Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 (GNB1)
The protein contains 340 amino acids for an estimated molecular weight of 37377 Da.
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. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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Biological Process
Adenylate cyclase-activating dopamine receptor signaling pathway
Blood coagulation
Cardiac muscle cell apoptotic process
Cell population proliferation
Cellular response to catecholamine stimulus
Cellular response to glucagon stimulus
Cellular response to hypoxia
Cellular response to prostaglandin E stimulus
Chemical synaptic transmission
Energy reserve metabolic process
G protein-coupled acetylcholine receptor signaling pathway
G protein-coupled receptor signaling pathway
Negative regulation of inflammatory response to antigenic stimulus
Phospholipase C-activating G protein-coupled receptor signaling pathway
Phototransduction, visible light
Platelet activation
Positive regulation of cytosolic calcium ion concentration
Positive regulation of potassium ion transmembrane transport
Protein folding
Protein heterotrimerization
Ras protein signal transduction
Regulation of rhodopsin mediated signaling pathway
Retina development in camera-type eye
Rhodopsin mediated signaling pathway
Sensory perception of taste
Signal transduction
Small molecule metabolic process
Wnt signaling pathway, calcium modulating pathway
Cellular Component
Cell body
Cytoplasm
Cytosol
Dendrite
Extracellular exosome
Extracellular vesicle
Heterotrimeric G-protein complex
Intracellular anatomical structure
Lysosomal membrane
Membrane
Myelin sheath
Obsolete cell
Photoreceptor disc membrane
Photoreceptor inner segment
Photoreceptor outer segment membrane
Plasma membrane
Synapse
Vesicle
The reference OMIM entry for this protein is 139380
Guanine nucleotide-binding protein, beta-1; gnb1
Transducin, beta polypeptide
DESCRIPTION
Heterotrimeric guanine nucleotide-binding proteins (G proteins) transduce extracellular signals received by transmembrane receptors to effector proteins. Each subunit of the G protein complex is encoded by a member of 1 of 3 corresponding gene families, alpha, beta, and gamma (Hurowitz et al., 2000).CLONING
Retinal transducin is a guanine nucleotide regulatory protein that activates a cGMP phosphodiesterase in photoreceptor cells. Fong et al. (1986) identified and analyzed cDNA clones of the bovine transducin beta subunit and deduced the primary structure of a 340-amino acid protein. Significant homology was found with the yeast CDC4 gene product. The beta-subunit polypeptide, of relative molecular mass 37,375 Da, is encoded by a 2.9-kb mRNA. All mammalian tissues and clonal cell lines examined contained at least 2 beta-related mRNAs, usually 1.8 and 2.9 kb long. The authors suggested that there may be a diversity of beta subunit-related mRNAs that could encode different proteins. Codina et al. (1986) cloned a full-length G protein beta-1 subunit (GNB1) from a human liver cDNA library. They found that the deduced 340-amino acid protein is identical to that encoded by bovine retinal rod cell cDNA of the beta subunit of transducin.GENE FUNCTION
Using coprecipitation analysis, Rosskopf et al. (2003) showed that GNB1 formed dimers with all gamma subunits analyzed. The strength of the interaction was variable and was strongest between GNB1 and GNG3 (608941), GNG10 (604389), GNG12, and GNG13 (607298).GENE STRUCTURE
Rosskopf et al. (2003) determined that the GNB1 gene contains 12 exons. The first 2 exons and the last exon are noncoding.MAPPING
Using a cDNA probe against a mouse/human somatic cell hybrid panel, Sparkes et al. (1987) mapped the human beta-1 polypeptide of G protein to human chromosome 1. Levine et al. (1990) confirmed the assignment to chromosome 1 by Southern analysis of somatic cell hybrids, and Levine et al. (1990) and Modi et al. (1991) regionalized the assignment to 1pter-p31.2 by in situ hybridization. Although Sparkes et al. (1987) had mapped the mouse Gnb1 gene to chromosome 19, later studies showed that Gnb1 is located on distal mouse chromosome 4 (Danciger et al., 1990).ANIMAL MODEL
In the Rd4/+ mouse, autosomal dominant retinal degeneration cosegregates with a large inversion spanning nearly all of chromosome 4 (Roderick et al., 1997). To identify the responsible gene for this phenotype, Kitamura et al. (2006) focused on the distal breakpoint and found that it lay in the second intron of the Gnb1 gene, coding for the transducin-beta-1 protein, which is directly involved in phototransduction and in the normal maintenance of photoreceptors. Kitamura et al. (2006) determined that before the beginning of retinal degeneration in the Rd4/+ retina, the levels of Gnb1 mRNA and transducin-beta-1 were 50% of those in wildtype retina. Kitamura et al. (2006) suggested that disruption of the Gnb1 gene is responsible for Rd4/+ retinal disease. ... More on the omim web site
May 12, 2019: Protein entry updated
Automatic update: model status changed
Nov. 17, 2018: Protein entry updated
Automatic update: model status changed
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
Oct. 27, 2017: Protein entry updated
Automatic update: model status changed
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 139380 was added.
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed