ID   GNB5_HUMAN              Reviewed;         395 AA.
AC   O14775; B2RBR5; Q9HAU9; Q9UFT3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2003, sequence version 2.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=Guanine nucleotide-binding protein subunit beta-5;
DE   AltName: Full=Gbeta5;
DE   AltName: Full=Transducin beta chain 5;
GN   Name=GNB5;
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 2), AND TISSUE SPECIFICITY.
RX   PubMed=9606987; DOI=10.1016/s0167-4889(98)00017-2;
RA   Jones P.G., Lombardi S.J., Cockett M.I.;
RT   "Cloning and tissue distribution of the human G protein beta 5 cDNA.";
RL   Biochim. Biophys. Acta 1402:288-291(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Uterus;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Cerebellum;
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 MRNA] (ISOFORM 2).
RC   TISSUE=Lymph;
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   [6]
RP   INTERACTION WITH RGS6 AND RGS7.
RX   PubMed=10521509; DOI=10.1074/jbc.274.43.31087;
RA   Posner B.A., Gilman A.G., Harris B.A.;
RT   "Regulators of G protein signaling 6 and 7. Purification of complexes with
RT   gbeta5 and assessment of their effects on g protein-mediated signaling
RT   pathways.";
RL   J. Biol. Chem. 274:31087-31093(1999).
RN   [7]
RP   INTERACTION WITH RGS6 AND RGS7.
RX   PubMed=10339615; DOI=10.1073/pnas.96.11.6489;
RA   Snow B.E., Betts L., Mangion J., Sondek J., Siderovski D.P.;
RT   "Fidelity of G protein beta-subunit association by the G protein gamma-
RT   subunit-like domains of RGS6, RGS7, and RGS11.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:6489-6494(1999).
RN   [8]
RP   INVOLVEMENT IN LDMLS1, INVOLVEMENT IN LDMLS2, AND VARIANT LDMLS2 LEU-123.
RX   PubMed=27523599; DOI=10.1016/j.ajhg.2016.06.025;
RA   Lodder E.M., De Nittis P., Koopman C.D., Wiszniewski W.,
RA   Moura de Souza C.F., Lahrouchi N., Guex N., Napolioni V., Tessadori F.,
RA   Beekman L., Nannenberg E.A., Boualla L., Blom N.A., de Graaff W.,
RA   Kamermans M., Cocciadiferro D., Malerba N., Mandriani B., Akdemir Z.H.,
RA   Fish R.J., Eldomery M.K., Ratbi I., Wilde A.A., de Boer T., Simonds W.F.,
RA   Neerman-Arbez M., Sutton V.R., Kok F., Lupski J.R., Reymond A.,
RA   Bezzina C.R., Bakkers J., Merla G.;
RT   "GNB5 mutations cause an autosomal-recessive multisystem syndrome with
RT   sinus bradycardia and cognitive disability.";
RL   Am. J. Hum. Genet. 99:704-710(2016).
RN   [9]
RP   INVOLVEMENT IN LDMLS2, VARIANT LDMLS2 LEU-123, FUNCTION, AND
RP   CHARACTERIZATION OF VARIANT LDMLS2 LEU-123.
RX   PubMed=27677260; DOI=10.1186/s13059-016-1061-6;
RA   Shamseldin H.E., Masuho I., Alenizi A., Alyamani S., Patil D.N.,
RA   Ibrahim N., Martemyanov K.A., Alkuraya F.S.;
RT   "GNB5 mutation causes a novel neuropsychiatric disorder featuring attention
RT   deficit hyperactivity disorder, severely impaired language development and
RT   normal cognition.";
RL   Genome Biol. 17:R195.1-R195.9(2016).
RN   [10] {ECO:0007744|PDB:7EWP, ECO:0007744|PDB:7EWR}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.30 ANGSTROMS) IN COMPLEX WITH GPR158
RP   AND RGS7.
RX   PubMed=34815401; DOI=10.1038/s41467-021-27147-1;
RA   Jeong E., Kim Y., Jeong J., Cho Y.;
RT   "Structure of the class C orphan GPCR GPR158 in complex with RGS7-Gbeta5.";
RL   Nat. Commun. 12:6805-6805(2021).
CC   -!- FUNCTION: Enhances GTPase-activating protein (GAP) activity of
CC       regulator of G protein signaling (RGS) proteins, such as RGS7 and RGS9,
CC       hence involved in the termination of the signaling initiated by the G
CC       protein coupled receptors (GPCRs) by accelerating the GTP hydrolysis on
CC       the G-alpha subunits, thereby promoting their inactivation
CC       (PubMed:27677260). Increases RGS7 GTPase-activating protein (GAP)
CC       activity, thereby regulating mood and cognition (By similarity).
CC       Increases RGS9 GTPase-activating protein (GAP) activity, hence
CC       contributes to the deactivation of G protein signaling initiated by
CC       D(2) dopamine receptors (PubMed:27677260). May play an important role
CC       in neuronal signaling, including in the parasympathetic, but not
CC       sympathetic, control of heart rate (By similarity).
CC       {ECO:0000250|UniProtKB:A1L271, ECO:0000250|UniProtKB:P62881,
CC       ECO:0000269|PubMed:27677260}.
CC   -!- SUBUNIT: Component of a complex composed of RGS9 (isoform RGS9-1), GNB5
CC       and RGS9BP; within this complex, the presence of GNB5 stabilizes both
CC       itself and RGS9 and increases RGS9 GTPase-activating protein (GAP)
CC       activity (PubMed:27677260). Interacts with RGS7, forming the RGS7-GNB5
CC       complex; within this complex, the presence of GNB5 increases RGS7
CC       GTPase-activating protein (GAP) activity (PubMed:34815401). Interacts
CC       with GPR158; promotes the GTPase activator activity of the RGS7-GNB5
CC       complex in absence of glycine, in contrast GTPase activator activity of
CC       the RGS7-GNB5 complex is inhibited in presence of glycine
CC       (PubMed:10339615, PubMed:10521509, PubMed:34815401). Interacts with
CC       RGS6 (PubMed:10339615, PubMed:10521509). {ECO:0000269|PubMed:10339615,
CC       ECO:0000269|PubMed:10521509, ECO:0000269|PubMed:27677260,
CC       ECO:0000269|PubMed:34815401}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62881}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Long, Beta-5L;
CC         IsoId=O14775-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O14775-2; Sequence=VSP_008765;
CC       Name=3;
CC         IsoId=O14775-3; Sequence=VSP_008765, VSP_039101;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9606987}.
CC   -!- DISEASE: Lodder-Merla syndrome, type 1, with impaired intellectual
CC       development and cardiac arrhythmia (LDMLS1) [MIM:617173]: An autosomal
CC       recessive multisystem disorder characterized by delayed psychomotor
CC       development, severe intellectual disability with poor or absent speech,
CC       and bradycardia and/or cardiac sinus arrhythmias. Additional features
CC       include visual abnormalities, seizures, hypotonia, and gastric reflux.
CC       {ECO:0000269|PubMed:27523599}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Lodder-Merla syndrome, type 2, with developmental delay and
CC       with or without cardiac arrhythmia (LDMLS2) [MIM:617182]: An autosomal
CC       recessive neurodevelopmental disorder characterized by speech
CC       impairment and variable expressivity of attention deficit hyperactivity
CC       disorder. Some patients manifest developmental and motor delay,
CC       hypotonia, and sinus-node dysfunction. {ECO:0000269|PubMed:27523599,
CC       ECO:0000269|PubMed:27677260}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC       {ECO:0000305}.
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DR   EMBL; AF017656; AAC63826.1; -; mRNA.
DR   EMBL; AL117471; CAB55946.1; -; mRNA.
DR   EMBL; AF501885; AAM15921.1; -; mRNA.
DR   EMBL; AF300650; AAG18444.1; -; mRNA.
DR   EMBL; AK314775; BAG37312.1; -; mRNA.
DR   EMBL; BC013997; AAH13997.1; -; mRNA.
DR   CCDS; CCDS10149.1; -. [O14775-1]
DR   CCDS; CCDS45261.1; -. [O14775-2]
DR   PIR; T17256; T17256.
DR   RefSeq; NP_006569.1; NM_006578.3. [O14775-2]
DR   RefSeq; NP_057278.2; NM_016194.3. [O14775-1]
DR   PDB; 7EWP; EM; 4.30 A; D=1-395.
DR   PDB; 7EWR; EM; 4.70 A; D/F=1-395.
DR   PDB; 8SG8; EM; 3.00 A; N=1-395.
DR   PDB; 8SG9; EM; 2.90 A; N=1-395.
DR   PDB; 8SGC; EM; 2.90 A; N=1-395.
DR   PDB; 8SGL; EM; 2.90 A; N=1-395.
DR   PDB; 8SH9; EM; 2.70 A; N=1-395.
DR   PDB; 8SHA; EM; 3.00 A; N=1-395.
DR   PDB; 8SHD; EM; 2.90 A; N=1-395.
DR   PDB; 8SHE; EM; 2.80 A; N=1-395.
DR   PDB; 8SHF; EM; 3.00 A; N=1-395.
DR   PDB; 8SHG; EM; 2.80 A; N=1-395.
DR   PDB; 8SHL; EM; 3.00 A; N=1-395.
DR   PDB; 8SHN; EM; 2.80 A; N=1-395.
DR   PDB; 8SHO; EM; 3.00 A; N=1-395.
DR   PDB; 8SHP; EM; 3.00 A; N=1-395.
DR   PDB; 8SHQ; EM; 2.90 A; N=1-395.
DR   PDB; 8SHT; EM; 3.00 A; N=1-395.
DR   PDBsum; 7EWP; -.
DR   PDBsum; 7EWR; -.
DR   PDBsum; 8SG8; -.
DR   PDBsum; 8SG9; -.
DR   PDBsum; 8SGC; -.
DR   PDBsum; 8SGL; -.
DR   PDBsum; 8SH9; -.
DR   PDBsum; 8SHA; -.
DR   PDBsum; 8SHD; -.
DR   PDBsum; 8SHE; -.
DR   PDBsum; 8SHF; -.
DR   PDBsum; 8SHG; -.
DR   PDBsum; 8SHL; -.
DR   PDBsum; 8SHN; -.
DR   PDBsum; 8SHO; -.
DR   PDBsum; 8SHP; -.
DR   PDBsum; 8SHQ; -.
DR   PDBsum; 8SHT; -.
DR   AlphaFoldDB; O14775; -.
DR   EMDB; EMD-25612; -.
DR   EMDB; EMD-25613; -.
DR   EMDB; EMD-25748; -.
DR   EMDB; EMD-25749; -.
DR   EMDB; EMD-25751; -.
DR   EMDB; EMD-25752; -.
DR   EMDB; EMD-26099; -.
DR   EMDB; EMD-26100; -.
DR   EMDB; EMD-26101; -.
DR   EMDB; EMD-26102; -.
DR   EMDB; EMD-26313; -.
DR   EMDB; EMD-27872; -.
DR   EMDB; EMD-27873; -.
DR   EMDB; EMD-27874; -.
DR   EMDB; EMD-27968; -.
DR   EMDB; EMD-27969; -.
DR   EMDB; EMD-28896; -.
DR   EMDB; EMD-29301; -.
DR   EMDB; EMD-29302; -.
DR   EMDB; EMD-29303; -.
DR   EMDB; EMD-29453; -.
DR   EMDB; EMD-29684; -.
DR   EMDB; EMD-29861; -.
DR   EMDB; EMD-31360; -.
DR   EMDB; EMD-31363; -.
DR   EMDB; EMD-31365; -.
DR   EMDB; EMD-31366; -.
DR   EMDB; EMD-32297; -.
DR   EMDB; EMD-32298; -.
DR   EMDB; EMD-32424; -.
DR   EMDB; EMD-32425; -.
DR   EMDB; EMD-33247; -.
DR   EMDB; EMD-33479; -.
DR   EMDB; EMD-33512; -.
DR   EMDB; EMD-33513; -.
DR   EMDB; EMD-33562; -.
DR   EMDB; EMD-33633; -.
DR   EMDB; EMD-33634; -.
DR   EMDB; EMD-33635; -.
DR   EMDB; EMD-33636; -.
DR   EMDB; EMD-33710; -.
DR   EMDB; EMD-33871; -.
DR   EMDB; EMD-33888; -.
DR   EMDB; EMD-33889; -.
DR   EMDB; EMD-33984; -.
DR   EMDB; EMD-33985; -.
DR   EMDB; EMD-34371; -.
DR   EMDB; EMD-34676; -.
DR   EMDB; EMD-34677; -.
DR   EMDB; EMD-34833; -.
DR   EMDB; EMD-35135; -.
DR   EMDB; EMD-35345; -.
DR   EMDB; EMD-35346; -.
DR   EMDB; EMD-35705; -.
DR   EMDB; EMD-35761; -.
DR   EMDB; EMD-35762; -.
DR   EMDB; EMD-35763; -.
DR   EMDB; EMD-35764; -.
DR   EMDB; EMD-35913; -.
DR   EMDB; EMD-35914; -.
DR   EMDB; EMD-35915; -.
DR   EMDB; EMD-36409; -.
DR   EMDB; EMD-40052; -.
DR   EMDB; EMD-40452; -.
DR   EMDB; EMD-40453; -.
DR   EMDB; EMD-40454; -.
DR   EMDB; EMD-40461; -.
DR   EMDB; EMD-40481; -.
DR   EMDB; EMD-40482; -.
DR   EMDB; EMD-40484; -.
DR   EMDB; EMD-40485; -.
DR   EMDB; EMD-40486; -.
DR   EMDB; EMD-40487; -.
DR   EMDB; EMD-40488; -.
DR   EMDB; EMD-40489; -.
DR   EMDB; EMD-40490; -.
DR   EMDB; EMD-40491; -.
DR   EMDB; EMD-40492; -.
DR   EMDB; EMD-40494; -.
DR   SMR; O14775; -.
DR   BioGRID; 115920; 49.
DR   CORUM; O14775; -.
DR   IntAct; O14775; 37.
DR   MINT; O14775; -.
DR   STRING; 9606.ENSP00000261837; -.
DR   GlyGen; O14775; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O14775; -.
DR   PhosphoSitePlus; O14775; -.
DR   BioMuta; GNB5; -.
DR   EPD; O14775; -.
DR   jPOST; O14775; -.
DR   MassIVE; O14775; -.
DR   MaxQB; O14775; -.
DR   PaxDb; 9606-ENSP00000261837; -.
DR   PeptideAtlas; O14775; -.
DR   ProteomicsDB; 48226; -. [O14775-1]
DR   ProteomicsDB; 48227; -. [O14775-2]
DR   ProteomicsDB; 48228; -. [O14775-3]
DR   Pumba; O14775; -.
DR   Antibodypedia; 24930; 336 antibodies from 32 providers.
DR   DNASU; 10681; -.
DR   Ensembl; ENST00000261837.12; ENSP00000261837.7; ENSG00000069966.19. [O14775-1]
DR   Ensembl; ENST00000358784.11; ENSP00000351635.7; ENSG00000069966.19. [O14775-2]
DR   Ensembl; ENST00000396335.8; ENSP00000379626.4; ENSG00000069966.19. [O14775-3]
DR   GeneID; 10681; -.
DR   KEGG; hsa:10681; -.
DR   MANE-Select; ENST00000261837.12; ENSP00000261837.7; NM_016194.4; NP_057278.2.
DR   UCSC; uc002abr.2; human. [O14775-1]
DR   AGR; HGNC:4401; -.
DR   DisGeNET; 10681; -.
DR   GeneCards; GNB5; -.
DR   GeneReviews; GNB5; -.
DR   HGNC; HGNC:4401; GNB5.
DR   HPA; ENSG00000069966; Tissue enhanced (retina).
DR   MalaCards; GNB5; -.
DR   MIM; 604447; gene.
DR   MIM; 617173; phenotype.
DR   MIM; 617182; phenotype.
DR   neXtProt; NX_O14775; -.
DR   OpenTargets; ENSG00000069966; -.
DR   Orphanet; 542306; GNB5-related intellectual disability-cardiac arrhythmia syndrome.
DR   PharmGKB; PA28780; -.
DR   VEuPathDB; HostDB:ENSG00000069966; -.
DR   eggNOG; KOG0286; Eukaryota.
DR   GeneTree; ENSGT01000000214413; -.
DR   HOGENOM; CLU_000288_57_34_1; -.
DR   InParanoid; O14775; -.
DR   OMA; WVMACSY; -.
DR   OrthoDB; 102097at2759; -.
DR   PhylomeDB; O14775; -.
DR   TreeFam; TF106149; -.
DR   PathwayCommons; O14775; -.
DR   Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-HSA-202040; G-protein activation.
DR   Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade. [O14775-1]
DR   Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Reactome; R-HSA-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-HSA-392851; Prostacyclin signalling through prostacyclin receptor.
DR   Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR   Reactome; R-HSA-4086398; Ca2+ pathway.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR   Reactome; R-HSA-418217; G beta:gamma signalling through PLC beta.
DR   Reactome; R-HSA-418555; G alpha (s) signalling events.
DR   Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   Reactome; R-HSA-418597; G alpha (z) signalling events.
DR   Reactome; R-HSA-420092; Glucagon-type ligand receptors.
DR   Reactome; R-HSA-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR   Reactome; R-HSA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
DR   Reactome; R-HSA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Reactome; R-HSA-8964315; G beta:gamma signalling through BTK.
DR   Reactome; R-HSA-8964616; G beta:gamma signalling through CDC42.
DR   Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-HSA-9634597; GPER1 signaling.
DR   Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR   Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR   SignaLink; O14775; -.
DR   SIGNOR; O14775; -.
DR   BioGRID-ORCS; 10681; 8 hits in 1155 CRISPR screens.
DR   ChiTaRS; GNB5; human.
DR   GeneWiki; GNB5; -.
DR   GenomeRNAi; 10681; -.
DR   Pharos; O14775; Tbio.
DR   PRO; PR:O14775; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; O14775; Protein.
DR   Bgee; ENSG00000069966; Expressed in middle temporal gyrus and 196 other cell types or tissues.
DR   ExpressionAtlas; O14775; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:1902773; C:GTPase activator complex; TAS:UniProtKB.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0098793; C:presynapse; IEA:Ensembl.
DR   GO; GO:0031682; F:G-protein gamma-subunit binding; IPI:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IPI:UniProtKB.
DR   GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR   GO; GO:1990603; P:dark adaptation; IEA:Ensembl.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0036367; P:light adaption; IEA:Ensembl.
DR   GO; GO:1901386; P:negative regulation of voltage-gated calcium channel activity; IDA:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; NAS:UniProtKB.
DR   CDD; cd00200; WD40; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR001632; Gprotein_B.
DR   InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR19850; GUANINE NUCLEOTIDE-BINDING PROTEIN BETA G PROTEIN BETA; 1.
DR   PANTHER; PTHR19850:SF36; GUANINE NUCLEOTIDE-BINDING PROTEIN SUBUNIT BETA-5; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PIRSF; PIRSF002394; GN-bd_beta; 1.
DR   PRINTS; PR00319; GPROTEINB.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   Genevisible; O14775; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disease variant;
KW   Intellectual disability; Membrane; Reference proteome; Repeat; Transducer;
KW   WD repeat.
FT   CHAIN           1..395
FT                   /note="Guanine nucleotide-binding protein subunit beta-5"
FT                   /id="PRO_0000127705"
FT   REPEAT          103..142
FT                   /note="WD 1"
FT   REPEAT          145..184
FT                   /note="WD 2"
FT   REPEAT          193..234
FT                   /note="WD 3"
FT   REPEAT          236..278
FT                   /note="WD 4"
FT   REPEAT          279..318
FT                   /note="WD 5"
FT   REPEAT          320..362
FT                   /note="WD 6"
FT   REPEAT          365..394
FT                   /note="WD 7"
FT   VAR_SEQ         1..42
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11230166,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9606987, ECO:0000303|Ref.3"
FT                   /id="VSP_008765"
FT   VAR_SEQ         140..209
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11230166"
FT                   /id="VSP_039101"
FT   VARIANT         123
FT                   /note="S -> L (in LDMLS2; severe, but incomplete loss of
FT                   activation of RGS9 GTPase activator activity, affecting the
FT                   deactivation of D(2) dopamine receptor-mediated signaling;
FT                   decreased stability; decreased RGS9 stabilization;
FT                   dbSNP:rs761399728)"
FT                   /evidence="ECO:0000269|PubMed:27523599,
FT                   ECO:0000269|PubMed:27677260"
FT                   /id="VAR_077994"
FT   VARIANT         213
FT                   /note="A -> V (in dbSNP:rs34637551)"
FT                   /id="VAR_049270"
FT   CONFLICT        223
FT                   /note="D -> G (in Ref. 4; BAG37312)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   395 AA;  43566 MW;  E001B07FCFA587AD CRC64;
     MCDQTFLVNV FGSCDKCFKQ RALRPVFKKS QQLSYCSTCA EIMATEGLHE NETLASLKSE
     AESLKGKLEE ERAKLHDVEL HQVAERVEAL GQFVMKTRRT LKGHGNKVLC MDWCKDKRRI
     VSSSQDGKVI VWDSFTTNKE HAVTMPCTWV MACAYAPSGC AIACGGLDNK CSVYPLTFDK
     NENMAAKKKS VAMHTNYLSA CSFTNSDMQI LTASGDGTCA LWDVESGQLL QSFHGHGADV
     LCLDLAPSET GNTFVSGGCD KKAMVWDMRS GQCVQAFETH ESDINSVRYY PSGDAFASGS
     DDATCRLYDL RADREVAIYS KESIIFGASS VDFSLSGRLL FAGYNDYTIN VWDVLKGSRV
     SILFGHENRV STLRVSPDGT AFCSGSWDHT LRVWA
//