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Protein

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Gene

GNB1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiREACT_271820. Thrombin signalling through proteinase activated receptors (PARs).
REACT_273525. ADP signalling through P2Y purinoceptor 1.
REACT_275792. Activation of G protein gated Potassium channels.
REACT_277683. G beta:gamma signalling through PLC beta.
REACT_287476. G alpha (q) signalling events.
REACT_288300. ADP signalling through P2Y purinoceptor 12.
REACT_292261. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_301171. G beta:gamma signalling through PI3Kgamma.
REACT_308557. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_310840. G alpha (z) signalling events.
REACT_312085. Olfactory Signaling Pathway.
REACT_320823. Prostacyclin signalling through prostacyclin receptor.
REACT_324896. G alpha (12/13) signalling events.
REACT_330097. G alpha (s) signalling events.
REACT_335730. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_337905. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_338486. G alpha (i) signalling events.
REACT_338991. Presynaptic function of Kainate receptors.
REACT_340577. Glucagon signaling in metabolic regulation.
REACT_342659. Ca2+ pathway.
REACT_344180. G-protein activation.
REACT_344521. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_347133. Thromboxane signalling through TP receptor.
REACT_347702. Glucagon-type ligand receptors.
REACT_352038. Activation of the phototransduction cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
Alternative name(s):
Transducin beta chain 1
Gene namesi
Name:GNB1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 16

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: Ensembl
  • heterotrimeric G-protein complex Source: BHF-UCL
  • intracellular Source: BHF-UCL
  • lysosomal membrane Source: Ensembl
  • membrane Source: BHF-UCL
  • myelin sheath Source: Ensembl
  • photoreceptor disc membrane Source: Reactome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 340339Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1PRO_0000127684Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei266 – 2661Phosphohistidine1 Publication

Post-translational modificationi

Phosphorylation at His-266 by NDKB contributes to G protein activation by increasing the high energetic phosphate transfer onto GDP.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP62871.
PRIDEiP62871.

Expressioni

Gene expression databases

ExpressionAtlasiP62871. baseline.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
NME2Q3T0Q43EBI-357141,EBI-8577979

Protein-protein interaction databases

BioGridi158560. 5 interactions.
DIPiDIP-29227N.
IntActiP62871. 5 interactions.
MINTiMINT-1864875.
STRINGi9913.ENSBTAP00000042481.

Structurei

Secondary structure

1
340
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2422Combined sources
Helixi30 – 334Combined sources
Turni34 – 363Combined sources
Beta strandi47 – 515Combined sources
Beta strandi58 – 636Combined sources
Beta strandi67 – 748Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 836Combined sources
Turni84 – 863Combined sources
Beta strandi89 – 946Combined sources
Beta strandi96 – 983Combined sources
Beta strandi100 – 1056Combined sources
Beta strandi109 – 1168Combined sources
Beta strandi120 – 1256Combined sources
Turni126 – 1283Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi134 – 1407Combined sources
Beta strandi146 – 1538Combined sources
Beta strandi156 – 1616Combined sources
Beta strandi166 – 1705Combined sources
Turni171 – 1744Combined sources
Beta strandi175 – 1806Combined sources
Beta strandi187 – 1926Combined sources
Beta strandi196 – 2038Combined sources
Beta strandi208 – 2125Combined sources
Turni213 – 2153Combined sources
Beta strandi217 – 2226Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi238 – 2458Combined sources
Beta strandi250 – 2545Combined sources
Turni255 – 2584Combined sources
Beta strandi259 – 2646Combined sources
Beta strandi273 – 2786Combined sources
Beta strandi282 – 2898Combined sources
Beta strandi292 – 2987Combined sources
Turni299 – 3013Combined sources
Beta strandi304 – 3096Combined sources
Beta strandi315 – 3206Combined sources
Beta strandi327 – 3315Combined sources
Beta strandi336 – 3394Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP62871.
SMRiP62871. Positions 2-340.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62871.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati53 – 8331WD 1Add
BLAST
Repeati95 – 12531WD 2Add
BLAST
Repeati141 – 17030WD 3Add
BLAST
Repeati182 – 21231WD 4Add
BLAST
Repeati224 – 25431WD 5Add
BLAST
Repeati268 – 29831WD 6Add
BLAST
Repeati310 – 34031WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat G protein beta family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119239.
HOGENOMiHOG000176356.
HOVERGENiHBG000188.
InParanoidiP62871.
KOiK04536.
OMAiRIVMRPR.
OrthoDBiEOG7GN2N5.
TreeFamiTF106149.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. 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]
PANTHERiPTHR19850. PTHR19850. 1 hit.
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62871-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT
60 70 80 90 100
LRGHLAKIYA MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV
110 120 130 140 150
MTCAYAPSGN YVACGGLDNI CSIYNLKTRE GNVRVSRELA GHTGYLSCCR
160 170 180 190 200
FLDDNQIVTS SGDTTCALWD IETGQQTTTF TGHTGDVMSL SLAPDTRLFV
210 220 230 240 250
SGACDASAKL WDVREGMCRQ TFTGHESDIN AICFFPNGNA FATGSDDATC
260 270 280 290 300
RLFDLRADQE LMTYSHDNII CGITSVSFSK SGRLLLAGYD DFNCNVWDAL
310 320 330 340
KADRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN
Length:340
Mass (Da):37,377
Last modified:January 23, 2007 - v3
Checksum:i896CBD32D2686598
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711V → L in CAA26875 (PubMed:2414128).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03073 mRNA. Translation: CAA26875.1.
M13236 mRNA. Translation: AAA30792.1.
BC105260 mRNA. Translation: AAI05261.1.
PIRiA24225. RGBOB1.
RefSeqiNP_786971.2. NM_175777.3.
XP_005217074.1. XM_005217017.1.
XP_010811610.1. XM_010813308.1.
UniGeneiBt.57702.

Genome annotation databases

EnsembliENSBTAT00000000259; ENSBTAP00000000259; ENSBTAG00000000215.
ENSBTAT00000045065; ENSBTAP00000042481; ENSBTAG00000000215.
GeneIDi281201.
KEGGibta:281201.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03073 mRNA. Translation: CAA26875.1.
M13236 mRNA. Translation: AAA30792.1.
BC105260 mRNA. Translation: AAI05261.1.
PIRiA24225. RGBOB1.
RefSeqiNP_786971.2. NM_175777.3.
XP_005217074.1. XM_005217017.1.
XP_010811610.1. XM_010813308.1.
UniGeneiBt.57702.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP62871.
SMRiP62871. Positions 2-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi158560. 5 interactions.
DIPiDIP-29227N.
IntActiP62871. 5 interactions.
MINTiMINT-1864875.
STRINGi9913.ENSBTAP00000042481.

Proteomic databases

PaxDbiP62871.
PRIDEiP62871.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000259; ENSBTAP00000000259; ENSBTAG00000000215.
ENSBTAT00000045065; ENSBTAP00000042481; ENSBTAG00000000215.
GeneIDi281201.
KEGGibta:281201.

Organism-specific databases

CTDi2782.

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119239.
HOGENOMiHOG000176356.
HOVERGENiHBG000188.
InParanoidiP62871.
KOiK04536.
OMAiRIVMRPR.
OrthoDBiEOG7GN2N5.
TreeFamiTF106149.

Enzyme and pathway databases

ReactomeiREACT_271820. Thrombin signalling through proteinase activated receptors (PARs).
REACT_273525. ADP signalling through P2Y purinoceptor 1.
REACT_275792. Activation of G protein gated Potassium channels.
REACT_277683. G beta:gamma signalling through PLC beta.
REACT_287476. G alpha (q) signalling events.
REACT_288300. ADP signalling through P2Y purinoceptor 12.
REACT_292261. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
REACT_301171. G beta:gamma signalling through PI3Kgamma.
REACT_308557. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_310840. G alpha (z) signalling events.
REACT_312085. Olfactory Signaling Pathway.
REACT_320823. Prostacyclin signalling through prostacyclin receptor.
REACT_324896. G alpha (12/13) signalling events.
REACT_330097. G alpha (s) signalling events.
REACT_335730. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_337905. Vasopressin regulates renal water homeostasis via Aquaporins.
REACT_338486. G alpha (i) signalling events.
REACT_338991. Presynaptic function of Kainate receptors.
REACT_340577. Glucagon signaling in metabolic regulation.
REACT_342659. Ca2+ pathway.
REACT_344180. G-protein activation.
REACT_344521. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_347133. Thromboxane signalling through TP receptor.
REACT_347702. Glucagon-type ligand receptors.
REACT_352038. Activation of the phototransduction cascade.

Miscellaneous databases

EvolutionaryTraceiP62871.
NextBioi20805257.
PROiP62871.

Gene expression databases

ExpressionAtlasiP62871. baseline.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. 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]
PANTHERiPTHR19850. PTHR19850. 1 hit.
PfamiPF00400. WD40. 7 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiGBB1_BOVIN
AccessioniPrimary (citable) accession number: P62871
Secondary accession number(s): P04697, P04901, Q3MHF1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.