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P50148

- GNAQ_HUMAN

UniProt

P50148 - GNAQ_HUMAN

Protein

Guanine nucleotide-binding protein G(q) subunit alpha

Gene

GNAQ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 4 (07 Jul 2009)
      Previous versions | rss
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    Functioni

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi53 – 531MagnesiumBy similarity
    Metal bindingi186 – 1861MagnesiumBy similarity
    Binding sitei331 – 3311GTP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi46 – 538GTPBy similarity
    Nucleotide bindingi180 – 1867GTPBy similarity
    Nucleotide bindingi205 – 2095GTPBy similarity
    Nucleotide bindingi274 – 2774GTPBy similarity

    GO - Molecular functioni

    1. G-protein beta/gamma-subunit complex binding Source: RefGenome
    2. GTPase activator activity Source: UniProtKB
    3. GTPase activity Source: RefGenome
    4. GTP binding Source: UniProtKB-KW
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: UniProtKB
    7. signal transducer activity Source: RefGenome
    8. type 2A serotonin receptor binding Source: RefGenome

    GO - Biological processi

    1. action potential Source: RefGenome
    2. activation of phospholipase C activity Source: ProtInc
    3. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: RefGenome
    4. blood coagulation Source: Reactome
    5. developmental pigmentation Source: Ensembl
    6. embryonic digit morphogenesis Source: Ensembl
    7. forebrain neuron development Source: Ensembl
    8. glutamate receptor signaling pathway Source: RefGenome
    9. heart development Source: Ensembl
    10. maternal behavior Source: Ensembl
    11. negative regulation of protein kinase activity Source: BHF-UCL
    12. neuron remodeling Source: Ensembl
    13. phospholipase C-activating dopamine receptor signaling pathway Source: RefGenome
    14. platelet activation Source: Reactome
    15. positive regulation of GTPase activity Source: GOC
    16. post-embryonic development Source: Ensembl
    17. protein stabilization Source: BHF-UCL
    18. regulation of catenin import into nucleus Source: BHF-UCL
    19. regulation of melanocyte differentiation Source: Ensembl
    20. skeletal system development Source: Ensembl

    Keywords - Molecular functioni

    Transducer

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_18283. G alpha (q) signalling events.
    REACT_18405. Acetylcholine regulates insulin secretion.
    REACT_19140. ADP signalling through P2Y purinoceptor 1.
    REACT_19193. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
    REACT_20647. Thromboxane signalling through TP receptor.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
    SignaLinkiP50148.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide-binding protein G(q) subunit alpha
    Alternative name(s):
    Guanine nucleotide-binding protein alpha-q
    Gene namesi
    Name:GNAQ
    Synonyms:GAQ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:4390. GNAQ.

    Subcellular locationi

    Nucleus By similarity. Membrane By similarity. Nucleus membrane By similarity
    Note: Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. extracellular vesicular exosome Source: UniProt
    3. heterotrimeric G-protein complex Source: RefGenome
    4. lysosomal membrane Source: UniProtKB
    5. nuclear membrane Source: UniProtKB-SubCell
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831R → Q in SWS; found as somatic mosaic mutation in CMC; also found in melanocytomas sample; somatic mutation; shows significant activation of EPHB2 compared to control. 2 Publications
    VAR_067270
    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, mental retardation, and recurrent stroke-like episodes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831R → Q in SWS; found as somatic mosaic mutation in CMC; also found in melanocytomas sample; somatic mutation; shows significant activation of EPHB2 compared to control. 2 Publications
    VAR_067270

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi163000. phenotype.
    185300. phenotype.
    Orphaneti624. Familial multiple nevi flammei.
    3205. Sturge-Weber syndrome.
    PharmGKBiPA174.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 359359Guanine nucleotide-binding protein G(q) subunit alphaPRO_0000203760Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi9 – 91S-palmitoyl cysteineBy similarity
    Lipidationi10 – 101S-palmitoyl cysteineBy similarity
    Modified residuei183 – 1831ADP-ribosylarginine; by cholera toxinBy similarity

    Keywords - PTMi

    ADP-ribosylation, Lipoprotein, Palmitate

    Proteomic databases

    MaxQBiP50148.
    PaxDbiP50148.
    PRIDEiP50148.

    PTM databases

    PhosphoSiteiP50148.

    Expressioni

    Tissue specificityi

    Predominantly expressed in ovary, prostate, testis and colon. Down-regulated in the peripheral blood lymphocytes (PBLs) of rheumatoid arthritis patients (at protein level).2 Publications

    Gene expression databases

    ArrayExpressiP50148.
    BgeeiP50148.
    CleanExiHS_GNAQ.
    GenevestigatoriP50148.

    Organism-specific databases

    HPAiCAB010036.
    HPA048886.

    Interactioni

    Subunit structurei

    G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Binds SLC9A3R1. Forms a complex with PECAM1 and BDKRB2. Interacts with PECAM1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARRB1P494072EBI-3909604,EBI-743313
    RARAP102764EBI-3909604,EBI-413374

    Protein-protein interaction databases

    BioGridi109038. 40 interactions.
    IntActiP50148. 9 interactions.
    MINTiMINT-262439.
    STRINGi9606.ENSP00000286548.

    Structurei

    3D structure databases

    ProteinModelPortaliP50148.
    SMRiP50148. Positions 18-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the G-alpha family. G(q) subfamily.Curated

    Phylogenomic databases

    eggNOGiNOG322962.
    HOGENOMiHOG000038729.
    HOVERGENiHBG063184.
    InParanoidiP50148.
    KOiK04634.
    OMAiLKISYGV.
    OrthoDBiEOG7ZWD1W.
    PhylomeDBiP50148.
    TreeFamiTF300673.

    Family and domain databases

    Gene3Di1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR000654. Gprotein_alpha_Q.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR10218. PTHR10218. 1 hit.
    PfamiPF00503. G-alpha. 1 hit.
    [Graphical view]
    PRINTSiPR00318. GPROTEINA.
    PR00442. GPROTEINAQ.
    SMARTiSM00275. G_alpha. 1 hit.
    [Graphical view]
    SUPFAMiSSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    P50148-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES    50
    GKSTFIKQMR IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP 100
    YKYEHNKAHA QLVREVDVEK VSAFENPYVD AIKSLWNDPG IQECYDRRRE 150
    YQLSDSTKYY LNDLDRVADP AYLPTQQDVL RVRVPTTGII EYPFDLQSVI 200
    FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV ESDNENRMEE 250
    SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR 300
    DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ 350
    LNLKEYNLV 359
    Length:359
    Mass (Da):42,142
    Last modified:July 7, 2009 - v4
    Checksum:i6F69C4F617DFA7C7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41E → D in AAB64301. 1 PublicationCurated
    Sequence conflicti28 – 292QL → HV in AAC50363. (PubMed:8825633)Curated
    Sequence conflicti92 – 921R → T in AAB64301. 1 PublicationCurated
    Sequence conflicti103 – 1031Y → C in AAB64301. 1 PublicationCurated
    Sequence conflicti324 – 3241I → N in AAB06875. (PubMed:8664309)Curated
    Sequence conflicti337 – 3371I → V in AAB64301. 1 PublicationCurated
    Sequence conflicti358 – 3581L → A in AAB39498. (PubMed:8836152)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831R → Q in SWS; found as somatic mosaic mutation in CMC; also found in melanocytomas sample; somatic mutation; shows significant activation of EPHB2 compared to control. 2 Publications
    VAR_067270
    Natural varianti209 – 2091Q → L Found in blue naevi and uveal melanoma samples; somatic mutation; constitutive activation.
    VAR_067271
    Natural varianti355 – 3551E → D.
    Corresponds to variant rs1059531 [ dbSNP | Ensembl ].
    VAR_059319

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40038 mRNA. Translation: AAC50363.1.
    U43083 mRNA. Translation: AAB06875.1.
    L76256 mRNA. Translation: AAB39498.1.
    AF329284 mRNA. Translation: AAG61117.1.
    AF011496 mRNA. Translation: AAB64301.1.
    AF493896 mRNA. Translation: AAM12610.1.
    AL160268, AL160278, AL355535 Genomic DNA. Translation: CAI12198.1.
    AL355535, AL160268, AL160278 Genomic DNA. Translation: CAI14669.1.
    AL160278, AL160268, AL355535 Genomic DNA. Translation: CAI15999.1.
    CH471089 Genomic DNA. Translation: EAW62607.1.
    BC057777 mRNA. Translation: AAH57777.1.
    BC067850 mRNA. Translation: AAH67850.1.
    BC069520 mRNA. Translation: AAH69520.1.
    BC075096 mRNA. Translation: AAH75096.1.
    BC075097 mRNA. Translation: AAH75097.1.
    L40629 mRNA. Translation: AAA99950.1.
    CCDSiCCDS6658.1.
    PIRiS59635.
    S71963.
    RefSeqiNP_002063.2. NM_002072.4.
    UniGeneiHs.269782.
    Hs.594695.

    Genome annotation databases

    EnsembliENST00000286548; ENSP00000286548; ENSG00000156052.
    GeneIDi2776.
    KEGGihsa:2776.
    UCSCiuc004akw.3. human.

    Polymorphism databases

    DMDMi251757492.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40038 mRNA. Translation: AAC50363.1 .
    U43083 mRNA. Translation: AAB06875.1 .
    L76256 mRNA. Translation: AAB39498.1 .
    AF329284 mRNA. Translation: AAG61117.1 .
    AF011496 mRNA. Translation: AAB64301.1 .
    AF493896 mRNA. Translation: AAM12610.1 .
    AL160268 , AL160278 , AL355535 Genomic DNA. Translation: CAI12198.1 .
    AL355535 , AL160268 , AL160278 Genomic DNA. Translation: CAI14669.1 .
    AL160278 , AL160268 , AL355535 Genomic DNA. Translation: CAI15999.1 .
    CH471089 Genomic DNA. Translation: EAW62607.1 .
    BC057777 mRNA. Translation: AAH57777.1 .
    BC067850 mRNA. Translation: AAH67850.1 .
    BC069520 mRNA. Translation: AAH69520.1 .
    BC075096 mRNA. Translation: AAH75096.1 .
    BC075097 mRNA. Translation: AAH75097.1 .
    L40629 mRNA. Translation: AAA99950.1 .
    CCDSi CCDS6658.1.
    PIRi S59635.
    S71963.
    RefSeqi NP_002063.2. NM_002072.4.
    UniGenei Hs.269782.
    Hs.594695.

    3D structure databases

    ProteinModelPortali P50148.
    SMRi P50148. Positions 18-354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109038. 40 interactions.
    IntActi P50148. 9 interactions.
    MINTi MINT-262439.
    STRINGi 9606.ENSP00000286548.

    PTM databases

    PhosphoSitei P50148.

    Polymorphism databases

    DMDMi 251757492.

    Proteomic databases

    MaxQBi P50148.
    PaxDbi P50148.
    PRIDEi P50148.

    Protocols and materials databases

    DNASUi 2776.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286548 ; ENSP00000286548 ; ENSG00000156052 .
    GeneIDi 2776.
    KEGGi hsa:2776.
    UCSCi uc004akw.3. human.

    Organism-specific databases

    CTDi 2776.
    GeneCardsi GC09M080331.
    HGNCi HGNC:4390. GNAQ.
    HPAi CAB010036.
    HPA048886.
    MIMi 163000. phenotype.
    185300. phenotype.
    600998. gene.
    neXtProti NX_P50148.
    Orphaneti 624. Familial multiple nevi flammei.
    3205. Sturge-Weber syndrome.
    PharmGKBi PA174.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322962.
    HOGENOMi HOG000038729.
    HOVERGENi HBG063184.
    InParanoidi P50148.
    KOi K04634.
    OMAi LKISYGV.
    OrthoDBi EOG7ZWD1W.
    PhylomeDBi P50148.
    TreeFami TF300673.

    Enzyme and pathway databases

    Reactomei REACT_18283. G alpha (q) signalling events.
    REACT_18405. Acetylcholine regulates insulin secretion.
    REACT_19140. ADP signalling through P2Y purinoceptor 1.
    REACT_19193. Fatty Acids bound to GPR40 (FFAR1) regulate insulin secretion.
    REACT_20647. Thromboxane signalling through TP receptor.
    REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
    SignaLinki P50148.

    Miscellaneous databases

    ChiTaRSi GNAQ. human.
    GeneWikii GNAQ.
    GenomeRNAii 2776.
    NextBioi 10922.
    PROi P50148.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50148.
    Bgeei P50148.
    CleanExi HS_GNAQ.
    Genevestigatori P50148.

    Family and domain databases

    Gene3Di 1.10.400.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR000654. Gprotein_alpha_Q.
    IPR001019. Gprotein_alpha_su.
    IPR011025. GproteinA_insert.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR10218. PTHR10218. 1 hit.
    Pfami PF00503. G-alpha. 1 hit.
    [Graphical view ]
    PRINTSi PR00318. GPROTEINA.
    PR00442. GPROTEINAQ.
    SMARTi SM00275. G_alpha. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47895. SSF47895. 1 hit.
    SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of human G alpha q cDNA and chromosomal localization of the G alpha q gene (GNAQ) and a processed pseudogene."
      Dong Q., Shenker A., Way J., Haddad B.R., Lin K., Hughes M.R., McBride W.O., Spiegel A.M., Battey J.
      Genomics 30:470-475(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Prostate.
    3. "Specificity of G alpha q and G alpha 11 gene expression in platelets and erythrocytes. Expressions of cellular differentiation and species differences."
      Johnson G.J., Leis L.A., Dunlop P.C.
      Biochem. J. 318:1023-1031(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "G alpha q cDNA sequence from human platelets."
      Gabbeta J., Dhanasekaran N., Rao A.K.
      Thromb. Res. 91:29-32(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Nucleotide sequence of human Gq guanine nucleotide binding protein."
      Bai X.H., Acharya R., Rivera C., Murtagh J.J.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Puhl H.L. III, Ikeda S.R., Aronstam R.S.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain and Placenta.
    10. "Signal-transducing G proteins and antidepressant drugs: evidence for modulation of alpha subunit gene expression in rat brain."
      Lesch K.-P., Manji H.K.
      Biol. Psychiatry 32:549-579(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-235.
      Tissue: Brain cortex.
    11. "Ca2+ signalling in K562 human erythroleukaemia cells: effect of dimethyl sulphoxide and role of G-proteins in thrombin- and thromboxane A2-activated pathways."
      Thomas C.P., Dunn M.J., Mattera R.
      Biochem. J. 312:151-158(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 244-337.
      Tissue: Hematopoietic.
    12. "Regulation of GTP-binding protein alpha q (Galpha q) signaling by the ezrin-radixin-moesin-binding phosphoprotein-50 (EBP50)."
      Rochdi M.D., Watier V., La Madeleine C., Nakata H., Kozasa T., Parent J.-L.
      J. Biol. Chem. 277:40751-40759(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC9A3R1.
    13. "Regulation of G protein-coupled receptor activities by the platelet-endothelial cell adhesion molecule, PECAM-1."
      Yeh J.C., Otte L.A., Frangos J.A.
      Biochemistry 47:9029-9039(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PECAM1.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Expression of G protein alphaq subunit is decreased in lymphocytes from rheumatoid arthritis patients and is correlated with disease activity."
      Wang Y., Li Y., He Y., Sun Y., Sun W., Xie Q., Yin G., Du Y., Wang L., Shi G.
      Scand. J. Immunol. 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    16. Cited for: INVOLVEMENT IN CMC, VARIANT SWS GLN-183, CHARACTERIZATION OF VARIANT SWS GLN-183.
    17. Cited for: CHARACTERIZATION OF VARIANT LEU-209.
    18. "GNAQ and GNA11 mutations in melanocytomas of the central nervous system."
      Murali R., Wiesner T., Rosenblum M.K., Bastian B.C.
      Acta Neuropathol. 123:457-459(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLN-183.

    Entry informationi

    Entry nameiGNAQ_HUMAN
    AccessioniPrimary (citable) accession number: P50148
    Secondary accession number(s): O15108
    , Q13462, Q6NT27, Q92471, Q9BZB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 141 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3