GABBR1
entrez
2550
canonical
uniprot
Q9UBS5
canonical
ensembl
ENSG00000204681
resolver
ensembl
ENSG00000206466
resolver
ensembl
ENSG00000206511
resolver
ensembl
ENSG00000232569
resolver
ensembl
ENSG00000232632
resolver
ensembl
ENSG00000237051
resolver
ensembl
ENSG00000237112
resolver
ensp
ENSP00000366211
resolver
ensp
ENSP00000366215
resolver
ensp
ENSP00000366233
resolver
ensp
ENSP00000416731
resolver
ensp
ENSP00000417332
resolver
ensp
ENSP00000419061
resolver
enst
ENST00000418225
resolver
enst
ENST00000476670
resolver
genesymbol
GABBR1
resolver
genesymbol_syn
GPRC3A
resolver
hgnc
HGNC:4070
resolver
uniprot
A0A0G2JKF9
resolver
uniprot
B0UXY7
resolver
uniprot
C9J342
resolver
uniprot
O95375
resolver
uniprot
O95468
resolver
uniprot
O95975
resolver
uniprot
O96022
resolver
uniprot
Q59HG8
resolver
uniprot
Q5STL4
resolver
uniprot
Q5SUJ8
resolver
uniprot
Q5SUJ9
resolver
uniprot
Q5SUL3
resolver
uniprot
Q71SG6
resolver
uniprot
Q86W60
resolver
uniprot
Q8IW08
resolver
uniprot
Q9UQQ0
resolver
uniprot_entry
A0A0G2JKF9_HUMAN
resolver
uniprot_entry
C9J342_HUMAN
resolver
uniprot_entry
GABR1_HUMAN
resolver
uniprot_entry
Q59HG8_HUMAN
resolver
uniprot_entry
Q5SUJ9_HUMAN
resolver
uniprot_entry
Q8IW08_HUMAN
resolver
uniprot_sec
B0UXY7
resolver
uniprot_sec
O95375
resolver
uniprot_sec
O95468
resolver
uniprot_sec
O95975
resolver
uniprot_sec
O96022
resolver
uniprot_sec
Q5STL4
resolver
uniprot_sec
Q5SUJ8
resolver
uniprot_sec
Q5SUL3
resolver
uniprot_sec
Q71SG6
resolver
uniprot_sec
Q86W60
resolver
uniprot_sec
Q9UQQ0
resolver
amino_acid_sequence
MLLLLLLAPLFLRPPGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKIYDPSINCTVDEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRNQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSRKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQLRSRRHPPTPPEPSGGLPRGPPEPPDRLSCDGSRVHLLYK
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with language delay and variable cognitive abnormalities (NEDLC) [MIM:620502]: An autosomal dominant disorder characterized by language delay ranging from mild to severe, varying degrees of intellectual disability, and learning difficulties. Additional features include early motor delay, muscular hypotonia, behavioral abnormalities, sleep disorders, and seizures. {ECO:0000269|PubMed:36103875}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Component of a heterodimeric G protein-coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:36103875, PubMed:9872316, PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). 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 (PubMed:10075644, PubMed:10773016, PubMed:10906333, PubMed:24305054, PubMed:9872744). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (PubMed:9844003). 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 (PubMed:10075644, PubMed:22660477, PubMed:9844003, PubMed:9872316, PubMed:9872744). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). Activated by (-)-baclofen, cgp27492 and blocked by phaclofen (PubMed:24305054, PubMed:9844003, PubMed:9872316). {ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016, ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:15617512, ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:36103875, ECO:0000269|PubMed:9844003, ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744, ECO:0000305}.; FUNCTION: 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.
uniprot
proteins
mass_dalton
108320
uniprot
proteins
mutagenesis
MUTAGEN 182; /note="W->A: Abolishes signaling via G proteins. Abolishes antagonist binding."; /evidence="ECO:0000269|PubMed:24305054"; MUTAGEN 230; /note="Y->A: Slightly decreases signaling via G proteins."; /evidence="ECO:0000269|PubMed:22660477"; MUTAGEN 234; /note="Y->A: Decreases signaling via G proteins."; /evidence="ECO:0000269|PubMed:22660477"; MUTAGEN 287; /note="H->A: Strongly reduces signaling via G proteins. Abolishes antagonist binding."; /evidence="ECO:0000269|PubMed:24305054"; MUTAGEN 367; /note="Y->A: Strongly reduces signaling via G proteins. No effect on antagonist binding."; /evidence="ECO:0000269|PubMed:24305054"; MUTAGEN 395; /note="W->A: Strongly reduces signaling via G proteins. Strongly reduces antagonist binding."; /evidence="ECO:0000269|PubMed:24305054
uniprot
proteins
protein_family
G protein-coupled receptor 3 family
uniprot
proteins
protein_family
GABA-B receptor subfamily
uniprot
proteins
pubmed
10075644
uniprot
proteins
pubmed
10402495
uniprot
proteins
pubmed
10773016
uniprot
proteins
pubmed
10906333
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14718537
uniprot
proteins
pubmed
14759258
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15617512
uniprot
proteins
pubmed
18165688
uniprot
proteins
pubmed
22660477
uniprot
proteins
pubmed
24305054
uniprot
proteins
pubmed
36103875
uniprot
proteins
pubmed
9753614
uniprot
proteins
pubmed
9798068
uniprot
proteins
pubmed
9844003
uniprot
proteins
pubmed
9872316
uniprot
proteins
pubmed
9872744
uniprot
proteins
pubmed
9889352
uniprot
proteins
pubmed
9933300
uniprot
proteins
sequence_length
961
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15617512}; Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9Z0U4}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9Z0U4}. 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 (PubMed:15617512). {ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:15617512}.; SUBCELLULAR LOCATION: [Isoform 1E]: Secreted {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 592..612; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 632..652; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 668..688; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 711..731; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 769..789; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 805..825; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 834..854; /note="Helical; Name=7"; /evidence="ECO:0000255
uniprot
proteins