ID GBRB1_HUMAN Reviewed; 474 AA. AC P18505; B2R6U7; D6REL3; Q16166; Q8TBK3; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 2. DT 05-FEB-2025, entry version 227. DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-1; DE AltName: Full=GABA(A) receptor subunit beta-1 {ECO:0000250|UniProtKB:P15431}; DE Short=GABAAR subunit beta-1 {ECO:0000250|UniProtKB:P14867}; DE Flags: Precursor; GN Name=GABRB1 {ECO:0000312|HGNC:HGNC:4081}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2465923; DOI=10.1016/0014-5793(89)80563-0; RA Schofield P.R., Pritchett D.B., Sontheimer H., Kettenmann H., Seeburg P.H.; RT "Sequence and expression of human GABAA receptor alpha 1 and beta 1 RT subunits."; RL FEBS Lett. 244:361-364(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1655634; DOI=10.1016/0888-7543(91)90189-l; RA Kirkness E.F., Kusiak J.W., Fleming J.T., Menninger J., Gocayne J.D., RA Ward D.C., Venter J.C.; RT "Isolation, characterization, and localization of human genomic DNA RT encoding the beta 1 subunit of the GABAA receptor (GABRB1)."; RL Genomics 10:985-995(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Fetal brain; RX PubMed=24722188; DOI=10.1038/ncomms4650; RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., RA Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., RA Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A., RA Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., RA Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.; RT "Protein interaction network of alternatively spliced isoforms from brain RT links genetic risk factors for autism."; RL Nat. Commun. 5:3650-3650(2014). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-429. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-474 (ISOFORM 1). RX PubMed=2160058; RA Garrett K.M., Saito N., Duman R.S., Abel M.S., Ashton R.A., Fujimori S., RA Beer B., Tallman J.F., Vitek M.P., Blume A.J.; RT "Differential expression of gamma-aminobutyric acidA receptor subunits."; RL Mol. Pharmacol. 37:652-657(1990). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 404-434 (ISOFORM 1), AND VARIANT GLN-421. RX PubMed=8178835; DOI=10.1002/ajmg.1320540105; RA Coon H., Sobell J., Heston L., Sommer S., Hoff M., Holik J., Umar F., RA Robertson M., Reimherr F., Wender P.; RT "Search for mutations in the beta 1 GABAA receptor subunit gene in patients RT with schizophrenia."; RL Am. J. Med. Genet. 54:12-20(1994). RN [10] RP FUNCTION, TRANSPORTER ACTIVITY, AND INTERACTION WITH GABRA2; GABRG1 AND RP GABRQ. RX PubMed=10449790; DOI=10.1073/pnas.96.17.9891; RA Bonnert T.P., McKernan R.M., Farrar S., le Bourdelles B., Heavens R.P., RA Smith D.W., Hewson L., Rigby M.R., Sirinathsinghji D.J.S., Brown N., RA Wafford K.A., Whiting P.J.; RT "Theta, a novel gamma-aminobutyric acid type A receptor subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 96:9891-9896(1999). RN [11] RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH RP GABRA3; GABRBT AND GABRE. RX PubMed=16412217; DOI=10.1186/1471-2210-6-1; RA Ranna M., Sinkkonen S.T., Moeykkynen T., Uusi-Oukari M., Korpi E.R.; RT "Impact of epsilon and theta subunits on pharmacological properties of RT alpha3beta1 GABAA receptors expressed in Xenopus oocytes."; RL BMC Pharmacol. 6:1-1(2006). RN [12] RP INVOLVEMENT IN DEE45, AND VARIANT DEE45 SER-246. RX PubMed=23934111; DOI=10.1038/nature12439; RG Epi4K Consortium; RG Epilepsy Phenome/Genome Project; RA Allen A.S., Berkovic S.F., Cossette P., Delanty N., Dlugos D., RA Eichler E.E., Epstein M.P., Glauser T., Goldstein D.B., Han Y., RA Heinzen E.L., Hitomi Y., Howell K.B., Johnson M.R., Kuzniecky R., RA Lowenstein D.H., Lu Y.F., Madou M.R., Marson A.G., Mefford H.C., RA Esmaeeli Nieh S., O'Brien T.J., Ottman R., Petrovski S., Poduri A., RA Ruzzo E.K., Scheffer I.E., Sherr E.H., Yuskaitis C.J., Abou-Khalil B., RA Alldredge B.K., Bautista J.F., Berkovic S.F., Boro A., Cascino G.D., RA Consalvo D., Crumrine P., Devinsky O., Dlugos D., Epstein M.P., Fiol M., RA Fountain N.B., French J., Friedman D., Geller E.B., Glauser T., Glynn S., RA Haut S.R., Hayward J., Helmers S.L., Joshi S., Kanner A., Kirsch H.E., RA Knowlton R.C., Kossoff E.H., Kuperman R., Kuzniecky R., Lowenstein D.H., RA McGuire S.M., Motika P.V., Novotny E.J., Ottman R., Paolicchi J.M., RA Parent J.M., Park K., Poduri A., Scheffer I.E., Shellhaas R.A., Sherr E.H., RA Shih J.J., Singh R., Sirven J., Smith M.C., Sullivan J., Lin Thio L., RA Venkat A., Vining E.P., Von Allmen G.K., Weisenberg J.L., Widdess-Walsh P., RA Winawer M.R.; RT "De novo mutations in epileptic encephalopathies."; RL Nature 501:217-221(2013). RN [13] RP VARIANT DEE45 ILE-287. RX PubMed=27273810; DOI=10.1002/ana.24699; RA Lien E., Vaatevik A.K., Oestern R., Haukanes B.I., Houge G.; RT "A second patient with a de novo GABRB1 mutation and epileptic RT encephalopathy."; RL Ann. Neurol. 80:311-312(2016). RN [14] RP CHARACTERIZATION OF VARIANT DEE45 SER-246, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=26950270; DOI=10.1002/ana.24631; RA Janve V.S., Hernandez C.C., Verdier K.M., Hu N., Macdonald R.L.; RT "Epileptic encephalopathy de novo GABRB mutations impair GABAA receptor RT function."; RL Ann. Neurol. 79:806-825(2016). CC -!- FUNCTION: Beta subunit of the heteropentameric ligand-gated chloride CC channel gated by gamma-aminobutyric acid (GABA), a major inhibitory CC neurotransmitter in the brain (PubMed:10449790, PubMed:16412217, CC PubMed:26950270). GABA-gated chloride channels, also named GABA(A) CC receptors (GABAAR), consist of five subunits arranged around a central CC pore and contain one or two GABA active binding sites located at the CC alpha and beta subunit interfaces, depending on subunit composition (By CC similarity). When activated by GABA, GABAARs selectively allow the flow CC of chloride anions across the cell membrane down their electrochemical CC gradient (PubMed:10449790, PubMed:16412217, PubMed:26950270). Chloride CC influx into the postsynaptic neuron following GABAAR opening decreases CC the neuron ability to generate a new action potential, thereby reducing CC nerve transmission (PubMed:16412217, PubMed:26950270). Beta-containing CC GABAARs can simultaneously bind GABA and histamine where histamine CC binds at the interface of two neighboring beta subunits, which may be CC involved in the regulation of sleep and wakefulness (By similarity). CC {ECO:0000250|UniProtKB:P15431, ECO:0000250|UniProtKB:P28472, CC ECO:0000269|PubMed:10449790, ECO:0000269|PubMed:16412217, CC ECO:0000269|PubMed:26950270}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10449790, CC ECO:0000269|PubMed:16412217}; CC -!- ACTIVITY REGULATION: Potentiated by etomidate, propofol, pregnanolone CC and flurazepam (PubMed:16412217). Potentiated by histamine (By CC similarity). {ECO:0000250|UniProtKB:P63138, CC ECO:0000269|PubMed:16412217}. CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha (GABRA1-6), CC beta (GABRB1-3), gamma (GABRG1-3), delta (GABRD), epsilon (GABRE), rho CC (GABRR1-3), pi (GABRP) and theta (GABRQ) chains, each subunit CC exhibiting distinct physiological and pharmacological properties CC (PubMed:10449790, PubMed:16412217). Binds UBQLN1 (By similarity). CC {ECO:0000250|UniProtKB:P50571, ECO:0000269|PubMed:10449790, CC ECO:0000269|PubMed:16412217}. CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane CC {ECO:0000250|UniProtKB:P08220}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P08220}. Cell membrane CC {ECO:0000269|PubMed:26950270}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P08220}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P18505-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=P18505-2; Sequence=VSP_055900, VSP_055901; CC -!- DOMAIN: GABAARs subunits share a common topological structure: a CC peptide sequence made up of a long extracellular N-terminal, four CC transmembrane domains, intracellular or cytoplasmic domain located CC between the third and the fourth transmembrane domains. CC {ECO:0000250|UniProtKB:P15431}. CC -!- DISEASE: Developmental and epileptic encephalopathy 45 (DEE45) CC [MIM:617153]: A form of epileptic encephalopathy, a heterogeneous group CC of severe early-onset epilepsies characterized by refractory seizures, CC neurodevelopmental impairment, and poor prognosis. Development is CC normal prior to seizure onset, after which cognitive and motor delays CC become apparent. {ECO:0000269|PubMed:23934111, CC ECO:0000269|PubMed:26950270, ECO:0000269|PubMed:27273810}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRB1 sub- CC subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Forbidden fruit - Issue 56 CC of March 2005; CC URL="https://web.expasy.org/spotlight/back_issues/056"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X14767; CAA32875.1; -; mRNA. DR EMBL; M59216; AAA35862.1; -; Genomic_DNA. DR EMBL; M59212; AAA35862.1; JOINED; Genomic_DNA. DR EMBL; M59214; AAA35862.1; JOINED; Genomic_DNA. DR EMBL; M59215; AAA35862.1; JOINED; Genomic_DNA. DR EMBL; KJ535054; AHW56693.1; -; mRNA. DR EMBL; AK312720; BAG35594.1; -; mRNA. DR EMBL; AC097712; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105394; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107383; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471069; EAW93031.1; -; Genomic_DNA. DR EMBL; BC022449; AAH22449.1; -; mRNA. DR EMBL; S70733; AAB30712.1; -; mRNA. DR CCDS; CCDS3474.1; -. [P18505-1] DR PIR; A40336; A40336. DR RefSeq; NP_000803.2; NM_000812.3. [P18505-1] DR AlphaFoldDB; P18505; -. DR SMR; P18505; -. DR BioGRID; 108834; 5. DR ComplexPortal; CPX-8636; GABA-A receptor, alpha1-beta1-gamma2. DR ComplexPortal; CPX-8702; GABA-A receptor, alpha2-beta1-gamma2 complex. DR ComplexPortal; CPX-8721; GABA-A receptor, alpha3-beta1-gamma2 complex. DR ComplexPortal; CPX-8723; GABA-A receptor, alpha4_beta1_gamma2 complex. DR ComplexPortal; CPX-8724; GABA-A receptor, alpha5-beta1-gamma2 complex. DR ComplexPortal; CPX-8727; GABA-A receptor alpha6-beta1-gamma2 complex. DR IntAct; P18505; 5. DR STRING; 9606.ENSP00000295454; -. DR BindingDB; P18505; -. DR ChEMBL; CHEMBL4558; -. DR DrugBank; DB12537; 1,2-Benzodiazepine. DR DrugBank; DB00546; Adinazolam. DR DrugBank; DB00404; Alprazolam. DR DrugBank; DB00543; Amoxapine. DR DrugBank; DB11901; Apalutamide. DR DrugBank; DB14719; Bentazepam. DR DrugBank; DB11859; Brexanolone. DR DrugBank; DB01558; Bromazepam. DR DrugBank; DB09017; Brotizolam. DR DrugBank; DB00237; Butabarbital. DR DrugBank; DB00241; Butalbital. DR DrugBank; DB01489; Camazepam. DR DrugBank; DB00475; Chlordiazepoxide. DR DrugBank; DB14715; Cinazepam. DR DrugBank; DB01594; Cinolazepam. DR DrugBank; DB00349; Clobazam. DR DrugBank; DB01068; Clonazepam. DR DrugBank; DB00628; Clorazepic acid. DR DrugBank; DB01559; Clotiazepam. DR DrugBank; DB01553; Cloxazolam. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB01511; Delorazepam. DR DrugBank; DB01189; Desflurane. DR DrugBank; DB00829; Diazepam. DR DrugBank; DB13837; Doxefazepam. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB01215; Estazolam. DR DrugBank; DB00402; Eszopiclone. DR DrugBank; DB00898; Ethanol. DR DrugBank; DB00189; Ethchlorvynol. DR DrugBank; DB01545; Ethyl loflazepate. DR DrugBank; DB09166; Etizolam. DR DrugBank; DB00292; Etomidate. DR DrugBank; DB01567; Fludiazepam. DR DrugBank; DB01205; Flumazenil. DR DrugBank; DB01544; Flunitrazepam. DR DrugBank; DB00690; Flurazepam. DR DrugBank; DB01440; gamma-Hydroxybutyric acid. DR DrugBank; DB05087; Ganaxolone. DR DrugBank; DB01437; Glutethimide. DR DrugBank; DB00801; Halazepam. DR DrugBank; DB01159; Halothane. DR DrugBank; DB00753; Isoflurane. DR DrugBank; DB01587; Ketazolam. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB00431; Lindane. DR DrugBank; DB13643; Loprazolam. DR DrugBank; DB00186; Lorazepam. DR DrugBank; DB13872; Lormetazepam. DR DrugBank; DB13437; Medazepam. DR DrugBank; DB00603; Medroxyprogesterone acetate. DR DrugBank; DB01043; Memantine. DR DrugBank; DB00371; Meprobamate. DR DrugBank; DB00463; Metharbital. DR DrugBank; DB01028; Methoxyflurane. DR DrugBank; DB01107; Methyprylon. DR DrugBank; DB15489; Mexazolam. DR DrugBank; DB00683; Midazolam. DR DrugBank; DB01595; Nitrazepam. DR DrugBank; DB14028; Nordazepam. DR DrugBank; DB00842; Oxazepam. DR DrugBank; DB14672; Oxazepam acetate. DR DrugBank; DB00312; Pentobarbital. DR DrugBank; DB00252; Phenytoin. DR DrugBank; DB13335; Pinazepam. DR DrugBank; DB01708; Prasterone. DR DrugBank; DB01588; Prazepam. DR DrugBank; DB00794; Primidone. DR DrugBank; DB00818; Propofol. DR DrugBank; DB01589; Quazepam. DR DrugBank; DB12404; Remimazolam. DR DrugBank; DB01236; Sevoflurane. DR DrugBank; DB09118; Stiripentol. DR DrugBank; DB00306; Talbutal. DR DrugBank; DB01956; Taurine. DR DrugBank; DB00231; Temazepam. DR DrugBank; DB11582; Thiocolchicoside. DR DrugBank; DB00897; Triazolam. DR DrugBank; DB15490; Zuranolone. DR DrugCentral; P18505; -. DR GlyCosmos; P18505; 2 sites, No reported glycans. DR GlyGen; P18505; 2 sites, 1 N-linked glycan (1 site). DR iPTMnet; P18505; -. DR PhosphoSitePlus; P18505; -. DR BioMuta; GABRB1; -. DR DMDM; 23831128; -. DR MassIVE; P18505; -. DR PaxDb; 9606-ENSP00000295454; -. DR PeptideAtlas; P18505; -. DR ProteomicsDB; 53568; -. [P18505-1] DR ABCD; P18505; 1 sequenced antibody. DR Antibodypedia; 12048; 508 antibodies from 41 providers. DR DNASU; 2560; -. DR Ensembl; ENST00000295454.8; ENSP00000295454.3; ENSG00000163288.14. [P18505-1] DR Ensembl; ENST00000510909.1; ENSP00000426766.1; ENSG00000163288.14. [P18505-2] DR GeneID; 2560; -. DR KEGG; hsa:2560; -. DR MANE-Select; ENST00000295454.8; ENSP00000295454.3; NM_000812.4; NP_000803.2. DR UCSC; uc062wjg.1; human. [P18505-1] DR AGR; HGNC:4081; -. DR CTD; 2560; -. DR DisGeNET; 2560; -. DR GeneCards; GABRB1; -. DR HGNC; HGNC:4081; GABRB1. DR HPA; ENSG00000163288; Tissue enhanced (brain, heart muscle). DR MalaCards; GABRB1; -. DR MIM; 137190; gene. DR MIM; 617153; phenotype. DR neXtProt; NX_P18505; -. DR OpenTargets; ENSG00000163288; -. DR PharmGKB; PA28495; -. DR VEuPathDB; HostDB:ENSG00000163288; -. DR eggNOG; KOG3643; Eukaryota. DR GeneTree; ENSGT00940000154245; -. DR HOGENOM; CLU_010920_0_2_1; -. DR InParanoid; P18505; -. DR OMA; DRPIGHK; -. DR OrthoDB; 8890589at2759; -. DR PhylomeDB; P18505; -. DR TreeFam; TF315453; -. DR PathwayCommons; P18505; -. DR Reactome; R-HSA-1236394; Signaling by ERBB4. DR Reactome; R-HSA-977443; GABA receptor activation. DR SignaLink; P18505; -. DR SIGNOR; P18505; -. DR BioGRID-ORCS; 2560; 9 hits in 1161 CRISPR screens. DR ChiTaRS; GABRB1; human. DR GeneWiki; GABRB1; -. DR GenomeRNAi; 2560; -. DR Pharos; P18505; Tclin. DR PRO; PR:P18505; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P18505; protein. DR Bgee; ENSG00000163288; Expressed in Brodmann (1909) area 23 and 126 other cell types or tissues. DR ExpressionAtlas; P18505; baseline and differential. DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:1902711; C:GABA-A receptor complex; IDA:UniProtKB. DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl. DR GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:1902495; C:transmembrane transporter complex; IBA:GO_Central. DR GO; GO:0150047; F:G protein-coupled neurotransmitter receptor activity involved in regulation of presynaptic membrane potential; IEA:Ensembl. DR GO; GO:0050811; F:GABA receptor binding; IEA:Ensembl. DR GO; GO:0004890; F:GABA-A receptor activity; IDA:UniProtKB. DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IDA:UniProtKB. DR GO; GO:0015276; F:ligand-gated monoatomic ion channel activity; ISS:UniProtKB. DR GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO. DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central. DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl. DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB. DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl. DR GO; GO:1902476; P:chloride transmembrane transport; IDA:GO_Central. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:UniProtKB. DR GO; GO:0006811; P:monoatomic ion transport; ISS:UniProtKB. DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd18999; LGIC_ECD_GABAAR_B; 1. DR CDD; cd19053; LGIC_TM_GABAAR_beta; 1. DR FunFam; 2.70.170.10:FF:000004; Gamma-aminobutyric acid receptor subunit beta-2 isoform A; 1. DR FunFam; 1.20.58.390:FF:000067; Glycine receptor subunit alpha-2; 1. DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1. DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1. DR InterPro; IPR006028; GABAA/Glycine_rcpt. DR InterPro; IPR002289; GABAAb_rcpt. DR InterPro; IPR006202; Neur_chan_lig-bd. DR InterPro; IPR036734; Neur_chan_lig-bd_sf. DR InterPro; IPR006201; Neur_channel. DR InterPro; IPR036719; Neuro-gated_channel_TM_sf. DR InterPro; IPR038050; Neuro_actylchol_rec. DR InterPro; IPR006029; Neurotrans-gated_channel_TM. DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS. DR NCBIfam; TIGR00860; LIC; 1. DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR01160; GABAARBETA. DR PRINTS; PR00253; GABAARECEPTR. DR PRINTS; PR00252; NRIONCHANNEL. DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1. DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Chloride; Chloride channel; KW Disease variant; Disulfide bond; Epilepsy; Glycoprotein; Ion channel; KW Ion transport; Ligand-gated ion channel; Membrane; KW Postsynaptic cell membrane; Proteomics identification; Receptor; KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix; KW Transport. FT SIGNAL 1..25 FT /evidence="ECO:0000255" FT CHAIN 26..474 FT /note="Gamma-aminobutyric acid receptor subunit beta-1" FT /id="PRO_0000000456" FT TOPO_DOM 26..245 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 246..267 FT /note="Helical" FT /evidence="ECO:0000305" FT TRANSMEM 271..293 FT /note="Helical" FT /evidence="ECO:0000305" FT TRANSMEM 305..327 FT /note="Helical" FT /evidence="ECO:0000305" FT TOPO_DOM 328..451 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 452..473 FT /note="Helical" FT /evidence="ECO:0000305" FT BINDING 122 FT /ligand="histamine" FT /ligand_id="ChEBI:CHEBI:58432" FT /ligand_note="ligand shared between two neighboring beta FT subunits" FT /note="in chain B" FT /evidence="ECO:0000250|UniProtKB:P28472" FT BINDING 181..182 FT /ligand="histamine" FT /ligand_id="ChEBI:CHEBI:58432" FT /ligand_note="ligand shared between two neighboring beta FT subunits" FT /note="in chain B" FT /evidence="ECO:0000250|UniProtKB:P28472" FT BINDING 182 FT /ligand="4-aminobutanoate" FT /ligand_id="ChEBI:CHEBI:59888" FT /ligand_note="ligand shared with the neighboring alpha FT subunit" FT /note="in chain A" FT /evidence="ECO:0000250|UniProtKB:P15431" FT BINDING 227 FT /ligand="4-aminobutanoate" FT /ligand_id="ChEBI:CHEBI:59888" FT /ligand_note="ligand shared with the neighboring alpha FT subunit" FT /note="in chain A" FT /evidence="ECO:0000250|UniProtKB:P15431" FT BINDING 227 FT /ligand="histamine" FT /ligand_id="ChEBI:CHEBI:58432" FT /ligand_note="ligand shared between two neighboring beta FT subunits" FT /note="in chain B" FT /evidence="ECO:0000250|UniProtKB:P28472" FT CARBOHYD 105 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 174 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 161..175 FT /evidence="ECO:0000250|UniProtKB:P15431" FT VAR_SEQ 59..87 FT /note="PPVDVGMRIDVASIDMVSEVNMDYTLTMY -> LYTHHVFPAVLERQKAFLF FT WNPTEPHPRQ (in isoform 2)" FT /evidence="ECO:0000303|PubMed:24722188" FT /id="VSP_055900" FT VAR_SEQ 88..474 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:24722188" FT /id="VSP_055901" FT VARIANT 246 FT /note="F -> S (in DEE45; no effect on localization to the FT plasma membrane; increased GABA-gated chloride ion channel FT activity; increased single channel burst duration; FT dbSNP:rs886039817)" FT /evidence="ECO:0000269|PubMed:23934111, FT ECO:0000269|PubMed:26950270" FT /id="VAR_077104" FT VARIANT 287 FT /note="T -> I (in DEE45; dbSNP:rs886039818)" FT /evidence="ECO:0000269|PubMed:27273810" FT /id="VAR_077105" FT VARIANT 421 FT /note="H -> Q (found in 1.1% of population and in some FT schizophrenic patients; dbSNP:rs41311286)" FT /evidence="ECO:0000269|PubMed:8178835" FT /id="VAR_000302" FT VARIANT 429 FT /note="I -> N (in dbSNP:rs17852014)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_035441" FT CONFLICT 35 FT /note="S -> P (in Ref. 1; CAA32875)" FT /evidence="ECO:0000305" FT CONFLICT 117 FT /note="W -> C (in Ref. 7; AAH22449)" FT /evidence="ECO:0000305" SQ SEQUENCE 474 AA; 54235 MW; 05DA70F6FCD04E54 CRC64; MWTVQNRESL GLLSFPVMIT MVCCAHSTNE PSNMSYVKET VDRLLKGYDI RLRPDFGGPP VDVGMRIDVA SIDMVSEVNM DYTLTMYFQQ SWKDKRLSYS GIPLNLTLDN RVADQLWVPD TYFLNDKKSF VHGVTVKNRM IRLHPDGTVL YGLRITTTAA CMMDLRRYPL DEQNCTLEIE SYGYTTDDIE FYWNGGEGAV TGVNKIELPQ FSIVDYKMVS KKVEFTTGAY PRLSLSFRLK RNIGYFILQT YMPSTLITIL SWVSFWINYD ASAARVALGI TTVLTMTTIS THLRETLPKI PYVKAIDIYL MGCFVFVFLA LLEYAFVNYI FFGKGPQKKG ASKQDQSANE KNKLEMNKVQ VDAHGNILLS TLEIRNETSG SEVLTSVSDP KATMYSYDSA SIQYRKPLSS REAYGRALDR HGVPSKGRIR RRASQLKVKI PDLTDVNSID KWSRMFFPIT FSLFNVVYWL YYVH //