ID GBB2_MOUSE Reviewed; 340 AA.
AC P62880; P11016; P54312;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 172.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/Kaplan;
RA Kuroda S., Tokunaga C., Konishi H., Kikkawa U.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=11913780; DOI=10.3109/10425170109084458;
RA Kitanaka J., Wang X., Kitanaka N., Hembree C.M., Uhl G.R.;
RT "Genomic organization of the murine G protein beta subunit genes and
RT related processed pseudogenes.";
RL DNA Seq. 12:345-354(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, and Embryo;
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 [5]
RP PROTEIN SEQUENCE OF 23-42; 58-96; 138-150; 198-209; 257-280 AND 284-301,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 182-297, AND DEVELOPMENTAL STAGE.
RC STRAIN=CF-1;
RX PubMed=8858601;
RX DOI=10.1002/(sici)1098-2795(199607)44:3<315::aid-mrd5>3.0.co;2-p;
RA Williams C.J., Schultz R.M., Kopf G.S.;
RT "G protein gene expression during mouse oocyte growth and maturation, and
RT preimplantation embryo development.";
RL Mol. Reprod. Dev. 44:315-323(1996).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). Interacts
CC with ARHGEF18 and RASD2. Interacts with ATXN10. Interacts with SCN8A.
CC {ECO:0000250|UniProtKB:P62879}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P62879}. Cell membrane
CC {ECO:0000250|UniProtKB:P62879}.
CC -!- DEVELOPMENTAL STAGE: Expressed in meiotically incompetent oocytes.
CC Expression increases in fully grown meiotically competent oocytes.
CC Expression then decreases during metaphase-II arrested eggs, one-cell
CC embryo, two-cell embryo and eight-cell embryo stages, and increases
CC again during blastocyst stage. {ECO:0000269|PubMed:8858601}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; U34960; AAC72250.1; -; mRNA.
DR EMBL; AB045007; BAB19816.1; -; Genomic_DNA.
DR EMBL; AF312033; AAK28828.1; -; Genomic_DNA.
DR EMBL; BC029077; AAH29077.1; -; mRNA.
DR EMBL; BC059942; AAH59942.1; -; mRNA.
DR EMBL; BC062178; AAH62178.1; -; mRNA.
DR EMBL; U38505; AAB01736.1; -; mRNA.
DR CCDS; CCDS19769.1; -.
DR RefSeq; NP_034442.1; NM_010312.4.
DR RefSeq; XP_006504616.1; XM_006504553.3.
DR AlphaFoldDB; P62880; -.
DR SMR; P62880; -.
DR BioGRID; 199977; 31.
DR IntAct; P62880; 8.
DR MINT; P62880; -.
DR STRING; 10090.ENSMUSP00000031726; -.
DR GlyGen; P62880; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62880; -.
DR PhosphoSitePlus; P62880; -.
DR SwissPalm; P62880; -.
DR REPRODUCTION-2DPAGE; IPI00162780; -.
DR EPD; P62880; -.
DR jPOST; P62880; -.
DR PaxDb; 10090-ENSMUSP00000031726; -.
DR PeptideAtlas; P62880; -.
DR ProteomicsDB; 273416; -.
DR Pumba; P62880; -.
DR Antibodypedia; 4100; 235 antibodies from 33 providers.
DR DNASU; 14693; -.
DR Ensembl; ENSMUST00000031726.15; ENSMUSP00000031726.9; ENSMUSG00000029713.16.
DR Ensembl; ENSMUST00000150063.9; ENSMUSP00000129353.2; ENSMUSG00000029713.16.
DR GeneID; 14693; -.
DR KEGG; mmu:14693; -.
DR UCSC; uc009act.1; mouse.
DR AGR; MGI:95784; -.
DR CTD; 2783; -.
DR MGI; MGI:95784; Gnb2.
DR VEuPathDB; HostDB:ENSMUSG00000029713; -.
DR eggNOG; KOG0286; Eukaryota.
DR GeneTree; ENSGT01000000214413; -.
DR InParanoid; P62880; -.
DR OrthoDB; 102097at2759; -.
DR PhylomeDB; P62880; -.
DR TreeFam; TF106149; -.
DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-MMU-202040; G-protein activation.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-MMU-392170; ADP signalling through P2Y purinoceptor 12.
DR Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
DR Reactome; R-MMU-392851; Prostacyclin signalling through prostacyclin receptor.
DR Reactome; R-MMU-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-MMU-4086398; Ca2+ pathway.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-418217; G beta:gamma signalling through PLC beta.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-418597; G alpha (z) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR Reactome; R-MMU-428930; Thromboxane signalling through TP receptor.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR Reactome; R-MMU-500657; Presynaptic function of Kainate receptors.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR Reactome; R-MMU-8964315; G beta:gamma signalling through BTK.
DR Reactome; R-MMU-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-MMU-9634597; GPER1 signaling.
DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 14693; 9 hits in 79 CRISPR screens.
DR ChiTaRS; Gnb2; mouse.
DR PRO; PR:P62880; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P62880; Protein.
DR Bgee; ENSMUSG00000029713; Expressed in granulocyte and 66 other cell types or tissues.
DR ExpressionAtlas; P62880; baseline and differential.
DR Genevisible; P62880; MM.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO: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; ISS: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.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transducer; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62879"
FT CHAIN 2..340
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(T)
FT subunit beta-2"
FT /id="PRO_0000127696"
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:0000250|UniProtKB:P62879"
FT MOD_RES 239
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT CONFLICT 106
FT /note="A -> G (in Ref. 1; AAC72250)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> S (in Ref. 1; AAC72250)"
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
//
