GNAQ
entrez
2776
canonical
uniprot
P50148
canonical
ensembl
ENSG00000156052
resolver
ensp
ENSP00000286548
resolver
ensp
ENSP00000585999
resolver
enst
ENST00000286548
resolver
enst
ENST00000915940
resolver
genesymbol
GNAQ
resolver
genesymbol_syn
GAQ
resolver
hgnc
HGNC:4390
resolver
uniprot
A0A024R240
resolver
uniprot
O15108
resolver
uniprot
Q13462
resolver
uniprot
Q6NT27
resolver
uniprot
Q92471
resolver
uniprot
Q9BZB9
resolver
uniprot_entry
A0A024R240_HUMAN
resolver
uniprot_entry
GNAQ_HUMAN
resolver
uniprot_sec
O15108
resolver
uniprot_sec
Q13462
resolver
uniprot_sec
Q6NT27
resolver
uniprot_sec
Q92471
resolver
uniprot_sec
Q9BZB9
resolver
amino_acid_sequence
MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
uniprot
proteins
disease_involvement
DISEASE: Capillary malformations, congenital (CMC) [MIM:163000]: A form of vascular malformations 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, which are highly proliferative lesions that appear shortly after birth and show rapid growth, slow involution, and endothelial hypercellularity. {ECO:0000269|PubMed:23656586}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Sturge-Weber syndrome (SWS) [MIM:185300]: A syndrome characterized by an intracranial vascular anomaly, leptomeningeal angiomatosis, most often involving the occipital and posterior parietal lobes. The most common features are facial cutaneous vascular malformations (port-wine stains), seizures, and glaucoma. Stasis results in ischemia underlying the leptomeningeal angiomatosis, leading to calcification and laminar cortical necrosis. The clinical course is highly variable and some children experience intractable seizures, intellectual disability, and recurrent stroke-like episodes. {ECO:0000269|PubMed:23656586}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades (PubMed:34556863, PubMed:35672283, PubMed:37991948). The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state (PubMed:37991948). Signaling by an activated GPCR promotes GDP release and GTP binding (PubMed:37991948). The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal (PubMed:37991948). Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (PubMed:37991948). Signaling is mediated via phospholipase C-beta-dependent inositol lipid hydrolysis for signal propagation: activates phospholipase C-beta: following GPCR activation, GNAQ activates PLC-beta (PLCB1, PLCB2, PLCB3 or PLCB4), leading to production of diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (PubMed:37991948). Required for platelet activation (By similarity). Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity (By similarity). Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity). Transduces FFAR4 signaling in response to long-chain fatty acids (LCFAs) (PubMed:27852822). Together with GNA11, required for heart development (By similarity). {ECO:0000250|UniProtKB:P21279, ECO:0000269|PubMed:27852822, ECO:0000269|PubMed:34556863, ECO:0000269|PubMed:35672283, ECO:0000269|PubMed:37991948}.
uniprot
proteins
mass_dalton
42142
uniprot
proteins
mutagenesis
MUTAGEN 2; /note="T->A: No effect on palmitoylation. No effect on phospholipase C-activating G protein-coupled receptor signaling pathway."; /evidence="ECO:0000269|PubMed:7957923"; MUTAGEN 9; /note="C->A: Abolishes palmitoylation. Inactive in phospholipase C-activating G protein-coupled receptor signaling pathway."; /evidence="ECO:0000269|PubMed:7957923"; MUTAGEN 10; /note="C->A: Abolishes palmitoylation. Inactive in phospholipase C-activating G protein-coupled receptor signaling pathway."; /evidence="ECO:0000269|PubMed:7957923
uniprot
proteins
post_translational_modification
PTM: Palmitoylated by ZDHHC3 and ZDHHC7 (PubMed:19001095). Palmitoylation occurs in the Golgi and participates in the localization of GNAQ to the plasma membrane (PubMed:19001095). {ECO:0000269|PubMed:19001095}.; PTM: (Microbial infection) Deamidated at Gln-209 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA. {ECO:0000269|PubMed:24141704}.; PTM: Histaminylated at Gln-209 residues by TGM2. {ECO:0000250|UniProtKB:P21279}.
uniprot
proteins
protein_family
G(q) subfamily
uniprot
proteins
protein_family
G-alpha family
uniprot
proteins
pubmed
12135370
uniprot
proteins
pubmed
12193606
uniprot
proteins
pubmed
1333286
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18672896
uniprot
proteins
pubmed
19001095
uniprot
proteins
pubmed
19078957
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21923740
uniprot
proteins
pubmed
22307269
uniprot
proteins
pubmed
23656586
uniprot
proteins
pubmed
23994616
uniprot
proteins
pubmed
24141704
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27852822
uniprot
proteins
pubmed
32126208
uniprot
proteins
pubmed
34556863
uniprot
proteins
pubmed
35672283
uniprot
proteins
pubmed
37991948
uniprot
proteins
pubmed
7492305
uniprot
proteins
pubmed
7957923
uniprot
proteins
pubmed
8664309
uniprot
proteins
pubmed
8825633
uniprot
proteins
pubmed
8836152
uniprot
proteins
pubmed
9700850
uniprot
proteins
sequence_length
359
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12135370, ECO:0000269|PubMed:19001095}; Peripheral membrane protein {ECO:0000269|PubMed:19001095}; Cytoplasmic side {ECO:0000269|PubMed:19001095}. Golgi apparatus {ECO:0000269|PubMed:19001095}. Nucleus {ECO:0000250|UniProtKB:P21279}. Nucleus membrane {ECO:0000250|UniProtKB:P21279}. Note=Associated to the plasma membrane via lipid-anchor (PubMed:19001095). Colocalizes with the adrenergic receptors ADRA1A and ADRA1B at the nuclear membrane of cardiac myocytes (By similarity). {ECO:0000250|UniProtKB:P21279, ECO:0000269|PubMed:19001095}.
uniprot
proteins