P62873 (GBB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	340 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Domain	Repeat WD repeat
Molecular function	Transducer
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled acetylcholine receptor signaling pathway Traceable author statement PubMed 8717044. Source: ProtInc 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 cardiac muscle cell apoptotic process Inferred from electronic annotation. Source: Compara cell proliferation Inferred from electronic annotation. Source: Compara 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: Compara cellular response to prostaglandin E stimulus Inferred from sequence or structural similarity. Source: BHF-UCL elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara energy reserve metabolic process Traceable author statement. Source: Reactome phospholipase C-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara platelet activation Traceable author statement. Source: Reactome retina development in camera-type eye Inferred from electronic annotation. Source: Compara sensory perception of taste Inferred from electronic annotation. Source: Compara synaptic transmission Traceable author statement. Source: Reactome
Cellular_component	cell body Inferred from electronic annotation. Source: Compara dendrite Inferred from electronic annotation. Source: Compara heterotrimeric G-protein complex Inferred from direct assay PubMed 1543505. Source: MGI photoreceptor inner segment Inferred from electronic annotation. Source: Compara photoreceptor outer segment membrane Inferred from electronic annotation. Source: Compara
Molecular_function	GTPase activity Inferred from direct assay PubMed 1543505. Source: MGI signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8 Ref.9
	Chain	2 – 340	339	Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1		PRO_0000127687
Regions
	Repeat	53 – 83	31	WD 1
	Repeat	95 – 125	31	WD 2
	Repeat	141 – 170	30	WD 3
	Repeat	182 – 212	31	WD 4
	Repeat	224 – 254	31	WD 5
	Repeat	268 – 298	31	WD 6
	Repeat	310 – 340	31	WD 7
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.8 Ref.9
	Modified residue	266	1	Phosphohistidine By similarity
Experimental info
	Mutagenesis	47	1	T → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-337 and A-339. Ref.14
	Mutagenesis	337	1	K → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-47 and A-339. Ref.14
	Mutagenesis	339	1	W → A: Abolishes interaction with PTH1R and signaling in response to PTH1R agonist; when associated with A-47 and A-337. Ref.14

Sequences

	Sequence		Length	Mass (Da)
	P62873 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 896CBD32D2686598	FASTA	340	37,377
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [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.
[15]	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.
IPI	IPI00026268.
PIR	RGHUB1. A24853.
RefSeq	NP_002065.1. NM_002074.3.
UniGene	Hs.430425.
3D structure databases
ProteinModelPortal	P62873.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-599N.
IntAct	P62873. 17 interactions.
MINT	MINT-94562.
STRING	9606.ENSP00000367872.
PTM databases
PhosphoSite	P62873.
Polymorphism databases
DMDM	51317302.
2D gel databases
OGP	P62873.
REPRODUCTION-2DPAGE	IPI00026268.
Proteomic databases
PaxDb	P62873.
PRIDE	P62873.
Protocols and materials databases
DNASU	2782.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378606; ENSP00000367869; ENSG00000078369. ENST00000378609; ENSP00000367872; ENSG00000078369.
GeneID	2782.
KEGG	hsa:2782.
UCSC	uc001aif.3. human.
Organism-specific databases
CTD	2782.
GeneCards	GC01M001748.
HGNC	HGNC:4396. GNB1.
HPA	HPA040736.
MIM	139380. gene.
neXtProt	NX_P62873.
PharmGKB	PA28776.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2319.
HOGENOM	HOG000176356.
HOVERGEN	HBG000188.
InParanoid	P62873.
KO	K04536.
OMA	CMLWDIE.
OrthoDB	EOG4HX51D.
PhylomeDB	P62873.
Enzyme and pathway databases
Pathway_Interaction_DB	hedgehog_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.
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_13685. Neuronal System. REACT_15518. Transmembrane transport of small molecules. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P62873.
Bgee	P62873.
CleanEx	HS_GNB1.
Genevestigator	P62873.
GermOnline	ENSG00000078369. Homo sapiens.
Family and domain databases
Gene3D	2.130.10.10. 1 hit.
InterPro	IPR020472. 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]
Pfam	PF00400. WD40. 7 hits. [Graphical view]
PIRSF	PIRSF002394. GN-bd_beta. 1 hit.
PRINTS	PR00319. GPROTEINB. PR00320. GPROTEINBRPT.
SMART	SM00320. WD40. 7 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 3 hits. PS50082. WD_REPEATS_2. 6 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	GNB1. human.
EvolutionaryTrace	P62873.
GenomeRNAi	2782.
NextBio	10959.
SOURCE	Search...

Entry information

Entry name

GBB1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.