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Q9UBS5

- GABR1_HUMAN

UniProt

Q9UBS5 - GABR1_HUMAN

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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

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

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
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.

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, UP000005640: Unplaced

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini15 – 591577ExtracellularSequence AnalysisAdd
BLAST
Transmembranei592 – 61221Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini613 – 63119CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei632 – 65221Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini653 – 66715ExtracellularSequence AnalysisAdd
BLAST
Transmembranei668 – 68821Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini689 – 71022CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei711 – 73121Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini732 – 76837ExtracellularSequence AnalysisAdd
BLAST
Transmembranei769 – 78921Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini790 – 80415CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei805 – 82521Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini826 – 8338ExtracellularSequence Analysis
Transmembranei834 – 85421Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini855 – 961107CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cell projection Source: UniProtKB-KW
  3. cytoplasm Source: Ensembl
  4. extracellular region Source: UniProtKB-KW
  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-KW
  9. presynaptic membrane Source: Ensembl
Complete GO annotation...

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

BgeeiQ9UBS5.
CleanExiHS_GABBR1.
ExpressionAtlasiQ9UBS5. baseline and differential.
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
GABBR2O758992EBI-724156,EBI-715469
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 – 1769Combined sources
Beta strandi178 – 1814Combined sources
Helixi185 – 20016Combined sources
Turni203 – 2053Combined sources
Beta strandi209 – 2179Combined sources
Helixi222 – 23312Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi240 – 2434Combined sources
Helixi247 – 25610Combined sources
Helixi257 – 2604Combined sources
Beta strandi263 – 2686Combined sources
Helixi272 – 2754Combined sources
Turni277 – 2793Combined sources
Beta strandi283 – 2875Combined sources
Helixi290 – 2923Combined sources
Helixi293 – 30311Combined sources
Beta strandi308 – 3169Combined sources
Helixi317 – 33216Combined sources
Beta strandi336 – 34510Combined sources
Helixi348 – 3569Combined sources
Beta strandi361 – 3655Combined sources
Helixi368 – 38114Combined sources
Beta strandi385 – 3873Combined sources
Beta strandi389 – 3935Combined sources
Helixi400 – 4023Combined sources
Helixi412 – 4198Combined sources
Beta strandi423 – 4275Combined sources
Helixi443 – 45311Combined sources
Helixi458 – 4603Combined sources
Turni462 – 4665Combined sources
Helixi467 – 48418Combined sources
Helixi495 – 4973Combined sources
Helixi504 – 51411Combined sources
Beta strandi517 – 5204Combined sources
Beta strandi523 – 5264Combined sources
Turni529 – 5313Combined sources
Beta strandi536 – 5438Combined sources
Beta strandi546 – 5549Combined sources
Turni555 – 5584Combined sources
Beta strandi559 – 5624Combined sources
Helixi569 – 5713Combined sources
Helixi885 – 91733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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, 884-918.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00530000063129.
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

        10         20         30         40         50
MLLLLLLAPL FLRPPGAGGA QTPNATSEGC QIIHPPWEGG IRYRGLTRDQ
60 70 80 90 100
VKAINFLPVD YEIEYVCRGE REVVGPKVRK CLANGSWTDM DTPSRCVRIC
110 120 130 140 150
SKSYLTLENG KVFLTGGDLP ALDGARVDFR CDPDFHLVGS SRSICSQGQW
160 170 180 190 200
STPKPHCQVN RTPHSERRAV YIGALFPMSG GWPGGQACQP AVEMALEDVN
210 220 230 240 250
SRRDILPDYE LKLIHHDSKC DPGQATKYLY ELLYNDPIKI ILMPGCSSVS
260 270 280 290 300
TLVAEAARMW NLIVLSYGSS SPALSNRQRF PTFFRTHPSA TLHNPTRVKL
310 320 330 340 350
FEKWGWKKIA TIQQTTEVFT STLDDLEERV KEAGIEITFR QSFFSDPAVP
360 370 380 390 400
VKNLKRQDAR IIVGLFYETE ARKVFCEVYK ERLFGKKYVW FLIGWYADNW
410 420 430 440 450
FKIYDPSINC TVDEMTEAVE GHITTEIVML NPANTRSISN MTSQEFVEKL
460 470 480 490 500
TKRLKRHPEE TGGFQEAPLA YDAIWALALA LNKTSGGGGR SGVRLEDFNY
510 520 530 540 550
NNQTITDQIY RAMNSSSFEG VSGHVVFDAS GSRMAWTLIE QLQGGSYKKI
560 570 580 590 600
GYYDSTKDDL SWSKTDKWIG GSPPADQTLV IKTFRFLSQK LFISVSVLSS
610 620 630 640 650
LGIVLAVVCL SFNIYNSHVR YIQNSQPNLN NLTAVGCSLA LAAVFPLGLD
660 670 680 690 700
GYHIGRNQFP FVCQARLWLL GLGFSLGYGS MFTKIWWVHT VFTKKEEKKE
710 720 730 740 750
WRKTLEPWKL YATVGLLVGM DVLTLAIWQI VDPLHRTIET FAKEEPKEDI
760 770 780 790 800
DVSILPQLEH CSSRKMNTWL GIFYGYKGLL LLLGIFLAYE TKSVSTEKIN
810 820 830 840 850
DHRAVGMAIY NVAVLCLITA PVTMILSSQQ DAAFAFASLA IVFSSYITLV
860 870 880 890 900
VLFVPKMRRL ITRGEWQSEA QDTMKTGSST NNNEEEKSRL LEKENRELEK
910 920 930 940 950
IIAEKEERVS ELRHQLQSRQ QLRSRRHPPT PPEPSGGLPR GPPEPPDRLS
960
CDGSRVHLLY K
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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, 884-918.
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.
DB01080. Vigabatrin.
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.
GeneTreei ENSGT00530000063129.
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

Bgeei Q9UBS5.
CleanExi HS_GABBR1.
ExpressionAtlasi Q9UBS5. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 150 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