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Protein

Guanine nucleotide-binding protein G(q) subunit alpha

Gene

GNAQ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • G-protein beta/gamma-subunit complex binding Source: GO_Central
  • GTPase activator activity Source: UniProtKB
  • GTPase activity Source: ProtInc
  • GTP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • signal transducer activity Source: GO_Central
  • type 2A serotonin receptor binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

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 Componenti: 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

  • cytoplasm Source: ProtInc
  • extracellular exosome Source: UniProtKB
  • heterotrimeric G-protein complex Source: GO_Central
  • lysosomal membrane Source: UniProtKB
  • nuclear membrane Source: UniProtKB-SubCell
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Capillary malformations, congenital (CMC)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:163000
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)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:185300
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.

Polymorphism and mutation databases

DMDMi251757492.

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

BgeeiP50148.
CleanExiHS_GNAQ.
ExpressionAtlasiP50148. baseline and differential.
GenevisibleiP50148. HS.

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. 63 interactions.
IntActiP50148. 10 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.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP50148.
KOiK04634.
OMAiGDQSEEL.
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

        10         20         30         40         50
MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES
60 70 80 90 100
GKSTFIKQMR IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP
110 120 130 140 150
YKYEHNKAHA QLVREVDVEK VSAFENPYVD AIKSLWNDPG IQECYDRRRE
160 170 180 190 200
YQLSDSTKYY LNDLDRVADP AYLPTQQDVL 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
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 (Ref. 5) Curated
Sequence conflicti28 – 292QL → HV in AAC50363 (PubMed:8825633).Curated
Sequence conflicti92 – 921R → T in AAB64301 (Ref. 5) Curated
Sequence conflicti103 – 1031Y → C in AAB64301 (Ref. 5) Curated
Sequence conflicti324 – 3241I → N in AAB06875 (PubMed:8664309).Curated
Sequence conflicti337 – 3371I → V in AAB64301 (Ref. 5) Curated
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. 1 Publication
VAR_067271
Natural varianti355 – 3551E → D.
Corresponds to variant rs1059531 [ dbSNP | Ensembl ].
VAR_059319

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi109038. 63 interactions.
IntActiP50148. 10 interactions.
MINTiMINT-262439.
STRINGi9606.ENSP00000286548.

Chemistry

ChEMBLiCHEMBL3286079.

PTM databases

PhosphoSiteiP50148.

Polymorphism and mutation databases

DMDMi251757492.

Proteomic databases

MaxQBiP50148.
PaxDbiP50148.
PRIDEiP50148.

Protocols and materials databases

DNASUi2776.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2776.
GeneCardsiGC09M080331.
HGNCiHGNC:4390. GNAQ.
HPAiCAB010036.
HPA048886.
MIMi163000. phenotype.
185300. phenotype.
600998. gene.
neXtProtiNX_P50148.
Orphaneti624. Familial multiple nevi flammei.
3205. Sturge-Weber syndrome.
PharmGKBiPA174.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG322962.
GeneTreeiENSGT00760000118851.
HOGENOMiHOG000038729.
HOVERGENiHBG063184.
InParanoidiP50148.
KOiK04634.
OMAiGDQSEEL.
OrthoDBiEOG7ZWD1W.
PhylomeDBiP50148.
TreeFamiTF300673.

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.

Miscellaneous databases

ChiTaRSiGNAQ. human.
GeneWikiiGNAQ.
GenomeRNAii2776.
NextBioi10922.
PROiP50148.
SOURCEiSearch...

Gene expression databases

BgeeiP50148.
CleanExiHS_GNAQ.
ExpressionAtlasiP50148. baseline and differential.
GenevisibleiP50148. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 75:203-209(2012) [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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: CHARACTERIZATION OF VARIANT LEU-209.
  19. "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: July 22, 2015
This is version 150 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.