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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, GPR51, GPRC3B
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
  2. protein binding Source: IntAct

GO - Biological processi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 483442Extracellular Reviewed prediction
Add
BLAST
Transmembranei484 – 50421Helical; Name=1; Reviewed prediction
Add
BLAST
Topological domaini505 – 52218Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei523 – 54321Helical; Name=2; Reviewed prediction
Add
BLAST
Topological domaini544 – 5518Extracellular Reviewed prediction
Transmembranei552 – 57221Helical; Name=3; Reviewed prediction
Add
BLAST
Topological domaini573 – 59725Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei598 – 61821Helical; Name=4; Reviewed prediction
Add
BLAST
Topological domaini619 – 65436Extracellular Reviewed prediction
Add
BLAST
Transmembranei655 – 67521Helical; Name=5; Reviewed prediction
Add
BLAST
Topological domaini676 – 69116Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei692 – 71221Helical; Name=6; Reviewed prediction
Add
BLAST
Topological domaini713 – 7208Extracellular Reviewed prediction
Transmembranei721 – 74121Helical; Name=7; Reviewed prediction
Add
BLAST
Topological domaini742 – 941200Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. G-protein coupled receptor heterodimeric complex Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. cytoplasm Source: Ensembl
  4. integral component of plasma membrane Source: UniProtKB
  5. neuron projection Source: Ensembl
  6. plasma membrane Source: Reactome
  7. postsynaptic membrane Source: UniProtKB-SubCell
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 – 4141 Reviewed prediction
Add
BLAST
Chaini42 – 941900Gamma-aminobutyric acid type B receptor subunit 2
PRO_0000012952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi90 – 901N-linked (GlcNAc...)1 Publication
Disulfide bondi108 ↔ 1352 Publications
Disulfide bondi237 ↔ 2662 Publications
Disulfide bondi265 ↔ 3022 Publications
Glycosylationi298 – 2981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi389 – 3891N-linked (GlcNAc...)1 Publication
Glycosylationi404 – 4041N-linked (GlcNAc...)2 Publications
Glycosylationi453 – 4531N-linked (GlcNAc...)1 Publication
Modified residuei884 – 8841Phosphoserine By 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

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.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili781 – 81939 Reviewed prediction
Add
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.

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 conflict

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

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

« 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: September 3, 2014
This is version 143 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

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