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Protein

Gamma-aminobutyric acid type B receptor subunit 1

Gene

GABBR1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei247Agonist1
Binding sitei270Agonist1
Binding sitei287Agonist1
Binding sitei367Agonist1
Binding sitei395Agonist1
Binding sitei466Agonist1

GO - Molecular functioni

  • G-protein coupled GABA receptor activity Source: UniProtKB

GO - Biological processi

  • adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: UniProtKB
  • gamma-aminobutyric acid signaling pathway Source: UniProtKB
  • negative regulation of adenylate cyclase activity Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

BioCyciZFISH:G66-33668-MONOMER.
ReactomeiR-HSA-1296041. Activation of G protein gated Potassium channels.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-420499. Class C/3 (Metabotropic glutamate/pheromone receptors).
R-HSA-977444. GABA B receptor activation.
R-HSA-997272. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
SIGNORiQ9UBS5.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4070. GABBR1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini15 – 591ExtracellularSequence analysisAdd BLAST577
Transmembranei592 – 612Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini613 – 631CytoplasmicSequence analysisAdd BLAST19
Transmembranei632 – 652Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini653 – 667ExtracellularSequence analysisAdd BLAST15
Transmembranei668 – 688Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini689 – 710CytoplasmicSequence analysisAdd BLAST22
Transmembranei711 – 731Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini732 – 768ExtracellularSequence analysisAdd BLAST37
Transmembranei769 – 789Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini790 – 804CytoplasmicSequence analysisAdd BLAST15
Transmembranei805 – 825Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini826 – 833ExtracellularSequence analysis8
Transmembranei834 – 854Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini855 – 961CytoplasmicSequence analysisAdd BLAST107

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi182W → A: Abolishes signaling via G-proteins. Abolishes antagonist binding. 1 Publication1
Mutagenesisi230Y → A: Slightly decreases signaling via G-proteins. 1 Publication1
Mutagenesisi234Y → A: Decreases signaling via G-proteins. 1 Publication1
Mutagenesisi287H → A: Strongly reduces signaling via G-proteins. Abolishes antagonist binding. 1 Publication1
Mutagenesisi367Y → A: Strongly reduces signaling via G-proteins. No effect on antagonist binding. 1 Publication1
Mutagenesisi395W → A: Strongly reduces signaling via G-proteins. Strongly reduces antagonist binding. 1 Publication1

Organism-specific databases

DisGeNETi2550.
OpenTargetsiENSG00000204681.
ENSG00000206466.
ENSG00000206511.
ENSG00000232569.
ENSG00000232632.
ENSG00000237051.
ENSG00000237112.
PharmGKBiPA28484.

Chemistry databases

ChEMBLiCHEMBL2064.
DrugBankiDB00181. Baclofen.
DB00837. Progabide.
DB01080. Vigabatrin.
GuidetoPHARMACOLOGYi240.

Polymorphism and mutation databases

BioMutaiGABBR1.
DMDMi12643873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 14Sequence analysisAdd BLAST14
ChainiPRO_000001294915 – 961Gamma-aminobutyric acid type B receptor subunit 1Add BLAST947

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi24N-linked (GlcNAc...)Sequence analysis1
Glycosylationi84N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi100 ↔ 145PROSITE-ProRule annotation
Disulfide bondi131 ↔ 157PROSITE-ProRule annotation
Disulfide bondi220 ↔ 246PROSITE-ProRule annotation1 Publication
Disulfide bondi376 ↔ 410PROSITE-ProRule annotation1 Publication
Glycosylationi409N-linked (GlcNAc...)Sequence analysis1
Glycosylationi440N-linked (GlcNAc...)1 Publication1
Glycosylationi482N-linked (GlcNAc...)1 Publication1
Glycosylationi502N-linked (GlcNAc...)Sequence analysis1
Glycosylationi514N-linked (GlcNAc...)Sequence analysis1
Modified residuei873PhosphothreonineBy similarity1
Modified residuei930PhosphothreonineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9UBS5.
PeptideAtlasiQ9UBS5.
PRIDEiQ9UBS5.

PTM databases

iPTMnetiQ9UBS5.
PhosphoSitePlusiQ9UBS5.

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

BgeeiENSG00000204681.
CleanExiHS_GABBR1.
ExpressionAtlasiQ9UBS5. baseline and differential.
GenevisibleiQ9UBS5. HS.

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. 11 interactors.
DIPiDIP-38394N.
IntActiQ9UBS5. 11 interactors.
MINTiMINT-2793192.
STRINGi9606.ENSP00000366233.

Chemistry databases

BindingDBiQ9UBS5.

Structurei

Secondary structure

1961
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi168 – 176Combined sources9
Beta strandi178 – 181Combined sources4
Helixi185 – 200Combined sources16
Turni203 – 205Combined sources3
Beta strandi209 – 217Combined sources9
Helixi222 – 233Combined sources12
Beta strandi234 – 237Combined sources4
Beta strandi240 – 243Combined sources4
Helixi247 – 256Combined sources10
Helixi257 – 260Combined sources4
Beta strandi263 – 268Combined sources6
Helixi272 – 275Combined sources4
Turni277 – 279Combined sources3
Beta strandi283 – 287Combined sources5
Helixi290 – 292Combined sources3
Helixi293 – 303Combined sources11
Beta strandi308 – 316Combined sources9
Helixi317 – 332Combined sources16
Beta strandi336 – 345Combined sources10
Helixi348 – 356Combined sources9
Beta strandi361 – 365Combined sources5
Helixi368 – 381Combined sources14
Beta strandi385 – 387Combined sources3
Beta strandi389 – 393Combined sources5
Helixi400 – 402Combined sources3
Helixi412 – 419Combined sources8
Beta strandi423 – 427Combined sources5
Helixi443 – 453Combined sources11
Helixi458 – 460Combined sources3
Turni462 – 466Combined sources5
Helixi467 – 484Combined sources18
Helixi495 – 497Combined sources3
Helixi504 – 514Combined sources11
Beta strandi517 – 520Combined sources4
Beta strandi523 – 526Combined sources4
Turni529 – 531Combined sources3
Beta strandi536 – 543Combined sources8
Beta strandi546 – 554Combined sources9
Turni555 – 558Combined sources4
Beta strandi559 – 562Combined sources4
Helixi569 – 571Combined sources3
Helixi885 – 917Combined sources33

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 96Sushi 1PROSITE-ProRule annotationAdd BLAST67
Domaini98 – 159Sushi 2PROSITE-ProRule annotationAdd BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni888 – 916Interaction with ATF4By similarityAdd BLAST29

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili869 – 925Sequence analysisAdd BLAST57

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

eggNOGiKOG1055. Eukaryota.
ENOG410XNN1. LUCA.
GeneTreeiENSGT00530000063129.
HOGENOMiHOG000171607.
HOVERGENiHBG051688.
InParanoidiQ9UBS5.
KOiK04615.
OMAiPKICQAR.
OrthoDBiEOG091G01WG.
PhylomeDBiQ9UBS5.
TreeFamiTF313965.

Family and domain databases

CDDicd00033. CCP. 1 hit.
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_dom.
[Graphical view]
PANTHERiPTHR10519. PTHR10519. 1 hit.
PTHR10519:SF42. PTHR10519:SF42. 1 hit.
PfamiPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF00084. Sushi. 1 hit.
[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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti2L → M in Y11044 (PubMed:9753614).Curated1
Sequence conflicti21Q → H in CAA09939 (PubMed:9872316).Curated1
Sequence conflicti21Q → H in CAA09941 (PubMed:9872316).Curated1
Sequence conflicti93P → L in AAC98508 (Ref. 3) Curated1
Sequence conflicti127V → A in CAA09939 (PubMed:9872316).Curated1
Sequence conflicti322Missing in CAA09031 (PubMed:9933300).Curated1
Sequence conflicti542L → P in Y11044 (PubMed:9753614).Curated1
Sequence conflicti691V → G in Y11044 (PubMed:9753614).Curated1
Sequence conflicti905 – 934Missing in CAA09031 (PubMed:9933300).CuratedAdd BLAST30

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01014620A → V.3 PublicationsCorresponds to variant rs1805056dbSNPEnsembl.1
Natural variantiVAR_010147489G → S.3 PublicationsCorresponds to variant rs1805057dbSNPEnsembl.1
Natural variantiVAR_049279645F → L.Corresponds to variant rs2076489dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0020371 – 164MLLLL…NRTPH → MGPGAPFARVGWPLPLLVVM AAGVAPVWASHSPHLPRPHS RVPPHPS in isoform 1B. 3 PublicationsAdd BLAST164
Alternative sequenceiVSP_00203898 – 159Missing in isoform 1C. 2 PublicationsAdd BLAST62
Alternative sequenceiVSP_002039570 – 961GGSPP…HLLYK → VISRTHSPT in isoform 1E. CuratedAdd BLAST392
Alternative sequenceiVSP_002040905 – 961KEERV…HLLYK → SGGLPRGPPEPPDRLSCDGS RVHLLYK in isoform 1D. CuratedAdd BLAST57

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_001305982.1. NM_001319053.1.
NP_001461.1. NM_001470.3. [Q9UBS5-1]
NP_068703.1. NM_021903.2. [Q9UBS5-2]
NP_068704.2. NM_021904.3. [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]
ENST00000551140; ENSP00000448654; ENSG00000237112. [Q9UBS5-5]
ENST00000551423; ENSP00000449342; ENSG00000206511. [Q9UBS5-5]
ENST00000552399; ENSP00000449449; ENSG00000206466. [Q9UBS5-5]
GeneIDi2550.
KEGGihsa:2550.
UCSCiuc003nmp.5. human. [Q9UBS5-1]

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.
CCDSiCCDS4663.1. [Q9UBS5-1]
CCDS4664.1. [Q9UBS5-3]
CCDS4665.1. [Q9UBS5-2]
PIRiJE0356.
RefSeqiNP_001305982.1. NM_001319053.1.
NP_001461.1. NM_001470.3. [Q9UBS5-1]
NP_068703.1. NM_021903.2. [Q9UBS5-2]
NP_068704.2. NM_021904.3. [Q9UBS5-3]
UniGeneiHs.167017.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108825. 11 interactors.
DIPiDIP-38394N.
IntActiQ9UBS5. 11 interactors.
MINTiMINT-2793192.
STRINGi9606.ENSP00000366233.

Chemistry databases

BindingDBiQ9UBS5.
ChEMBLiCHEMBL2064.
DrugBankiDB00181. Baclofen.
DB00837. Progabide.
DB01080. Vigabatrin.
GuidetoPHARMACOLOGYi240.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiQ9UBS5.
PhosphoSitePlusiQ9UBS5.

Polymorphism and mutation databases

BioMutaiGABBR1.
DMDMi12643873.

Proteomic databases

PaxDbiQ9UBS5.
PeptideAtlasiQ9UBS5.
PRIDEiQ9UBS5.

Protocols and materials databases

DNASUi2550.
Structural Biology KnowledgebaseSearch...

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]
ENST00000551140; ENSP00000448654; ENSG00000237112. [Q9UBS5-5]
ENST00000551423; ENSP00000449342; ENSG00000206511. [Q9UBS5-5]
ENST00000552399; ENSP00000449449; ENSG00000206466. [Q9UBS5-5]
GeneIDi2550.
KEGGihsa:2550.
UCSCiuc003nmp.5. human. [Q9UBS5-1]

Organism-specific databases

CTDi2550.
DisGeNETi2550.
GeneCardsiGABBR1.
HGNCiHGNC:4070. GABBR1.
HPAiHPA050483.
MIMi603540. gene.
neXtProtiNX_Q9UBS5.
OpenTargetsiENSG00000204681.
ENSG00000206466.
ENSG00000206511.
ENSG00000232569.
ENSG00000232632.
ENSG00000237051.
ENSG00000237112.
PharmGKBiPA28484.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1055. Eukaryota.
ENOG410XNN1. LUCA.
GeneTreeiENSGT00530000063129.
HOGENOMiHOG000171607.
HOVERGENiHBG051688.
InParanoidiQ9UBS5.
KOiK04615.
OMAiPKICQAR.
OrthoDBiEOG091G01WG.
PhylomeDBiQ9UBS5.
TreeFamiTF313965.

Enzyme and pathway databases

BioCyciZFISH:G66-33668-MONOMER.
ReactomeiR-HSA-1296041. Activation of G protein gated Potassium channels.
R-HSA-418594. G alpha (i) signalling events.
R-HSA-420499. Class C/3 (Metabotropic glutamate/pheromone receptors).
R-HSA-977444. GABA B receptor activation.
R-HSA-997272. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
SIGNORiQ9UBS5.

Miscellaneous databases

ChiTaRSiGABBR1. human.
GeneWikiiGABBR1.
GenomeRNAii2550.
PROiQ9UBS5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204681.
CleanExiHS_GABBR1.
ExpressionAtlasiQ9UBS5. baseline and differential.
GenevisibleiQ9UBS5. HS.

Family and domain databases

CDDicd00033. CCP. 1 hit.
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_dom.
[Graphical view]
PANTHERiPTHR10519. PTHR10519. 1 hit.
PTHR10519:SF42. PTHR10519:SF42. 1 hit.
PfamiPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
PF00084. Sushi. 1 hit.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 169 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.