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P62873 (GBB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Ref.16

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). Ref.11 Ref.13 Ref.16

Post-translational modification

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

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
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled acetylcholine receptor signaling pathway

Traceable author statement PubMed 8717044. Source: ProtInc

GTP catabolic process

Inferred from direct assay PubMed 1543505. Source: GOC

Ras protein signal transduction

Traceable author statement PubMed 8717044. Source: ProtInc

adenylate cyclase-activating dopamine receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

cardiac muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cellular response to catecholamine stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to glucagon stimulus

Traceable author statement. Source: Reactome

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cellular response to prostaglandin E stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

energy reserve metabolic process

Traceable author statement. Source: Reactome

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

phototransduction, visible light

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

regulation of rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

rhodopsin mediated signaling pathway

Traceable author statement. Source: Reactome

sensory perception of taste

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 7649993PubMed 8717044. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentcell body

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 20458337. Source: UniProt

heterotrimeric G-protein complex

Inferred from direct assay PubMed 1543505. Source: MGI

intracellular

Inferred from sequence or structural similarity. Source: BHF-UCL

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

photoreceptor disc membrane

Traceable author statement. Source: Reactome

photoreceptor inner segment

Inferred from electronic annotation. Source: Ensembl

photoreceptor outer segment membrane

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionGTPase activity

Inferred from direct assay PubMed 1543505. Source: MGI

GTPase binding

Inferred from physical interaction Ref.13. Source: UniProtKB

protein complex binding

Inferred from direct assay PubMed 23209302. Source: MGI

signal transducer activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NCF2P198782EBI-357130,EBI-489611

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.9
Chain2 – 340339Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1
PRO_0000127687

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 Ref.8 Ref.9 Ref.12 Ref.15
Modified residue2661Phosphohistidine By similarity

Experimental info

Mutagenesis471T → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-337 and A-339. Ref.16
Mutagenesis3371K → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-47 and A-339. Ref.16
Mutagenesis3391W → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-47 and A-337. Ref.16

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P62873 [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]"Beta-subunits of the human liver Gs/Gi signal-transducing proteins and those of bovine retinal rod cell transducin are identical."
Codina J., Stengel D., Woo S.L.C., Birnbaumer L.
FEBS Lett. 207:187-192(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Muscle and Uterus.
[8]Bienvenut W.V., Quadroni M.
Submitted (JUL-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-15; 58-89; 284-301 AND 305-314, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma and Melanoma.
[9]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-8; 69-78 AND 90-96, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[10]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 23-42; 58-78; 138-150; 198-209 AND 315-337, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[11]"G Protein betagamma subunits stimulate p114RhoGEF, a guanine nucleotide exchange factor for RhoA and Rac1: regulation of cell shape and reactive oxygen species production."
Niu J., Profirovic J., Pan H., Vaiskunaite R., Voyno-Yasenetskaya T.
Circ. Res. 93:848-856(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF18.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The cationic region of Rhes mediates its interactions with specific Gbeta subunits."
Hill C., Goddard A., Ladds G., Davey J.
Cell. Physiol. Biochem. 23:1-8(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RASD2.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2."
Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.
Structure 16:1086-1094(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEXES WITH GNG2 AND PTH1R, FUNCTION, SUBUNIT, MUTAGENESIS OF THR-47; LYS-337 AND TRP-339.
[17]Erratum
Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.
Structure 19:1200-1200(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: RETRACTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04526 mRNA. Translation: CAA28207.1.
AF501882 mRNA. Translation: AAM15918.1.
BT007305 mRNA. Translation: AAP35969.1.
CR456784 mRNA. Translation: CAG33065.1.
AL031282, AL109917 Genomic DNA. Translation: CAI20029.1.
AL109917, AL031282 Genomic DNA. Translation: CAI95654.1.
CH471183 Genomic DNA. Translation: EAW56147.1.
BC004186 mRNA. Translation: AAH04186.1.
BC005888 mRNA. Translation: AAH05888.1.
BC008991 mRNA. Translation: AAH08991.1.
M36430 mRNA. Translation: AAA63265.1.
PIRRGHUB1. A24853.
RefSeqNP_001269467.1. NM_001282538.1.
NP_001269468.1. NM_001282539.1.
NP_002065.1. NM_002074.4.
UniGeneHs.430425.
Hs.721030.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4KFMX-ray3.45B1-340[»]
ProteinModelPortalP62873.
SMRP62873. Positions 2-340.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109044. 70 interactions.
DIPDIP-599N.
IntActP62873. 21 interactions.
MINTMINT-94562.
STRING9606.ENSP00000367872.

PTM databases

PhosphoSiteP62873.

Polymorphism databases

DMDM51317302.

2D gel databases

OGPP62873.
REPRODUCTION-2DPAGEIPI00026268.

Proteomic databases

PaxDbP62873.
PRIDEP62873.

Protocols and materials databases

DNASU2782.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378609; ENSP00000367872; ENSG00000078369.
GeneID2782.
KEGGhsa:2782.
UCSCuc001aif.3. human.

Organism-specific databases

CTD2782.
GeneCardsGC01M001748.
HGNCHGNC:4396. GNB1.
HPAHPA040736.
MIM139380. gene.
neXtProtNX_P62873.
PharmGKBPA28776.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000176356.
HOVERGENHBG000188.
InParanoidP62873.
KOK04536.
OMARIVMRPR.
OrthoDBEOG7GN2N5.
PhylomeDBP62873.
TreeFamTF106149.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.
SignaLinkP62873.

Gene expression databases

ArrayExpressP62873.
BgeeP62873.
CleanExHS_GNB1.
GenevestigatorP62873.

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

ChiTaRSGNB1. human.
EvolutionaryTraceP62873.
GeneWikiGNB1.
GenomeRNAi2782.
NextBio10959.
PROP62873.
SOURCESearch...

Entry information

Entry nameGBB1_HUMAN
AccessionPrimary (citable) accession number: P62873
Secondary accession number(s): B1AJZ7, P04697, P04901
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM