Full text data of GNB2
GNB2
[Confidence: high (present in two of the MS resources)]
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2 (G protein subunit beta-2; Transducin beta chain 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2 (G protein subunit beta-2; Transducin beta chain 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00003348
IPI00003348 Guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 2 membrane 2 n/a n/a n/a n/a 1 2 n/a 3 n/a n/a n/a n/a n/a 1 n/a n/a 6 3 2 inner surface of plasma membrane n/a found at its expected molecular weight found at molecular weight
IPI00003348 Guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 2 Guanine nucleotide-binding protein G(I)/G(S)/G(T) beta subunit 2 membrane 2 n/a n/a n/a n/a 1 2 n/a 3 n/a n/a n/a n/a n/a 1 n/a n/a 6 3 2 inner surface of plasma membrane n/a found at its expected molecular weight found at molecular weight
UniProt
P62879
ID GBB2_HUMAN Reviewed; 340 AA.
AC P62879; P11016; P54312;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 111.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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].
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;
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:
RT analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci
RT reveals 17 genes.";
RL Genome Res. 8:1060-1073(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by 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].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-15 AND 58-78, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [7]
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
RT nucleotide exchange factor for RhoA and Rac1: regulation of cell shape
RT and reactive oxygen species production.";
RL Circ. Res. 93:848-856(2003).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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
RT Gbeta subunits.";
RL Cell. Physiol. Biochem. 23:1-8(2009).
RN [11]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC involved as a modulator or transducer in various transmembrane
CC signaling systems. The beta and gamma chains are required for the
CC GTPase activity, for replacement of GDP by GTP, and for G protein-
CC effector interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC gamma. Interacts with ARHGEF18 and RASD2. Interacts with ATXN10.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; BC010073; AAH10073.1; -; mRNA.
DR EMBL; BC012348; AAH12348.1; -; mRNA.
DR EMBL; BC068003; AAH68003.1; -; mRNA.
DR PIR; B26617; RGHUB2.
DR RefSeq; NP_005264.2; NM_005273.3.
DR UniGene; Hs.185172; -.
DR ProteinModelPortal; P62879; -.
DR SMR; P62879; 1-340.
DR IntAct; P62879; 25.
DR MINT; MINT-1139073; -.
DR STRING; 9606.ENSP00000305260; -.
DR PhosphoSite; P62879; -.
DR DMDM; 51317304; -.
DR OGP; P62879; -.
DR REPRODUCTION-2DPAGE; P62879; -.
DR PaxDb; P62879; -.
DR PRIDE; P62879; -.
DR DNASU; 2783; -.
DR Ensembl; ENST00000303210; ENSP00000305260; ENSG00000172354.
DR Ensembl; ENST00000393924; ENSP00000377501; ENSG00000172354.
DR Ensembl; ENST00000393926; ENSP00000377503; ENSG00000172354.
DR GeneID; 2783; -.
DR KEGG; hsa:2783; -.
DR UCSC; uc003uwb.3; human.
DR CTD; 2783; -.
DR GeneCards; GC07P100271; -.
DR HGNC; HGNC:4398; GNB2.
DR HPA; CAB010032; -.
DR HPA; HPA040736; -.
DR MIM; 139390; gene.
DR neXtProt; NX_P62879; -.
DR PharmGKB; PA28778; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000176356; -.
DR HOVERGEN; HBG000188; -.
DR InParanoid; P62879; -.
DR KO; K04537; -.
DR OMA; WDIETSQ; -.
DR OrthoDB; EOG7GN2N5; -.
DR PhylomeDB; P62879; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; P62879; -.
DR GeneWiki; GNB2; -.
DR GenomeRNAi; 2783; -.
DR NextBio; 10963; -.
DR PRO; PR:P62879; -.
DR ArrayExpress; P62879; -.
DR Bgee; P62879; -.
DR CleanEx; HS_GNB2; -.
DR Genevestigator; P62879; -.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
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; 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; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat; Transducer; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 340 Guanine nucleotide-binding protein
FT G(I)/G(S)/G(T) subunit beta-2.
FT /FTId=PRO_0000127695.
FT REPEAT 53 83 WD 1.
FT REPEAT 95 125 WD 2.
FT REPEAT 141 170 WD 3.
FT REPEAT 182 212 WD 4.
FT REPEAT 224 254 WD 5.
FT REPEAT 268 298 WD 6.
FT REPEAT 310 340 WD 7.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 239 239 Phosphotyrosine (By similarity).
FT CONFLICT 195 195 D -> N (in Ref. 2; AAA35922).
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
//
ID GBB2_HUMAN Reviewed; 340 AA.
AC P62879; P11016; P54312;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 111.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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].
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;
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:
RT analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci
RT reveals 17 genes.";
RL Genome Res. 8:1060-1073(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by 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].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-15 AND 58-78, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [7]
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
RT nucleotide exchange factor for RhoA and Rac1: regulation of cell shape
RT and reactive oxygen species production.";
RL Circ. Res. 93:848-856(2003).
RN [8]
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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
RT Gbeta subunits.";
RL Cell. Physiol. Biochem. 23:1-8(2009).
RN [11]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC involved as a modulator or transducer in various transmembrane
CC signaling systems. The beta and gamma chains are required for the
CC GTPase activity, for replacement of GDP by GTP, and for G protein-
CC effector interaction.
CC -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC gamma. Interacts with ARHGEF18 and RASD2. Interacts with ATXN10.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC -!- SIMILARITY: Contains 7 WD repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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; BC010073; AAH10073.1; -; mRNA.
DR EMBL; BC012348; AAH12348.1; -; mRNA.
DR EMBL; BC068003; AAH68003.1; -; mRNA.
DR PIR; B26617; RGHUB2.
DR RefSeq; NP_005264.2; NM_005273.3.
DR UniGene; Hs.185172; -.
DR ProteinModelPortal; P62879; -.
DR SMR; P62879; 1-340.
DR IntAct; P62879; 25.
DR MINT; MINT-1139073; -.
DR STRING; 9606.ENSP00000305260; -.
DR PhosphoSite; P62879; -.
DR DMDM; 51317304; -.
DR OGP; P62879; -.
DR REPRODUCTION-2DPAGE; P62879; -.
DR PaxDb; P62879; -.
DR PRIDE; P62879; -.
DR DNASU; 2783; -.
DR Ensembl; ENST00000303210; ENSP00000305260; ENSG00000172354.
DR Ensembl; ENST00000393924; ENSP00000377501; ENSG00000172354.
DR Ensembl; ENST00000393926; ENSP00000377503; ENSG00000172354.
DR GeneID; 2783; -.
DR KEGG; hsa:2783; -.
DR UCSC; uc003uwb.3; human.
DR CTD; 2783; -.
DR GeneCards; GC07P100271; -.
DR HGNC; HGNC:4398; GNB2.
DR HPA; CAB010032; -.
DR HPA; HPA040736; -.
DR MIM; 139390; gene.
DR neXtProt; NX_P62879; -.
DR PharmGKB; PA28778; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000176356; -.
DR HOVERGEN; HBG000188; -.
DR InParanoid; P62879; -.
DR KO; K04537; -.
DR OMA; WDIETSQ; -.
DR OrthoDB; EOG7GN2N5; -.
DR PhylomeDB; P62879; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_604; Hemostasis.
DR SignaLink; P62879; -.
DR GeneWiki; GNB2; -.
DR GenomeRNAi; 2783; -.
DR NextBio; 10963; -.
DR PRO; PR:P62879; -.
DR ArrayExpress; P62879; -.
DR Bgee; P62879; -.
DR CleanEx; HS_GNB2; -.
DR Genevestigator; P62879; -.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
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; 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; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat; Transducer; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 340 Guanine nucleotide-binding protein
FT G(I)/G(S)/G(T) subunit beta-2.
FT /FTId=PRO_0000127695.
FT REPEAT 53 83 WD 1.
FT REPEAT 95 125 WD 2.
FT REPEAT 141 170 WD 3.
FT REPEAT 182 212 WD 4.
FT REPEAT 224 254 WD 5.
FT REPEAT 268 298 WD 6.
FT REPEAT 310 340 WD 7.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 239 239 Phosphotyrosine (By similarity).
FT CONFLICT 195 195 D -> N (in Ref. 2; AAA35922).
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
//
MIM
139390
*RECORD*
*FIELD* NO
139390
*FIELD* TI
*139390 GUANINE NUCLEOTIDE-BINDING PROTEIN, BETA-2; GNB2
*FIELD* TX
DESCRIPTION
Heterotrimeric G proteins, made up of an alpha subunit (see GNAS,
read more139320), a beta subunit, like GNB2, and a gamma subunit (see GNG2,
606981), relay signals from cell surface receptors to internal
effectors. The alpha subunit is a GTPase that interacts in the GDP-bound
state with beta-gamma dimers (Rosskopf et al., 2003).
CLONING
Gao et al. (1987) isolated a cDNA that encodes a second form of the
beta-subunit of signal-transducing guanine nucleotide-binding regulatory
proteins (G proteins). The cDNA corresponded to a 1.8-kb mRNA, and
nucleotide sequence analysis indicated that the encoded polypeptide
consists of 340 amino acid residues with a molecular weight of 37,335.
Although the deduced polypeptide was found to be of the same size as
that reported previously for the beta subunit (beta-1), 10% of the amino
acid residues were different.
GENE FUNCTION
Peng et al. (1992) pointed out that although the alpha subunit shows
great diversity and is thought to confer functional specificity to a
particular G protein, the beta subunit, which is much less diverse, is
believed to have no role in G protein specificity. Using
immunocytochemistry, they found, however, distinct distribution patterns
for different beta and gamma subunits in the retina. In particular, rod
and cone photoreceptors, which both subserve phototransduction but
differ in light-response properties, have different beta and gamma
subunits in their outer segments. Thus, the G protein mediating
phototransduction shows cell-specific forms of the beta and gamma
subunits in addition to the alpha subunit. This surprising finding
supported the hypothesis that these subunits contribute to functional
specificity of the G protein.
Wolfe et al. (2003) demonstrated that inhibition of the alpha-1H
(Ca(v)3.2) (CACNA1H; 607904), but not alpha-1G (Ca(v)3.1) (CACNA1G;
604065), low voltage-activated calcium channels is mediated selectively
by G protein beta-2-gamma-2 subunits (GNB2 and GNG2) subunits that bind
to the intracellular loop connecting channel transmembrane domains II
and III. This region of the alpha-1H channel is crucial for inhibition,
because its replacement abrogates inhibition and its transfer to
nonmodulated alpha-1G channels confers beta-2-gamma-2-dependent
inhibition. Beta-gamma reduces channel activity independent of voltage,
a mechanism distinct from the established beta-gamma-dependent
inhibition of non-L-type high voltage-activated channels of the Ca(v)2
family. Wolfe et al. (2003) concluded that their studies identified the
alpha-1H channel as a new effector for G protein beta-gamma subunits,
and highlight the selective signaling roles available for particular
beta-gamma combinations.
GENE STRUCTURE
Rosskopf et al. (2003) determined that the GNB2 gene contains 10 exons.
The first exon is noncoding.
MAPPING
Blatt et al. (1988) assigned the GNB2 gene to human chromosome 7 by
hybridization of clones to DNA from somatic cell hybrids. By studying a
YAC containing the EPO gene (133170), Kere et al. (1991) demonstrated
that the GNB2 gene is located within 30 to 80 kb of EPO and most likely
centromeric of it. GNAI1 (139310) is located in the same area.
Lovett et al. (1991) developed a strategy for the rapid enrichment and
identification of cDNAs encoded by large genomic regions. The basis of
this 'direct selection' scheme was the hybridization of an entire
library of cDNAs to an immobilized genomic clone. The scheme was tested
using a 550-kb YAC clone that contained the EPO gene. Using this clone
and a fetal kidney cDNA library, they achieved a 1,000-fold enrichment
of EPO cDNAs in one cycle of enrichment. An anonymous cDNA encoded by
the YAC was greatly enriched and found to represent the GNB2 gene.
Restriction mapping located it within 30-70 kb of the EPO gene. Parimoo
et al. (1991) likewise developed a method of cDNA selection based on
hybridization of cDNA fragments to immobilized DNA and recovery of the
selected cDNAs by polymerase chain reaction (PCR). These methods address
the recurrent problem in genome mapping and positional cloning, namely,
identification of coding segments in large fragments of genomic DNA.
*FIELD* RF
1. Blatt, C.; Eversole-Cire, P.; Cohn, V. H.; Zollman, S.; Fournier,
R. E. K.; Mohandas, L. T.; Nesbitt, M.; Lugo, T.; Jones, D. T.; Reed,
R. R.; Weiner, L. P.; Sparkes, R. S.; Simon, M. I.: Chromosomal localization
of genes encoding guanine nucleotide-binding protein subunits in mouse
and human. Proc. Nat. Acad. Sci. 85: 7642-7646, 1988.
2. Gao, B.; Gilman, A. G.; Robishaw, J. D.: A second form of the
beta subunit of signal-transducing G proteins. Proc. Nat. Acad. Sci. 84:
6122-6125, 1987.
3. Kere, J.; Taillon-Miller, P.; Lovett, M.; de la Chapelle, A.; Donis-Keller,
H.: Construction of human chromosome 7 YAC contigs around the COL1A2
and EPO genes and mapping of the GNB2 gene. (Abstract) Cytogenet.
Cell Genet. 58: 1922-1923, 1991.
4. Lovett, M.; Kere, J.; Hinton, L. M.: Direct selection: a method
for the isolation of cDNAs encoded by large genomic regions. Proc.
Nat. Acad. Sci. 88: 9628-9632, 1991.
5. Parimoo, S.; Patanjali, S. R.; Shukla, H.; Chaplin, D. D.; Weissman,
S. M.: cDNA selection: efficient PCR approach for the selection of
cDNAs encoded in large chromosomal DNA fragments. Proc. Nat. Acad.
Sci. 88: 9623-9627, 1991.
6. Peng, Y.-W.; Robishaw, J. D.; Levine, M. A.; Yau, K.-W.: Retinal
rods and cones have distinct G protein beta and gamma subunits. Proc.
Nat. Acad. Sci. 89: 10882-10886, 1992.
7. Rosskopf, D.; Nikula, C.; Manthey, I.; Joisten, M.; Frey, U.; Kohnen,
S.; Siffert, W.: The human G protein beta-4 subunit: gene structure,
expression, G-gamma and effector interaction. FEBS Lett. 544: 27-32,
2003.
8. Wolfe, J. T.; Wang, H.; Howard, J.; Garrison, J. C.; Barrett, P.
Q.: T-type calcium channel regulation by specific G-protein beta-gamma
subunits. Nature 424: 209-213, 2003.
*FIELD* CN
Patricia A. Hartz - updated: 3/14/2007
Ada Hamosh - updated: 8/4/2003
*FIELD* CD
Victor A. McKusick: 9/29/1987
*FIELD* ED
wwang: 03/20/2007
terry: 3/14/2007
alopez: 8/6/2003
terry: 8/4/2003
alopez: 5/12/1998
mark: 6/10/1997
carol: 12/14/1992
supermim: 3/16/1992
carol: 2/22/1992
carol: 12/4/1991
carol: 8/8/1991
supermim: 3/20/1990
*RECORD*
*FIELD* NO
139390
*FIELD* TI
*139390 GUANINE NUCLEOTIDE-BINDING PROTEIN, BETA-2; GNB2
*FIELD* TX
DESCRIPTION
Heterotrimeric G proteins, made up of an alpha subunit (see GNAS,
read more139320), a beta subunit, like GNB2, and a gamma subunit (see GNG2,
606981), relay signals from cell surface receptors to internal
effectors. The alpha subunit is a GTPase that interacts in the GDP-bound
state with beta-gamma dimers (Rosskopf et al., 2003).
CLONING
Gao et al. (1987) isolated a cDNA that encodes a second form of the
beta-subunit of signal-transducing guanine nucleotide-binding regulatory
proteins (G proteins). The cDNA corresponded to a 1.8-kb mRNA, and
nucleotide sequence analysis indicated that the encoded polypeptide
consists of 340 amino acid residues with a molecular weight of 37,335.
Although the deduced polypeptide was found to be of the same size as
that reported previously for the beta subunit (beta-1), 10% of the amino
acid residues were different.
GENE FUNCTION
Peng et al. (1992) pointed out that although the alpha subunit shows
great diversity and is thought to confer functional specificity to a
particular G protein, the beta subunit, which is much less diverse, is
believed to have no role in G protein specificity. Using
immunocytochemistry, they found, however, distinct distribution patterns
for different beta and gamma subunits in the retina. In particular, rod
and cone photoreceptors, which both subserve phototransduction but
differ in light-response properties, have different beta and gamma
subunits in their outer segments. Thus, the G protein mediating
phototransduction shows cell-specific forms of the beta and gamma
subunits in addition to the alpha subunit. This surprising finding
supported the hypothesis that these subunits contribute to functional
specificity of the G protein.
Wolfe et al. (2003) demonstrated that inhibition of the alpha-1H
(Ca(v)3.2) (CACNA1H; 607904), but not alpha-1G (Ca(v)3.1) (CACNA1G;
604065), low voltage-activated calcium channels is mediated selectively
by G protein beta-2-gamma-2 subunits (GNB2 and GNG2) subunits that bind
to the intracellular loop connecting channel transmembrane domains II
and III. This region of the alpha-1H channel is crucial for inhibition,
because its replacement abrogates inhibition and its transfer to
nonmodulated alpha-1G channels confers beta-2-gamma-2-dependent
inhibition. Beta-gamma reduces channel activity independent of voltage,
a mechanism distinct from the established beta-gamma-dependent
inhibition of non-L-type high voltage-activated channels of the Ca(v)2
family. Wolfe et al. (2003) concluded that their studies identified the
alpha-1H channel as a new effector for G protein beta-gamma subunits,
and highlight the selective signaling roles available for particular
beta-gamma combinations.
GENE STRUCTURE
Rosskopf et al. (2003) determined that the GNB2 gene contains 10 exons.
The first exon is noncoding.
MAPPING
Blatt et al. (1988) assigned the GNB2 gene to human chromosome 7 by
hybridization of clones to DNA from somatic cell hybrids. By studying a
YAC containing the EPO gene (133170), Kere et al. (1991) demonstrated
that the GNB2 gene is located within 30 to 80 kb of EPO and most likely
centromeric of it. GNAI1 (139310) is located in the same area.
Lovett et al. (1991) developed a strategy for the rapid enrichment and
identification of cDNAs encoded by large genomic regions. The basis of
this 'direct selection' scheme was the hybridization of an entire
library of cDNAs to an immobilized genomic clone. The scheme was tested
using a 550-kb YAC clone that contained the EPO gene. Using this clone
and a fetal kidney cDNA library, they achieved a 1,000-fold enrichment
of EPO cDNAs in one cycle of enrichment. An anonymous cDNA encoded by
the YAC was greatly enriched and found to represent the GNB2 gene.
Restriction mapping located it within 30-70 kb of the EPO gene. Parimoo
et al. (1991) likewise developed a method of cDNA selection based on
hybridization of cDNA fragments to immobilized DNA and recovery of the
selected cDNAs by polymerase chain reaction (PCR). These methods address
the recurrent problem in genome mapping and positional cloning, namely,
identification of coding segments in large fragments of genomic DNA.
*FIELD* RF
1. Blatt, C.; Eversole-Cire, P.; Cohn, V. H.; Zollman, S.; Fournier,
R. E. K.; Mohandas, L. T.; Nesbitt, M.; Lugo, T.; Jones, D. T.; Reed,
R. R.; Weiner, L. P.; Sparkes, R. S.; Simon, M. I.: Chromosomal localization
of genes encoding guanine nucleotide-binding protein subunits in mouse
and human. Proc. Nat. Acad. Sci. 85: 7642-7646, 1988.
2. Gao, B.; Gilman, A. G.; Robishaw, J. D.: A second form of the
beta subunit of signal-transducing G proteins. Proc. Nat. Acad. Sci. 84:
6122-6125, 1987.
3. Kere, J.; Taillon-Miller, P.; Lovett, M.; de la Chapelle, A.; Donis-Keller,
H.: Construction of human chromosome 7 YAC contigs around the COL1A2
and EPO genes and mapping of the GNB2 gene. (Abstract) Cytogenet.
Cell Genet. 58: 1922-1923, 1991.
4. Lovett, M.; Kere, J.; Hinton, L. M.: Direct selection: a method
for the isolation of cDNAs encoded by large genomic regions. Proc.
Nat. Acad. Sci. 88: 9628-9632, 1991.
5. Parimoo, S.; Patanjali, S. R.; Shukla, H.; Chaplin, D. D.; Weissman,
S. M.: cDNA selection: efficient PCR approach for the selection of
cDNAs encoded in large chromosomal DNA fragments. Proc. Nat. Acad.
Sci. 88: 9623-9627, 1991.
6. Peng, Y.-W.; Robishaw, J. D.; Levine, M. A.; Yau, K.-W.: Retinal
rods and cones have distinct G protein beta and gamma subunits. Proc.
Nat. Acad. Sci. 89: 10882-10886, 1992.
7. Rosskopf, D.; Nikula, C.; Manthey, I.; Joisten, M.; Frey, U.; Kohnen,
S.; Siffert, W.: The human G protein beta-4 subunit: gene structure,
expression, G-gamma and effector interaction. FEBS Lett. 544: 27-32,
2003.
8. Wolfe, J. T.; Wang, H.; Howard, J.; Garrison, J. C.; Barrett, P.
Q.: T-type calcium channel regulation by specific G-protein beta-gamma
subunits. Nature 424: 209-213, 2003.
*FIELD* CN
Patricia A. Hartz - updated: 3/14/2007
Ada Hamosh - updated: 8/4/2003
*FIELD* CD
Victor A. McKusick: 9/29/1987
*FIELD* ED
wwang: 03/20/2007
terry: 3/14/2007
alopez: 8/6/2003
terry: 8/4/2003
alopez: 5/12/1998
mark: 6/10/1997
carol: 12/14/1992
supermim: 3/16/1992
carol: 2/22/1992
carol: 12/4/1991
carol: 8/8/1991
supermim: 3/20/1990