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Q9UBS5 (GABR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-aminobutyric acid type B receptor subunit 1

Short name=GABA-B receptor 1
Short name=GABA-B-R1
Short name=GABA-BR1
Short name=GABABR1
Short name=Gb1
Gene names
Name:GABBR1
Synonyms:GPRC3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length961 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2. Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins. 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. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. 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. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception. Activated by (-)-baclofen, cgp27492 and blocked by phaclofen. Ref.1 Ref.2 Ref.18 Ref.19 Ref.20

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. Ref.1 Ref.2 Ref.18 Ref.19 Ref.20

Subunit structure

Heterodimer of GABBR1 and GABBR2. Homodimers may form, but are inactive. Isoform 1E (without C-terminal intracellular domain) is unable to dimerize via a coiled-coil interaction with GABBR2. Interacts with the leucine zipper of the C-terminal bZIP domain of ATF4 via its C-terminal region. Interacts with JAKMIP1. Ref.2 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell projectiondendrite By similarity. 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. Ref.1 Ref.2 Ref.17

Isoform 1E: Secreted Probable Ref.1 Ref.2 Ref.17.

Tissue specificity

Highly expressed in brain and weakly in heart, small intestine and uterus. Isoform 1A is mostly expressed in granular cell and molecular layer. Isoform 1B is mostly expressed in Purkinje cells. Isoform 1E is predominantly expressed in peripheral tissues as kidney, lung, trachea, colon, small intestine, stomach, bone marrow, thymus and mammary gland. Ref.1

Domain

Alpha-helical parts of the C-terminal intracellular region mediate heterodimeric interaction with GABBR2. 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.

Sequence similarities

Belongs to the G-protein coupled receptor 3 family. GABA-B receptor subfamily.

Contains 2 Sushi (CCP/SCR) domains.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Membrane
Postsynaptic cell membrane
Secreted
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
Signal
Sushi
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-inhibiting G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 10328880. Source: UniProtKB

gamma-aminobutyric acid signaling pathway

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of adenylate cyclase activity

Traceable author statement PubMed 9069281. Source: ProtInc

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentG-protein coupled receptor heterodimeric complex

Inferred from physical interaction Ref.2. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

presynaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionG-protein coupled GABA receptor activity

Inferred from direct assay PubMed 10328880. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoforms corresponding to the full receptor are essentially found in the central nervous system (CNS).
Isoform 1A (identifier: Q9UBS5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1B (identifier: Q9UBS5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-164: MLLLLLLAPL...PHCQVNRTPH → MGPGAPFARV...PHSRVPPHPS
Isoform 1C (identifier: Q9UBS5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     98-159: Missing.
Isoform 1D (identifier: Q9UBS5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     905-961: KEERVSELRH...DGSRVHLLYK → SGGLPRGPPEPPDRLSCDGSRVHLLYK
Isoform 1E (identifier: Q9UBS5-5)

Also known as: Truncated;

The sequence of this isoform differs from the canonical sequence as follows:
     570-961: GGSPPADQTL...DGSRVHLLYK → VISRTHSPT
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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1414 Potential
Chain15 – 961947Gamma-aminobutyric acid type B receptor subunit 1
PRO_0000012949

Regions

Topological domain15 – 591577Extracellular Potential
Transmembrane592 – 61221Helical; Name=1; Potential
Topological domain613 – 63119Cytoplasmic Potential
Transmembrane632 – 65221Helical; Name=2; Potential
Topological domain653 – 66715Extracellular Potential
Transmembrane668 – 68821Helical; Name=3; Potential
Topological domain689 – 71022Cytoplasmic Potential
Transmembrane711 – 73121Helical; Name=4; Potential
Topological domain732 – 76837Extracellular Potential
Transmembrane769 – 78921Helical; Name=5; Potential
Topological domain790 – 80415Cytoplasmic Potential
Transmembrane805 – 82521Helical; Name=6; Potential
Topological domain826 – 8338Extracellular Potential
Transmembrane834 – 85421Helical; Name=7; Potential
Topological domain855 – 961107Cytoplasmic Potential
Domain30 – 9667Sushi 1
Domain98 – 15962Sushi 2
Region888 – 91629Interaction with ATF4 By similarity
Coiled coil869 – 92557 Potential

Sites

Binding site2471Agonist
Binding site2701Agonist
Binding site2871Agonist
Binding site3671Agonist
Binding site3951Agonist
Binding site4661Agonist

Amino acid modifications

Glycosylation241N-linked (GlcNAc...) Potential
Glycosylation841N-linked (GlcNAc...) Potential
Glycosylation4091N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Ref.20
Glycosylation4821N-linked (GlcNAc...) Ref.20
Glycosylation5021N-linked (GlcNAc...) Potential
Glycosylation5141N-linked (GlcNAc...) Potential
Disulfide bond100 ↔ 145 By similarity
Disulfide bond131 ↔ 157 By similarity
Disulfide bond220 ↔ 246 Ref.20
Disulfide bond376 ↔ 410 Ref.20

Natural variations

Alternative sequence1 – 164164MLLLL…NRTPH → MGPGAPFARVGWPLPLLVVM AAGVAPVWASHSPHLPRPHS RVPPHPS in isoform 1B.
VSP_002037
Alternative sequence98 – 15962Missing in isoform 1C.
VSP_002038
Alternative sequence570 – 961392GGSPP…HLLYK → VISRTHSPT in isoform 1E.
VSP_002039
Alternative sequence905 – 96157KEERV…HLLYK → SGGLPRGPPEPPDRLSCDGS RVHLLYK in isoform 1D.
VSP_002040
Natural variant201A → V. Ref.7 Ref.10 Ref.21
Corresponds to variant rs1805056 [ dbSNP | Ensembl ].
VAR_010146
Natural variant4891G → S. Ref.7 Ref.9 Ref.21
Corresponds to variant rs1805057 [ dbSNP | Ensembl ].
VAR_010147
Natural variant6451F → L.
Corresponds to variant rs2076489 [ dbSNP | Ensembl ].
VAR_049279

Experimental info

Mutagenesis1821W → A: Abolishes signaling via G-proteins. Abolishes antagonist binding. Ref.20
Mutagenesis2301Y → A: Slightly decreases signaling via G-proteins. Ref.19
Mutagenesis2341Y → A: Decreases signaling via G-proteins. Ref.19
Mutagenesis2871H → A: Strongly reduces signaling via G-proteins. Abolishes antagonist binding. Ref.20
Mutagenesis3671Y → A: Strongly reduces signaling via G-proteins. No effect on antagonist binding. Ref.20
Mutagenesis3951W → A: Strongly reduces signaling via G-proteins. Strongly reduces antagonist binding. Ref.20
Sequence conflict21L → M in Y11044. Ref.4
Sequence conflict211Q → H in CAA09939. Ref.2
Sequence conflict211Q → H in CAA09941. Ref.2
Sequence conflict931P → L in AAC98508. Ref.3
Sequence conflict1271V → A in CAA09939. Ref.2
Sequence conflict3221Missing in CAA09031. Ref.7
Sequence conflict5421L → P in Y11044. Ref.4
Sequence conflict6911V → G in Y11044. Ref.4
Sequence conflict905 – 93430Missing in CAA09031. Ref.7

Secondary structure

............................................................................ 961
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1A [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 54E7349CD02B633F

FASTA961108,320
        10         20         30         40         50         60 
MLLLLLLAPL FLRPPGAGGA QTPNATSEGC QIIHPPWEGG IRYRGLTRDQ VKAINFLPVD 

        70         80         90        100        110        120 
YEIEYVCRGE REVVGPKVRK CLANGSWTDM DTPSRCVRIC SKSYLTLENG KVFLTGGDLP 

       130        140        150        160        170        180 
ALDGARVDFR CDPDFHLVGS SRSICSQGQW STPKPHCQVN RTPHSERRAV YIGALFPMSG 

       190        200        210        220        230        240 
GWPGGQACQP AVEMALEDVN SRRDILPDYE LKLIHHDSKC DPGQATKYLY ELLYNDPIKI 

       250        260        270        280        290        300 
ILMPGCSSVS TLVAEAARMW NLIVLSYGSS SPALSNRQRF PTFFRTHPSA TLHNPTRVKL 

       310        320        330        340        350        360 
FEKWGWKKIA TIQQTTEVFT STLDDLEERV KEAGIEITFR QSFFSDPAVP VKNLKRQDAR 

       370        380        390        400        410        420 
IIVGLFYETE ARKVFCEVYK ERLFGKKYVW FLIGWYADNW FKIYDPSINC TVDEMTEAVE 

       430        440        450        460        470        480 
GHITTEIVML NPANTRSISN MTSQEFVEKL TKRLKRHPEE TGGFQEAPLA YDAIWALALA 

       490        500        510        520        530        540 
LNKTSGGGGR SGVRLEDFNY NNQTITDQIY RAMNSSSFEG VSGHVVFDAS GSRMAWTLIE 

       550        560        570        580        590        600 
QLQGGSYKKI GYYDSTKDDL SWSKTDKWIG GSPPADQTLV IKTFRFLSQK LFISVSVLSS 

       610        620        630        640        650        660 
LGIVLAVVCL SFNIYNSHVR YIQNSQPNLN NLTAVGCSLA LAAVFPLGLD GYHIGRNQFP 

       670        680        690        700        710        720 
FVCQARLWLL GLGFSLGYGS MFTKIWWVHT VFTKKEEKKE WRKTLEPWKL YATVGLLVGM 

       730        740        750        760        770        780 
DVLTLAIWQI VDPLHRTIET FAKEEPKEDI DVSILPQLEH CSSRKMNTWL GIFYGYKGLL 

       790        800        810        820        830        840 
LLLGIFLAYE TKSVSTEKIN DHRAVGMAIY NVAVLCLITA PVTMILSSQQ DAAFAFASLA 

       850        860        870        880        890        900 
IVFSSYITLV VLFVPKMRRL ITRGEWQSEA QDTMKTGSST NNNEEEKSRL LEKENRELEK 

       910        920        930        940        950        960 
IIAEKEERVS ELRHQLQSRQ QLRSRRHPPT PPEPSGGLPR GPPEPPDRLS CDGSRVHLLY 


K 

« Hide

Isoform 1B [UniParc].

Checksum: D926376823699485
Show »

FASTA84495,148
Isoform 1C [UniParc].

Checksum: 65DD7A31D68114AE
Show »

FASTA899101,543
Isoform 1D [UniParc].

Checksum: 6FD16A36835AAB34
Show »

FASTA931104,665
Isoform 1E (Truncated) [UniParc].

Checksum: 9B15DFD4E097428F
Show »

FASTA57865,082

References

« Hide 'large scale' references
[1]"Human gamma-aminobutyric acid type B receptors are differentially expressed and regulate inwardly rectifying K+ channels."
Kaupmann K., Schuler V., Mosbacher J., Bischoff S., Bittiger H., Heid J., Froestl W., Leonhard S., Pfaff T., Karschin A., Bettler B.
Proc. Natl. Acad. Sci. U.S.A. 95:14991-14996(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Cerebellum.
[2]"Heterodimerization is required for the formation of a functional GABA(B) receptor."
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.
Nature 396:679-682(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C), FUNCTION, SUBUNIT, INTERACTION WITH GABBR2, SUBCELLULAR LOCATION.
Tissue: Cerebellum.
[3]"Human mRNA for GABA-B1a receptor."
Stropp U., Raming K.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
Tissue: Brain.
[4]"GABA (gamma-amino-butyric acid) neurotransmission: identification and fine mapping of the human GABAB receptor gene."
Grifa A., Totaro A., Rommens J.M., Carella M., Roetto A., Borgato L., Zelante L., Gasparini P.
Biochem. Biophys. Res. Commun. 250:240-245(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
Tissue: Fetal brain.
[5]"Human gamma-aminobutyric acid B receptor gene: complementary DNA cloning, expression, chromosomal location, and genomic organization."
Goei V.L., Choi J., Ahn J., Bowlus C.L., Raha-Chowdhury R., Gruen J.R.
Biol. Psychiatry 44:659-666(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1A).
[6]Fraser N.J.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1C).
Tissue: Cerebellum.
[7]"Mapping, genomic structure, and polymorphisms of the human GABABR1 receptor gene: evaluation of its involvement in idiopathic generalized epilepsy."
Peters H.C., Kaemmer G., Volz A., Kaupmann K., Ziegler A., Bettler B., Epplen J.T., Sander T., Riess O.
Neurogenetics 2:47-54(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A AND 1B), VARIANTS VAL-20 AND SER-489.
Tissue: Fetal brain.
[8]"Molecular cloning of human GABABR1 and its tissue distribution."
Makoff A.
Brain Res. Mol. Brain Res. 64:137-140(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
Tissue: Cerebellum.
[9]"Characterization of gamma-aminobutyric acid receptor GABAB(1e), a GABAB(1) splice variant encoding a truncated receptor."
Schwarz D.A., Barry G., Eliasof S.D., Petroski R.E., Conlon P.J., Maki R.A.
J. Biol. Chem. 275:32174-32181(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1E), VARIANT SER-489.
Tissue: Prostate.
[10]"The DNA sequence and analysis of human chromosome 6."
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. expand/collapse author list , 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.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-20.
[11]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B).
Tissue: Brain.
[13]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[14]"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."
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.
J. Pharmacol. Exp. Ther. 293:460-467(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GABBR2.
[15]"Role of heteromer formation in GABAB receptor function."
Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A., Kornau H.-C.
Science 283:74-77(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GABBR2.
[16]"Marlin-1, a novel RNA-binding protein associates with GABA receptors."
Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H., Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.
J. Biol. Chem. 279:13934-13943(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH JAKMIP1.
[17]"Subcellular distribution of GABA(B) receptor homo- and hetero-dimers."
Villemure J.F., Adam L., Bevan N.J., Gearing K., Chenier S., Bouvier M.
Biochem. J. 388:47-55(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION.
[18]"Direct detection of the interaction between recombinant soluble extracellular regions in the heterodimeric metabotropic gamma-aminobutyric acid receptor."
Nomura R., Suzuki Y., Kakizuka A., Jingami H.
J. Biol. Chem. 283:4665-4673(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GABBR2.
[19]"Structure and functional interaction of the extracellular domain of human GABA(B) receptor GBR2."
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.
Nat. Neurosci. 15:970-978(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PARTIAL PROTEIN SEQUENCE, AGONIST BINDING, MUTAGENESIS OF TYR-230 AND TYR-234, INTERACTION WITH GABBR2.
[20]"Structural mechanism of ligand activation in human GABA(B) receptor."
Geng Y., Bush M., Mosyak L., Wang F., Fan Q.R.
Nature 504:254-259(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, MUTAGENESIS OF TRP-182; HIS-287; TYR-367 AND TRP-395.
[21]"Association analysis of exonic variants of the gene encoding the GABAB receptor and idiopathic generalized epilepsy."
Sander T., Peters C., Kaemmer G., Samochowiec J., Zirra M., Mischke D., Ziegler A., Kaupmann K., Bettler B., Epplen J.T., Riess O.
Am. J. Med. Genet. 88:305-310(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-20 AND SER-489.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ225028 mRNA. Translation: CAA12359.1.
AJ225029 mRNA. Translation: CAA12360.1.
AJ012185 mRNA. Translation: CAA09939.1.
AJ012186 mRNA. Translation: CAA09940.1.
AF099148 mRNA. Translation: AAC98508.1.
Y11044 mRNA. No translation available.
AJ012187 mRNA. Translation: CAA09941.1.
AJ010170 expand/collapse EMBL AC list , AJ010171, AJ010172, AJ010173, AJ010174, AJ010175, AJ010176, AJ010177, AJ010178, AJ010179, AJ010180, AJ010181, AJ010182, AJ010183, AJ010184, AJ010185, AJ010186, AJ010187, AJ010188, AJ010189, AJ010190, AJ010191 Genomic DNA. Translation: CAA09031.1.
AJ012288 mRNA. Translation: CAA09980.1.
AF301005 mRNA. Translation: AAG23962.1.
AL031983 Genomic DNA. Translation: CAA21453.1.
AL031983 Genomic DNA. Translation: CAA21454.1.
AL662826 Genomic DNA. Translation: CAI17390.1.
AL662826 Genomic DNA. Translation: CAI17391.2.
AL645936 Genomic DNA. Translation: CAI18016.1.
AL645936 Genomic DNA. Translation: CAI18017.1.
BX000688 Genomic DNA. Translation: CAI18605.1.
BX000688 Genomic DNA. Translation: CAI18606.1.
CR759766 Genomic DNA. Translation: CAQ06609.1.
CR759766 Genomic DNA. Translation: CAQ06610.1.
CR788300, CR936483 Genomic DNA. Translation: CAQ07763.1.
CR788300, CR936483 Genomic DNA. Translation: CAQ07764.1.
CR388210 Genomic DNA. Translation: CAQ09395.1.
CR759870 Genomic DNA. Translation: CAQ09878.1.
CR759870 Genomic DNA. Translation: CAQ09879.1.
CR936483, CR788300 Genomic DNA. Translation: CAQ10082.1.
CR936483, CR788300 Genomic DNA. Translation: CAQ10083.1.
CH471081 Genomic DNA. Translation: EAX03205.1.
CH471081 Genomic DNA. Translation: EAX03210.1.
BC042598 mRNA. Translation: AAH42598.1.
BC050532 mRNA. Translation: AAH50532.2.
PIRJE0356.
RefSeqNP_001461.1. NM_001470.2.
NP_068703.1. NM_021903.2.
NP_068704.2. NM_021904.2.
UniGeneHs.167017.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4MQEX-ray2.35A165-576[»]
4MQFX-ray2.22A165-576[»]
4MR7X-ray2.15A165-576[»]
4MR8X-ray2.15A165-576[»]
4MR9X-ray2.35A165-576[»]
4MRMX-ray2.86A165-576[»]
4MS1X-ray2.25A165-576[»]
4MS3X-ray2.50A165-576[»]
4MS4X-ray1.90A165-576[»]
ProteinModelPortalQ9UBS5.
SMRQ9UBS5. Positions 55-160, 185-574.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108825. 10 interactions.
DIPDIP-38394N.
IntActQ9UBS5. 11 interactions.
MINTMINT-2793192.
STRING9606.ENSP00000388035.

Chemistry

BindingDBQ9UBS5.
ChEMBLCHEMBL2064.
DrugBankDB00181. Baclofen.
DB00837. Progabide.
GuidetoPHARMACOLOGY240.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ9UBS5.

Polymorphism databases

DMDM12643873.

Proteomic databases

PaxDbQ9UBS5.
PRIDEQ9UBS5.

Protocols and materials databases

DNASU2550.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355973; ENSP00000348248; ENSG00000204681. [Q9UBS5-2]
ENST00000376977; ENSP00000366176; ENSG00000204681. [Q9UBS5-5]
ENST00000377012; ENSP00000366211; ENSG00000204681. [Q9UBS5-2]
ENST00000377016; ENSP00000366215; ENSG00000204681. [Q9UBS5-3]
ENST00000377034; ENSP00000366233; ENSG00000204681. [Q9UBS5-1]
ENST00000383537; ENSP00000373029; ENSG00000206466. [Q9UBS5-2]
ENST00000383541; ENSP00000373033; ENSG00000206466. [Q9UBS5-3]
ENST00000383542; ENSP00000373034; ENSG00000206466. [Q9UBS5-1]
ENST00000383543; ENSP00000373035; ENSG00000206466. [Q9UBS5-2]
ENST00000383636; ENSP00000373132; ENSG00000206511. [Q9UBS5-2]
ENST00000383637; ENSP00000373133; ENSG00000206511. [Q9UBS5-3]
ENST00000383638; ENSP00000373134; ENSG00000206511. [Q9UBS5-1]
ENST00000383639; ENSP00000373135; ENSG00000206511. [Q9UBS5-2]
ENST00000414980; ENSP00000406499; ENSG00000232632. [Q9UBS5-2]
ENST00000417759; ENSP00000391572; ENSG00000237112. [Q9UBS5-2]
ENST00000419674; ENSP00000399861; ENSG00000232569. [Q9UBS5-3]
ENST00000423604; ENSP00000388035; ENSG00000232632. [Q9UBS5-1]
ENST00000425097; ENSP00000411286; ENSG00000237112. [Q9UBS5-1]
ENST00000434660; ENSP00000412167; ENSG00000232632. [Q9UBS5-3]
ENST00000438094; ENSP00000406285; ENSG00000232632. [Q9UBS5-2]
ENST00000439457; ENSP00000406066; ENSG00000232569. [Q9UBS5-1]
ENST00000443440; ENSP00000399318; ENSG00000237112. [Q9UBS5-3]
ENST00000446436; ENSP00000394528; ENSG00000237112. [Q9UBS5-2]
ENST00000448754; ENSP00000405709; ENSG00000237051. [Q9UBS5-2]
ENST00000449163; ENSP00000411263; ENSG00000232569. [Q9UBS5-2]
ENST00000452300; ENSP00000408938; ENSG00000232569. [Q9UBS5-2]
ENST00000458612; ENSP00000416903; ENSG00000237051. [Q9UBS5-2]
ENST00000494877; ENSP00000419061; ENSG00000204681. [Q9UBS5-5]
ENST00000546913; ENSP00000448999; ENSG00000232569. [Q9UBS5-1]
ENST00000547410; ENSP00000448531; ENSG00000232569. [Q9UBS5-5]
ENST00000548767; ENSP00000446983; ENSG00000232632. [Q9UBS5-5]
ENST00000550428; ENSP00000449727; ENSG00000232569. [Q9UBS5-3]
ENST00000551140; ENSP00000448654; ENSG00000237112. [Q9UBS5-5]
ENST00000551423; ENSP00000449342; ENSG00000206511. [Q9UBS5-5]
ENST00000552399; ENSP00000449449; ENSG00000206466. [Q9UBS5-5]
GeneID2550.
KEGGhsa:2550.
UCSCuc003nmt.4. human. [Q9UBS5-1]
uc003nmu.4. human. [Q9UBS5-3]
uc011dls.1. human. [Q9UBS5-5]

Organism-specific databases

CTD2550.
GeneCardsGC06M029523.
GC06Mi29524.
GC06Mj29520.
GC06Mk29524.
GC06Ml29523.
GC06Mm29524.
GC06Mn29524.
HGNCHGNC:4070. GABBR1.
HPAHPA050483.
MIM603540. gene.
neXtProtNX_Q9UBS5.
PharmGKBPA28484.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG273984.
HOVERGENHBG051688.
InParanoidQ9UBS5.
KOK04615.
OMASTQFLGV.
PhylomeDBQ9UBS5.
TreeFamTF313965.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ9UBS5.
BgeeQ9UBS5.
CleanExHS_GABBR1.
GenevestigatorQ9UBS5.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR017978. GPCR_3_C.
IPR002455. GPCR_3_GABA_rcpt_B.
IPR002456. GPCR_3_GABA_rcpt_B1.
IPR028082. Peripla_BP_I.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF00084. Sushi. 2 hits.
[Graphical view]
PRINTSPR01177. GABAB1RECPTR.
PR01176. GABABRECEPTR.
SMARTSM00032. CCP. 2 hits.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEPS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGABBR1. human.
GeneWikiGABBR1.
GenomeRNAi2550.
NextBio10061.
PROQ9UBS5.
SOURCESearch...

Entry information

Entry nameGABR1_HUMAN
AccessionPrimary (citable) accession number: Q9UBS5
Secondary accession number(s): B0UXY7 expand/collapse secondary AC list , O95375, O95468, O95975, O96022, Q5STL4, Q5SUJ8, Q5SUL3, Q71SG6, Q86W60, Q9UQQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries