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Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (Transducin beta chain 1)

 GBB1_HUMAN              Reviewed;         340 AA.
P62873; B1AJZ7; P04697; P04901; Q1RMY8;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 154.
RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1;
AltName: Full=Transducin beta chain 1;
Name=GNB1 {ECO:0000312|HGNC:HGNC:4396};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=3095147; DOI=10.1016/0014-5793(86)81486-7;
Codina J., Stengel D., Woo S.L.C., Birnbaumer L.;
"Beta-subunits of the human liver Gs/Gi signal-transducing proteins
and those of bovine retinal rod cell transducin are identical.";
FEBS Lett. 207:187-192(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, Muscle, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-15; 58-89; 284-301 AND 305-314, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma, and Melanoma;
Bienvenut W.V., Quadroni M.;
Submitted (JUL-2005) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 2-8; 69-78 AND 90-96, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 23-42; 58-78; 138-150; 198-209 AND 315-337, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[11]
INTERACTION WITH ARHGEF18.
PubMed=14512443; DOI=10.1161/01.RES.0000097607.14733.0C;
Niu J., Profirovic J., Pan H., Vaiskunaite R., Voyno-Yasenetskaya T.;
"G Protein betagamma subunits stimulate p114RhoGEF, a guanine
nucleotide exchange factor for RhoA and Rac1: regulation of cell shape
and reactive oxygen species production.";
Circ. Res. 93:848-856(2003).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
INTERACTION WITH RASD2.
PubMed=19255495; DOI=10.1159/000204075;
Hill C., Goddard A., Ladds G., Davey J.;
"The cationic region of Rhes mediates its interactions with specific
Gbeta subunits.";
Cell. Physiol. Biochem. 23:1-8(2009).
[14]
INTERACTION WITH ARHGEF5.
PubMed=19713215; DOI=10.1074/jbc.M109.047282;
Wang Z., Kumamoto Y., Wang P., Gan X., Lehmann D., Smrcka A.V.,
Cohn L., Iwasaki A., Li L., Wu D.;
"Regulation of immature dendritic cell migration by RhoA guanine
nucleotide exchange factor Arhgef5.";
J. Biol. Chem. 284:28599-28606(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[19]
INVOLVEMENT IN MRD42, AND VARIANTS MRD42 GLU-76; GLY-76; SER-77;
ARG-78; ASN-80; THR-80; PRO-95; VAL-101 AND THR-326.
PubMed=27108799; DOI=10.1016/j.ajhg.2016.03.011;
University of Washington Center for Mendelian Genomics;
Petrovski S., Kuery S., Myers C.T., Anyane-Yeboa K., Cogne B.,
Bialer M., Xia F., Hemati P., Riviello J., Mehaffey M., Besnard T.,
Becraft E., Wadley A., Politi A.R., Colombo S., Zhu X., Ren Z.,
Andrews I., Dudding-Byth T., Schneider A.L., Wallace G., Rosen A.B.,
Schelley S., Enns G.M., Corre P., Dalton J., Mercier S., Latypova X.,
Schmitt S., Guzman E., Moore C., Bier L., Heinzen E.L.,
Karachunski P., Shur N., Grebe T., Basinger A., Nguyen J.M.,
Bezieau S., Wierenga K., Bernstein J.A., Scheffer I.E.,
Rosenfeld J.A., Mefford H.C., Isidor B., Goldstein D.B.;
"Germline de novo mutations in GNB1 cause severe neurodevelopmental
disability, hypotonia, and seizures.";
Am. J. Hum. Genet. 98:1001-1010(2016).
[20]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GNG2.
PubMed=18611381; DOI=10.1016/j.str.2008.04.010;
Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.;
"Structure of the parathyroid hormone receptor C terminus bound to the
G-protein dimer Gbeta1gamma2.";
Structure 16:1086-1094(2008).
[21]
ERRATUM, AND RETRACTION.
PubMed=21827955; DOI=10.1016/j.str.2011.07.010;
Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.;
Structure 19:1200-1200(2011).
[22]
CHARACTERIZATION VARIANTS MRD42 ASN-80 AND THR-80.
PubMed=25485910; DOI=10.1038/nm.3751;
Yoda A., Adelmant G., Tamburini J., Chapuy B., Shindoh N., Yoda Y.,
Weigert O., Kopp N., Wu S.C., Kim S.S., Liu H., Tivey T.,
Christie A.L., Elpek K.G., Card J., Gritsman K., Gotlib J.,
Deininger M.W., Makishima H., Turley S.J., Javidi-Sharifi N.,
Maciejewski J.P., Jaiswal S., Ebert B.L., Rodig S.J., Tyner J.W.,
Marto J.A., Weinstock D.M., Lane A.A.;
"Mutations in G protein beta subunits promote transformation and
kinase inhibitor resistance.";
Nat. Med. 21:71-75(2015).
[23]
VARIANT MRD42 GLY-118.
PubMed=27668284; DOI=10.1212/NXG.0000000000000106;
Steinruecke S., Lohmann K., Domingo A., Rolfs A., Baeumer T.,
Spiegler J., Hartmann C., Muenchau A.;
"Novel GNB1 missense mutation in a patient with generalized dystonia,
hypotonia, and intellectual disability.";
Neurol. Genet. 2:E106-E106(2016).
[24]
VARIANTS MRD42 PHE-30; GLY-52; VAL-64; ARG-91; THR-92; SER-94; LEU-96;
THR-106; GLY-118 AND GLN-337, AND CHARACTERIZATION OF VARIANTS MRD42
PHE-30; GLY-52; VAL-64; ARG-91; THR-92; SER-94; LEU-96; THR-106;
GLY-118 AND GLN-337.
PubMed=28087732; DOI=10.1093/hmg/ddx018;
Lohmann K., Masuho I., Patil D.N., Baumann H., Hebert E.,
Steinruecke S., Trujillano D., Skamangas N.K., Dobricic V.,
Huening I., Gillessen-Kaesbach G., Westenberger A.,
Savic-Pavicevic D., Muenchau A., Oprea G., Klein C., Rolfs A.,
Martemyanov K.A.;
"Novel GNB1 mutations disrupt assembly and function of G protein
heterotrimers and cause global developmental delay in humans.";
Hum. Mol. Genet. 26:1078-1086(2017).
-!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
involved as a modulator or transducer in various transmembrane
signaling systems. The beta and gamma chains are required for the
GTPase activity, for replacement of GDP by GTP, and for G protein-
effector interaction.
-!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
gamma. Interacts with ARHGEF18 and RASD2 (PubMed:14512443,
PubMed:19255495). The heterodimer formed by GNB1 and GNG2
interacts with ARHGEF5 (PubMed:19713215).
{ECO:0000269|PubMed:14512443, ECO:0000269|PubMed:19255495,
ECO:0000269|PubMed:19713215}.
-!- INTERACTION:
P19878:NCF2; NbExp=2; IntAct=EBI-357130, EBI-489611;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P62873-1; Sequence=Displayed;
Name=2;
IsoId=P62873-2; Sequence=VSP_055232;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation at His-266 by NDKB contributes to G protein
activation by increasing the high energetic phosphate transfer
onto GDP. {ECO:0000250}.
-!- DISEASE: Mental retardation, autosomal dominant 42 (MRD42)
[MIM:616973]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period. MRD42 patients
manifest global developmental delay commonly accompanied by
hypotonia, seizures of various types, ophthalmological
manifestations, and poor growth. {ECO:0000269|PubMed:25485910,
ECO:0000269|PubMed:27108799, ECO:0000269|PubMed:27668284,
ECO:0000269|PubMed:28087732}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the WD repeat G protein beta family.
{ECO:0000305}.
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EMBL; X04526; CAA28207.1; -; mRNA.
EMBL; AF501882; AAM15918.1; -; mRNA.
EMBL; BT007305; AAP35969.1; -; mRNA.
EMBL; CR456784; CAG33065.1; -; mRNA.
EMBL; AL031282; CAI20029.1; -; Genomic_DNA.
EMBL; AL109917; CAI20029.1; JOINED; Genomic_DNA.
EMBL; AL109917; CAI95654.1; -; Genomic_DNA.
EMBL; AL031282; CAI95654.1; JOINED; Genomic_DNA.
EMBL; CH471183; EAW56147.1; -; Genomic_DNA.
EMBL; BC004186; AAH04186.1; -; mRNA.
EMBL; BC005888; AAH05888.1; -; mRNA.
EMBL; BC008991; AAH08991.1; -; mRNA.
EMBL; BC114618; AAI14619.1; -; mRNA.
EMBL; M36430; AAA63265.1; -; mRNA.
CCDS; CCDS34.1; -. [P62873-1]
PIR; A24853; RGHUB1.
RefSeq; NP_001269467.1; NM_001282538.1.
RefSeq; NP_001269468.1; NM_001282539.1. [P62873-1]
RefSeq; NP_002065.1; NM_002074.4. [P62873-1]
RefSeq; XP_016856548.1; XM_017001059.1. [P62873-1]
RefSeq; XP_016856549.1; XM_017001060.1. [P62873-1]
RefSeq; XP_016856550.1; XM_017001061.1. [P62873-1]
UniGene; Hs.430425; -.
UniGene; Hs.721030; -.
PDB; 4KFM; X-ray; 3.45 A; B=1-340.
PDB; 4PNK; X-ray; 2.56 A; B=1-340.
PDB; 5HE0; X-ray; 2.56 A; B=2-340.
PDB; 5HE1; X-ray; 3.15 A; B=2-340.
PDB; 5HE2; X-ray; 2.79 A; B=2-340.
PDB; 5HE3; X-ray; 2.74 A; B=2-340.
PDB; 5UKK; X-ray; 2.60 A; B=2-340.
PDB; 5UKL; X-ray; 2.15 A; B=2-340.
PDB; 5UKM; X-ray; 3.03 A; B=2-340.
PDB; 5UZ7; EM; 4.10 A; B=2-340.
PDBsum; 4KFM; -.
PDBsum; 4PNK; -.
PDBsum; 5HE0; -.
PDBsum; 5HE1; -.
PDBsum; 5HE2; -.
PDBsum; 5HE3; -.
PDBsum; 5UKK; -.
PDBsum; 5UKL; -.
PDBsum; 5UKM; -.
PDBsum; 5UZ7; -.
ProteinModelPortal; P62873; -.
SMR; P62873; -.
BioGrid; 109044; 103.
CORUM; P62873; -.
DIP; DIP-599N; -.
IntAct; P62873; 49.
MINT; MINT-94562; -.
STRING; 9606.ENSP00000367869; -.
TCDB; 8.A.92.1.1; the g-protein AlphaBetaGama complex (gpc) family.
iPTMnet; P62873; -.
PhosphoSitePlus; P62873; -.
SwissPalm; P62873; -.
DMDM; 51317302; -.
OGP; P62873; -.
REPRODUCTION-2DPAGE; IPI00026268; -.
EPD; P62873; -.
MaxQB; P62873; -.
PaxDb; P62873; -.
PeptideAtlas; P62873; -.
PRIDE; P62873; -.
DNASU; 2782; -.
Ensembl; ENST00000378609; ENSP00000367872; ENSG00000078369. [P62873-1]
Ensembl; ENST00000610897; ENSP00000481878; ENSG00000078369. [P62873-1]
GeneID; 2782; -.
KEGG; hsa:2782; -.
UCSC; uc001aif.5; human. [P62873-1]
CTD; 2782; -.
DisGeNET; 2782; -.
EuPathDB; HostDB:ENSG00000078369.17; -.
GeneCards; GNB1; -.
HGNC; HGNC:4396; GNB1.
HPA; HPA040736; -.
MalaCards; GNB1; -.
MIM; 139380; gene.
MIM; 616973; phenotype.
neXtProt; NX_P62873; -.
OpenTargets; ENSG00000078369; -.
PharmGKB; PA28776; -.
eggNOG; KOG0286; Eukaryota.
eggNOG; ENOG410XQUX; LUCA.
GeneTree; ENSGT00760000119239; -.
HOGENOM; HOG000176356; -.
HOVERGEN; HBG000188; -.
InParanoid; P62873; -.
KO; K04536; -.
OMA; TCNVWDT; -.
OrthoDB; EOG091G0A7T; -.
PhylomeDB; P62873; -.
TreeFam; TF106149; -.
Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
Reactome; R-HSA-202040; G-protein activation.
Reactome; R-HSA-2485179; Activation of the phototransduction cascade.
Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-HSA-381753; Olfactory Signaling Pathway.
Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-392851; Prostacyclin signalling through prostacyclin receptor.
Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
Reactome; R-HSA-4086398; Ca2+ pathway.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-418597; G alpha (z) signalling events.
Reactome; R-HSA-420092; Glucagon-type ligand receptors.
Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
SignaLink; P62873; -.
SIGNOR; P62873; -.
ChiTaRS; GNB1; human.
EvolutionaryTrace; P62873; -.
GeneWiki; GNB1; -.
GenomeRNAi; 2782; -.
PRO; PR:P62873; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000078369; -.
CleanEx; HS_GNB1; -.
ExpressionAtlas; P62873; baseline and differential.
Genevisible; P62873; HS.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:MGI.
GO; GO:0005622; C:intracellular; ISS:BHF-UCL.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; ISS:BHF-UCL.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
GO; GO:0042622; C:photoreceptor outer segment membrane; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; IEA:Ensembl.
GO; GO:0003924; F:GTPase activity; IDA:MGI.
GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:MGI.
GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
GO; GO:0030507; F:spectrin binding; IEA:Ensembl.
GO; GO:0031702; F:type 1 angiotensin receptor binding; IEA:Ensembl.
GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0071870; P:cellular response to catecholamine stimulus; ISS:BHF-UCL.
GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISS:BHF-UCL.
GO; GO:0007213; P:G-protein coupled acetylcholine receptor signaling pathway; TAS:ProtInc.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0006457; P:protein folding; TAS:Reactome.
GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; TAS:ProtInc.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0016056; P:rhodopsin mediated signaling pathway; TAS:Reactome.
GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0007223; P:Wnt signaling pathway, calcium modulating pathway; TAS:Reactome.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR001632; Gprotein_B.
InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
PANTHER; PTHR19850; PTHR19850; 1.
Pfam; PF00400; WD40; 7.
PRINTS; PR00319; GPROTEINB.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Mental retardation;
Phosphoprotein; Reference proteome; Repeat; Transducer; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
CHAIN 2 340 Guanine nucleotide-binding protein
G(I)/G(S)/G(T) subunit beta-1.
/FTId=PRO_0000127687.
REPEAT 53 83 WD 1.
REPEAT 95 125 WD 2.
REPEAT 141 170 WD 3.
REPEAT 182 212 WD 4.
REPEAT 224 254 WD 5.
REPEAT 268 298 WD 6.
REPEAT 310 340 WD 7.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.8, ECO:0000269|Ref.9}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 266 266 Phosphohistidine.
{ECO:0000250|UniProtKB:P62871}.
VAR_SEQ 329 340 TGSWDSFLKIWN -> SVLG (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055232.
VARIANT 30 30 L -> F (in MRD42; unknown pathological
significance; no effect on protein
abundance; no effect on complex formation
with gamma subunit; no effect on trimer
formation with alpha and gamma subunits;
no effect on receptor-driven G protein
activation; dbSNP:rs764997309).
{ECO:0000269|PubMed:28087732}.
/FTId=VAR_078279.
VARIANT 52 52 R -> G (in MRD42; decreases receptor-
driven G protein activation; no effect on
protein abundance; no effect on complex
formation with gamma subunit; decrases
trimer formation with alpha and gamma
subunit). {ECO:0000269|PubMed:28087732}.
/FTId=VAR_078280.
VARIANT 64 64 G -> V (in MRD42; decreases receptor-
driven G protein activation; decresases
protein abundance; decreases complex
formation with gamma subunit; decrases
trimer formation with alpha and gamma
subunit). {ECO:0000269|PubMed:28087732}.
/FTId=VAR_078281.
VARIANT 76 76 D -> E (in MRD42; dbSNP:rs869312822).
{ECO:0000269|PubMed:27108799}.
/FTId=VAR_076644.
VARIANT 76 76 D -> G (in MRD42; dbSNP:rs869312821).
{ECO:0000269|PubMed:27108799}.
/FTId=VAR_076643.
VARIANT 77 77 G -> S (in MRD42; dbSNP:rs758432471).
{ECO:0000269|PubMed:27108799}.
/FTId=VAR_076645.
VARIANT 78 78 K -> R (in MRD42; dbSNP:rs869312823).
{ECO:0000269|PubMed:27108799}.
/FTId=VAR_076646.
VARIANT 80 80 I -> N (in MRD42; also found in patients
with acute lymphoblastic T-cell leukemia;
reduces interaction with GNAI2, GNAI3,
GNA13 and GNA11; induces activation of
PI3K-AKT-mTOR and MAPK pathways).
{ECO:0000269|PubMed:25485910,
ECO:0000269|PubMed:27108799}.
/FTId=VAR_076647.
VARIANT 80 80 I -> T (in MRD42; also found in patient
with hematologic malignancies; reduces
interaction with GNAI2, GNAI3, GNA13 and
GNA11; induces activation of PI3K-AKT-
mTOR and MAPK pathways;
dbSNP:rs752746786).
{ECO:0000269|PubMed:25485910,
ECO:0000269|PubMed:27108799}.
/FTId=VAR_076648.
VARIANT 91 91 H -> R (in MRD42; unknown pathological
significance; no effect on protein
abundance; no effect on complex formation
with gamma subunit; no effect on trimer
formation with apha and gamma subunits;
no effect on receptor-driven G protein
activation).
{ECO:0000269|PubMed:28087732}.
/FTId=VAR_078282.
VARIANT 92 92 A -> T (in MRD42; decreases receptor-
driven G protein activation; increases
trimer formation with alpha and gamma
subunits; no effect on protein abundance;
no effect on complex formation with gamma
subunit). {ECO:0000269|PubMed:28087732}.
/FTId=VAR_078283.
VARIANT 94 94 P -> S (in MRD42; decreases receptor-
driven G protein activation; decrases
trimer formation with alpha and gamma
subunit; no effect on protein
abundance;no effect on complex formation
with gamma subunit).
{ECO:0000269|PubMed:28087732}.
/FTId=VAR_078284.
VARIANT 95 95 L -> P (in MRD42; dbSNP:rs869312824).
{ECO:0000269|PubMed:27108799}.
/FTId=VAR_076649.
VARIANT 96 96 R -> L (in MRD42; decreases receptor-
driven G protein activation; decrases
trimer formation with alpha and gamma
subunit; no effect on protein abundance;
no effect on complex formation with gamma
subunit). {ECO:0000269|PubMed:28087732}.
/FTId=VAR_078285.
VARIANT 101 101 M -> V (in MRD42; dbSNP:rs869312825).
{ECO:0000269|PubMed:27108799}.
/FTId=VAR_076650.
VARIANT 106 106 A -> T (in MRD42; decreases receptor-
driven G protein activation; decreases
complex formation with gamma subunit;
decrases trimer formation with alpha and
gamma subunit; no effect on protein
abundance).
{ECO:0000269|PubMed:28087732}.
/FTId=VAR_078286.
VARIANT 118 118 D -> G (in MRD42; decreases receptor-
driven G protein activation; no effect on
protein abundance; no effect on complex
formation with gamma subunit; no effect
on trimer formation with alpha and gamma
subunits). {ECO:0000269|PubMed:27668284,
ECO:0000269|PubMed:28087732}.
/FTId=VAR_078287.
VARIANT 326 326 A -> T (in MRD42; dbSNP:rs869312826).
{ECO:0000269|PubMed:27108799}.
/FTId=VAR_076651.
VARIANT 337 337 K -> Q (in MRD42; unknown pathological
significance; no effect on protein
abundance; no effect on complex formation
with gamma subunit; no effect on trimer
formation with alpha and gamma subunits;
no effect on receptor-driven G protein
activation).
{ECO:0000269|PubMed:28087732}.
/FTId=VAR_078288.
HELIX 3 23 {ECO:0000244|PDB:4PNK}.
HELIX 30 33 {ECO:0000244|PDB:4PNK}.
STRAND 35 37 {ECO:0000244|PDB:4PNK}.
STRAND 47 51 {ECO:0000244|PDB:4PNK}.
STRAND 58 63 {ECO:0000244|PDB:4PNK}.
STRAND 67 74 {ECO:0000244|PDB:4PNK}.
TURN 75 77 {ECO:0000244|PDB:4PNK}.
STRAND 78 83 {ECO:0000244|PDB:4PNK}.
TURN 84 86 {ECO:0000244|PDB:4PNK}.
STRAND 89 94 {ECO:0000244|PDB:4PNK}.
STRAND 96 98 {ECO:0000244|PDB:4PNK}.
STRAND 100 105 {ECO:0000244|PDB:4PNK}.
STRAND 109 116 {ECO:0000244|PDB:4PNK}.
STRAND 120 127 {ECO:0000244|PDB:4PNK}.
STRAND 135 140 {ECO:0000244|PDB:4PNK}.
STRAND 146 153 {ECO:0000244|PDB:4PNK}.
STRAND 156 161 {ECO:0000244|PDB:4PNK}.
STRAND 166 170 {ECO:0000244|PDB:4PNK}.
TURN 171 173 {ECO:0000244|PDB:4PNK}.
STRAND 176 180 {ECO:0000244|PDB:4PNK}.
STRAND 187 192 {ECO:0000244|PDB:4PNK}.
STRAND 196 203 {ECO:0000244|PDB:4PNK}.
STRAND 208 212 {ECO:0000244|PDB:4PNK}.
TURN 213 216 {ECO:0000244|PDB:4PNK}.
STRAND 217 222 {ECO:0000244|PDB:4PNK}.
STRAND 229 234 {ECO:0000244|PDB:4PNK}.
STRAND 238 245 {ECO:0000244|PDB:4PNK}.
STRAND 250 254 {ECO:0000244|PDB:4PNK}.
TURN 255 258 {ECO:0000244|PDB:4PNK}.
STRAND 259 264 {ECO:0000244|PDB:4PNK}.
STRAND 273 278 {ECO:0000244|PDB:4PNK}.
STRAND 280 282 {ECO:0000244|PDB:5HE1}.
STRAND 284 289 {ECO:0000244|PDB:4PNK}.
STRAND 294 298 {ECO:0000244|PDB:4PNK}.
TURN 299 301 {ECO:0000244|PDB:4PNK}.
STRAND 304 308 {ECO:0000244|PDB:4PNK}.
STRAND 315 320 {ECO:0000244|PDB:4PNK}.
STRAND 327 331 {ECO:0000244|PDB:4PNK}.
STRAND 336 339 {ECO:0000244|PDB:4PNK}.
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


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