LipidDB ID

LipidDB-9606-00752

Entry Name

UniProt Accession

P50148; O15108; Q13462; Q6NT27; Q92471; Q9BZB9;

Theoretical PI

5.48

Molecular Weight

42142.09

Genbank Protein ID

AAC50363.1; AAB06875.1; AAB39498.1; AAG61117.1; AAB64301.1; AAM12610.1; CAI12198.1; CAI12198.1; CAI12198.1; CAI14669.1; CAI14669.1; CAI14669.1; CAI15999.1; CAI15999.1; CAI15999.1; EAW62607.1; AAH57777.1; AAH67850.1; AAH69520.1; AAH75096.1; AAH75097.1; AAA99950.1;

Genbank Nucleotide ID

U40038; U43083; L76256; AF329284; AF011496; AF493896; AL160268; AL160278; AL355535; AL355535; AL160268; AL160278; AL160278; AL160268; AL355535; CH471089; BC057777; BC067850; BC069520; BC075096; BC075097; L40629;

Protein Name

Guanine nucleotide-binding protein G(q) subunit alpha

Protein Synonyms/Alias

Guanine nucleotide-binding protein alpha-q;

Gene Name

GNAQ

Gene Synonyms/Alias

GAQ;

Created Date

01-OCT-1996

Organism

Homo sapiens (Human)

NCBI Taxa ID

9606

Reference

[1] Wilson PT, Bourne HR. Fatty acylation of alpha z. Effects of palmitoylationand myristoylation on alpha z signaling. J Biol Chem. 1995 Apr21;270(16):9667-75.[PMID:7536745]

Functional Description

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).

Sequence Annotation

Nucleotide-binding: 46 53 GTP.
Nucleotide-binding: 180 186 GTP.
Nucleotide-binding: 205 209 GTP.
Nucleotide-binding: 274 277 GTP.
Metal binding site: 53 53 Magnesium.
Metal binding site: 186 186 Magnesium.
Binding site: 331 331 GTP; via amide nitrogen.
Modified residue: 183 183 ADP-ribosylarginine; by cholera toxin.

Protein Length

359 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0005737; C:cytoplasm; TAS:ProtInc
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome
GO:0005765; C:lysosomal membrane; IDA:UniProtKB
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0005096; F:GTPase activator activity; IDA:UniProtKB
GO:0003924; F:GTPase activity; IBA:RefGenome
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004871; F:signal transducer activity; IBA:RefGenome
GO:0031826; F:type 2A serotonin receptor binding; IBA:RefGenome
GO:0001508; P:action potential; IBA:RefGenome
GO:0007202; P:activation of phospholipase C activity; TAS:ProtInc
GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IBA:RefGenome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0048066; P:developmental pigmentation; IEA:Ensembl
GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl
GO:0021884; P:forebrain neuron development; IEA:Ensembl
GO:0007215; P:glutamate receptor signaling pathway; IBA:RefGenome
GO:0007507; P:heart development; IEA:Ensembl
GO:0042711; P:maternal behavior; IEA:Ensembl
GO:0006469; P:negative regulation of protein kinase activity; IMP:BHF-UCL
GO:0016322; P:neuron remodeling; IEA:Ensembl
GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IBA:RefGenome
GO:0030168; P:platelet activation; TAS:Reactome
GO:0043547; P:positive regulation of GTPase activity; IDA:GOC
GO:0009791; P:post-embryonic development; IEA:Ensembl
GO:0050821; P:protein stabilization; IMP:BHF-UCL
GO:0035412; P:regulation of catenin import into nucleus; IMP:BHF-UCL
GO:0045634; P:regulation of melanocyte differentiation; IEA:Ensembl
GO:0001501; P:skeletal system development; IEA:Ensembl

Interpro

InterPro; IPR000654; Gprotein_alpha_Q
InterPro; IPR001019; Gprotein_alpha_su
InterPro; IPR011025; GproteinA_insert
InterPro; IPR027417; P-loop_NTPase

Pfam

Pfam; PF00503; G-alpha;

SMART

SMART; SM00275; G_alpha;

PROSITE

PRINTS

PRINTS; PR00318; GPROTEINA;
PRINTS; PR00442; GPROTEINAQ;