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GBB2_BOVIN
ID   GBB2_BOVIN              Reviewed;         340 AA.
AC   P11017; A5D7A9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 3.
DT   03-AUG-2022, entry version 164.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 15-340.
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 102-316.
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).
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   -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC       {ECO:0000305}.
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DR   EMBL; BC140489; AAI40490.1; -; mRNA.
DR   EMBL; M16480; AAA30553.1; -; mRNA.
DR   EMBL; M36431; AAA62717.1; -; mRNA.
DR   EMBL; M16539; AAA30552.1; -; mRNA.
DR   PIR; A26617; RGBOB2.
DR   RefSeq; NP_001091030.1; NM_001097561.1.
DR   AlphaFoldDB; P11017; -.
DR   SMR; P11017; -.
DR   STRING; 9913.ENSBTAP00000008508; -.
DR   PaxDb; P11017; -.
DR   PeptideAtlas; P11017; -.
DR   PRIDE; P11017; -.
DR   Ensembl; ENSBTAT00000008508; ENSBTAP00000008508; ENSBTAG00000006495.
DR   GeneID; 281202; -.
DR   KEGG; bta:281202; -.
DR   CTD; 2783; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006495; -.
DR   VGNC; VGNC:29459; GNB2.
DR   eggNOG; KOG0286; Eukaryota.
DR   GeneTree; ENSGT01000000214413; -.
DR   HOGENOM; CLU_000288_57_34_1; -.
DR   InParanoid; P11017; -.
DR   OMA; HVWDTLR; -.
DR   OrthoDB; 704786at2759; -.
DR   TreeFam; TF106149; -.
DR   Reactome; R-BTA-392170; ADP signalling through P2Y purinoceptor 12.
DR   Reactome; R-BTA-392451; G beta:gamma signalling through PI3Kgamma.
DR   Reactome; R-BTA-416476; G alpha (q) signalling events.
DR   Reactome; R-BTA-418594; G alpha (i) signalling events.
DR   Reactome; R-BTA-418597; G alpha (z) signalling events.
DR   Reactome; R-BTA-428930; Thromboxane signalling through TP receptor.
DR   Reactome; R-BTA-456926; Thrombin signalling through proteinase activated receptors (PARs).
DR   Reactome; R-BTA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Proteomes; UP000009136; Chromosome 25.
DR   Bgee; ENSBTAG00000006495; Expressed in granulosa cell and 106 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR   GO; GO:0051020; F:GTPase binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
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   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   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW   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_0000127694"
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:0000250|UniProtKB:P62880"
FT   CONFLICT        285
FT                   /note="L -> V (in Ref. 3; AAA30552)"
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
 
 
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