Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00531
Entry Name
UniProt Accession
Theoretical PI
5.48
Molecular Weight
42158.09
Genbank Protein ID
Genbank Nucleotide ID
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
Created Date
01-MAY-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
9
Canonical
TLESIMACCLSEEAK
[1]
S-Palmitoylation
10
Canonical
LESIMACCLSEEAKE
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Wedegaertner PB, Chu DH, Wilson PT, Levis MJ, Bourne HR. Palmitoylation isrequired for signaling functions and membrane attachment of Gq alpha and Gsalpha. J Biol Chem. 1993 Nov 25;268(33):25001-8.[PMID:8227063]
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).
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.
Protein Length
359 AA.
Protein Sequence
(Canonical)
MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR  60
IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP YKYEHNKAHA QLVREVDVEK  120
VSAFENPYVD AIKSLWNDPG IQECYDRRRE YQLSDSTKYY LNDLDRVADP SYLPTQQDVL  180
RVRVPTTGII EYPFDLQSVI FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV  240
ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR  300
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV   359
FASTA
(Canonical)
>LipidDB-10090-00531|P21279
MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMR
IIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEK
VSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVL
RVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLV
ESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQR
DAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV
Gene Ontology
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome
GO:0005765; C:lysosomal membrane; IEA:Ensembl
GO:0016020; C:membrane; IDA:MGI
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; IBA:RefGenome
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; IMP:MGI
GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:MGI
GO:0048066; P:developmental pigmentation; IMP:MGI
GO:0042733; P:embryonic digit morphogenesis; IGI:MGI
GO:0021884; P:forebrain neuron development; IMP:MGI
GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:MGI
GO:0007215; P:glutamate receptor signaling pathway; IMP:MGI
GO:0007507; P:heart development; IMP:MGI
GO:0042711; P:maternal behavior; IMP:MGI
GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl
GO:0016322; P:neuron remodeling; IMP:MGI
GO:0060158; P:phospholipase C-activating dopamine receptor signaling pathway; IGI:MGI
GO:0009791; P:post-embryonic development; IMP:MGI
GO:0050821; P:protein stabilization; IEA:Ensembl
GO:0035412; P:regulation of catenin import into nucleus; IEA:Ensembl
GO:0045634; P:regulation of melanocyte differentiation; IMP:MGI
GO:0001501; P:skeletal system development; IMP:MGI
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;