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P62871 (GBB1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Alternative name(s):
Transducin beta chain 1
Gene names
Name:GNB1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

Subunit structure

G proteins are composed of 3 units, alpha, beta and gamma. Interacts with ARHGEF18 and RASD2. The heterodimer formed by GNB1 and GNG2 interacts with PTH1R (via C-terminus) By similarity.

Post-translational modification

Phosphorylation at His-266 by NDKB contributes to G protein activation by increasing the high energetic phosphate transfer onto GDP.

Sequence similarities

Belongs to the WD repeat G protein beta family.

Contains 7 WD repeats.

Ontologies

Keywords
   DomainRepeat
WD repeat
   Molecular functionTransducer
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-activating dopamine receptor signaling pathway

Inferred from direct assay PubMed 18403039. Source: BHF-UCL

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to catecholamine stimulus

Inferred from direct assay PubMed 18403039. Source: BHF-UCL

cellular response to prostaglandin E stimulus

Inferred from direct assay PubMed 18403039. Source: BHF-UCL

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

sensory perception of taste

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentheterotrimeric G-protein complex

Inferred from direct assay PubMed 18403039. Source: BHF-UCL

intracellular

Inferred from direct assay PubMed 18403039. Source: BHF-UCL

lysosomal membrane

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 18403039. Source: BHF-UCL

photoreceptor disc membrane

Traceable author statement. Source: Reactome

   Molecular_functionGTPase activity

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.4. Source: IntAct

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NME2Q3T0Q43EBI-357141,EBI-8577979

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 340339Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
PRO_0000127684

Regions

Repeat53 – 8331WD 1
Repeat95 – 12531WD 2
Repeat141 – 17030WD 3
Repeat182 – 21231WD 4
Repeat224 – 25431WD 5
Repeat268 – 29831WD 6
Repeat310 – 34031WD 7

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue2661Phosphohistidine Ref.4

Experimental info

Sequence conflict711V → L in CAA26875. Ref.2

Secondary structure

...................................................................... 340
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62871 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 896CBD32D2686598

FASTA34037,377
        10         20         30         40         50         60 
MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA 

        70         80         90        100        110        120 
MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN YVACGGLDNI 

       130        140        150        160        170        180 
CSIYNLKTRE GNVRVSRELA GHTGYLSCCR FLDDNQIVTS SGDTTCALWD IETGQQTTTF 

       190        200        210        220        230        240 
TGHTGDVMSL SLAPDTRLFV SGACDASAKL WDVREGMCRQ TFTGHESDIN AICFFPNGNA 

       250        260        270        280        290        300 
FATGSDDATC RLFDLRADQE LMTYSHDNII CGITSVSFSK SGRLLLAGYD DFNCNVWDAL 

       310        320        330        340 
KADRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN 

« Hide

References

« Hide 'large scale' references
[1]"Repetitive segmental structure of the transducin beta subunit: homology with the CDC4 gene and identification of related mRNAs."
Fong H.K.W., Hurley J.B., Hopkins R.S., Miake-Lye R., Johnson M.S., Doolittle R.F., Simon M.I.
Proc. Natl. Acad. Sci. U.S.A. 83:2162-2166(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Primary structure of the beta-subunit of bovine transducin deduced from the cDNA sequence."
Sugimoto K., Nukada T., Tanabe T., Takahashi H., Noda M., Minamino N., Kangawa K., Matsuo H., Hirose T., Inayama S., Numa S.
FEBS Lett. 191:235-240(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Ascending colon.
[4]"Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gbeta subunits. Complex formation of NDPK B with Gbeta gamma dimers and phosphorylation of His-266 IN Gbeta."
Cuello F., Schulze R.A., Heemeyer F., Meyer H.E., Lutz S., Jakobs K.H., Niroomand F., Wieland T.
J. Biol. Chem. 278:7220-7226(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT HIS-266.
[5]"The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2."
Wall M.A., Coleman D.E., Lee E., Iniguez-Lluhi J.A., Posner B.A., Gilman A.G., Sprang S.R.
Cell 83:1047-1058(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF HETEROTRIMER.
[6]"Crystal structure of a G-protein beta gamma dimer at 2.1-A resolution."
Sondek J., Bohm A., Lambright D.G., Hamm H.E., Sigler P.B.
Nature 379:369-374(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF BETA-GAMMA DIMER.
[7]"Phosducin induces a structural change in transducin beta gamma."
Loew A., Ho Y.K., Blundell T., Bax B.
Structure 6:1007-1019(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF COMPLEX WITH PHOSDUCIN.
[8]"Keeping G proteins at bay: a complex between G protein-coupled receptor kinase 2 and Gbetagamma."
Lodowski D.T., Pitcher J.A., Capel W.D., Lefkowitz R.J., Tesmer J.J.
Science 300:1256-1262(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH ADRBK1 AND GNG2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03073 mRNA. Translation: CAA26875.1.
M13236 mRNA. Translation: AAA30792.1.
BC105260 mRNA. Translation: AAI05261.1.
PIRRGBOB1. A24225.
RefSeqNP_786971.2. NM_175777.3.
XP_005217074.1. XM_005217017.1.
UniGeneBt.57702.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0RX-ray2.80B2-340[»]
1B9XX-ray3.00A1-340[»]
1B9YX-ray3.00A1-340[»]
1GG2X-ray2.40B1-340[»]
1GOTX-ray2.00B1-340[»]
1GP2X-ray2.30B1-340[»]
1OMWX-ray2.50B1-340[»]
1TBGX-ray2.10A/B/C/D1-340[»]
1XHMX-ray2.70A1-340[»]
2BCJX-ray3.06B2-340[»]
2TRCX-ray2.40B1-340[»]
3AH8X-ray2.90B1-340[»]
3CIKX-ray2.75B1-340[»]
3KRWX-ray2.90B1-340[»]
3KRXX-ray3.10B1-340[»]
3PSCX-ray2.67B1-340[»]
3PVUX-ray2.48B1-340[»]
3PVWX-ray2.49B1-340[»]
3UZSX-ray4.52B1-340[»]
3V5WX-ray2.07B1-340[»]
4MK0X-ray2.40B2-340[»]
ProteinModelPortalP62871.
SMRP62871. Positions 2-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid158560. 5 interactions.
DIPDIP-29227N.
IntActP62871. 5 interactions.
MINTMINT-1864875.

Proteomic databases

PaxDbP62871.
PRIDEP62871.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000000259; ENSBTAP00000000259; ENSBTAG00000000215.
ENSBTAT00000045065; ENSBTAP00000042481; ENSBTAG00000000215.
GeneID281201.
KEGGbta:281201.

Organism-specific databases

CTD2782.

Phylogenomic databases

eggNOGCOG2319.
GeneTreeENSGT00740000115196.
HOGENOMHOG000176356.
HOVERGENHBG000188.
InParanoidP62871.
KOK04536.
OMARIVMRPR.
OrthoDBEOG7GN2N5.
TreeFamTF106149.

Enzyme and pathway databases

ReactomeREACT_207087. Disease.
REACT_214353. Signal Transduction.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR001632. Gprotein_B.
IPR016346. Guanine_nucleotide-bd_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 7 hits.
[Graphical view]
PIRSFPIRSF002394. GN-bd_beta. 1 hit.
PRINTSPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP62871.
NextBio20805257.

Entry information

Entry nameGBB1_BOVIN
AccessionPrimary (citable) accession number: P62871
Secondary accession number(s): P04697, P04901, Q3MHF1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references