GBB2_HUMAN
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 03-AUG-2022, entry version 181.
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; 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; 312.
DR CORUM; P62879; -.
DR IntAct; P62879; 169.
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; P62879; -.
DR PeptideAtlas; P62879; -.
DR PRIDE; P62879; -.
DR ProteomicsDB; 3536; -.
DR ProteomicsDB; 57444; -. [P62879-1]
DR TopDownProteomics; P62879-1; -. [P62879-1]
DR Antibodypedia; 4100; 204 antibodies from 32 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 CTD; 2783; -.
DR DisGeNET; 2783; -.
DR GeneCards; GNB2; -.
DR HGNC; HGNC:4398; GNB2.
DR HPA; ENSG00000172354; Low tissue specificity.
DR MIM; 139390; gene.
DR MIM; 619464; phenotype.
DR MIM; 619503; phenotype.
DR neXtProt; NX_P62879; -.
DR OpenTargets; ENSG00000172354; -.
DR PharmGKB; PA28778; -.
DR VEuPathDB; HostDB:ENSG00000172354; -.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR InParanoid; P62879; -.
DR OMA; HVWDTLR; -.
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; 58 hits in 1078 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 196 other tissues.
DR ExpressionAtlas; P62879; baseline and differential.
DR Genevisible; P62879; HS.
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 Gene3D; 2.130.10.10; -; 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; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19850; PTHR19850; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00319; GPROTEINB.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
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
