Full text data of GNB1
GNB1
[Confidence: high (present in two of the MS resources)]
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (Transducin beta chain 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (Transducin beta chain 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00026268
IPI00026268 Guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 1 membrane n/a 3 2 n/a 3 n/a n/a n/a n/a n/a 3 2 2 2 n/a n/a 2 n/a 3 2 inner surface of plasma membrane n/a found at its expected molecular weight found at molecular weight
IPI00026268 Guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 1 membrane n/a 3 2 n/a 3 n/a n/a n/a n/a n/a 3 2 2 2 n/a n/a 2 n/a 3 2 inner surface of plasma membrane n/a found at its expected molecular weight found at molecular weight
UniProt
P62873
ID GBB1_HUMAN Reviewed; 340 AA.
AC P62873; B1AJZ7; P04697; P04901;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 114.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT and those of bovine retinal rod cell transducin are identical.";
RL FEBS Lett. 207:187-192(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by 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].
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: 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
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND 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
RP METHIONINE, ACETYLATION AT SER-2, AND 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 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
RT nucleotide exchange factor for RhoA and Rac1: regulation of cell shape
RT and reactive oxygen species production.";
RL Circ. Res. 93:848-856(2003).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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
RT Gbeta subunits.";
RL Cell. Physiol. Biochem. 23:1-8(2009).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEXES WITH GNG2 AND
RP PTH1R, FUNCTION, SUBUNIT, AND MUTAGENESIS OF THR-47; LYS-337 AND
RP TRP-339.
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
RT G-protein dimer Gbeta1gamma2.";
RL Structure 16:1086-1094(2008).
RN [16]
RP ERRATUM, AND RETRACTION.
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).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC involved as a modulator or transducer in various transmembrane
CC signaling systems. The beta and gamma chains are required for the
CC GTPase activity, for replacement of GDP by GTP, and for G protein-
CC effector interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC gamma. Interacts with ARHGEF18 and RASD2. The heterodimer formed
CC by GNB1 and GNG2 interacts with PTH1R (via C-terminus).
CC -!- INTERACTION:
CC P19878:NCF2; NbExp=2; IntAct=EBI-357130, EBI-489611;
CC -!- PTM: Phosphorylation at His-266 by NDKB contributes to G protein
CC activation by increasing the high energetic phosphate transfer
CC onto GDP (By similarity).
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC -!- SIMILARITY: Contains 7 WD repeats.
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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; CAI20029.1; -; Genomic_DNA.
DR EMBL; AL109917; CAI20029.1; JOINED; Genomic_DNA.
DR EMBL; AL109917; CAI95654.1; -; Genomic_DNA.
DR EMBL; AL031282; CAI95654.1; JOINED; 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; M36430; AAA63265.1; -; mRNA.
DR PIR; A24853; RGHUB1.
DR RefSeq; NP_001269467.1; NM_001282538.1.
DR RefSeq; NP_001269468.1; NM_001282539.1.
DR RefSeq; NP_002065.1; NM_002074.4.
DR RefSeq; XP_005244799.1; XM_005244742.1.
DR UniGene; Hs.430425; -.
DR PDB; 4KFM; X-ray; 3.45 A; B=1-340.
DR PDBsum; 4KFM; -.
DR ProteinModelPortal; P62873; -.
DR SMR; P62873; 2-340.
DR DIP; DIP-599N; -.
DR IntAct; P62873; 20.
DR MINT; MINT-94562; -.
DR STRING; 9606.ENSP00000367872; -.
DR PhosphoSite; P62873; -.
DR DMDM; 51317302; -.
DR OGP; P62873; -.
DR REPRODUCTION-2DPAGE; IPI00026268; -.
DR PaxDb; P62873; -.
DR PRIDE; P62873; -.
DR DNASU; 2782; -.
DR Ensembl; ENST00000378609; ENSP00000367872; ENSG00000078369.
DR GeneID; 2782; -.
DR KEGG; hsa:2782; -.
DR UCSC; uc001aif.3; human.
DR CTD; 2782; -.
DR GeneCards; GC01M001748; -.
DR HGNC; HGNC:4396; GNB1.
DR HPA; HPA040736; -.
DR MIM; 139380; gene.
DR neXtProt; NX_P62873; -.
DR PharmGKB; PA28776; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000176356; -.
DR HOVERGEN; HBG000188; -.
DR InParanoid; P62873; -.
DR KO; K04536; -.
DR OMA; RIVMRPR; -.
DR OrthoDB; EOG7GN2N5; -.
DR PhylomeDB; P62873; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; P62873; -.
DR ChiTaRS; GNB1; human.
DR EvolutionaryTrace; P62873; -.
DR GeneWiki; GNB1; -.
DR GenomeRNAi; 2782; -.
DR NextBio; 10959; -.
DR PRO; PR:P62873; -.
DR ArrayExpress; P62873; -.
DR Bgee; P62873; -.
DR CleanEx; HS_GNB1; -.
DR Genevestigator; P62873; -.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISS:BHF-UCL.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0007213; P:G-protein coupled acetylcholine receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 7.
DR PIRSF; PIRSF002394; GN-bd_beta; 1.
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; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat;
KW Transducer; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 340 Guanine nucleotide-binding protein
FT G(I)/G(S)/G(T) subunit beta-1.
FT /FTId=PRO_0000127687.
FT REPEAT 53 83 WD 1.
FT REPEAT 95 125 WD 2.
FT REPEAT 141 170 WD 3.
FT REPEAT 182 212 WD 4.
FT REPEAT 224 254 WD 5.
FT REPEAT 268 298 WD 6.
FT REPEAT 310 340 WD 7.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 266 266 Phosphohistidine (By similarity).
FT MUTAGEN 47 47 T->A: Abolishes interaction with PTH1R
FT and signaling in response to PTH1R
FT agonist; when associated with A-337 and
FT A-339.
FT MUTAGEN 337 337 K->A: Abolishes interaction with PTH1R
FT and signaling in response to PTH1R
FT agonist; when associated with A-47 and A-
FT 339.
FT MUTAGEN 339 339 W->A: Abolishes interaction with PTH1R
FT and signaling in response to PTH1R
FT agonist; when associated with A-47 and A-
FT 337.
FT HELIX 3 25
FT HELIX 30 34
FT STRAND 47 51
FT STRAND 58 63
FT STRAND 67 74
FT STRAND 77 83
FT TURN 84 86
FT STRAND 89 94
FT STRAND 100 105
FT STRAND 109 116
FT STRAND 121 127
FT STRAND 134 139
FT STRAND 146 153
FT STRAND 156 161
FT STRAND 164 170
FT TURN 171 173
FT STRAND 176 181
FT STRAND 187 192
FT STRAND 196 203
FT STRAND 208 212
FT TURN 213 216
FT STRAND 217 222
FT STRAND 229 234
FT STRAND 238 245
FT STRAND 250 254
FT TURN 255 258
FT STRAND 259 264
FT STRAND 273 278
FT STRAND 284 289
FT STRAND 292 298
FT TURN 299 301
FT STRAND 303 309
FT STRAND 315 320
FT STRAND 327 331
FT STRAND 336 339
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
//
ID GBB1_HUMAN Reviewed; 340 AA.
AC P62873; B1AJZ7; P04697; P04901;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 114.
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT and those of bovine retinal rod cell transducin are identical.";
RL FEBS Lett. 207:187-192(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by 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].
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: 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
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND 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
RP METHIONINE, ACETYLATION AT SER-2, AND 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 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
RT nucleotide exchange factor for RhoA and Rac1: regulation of cell shape
RT and reactive oxygen species production.";
RL Circ. Res. 93:848-856(2003).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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
RT Gbeta subunits.";
RL Cell. Physiol. Biochem. 23:1-8(2009).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEXES WITH GNG2 AND
RP PTH1R, FUNCTION, SUBUNIT, AND MUTAGENESIS OF THR-47; LYS-337 AND
RP TRP-339.
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
RT G-protein dimer Gbeta1gamma2.";
RL Structure 16:1086-1094(2008).
RN [16]
RP ERRATUM, AND RETRACTION.
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).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC involved as a modulator or transducer in various transmembrane
CC signaling systems. The beta and gamma chains are required for the
CC GTPase activity, for replacement of GDP by GTP, and for G protein-
CC effector interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC gamma. Interacts with ARHGEF18 and RASD2. The heterodimer formed
CC by GNB1 and GNG2 interacts with PTH1R (via C-terminus).
CC -!- INTERACTION:
CC P19878:NCF2; NbExp=2; IntAct=EBI-357130, EBI-489611;
CC -!- PTM: Phosphorylation at His-266 by NDKB contributes to G protein
CC activation by increasing the high energetic phosphate transfer
CC onto GDP (By similarity).
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
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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; CAI20029.1; -; Genomic_DNA.
DR EMBL; AL109917; CAI20029.1; JOINED; Genomic_DNA.
DR EMBL; AL109917; CAI95654.1; -; Genomic_DNA.
DR EMBL; AL031282; CAI95654.1; JOINED; 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; M36430; AAA63265.1; -; mRNA.
DR PIR; A24853; RGHUB1.
DR RefSeq; NP_001269467.1; NM_001282538.1.
DR RefSeq; NP_001269468.1; NM_001282539.1.
DR RefSeq; NP_002065.1; NM_002074.4.
DR RefSeq; XP_005244799.1; XM_005244742.1.
DR UniGene; Hs.430425; -.
DR PDB; 4KFM; X-ray; 3.45 A; B=1-340.
DR PDBsum; 4KFM; -.
DR ProteinModelPortal; P62873; -.
DR SMR; P62873; 2-340.
DR DIP; DIP-599N; -.
DR IntAct; P62873; 20.
DR MINT; MINT-94562; -.
DR STRING; 9606.ENSP00000367872; -.
DR PhosphoSite; P62873; -.
DR DMDM; 51317302; -.
DR OGP; P62873; -.
DR REPRODUCTION-2DPAGE; IPI00026268; -.
DR PaxDb; P62873; -.
DR PRIDE; P62873; -.
DR DNASU; 2782; -.
DR Ensembl; ENST00000378609; ENSP00000367872; ENSG00000078369.
DR GeneID; 2782; -.
DR KEGG; hsa:2782; -.
DR UCSC; uc001aif.3; human.
DR CTD; 2782; -.
DR GeneCards; GC01M001748; -.
DR HGNC; HGNC:4396; GNB1.
DR HPA; HPA040736; -.
DR MIM; 139380; gene.
DR neXtProt; NX_P62873; -.
DR PharmGKB; PA28776; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000176356; -.
DR HOVERGEN; HBG000188; -.
DR InParanoid; P62873; -.
DR KO; K04536; -.
DR OMA; RIVMRPR; -.
DR OrthoDB; EOG7GN2N5; -.
DR PhylomeDB; P62873; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; P62873; -.
DR ChiTaRS; GNB1; human.
DR EvolutionaryTrace; P62873; -.
DR GeneWiki; GNB1; -.
DR GenomeRNAi; 2782; -.
DR NextBio; 10959; -.
DR PRO; PR:P62873; -.
DR ArrayExpress; P62873; -.
DR Bgee; P62873; -.
DR CleanEx; HS_GNB1; -.
DR Genevestigator; P62873; -.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISS:BHF-UCL.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0007213; P:G-protein coupled acetylcholine receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
DR GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 7.
DR PIRSF; PIRSF002394; GN-bd_beta; 1.
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; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat;
KW Transducer; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 340 Guanine nucleotide-binding protein
FT G(I)/G(S)/G(T) subunit beta-1.
FT /FTId=PRO_0000127687.
FT REPEAT 53 83 WD 1.
FT REPEAT 95 125 WD 2.
FT REPEAT 141 170 WD 3.
FT REPEAT 182 212 WD 4.
FT REPEAT 224 254 WD 5.
FT REPEAT 268 298 WD 6.
FT REPEAT 310 340 WD 7.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 266 266 Phosphohistidine (By similarity).
FT MUTAGEN 47 47 T->A: Abolishes interaction with PTH1R
FT and signaling in response to PTH1R
FT agonist; when associated with A-337 and
FT A-339.
FT MUTAGEN 337 337 K->A: Abolishes interaction with PTH1R
FT and signaling in response to PTH1R
FT agonist; when associated with A-47 and A-
FT 339.
FT MUTAGEN 339 339 W->A: Abolishes interaction with PTH1R
FT and signaling in response to PTH1R
FT agonist; when associated with A-47 and A-
FT 337.
FT HELIX 3 25
FT HELIX 30 34
FT STRAND 47 51
FT STRAND 58 63
FT STRAND 67 74
FT STRAND 77 83
FT TURN 84 86
FT STRAND 89 94
FT STRAND 100 105
FT STRAND 109 116
FT STRAND 121 127
FT STRAND 134 139
FT STRAND 146 153
FT STRAND 156 161
FT STRAND 164 170
FT TURN 171 173
FT STRAND 176 181
FT STRAND 187 192
FT STRAND 196 203
FT STRAND 208 212
FT TURN 213 216
FT STRAND 217 222
FT STRAND 229 234
FT STRAND 238 245
FT STRAND 250 254
FT TURN 255 258
FT STRAND 259 264
FT STRAND 273 278
FT STRAND 284 289
FT STRAND 292 298
FT TURN 299 301
FT STRAND 303 309
FT STRAND 315 320
FT STRAND 327 331
FT STRAND 336 339
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
//
MIM
139380
*RECORD*
*FIELD* NO
139380
*FIELD* TI
*139380 GUANINE NUCLEOTIDE-BINDING PROTEIN, BETA-1; GNB1
;;TRANSDUCIN, BETA POLYPEPTIDE
read more*FIELD* TX
DESCRIPTION
Heterotrimeric guanine nucleotide-binding proteins (G proteins)
transduce extracellular signals received by transmembrane receptors to
effector proteins. Each subunit of the G protein complex is encoded by a
member of 1 of 3 corresponding gene families, alpha, beta, and gamma
(Hurowitz et al., 2000).
CLONING
Retinal transducin is a guanine nucleotide regulatory protein that
activates a cGMP phosphodiesterase in photoreceptor cells. Fong et al.
(1986) identified and analyzed cDNA clones of the bovine transducin beta
subunit and deduced the primary structure of a 340-amino acid protein.
Significant homology was found with the yeast CDC4 gene product. The
beta-subunit polypeptide, of relative molecular mass 37,375 Da, is
encoded by a 2.9-kb mRNA. All mammalian tissues and clonal cell lines
examined contained at least 2 beta-related mRNAs, usually 1.8 and 2.9 kb
long. The authors suggested that there may be a diversity of beta
subunit-related mRNAs that could encode different proteins.
Codina et al. (1986) cloned a full-length G protein beta-1 subunit
(GNB1) from a human liver cDNA library. They found that the deduced
340-amino acid protein is identical to that encoded by bovine retinal
rod cell cDNA of the beta subunit of transducin.
GENE FUNCTION
Using coprecipitation analysis, Rosskopf et al. (2003) showed that GNB1
formed dimers with all gamma subunits analyzed. The strength of the
interaction was variable and was strongest between GNB1 and GNG3
(608941), GNG10 (604389), GNG12, and GNG13 (607298).
GENE STRUCTURE
Rosskopf et al. (2003) determined that the GNB1 gene contains 12 exons.
The first 2 exons and the last exon are noncoding.
MAPPING
Using a cDNA probe against a mouse/human somatic cell hybrid panel,
Sparkes et al. (1987) mapped the human beta-1 polypeptide of G protein
to human chromosome 1. Levine et al. (1990) confirmed the assignment to
chromosome 1 by Southern analysis of somatic cell hybrids, and Levine et
al. (1990) and Modi et al. (1991) regionalized the assignment to
1pter-p31.2 by in situ hybridization. Although Sparkes et al. (1987) had
mapped the mouse Gnb1 gene to chromosome 19, later studies showed that
Gnb1 is located on distal mouse chromosome 4 (Danciger et al., 1990).
ANIMAL MODEL
In the Rd4/+ mouse, autosomal dominant retinal degeneration cosegregates
with a large inversion spanning nearly all of chromosome 4 (Roderick et
al., 1997). To identify the responsible gene for this phenotype,
Kitamura et al. (2006) focused on the distal breakpoint and found that
it lay in the second intron of the Gnb1 gene, coding for the
transducin-beta-1 protein, which is directly involved in
phototransduction and in the normal maintenance of photoreceptors.
Kitamura et al. (2006) determined that before the beginning of retinal
degeneration in the Rd4/+ retina, the levels of Gnb1 mRNA and
transducin-beta-1 were 50% of those in wildtype retina. Kitamura et al.
(2006) suggested that disruption of the Gnb1 gene is responsible for
Rd4/+ retinal disease.
*FIELD* RF
1. Codina, J.; Stengel, D.; Woo, S. L. C.; Birnbaumer, L.: Beta-subunits
of the human liver G(s)/G(i) signal-transducing proteins and those
of bovine rod cell transducin are identical. FEBS Lett. 207: 187-192,
1986.
2. Danciger, M.; Farber, D. B.; Peyser, M.; Kozak, C. A.: The gene
for the beta-subunit of retinal transducin (Gnb-1) maps to distal
mouse chromosome 4, and related sequences map to mouse chromosomes
5 and 8. Genomics 6: 428-435, 1990.
3. Fong, H. K. W.; Hurley, J. B.; Hopkins, R. S.; Miake-Lye, R.; Johnson,
M. S.; Doolittle, R. F.; Simon, M. I.: Repetitive segmental structure
of the transducin beta-subunit: homology with the CDC4 gene and identification
of related mRNAs. Proc. Nat. Acad. Sci. 83: 2162-2166, 1986.
4. Hurowitz, E. H.; Melnyk, J. M.; Chen, Y.-J.; Kouros-Mehr, H.; Simon,
M. I.; Shizuya, H.: Genomic characterization of the human heterotrimeric
G protein alpha, beta, and gamma subunit genes. DNA Res. 7: 111-120,
2000.
5. Kitamura, E.; Danciger, M.; Yamashita, C.; Rao, N. P.; Nusinowitz,
S.; Chang, B.; Farber, D. B.: Disruption of the gene encoding the
beta-1-subunit of transducin in the Rd4/+ mouse. Invest. Ophthal.
Vis. Sci. 47: 1293-1301, 2006.
6. Levine, M. A.; Modi, W. S.; O'Brien, S. J.: Chromosomal localization
of the genes encoding two forms of the G-protein beta polypeptide,
beta-1 and beta-3, in man. Genomics 8: 380-386, 1990.
7. Modi, W. S.; O'Brien, S. J.; Levine, M. A.: Chromosomal assignment
of 2 GTP binding protein subunit genes: the alpha subunit of adenylyl
cyclase (GNAS) and the beta 1 polypeptide (GNB). (Abstract) Cytogenet.
Cell Genet. 58: 1860 only, 1991.
8. Roderick, T. H.; Chang, B.; Hawes, N. L.; Heckenlively, J. R.:
A new dominant retinal degeneration (Rd4) associated with a chromosomal
inversion in the mouse. Genomics 42: 393-396, 1997.
9. Rosskopf, D.; Nikula, C.; Manthey, I.; Joisten, M.; Frey, U.; Kohnen,
S.; Siffert, W.: The human G protein beta-4 subunit: gene structure,
expression, G-gamma and effector interaction. FEBS Lett. 544: 27-32,
2003.
10. Sparkes, R. S.; Cohn, V. H.; Cire-Eversole, P.; Blatt, C.; Amatruda,
T. T.; Weiner, L. P.; Nesbitt, M.; Reed, R. R.; Lochrie, M. A.; Fournier,
R. E. K.; Simon, M. I.: Mapping of genes encoding the subunits of
guanine nucleotide-binding proteins (G-proteins) in the mouse. (Abstract) Cytogenet.
Cell Genet. 46: 696 only, 1987.
11. Sparkes, R. S.; Cohn, V. H.; Mohandas, T.; Zollman, S.; Cire-Eversole,
P.; Amatruda, T. T.; Reed, R. R.; Lochrie, M. A.; Simon, M. I.: Mapping
of genes encoding the subunits of guanine nucleotide-binding protein
(G-proteins) in humans. (Abstract) Cytogenet. Cell Genet. 46: 696
only, 1987.
*FIELD* CN
Jane Kelly - updated: 10/31/2007
Carol A. Bocchini - updated: 10/31/2007
Patricia A. Hartz - updated: 3/14/2007
Victor A. McKusick - updated: 6/7/2000
Carol A. Bocchini - updated: 12/1/1999
*FIELD* CD
Victor A. McKusick: 9/22/1987
*FIELD* ED
carol: 06/25/2012
carol: 10/31/2007
wwang: 3/20/2007
terry: 3/14/2007
mcapotos: 6/28/2000
mcapotos: 6/23/2000
terry: 6/7/2000
terry: 12/1/1999
carol: 12/1/1999
alopez: 5/12/1998
supermim: 3/16/1992
carol: 2/22/1992
carol: 8/8/1991
carol: 8/7/1991
carol: 10/10/1990
carol: 7/7/1990
*RECORD*
*FIELD* NO
139380
*FIELD* TI
*139380 GUANINE NUCLEOTIDE-BINDING PROTEIN, BETA-1; GNB1
;;TRANSDUCIN, BETA POLYPEPTIDE
read more*FIELD* TX
DESCRIPTION
Heterotrimeric guanine nucleotide-binding proteins (G proteins)
transduce extracellular signals received by transmembrane receptors to
effector proteins. Each subunit of the G protein complex is encoded by a
member of 1 of 3 corresponding gene families, alpha, beta, and gamma
(Hurowitz et al., 2000).
CLONING
Retinal transducin is a guanine nucleotide regulatory protein that
activates a cGMP phosphodiesterase in photoreceptor cells. Fong et al.
(1986) identified and analyzed cDNA clones of the bovine transducin beta
subunit and deduced the primary structure of a 340-amino acid protein.
Significant homology was found with the yeast CDC4 gene product. The
beta-subunit polypeptide, of relative molecular mass 37,375 Da, is
encoded by a 2.9-kb mRNA. All mammalian tissues and clonal cell lines
examined contained at least 2 beta-related mRNAs, usually 1.8 and 2.9 kb
long. The authors suggested that there may be a diversity of beta
subunit-related mRNAs that could encode different proteins.
Codina et al. (1986) cloned a full-length G protein beta-1 subunit
(GNB1) from a human liver cDNA library. They found that the deduced
340-amino acid protein is identical to that encoded by bovine retinal
rod cell cDNA of the beta subunit of transducin.
GENE FUNCTION
Using coprecipitation analysis, Rosskopf et al. (2003) showed that GNB1
formed dimers with all gamma subunits analyzed. The strength of the
interaction was variable and was strongest between GNB1 and GNG3
(608941), GNG10 (604389), GNG12, and GNG13 (607298).
GENE STRUCTURE
Rosskopf et al. (2003) determined that the GNB1 gene contains 12 exons.
The first 2 exons and the last exon are noncoding.
MAPPING
Using a cDNA probe against a mouse/human somatic cell hybrid panel,
Sparkes et al. (1987) mapped the human beta-1 polypeptide of G protein
to human chromosome 1. Levine et al. (1990) confirmed the assignment to
chromosome 1 by Southern analysis of somatic cell hybrids, and Levine et
al. (1990) and Modi et al. (1991) regionalized the assignment to
1pter-p31.2 by in situ hybridization. Although Sparkes et al. (1987) had
mapped the mouse Gnb1 gene to chromosome 19, later studies showed that
Gnb1 is located on distal mouse chromosome 4 (Danciger et al., 1990).
ANIMAL MODEL
In the Rd4/+ mouse, autosomal dominant retinal degeneration cosegregates
with a large inversion spanning nearly all of chromosome 4 (Roderick et
al., 1997). To identify the responsible gene for this phenotype,
Kitamura et al. (2006) focused on the distal breakpoint and found that
it lay in the second intron of the Gnb1 gene, coding for the
transducin-beta-1 protein, which is directly involved in
phototransduction and in the normal maintenance of photoreceptors.
Kitamura et al. (2006) determined that before the beginning of retinal
degeneration in the Rd4/+ retina, the levels of Gnb1 mRNA and
transducin-beta-1 were 50% of those in wildtype retina. Kitamura et al.
(2006) suggested that disruption of the Gnb1 gene is responsible for
Rd4/+ retinal disease.
*FIELD* RF
1. Codina, J.; Stengel, D.; Woo, S. L. C.; Birnbaumer, L.: Beta-subunits
of the human liver G(s)/G(i) signal-transducing proteins and those
of bovine rod cell transducin are identical. FEBS Lett. 207: 187-192,
1986.
2. Danciger, M.; Farber, D. B.; Peyser, M.; Kozak, C. A.: The gene
for the beta-subunit of retinal transducin (Gnb-1) maps to distal
mouse chromosome 4, and related sequences map to mouse chromosomes
5 and 8. Genomics 6: 428-435, 1990.
3. Fong, H. K. W.; Hurley, J. B.; Hopkins, R. S.; Miake-Lye, R.; Johnson,
M. S.; Doolittle, R. F.; Simon, M. I.: Repetitive segmental structure
of the transducin beta-subunit: homology with the CDC4 gene and identification
of related mRNAs. Proc. Nat. Acad. Sci. 83: 2162-2166, 1986.
4. Hurowitz, E. H.; Melnyk, J. M.; Chen, Y.-J.; Kouros-Mehr, H.; Simon,
M. I.; Shizuya, H.: Genomic characterization of the human heterotrimeric
G protein alpha, beta, and gamma subunit genes. DNA Res. 7: 111-120,
2000.
5. Kitamura, E.; Danciger, M.; Yamashita, C.; Rao, N. P.; Nusinowitz,
S.; Chang, B.; Farber, D. B.: Disruption of the gene encoding the
beta-1-subunit of transducin in the Rd4/+ mouse. Invest. Ophthal.
Vis. Sci. 47: 1293-1301, 2006.
6. Levine, M. A.; Modi, W. S.; O'Brien, S. J.: Chromosomal localization
of the genes encoding two forms of the G-protein beta polypeptide,
beta-1 and beta-3, in man. Genomics 8: 380-386, 1990.
7. Modi, W. S.; O'Brien, S. J.; Levine, M. A.: Chromosomal assignment
of 2 GTP binding protein subunit genes: the alpha subunit of adenylyl
cyclase (GNAS) and the beta 1 polypeptide (GNB). (Abstract) Cytogenet.
Cell Genet. 58: 1860 only, 1991.
8. Roderick, T. H.; Chang, B.; Hawes, N. L.; Heckenlively, J. R.:
A new dominant retinal degeneration (Rd4) associated with a chromosomal
inversion in the mouse. Genomics 42: 393-396, 1997.
9. Rosskopf, D.; Nikula, C.; Manthey, I.; Joisten, M.; Frey, U.; Kohnen,
S.; Siffert, W.: The human G protein beta-4 subunit: gene structure,
expression, G-gamma and effector interaction. FEBS Lett. 544: 27-32,
2003.
10. Sparkes, R. S.; Cohn, V. H.; Cire-Eversole, P.; Blatt, C.; Amatruda,
T. T.; Weiner, L. P.; Nesbitt, M.; Reed, R. R.; Lochrie, M. A.; Fournier,
R. E. K.; Simon, M. I.: Mapping of genes encoding the subunits of
guanine nucleotide-binding proteins (G-proteins) in the mouse. (Abstract) Cytogenet.
Cell Genet. 46: 696 only, 1987.
11. Sparkes, R. S.; Cohn, V. H.; Mohandas, T.; Zollman, S.; Cire-Eversole,
P.; Amatruda, T. T.; Reed, R. R.; Lochrie, M. A.; Simon, M. I.: Mapping
of genes encoding the subunits of guanine nucleotide-binding protein
(G-proteins) in humans. (Abstract) Cytogenet. Cell Genet. 46: 696
only, 1987.
*FIELD* CN
Jane Kelly - updated: 10/31/2007
Carol A. Bocchini - updated: 10/31/2007
Patricia A. Hartz - updated: 3/14/2007
Victor A. McKusick - updated: 6/7/2000
Carol A. Bocchini - updated: 12/1/1999
*FIELD* CD
Victor A. McKusick: 9/22/1987
*FIELD* ED
carol: 06/25/2012
carol: 10/31/2007
wwang: 3/20/2007
terry: 3/14/2007
mcapotos: 6/28/2000
mcapotos: 6/23/2000
terry: 6/7/2000
terry: 12/1/1999
carol: 12/1/1999
alopez: 5/12/1998
supermim: 3/16/1992
carol: 2/22/1992
carol: 8/8/1991
carol: 8/7/1991
carol: 10/10/1990
carol: 7/7/1990