Guanine nucleotide-binding protein G(q) subunit alpha (GNAQ)
The protein contains 359 amino acids for an estimated molecular weight of 42142 Da.
Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs). (updated: April 22, 2020)
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, is annotated as membranous in UniProt.
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| Variant | Description |
|---|---|
| SWS | |
| Found in blue naevi and uveal melanoma samples | |
| dbSNP:rs1059531 |
Biological Process
Action potential
Activation of phospholipase C activity
Adenylate cyclase-activating G protein-coupled receptor signaling pathway
Adenylate cyclase-modulating G protein-coupled receptor signaling pathway
Blood coagulation
Developmental pigmentation
Embryonic digit morphogenesis
Entrainment of circadian clock
Forebrain neuron development
G protein-coupled acetylcholine receptor signaling pathway
G protein-coupled receptor signaling pathway
Glutamate receptor signaling pathway
Heart development
Maternal behavior
Metabolic process
Negative regulation of protein kinase activity
Neuron remodeling
Phospholipase C-activating dopamine receptor signaling pathway
Phototransduction, visible light
Platelet activation
Positive regulation of GTPase activity
Post-embryonic development
Protein stabilization
Regulation of canonical Wnt signaling pathway
Regulation of catenin import into nucleus
Regulation of melanocyte differentiation
Skeletal system development
The reference OMIM entry for this protein is 163000
Capillary malformations, congenital; cmc
Nevi flammei, familial multiple
Port-wine stain
Capillary malformations; cmal
A number sign (#) is used with this entry because of evidence that congenital capillary malformations can be caused by somatic mosaic mutation in the GNAQ gene (600998) on chromosome 9q21. Sturge-Weber syndrome (185300), which includes port-wine stains, is also caused by somatic mosaic mutation in the GNAQ gene.
DESCRIPTION
Capillary malformations are a form of vascular malformation that are present from birth, tend to grow with the individual, do not regress spontaneously, and show normal rates of endothelial cell turnover. Capillary malformations are distinct from capillary hemangiomas (602089), which are highly proliferative lesions that appear shortly after birth and show rapid growth, slow involution, and endothelial hypercellularity (Spring and Bentz, 2005; Legiehn and Heran, 2006).CLINICAL FEATURES
Referred to as birthmarks, nevi flammei consist of dark red, nonelevated, sharply circumscribed patches which blanch on pressure with a glass, leaving a residual brown hyperpigmentation. Nevus flammeus is a frequent birthmark in the newborn infant, especially located in the central forehead; it fades spontaneously over a few months or years, as a rule. Shuper et al. (1984) referred to this lesion in the newborn as salmon patch and stated that it is incorrect to call it nevus flammeus. The proposita of the family described by Shuper et al. (1984) had 5 nevi flammei, 2 on her neck, 2 on her arms, and a very large purple one on her right groin and upper leg. Selmanowitz (1968) described a family with nevus flammeus of the forehead. Association with Unna nevus (163100) in several members of a family was reported by Merlob and Reisner (1985). In the family reported by Breugem et al. (2002), 12 members were affected and 11 were examined. The proband was a 6-year-old girl with a capillary malformation on the upper part of the left leg measuring 31 x 27 cm. She had several smaller capillary malformations on both feet and the left arm. The mother had several capillary malformations on her right arm, inside her left lower arm, and on her right lower leg. The sister of the proband had a large capillary malformations (30 x 30 cm) on her right upper leg. Several smaller capillary malformations were seen all over her body. The deceased grandmother was reported to have multiple small capillary malformations on her thorax. An uncle of the proband had a large capillary malformation on the anterolateral side of his left upper leg (30 x 30 cm) and a smaller capillary malformation on the anterior side of his left lower leg (10 x 5 cm). When he was 9 years old, he had an overgrowth of this leg with a 9-cm difference in leg length, which was subsequently treated with an epiphysodesis. As a result, that leg was 0.5 cm shorter when he was an adult, but the difference in leg circumference remained unchanged. He had no symptoms indicative of Klippel-Trenaunay syndrome (149000). Of 60 subjects with inherited capillary malformation from 13 families studied by Eerola et al. (2002), 19 had a lesion on the face, 15 in the nuchal region, and 26 in other parts of the body.INHERITANCE
Shelley and Livingood (1949) described 12 cases in 7 sibships in 4 generations of a family, with 5 instances of male-to-male transmission. Two generations were skipped in one branch of the family. In a family reported by Shuper et al. (1984), affected persons occurred in 3 generations and by inference someone in a fourth (earliest) generation may have be ... More on the omim web site
April 25, 2020: Protein entry updated
Automatic update: Entry updated from uniprot information.
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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 163000 was added.