P50148 (GNAQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide-binding protein G(q) subunit alpha

Alternative name(s):
Guanine nucleotide-binding protein alpha-q

Gene names

Name:	GNAQ
Synonyms:	GAQ

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Subunit structure	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. Ref.12 Ref.13
Tissue specificity	Predominantly expressed in ovary, prostate, testis and colon. Ref.2
Sequence similarities	Belongs to the G-alpha family. G(q) subfamily.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transducer
PTM	ADP-ribosylation Acetylation Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	activation of adenylate cyclase activity by G-protein signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome activation of phospholipase C activity by dopamine receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome glutamate signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of protein kinase activity Inferred from mutant phenotype. Source: BHF-UCL platelet activation Traceable author statement. Source: Reactome protein ADP-ribosylation Inferred from electronic annotation. Source: InterPro protein stabilization Inferred from mutant phenotype. Source: BHF-UCL regulation of action potential Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of catenin import into nucleus Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	cytoplasm Traceable author statement. Source: ProtInc heterotrimeric G-protein complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	G-protein beta/gamma-subunit complex binding Inferred from Biological aspect of Ancestor. Source: RefGenome G-protein coupled receptor binding Inferred from Biological aspect of Ancestor. Source: RefGenome GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activator activity Inferred from direct assay. Source: UniProtKB GTPase activity Traceable author statement. Source: ProtInc guanyl-nucleotide exchange factor activity Traceable author statement. Source: Reactome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase C activity Traceable author statement. Source: Reactome signal transducer activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 359	359	Guanine nucleotide-binding protein G(q) subunit alpha		PRO_0000203760
Regions
	Nucleotide binding	46 – 53	8	GTP By similarity
	Nucleotide binding	180 – 186	7	GTP By similarity
	Nucleotide binding	205 – 209	5	GTP By similarity
	Nucleotide binding	274 – 277	4	GTP By similarity
Sites
	Metal binding	53	1	Magnesium By similarity
	Metal binding	186	1	Magnesium By similarity
	Binding site	331	1	GTP; via amide nitrogen By similarity
Amino acid modifications
	Modified residue	102	1	N6-acetyllysine Ref.14
	Modified residue	183	1	ADP-ribosylarginine; by cholera toxin By similarity
	Lipidation	9	1	S-palmitoyl cysteine By similarity
	Lipidation	10	1	S-palmitoyl cysteine By similarity
Natural variations
	Natural variant	355	1	E → D. Corresponds to variant rs1059531 [ dbSNP | Ensembl ].		VAR_059319
Experimental info
	Sequence conflict	4	1	E → D in AAB64301. Ref.5
	Sequence conflict	28 – 29	2	QL → HV in AAC50363. Ref.1
	Sequence conflict	92	1	R → T in AAB64301. Ref.5
	Sequence conflict	103	1	Y → C in AAB64301. Ref.5
	Sequence conflict	324	1	I → N in AAB06875. Ref.2
	Sequence conflict	337	1	I → V in AAB64301. Ref.5
	Sequence conflict	358	1	L → A in AAB39498. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P50148 [UniParc]. Last modified July 7, 2009. Version 4. Checksum: 6F69C4F617DFA7C7	FASTA	359	42,142
	10 20 30 40 50 60 MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR 70 80 90 100 110 120 IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP YKYEHNKAHA QLVREVDVEK 130 140 150 160 170 180 VSAFENPYVD AIKSLWNDPG IQECYDRRRE YQLSDSTKYY LNDLDRVADP AYLPTQQDVL 190 200 210 220 230 240 RVRVPTTGII EYPFDLQSVI FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV 250 260 270 280 290 300 ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR 310 320 330 340 350 DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8825633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Human G(alpha q): cDNA and tissue distribution." Chen B., Leverette R.D., Schwinn D.A., Kwatra M.M. Biochim. Biophys. Acta 1281:125-128(1996) [PubMed: 8664309] [Abstract] 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: 8836152] [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: 9700850] [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: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 1333286] [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: 7492305] [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: 12193606] [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: 18672896] [Abstract] Cited for: INTERACTION WITH PECAM1.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, MASS SPECTROMETRY.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00288947.
PIR	S59635. S71963.
RefSeq	NP_002063.2. NM_002072.3.
UniGene	Hs.269782.
3D structure databases
ProteinModelPortal	P50148.
SMR	P50148. Positions 37-354.
ModBase	Search...
Protein-protein interaction databases
IntAct	P50148. 4 interactions.
MINT	MINT-262439.
STRING	P50148.
PTM databases
PhosphoSite	P50148.
Polymorphism databases
DMDM	251757492.
2D gel databases
Cornea-2DPAGE	P50148.
Proteomic databases
PRIDE	P50148.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000286548; ENSP00000286548; ENSG00000156052.
GeneID	2776.
KEGG	hsa:2776.
UCSC	uc004akw.1. human.
Organism-specific databases
CTD	2776.
GeneCards	GC09M080331.
H-InvDB	HIX0034745. HIX0180478.
HGNC	HGNC:4390. GNAQ.
HPA	CAB010036.
MIM	600998. gene.
neXtProt	NX_P50148.
PharmGKB	PA174.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10066.
GeneTree	ENSGT00560000076871.
HOGENOM	HBG444960.
HOVERGEN	HBG063184.
InParanoid	P50148.
OMA	HNKANAN.
OrthoDB	EOG4S4PGD.
PhylomeDB	P50148.
Enzyme and pathway databases
Pathway_Interaction_DB	arf6cyclingpathway. Arf6 signaling events. endothelinpathway. Endothelins. lysophospholipid_pathway. LPA receptor mediated events. er_nongenomic_pathway. Plasma membrane estrogen receptor signaling. s1p_s1p2_pathway. S1P2 pathway. s1p_s1p3_pathway. S1P3 pathway. s1p_meta_pathway. Sphingosine 1-phosphate (S1P) pathway. txa2pathway. Thromboxane A2 receptor signaling.
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P50148.
Bgee	P50148.
CleanEx	HS_GNAQ.
Genevestigator	P50148.
GermOnline	ENSG00000156052. Homo sapiens.
Family and domain databases
InterPro	IPR000654. Gprotein_alpha_Q. IPR001019. Gprotein_alpha_su. IPR011025. GproteinA_insert. [Graphical view]
Gene3D	G3DSA:1.10.400.10. GproteinA_insert. 1 hit.
KO	K04634.
PANTHER	PTHR10218. Gprotein_alph_bd. 1 hit.
Pfam	PF00503. G-alpha. 1 hit. [Graphical view]
PRINTS	PR00318. GPROTEINA. PR00442. GPROTEINAQ.
SMART	SM00275. G_alpha. 1 hit. [Graphical view]
SUPFAM	SSF47895. Transducn_insert. 1 hit.
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

GNAQ_HUMAN

Accession

Primary (citable) accession number: P50148
Secondary accession number(s): O15108 , Q13462, Q6NT27, Q92471, Q9BZB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	July 7, 2009
Last modified:	January 25, 2012
This is version 112 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.