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O75899

- GABR2_HUMAN

UniProt

O75899 - GABR2_HUMAN

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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

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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiO75899.
CleanExiHS_GABBR2.
ExpressionAtlasiO75899. baseline and differential.
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
GABBR1Q9UBS52EBI-715469,EBI-724156
NSFP464594EBI-715469,EBI-712251

Protein-protein interaction databases

BioGridi114938. 6 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, 779-817.
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.
GeneTreeiENSGT00530000063129.
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

        10         20         30         40         50
MASPRSSGQP GPPPPPPPPP ARLLLLLLLP LLLPLAPGAW GWARGAPRPP
60 70 80 90 100
PSSPPLSIMG LMPLTKEVAK GSIGRGVLPA VELAIEQIRN ESLLRPYFLD
110 120 130 140 150
LRLYDTECDN AKGLKAFYDA IKYGPNHLMV FGGVCPSVTS IIAESLQGWN
160 170 180 190 200
LVQLSFAATT PVLADKKKYP YFFRTVPSDN AVNPAILKLL KHYQWKRVGT
210 220 230 240 250
LTQDVQRFSE VRNDLTGVLY GEDIEISDTE SFSNDPCTSV KKLKGNDVRI
260 270 280 290 300
ILGQFDQNMA AKVFCCAYEE NMYGSKYQWI IPGWYEPSWW EQVHTEANSS
310 320 330 340 350
RCLRKNLLAA MEGYIGVDFE PLSSKQIKTI SGKTPQQYER EYNNKRSGVG
360 370 380 390 400
PSKFHGYAYD GIWVIAKTLQ RAMETLHASS RHQRIQDFNY TDHTLGRIIL
410 420 430 440 450
NAMNETNFFG VTGQVVFRNG ERMGTIKFTQ FQDSREVKVG EYNAVADTLE
460 470 480 490 500
IINDTIRFQG SEPPKDKTII LEQLRKISLP LYSILSALTI LGMIMASAFL
510 520 530 540 550
FFNIKNRNQK LIKMSSPYMN NLIILGGMLS YASIFLFGLD GSFVSEKTFE
560 570 580 590 600
TLCTVRTWIL TVGYTTAFGA MFAKTWRVHA IFKNVKMKKK IIKDQKLLVI
610 620 630 640 650
VGGMLLIDLC ILICWQAVDP LRRTVEKYSM EPDPAGRDIS IRPLLEHCEN
660 670 680 690 700
THMTIWLGIV YAYKGLLMLF GCFLAWETRN VSIPALNDSK YIGMSVYNVG
710 720 730 740 750
IMCIIGAAVS FLTRDQPNVQ FCIVALVIIF CSTITLCLVF VPKLITLRTN
760 770 780 790 800
PDAATQNRRF QFTQNQKKED SKTSTSVTSV NQASTSRLEG LQSENHRLRM
810 820 830 840 850
KITELDKDLE EVTMQLQDTP EKTTYIKQNH YQELNDILNL GNFTESTDGG
860 870 880 890 900
KAILKNHLDQ NPQLQWNTTE PSRTCKDPIE DINSPEHIQR RLSLQLPILH
910 920 930 940
HAYLPSIGGV DASCVSPCVS PTASPRHRHV PPSFRVMVSG L
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, 779-817.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114938. 6 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.
GeneTreei ENSGT00530000063129.
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

Bgeei O75899.
CleanExi HS_GABBR2.
ExpressionAtlasi O75899. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 145 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

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