GBB1_CRIGR
ID GBB1_CRIGR Reviewed; 340 AA.
AC Q6TMK6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 29-SEP-2021, entry version 83.
DE RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1;
DE AltName: Full=Transducin beta chain 1;
GN Name=GNB1;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Guang L., Shibuya M., Yoshiro M.;
RT "Differential display analysis of BCR/ABL-regulated genes.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). The heterodimer formed by GNB1 and GNG2 interacts with
CC ARHGEF5 (By similarity). The heterodimer formed by GNB1 and GNG2
CC interacts with GRK2 (By similarity). Interacts with ARHGEF18 and RASD2
CC (By similarity). {ECO:0000250|UniProtKB:P62871,
CC ECO:0000250|UniProtKB:P62873}.
CC -!- PTM: Phosphorylation at His-266 by NDKB contributes to G protein
CC activation by increasing the high energetic phosphate transfer onto
CC GDP. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC {ECO:0000305}.
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DR EMBL; AY392427; AAQ94086.1; -; mRNA.
DR RefSeq; NP_001233630.1; NM_001246701.1.
DR BioGRID; 1614024; 1.
DR STRING; 10029.NP_001233630.1; -.
DR PRIDE; Q6TMK6; -.
DR GeneID; 100689442; -.
DR KEGG; cge:100689442; -.
DR CTD; 2782; -.
DR eggNOG; KOG0286; Eukaryota.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
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; Phosphoprotein; Repeat; Transducer; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62873"
FT CHAIN 2..340
FT /note="Guanine nucleotide-binding protein G(I)/G(S)/G(T)
FT subunit beta-1"
FT /id="PRO_0000127686"
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:P62873"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62873"
FT MOD_RES 266
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P62871"
SQ SEQUENCE 340 AA; 37418 MW; 603D4165D059C37C CRC64;
MSELDQLRQE AEQLKNQIRD ARKACADATL SXITTNIDPV GRIQMRTRRT LRGHLAKIYA
MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN YVACGGLDNI
CSIYNLKTRE GNVRVSRELA GHTGYLSCCR FLNDNQIVTS SEDTTCALWD IETGQQTTTF
TGHTGDVMSL SLAPDTRLFV SGACDASAKL WDVREGMCRQ TFTGHESDIN AICFFPNGNA
FATGSDDATC RLFDLRADQE LMTYSHDNII CGITSVSFSK SGRLLLAGYD DFNCNVWDAL
KADRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN