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Q9UBS5

- GABR1_HUMAN

UniProt

Q9UBS5 - GABR1_HUMAN

Protein

Gamma-aminobutyric acid type B receptor subunit 1

Gene

GABBR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    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.
    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei247 – 2471Agonist
    Binding sitei270 – 2701Agonist
    Binding sitei287 – 2871Agonist
    Binding sitei367 – 3671Agonist
    Binding sitei395 – 3951Agonist
    Binding sitei466 – 4661Agonist

    GO - Molecular functioni

    1. G-protein coupled GABA receptor activity Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: UniProtKB
    2. gamma-aminobutyric acid signaling pathway Source: UniProtKB
    3. negative regulation of adenylate cyclase activity Source: ProtInc
    4. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_18319. Class C/3 (Metabotropic glutamate/pheromone receptors).
    REACT_19231. G alpha (i) signalling events.
    REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
    REACT_25031. GABA B receptor activation.
    REACT_75831. Activation of G protein gated Potassium channels.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:GABBR1
    Synonyms:GPRC3A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4070. GABBR1.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: Ensembl
    3. dendrite Source: UniProtKB-SubCell
    4. extracellular region Source: UniProtKB-SubCell
    5. G-protein coupled receptor heterodimeric complex Source: UniProtKB
    6. integral component of plasma membrane Source: UniProtKB
    7. plasma membrane Source: Reactome
    8. postsynaptic membrane Source: UniProtKB-SubCell
    9. presynaptic membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Secreted, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi182 – 1821W → A: Abolishes signaling via G-proteins. Abolishes antagonist binding. 1 Publication
    Mutagenesisi230 – 2301Y → A: Slightly decreases signaling via G-proteins. 1 Publication
    Mutagenesisi234 – 2341Y → A: Decreases signaling via G-proteins. 1 Publication
    Mutagenesisi287 – 2871H → A: Strongly reduces signaling via G-proteins. Abolishes antagonist binding. 1 Publication
    Mutagenesisi367 – 3671Y → A: Strongly reduces signaling via G-proteins. No effect on antagonist binding. 1 Publication
    Mutagenesisi395 – 3951W → A: Strongly reduces signaling via G-proteins. Strongly reduces antagonist binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA28484.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414Sequence AnalysisAdd
    BLAST
    Chaini15 – 961947Gamma-aminobutyric acid type B receptor subunit 1PRO_0000012949Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi100 ↔ 145PROSITE-ProRule annotation
    Disulfide bondi131 ↔ 157PROSITE-ProRule annotation
    Disulfide bondi220 ↔ 2461 PublicationPROSITE-ProRule annotation
    Disulfide bondi376 ↔ 4101 PublicationPROSITE-ProRule annotation
    Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)1 Publication
    Glycosylationi482 – 4821N-linked (GlcNAc...)1 Publication
    Glycosylationi502 – 5021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi514 – 5141N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9UBS5.
    PRIDEiQ9UBS5.

    PTM databases

    PhosphoSiteiQ9UBS5.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBS5.
    BgeeiQ9UBS5.
    CleanExiHS_GABBR1.
    GenevestigatoriQ9UBS5.

    Organism-specific databases

    HPAiHPA050483.

    Interactioni

    Subunit structurei

    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 JAKMIP1.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAXP612443EBI-724156,EBI-751711
    NCK1P163333EBI-724156,EBI-389883
    NSFP464593EBI-724156,EBI-712251

    Protein-protein interaction databases

    BioGridi108825. 10 interactions.
    DIPiDIP-38394N.
    IntActiQ9UBS5. 11 interactions.
    MINTiMINT-2793192.
    STRINGi9606.ENSP00000388035.

    Structurei

    Secondary structure

    1
    961
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi168 – 1769
    Beta strandi178 – 1814
    Helixi185 – 20016
    Turni203 – 2053
    Beta strandi209 – 2179
    Helixi222 – 23312
    Beta strandi234 – 2374
    Beta strandi240 – 2434
    Helixi247 – 25610
    Helixi257 – 2604
    Beta strandi263 – 2686
    Helixi272 – 2754
    Turni277 – 2793
    Beta strandi283 – 2875
    Helixi290 – 2923
    Helixi293 – 30311
    Beta strandi308 – 3169
    Helixi317 – 33216
    Beta strandi336 – 34510
    Helixi348 – 3569
    Beta strandi361 – 3655
    Helixi368 – 38114
    Beta strandi385 – 3873
    Beta strandi389 – 3935
    Helixi400 – 4023
    Helixi412 – 4198
    Beta strandi423 – 4275
    Helixi443 – 45311
    Helixi458 – 4603
    Turni462 – 4665
    Helixi467 – 48418
    Helixi495 – 4973
    Helixi504 – 51411
    Beta strandi517 – 5204
    Beta strandi523 – 5264
    Turni529 – 5313
    Beta strandi536 – 5438
    Beta strandi546 – 5549
    Turni555 – 5584
    Beta strandi559 – 5624
    Helixi569 – 5713
    Helixi885 – 91733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    4PASX-ray1.62A879-919[»]
    ProteinModelPortaliQ9UBS5.
    SMRiQ9UBS5. Positions 55-160, 165-576.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini15 – 591577ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini613 – 63119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini653 – 66715ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini689 – 71022CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini732 – 76837ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini790 – 80415CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini826 – 8338ExtracellularSequence Analysis
    Topological domaini855 – 961107CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei592 – 61221Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei632 – 65221Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei668 – 68821Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei711 – 73121Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei769 – 78921Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei805 – 82521Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei834 – 85421Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 9667Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini98 – 15962Sushi 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni888 – 91629Interaction with ATF4By similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili869 – 92557Sequence AnalysisAdd
    BLAST

    Domaini

    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 similaritiesi

    Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG273984.
    HOVERGENiHBG051688.
    InParanoidiQ9UBS5.
    KOiK04615.
    OMAiSTQFLGV.
    PhylomeDBiQ9UBS5.
    TreeFamiTF313965.

    Family and domain databases

    InterProiIPR001828. ANF_lig-bd_rcpt.
    IPR002455. GPCR3_GABA-B.
    IPR017978. GPCR_3_C.
    IPR002456. GPCR_3_GABA_rcpt_B1.
    IPR028082. Peripla_BP_I.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PANTHERiPTHR10519. PTHR10519. 1 hit.
    PfamiPF00003. 7tm_3. 1 hit.
    PF01094. ANF_receptor. 1 hit.
    PF00084. Sushi. 2 hits.
    [Graphical view]
    PRINTSiPR01177. GABAB1RECPTR.
    SMARTiSM00032. CCP. 2 hits.
    [Graphical view]
    SUPFAMiSSF53822. SSF53822. 1 hit.
    SSF57535. SSF57535. 2 hits.
    PROSITEiPS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
    PS50923. SUSHI. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Isoforms corresponding to the full receptor are essentially found in the central nervous system (CNS).

    Isoform 1A (identifier: Q9UBS5-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLLLLLLAPL FLRPPGAGGA QTPNATSEGC QIIHPPWEGG IRYRGLTRDQ    50
    VKAINFLPVD YEIEYVCRGE REVVGPKVRK CLANGSWTDM DTPSRCVRIC 100
    SKSYLTLENG KVFLTGGDLP ALDGARVDFR CDPDFHLVGS SRSICSQGQW 150
    STPKPHCQVN RTPHSERRAV YIGALFPMSG GWPGGQACQP AVEMALEDVN 200
    SRRDILPDYE LKLIHHDSKC DPGQATKYLY ELLYNDPIKI ILMPGCSSVS 250
    TLVAEAARMW NLIVLSYGSS SPALSNRQRF PTFFRTHPSA TLHNPTRVKL 300
    FEKWGWKKIA TIQQTTEVFT STLDDLEERV KEAGIEITFR QSFFSDPAVP 350
    VKNLKRQDAR IIVGLFYETE ARKVFCEVYK ERLFGKKYVW FLIGWYADNW 400
    FKIYDPSINC TVDEMTEAVE GHITTEIVML NPANTRSISN MTSQEFVEKL 450
    TKRLKRHPEE TGGFQEAPLA YDAIWALALA LNKTSGGGGR SGVRLEDFNY 500
    NNQTITDQIY RAMNSSSFEG VSGHVVFDAS GSRMAWTLIE QLQGGSYKKI 550
    GYYDSTKDDL SWSKTDKWIG GSPPADQTLV IKTFRFLSQK LFISVSVLSS 600
    LGIVLAVVCL SFNIYNSHVR YIQNSQPNLN NLTAVGCSLA LAAVFPLGLD 650
    GYHIGRNQFP FVCQARLWLL GLGFSLGYGS MFTKIWWVHT VFTKKEEKKE 700
    WRKTLEPWKL YATVGLLVGM DVLTLAIWQI VDPLHRTIET FAKEEPKEDI 750
    DVSILPQLEH CSSRKMNTWL GIFYGYKGLL LLLGIFLAYE TKSVSTEKIN 800
    DHRAVGMAIY NVAVLCLITA PVTMILSSQQ DAAFAFASLA IVFSSYITLV 850
    VLFVPKMRRL ITRGEWQSEA QDTMKTGSST NNNEEEKSRL LEKENRELEK 900
    IIAEKEERVS ELRHQLQSRQ QLRSRRHPPT PPEPSGGLPR GPPEPPDRLS 950
    CDGSRVHLLY K 961
    Length:961
    Mass (Da):108,320
    Last modified:May 1, 2000 - v1
    Checksum:i54E7349CD02B633F
    GO
    Isoform 1B (identifier: Q9UBS5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-164: MLLLLLLAPL...PHCQVNRTPH → MGPGAPFARV...PHSRVPPHPS

    Show »
    Length:844
    Mass (Da):95,148
    Checksum:iD926376823699485
    GO
    Isoform 1C (identifier: Q9UBS5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         98-159: Missing.

    Show »
    Length:899
    Mass (Da):101,543
    Checksum:i65DD7A31D68114AE
    GO
    Isoform 1D (identifier: Q9UBS5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         905-961: KEERVSELRH...DGSRVHLLYK → SGGLPRGPPEPPDRLSCDGSRVHLLYK

    Show »
    Length:931
    Mass (Da):104,665
    Checksum:i6FD16A36835AAB34
    GO
    Isoform 1E (identifier: Q9UBS5-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:578
    Mass (Da):65,082
    Checksum:i9B15DFD4E097428F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21L → M in Y11044. (PubMed:9753614)Curated
    Sequence conflicti21 – 211Q → H in CAA09939. (PubMed:9872316)Curated
    Sequence conflicti21 – 211Q → H in CAA09941. (PubMed:9872316)Curated
    Sequence conflicti93 – 931P → L in AAC98508. 1 PublicationCurated
    Sequence conflicti127 – 1271V → A in CAA09939. (PubMed:9872316)Curated
    Sequence conflicti322 – 3221Missing in CAA09031. (PubMed:9933300)Curated
    Sequence conflicti542 – 5421L → P in Y11044. (PubMed:9753614)Curated
    Sequence conflicti691 – 6911V → G in Y11044. (PubMed:9753614)Curated
    Sequence conflicti905 – 93430Missing in CAA09031. (PubMed:9933300)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201A → V.3 Publications
    Corresponds to variant rs1805056 [ dbSNP | Ensembl ].
    VAR_010146
    Natural varianti489 – 4891G → S.3 Publications
    Corresponds to variant rs1805057 [ dbSNP | Ensembl ].
    VAR_010147
    Natural varianti645 – 6451F → L.
    Corresponds to variant rs2076489 [ dbSNP | Ensembl ].
    VAR_049279

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 164164MLLLL…NRTPH → MGPGAPFARVGWPLPLLVVM AAGVAPVWASHSPHLPRPHS RVPPHPS in isoform 1B. 3 PublicationsVSP_002037Add
    BLAST
    Alternative sequencei98 – 15962Missing in isoform 1C. 2 PublicationsVSP_002038Add
    BLAST
    Alternative sequencei570 – 961392GGSPP…HLLYK → VISRTHSPT in isoform 1E. CuratedVSP_002039Add
    BLAST
    Alternative sequencei905 – 96157KEERV…HLLYK → SGGLPRGPPEPPDRLSCDGS RVHLLYK in isoform 1D. CuratedVSP_002040Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSiCCDS4663.1. [Q9UBS5-1]
    CCDS4664.1. [Q9UBS5-3]
    CCDS4665.1. [Q9UBS5-2]
    PIRiJE0356.
    RefSeqiNP_001461.1. NM_001470.2. [Q9UBS5-1]
    NP_068703.1. NM_021903.2. [Q9UBS5-2]
    NP_068704.2. NM_021904.2. [Q9UBS5-3]
    UniGeneiHs.167017.

    Genome annotation databases

    EnsembliENST00000355973; 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]
    GeneIDi2550.
    KEGGihsa:2550.
    UCSCiuc003nmt.4. human. [Q9UBS5-1]
    uc003nmu.4. human. [Q9UBS5-3]
    uc011dls.1. human. [Q9UBS5-5]

    Polymorphism databases

    DMDMi12643873.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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 .
    CCDSi CCDS4663.1. [Q9UBS5-1 ]
    CCDS4664.1. [Q9UBS5-3 ]
    CCDS4665.1. [Q9UBS5-2 ]
    PIRi JE0356.
    RefSeqi NP_001461.1. NM_001470.2. [Q9UBS5-1 ]
    NP_068703.1. NM_021903.2. [Q9UBS5-2 ]
    NP_068704.2. NM_021904.2. [Q9UBS5-3 ]
    UniGenei Hs.167017.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4MQE X-ray 2.35 A 165-576 [» ]
    4MQF X-ray 2.22 A 165-576 [» ]
    4MR7 X-ray 2.15 A 165-576 [» ]
    4MR8 X-ray 2.15 A 165-576 [» ]
    4MR9 X-ray 2.35 A 165-576 [» ]
    4MRM X-ray 2.86 A 165-576 [» ]
    4MS1 X-ray 2.25 A 165-576 [» ]
    4MS3 X-ray 2.50 A 165-576 [» ]
    4MS4 X-ray 1.90 A 165-576 [» ]
    4PAS X-ray 1.62 A 879-919 [» ]
    ProteinModelPortali Q9UBS5.
    SMRi Q9UBS5. Positions 55-160, 165-576.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108825. 10 interactions.
    DIPi DIP-38394N.
    IntActi Q9UBS5. 11 interactions.
    MINTi MINT-2793192.
    STRINGi 9606.ENSP00000388035.

    Chemistry

    BindingDBi Q9UBS5.
    ChEMBLi CHEMBL2064.
    DrugBanki DB00181. Baclofen.
    DB00837. Progabide.
    GuidetoPHARMACOLOGYi 240.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q9UBS5.

    Polymorphism databases

    DMDMi 12643873.

    Proteomic databases

    PaxDbi Q9UBS5.
    PRIDEi Q9UBS5.

    Protocols and materials databases

    DNASUi 2550.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355973 ; 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 ]
    GeneIDi 2550.
    KEGGi hsa:2550.
    UCSCi uc003nmt.4. human. [Q9UBS5-1 ]
    uc003nmu.4. human. [Q9UBS5-3 ]
    uc011dls.1. human. [Q9UBS5-5 ]

    Organism-specific databases

    CTDi 2550.
    GeneCardsi GC06M029523.
    GC06Mi29524.
    GC06Mj29520.
    GC06Mk29524.
    GC06Ml29523.
    GC06Mm29524.
    GC06Mn29524.
    HGNCi HGNC:4070. GABBR1.
    HPAi HPA050483.
    MIMi 603540. gene.
    neXtProti NX_Q9UBS5.
    PharmGKBi PA28484.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG273984.
    HOVERGENi HBG051688.
    InParanoidi Q9UBS5.
    KOi K04615.
    OMAi STQFLGV.
    PhylomeDBi Q9UBS5.
    TreeFami TF313965.

    Enzyme and pathway databases

    Reactomei REACT_18319. Class C/3 (Metabotropic glutamate/pheromone receptors).
    REACT_19231. G alpha (i) signalling events.
    REACT_25004. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
    REACT_25031. GABA B receptor activation.
    REACT_75831. Activation of G protein gated Potassium channels.

    Miscellaneous databases

    ChiTaRSi GABBR1. human.
    GeneWikii GABBR1.
    GenomeRNAii 2550.
    NextBioi 10061.
    PROi Q9UBS5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBS5.
    Bgeei Q9UBS5.
    CleanExi HS_GABBR1.
    Genevestigatori Q9UBS5.

    Family and domain databases

    InterProi IPR001828. ANF_lig-bd_rcpt.
    IPR002455. GPCR3_GABA-B.
    IPR017978. GPCR_3_C.
    IPR002456. GPCR_3_GABA_rcpt_B1.
    IPR028082. Peripla_BP_I.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    PANTHERi PTHR10519. PTHR10519. 1 hit.
    Pfami PF00003. 7tm_3. 1 hit.
    PF01094. ANF_receptor. 1 hit.
    PF00084. Sushi. 2 hits.
    [Graphical view ]
    PRINTSi PR01177. GABAB1RECPTR.
    SMARTi SM00032. CCP. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53822. SSF53822. 1 hit.
    SSF57535. SSF57535. 2 hits.
    PROSITEi PS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
    PS50923. SUSHI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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. 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.

    Entry informationi

    Entry nameiGABR1_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBS5
    Secondary accession number(s): B0UXY7
    , O95375, O95468, O95975, O96022, Q5STL4, Q5SUJ8, Q5SUL3, Q71SG6, Q86W60, Q9UQQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3