTDVIIKNNLKDCGLF -> SRKLFRETYLKLSGPDQHPHPSPA
FT PAPPLSSDSVP (in isoform sGi2)"
FT /evidence="ECO:0000303|PubMed:17550964"
FT /id="VSP_043903"
FT HELIX 12..29
FT /evidence="ECO:0007829|PDB:7LD3"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:7LD3"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:7LD3"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:7LD3"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:7LD3"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:7F8V"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:7F8V"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:7F8V"
FT STRAND 261..270
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:7LD3"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 297..309
FT /evidence="ECO:0007829|PDB:7LD3"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:7LD3"
FT STRAND 320..324
FT /evidence="ECO:0007829|PDB:7LD3"
FT HELIX 329..352
FT /evidence="ECO:0007829|PDB:7LD3"
SQ SEQUENCE 355 AA; 40451 MW; BE6D6FF720CF3DCC CRC64;
MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG
YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPSR ADDARQLFAL SCTAEEQGVL
PDDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV
KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE
MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT HSPLTICFPE YTGANKYDEA
ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF
