GBB1_HUMAN
ID GBB1_HUMAN Reviewed; 340 AA.
AC P62873; B1AJZ7; P04697; P04901; Q1RMY8;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1;
DE AltName: Full=Transducin beta chain 1;
GN Name=GNB1 {ECO:0000312|HGNC:HGNC:4396};
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).
RC TISSUE=Liver;
RX PubMed=3095147; DOI=10.1016/0014-5793(86)81486-7;
RA Codina J., Stengel D., Woo S.L.C., Birnbaumer L.;
RT "Beta-subunits of the human liver Gs/Gi signal-transducing proteins and
RT those of bovine retinal rod cell transducin are identical.";
RL FEBS Lett. 207:187-192(1986).
RN [2]
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 [3]
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Muscle, and Uterus;
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 [8]
RP PROTEIN SEQUENCE OF 2-15; 58-89; 284-301 AND 305-314, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma, and Melanoma;
RA Bienvenut W.V., Quadroni M.;
RL Submitted (JUL-2005) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 2-8; 69-78 AND 90-96, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 23-42; 58-78; 138-150; 198-209 AND 315-337, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP INTERACTION WITH ARHGEF18.
RX PubMed=14512443; DOI=10.1161/01.res.0000097607.14733.0c;
RA Niu J., Profirovic J., Pan H., Vaiskunaite R., Voyno-Yasenetskaya T.;
RT "G Protein betagamma subunits stimulate p114RhoGEF, a guanine nucleotide
RT exchange factor for RhoA and Rac1: regulation of cell shape and reactive
RT oxygen species production.";
RL Circ. Res. 93:848-856(2003).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INTERACTION WITH RASD2.
RX PubMed=19255495; DOI=10.1159/000204075;
RA Hill C., Goddard A., Ladds G., Davey J.;
RT "The cationic region of Rhes mediates its interactions with specific Gbeta
RT subunits.";
RL Cell. Physiol. Biochem. 23:1-8(2009).
RN [14]
RP INTERACTION WITH ARHGEF5.
RX PubMed=19713215; DOI=10.1074/jbc.m109.047282;
RA Wang Z., Kumamoto Y., Wang P., Gan X., Lehmann D., Smrcka A.V., Cohn L.,
RA Iwasaki A., Li L., Wu D.;
RT "Regulation of immature dendritic cell migration by RhoA guanine nucleotide
RT exchange factor Arhgef5.";
RL J. Biol. Chem. 284:28599-28606(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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19]
RP INVOLVEMENT IN MRD42, AND VARIANTS MRD42 GLU-76; GLY-76; SER-77; ARG-78;
RP ASN-80; THR-80; PRO-95; VAL-101 AND THR-326.
RX PubMed=27108799; DOI=10.1016/j.ajhg.2016.03.011;
RG University of Washington Center for Mendelian Genomics;
RA Petrovski S., Kuery S., Myers C.T., Anyane-Yeboa K., Cogne B., Bialer M.,
RA Xia F., Hemati P., Riviello J., Mehaffey M., Besnard T., Becraft E.,
RA Wadley A., Politi A.R., Colombo S., Zhu X., Ren Z., Andrews I.,
RA Dudding-Byth T., Schneider A.L., Wallace G., Rosen A.B., Schelley S.,
RA Enns G.M., Corre P., Dalton J., Mercier S., Latypova X., Schmitt S.,
RA Guzman E., Moore C., Bier L., Heinzen E.L., Karachunski P., Shur N.,
RA Grebe T., Basinger A., Nguyen J.M., Bezieau S., Wierenga K.,
RA Bernstein J.A., Scheffer I.E., Rosenfeld J.A., Mefford H.C., Isidor B.,
RA Goldstein D.B.;
RT "Germline de novo mutations in GNB1 cause severe neurodevelopmental
RT disability, hypotonia, and seizures.";
RL Am. J. Hum. Genet. 98:1001-1010(2016).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GNG2.
RX PubMed=18611381; DOI=10.1016/j.str.2008.04.010;
RA Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.;
RT "Structure of the parathyroid hormone receptor C terminus bound to the G-
RT protein dimer Gbeta1gamma2.";
RL Structure 16:1086-1094(2008).
RN [21]
RP ERRATUM OF PUBMED:18611381, AND RETRACTION NOTICE OF PUBMED:18611381.
RX PubMed=21827955; DOI=10.1016/j.str.2011.07.010;
RA Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.;
RL Structure 19:1200-1200(2011).
RN [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 2-340 IN COMPLEX WITH
RP GNAI1; GNG2 AND HHV-5 US27, AND STRUCTURE BY ELECTRON MICROSCOPY (3.50
RP ANGSTROMS) OF 2-340 IN COMPLEX WITH GNA11; GNG2; CX3CL1 AND HHV-5 US28.
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 [23]
RP CHARACTERIZATION OF VARIANTS MRD42 ASN-80 AND THR-80.
RX PubMed=25485910; DOI=10.1038/nm.3751;
RA Yoda A., Adelmant G., Tamburini J., Chapuy B., Shindoh N., Yoda Y.,
RA Weigert O., Kopp N., Wu S.C., Kim S.S., Liu H., Tivey T., Christie A.L.,
RA Elpek K.G., Card J., Gritsman K., Gotlib J., Deininger M.W., Makishima H.,
RA Turley S.J., Javidi-Sharifi N., Maciejewski J.P., Jaiswal S., Ebert B.L.,
RA Rodig S.J., Tyner J.W., Marto J.A., Weinstock D.M., Lane A.A.;
RT "Mutations in G protein beta subunits promote transformation and kinase
RT inhibitor resistance.";
RL Nat. Med. 21:71-75(2015).
RN [24]
RP VARIANT MRD42 GLY-118.
RX PubMed=27668284; DOI=10.1212/nxg.0000000000000106;
RA Steinruecke S., Lohmann K., Domingo A., Rolfs A., Baeumer T., Spiegler J.,
RA Hartmann C., Muenchau A.;
RT "Novel GNB1 missense mutation in a patient with generalized dystonia,
RT hypotonia, and intellectual disability.";
RL Neurol. Genet. 2:E106-E106(2016).
RN [25]
RP VARIANTS MRD42 PHE-30; GLY-52; VAL-64; ARG-91; THR-92; SER-94; LEU-96;
RP THR-106; GLY-118 AND GLN-337, AND CHARACTERIZATION OF VARIANTS MRD42
RP PHE-30; GLY-52; VAL-64; ARG-91; THR-92; SER-94; LEU-96; THR-106; GLY-118
RP AND GLN-337.
RX PubMed=28087732; DOI=10.1093/hmg/ddx018;
RA Lohmann K., Masuho I., Patil D.N., Baumann H., Hebert E., Steinruecke S.,
RA Trujillano D., Skamangas N.K., Dobricic V., Huening I.,
RA Gillessen-Kaesbach G., Westenberger A., Savic-Pavicevic D., Muenchau A.,
RA Oprea G., Klein C., Rolfs A., Martemyanov K.A.;
RT "Novel GNB1 mutations disrupt assembly and function of G protein
RT heterotrimers and cause global developmental delay in humans.";
RL Hum. Mol. Genet. 26:1078-1086(2017).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC as a modulator or transducer in various transmembrane signaling
CC systems. The beta and gamma chains are required for the GTPase
CC activity, for replacement of GDP by GTP, and for G protein-effector
CC interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma (By
CC similarity). The heterodimer formed by GNB1 and GNG2 interacts with
CC ARHGEF5 (PubMed:19713215). The heterodimer formed by GNB1 and GNG2
CC interacts with GRK2 (By similarity). Interacts with ARHGEF18 and RASD2
CC (PubMed:14512443, PubMed:19255495). {ECO:0000250|UniProtKB:P62871,
CC ECO:0000269|PubMed:14512443, ECO:0000269|PubMed:19255495,
CC ECO:0000269|PubMed:19713215}.
CC -!- INTERACTION:
CC P62873; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-357130, EBI-11962928;
CC P62873; Q92782-2: DPF1; NbExp=3; IntAct=EBI-357130, EBI-23669343;
CC P62873; P59768: GNG2; NbExp=6; IntAct=EBI-357130, EBI-602681;
CC P62873; P42858: HTT; NbExp=10; IntAct=EBI-357130, EBI-466029;
CC P62873; P19878: NCF2; NbExp=2; IntAct=EBI-357130, EBI-489611;
CC P62873; P07237: P4HB; NbExp=3; IntAct=EBI-357130, EBI-395883;
CC P62873; Q08AM6: VAC14; NbExp=3; IntAct=EBI-357130, EBI-2107455;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62873-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62873-2; Sequence=VSP_055232;
CC -!- PTM: Phosphorylation at His-266 by NDKB contributes to G protein
CC activation by increasing the high energetic phosphate transfer onto
CC GDP. {ECO:0000250}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 42
CC (MRD42) [MIM:616973]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRD42
CC patients manifest global developmental delay commonly accompanied by
CC hypotonia, seizures of various types, ophthalmological manifestations,
CC and poor growth. {ECO:0000269|PubMed:25485910,
CC ECO:0000269|PubMed:27108799, ECO:0000269|PubMed:27668284,
CC ECO:0000269|PubMed:28087732}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; X04526; CAA28207.1; -; mRNA.
DR EMBL; AF501882; AAM15918.1; -; mRNA.
DR EMBL; BT007305; AAP35969.1; -; mRNA.
DR EMBL; CR456784; CAG33065.1; -; mRNA.
DR EMBL; AL031282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56147.1; -; Genomic_DNA.
DR EMBL; BC004186; AAH04186.1; -; mRNA.
DR EMBL; BC005888; AAH05888.1; -; mRNA.
DR EMBL; BC008991; AAH08991.1; -; mRNA.
DR EMBL; BC114618; AAI14619.1; -; mRNA.
DR EMBL; M36430; AAA63265.1; -; mRNA.
DR CCDS; CCDS34.1; -. [P62873-1]
DR PIR; A24853; RGHUB1.
DR RefSeq; NP_001269467.1; NM_001282538.1.
DR RefSeq; NP_001269468.1; NM_001282539.1. [P62873-1]
DR RefSeq; NP_002065.1; NM_002074.4. [P62873-1]
DR RefSeq; XP_016856548.1; XM_017001059.1. [P62873-1]
DR RefSeq; XP_016856549.1; XM_017001060.1. [P62873-1]
DR RefSeq; XP_016856550.1; XM_017001061.1. [P62873-1]
DR PDB; 4KFM; X-ray; 3.45 A; B=1-340.
DR PDB; 4PNK; X-ray; 2.56 A; B=1-340.
DR PDB; 5HE0; X-ray; 2.56 A; B=2-340.
DR PDB; 5HE1; X-ray; 3.15 A; B=2-340.
DR PDB; 5HE2; X-ray; 2.79 A; B=2-340.
DR PDB; 5HE3; X-ray; 2.74 A; B=2-340.
DR PDB; 5UKK; X-ray; 2.60 A; B=2-340.
DR PDB; 5UKL; X-ray; 2.15 A; B=2-340.
DR PDB; 5UKM; X-ray; 3.03 A; B=2-340.
DR PDB; 5UZ7; EM; 4.10 A; B=2-340.
DR PDB; 6B3J; EM; 3.30 A; B=2-340.
DR PDB; 6CRK; X-ray; 2.00 A; B=2-340.
DR PDB; 6D9H; EM; 3.60 A; B=2-340.
DR PDB; 6DDE; EM; 3.50 A; B=2-340.
DR PDB; 6DDF; EM; 3.50 A; B=2-340.
DR PDB; 6E3Y; EM; 3.30 A; B=2-340.
DR PDB; 6EG8; X-ray; 2.80 A; A/B/D/F=2-340.
DR PDB; 6G79; EM; 3.78 A; B=2-340.
DR PDB; 6GDG; EM; 4.11 A; B=2-340.
DR PDB; 6KPF; EM; 2.90 A; B=1-340.
DR PDB; 6KPG; EM; 3.00 A; B=2-340.
DR PDB; 6LFM; EM; 3.50 A; B=2-340.
DR PDB; 6LFO; EM; 3.40 A; B=2-340.
DR PDB; 6LI3; EM; 3.32 A; B=1-340.
DR PDB; 6LMK; EM; 3.70 A; B=2-340.
DR PDB; 6LML; EM; 3.90 A; B=2-340.
DR PDB; 6M1H; EM; 3.60 A; E=1-340.
DR PDB; 6M1I; EM; 3.50 A; E=1-340.
DR PDB; 6M8S; X-ray; 3.71 A; C/D/G/H/K=2-340.
DR PDB; 6N4B; EM; 3.00 A; B=2-340.
DR PDB; 6NI3; EM; 3.80 A; B=2-340.
DR PDB; 6NIY; EM; 3.34 A; B=1-340.
DR PDB; 6OIJ; EM; 3.30 A; B=2-340.
DR PDB; 6OIK; EM; 3.60 A; B=2-340.
DR PDB; 6OMM; EM; 3.17 A; B=2-340.
DR PDB; 6ORV; EM; 3.00 A; BP=2-340.
DR PDB; 6OS9; EM; 3.00 A; B=2-340.
DR PDB; 6OSA; EM; 3.00 A; B=2-340.
DR PDB; 6OT0; EM; 3.90 A; B=2-340.
DR PDB; 6P9X; EM; 2.91 A; B=2-340.
DR PDB; 6P9Y; EM; 3.01 A; B=2-340.
DR PDB; 6PB0; EM; 3.00 A; B=2-340.
DR PDB; 6PB1; EM; 2.80 A; B=2-340.
DR PDB; 6PT0; EM; 3.20 A; B=2-340.
DR PDB; 6UUN; EM; 3.00 A; B=2-340.
DR PDB; 6UUS; EM; 2.40 A; B=2-340.
DR PDB; 6UVA; EM; 2.30 A; B=2-340.
DR PDB; 6VCB; EM; 3.30 A; B=2-340.
DR PDB; 6VMS; EM; 3.80 A; B=1-340.
DR PDB; 6VN7; EM; 3.20 A; B=2-340.
DR PDB; 6WHA; EM; 3.36 A; C=2-340.
DR PDB; 6WHC; EM; 3.40 A; B=1-340.
DR PDB; 6WI9; EM; 4.30 A; B=1-340.
DR PDB; 6WPW; EM; 3.10 A; D=2-340.
DR PDB; 6WZG; EM; 2.30 A; B=1-340.
DR PDB; 6X18; EM; 2.10 A; B=2-340.
DR PDB; 6X19; EM; 2.10 A; B=2-340.
DR PDB; 6X1A; EM; 2.50 A; B=2-340.
DR PDB; 6XBJ; EM; 3.88 A; B=2-340.
DR PDB; 6XBK; EM; 3.24 A; B=2-340.
DR PDB; 6XBL; EM; 3.90 A; B=2-340.
DR PDB; 6XBM; EM; 3.15 A; B=2-340.
DR PDB; 6XOX; EM; 3.10 A; B=2-340.
DR PDB; 7AUE; EM; 2.97 A; B=2-340.
DR PDB; 7BB6; EM; 4.20 A; C=2-340.
DR PDB; 7BB7; EM; 4.40 A; C=2-340.
DR PDB; 7C2E; EM; 4.20 A; B=2-340.
DR PDB; 7CFM; EM; 3.00 A; B=2-340.
DR PDB; 7CFN; EM; 3.00 A; B=2-340.
DR PDB; 7CKW; EM; 3.22 A; B=2-340.
DR PDB; 7CKX; EM; 3.54 A; B=2-340.
DR PDB; 7CKY; EM; 3.20 A; B=2-340.
DR PDB; 7CKZ; EM; 3.10 A; B=2-340.
DR PDB; 7CMU; EM; 3.00 A; B=2-340.
DR PDB; 7CMV; EM; 2.70 A; B=2-340.
DR PDB; 7CRH; EM; 3.30 A; B=2-340.
DR PDB; 7CX2; EM; 2.80 A; B=2-340.
DR PDB; 7CX3; EM; 2.80 A; B=2-340.
DR PDB; 7CX4; EM; 2.90 A; B=2-340.
DR PDB; 7D76; EM; 3.10 A; B=1-340.
DR PDB; 7D77; EM; 2.90 A; B=1-340.
DR PDB; 7D7M; EM; 3.30 A; B=2-340.
DR PDB; 7DB6; EM; 3.30 A; B=1-340.
DR PDB; 7DFL; EM; 3.30 A; B=2-340.
DR PDB; 7E2X; EM; 3.00 A; B=2-340.
DR PDB; 7E2Y; EM; 3.00 A; B=2-340.
DR PDB; 7E2Z; EM; 3.10 A; B=2-340.
DR PDB; 7E32; EM; 2.90 A; B=2-340.
DR PDB; 7E33; EM; 2.90 A; B=2-340.
DR PDB; 7E9G; EM; 3.50 A; B=2-340.
DR PDB; 7E9H; EM; 4.00 A; B=2-340.
DR PDB; 7EB2; EM; 3.50 A; B=2-340.
DR PDB; 7EJ0; EM; 3.20 A; B=2-340.
DR PDB; 7EJ8; EM; 3.00 A; B=2-340.
DR PDB; 7EJA; EM; 3.60 A; B=2-340.
DR PDB; 7EJK; EM; 3.40 A; B=2-340.
DR PDB; 7EJX; EM; 2.40 A; B=2-340.
DR PDB; 7EO2; EM; 2.89 A; C=2-340.
DR PDB; 7EO4; EM; 2.86 A; C=2-340.
DR PDB; 7EVW; EM; 3.22 A; B=1-340.
DR PDB; 7EVY; EM; 2.98 A; B=2-340.
DR PDB; 7EVZ; EM; 3.07 A; B=2-340.
DR PDB; 7EW0; EM; 3.42 A; B=2-340.
DR PDB; 7EW1; EM; 3.40 A; B=2-340.
DR PDB; 7EW2; EM; 3.10 A; B=2-340.
DR PDB; 7EW3; EM; 3.10 A; B=2-340.
DR PDB; 7EW4; EM; 3.20 A; B=2-340.
DR PDB; 7EW7; EM; 3.27 A; B=2-340.
DR PDB; 7EXD; EM; 3.40 A; B=2-340.
DR PDB; 7EZH; EM; 3.20 A; B=2-340.
DR PDB; 7EZK; EM; 3.10 A; B=2-340.
DR PDB; 7EZM; EM; 2.90 A; B=2-340.
DR PDB; 7F1Q; EM; 2.90 A; B=1-340.
DR PDB; 7F1R; EM; 3.00 A; B=1-340.
DR PDB; 7F1S; EM; 2.80 A; B=1-340.
DR PDB; 7F4D; EM; 3.00 A; B=2-340.
DR PDB; 7F4F; EM; 2.90 A; B=2-340.
DR PDB; 7F4H; EM; 2.70 A; B=2-340.
DR PDB; 7F4I; EM; 3.10 A; B=2-340.
DR PDB; 7F53; EM; 3.00 A; B=2-340.
DR PDB; 7F54; EM; 3.00 A; B=2-340.
DR PDB; 7F55; EM; 3.10 A; B=2-340.
DR PDB; 7F58; EM; 3.10 A; B=2-340.
DR PDB; 7F6H; EM; 2.90 A; C=2-340.
DR PDB; 7F6I; EM; 2.80 A; C=2-340.
DR PDB; 7F8V; EM; 3.30 A; B=2-340.
DR PDB; 7F8W; EM; 3.10 A; B=2-340.
DR PDB; 7F9Y; EM; 2.90 A; B=2-340.
DR PDB; 7F9Z; EM; 3.20 A; B=2-340.
DR PDB; 7JHJ; EM; 3.20 A; B=2-340.
DR PDB; 7JOZ; X-ray; 3.80 A; B=2-340.
DR PDB; 7JV5; EM; 3.00 A; B=2-340.
DR PDB; 7JVP; EM; 2.90 A; B=2-340.
DR PDB; 7JVQ; EM; 3.00 A; B=2-340.
DR PDB; 7JVR; EM; 2.80 A; B=2-340.
DR PDB; 7K7L; X-ray; 2.54 A; B=2-340.
DR PDB; 7K7Z; X-ray; 2.61 A; B=2-340.
DR PDB; 7KH0; EM; 2.80 A; B=2-340.
DR PDB; 7KI0; EM; 2.50 A; B=2-340.
DR PDB; 7KI1; EM; 2.50 A; B=2-340.
DR PDB; 7L0P; EM; 4.10 A; B=2-340.
DR PDB; 7L0Q; EM; 4.30 A; B=2-340.
DR PDB; 7L0R; EM; 4.20 A; B=2-340.
DR PDB; 7L0S; EM; 4.50 A; B=2-340.
DR PDB; 7L1U; EM; 3.20 A; B=2-340.
DR PDB; 7L1V; EM; 3.00 A; B=2-340.
DR PDB; 7LCI; EM; 2.90 A; B=2-340.
DR PDB; 7LD3; EM; 3.20 A; B=2-340.
DR PDB; 7LD4; EM; 3.30 A; B=2-340.
DR PDB; 7LLL; EM; 3.70 A; B=2-340.
DR PDB; 7LLY; EM; 3.30 A; B=2-340.
DR PDB; 7MTS; EM; 3.20 A; D=2-340.
DR PDB; 7NA7; EM; 2.70 A; B=1-340.
DR PDB; 7NA8; EM; 2.70 A; B=1-340.
DR PDB; 7P00; EM; 2.71 A; B=2-340.
DR PDB; 7P02; EM; 2.87 A; B=2-340.
DR PDB; 7RA3; EM; 3.24 A; B=2-340.
DR PDB; 7RBT; EM; 3.08 A; B=2-340.
DR PDB; 7RG9; EM; 3.20 A; B=2-340.
DR PDB; 7RGP; EM; 2.90 A; B=2-340.
DR PDB; 7RKF; EM; 4.00 A; B=2-340.
DR PDB; 7RKM; EM; 3.50 A; B=2-340.
DR PDB; 7RKN; EM; 3.60 A; B=2-340.
DR PDB; 7RKX; EM; 3.10 A; B=2-340.
DR PDB; 7RKY; EM; 3.80 A; B=2-340.
DR PDB; 7RMG; EM; 3.00 A; B=2-340.
DR PDB; 7RMH; EM; 3.10 A; B=2-340.
DR PDB; 7RMI; EM; 3.20 A; B=2-340.
DR PDB; 7RTB; EM; 2.14 A; B=2-340.
DR PDB; 7RYC; EM; 2.90 A; C=2-340.
DR PDB; 7S1M; EM; 2.41 A; B=2-340.
DR PDB; 7S3I; EM; 2.51 A; B=2-340.
DR PDB; 7S8L; EM; 2.45 A; C=2-340.
DR PDB; 7S8M; EM; 2.54 A; C=2-340.
DR PDB; 7S8N; EM; 2.90 A; C=2-340.
DR PDB; 7S8O; EM; 2.58 A; C=2-340.
DR PDB; 7S8P; EM; 2.60 A; C=2-340.
DR PDB; 7T10; EM; 2.50 A; B=2-340.
DR PDB; 7T11; EM; 2.70 A; B=2-340.
DR PDB; 7T6B; EM; 3.19 A; C=2-340.
DR PDB; 7TUZ; EM; 3.12 A; B=2-340.
DR PDB; 7TYF; EM; 2.20 A; B=2-340.
DR PDB; 7TYH; EM; 3.30 A; B=2-340.
DR PDB; 7TYI; EM; 3.30 A; B=2-340.
DR PDB; 7TYL; EM; 3.30 A; B=2-340.
DR PDB; 7TYN; EM; 2.60 A; B=2-340.
DR PDB; 7TYO; EM; 2.70 A; B=2-340.
DR PDB; 7TYW; EM; 3.00 A; B=2-340.
DR PDB; 7TYX; EM; 2.55 A; B=2-340.
DR PDB; 7TYY; EM; 3.00 A; B=2-340.
DR PDB; 7TZF; EM; 2.40 A; B=2-340.
DR PDB; 7VDH; EM; 2.90 A; B=2-340.
DR PDB; 7VDL; EM; 3.22 A; B=2-340.
DR PDB; 7VDM; EM; 2.98 A; B=2-340.
DR PDB; 7VGX; EM; 3.20 A; B=2-340.
DR PDB; 7VKT; EM; 2.90 A; C=2-340.
DR PDB; 7VL8; EM; 2.90 A; B=2-340.
DR PDB; 7VL9; EM; 2.60 A; B=2-340.
DR PDB; 7VLA; EM; 2.70 A; B=2-340.
DR PDB; 7VUG; EM; 3.20 A; B=2-340.
DR PDB; 7VUH; EM; 3.22 A; B=2-340.
DR PDB; 7VUI; EM; 3.30 A; B=2-340.
DR PDB; 7VUJ; EM; 3.80 A; B=2-340.
DR PDB; 7VUY; EM; 2.84 A; B=2-340.
DR PDB; 7VUZ; EM; 2.89 A; B=2-340.
DR PDB; 7VV3; EM; 2.97 A; B=2-340.
DR PDB; 7VV5; EM; 2.76 A; B=2-340.
DR PDB; 7W2Z; EM; 2.80 A; B=2-340.
DR PDB; 7WF7; EM; 3.40 A; C=2-340.
DR PDB; 7WVU; EM; 3.30 A; B=2-340.
DR PDB; 7WVV; EM; 2.90 A; B=2-340.
DR PDB; 7WVW; EM; 3.10 A; B=2-340.
DR PDB; 7WVX; EM; 2.80 A; B=2-340.
DR PDB; 7WVY; EM; 3.00 A; B=2-340.
DR PDBsum; 4KFM; -.
DR PDBsum; 4PNK; -.
DR PDBsum; 5HE0; -.
DR PDBsum; 5HE1; -.
DR PDBsum; 5HE2; -.
DR PDBsum; 5HE3; -.
DR PDBsum; 5UKK; -.
DR PDBsum; 5UKL; -.
DR PDBsum; 5UKM; -.
DR PDBsum; 5UZ7; -.
DR PDBsum; 6B3J; -.
DR PDBsum; 6CRK; -.
DR PDBsum; 6D9H; -.
DR PDBsum; 6DDE; -.
DR PDBsum; 6DDF; -.
DR PDBsum; 6E3Y; -.
DR PDBsum; 6EG8; -.
DR PDBsum; 6G79; -.
DR PDBsum; 6GDG; -.
DR PDBsum; 6KPF; -.
DR PDBsum; 6KPG; -.
DR PDBsum; 6LFM; -.
DR PDBsum; 6LFO; -.
DR PDBsum; 6LI3; -.
DR PDBsum; 6LMK; -.
DR PDBsum; 6LML; -.
DR PDBsum; 6M1H; -.
DR PDBsum; 6M1I; -.
DR PDBsum; 6M8S; -.
DR PDBsum; 6N4B; -.
DR PDBsum; 6NI3; -.
DR PDBsum; 6NIY; -.
DR PDBsum; 6OIJ; -.
DR PDBsum; 6OIK; -.
DR PDBsum; 6OMM; -.
DR PDBsum; 6ORV; -.
DR PDBsum; 6OS9; -.
DR PDBsum; 6OSA; -.
DR PDBsum; 6OT0; -.
DR PDBsum; 6P9X; -.
DR PDBsum; 6P9Y; -.
DR PDBsum; 6PB0; -.
DR PDBsum; 6PB1; -.
DR PDBsum; 6PT0; -.
DR PDBsum; 6UUN; -.
DR PDBsum; 6UUS; -.
DR PDBsum; 6UVA; -.
DR PDBsum; 6VCB; -.
DR PDBsum; 6VMS; -.
DR PDBsum; 6VN7; -.
DR PDBsum; 6WHA; -.
DR PDBsum; 6WHC; -.
DR PDBsum; 6WI9; -.
DR PDBsum; 6WPW; -.
DR PDBsum; 6WZG; -.
DR PDBsum; 6X18; -.
DR PDBsum; 6X19; -.
DR PDBsum; 6X1A; -.
DR PDBsum; 6XBJ; -.
DR PDBsum; 6XBK; -.
DR PDBsum; 6XBL; -.
DR PDBsum; 6XBM; -.
DR PDBsum; 6XOX; -.
DR PDBsum; 7AUE; -.
DR PDBsum; 7BB6; -.
DR PDBsum; 7BB7; -.
DR PDBsum; 7C2E; -.
DR PDBsum; 7CFM; -.
DR PDBsum; 7CFN; -.
DR PDBsum; 7CKW; -.
DR PDBsum; 7CKX; -.
DR PDBsum; 7CKY; -.
DR PDBsum; 7CKZ; -.
DR PDBsum; 7CMU; -.
DR PDBsum; 7CMV; -.
DR PDBsum; 7CRH; -.
DR PDBsum; 7CX2; -.
DR PDBsum; 7CX3; -.
DR PDBsum; 7CX4; -.
DR PDBsum; 7D76; -.
DR PDBsum; 7D77; -.
DR PDBsum; 7D7M; -.
DR PDBsum; 7DB6; -.
DR PDBsum; 7DFL; -.
DR PDBsum; 7E2X; -.
DR PDBsum; 7E2Y; -.
DR PDBsum; 7E2Z; -.
DR PDBsum; 7E32; -.
DR PDBsum; 7E33; -.
DR PDBsum; 7E9G; -.
DR PDBsum; 7E9H; -.
DR PDBsum; 7EB2; -.
DR PDBsum; 7EJ0; -.
DR PDBsum; 7EJ8; -.
DR PDBsum; 7EJA; -.
DR PDBsum; 7EJK; -.
DR PDBsum; 7EJX; -.
DR PDBsum; 7EO2; -.
DR PDBsum; 7EO4; -.
DR PDBsum; 7EVW; -.
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; 7F53; -.
DR PDBsum; 7F54; -.
DR PDBsum; 7F55; -.
DR PDBsum; 7F58; -.
DR PDBsum; 7F6H; -.
DR PDBsum; 7F6I; -.
DR PDBsum; 7F8V; -.
DR PDBsum; 7F8W; -.
DR PDBsum; 7F9Y; -.
DR PDBsum; 7F9Z; -.
DR PDBsum; 7JHJ; -.
DR PDBsum; 7JOZ; -.
DR PDBsum; 7JV5; -.
DR PDBsum; 7JVP; -.
DR PDBsum; 7JVQ; -.
DR PDBsum; 7JVR; -.
DR PDBsum; 7K7L; -.
DR PDBsum; 7K7Z; -.
DR PDBsum; 7KH0; -.
DR PDBsum; 7KI0; -.
DR PDBsum; 7KI1; -.
DR PDBsum; 7L0P; -.
DR PDBsum; 7L0Q; -.
DR PDBsum; 7L0R; -.
DR PDBsum; 7L0S; -.
DR PDBsum; 7L1U; -.
DR PDBsum; 7L1V; -.
DR PDBsum; 7LCI; -.
DR PDBsum; 7LD3; -.
DR PDBsum; 7LD4; -.
DR PDBsum; 7LLL; -.
DR PDBsum; 7LLY; -.
DR PDBsum; 7MTS; -.
DR PDBsum; 7NA7; -.
DR PDBsum; 7NA8; -.
DR PDBsum; 7P00; -.
DR PDBsum; 7P02; -.
DR PDBsum; 7RA3; -.
DR PDBsum; 7RBT; -.
DR PDBsum; 7RG9; -.
DR PDBsum; 7RGP; -.
DR PDBsum; 7RKF; -.
DR PDBsum; 7RKM; -.
DR PDBsum; 7RKN; -.
DR PDBsum; 7RKX; -.
DR PDBsum; 7RKY; -.
DR PDBsum; 7RMG; -.
DR PDBsum; 7RMH; -.
DR PDBsum; 7RMI; -.
DR PDBsum; 7RTB; -.
DR PDBsum; 7RYC; -.
DR PDBsum; 7S1M; -.
DR PDBsum; 7S3I; -.
DR PDBsum; 7S8L; -.
DR PDBsum; 7S8M; -.
DR PDBsum; 7S8N; -.
DR PDBsum; 7S8O; -.
DR PDBsum; 7S8P; -.
DR PDBsum; 7T10; -.
DR PDBsum; 7T11; -.
DR PDBsum; 7T6B; -.
DR PDBsum; 7TUZ; -.
DR PDBsum; 7TYF; -.
DR PDBsum; 7TYH; -.
DR PDBsum; 7TYI; -.
DR PDBsum; 7TYL; -.
DR PDBsum; 7TYN; -.
DR PDBsum; 7TYO; -.
DR PDBsum; 7TYW; -.
DR PDBsum; 7TYX; -.
DR PDBsum; 7TYY; -.
DR PDBsum; 7TZF; -.
DR PDBsum; 7VDH; -.
DR PDBsum; 7VDL; -.
DR PDBsum; 7VDM; -.
DR PDBsum; 7VGX; -.
DR PDBsum; 7VKT; -.
DR PDBsum; 7VL8; -.
DR PDBsum; 7VL9; -.
DR PDBsum; 7VLA; -.
DR PDBsum; 7VUG; -.
DR PDBsum; 7VUH; -.
DR PDBsum; 7VUI; -.
DR PDBsum; 7VUJ; -.
DR PDBsum; 7VUY; -.
DR PDBsum; 7VUZ; -.
DR PDBsum; 7VV3; -.
DR PDBsum; 7VV5; -.
DR PDBsum; 7W2Z; -.
DR PDBsum; 7WF7; -.
DR PDBsum; 7WVU; -.
DR PDBsum; 7WVV; -.
DR PDBsum; 7WVW; -.
DR PDBsum; 7WVX; -.
DR PDBsum; 7WVY; -.
DR AlphaFoldDB; P62873; -.
DR SMR; P62873; -.
DR BioGRID; 109044; 216.
DR CORUM; P62873; -.
DR DIP; DIP-599N; -.
DR IntAct; P62873; 94.
DR MINT; P62873; -.
DR STRING; 9606.ENSP00000481878; -.
DR BindingDB; P62873; -.
DR ChEMBL; CHEMBL3883319; -.
DR TCDB; 8.A.92.1.1; the g-protein AlphaBetaGama complex (gpc) family.
DR GlyGen; P62873; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P62873; -.
DR MetOSite; P62873; -.
DR PhosphoSitePlus; P62873; -.
DR SwissPalm; P62873; -.
DR BioMuta; GNB1; -.
DR DMDM; 51317302; -.
DR OGP; P62873; -.
DR REPRODUCTION-2DPAGE; IPI00026268; -.
DR EPD; P62873; -.
DR jPOST; P62873; -.
DR MassIVE; P62873; -.
DR MaxQB; P62873; -.
DR PaxDb; P62873; -.
DR PeptideAtlas; P62873; -.
DR PRIDE; P62873; -.
DR ProteomicsDB; 57441; -. [P62873-1]
DR ABCD; P62873; 1 sequenced antibody.
DR Antibodypedia; 26613; 253 antibodies from 31 providers.
DR DNASU; 2782; -.
DR Ensembl; ENST00000378609.9; ENSP00000367872.3; ENSG00000078369.18. [P62873-1]
DR Ensembl; ENST00000610897.4; ENSP00000481878.1; ENSG00000078369.18. [P62873-1]
DR GeneID; 2782; -.
DR KEGG; hsa:2782; -.
DR MANE-Select; ENST00000378609.9; ENSP00000367872.3; NM_002074.5; NP_002065.1.
DR UCSC; uc001aif.5; human. [P62873-1]
DR CTD; 2782; -.
DR DisGeNET; 2782; -.
DR GeneCards; GNB1; -.
DR GeneReviews; GNB1; -.
DR HGNC; HGNC:4396; GNB1.
DR HPA; ENSG00000078369; Tissue enriched (retina).
DR MalaCards; GNB1; -.
DR MIM; 139380; gene.
DR MIM; 616973; phenotype.
DR neXtProt; NX_P62873; -.
DR OpenTargets; ENSG00000078369; -.
DR Orphanet; 488613; Global developmental delay-neuro-ophthalmological abnormalities-seizures-intellectual disability syndrome.
DR PharmGKB; PA28776; -.
DR VEuPathDB; HostDB:ENSG00000078369; -.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR InParanoid; P62873; -.
DR OMA; PLDSQWV; -.
DR PhylomeDB; P62873; -.
DR TreeFam; TF106149; -.
DR PathwayCommons; P62873; -.
DR Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
DR Reactome; R-HSA-202040; G-protein activation.
DR Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
DR Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-HSA-381753; Olfactory Signaling Pathway.
DR Reactome; R-HSA-381771; Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1).
DR Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-HSA-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-HSA-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-HSA-8964616; G beta:gamma signalling through CDC42.
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 Reactome; R-HSA-9717207; Sensory perception of sweet, bitter, and umami (glutamate) taste.
DR Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR SignaLink; P62873; -.
DR SIGNOR; P62873; -.
DR BioGRID-ORCS; 2782; 49 hits in 1086 CRISPR screens.
DR ChiTaRS; GNB1; human.
DR EvolutionaryTrace; P62873; -.
DR GeneWiki; GNB1; -.
DR GenomeRNAi; 2782; -.
DR Pharos; P62873; Tbio.
DR PRO; PR:P62873; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P62873; protein.
DR Bgee; ENSG00000078369; Expressed in cortical plate and 209 other tissues.
DR ExpressionAtlas; P62873; baseline and differential.
DR Genevisible; P62873; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IDA:MGI.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:BHF-UCL.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISS:BHF-UCL.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL.
DR GO; GO:0007213; P:G protein-coupled acetylcholine receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR001632; Gprotein_B.
DR InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19850; PTHR19850; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00319; GPROTEINB.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Disease variant; Host-virus interaction; Intellectual disability;
KW Phosphoprotein; Reference proteome; Repeat; Transducer; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0000269|Ref.9,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..340
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(T)
FT subunit beta-1"
FT /id="PRO_0000127687"
FT REPEAT 53..83
FT /note="WD 1"
FT REPEAT 95..125
FT /note="WD 2"
FT REPEAT 141..170
FT /note="WD 3"
FT REPEAT 182..212
FT /note="WD 4"
FT REPEAT 224..254
FT /note="WD 5"
FT REPEAT 268..298
FT /note="WD 6"
FT REPEAT 310..340
FT /note="WD 7"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.8, ECO:0000269|Ref.9,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P62871"
FT VAR_SEQ 329..340
FT /note="TGSWDSFLKIWN -> SVLG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055232"
FT VARIANT 30
FT /note="L -> F (in MRD42; unknown pathological significance;
FT no effect on protein abundance; no effect on complex
FT formation with gamma subunit; no effect on trimer formation
FT with alpha and gamma subunits; no effect on receptor-driven
FT G protein activation; dbSNP:rs764997309)"
FT /evidence="ECO:0000269|PubMed:28087732"
FT /id="VAR_078279"
FT VARIANT 52
FT /note="R -> G (in MRD42; decreases receptor-driven G
FT protein activation; no effect on protein abundance; no
FT effect on complex formation with gamma subunit; decreases
FT trimer formation with alpha and gamma subunit)"
FT /evidence="ECO:0000269|PubMed:28087732"
FT /id="VAR_078280"
FT VARIANT 64
FT /note="G -> V (in MRD42; decreases receptor-driven G
FT protein activation; decreases protein abundance; decreases
FT complex formation with gamma subunit; decreases trimer
FT formation with alpha and gamma subunit)"
FT /evidence="ECO:0000269|PubMed:28087732"
FT /id="VAR_078281"
FT VARIANT 76
FT /note="D -> E (in MRD42; dbSNP:rs869312822)"
FT /evidence="ECO:0000269|PubMed:27108799"
FT /id="VAR_076644"
FT VARIANT 76
FT /note="D -> G (in MRD42; dbSNP:rs869312821)"
FT /evidence="ECO:0000269|PubMed:27108799"
FT /id="VAR_076643"
FT VARIANT 77
FT /note="G -> S (in MRD42; dbSNP:rs758432471)"
FT /evidence="ECO:0000269|PubMed:27108799"
FT /id="VAR_076645"
FT VARIANT 78
FT /note="K -> R (in MRD42; dbSNP:rs869312823)"
FT /evidence="ECO:0000269|PubMed:27108799"
FT /id="VAR_076646"
FT VARIANT 80
FT /note="I -> N (in MRD42; also found in patients with acute
FT lymphoblastic T-cell leukemia; reduces interaction with
FT GNAI2, GNAI3, GNA13 and GNA11; induces activation of PI3K-
FT AKT-mTOR and MAPK pathways; dbSNP:rs752746786)"
FT /evidence="ECO:0000269|PubMed:25485910,
FT ECO:0000269|PubMed:27108799"
FT /id="VAR_076647"
FT VARIANT 80
FT /note="I -> T (in MRD42; also found in patient with
FT hematologic malignancies; reduces interaction with GNAI2,
FT GNAI3, GNA13 and GNA11; induces activation of PI3K-AKT-mTOR
FT and MAPK pathways; dbSNP:rs752746786)"
FT /evidence="ECO:0000269|PubMed:25485910,
FT ECO:0000269|PubMed:27108799"
FT /id="VAR_076648"
FT VARIANT 91
FT /note="H -> R (in MRD42; unknown pathological significance;
FT no effect on protein abundance; no effect on complex
FT formation with gamma subunit; no effect on trimer formation
FT with apha and gamma subunits; no effect on receptor-driven
FT G protein activation)"
FT /evidence="ECO:0000269|PubMed:28087732"
FT /id="VAR_078282"
FT VARIANT 92
FT /note="A -> T (in MRD42; decreases receptor-driven G
FT protein activation; increases trimer formation with alpha
FT and gamma subunits; no effect on protein abundance; no
FT effect on complex formation with gamma subunit)"
FT /evidence="ECO:0000269|PubMed:28087732"
FT /id="VAR_078283"
FT VARIANT 94
FT /note="P -> S (in MRD42; decreases receptor-driven G
FT protein activation; decreases trimer formation with alpha
FT and gamma subunit; no effect on protein abundance;no effect
FT on complex formation with gamma subunit)"
FT /evidence="ECO:0000269|PubMed:28087732"
FT /id="VAR_078284"
FT VARIANT 95
FT /note="L -> P (in MRD42; dbSNP:rs869312824)"
FT /evidence="ECO:0000269|PubMed:27108799"
FT /id="VAR_076649"
FT VARIANT 96
FT /note="R -> L (in MRD42; decreases receptor-driven G
FT protein activation; decreases trimer formation with alpha
FT and gamma subunit; no effect on protein abundance; no
FT effect on complex formation with gamma subunit)"
FT /evidence="ECO:0000269|PubMed:28087732"
FT /id="VAR_078285"
FT VARIANT 101
FT /note="M -> V (in MRD42; dbSNP:rs869312825)"
FT /evidence="ECO:0000269|PubMed:27108799"
FT /id="VAR_076650"
FT VARIANT 106
FT /note="A -> T (in MRD42; decreases receptor-driven G
FT protein activation; decreases complex formation with gamma
FT subunit; decreases trimer formation with alpha and gamma
FT subunit; no effect on protein abundance)"
FT /evidence="ECO:0000269|PubMed:28087732"
FT /id="VAR_078286"
FT VARIANT 118
FT /note="D -> G (in MRD42; decreases receptor-driven G
FT protein activation; no effect on protein abundance; no
FT effect on complex formation with gamma subunit; no effect
FT on trimer formation with alpha and gamma subunits;
FT dbSNP:rs1553194162)"
FT /evidence="ECO:0000269|PubMed:27668284,
FT ECO:0000269|PubMed:28087732"
FT /id="VAR_078287"
FT VARIANT 326
FT /note="A -> T (in MRD42; dbSNP:rs869312826)"
FT /evidence="ECO:0000269|PubMed:27108799"
FT /id="VAR_076651"
FT VARIANT 337
FT /note="K -> Q (in MRD42; unknown pathological significance;
FT no effect on protein abundance; no effect on complex
FT formation with gamma subunit; no effect on trimer formation
FT with alpha and gamma subunits; no effect on receptor-driven
FT G protein activation)"
FT /evidence="ECO:0000269|PubMed:28087732"
FT /id="VAR_078288"
FT HELIX 3..25
FT /evidence="ECO:0007829|PDB:6CRK"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 67..74
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6X18"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:7AUE"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6X18"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:7S8M"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 196..203
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:7F4H"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:7EO2"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:7S8L"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:6CRK"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:6WZG"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:6CRK"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:7L1U"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:6CRK"
SQ SEQUENCE 340 AA; 37377 MW; 896CBD32D2686598 CRC64;
MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA
MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN YVACGGLDNI
CSIYNLKTRE GNVRVSRELA GHTGYLSCCR FLDDNQIVTS SGDTTCALWD IETGQQTTTF
TGHTGDVMSL SLAPDTRLFV SGACDASAKL WDVREGMCRQ TFTGHESDIN AICFFPNGNA
FATGSDDATC RLFDLRADQE LMTYSHDNII CGITSVSFSK SGRLLLAGYD DFNCNVWDAL
KADRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN
