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Gamma-aminobutyric acid type B receptor subunit 1 (GABA-B receptor 1) (GABA-B-R1) (GABA-BR1) (GABABR1) (Gb1)

 GABR1_HUMAN             Reviewed;         961 AA.
Q9UBS5; B0UXY7; O95375; O95468; O95975; O96022; Q5STL4; Q5SUJ8;
Q5SUL3; Q71SG6; Q86W60; Q9UQQ0;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 177.
RecName: Full=Gamma-aminobutyric acid type B receptor subunit 1;
Short=GABA-B receptor 1;
Short=GABA-B-R1;
Short=GABA-BR1;
Short=GABABR1;
Short=Gb1;
Flags: Precursor;
Name=GABBR1; Synonyms=GPRC3A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
TISSUE=Cerebellum {ECO:0000303|PubMed:9844003};
PubMed=9844003; DOI=10.1073/pnas.95.25.14991;
Kaupmann K., Schuler V., Mosbacher J., Bischoff S., Bittiger H.,
Heid J., Froestl W., Leonhard S., Pfaff T., Karschin A., Bettler B.;
"Human gamma-aminobutyric acid type B receptors are differentially
expressed and regulate inwardly rectifying K+ channels.";
Proc. Natl. Acad. Sci. U.S.A. 95:14991-14996(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C), FUNCTION,
SUBUNIT, INTERACTION WITH GABBR2, AND SUBCELLULAR LOCATION.
TISSUE=Cerebellum {ECO:0000303|PubMed:9872316};
PubMed=9872316; DOI=10.1038/25354;
White J.H., Wise A., Main M.J., Green A., Fraser N.J., Disney G.H.,
Barnes A.A., Emson P., Foord S.M., Marshall F.H.;
"Heterodimerization is required for the formation of a functional
GABA(B) receptor.";
Nature 396:679-682(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
TISSUE=Brain {ECO:0000303|Ref.3};
Stropp U., Raming K.;
"Human mRNA for GABA-B1a receptor.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), AND TISSUE SPECIFICITY.
TISSUE=Fetal brain {ECO:0000303|PubMed:9753614};
PubMed=9753614; DOI=10.1006/bbrc.1998.9296;
Grifa A., Totaro A., Rommens J.M., Carella M., Roetto A., Borgato L.,
Zelante L., Gasparini P.;
"GABA (gamma-amino-butyric acid) neurotransmission: identification and
fine mapping of the human GABAB receptor gene.";
Biochem. Biophys. Res. Commun. 250:240-245(1998).
[5]
NUCLEOTIDE SEQUENCE (ISOFORM 1A).
PubMed=9798068; DOI=10.1016/S0006-3223(98)00244-3;
Goei V.L., Choi J., Ahn J., Bowlus C.L., Raha-Chowdhury R.,
Gruen J.R.;
"Human gamma-aminobutyric acid B receptor gene: complementary DNA
cloning, expression, chromosomal location, and genomic organization.";
Biol. Psychiatry 44:659-666(1998).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1C).
TISSUE=Cerebellum {ECO:0000303|Ref.6};
Fraser N.J.;
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A AND 1B), AND VARIANTS
VAL-20 AND SER-489.
TISSUE=Fetal brain {ECO:0000303|PubMed:9933300};
PubMed=9933300; DOI=10.1007/s100480050051;
Peters H.C., Kaemmer G., Volz A., Kaupmann K., Ziegler A., Bettler B.,
Epplen J.T., Sander T., Riess O.;
"Mapping, genomic structure, and polymorphisms of the human GABABR1
receptor gene: evaluation of its involvement in idiopathic generalized
epilepsy.";
Neurogenetics 2:47-54(1998).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
TISSUE=Cerebellum {ECO:0000303|PubMed:9889352};
PubMed=9889352; DOI=10.1016/S0169-328X(98)00316-7;
Makoff A.;
"Molecular cloning of human GABABR1 and its tissue distribution.";
Brain Res. Mol. Brain Res. 64:137-140(1999).
[9]
NUCLEOTIDE SEQUENCE (ISOFORM 1E), FUNCTION, SUBUNIT, INTERACTION WITH
GABBR2, TISSUE SPECIFICITY, AND VARIANT SER-489.
TISSUE=Prostate {ECO:0000303|PubMed:10906333};
PubMed=10906333; DOI=10.1074/jbc.M005333200;
Schwarz D.A., Barry G., Eliasof S.D., Petroski R.E., Conlon P.J.,
Maki R.A.;
"Characterization of gamma-aminobutyric acid receptor GABAB(1e), a
GABAB(1) splice variant encoding a truncated receptor.";
J. Biol. Chem. 275:32174-32181(2000).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-20.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[11]
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.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B).
TISSUE=Brain {ECO:0000303|PubMed:15489334};
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).
[13]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[14]
FUNCTION, AND INTERACTION WITH GABBR2.
PubMed=10773016;
Sullivan R., Chateauneuf A., Coulombe N., Kolakowski L.F. Jr.,
Johnson M.P., Hebert T.E., Ethier N., Belley M., Metters K.,
Abramovitz M., O'Neill G.P., Ng G.Y.K.;
"Coexpression of full-length gamma-aminobutyric acid(B) (GABA(B))
receptors with truncated receptors and metabotropic glutamate receptor
4 supports the GABA(B) heterodimer as the functional receptor.";
J. Pharmacol. Exp. Ther. 293:460-467(2000).
[15]
FUNCTION.
PubMed=10075644; DOI=10.1074/jbc.274.12.7607;
Ng G.Y.K., Clark J., Coulombe N., Ethier N., Hebert T.E., Sullivan R.,
Kargman S., Chateauneuf A., Tsukamoto N., McDonald T., Whiting P.,
Mezey E., Johnson M.P., Liu Q., Kolakowski L.F. Jr., Evans J.F.,
Bonner T.I., O'Neill G.P.;
"Identification of a GABAB receptor subunit, gb2, required for
functional GABAB receptor activity.";
J. Biol. Chem. 274:7607-7610(1999).
[16]
FUNCTION, INTERACTION WITH GABBR2, TISSUE SPECIFICITY, AND DOMAIN.
PubMed=9872744; DOI=10.1126/science.283.5398.74;
Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A.,
Kornau H.-C.;
"Role of heteromer formation in GABAB receptor function.";
Science 283:74-77(1999).
[17]
INTERACTION WITH JAKMIP1.
PubMed=14718537; DOI=10.1074/jbc.M311737200;
Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
"Marlin-1, a novel RNA-binding protein associates with GABA
receptors.";
J. Biol. Chem. 279:13934-13943(2004).
[18]
FUNCTION, INTERACTION WITH GABBR2, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15617512; DOI=10.1042/BJ20041435;
Villemure J.F., Adam L., Bevan N.J., Gearing K., Chenier S.,
Bouvier M.;
"Subcellular distribution of GABA(B) receptor homo- and hetero-
dimers.";
Biochem. J. 388:47-55(2005).
[19]
FUNCTION, AND INTERACTION WITH GABBR2.
PubMed=18165688; DOI=10.1074/jbc.M705202200;
Nomura R., Suzuki Y., Kakizuka A., Jingami H.;
"Direct detection of the interaction between recombinant soluble
extracellular regions in the heterodimeric metabotropic gamma-
aminobutyric acid receptor.";
J. Biol. Chem. 283:4665-4673(2008).
[20]
FUNCTION, PARTIAL PROTEIN SEQUENCE, AGONIST BINDING, MUTAGENESIS OF
TYR-230 AND TYR-234, AND INTERACTION WITH GABBR2.
PubMed=22660477; DOI=10.1038/nn.3133;
Geng Y., Xiong D., Mosyak L., Malito D.L., Kniazeff J., Chen Y.,
Burmakina S., Quick M., Bush M., Javitch J.A., Pin J.P., Fan Q.R.;
"Structure and functional interaction of the extracellular domain of
human GABA(B) receptor GBR2.";
Nat. Neurosci. 15:970-978(2012).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 165-576 IN COMPLEXES WITH
GABBR2; AGONISTS AND ANTAGONISTS, FUNCTION, SUBUNIT, DISULFIDE BOND,
GLYCOSYLATION AT ASN-440 AND ASN-482, AND MUTAGENESIS OF TRP-182;
HIS-287; TYR-367 AND TRP-395.
PubMed=24305054; DOI=10.1038/nature12725;
Geng Y., Bush M., Mosyak L., Wang F., Fan Q.R.;
"Structural mechanism of ligand activation in human GABA(B)
receptor.";
Nature 504:254-259(2013).
[22]
VARIANTS VAL-20 AND SER-489.
PubMed=10402495;
DOI=10.1002/(SICI)1096-8628(19990820)88:4<305::AID-AJMG5>3.0.CO;2-X;
Sander T., Peters C., Kaemmer G., Samochowiec J., Zirra M.,
Mischke D., Ziegler A., Kaupmann K., Bettler B., Epplen J.T.,
Riess O.;
"Association analysis of exonic variants of the gene encoding the
GABAB receptor and idiopathic generalized epilepsy.";
Am. J. Med. Genet. 88:305-310(1999).
-!- FUNCTION: Component of a heterodimeric G-protein coupled receptor
for GABA, formed by GABBR1 and GABBR2 (PubMed:9872316,
PubMed:9872744, PubMed:15617512, PubMed:18165688, PubMed:22660477,
PubMed:24305054). Within the heterodimeric GABA receptor, only
GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G
proteins (PubMed:18165688). Ligand binding causes a conformation
change that triggers signaling via guanine nucleotide-binding
proteins (G proteins) and modulates the activity of down-stream
effectors, such as adenylate cyclase (PubMed:10906333,
PubMed:10773016, PubMed:10075644, PubMed:9872744,
PubMed:24305054). Signaling inhibits adenylate cyclase, stimulates
phospholipase A2, activates potassium channels, inactivates
voltage-dependent calcium-channels and modulates inositol
phospholipid hydrolysis (PubMed:10075644). Calcium is required for
high affinity binding to GABA (By similarity). Plays a critical
role in the fine-tuning of inhibitory synaptic transmission
(PubMed:9844003). Pre-synaptic GABA receptor inhibits
neurotransmitter release by down-regulating high-voltage activated
calcium channels, whereas postsynaptic GABA receptor decreases
neuronal excitability by activating a prominent inwardly
rectifying potassium (Kir) conductance that underlies the late
inhibitory postsynaptic potentials (PubMed:9844003,
PubMed:9872316, PubMed:10075644, PubMed:9872744, PubMed:22660477).
Not only implicated in synaptic inhibition but also in hippocampal
long-term potentiation, slow wave sleep, muscle relaxation and
antinociception (Probable). Activated by (-)-baclofen, cgp27492
and blocked by phaclofen (PubMed:9844003, PubMed:9872316,
PubMed:24305054). {ECO:0000250|UniProtKB:Q9Z0U4,
ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016,
ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:15617512,
ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477,
ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9844003,
ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744,
ECO:0000305}.
-!- FUNCTION: Isoform 1E may regulate the formation of functional
GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This
could explain the observation that certain small molecule ligands
exhibit differential affinity for central versus peripheral sites.
-!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:9872316,
PubMed:10773016, PubMed:9872744, PubMed:15617512, PubMed:18165688,
PubMed:22660477, PubMed:24305054). Homodimers may form, but are
inactive (PubMed:9872316, PubMed:15617512). Isoform 1E (without C-
terminal intracellular domain) is unable to dimerize via a coiled-
coil interaction with GABBR2 (PubMed:10906333). Interacts (via C-
terminus) with ATF4 (via leucine zipper domain) (By similarity).
Interacts with JAKMIP1 (PubMed:14718537).
{ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:10773016,
ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:14718537,
ECO:0000269|PubMed:15617512, ECO:0000269|PubMed:18165688,
ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054,
ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744}.
-!- INTERACTION:
O75899:GABBR2; NbExp=3; IntAct=EBI-16084001, EBI-715469;
P61244:MAX; NbExp=3; IntAct=EBI-724156, EBI-751711;
P16333:NCK1; NbExp=3; IntAct=EBI-724156, EBI-389883;
P46459:NSF; NbExp=3; IntAct=EBI-724156, EBI-712251;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15617512};
Multi-pass membrane protein {ECO:0000305}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9Z0U4}; Multi-
pass membrane protein {ECO:0000305}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q9Z0U4}. Note=Colocalizes with ATF4 in
hippocampal neuron dendritic membranes (By similarity).
Coexpression of GABBR1 and GABBR2 is required for GABBR1
maturation and transport to the plasma membrane (PubMed:15617512).
{ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:15617512}.
-!- SUBCELLULAR LOCATION: Isoform 1E: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Comment=Isoforms corresponding to the full receptor are
essentially found in the central nervous system (CNS).;
Name=1A;
IsoId=Q9UBS5-1; Sequence=Displayed;
Name=1B;
IsoId=Q9UBS5-2; Sequence=VSP_002037;
Name=1C;
IsoId=Q9UBS5-3; Sequence=VSP_002038;
Name=1D;
IsoId=Q9UBS5-4; Sequence=VSP_002040;
Name=1E; Synonyms=Truncated;
IsoId=Q9UBS5-5; Sequence=VSP_002039;
Note=Major isoform in almost all peripheral tissues, although
containing a premature stop codon in the mRNA and thus being a
potential target for nonsense-mediated mRNA decay. May act as an
antagonist of GABA-B receptors, being able to disrupt the normal
association between isoform 1A and GABBR2.
{ECO:0000269|PubMed:10906333};
-!- TISSUE SPECIFICITY: Highly expressed in brain (PubMed:9844003,
PubMed:9753614, PubMed:9872744). Weakly expressed in heart, small
intestine and uterus. Isoform 1A: Mainly expressed in granular
cell and molecular layer (PubMed:9844003). Isoform 1B: Mainly
expressed in Purkinje cells (PubMed:9844003). Isoform 1E:
Predominantly expressed in peripheral tissues as kidney, lung,
trachea, colon, small intestine, stomach, bone marrow, thymus and
mammary gland (PubMed:10906333). {ECO:0000269|PubMed:10906333,
ECO:0000269|PubMed:9753614, ECO:0000269|PubMed:9844003,
ECO:0000269|PubMed:9872744}.
-!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
mediate heterodimeric interaction with GABBR2 (PubMed:9872744).
The linker region between the transmembrane domain 3 (TM3) and the
transmembrane domain 4 (TM4) probably plays a role in the
specificity for G-protein coupling (PubMed:9844003).
{ECO:0000305|PubMed:9844003, ECO:0000305|PubMed:9872744}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
GABA-B receptor subfamily. {ECO:0000305}.
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EMBL; AJ225028; CAA12359.1; -; mRNA.
EMBL; AJ225029; CAA12360.1; -; mRNA.
EMBL; AJ012185; CAA09939.1; -; mRNA.
EMBL; AJ012186; CAA09940.1; -; mRNA.
EMBL; AF099148; AAC98508.1; -; mRNA.
EMBL; Y11044; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AJ012187; CAA09941.1; -; mRNA.
EMBL; AJ010170; CAA09031.1; -; Genomic_DNA.
EMBL; AJ010171; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010172; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010173; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010174; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010175; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010176; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010177; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010178; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010179; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010180; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010181; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010182; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010183; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010184; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010185; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010186; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010187; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010188; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010189; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010190; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ010191; CAA09031.1; JOINED; Genomic_DNA.
EMBL; AJ012288; CAA09980.1; -; mRNA.
EMBL; AF301005; AAG23962.1; -; mRNA.
EMBL; AL031983; CAA21453.1; -; Genomic_DNA.
EMBL; AL031983; CAA21454.1; -; Genomic_DNA.
EMBL; AL662826; CAI17390.1; -; Genomic_DNA.
EMBL; AL662826; CAI17391.2; -; Genomic_DNA.
EMBL; AL645936; CAI18016.1; -; Genomic_DNA.
EMBL; AL645936; CAI18017.1; -; Genomic_DNA.
EMBL; BX000688; CAI18605.1; -; Genomic_DNA.
EMBL; BX000688; CAI18606.1; -; Genomic_DNA.
EMBL; CR759766; CAQ06609.1; -; Genomic_DNA.
EMBL; CR759766; CAQ06610.1; -; Genomic_DNA.
EMBL; CR788300; CAQ07763.1; -; Genomic_DNA.
EMBL; CR936483; CAQ07763.1; JOINED; Genomic_DNA.
EMBL; CR788300; CAQ07764.1; -; Genomic_DNA.
EMBL; CR936483; CAQ07764.1; JOINED; Genomic_DNA.
EMBL; CR388210; CAQ09395.1; -; Genomic_DNA.
EMBL; CR759870; CAQ09878.1; -; Genomic_DNA.
EMBL; CR759870; CAQ09879.1; -; Genomic_DNA.
EMBL; CR936483; CAQ10082.1; -; Genomic_DNA.
EMBL; CR788300; CAQ10082.1; JOINED; Genomic_DNA.
EMBL; CR936483; CAQ10083.1; -; Genomic_DNA.
EMBL; CR788300; CAQ10083.1; JOINED; Genomic_DNA.
EMBL; CH471081; EAX03205.1; -; Genomic_DNA.
EMBL; CH471081; EAX03210.1; -; Genomic_DNA.
EMBL; BC042598; AAH42598.1; -; mRNA.
EMBL; BC050532; AAH50532.2; -; mRNA.
CCDS; CCDS4663.1; -. [Q9UBS5-1]
CCDS; CCDS4664.1; -. [Q9UBS5-3]
CCDS; CCDS4665.1; -. [Q9UBS5-2]
PIR; JE0356; JE0356.
RefSeq; NP_001305982.1; NM_001319053.1.
RefSeq; NP_001461.1; NM_001470.3. [Q9UBS5-1]
RefSeq; NP_068703.1; NM_021903.2. [Q9UBS5-2]
RefSeq; NP_068704.2; NM_021904.3. [Q9UBS5-3]
UniGene; Hs.167017; -.
PDB; 4MQE; X-ray; 2.35 A; A=165-576.
PDB; 4MQF; X-ray; 2.22 A; A=165-576.
PDB; 4MR7; X-ray; 2.15 A; A=165-576.
PDB; 4MR8; X-ray; 2.15 A; A=165-576.
PDB; 4MR9; X-ray; 2.35 A; A=165-576.
PDB; 4MRM; X-ray; 2.86 A; A=165-576.
PDB; 4MS1; X-ray; 2.25 A; A=165-576.
PDB; 4MS3; X-ray; 2.50 A; A=165-576.
PDB; 4MS4; X-ray; 1.90 A; A=165-576.
PDB; 4PAS; X-ray; 1.62 A; A=879-919.
PDBsum; 4MQE; -.
PDBsum; 4MQF; -.
PDBsum; 4MR7; -.
PDBsum; 4MR8; -.
PDBsum; 4MR9; -.
PDBsum; 4MRM; -.
PDBsum; 4MS1; -.
PDBsum; 4MS3; -.
PDBsum; 4MS4; -.
PDBsum; 4PAS; -.
ProteinModelPortal; Q9UBS5; -.
SMR; Q9UBS5; -.
BioGrid; 108825; 22.
CORUM; Q9UBS5; -.
DIP; DIP-38394N; -.
IntAct; Q9UBS5; 11.
MINT; MINT-2793192; -.
STRING; 9606.ENSP00000366233; -.
BindingDB; Q9UBS5; -.
ChEMBL; CHEMBL2064; -.
DrugBank; DB08891; Arbaclofen.
DrugBank; DB08892; Arbaclofen Placarbil.
DrugBank; DB00181; Baclofen.
DrugBank; DB00837; Progabide.
DrugBank; DB05010; SGS742.
DrugBank; DB01080; Vigabatrin.
GuidetoPHARMACOLOGY; 240; -.
iPTMnet; Q9UBS5; -.
PhosphoSitePlus; Q9UBS5; -.
BioMuta; GABBR1; -.
DMDM; 12643873; -.
PaxDb; Q9UBS5; -.
PeptideAtlas; Q9UBS5; -.
PRIDE; Q9UBS5; -.
DNASU; 2550; -.
Ensembl; ENST00000355973; ENSP00000348248; ENSG00000204681. [Q9UBS5-2]
Ensembl; ENST00000376977; ENSP00000366176; ENSG00000204681. [Q9UBS5-5]
Ensembl; ENST00000377012; ENSP00000366211; ENSG00000204681. [Q9UBS5-2]
Ensembl; ENST00000377016; ENSP00000366215; ENSG00000204681. [Q9UBS5-3]
Ensembl; ENST00000377034; ENSP00000366233; ENSG00000204681. [Q9UBS5-1]
Ensembl; ENST00000383537; ENSP00000373029; ENSG00000206466. [Q9UBS5-2]
Ensembl; ENST00000383541; ENSP00000373033; ENSG00000206466. [Q9UBS5-3]
Ensembl; ENST00000383542; ENSP00000373034; ENSG00000206466. [Q9UBS5-1]
Ensembl; ENST00000383543; ENSP00000373035; ENSG00000206466. [Q9UBS5-2]
Ensembl; ENST00000383636; ENSP00000373132; ENSG00000206511. [Q9UBS5-2]
Ensembl; ENST00000383637; ENSP00000373133; ENSG00000206511. [Q9UBS5-3]
Ensembl; ENST00000383638; ENSP00000373134; ENSG00000206511. [Q9UBS5-1]
Ensembl; ENST00000383639; ENSP00000373135; ENSG00000206511. [Q9UBS5-2]
Ensembl; ENST00000414980; ENSP00000406499; ENSG00000232632. [Q9UBS5-2]
Ensembl; ENST00000417759; ENSP00000391572; ENSG00000237112. [Q9UBS5-2]
Ensembl; ENST00000419674; ENSP00000399861; ENSG00000232569. [Q9UBS5-3]
Ensembl; ENST00000423604; ENSP00000388035; ENSG00000232632. [Q9UBS5-1]
Ensembl; ENST00000425097; ENSP00000411286; ENSG00000237112. [Q9UBS5-1]
Ensembl; ENST00000434660; ENSP00000412167; ENSG00000232632. [Q9UBS5-3]
Ensembl; ENST00000438094; ENSP00000406285; ENSG00000232632. [Q9UBS5-2]
Ensembl; ENST00000439457; ENSP00000406066; ENSG00000232569. [Q9UBS5-1]
Ensembl; ENST00000443440; ENSP00000399318; ENSG00000237112. [Q9UBS5-3]
Ensembl; ENST00000446436; ENSP00000394528; ENSG00000237112. [Q9UBS5-2]
Ensembl; ENST00000448754; ENSP00000405709; ENSG00000237051. [Q9UBS5-2]
Ensembl; ENST00000449163; ENSP00000411263; ENSG00000232569. [Q9UBS5-2]
Ensembl; ENST00000452300; ENSP00000408938; ENSG00000232569. [Q9UBS5-2]
Ensembl; ENST00000458612; ENSP00000416903; ENSG00000237051. [Q9UBS5-2]
Ensembl; ENST00000494877; ENSP00000419061; ENSG00000204681. [Q9UBS5-5]
Ensembl; ENST00000546913; ENSP00000448999; ENSG00000232569. [Q9UBS5-1]
Ensembl; ENST00000547410; ENSP00000448531; ENSG00000232569. [Q9UBS5-5]
Ensembl; ENST00000548767; ENSP00000446983; ENSG00000232632. [Q9UBS5-5]
Ensembl; ENST00000551140; ENSP00000448654; ENSG00000237112. [Q9UBS5-5]
Ensembl; ENST00000551423; ENSP00000449342; ENSG00000206511. [Q9UBS5-5]
Ensembl; ENST00000552399; ENSP00000449449; ENSG00000206466. [Q9UBS5-5]
GeneID; 2550; -.
KEGG; hsa:2550; -.
UCSC; uc003nmp.5; human. [Q9UBS5-1]
CTD; 2550; -.
DisGeNET; 2550; -.
EuPathDB; HostDB:ENSG00000204681.10; -.
GeneCards; GABBR1; -.
HGNC; HGNC:4070; GABBR1.
HPA; HPA050483; -.
HPA; HPA058459; -.
MIM; 603540; gene.
neXtProt; NX_Q9UBS5; -.
OpenTargets; ENSG00000204681; -.
PharmGKB; PA28484; -.
eggNOG; KOG1055; Eukaryota.
eggNOG; ENOG410XNN1; LUCA.
GeneTree; ENSGT00530000063129; -.
HOGENOM; HOG000171607; -.
HOVERGEN; HBG051688; -.
InParanoid; Q9UBS5; -.
KO; K04615; -.
OMA; PKICQAR; -.
OrthoDB; EOG091G01WG; -.
PhylomeDB; Q9UBS5; -.
TreeFam; TF313965; -.
Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
Reactome; R-HSA-977444; GABA B receptor activation.
Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
SIGNOR; Q9UBS5; -.
ChiTaRS; GABBR1; human.
GeneWiki; GABBR1; -.
GenomeRNAi; 2550; -.
PRO; PR:Q9UBS5; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204681; -.
CleanEx; HS_GABBR1; -.
ExpressionAtlas; Q9UBS5; baseline and differential.
Genevisible; Q9UBS5; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0038039; C:G-protein coupled receptor heterodimeric complex; IPI:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
GO; GO:0004965; F:G-protein coupled GABA receptor activity; IDA:UniProtKB.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:UniProtKB.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc.
CDD; cd15291; 7tmC_GABA-B-R1; 1.
CDD; cd00033; CCP; 1.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR002455; GPCR3_GABA-B.
InterPro; IPR017978; GPCR_3_C.
InterPro; IPR002456; GPCR_3_GABA_rcpt_B1.
InterPro; IPR028082; Peripla_BP_I.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
PANTHER; PTHR10519; PTHR10519; 1.
Pfam; PF00003; 7tm_3; 1.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00084; Sushi; 1.
SMART; SM00032; CCP; 2.
SUPFAM; SSF53822; SSF53822; 1.
SUPFAM; SSF57535; SSF57535; 2.
PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PROSITE; PS50923; SUSHI; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Coiled coil; Complete proteome;
Direct protein sequencing; Disulfide bond; G-protein coupled receptor;
Glycoprotein; Membrane; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Receptor; Reference proteome; Repeat;
Secreted; Signal; Sushi; Synapse; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 14 {ECO:0000255}.
CHAIN 15 961 Gamma-aminobutyric acid type B receptor
subunit 1.
/FTId=PRO_0000012949.
TOPO_DOM 15 591 Extracellular. {ECO:0000255}.
TRANSMEM 592 612 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 613 631 Cytoplasmic. {ECO:0000255}.
TRANSMEM 632 652 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 653 667 Extracellular. {ECO:0000255}.
TRANSMEM 668 688 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 689 710 Cytoplasmic. {ECO:0000255}.
TRANSMEM 711 731 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 732 768 Extracellular. {ECO:0000255}.
TRANSMEM 769 789 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 790 804 Cytoplasmic. {ECO:0000255}.
TRANSMEM 805 825 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 826 833 Extracellular. {ECO:0000255}.
TRANSMEM 834 854 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 855 961 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 96 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 98 159 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 888 916 Interaction with ATF4. {ECO:0000250}.
COILED 869 925 {ECO:0000255}.
BINDING 247 247 Agonist.
BINDING 270 270 Agonist.
BINDING 287 287 Agonist.
BINDING 367 367 Agonist.
BINDING 395 395 Agonist.
BINDING 466 466 Agonist.
MOD_RES 873 873 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9WV18}.
MOD_RES 930 930 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9WV18}.
CARBOHYD 24 24 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 84 84 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 440 440 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:24305054}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:24305054}.
CARBOHYD 502 502 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 514 514 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 100 145 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 131 157 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 220 246 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:24305054}.
DISULFID 376 410 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:24305054}.
VAR_SEQ 1 164 MLLLLLLAPLFLRPPGAGGAQTPNATSEGCQIIHPPWEGGI
RYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCL
ANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALD
GARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH
-> MGPGAPFARVGWPLPLLVVMAAGVAPVWASHSPHLPRP
HSRVPPHPS (in isoform 1B).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9844003,
ECO:0000303|PubMed:9872316}.
/FTId=VSP_002037.
VAR_SEQ 98 159 Missing (in isoform 1C).
{ECO:0000303|PubMed:9872316,
ECO:0000303|Ref.6}.
/FTId=VSP_002038.
VAR_SEQ 570 961 GGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCL
SFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDG
YHIGRNQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVF
TKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDP
LHRTIETFAKEEPKEDIDVSILPQLEHCSSRKMNTWLGIFY
GYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVL
CLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPK
MRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRE
LEKIIAEKEERVSELRHQLQSRQQLRSRRHPPTPPEPSGGL
PRGPPEPPDRLSCDGSRVHLLYK -> VISRTHSPT (in
isoform 1E). {ECO:0000305}.
/FTId=VSP_002039.
VAR_SEQ 905 961 KEERVSELRHQLQSRQQLRSRRHPPTPPEPSGGLPRGPPEP
PDRLSCDGSRVHLLYK -> SGGLPRGPPEPPDRLSCDGSR
VHLLYK (in isoform 1D). {ECO:0000305}.
/FTId=VSP_002040.
VARIANT 20 20 A -> V (in dbSNP:rs1805056).
{ECO:0000269|PubMed:10402495,
ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:9933300}.
/FTId=VAR_010146.
VARIANT 489 489 G -> S (in dbSNP:rs1805057).
{ECO:0000269|PubMed:10402495,
ECO:0000269|PubMed:10906333,
ECO:0000269|PubMed:9933300}.
/FTId=VAR_010147.
VARIANT 645 645 F -> L (in dbSNP:rs2076489).
/FTId=VAR_049279.
MUTAGEN 182 182 W->A: Abolishes signaling via G-proteins.
Abolishes antagonist binding.
{ECO:0000269|PubMed:24305054}.
MUTAGEN 230 230 Y->A: Slightly decreases signaling via G-
proteins. {ECO:0000269|PubMed:22660477}.
MUTAGEN 234 234 Y->A: Decreases signaling via G-proteins.
{ECO:0000269|PubMed:22660477}.
MUTAGEN 287 287 H->A: Strongly reduces signaling via G-
proteins. Abolishes antagonist binding.
{ECO:0000269|PubMed:24305054}.
MUTAGEN 367 367 Y->A: Strongly reduces signaling via G-
proteins. No effect on antagonist
binding. {ECO:0000269|PubMed:24305054}.
MUTAGEN 395 395 W->A: Strongly reduces signaling via G-
proteins. Strongly reduces antagonist
binding. {ECO:0000269|PubMed:24305054}.
CONFLICT 2 2 L -> M (in Ref. 4; Y11044).
{ECO:0000305}.
CONFLICT 21 21 Q -> H (in Ref. 2; CAA09939/CAA09941).
{ECO:0000305}.
CONFLICT 93 93 P -> L (in Ref. 3; AAC98508).
{ECO:0000305}.
CONFLICT 127 127 V -> A (in Ref. 2; CAA09939).
{ECO:0000305}.
CONFLICT 322 322 Missing (in Ref. 7; CAA09031).
{ECO:0000305}.
CONFLICT 542 542 L -> P (in Ref. 4; Y11044).
{ECO:0000305}.
CONFLICT 691 691 V -> G (in Ref. 4; Y11044).
{ECO:0000305}.
CONFLICT 905 934 Missing (in Ref. 7; CAA09031).
{ECO:0000305}.
STRAND 168 176 {ECO:0000244|PDB:4MS4}.
STRAND 178 181 {ECO:0000244|PDB:4MS4}.
HELIX 185 200 {ECO:0000244|PDB:4MS4}.
TURN 203 205 {ECO:0000244|PDB:4MS4}.
STRAND 209 217 {ECO:0000244|PDB:4MS4}.
HELIX 222 233 {ECO:0000244|PDB:4MS4}.
STRAND 234 237 {ECO:0000244|PDB:4MS4}.
STRAND 240 243 {ECO:0000244|PDB:4MS4}.
HELIX 247 256 {ECO:0000244|PDB:4MS4}.
HELIX 257 260 {ECO:0000244|PDB:4MS4}.
STRAND 263 268 {ECO:0000244|PDB:4MS4}.
HELIX 272 275 {ECO:0000244|PDB:4MS4}.
TURN 277 279 {ECO:0000244|PDB:4MS4}.
STRAND 283 287 {ECO:0000244|PDB:4MS4}.
HELIX 290 292 {ECO:0000244|PDB:4MS4}.
HELIX 293 303 {ECO:0000244|PDB:4MS4}.
STRAND 308 316 {ECO:0000244|PDB:4MS4}.
HELIX 317 332 {ECO:0000244|PDB:4MS4}.
STRAND 336 345 {ECO:0000244|PDB:4MS4}.
HELIX 348 356 {ECO:0000244|PDB:4MS4}.
STRAND 361 365 {ECO:0000244|PDB:4MS4}.
HELIX 368 381 {ECO:0000244|PDB:4MS4}.
STRAND 385 387 {ECO:0000244|PDB:4MRM}.
STRAND 389 393 {ECO:0000244|PDB:4MS4}.
HELIX 400 402 {ECO:0000244|PDB:4MS4}.
HELIX 412 419 {ECO:0000244|PDB:4MS4}.
STRAND 423 427 {ECO:0000244|PDB:4MS4}.
HELIX 443 453 {ECO:0000244|PDB:4MS4}.
HELIX 458 460 {ECO:0000244|PDB:4MS4}.
TURN 462 466 {ECO:0000244|PDB:4MS4}.
HELIX 467 484 {ECO:0000244|PDB:4MS4}.
HELIX 495 497 {ECO:0000244|PDB:4MS4}.
HELIX 504 514 {ECO:0000244|PDB:4MS4}.
STRAND 517 520 {ECO:0000244|PDB:4MS4}.
STRAND 523 526 {ECO:0000244|PDB:4MS4}.
TURN 529 531 {ECO:0000244|PDB:4MS4}.
STRAND 536 543 {ECO:0000244|PDB:4MS4}.
STRAND 546 554 {ECO:0000244|PDB:4MS4}.
TURN 555 558 {ECO:0000244|PDB:4MS4}.
STRAND 559 562 {ECO:0000244|PDB:4MS4}.
HELIX 569 571 {ECO:0000244|PDB:4MS4}.
HELIX 885 917 {ECO:0000244|PDB:4PAS}.
SEQUENCE 961 AA; 108320 MW; 54E7349CD02B633F CRC64;
MLLLLLLAPL FLRPPGAGGA QTPNATSEGC QIIHPPWEGG IRYRGLTRDQ VKAINFLPVD
YEIEYVCRGE REVVGPKVRK CLANGSWTDM DTPSRCVRIC SKSYLTLENG KVFLTGGDLP
ALDGARVDFR CDPDFHLVGS SRSICSQGQW STPKPHCQVN RTPHSERRAV YIGALFPMSG
GWPGGQACQP AVEMALEDVN SRRDILPDYE LKLIHHDSKC DPGQATKYLY ELLYNDPIKI
ILMPGCSSVS TLVAEAARMW NLIVLSYGSS SPALSNRQRF PTFFRTHPSA TLHNPTRVKL
FEKWGWKKIA TIQQTTEVFT STLDDLEERV KEAGIEITFR QSFFSDPAVP VKNLKRQDAR
IIVGLFYETE ARKVFCEVYK ERLFGKKYVW FLIGWYADNW FKIYDPSINC TVDEMTEAVE
GHITTEIVML NPANTRSISN MTSQEFVEKL TKRLKRHPEE TGGFQEAPLA YDAIWALALA
LNKTSGGGGR SGVRLEDFNY NNQTITDQIY RAMNSSSFEG VSGHVVFDAS GSRMAWTLIE
QLQGGSYKKI GYYDSTKDDL SWSKTDKWIG GSPPADQTLV IKTFRFLSQK LFISVSVLSS
LGIVLAVVCL SFNIYNSHVR YIQNSQPNLN NLTAVGCSLA LAAVFPLGLD GYHIGRNQFP
FVCQARLWLL GLGFSLGYGS MFTKIWWVHT VFTKKEEKKE WRKTLEPWKL YATVGLLVGM
DVLTLAIWQI VDPLHRTIET FAKEEPKEDI DVSILPQLEH CSSRKMNTWL GIFYGYKGLL
LLLGIFLAYE TKSVSTEKIN DHRAVGMAIY NVAVLCLITA PVTMILSSQQ DAAFAFASLA
IVFSSYITLV VLFVPKMRRL ITRGEWQSEA QDTMKTGSST NNNEEEKSRL LEKENRELEK
IIAEKEERVS ELRHQLQSRQ QLRSRRHPPT PPEPSGGLPR GPPEPPDRLS CDGSRVHLLY
K


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18-001-30022 Gamma-aminobutyric acid type B receptor. subunit 2 - GABA-B receptor 2; GABA-B-R2; Gb2; GABABR2; G-protein coupled receptor 51 Polyclonal 0.1 mg
18-662-20062 Gamma-aminobutyric acid type B receptor. subunit 2 - GABA-B receptor 2; GABA-B-R2; Gb2; GABABR2; G-protein coupled receptor 51 Polyclonal 0.1 ml
27-228 GABRG2 is a gamma-aminobutyric acid (GABA) receptor. GABA is the major inhibitory neurotransmitter in the mammlian brain, where it acts at GABA-A receptors, which are ligand-gated chloride channels. G 0.05 mg
28-313 Gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain, mediates neuronal inhibition by binding to GABA receptors. The type A GABA receptors are pentameric chloride channel 0.1 mg
31-104 The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes GABA A rece 0.1 mg
28-272 The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes GABA A rece 0.1 mg
28-229 The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. GABRB2 encodes GABA A recepto 0.05 mg
28-265 The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes GABA A rece 0.05 mg
18-003-42956 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.1 mg Protein A
18-003-42957 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.1 mg Protein A
18-003-42955 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.1 mg Protein A
18-003-42956 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.05 mg Aff Pur
18-003-42955 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.05 mg Aff Pur


 

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