Guanine nucleotide-binding protein G(q) subunit alpha

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• alkylglycerophosphoethanolamine phosphodiesterase activity Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "The heterotrimeric G protein subunits Galpha(q) and Gbeta(1) have lysophospholipase D activity."
    Aoyama C., Sugimoto H., Ando H., Yamashita S., Horibata Y., Sugimoto S., Satou M.
    Biochem J 440:241-250(2011) [PubMed] [Europe PMC] [Abstract]
• G-protein beta/gamma-subunit complex binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• G protein-coupled receptor binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• GTPase activator activity Source: RGD
• GTPase activity Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• GTP binding Source: UniProtKB-KW
• metal ion binding Source: UniProtKB-KW
• protein-containing complex binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Sex differences in corticotropin-releasing factor receptor signaling and trafficking: potential role in female vulnerability to stress-related psychopathology."
    Bangasser D.A., Curtis A., Reyes B.A., Bethea T.T., Parastatidis I., Ischiropoulos H., Van Bockstaele E.J., Valentino R.J.
    Mol Psychiatry 15:877, 2010:896-904(2010) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• action potential Source: RGD
• activation of phospholipase C activity Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Role of Galphaq in smooth muscle cell proliferation."
    Tanski W.J., Roztocil E., Hemady E.A., Williams J.A., Davies M.G.
    J Vasc Surg 39:639-644(2004) [PubMed] [Europe PMC] [Abstract]
• adenylate cyclase-activating G protein-coupled receptor signaling pathway Source: RGD
• adenylate cyclase-modulating G protein-coupled receptor signaling pathway Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cranial skeletal system development Source: RGD
• developmental pigmentation Source: RGD
• embryonic digit morphogenesis Source: RGD
• endothelin receptor signaling pathway Source: RGD
• forebrain neuron development Source: RGD
• glutamate receptor signaling pathway Source: RGD
• G protein-coupled receptor signaling pathway Source: RGD
• heart development Source: RGD
• maternal behavior Source: RGD
• multicellular organism aging Source: RGD
• negative regulation of apoptotic process Source: RGDInferred from mutant phenotypeⁱ
  • "Galphaq expression activates EGFR and induces Akt mediated cardiomyocyte survival: dissociation from Galphaq mediated hypertrophy."
    Howes A.L., Miyamoto S., Adams J.W., Woodcock E.A., Brown J.H.
    J Mol Cell Cardiol 40:597-604(2006) [PubMed] [Europe PMC] [Abstract]
• negative regulation of potassium ion transport Source: RGDInferred from mutant phenotypeⁱ
  • "The alpha subunit of Gq contributes to muscarinic inhibition of the M-type potassium current in sympathetic neurons."
    Haley J.E., Abogadie F.C., Delmas P., Dayrell M., Vallis Y., Milligan G., Caulfield M.P., Brown D.A., Buckley N.J.
    J Neurosci 18:4521-4531(1998) [PubMed] [Europe PMC] [Abstract]
• negative regulation of protein kinase activity Source: RGD
• neuron remodeling Source: RGD
• phospholipase C-activating dopamine receptor signaling pathway Source: RGD
• phospholipase C-activating G protein-coupled receptor signaling pathway Source: RGDInferred from mutant phenotypeⁱ
  • "Temporal dispersion of activation of phospholipase C-beta1 and -gamma isoforms by angiotensin II in vascular smooth muscle cells. Role of alphaq/11, alpha12, and beta gamma G protein subunits."
    Ushio-Fukai M., Griendling K.K., Akers M., Lyons P.R., Alexander R.W.
    J Biol Chem 273:19772-19777(1998) [PubMed] [Europe PMC] [Abstract]
• positive regulation of smooth muscle cell proliferation Source: RGDInferred from mutant phenotypeⁱ
  • "Role of Galphaq in smooth muscle cell proliferation."
    Tanski W.J., Roztocil E., Hemady E.A., Williams J.A., Davies M.G.
    J Vasc Surg 39:639-644(2004) [PubMed] [Europe PMC] [Abstract]
• post-embryonic development Source: RGD
• protein stabilization Source: RGD
• regulation of blood pressure Source: RGD
• regulation of canonical Wnt signaling pathway Source: RGD
• regulation of melanocyte differentiation Source: RGD
• skeletal system development Source: RGD

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

2D gel databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• G protein-coupled receptor binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES 
        60         70         80         90        100
GKSTFIKQMR IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM VRAMDTLKIP 
       110        120        130        140        150
YKYEHNKAHA QLVREVDVEK VSAFENPYVD AIKSLWNDPG IQECYDRRRE 
       160        170        180        190        200
YQLSDSTKYY LNDLDRVADP SYLPTQQDVL RVRVPTTGII EYPFDLQSVI 
       210        220        230        240        250
FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV ESDNENRMEE 
       260        270        280        290        300
SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR 
       310        320        330        340        350
DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ 

LNLKEYNLV                                              

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. SIMILARITY comments
   Index of protein domains and families