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O75899

- GABR2_HUMAN

UniProt

O75899 - GABR2_HUMAN

Protein

Gamma-aminobutyric acid type B receptor subunit 2

Gene

GABBR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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. 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.5 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. gamma-aminobutyric acid signaling pathway Source: UniProtKB
    2. G-protein coupled receptor signaling pathway Source: ProtInc
    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.

    Protein family/group databases

    TCDBi9.A.14.15.1. the g-protein-coupled receptor (gpcr) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-aminobutyric acid type B receptor subunit 2
    Short name:
    GABA-B receptor 2
    Short name:
    GABA-B-R2
    Short name:
    GABA-BR2
    Short name:
    GABABR2
    Short name:
    Gb2
    Alternative name(s):
    G-protein coupled receptor 51
    HG20
    Gene namesi
    Name:GABBR2
    Synonyms:GPR51, GPRC3B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:4507. GABBR2.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein
    Note: Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma membrane. In contrast, GABBR2 does not depend on GABBR1 for transport to the cell membrane.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: Ensembl
    3. G-protein coupled receptor heterodimeric complex Source: UniProtKB
    4. integral component of plasma membrane Source: UniProtKB
    5. neuron projection Source: Ensembl
    6. plasma membrane Source: Reactome
    7. postsynaptic membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi118 – 1181Y → A: Impairs interaction with GABBR1. Decreases signaling via G-proteins. 1 Publication

    Organism-specific databases

    PharmGKBiPA28896.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Sequence AnalysisAdd
    BLAST
    Chaini42 – 941900Gamma-aminobutyric acid type B receptor subunit 2PRO_0000012952Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi90 – 901N-linked (GlcNAc...)1 Publication
    Disulfide bondi108 ↔ 135
    Disulfide bondi237 ↔ 266
    Disulfide bondi265 ↔ 302
    Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi389 – 3891N-linked (GlcNAc...)1 Publication
    Glycosylationi404 – 4041N-linked (GlcNAc...)2 Publications
    Glycosylationi453 – 4531N-linked (GlcNAc...)1 Publication
    Modified residuei884 – 8841PhosphoserineBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiO75899.
    PRIDEiO75899.

    PTM databases

    PhosphoSiteiO75899.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, especially in cerebral cortex, thalamus, hippocampus, frontal, occipital and temporal lobe, occipital pole and cerebellum, followed by corpus callosum, caudate nucleus, spinal cord, amygdala and medulla. Weakly expressed in heart, testis and skeletal muscle.3 Publications

    Gene expression databases

    ArrayExpressiO75899.
    BgeeiO75899.
    CleanExiHS_GABBR2.
    GenevestigatoriO75899.

    Organism-specific databases

    HPAiHPA013820.
    HPA031684.

    Interactioni

    Subunit structurei

    Heterodimer of GABBR1 and GABBR2. Homodimers may form, but are inactive. Interacts with ATF4 via its C-terminal region.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NSFP464594EBI-715469,EBI-712251

    Protein-protein interaction databases

    BioGridi114938. 5 interactions.
    DIPiDIP-42851N.
    IntActiO75899. 6 interactions.
    MINTiMINT-1398863.
    STRINGi9606.ENSP00000259455.

    Structurei

    Secondary structure

    1
    941
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi55 – 628
    Beta strandi66 – 683
    Helixi71 – 9020
    Turni91 – 966
    Beta strandi98 – 1058
    Helixi110 – 12314
    Beta strandi128 – 1325
    Helixi136 – 14510
    Helixi146 – 1494
    Beta strandi152 – 1576
    Helixi161 – 1644
    Turni166 – 1683
    Beta strandi172 – 1765
    Helixi179 – 1813
    Helixi182 – 19211
    Beta strandi197 – 2059
    Helixi206 – 21914
    Turni220 – 2234
    Beta strandi225 – 23410
    Helixi237 – 2459
    Beta strandi250 – 2545
    Helixi257 – 26913
    Beta strandi278 – 2836
    Turni287 – 2904
    Helixi304 – 3118
    Beta strandi315 – 3195
    Helixi335 – 34511
    Turni346 – 3483
    Helixi355 – 37218
    Helixi378 – 38710
    Helixi393 – 40412
    Beta strandi407 – 4104
    Beta strandi413 – 4186
    Beta strandi421 – 4233
    Beta strandi425 – 4317
    Beta strandi436 – 4438
    Turni444 – 4474
    Beta strandi448 – 4514
    Turni453 – 4553
    Beta strandi459 – 4624
    Helixi780 – 81637

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4F11X-ray2.38A42-466[»]
    4F12X-ray3.02A42-466[»]
    4MQEX-ray2.35B42-466[»]
    4MQFX-ray2.22B42-466[»]
    4MR7X-ray2.15B42-466[»]
    4MR8X-ray2.15B42-466[»]
    4MR9X-ray2.35B42-466[»]
    4MRMX-ray2.86B42-466[»]
    4MS1X-ray2.25B42-466[»]
    4MS3X-ray2.50B42-466[»]
    4MS4X-ray1.90B42-466[»]
    4PASX-ray1.62B779-819[»]
    ProteinModelPortaliO75899.
    SMRiO75899. Positions 52-464, 484-752.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini42 – 483442ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini505 – 52218CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini544 – 5518ExtracellularSequence Analysis
    Topological domaini573 – 59725CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini619 – 65436ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini676 – 69116CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini713 – 7208ExtracellularSequence Analysis
    Topological domaini742 – 941200CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei484 – 50421Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei523 – 54321Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei552 – 57221Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei598 – 61821Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei655 – 67521Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei692 – 71221Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei721 – 74121Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili781 – 81939Sequence AnalysisAdd
    BLAST

    Domaini

    Alpha-helical parts of the C-terminal intracellular region mediate heterodimeric interaction with GABBR1.

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG273984.
    HOVERGENiHBG080355.
    InParanoidiO75899.
    KOiK04615.
    OMAiHENIDDV.
    OrthoDBiEOG7D2FCV.
    PhylomeDBiO75899.
    TreeFamiTF313965.

    Family and domain databases

    InterProiIPR001828. ANF_lig-bd_rcpt.
    IPR002455. GPCR3_GABA-B.
    IPR000337. GPCR_3.
    IPR017978. GPCR_3_C.
    IPR017979. GPCR_3_CS.
    IPR002457. GPCR_3_GABA_rcpt_B2.
    IPR028082. Peripla_BP_I.
    [Graphical view]
    PANTHERiPTHR10519. PTHR10519. 1 hit.
    PfamiPF00003. 7tm_3. 1 hit.
    PF01094. ANF_receptor. 1 hit.
    [Graphical view]
    PRINTSiPR01178. GABAB2RECPTR.
    PR00248. GPCRMGR.
    SUPFAMiSSF53822. SSF53822. 1 hit.
    PROSITEiPS00981. G_PROTEIN_RECEP_F3_3. 1 hit.
    PS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O75899-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASPRSSGQP GPPPPPPPPP ARLLLLLLLP LLLPLAPGAW GWARGAPRPP    50
    PSSPPLSIMG LMPLTKEVAK GSIGRGVLPA VELAIEQIRN ESLLRPYFLD 100
    LRLYDTECDN AKGLKAFYDA IKYGPNHLMV FGGVCPSVTS IIAESLQGWN 150
    LVQLSFAATT PVLADKKKYP YFFRTVPSDN AVNPAILKLL KHYQWKRVGT 200
    LTQDVQRFSE VRNDLTGVLY GEDIEISDTE SFSNDPCTSV KKLKGNDVRI 250
    ILGQFDQNMA AKVFCCAYEE NMYGSKYQWI IPGWYEPSWW EQVHTEANSS 300
    RCLRKNLLAA MEGYIGVDFE PLSSKQIKTI SGKTPQQYER EYNNKRSGVG 350
    PSKFHGYAYD GIWVIAKTLQ RAMETLHASS RHQRIQDFNY TDHTLGRIIL 400
    NAMNETNFFG VTGQVVFRNG ERMGTIKFTQ FQDSREVKVG EYNAVADTLE 450
    IINDTIRFQG SEPPKDKTII LEQLRKISLP LYSILSALTI LGMIMASAFL 500
    FFNIKNRNQK LIKMSSPYMN NLIILGGMLS YASIFLFGLD GSFVSEKTFE 550
    TLCTVRTWIL TVGYTTAFGA MFAKTWRVHA IFKNVKMKKK IIKDQKLLVI 600
    VGGMLLIDLC ILICWQAVDP LRRTVEKYSM EPDPAGRDIS IRPLLEHCEN 650
    THMTIWLGIV YAYKGLLMLF GCFLAWETRN VSIPALNDSK YIGMSVYNVG 700
    IMCIIGAAVS FLTRDQPNVQ FCIVALVIIF CSTITLCLVF VPKLITLRTN 750
    PDAATQNRRF QFTQNQKKED SKTSTSVTSV NQASTSRLEG LQSENHRLRM 800
    KITELDKDLE EVTMQLQDTP EKTTYIKQNH YQELNDILNL GNFTESTDGG 850
    KAILKNHLDQ NPQLQWNTTE PSRTCKDPIE DINSPEHIQR RLSLQLPILH 900
    HAYLPSIGGV DASCVSPCVS PTASPRHRHV PPSFRVMVSG L 941
    Length:941
    Mass (Da):105,821
    Last modified:November 1, 1998 - v1
    Checksum:i09F1773DB0673C5D
    GO

    Sequence cautioni

    The sequence AAH35071.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61S → R in AAC99345. (PubMed:10087195)Curated
    Sequence conflicti12 – 121P → R in AAC99345. (PubMed:10087195)Curated
    Sequence conflicti424 – 4241G → E in AAD30389. 1 PublicationCurated
    Sequence conflicti797 – 7971R → H in AAH35071. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti163 – 1631L → P.
    Corresponds to variant rs35449008 [ dbSNP | Ensembl ].
    VAR_049280
    Natural varianti628 – 6281Y → F.1 Publication
    VAR_010148
    Natural varianti869 – 8691T → A.1 Publication
    Corresponds to variant rs10985765 [ dbSNP | Ensembl ].
    VAR_010149

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012188 mRNA. Translation: CAA09942.1.
    AF069755 mRNA. Translation: AAC99345.1.
    AF099033 mRNA. Translation: AAD45867.1.
    AF056085 mRNA. Translation: AAC63228.1.
    AF095784 mRNA. Translation: AAD30389.1.
    AF074483 mRNA. Translation: AAD03336.1.
    AL445495
    , AL353782, AL356282, AL591502 Genomic DNA. Translation: CAD13322.2.
    AL353782
    , AL356282, AL445495, AL591502 Genomic DNA. Translation: CAH71298.1.
    AL356282
    , AL353782, AL445495, AL591502 Genomic DNA. Translation: CAH72233.1.
    AL591502
    , AL353782, AL356282, AL445495 Genomic DNA. Translation: CAI12581.1.
    BC035071 mRNA. Translation: AAH35071.2. Different initiation.
    CCDSiCCDS6736.1.
    RefSeqiNP_005449.5. NM_005458.7.
    UniGeneiHs.198612.

    Genome annotation databases

    EnsembliENST00000259455; ENSP00000259455; ENSG00000136928.
    GeneIDi9568.
    KEGGihsa:9568.
    UCSCiuc004ays.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ012188 mRNA. Translation: CAA09942.1 .
    AF069755 mRNA. Translation: AAC99345.1 .
    AF099033 mRNA. Translation: AAD45867.1 .
    AF056085 mRNA. Translation: AAC63228.1 .
    AF095784 mRNA. Translation: AAD30389.1 .
    AF074483 mRNA. Translation: AAD03336.1 .
    AL445495
    , AL353782 , AL356282 , AL591502 Genomic DNA. Translation: CAD13322.2 .
    AL353782
    , AL356282 , AL445495 , AL591502 Genomic DNA. Translation: CAH71298.1 .
    AL356282
    , AL353782 , AL445495 , AL591502 Genomic DNA. Translation: CAH72233.1 .
    AL591502
    , AL353782 , AL356282 , AL445495 Genomic DNA. Translation: CAI12581.1 .
    BC035071 mRNA. Translation: AAH35071.2 . Different initiation.
    CCDSi CCDS6736.1.
    RefSeqi NP_005449.5. NM_005458.7.
    UniGenei Hs.198612.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4F11 X-ray 2.38 A 42-466 [» ]
    4F12 X-ray 3.02 A 42-466 [» ]
    4MQE X-ray 2.35 B 42-466 [» ]
    4MQF X-ray 2.22 B 42-466 [» ]
    4MR7 X-ray 2.15 B 42-466 [» ]
    4MR8 X-ray 2.15 B 42-466 [» ]
    4MR9 X-ray 2.35 B 42-466 [» ]
    4MRM X-ray 2.86 B 42-466 [» ]
    4MS1 X-ray 2.25 B 42-466 [» ]
    4MS3 X-ray 2.50 B 42-466 [» ]
    4MS4 X-ray 1.90 B 42-466 [» ]
    4PAS X-ray 1.62 B 779-819 [» ]
    ProteinModelPortali O75899.
    SMRi O75899. Positions 52-464, 484-752.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114938. 5 interactions.
    DIPi DIP-42851N.
    IntActi O75899. 6 interactions.
    MINTi MINT-1398863.
    STRINGi 9606.ENSP00000259455.

    Chemistry

    BindingDBi O75899.
    ChEMBLi CHEMBL2111463.
    DrugBanki DB00181. Baclofen.

    Protein family/group databases

    TCDBi 9.A.14.15.1. the g-protein-coupled receptor (gpcr) family.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei O75899.

    Proteomic databases

    PaxDbi O75899.
    PRIDEi O75899.

    Protocols and materials databases

    DNASUi 9568.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259455 ; ENSP00000259455 ; ENSG00000136928 .
    GeneIDi 9568.
    KEGGi hsa:9568.
    UCSCi uc004ays.3. human.

    Organism-specific databases

    CTDi 9568.
    GeneCardsi GC09M101050.
    HGNCi HGNC:4507. GABBR2.
    HPAi HPA013820.
    HPA031684.
    MIMi 607340. gene.
    neXtProti NX_O75899.
    PharmGKBi PA28896.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG273984.
    HOVERGENi HBG080355.
    InParanoidi O75899.
    KOi K04615.
    OMAi HENIDDV.
    OrthoDBi EOG7D2FCV.
    PhylomeDBi O75899.
    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 GABBR2. human.
    GeneWikii GABBR2.
    GenomeRNAii 9568.
    NextBioi 35881.
    PROi O75899.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75899.
    Bgeei O75899.
    CleanExi HS_GABBR2.
    Genevestigatori O75899.

    Family and domain databases

    InterProi IPR001828. ANF_lig-bd_rcpt.
    IPR002455. GPCR3_GABA-B.
    IPR000337. GPCR_3.
    IPR017978. GPCR_3_C.
    IPR017979. GPCR_3_CS.
    IPR002457. GPCR_3_GABA_rcpt_B2.
    IPR028082. Peripla_BP_I.
    [Graphical view ]
    PANTHERi PTHR10519. PTHR10519. 1 hit.
    Pfami PF00003. 7tm_3. 1 hit.
    PF01094. ANF_receptor. 1 hit.
    [Graphical view ]
    PRINTSi PR01178. GABAB2RECPTR.
    PR00248. GPCRMGR.
    SUPFAMi SSF53822. SSF53822. 1 hit.
    PROSITEi PS00981. G_PROTEIN_RECEP_F3_3. 1 hit.
    PS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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], FUNCTION, SUBUNIT, INTERACTION WITH GABBR1, SUBCELLULAR LOCATION.
      Tissue: Cerebellum.
    2. "Cloning of a novel G-protein-coupled receptor GPR 51 resembling GABAB receptors expressed predominantly in nervous tissues and mapped proximal to the hereditary sensory neuropathy type 1 locus on chromosome 9."
      Ng G.Y.K., McDonald T., Bonnert T., Rigby M., Heavens R., Whiting P., Chateauneuf A., Coulombe N., Kargman S., Caskey T., Evans J.F., O'Neill G.P., Liu Q.
      Genomics 56:288-295(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    3. "Molecular identification of the human GABABR2: cell surface expression and coupling to adenylyl cyclase in the absence of GABABR1."
      Martin S.C., Russek S.J., Farb D.H.
      Mol. Cell. Neurosci. 13:180-191(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS PHE-628 AND ALA-869.
      Tissue: Brain.
    4. "Distribution of the GABA(B) receptor subunit gb2 in rat CNS."
      Clark J.A., Mezey E., Lam A.S., Bonner T.I.
      Brain Res. 860:41-52(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Brain.
    5. "Cloning and characterization of a novel human GABA-B receptor subtype with high affinity for GABA and low affinity for baclofen."
      Liu M., Parker R., McCrea K., Watson J., Baker E., Sutherland G., Herzog H.
      Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. Borowsky B., Laz T., Gerald C.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Hippocampus.
    7. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] OF 14-941.
      Tissue: Hippocampus.
    9. Cited for: INTERACTION WITH GABBR1.
    10. "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 GABBR1.
    11. "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.
    12. "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, SUBUNIT, INTERACTION WITH GABBR1.
    13. "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: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 42-466, PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH GABBR1, MUTAGENESIS OF TYR-118, GLYCOSYLATION AT ASN-90; ASN-389; ASN-404 AND ASN-453, DISULFIDE BONDS.
    14. "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 42-466 IN COMPLEXES WITH GABBR1; AGONISTS AND ANTAGONISTS, FUNCTION, SUBUNIT, GLYCOSYLATION AT ASN-404, DISULFIDE BOND.

    Entry informationi

    Entry nameiGABR2_HUMAN
    AccessioniPrimary (citable) accession number: O75899
    Secondary accession number(s): O75974
    , O75975, Q5VXZ2, Q8WX04, Q9P1R2, Q9UNR1, Q9UNS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 144 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 9
      Human chromosome 9: 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