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P62873 (GBB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 94. 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·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)
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.14

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.12 Ref.14

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.

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
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.14
Mutagenesis3371K → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-47 and A-339. Ref.14
Mutagenesis3391W → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-47 and A-337. Ref.14

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: 3095147] [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: 16710414] [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: 15489334] [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, 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, 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, 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: 14512443] [Abstract]
Cited for: INTERACTION WITH ARHGEF18.
[12]"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: 19255495] [Abstract]
Cited for: INTERACTION WITH RASD2.
[13]"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: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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: 18611381] [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.
+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.
IPIIPI00026268.
PIRRGHUB1. A24853.
RefSeqNP_002065.1. NM_002074.3.
UniGeneHs.430425.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QNSX-ray3.00A1-340[»]
3KJ5X-ray3.00A1-340[»]
ProteinModelPortalP62873.
SMRP62873. Positions 1-340.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-599N.
IntActP62873. 15 interactions.
MINTMINT-94562.
STRINGP62873.

PTM databases

PhosphoSiteP62873.

Polymorphism databases

DMDM51317302.

2D gel databases

OGPP62873.
REPRODUCTION-2DPAGEIPI00026268.

Proteomic databases

PRIDEP62873.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378609; ENSP00000367872; ENSG00000078369.
ENST00000455156; ENSP00000416870; ENSG00000078369.
GeneID2782.
KEGGhsa:2782.
UCSCuc001aif.1. human.

Organism-specific databases

CTD2782.
GeneCardsGC01M001748.
H-InvDBHIX0000041.
HGNCHGNC:4396. GNB1.
MIM139380. gene.
neXtProtNX_P62873.
PharmGKBPA28776.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12689.
HOGENOMHBG396231.
HOVERGENHBG000188.
InParanoidP62873.
OMACMLWDIE.
OrthoDBEOG4HX51D.
PhylomeDBP62873.

Enzyme and pathway databases

Pathway_Interaction_DBhedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
lysophospholipid_pathway. LPA receptor mediated events.
wnt_calcium_pathway. Noncanonical Wnt signaling pathway.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
txa2pathway. Thromboxane A2 receptor signaling.
rhodopsin_pathway. Visual signal transduction: Rods.
ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_13685. Neuronal System.
REACT_15518. Transmembrane transport of small molecules.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP62873.
BgeeP62873.
CleanExHS_GNB1.
GenevestigatorP62873.
GermOnlineENSG00000078369. Homo sapiens.

Family and domain databases

InterProIPR020472. G-protein_beta_WD-40_rep.
IPR001632. Gprotein_B.
IPR016346. Guanine_nucleotide-bd_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KOK04536.
PfamPF00400. WD40. 7 hits.
[Graphical view]
PIRSFPIRSF002394. GN-bd_beta. 1 hit.
PRINTSPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. WD40_like. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio10959.
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: January 25, 2012
This is version 94 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

Human chromosome 1

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families