ID   GBB2_HUMAN              Reviewed;         340 AA.
AC   P62879; B3KPU1; P11016; P54312;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2;
DE   AltName: Full=G protein subunit beta-2;
DE   AltName: Full=Transducin beta chain 2;
GN   Name=GNB2;
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=3108879; DOI=10.1073/pnas.84.11.3792;
RA   Fong H.K.W., Amatruda T.T. III, Birren B.W., Simon M.I.;
RT   "Distinct forms of the beta subunit of GTP-binding regulatory proteins
RT   identified by molecular cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:3792-3796(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3114742; DOI=10.1073/pnas.84.17.6122;
RA   Gao B., Gilman A.G., Robishaw J.D.;
RT   "A second form of the beta subunit of signal-transducing G proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:6122-6125(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9799793; DOI=10.1101/gr.8.10.1060;
RA   Gloeckner G., Scherer S., Schattevoy R., Boright A.P., Weber J.,
RA   Tsui L.-C., Rosenthal A.;
RT   "Large-scale sequencing of two regions in human chromosome 7q22: analysis
RT   of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17
RT   genes.";
RL   Genome Res. 8:1060-1073(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreas, Skin, and Uterus;
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   PROTEIN SEQUENCE OF 2-15 AND 58-78, CLEAVAGE OF INITIATOR METHIONINE,
RP   ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RA   Bienvenut W.V.;
RL   Submitted (JUL-2005) to UniProtKB.
RN   [9]
RP   INTERACTION WITH ARHGEF18.
RX   PubMed=14512443; DOI=10.1161/01.res.0000097607.14733.0c;
RA   Niu J., Profirovic J., Pan H., Vaiskunaite R., Voyno-Yasenetskaya T.;
RT   "G Protein betagamma subunits stimulate p114RhoGEF, a guanine nucleotide
RT   exchange factor for RhoA and Rac1: regulation of cell shape and reactive
RT   oxygen species production.";
RL   Circ. Res. 93:848-856(2003).
RN   [10]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ATXN10.
RX   PubMed=16498633; DOI=10.1002/jnr.20807;
RA   Waragai M., Nagamitsu S., Xu W., Li Y.J., Lin X., Ashizawa T.;
RT   "Ataxin 10 induces neuritogenesis via interaction with G-protein beta2
RT   subunit.";
RL   J. Neurosci. Res. 83:1170-1178(2006).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   INTERACTION WITH RASD2.
RX   PubMed=19255495; DOI=10.1159/000204075;
RA   Hill C., Goddard A., Ladds G., Davey J.;
RT   "The cationic region of Rhes mediates its interactions with specific Gbeta
RT   subunits.";
RL   Cell. Physiol. Biochem. 23:1-8(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [15]
RP   INTERACTION WITH SCN8A.
RX   PubMed=26900580; DOI=10.1002/acn3.276;
RA   Wagnon J.L., Barker B.S., Hounshell J.A., Haaxma C.A., Shealy A., Moss T.,
RA   Parikh S., Messer R.D., Patel M.K., Meisler M.H.;
RT   "Pathogenic mechanism of recurrent mutations of SCN8A in epileptic
RT   encephalopathy.";
RL   Ann. Clin. Transl. Neurol. 3:114-123(2016).
RN   [16]
RP   INVOLVEMENT IN SSS4, VARIANT SSS4 LEU-52, CHARACTERIZATION OF VARIANT SSS4
RP   LEU-52, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP   GNAI2 AND GNG2.
RX   PubMed=28219978; DOI=10.1161/circresaha.116.310112;
RA   Stallmeyer B., Kuss J., Kotthoff S., Zumhagen S., Vowinkel K., Rinne S.,
RA   Matschke L.A., Friedrich C., Schulze-Bahr E., Rust S., Seebohm G.,
RA   Decher N., Schulze-Bahr E.;
RT   "A Mutation in the G-Protein Gene GNB2 Causes Familial Sinus Node and
RT   Atrioventricular Conduction Dysfunction.";
RL   Circ. Res. 120:e33-e44(2017).
RN   [17]
RP   INVOLVEMENT IN NEDHYDF, AND VARIANT NEDHYDF ARG-77.
RX   PubMed=31698099; DOI=10.1016/j.ejmg.2019.103804;
RA   Fukuda T., Hiraide T., Yamoto K., Nakashima M., Kawai T., Yanagi K.,
RA   Ogata T., Saitsu H.;
RT   "Exome reports A de novo GNB2 variant associated with global developmental
RT   delay, intellectual disability, and dysmorphic features.";
RL   Eur. J. Med. Genet. 63:103804-103804(2020).
RN   [18]
RP   INVOLVEMENT IN NEDHYDF, AND VARIANTS NEDHYDF THR-73; ARG-77; GLU-89; THR-89
RP   AND LEU-147.
RX   PubMed=34183358; DOI=10.1136/jmedgenet-2020-107462;
RA   Tan N.B., Pagnamenta A.T., Ferla M.P., Gadian J., Chung B.H., Chan M.C.,
RA   Fung J.L., Cook E., Guter S., Boschann F., Heinen A., Schallner J.,
RA   Mignot C., Keren B., Whalen S., Sarret C., Mittag D., Demmer L.,
RA   Stapleton R., Saida K., Matsumoto N., Miyake N., Sheffer R., Mor-Shaked H.,
RA   Barnett C.P., Byrne A.B., Scott H.S., Kraus A., Cappuccio G.,
RA   Brunetti-Pierri N., Iorio R., Di Dato F., Pais L.S., Yeung A., Tan T.Y.,
RA   Taylor J.C., Christodoulou J., White S.M.;
RT   "Recurrent de novo missense variants in GNB2 can cause syndromic
RT   intellectual disability.";
RL   J. Med. Genet. 59:511-516(2022).
RN   [19]
RP   INVOLVEMENT IN NEDHYDF, AND VARIANT NEDHYDF TRP-77.
RX   PubMed=33971351; DOI=10.1016/j.ejmg.2021.104243;
RA   Lansdon L.A., Fleming E.A., Viso F.D., Sullivan B.R., Saunders C.J.;
RT   "Second patient with GNB2-related neurodevelopmental disease: Further
RT   evidence for a gene-disease association.";
RL   Eur. J. Med. Genet. 64:104243-104243(2021).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as a modulator or transducer in various transmembrane signaling
CC       systems. The beta and gamma chains are required for the GTPase
CC       activity, for replacement of GDP by GTP, and for G protein-effector
CC       interaction.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and gamma. In
CC       this context, interacts with GNAI2 and GNG2 (PubMed:28219978).
CC       Interacts with ARHGEF18 and RASD2. Interacts with ATXN10. Interacts
CC       with SCN8A (PubMed:26900580). {ECO:0000269|PubMed:14512443,
CC       ECO:0000269|PubMed:16498633, ECO:0000269|PubMed:19255495,
CC       ECO:0000269|PubMed:26900580, ECO:0000269|PubMed:28219978}.
CC   -!- INTERACTION:
CC       P62879; Q9H0Y0: ATG10; NbExp=3; IntAct=EBI-356942, EBI-1048913;
CC       P62879; Q9NT62: ATG3; NbExp=3; IntAct=EBI-356942, EBI-988094;
CC       P62879; P13569: CFTR; NbExp=12; IntAct=EBI-356942, EBI-349854;
CC       P62879; P42858: HTT; NbExp=10; IntAct=EBI-356942, EBI-466029;
CC       P62879; O60260-5: PRKN; NbExp=3; IntAct=EBI-356942, EBI-21251460;
CC       P62879; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-356942, EBI-396669;
CC       P62879; P37840: SNCA; NbExp=3; IntAct=EBI-356942, EBI-985879;
CC       P62879; P00441: SOD1; NbExp=3; IntAct=EBI-356942, EBI-990792;
CC       P62879; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-356942, EBI-5235340;
CC       P62879; Q13148: TARDBP; NbExp=7; IntAct=EBI-356942, EBI-372899;
CC       P62879; O00762: UBE2C; NbExp=3; IntAct=EBI-356942, EBI-719691;
CC       P62879; P51668: UBE2D1; NbExp=3; IntAct=EBI-356942, EBI-743540;
CC       P62879; P62837: UBE2D2; NbExp=3; IntAct=EBI-356942, EBI-347677;
CC       P62879; P61077: UBE2D3; NbExp=3; IntAct=EBI-356942, EBI-348268;
CC       P62879; Q9Y2X8: UBE2D4; NbExp=3; IntAct=EBI-356942, EBI-745527;
CC       P62879; Q969M7: UBE2F; NbExp=3; IntAct=EBI-356942, EBI-1056876;
CC       P62879; P62253: UBE2G1; NbExp=3; IntAct=EBI-356942, EBI-2340619;
CC       P62879; P62256: UBE2H; NbExp=3; IntAct=EBI-356942, EBI-2129909;
CC       P62879; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-356942, EBI-10180829;
CC       P62879; Q8N2K1: UBE2J2; NbExp=3; IntAct=EBI-356942, EBI-2340110;
CC       P62879; P61086: UBE2K; NbExp=3; IntAct=EBI-356942, EBI-473850;
CC       P62879; O14933: UBE2L6; NbExp=3; IntAct=EBI-356942, EBI-2129974;
CC       P62879; P61081: UBE2M; NbExp=3; IntAct=EBI-356942, EBI-1041660;
CC       P62879; Q9C0C9: UBE2O; NbExp=6; IntAct=EBI-356942, EBI-2339946;
CC       P62879; Q7Z7E8-2: UBE2Q1; NbExp=3; IntAct=EBI-356942, EBI-10258181;
CC       P62879; Q8WVN8: UBE2Q2; NbExp=3; IntAct=EBI-356942, EBI-2130157;
CC       P62879; Q16763: UBE2S; NbExp=3; IntAct=EBI-356942, EBI-2339823;
CC       P62879; Q6NXQ4: UBE2S; NbExp=3; IntAct=EBI-356942, EBI-25859532;
CC       P62879; Q9NPD8: UBE2T; NbExp=3; IntAct=EBI-356942, EBI-2130165;
CC       P62879; Q5VVX9-2: UBE2U; NbExp=3; IntAct=EBI-356942, EBI-21897992;
CC       P62879; P40337-2: VHL; NbExp=3; IntAct=EBI-356942, EBI-12157263;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:16498633}. Cell membrane
CC       {ECO:0000269|PubMed:28219978}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P62879-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P62879-2; Sequence=VSP_056515;
CC   -!- TISSUE SPECIFICITY: Expressed in all cardiac subcompartments and in the
CC       brain, with highest levels in the atrioventricular node and brain.
CC       {ECO:0000269|PubMed:28219978}.
CC   -!- DISEASE: Neurodevelopmental disorder with hypotonia and dysmorphic
CC       facies (NEDHYDF) [MIM:619503]: An autosomal dominant disorder
CC       characterized by global developmental delay, hypotonia, and variably
CC       impaired intellectual development, often with speech delay and delayed
CC       walking. Most patients have dysmorphic facial features. Clinical
CC       features are highly variable and may include congenital cardiac
CC       defects, non-specific renal anomalies, joint contractures or joint
CC       hyperextensibility, dry skin, and cryptorchidism.
CC       {ECO:0000269|PubMed:31698099, ECO:0000269|PubMed:33971351,
CC       ECO:0000269|PubMed:34183358}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Sick sinus syndrome 4 (SSS4) [MIM:619464]: The term 'sick
CC       sinus syndrome' encompasses a variety of conditions caused by sinus
CC       node dysfunction. The most common clinical manifestations are syncope,
CC       presyncope, dizziness, and fatigue. Electrocardiogram typically shows
CC       sinus bradycardia, sinus arrest, and/or sinoatrial block. Episodes of
CC       atrial tachycardias coexisting with sinus bradycardia ('tachycardia-
CC       bradycardia syndrome') are also common in this disorder. SSS occurs
CC       most often in the elderly associated with underlying heart disease or
CC       previous cardiac surgery, but can also occur in the fetus, infant, or
CC       child without heart disease or other contributing factors. SSS4 is
CC       characterized by early and progressive sinus node and atrioventricular
CC       conduction dysfunction. Some affected individuals are asymptomatic.
CC       SSS4 inheritance is autosomal dominant. {ECO:0000269|PubMed:28219978}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC       {ECO:0000305}.
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DR   EMBL; M16514; AAA03179.1; -; mRNA.
DR   EMBL; M36429; AAA63264.1; -; mRNA.
DR   EMBL; M16538; AAA35922.1; -; mRNA.
DR   EMBL; AF053356; AAC78794.1; -; Genomic_DNA.
DR   EMBL; AF501883; AAM15919.1; -; mRNA.
DR   EMBL; AK056750; BAG51803.1; -; mRNA.
DR   EMBL; AC009488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC010073; AAH10073.1; -; mRNA.
DR   EMBL; BC012348; AAH12348.1; -; mRNA.
DR   EMBL; BC068003; AAH68003.1; -; mRNA.
DR   CCDS; CCDS5703.1; -. [P62879-1]
DR   PIR; B26617; RGHUB2.
DR   RefSeq; NP_005264.2; NM_005273.3. [P62879-1]
DR   AlphaFoldDB; P62879; -.
DR   SMR; P62879; -.
DR   BioGRID; 109045; 545.
DR   CORUM; P62879; -.
DR   IntAct; P62879; 171.
DR   MINT; P62879; -.
DR   STRING; 9606.ENSP00000305260; -.
DR   TCDB; 8.A.92.1.7; the g-protein AlphaBetaGama complex (gpc) family.
DR   GlyGen; P62879; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62879; -.
DR   PhosphoSitePlus; P62879; -.
DR   SwissPalm; P62879; -.
DR   BioMuta; GNB2; -.
DR   DMDM; 51317304; -.
DR   OGP; P62879; -.
DR   REPRODUCTION-2DPAGE; P62879; -.
DR   EPD; P62879; -.
DR   jPOST; P62879; -.
DR   MassIVE; P62879; -.
DR   MaxQB; P62879; -.
DR   PaxDb; 9606-ENSP00000305260; -.
DR   PeptideAtlas; P62879; -.
DR   PRIDE; P62879; -.
DR   ProteomicsDB; 3536; -.
DR   ProteomicsDB; 57444; -. [P62879-1]
DR   Pumba; P62879; -.
DR   TopDownProteomics; P62879-1; -. [P62879-1]
DR   Antibodypedia; 4100; 235 antibodies from 33 providers.
DR   DNASU; 2783; -.
DR   Ensembl; ENST00000303210.9; ENSP00000305260.4; ENSG00000172354.10. [P62879-1]
DR   Ensembl; ENST00000393924.1; ENSP00000377501.1; ENSG00000172354.10. [P62879-1]
DR   Ensembl; ENST00000393926.5; ENSP00000377503.1; ENSG00000172354.10. [P62879-1]
DR   Ensembl; ENST00000419828.5; ENSP00000390543.1; ENSG00000172354.10. [P62879-2]
DR   Ensembl; ENST00000427895.5; ENSP00000400286.1; ENSG00000172354.10. [P62879-2]
DR   GeneID; 2783; -.
DR   KEGG; hsa:2783; -.
DR   MANE-Select; ENST00000303210.9; ENSP00000305260.4; NM_005273.4; NP_005264.2.
DR   UCSC; uc064ggx.1; human. [P62879-1]
DR   AGR; HGNC:4398; -.
DR   CTD; 2783; -.
DR   DisGeNET; 2783; -.
DR   GeneCards; GNB2; -.
DR   HGNC; HGNC:4398; GNB2.
DR   HPA; ENSG00000172354; Low tissue specificity.
DR   MalaCards; GNB2; -.
DR   MIM; 139390; gene.
DR   MIM; 619464; phenotype.
DR   MIM; 619503; phenotype.
DR   neXtProt; NX_P62879; -.
DR   OpenTargets; ENSG00000172354; -.
DR   Orphanet; 166282; Familial sick sinus syndrome.
DR   Orphanet; 528084; Non-specific syndromic intellectual disability.
DR   PharmGKB; PA28778; -.
DR   VEuPathDB; HostDB:ENSG00000172354; -.
DR   eggNOG; KOG0286; Eukaryota.
DR   GeneTree; ENSGT01000000214413; -.
DR   InParanoid; P62879; -.
DR   OMA; HDDRISC; -.
DR   OrthoDB; 102097at2759; -.
DR   PhylomeDB; P62879; -.
DR   TreeFam; TF106149; -.
DR   PathwayCommons; P62879; -.
DR   Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR   Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
DR   Reactome; R-HSA-202040; G-protein activation.
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; P62879; -.
DR   SIGNOR; P62879; -.
DR   BioGRID-ORCS; 2783; 65 hits in 1156 CRISPR screens.
DR   ChiTaRS; GNB2; human.
DR   GeneWiki; GNB2; -.
DR   GenomeRNAi; 2783; -.
DR   Pharos; P62879; Tbio.
DR   PRO; PR:P62879; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; P62879; Protein.
DR   Bgee; ENSG00000172354; Expressed in lower esophagus mucosa and 198 other cell types or tissues.
DR   ExpressionAtlas; P62879; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR   GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR   GO; GO:0030159; F:signaling receptor complex adaptor activity; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IMP: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:SF27; GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)_G(S)_G(T) SUBUNIT BETA-2; 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; P62879; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW   Direct protein sequencing; Disease variant; Intellectual disability;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Transducer;
KW   WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT   CHAIN           2..340
FT                   /note="Guanine nucleotide-binding protein G(I)/G(S)/G(T)
FT                   subunit beta-2"
FT                   /id="PRO_0000127695"
FT   REPEAT          53..83
FT                   /note="WD 1"
FT   REPEAT          95..125
FT                   /note="WD 2"
FT   REPEAT          141..170
FT                   /note="WD 3"
FT   REPEAT          182..212
FT                   /note="WD 4"
FT   REPEAT          224..254
FT                   /note="WD 5"
FT   REPEAT          268..298
FT                   /note="WD 6"
FT   REPEAT          310..340
FT                   /note="WD 7"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330"
FT   MOD_RES         239
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P62880"
FT   VAR_SEQ         1..100
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056515"
FT   VARIANT         52
FT                   /note="R -> L (in SSS4; leads to a sustained activation of
FT                   cardiac G protein-coupled inwardly-rectifying potassium
FT                   (GIRK) channels, which is likely to hyperpolarize the
FT                   myocellular membrane potential and reduce their spontaneous
FT                   activity; does not affect protein levels, subcellular
FT                   location, nor interaction with GNAI2 and GNG2)"
FT                   /evidence="ECO:0000269|PubMed:28219978"
FT                   /id="VAR_086042"
FT   VARIANT         73
FT                   /note="A -> T (in NEDHYDF)"
FT                   /evidence="ECO:0000269|PubMed:34183358"
FT                   /id="VAR_086043"
FT   VARIANT         77
FT                   /note="G -> R (in NEDHYDF)"
FT                   /evidence="ECO:0000269|PubMed:31698099,
FT                   ECO:0000269|PubMed:34183358"
FT                   /id="VAR_086044"
FT   VARIANT         77
FT                   /note="G -> W (in NEDHYDF)"
FT                   /evidence="ECO:0000269|PubMed:33971351"
FT                   /id="VAR_086045"
FT   VARIANT         89
FT                   /note="K -> E (in NEDHYDF)"
FT                   /evidence="ECO:0000269|PubMed:34183358"
FT                   /id="VAR_086046"
FT   VARIANT         89
FT                   /note="K -> T (in NEDHYDF)"
FT                   /evidence="ECO:0000269|PubMed:34183358"
FT                   /id="VAR_086047"
FT   VARIANT         147
FT                   /note="S -> L (in NEDHYDF)"
FT                   /evidence="ECO:0000269|PubMed:34183358"
FT                   /id="VAR_086048"
FT   CONFLICT        195
FT                   /note="D -> N (in Ref. 2; AAA35922)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   340 AA;  37331 MW;  5D08FFA240ADEEE6 CRC64;
     MSELEQLRQE AEQLRNQIRD ARKACGDSTL TQITAGLDPV GRIQMRTRRT LRGHLAKIYA
     MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN FVACGGLDNI
     CSIYSLKTRE GNVRVSRELP GHTGYLSCCR FLDDNQIITS SGDTTCALWD IETGQQTVGF
     AGHSGDVMSL SLAPDGRTFV SGACDASIKL WDVRDSMCRQ TFIGHESDIN AVAFFPNGYA
     FTTGSDDATC RLFDLRADQE LLMYSHDNII CGITSVAFSR SGRLLLAGYD DFNCNIWDAM
     KGDRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN
//