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Protein Page:
G-alpha(q) (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
G-alpha(q) a guanine nucleotide-binding protein of the G12 class of G-alpha proteins. Agonist binding to Gq-coupled receptors may block Akt activation via the release of active G-alpha(q) subunits that inhibit phosphatidylinositol 3-kinase. Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Note: This description may include information from UniProtKB.
Protein type: G protein, heterotrimeric alpha G(q); G protein; G protein, heterotrimeric
Cellular Component: nuclear membrane; extrinsic to internal side of plasma membrane; lysosomal membrane; cytoplasm; plasma membrane; heterotrimeric G-protein complex
Molecular Function: GTPase activity; protein binding; signal transducer activity; G-protein-coupled receptor binding; GTP binding; metal ion binding; G-protein beta/gamma-subunit binding; GTPase activator activity
Biological Process: platelet activation; regulation of action potential; protein stabilization; glutamate signaling pathway; maternal behavior; heart development; pigmentation during development; G-protein signaling, adenylate cyclase activating pathway; post-embryonic development; regulation of melanocyte differentiation; GTP catabolic process; forebrain neuron development; phospholipase C activation; negative regulation of protein kinase activity; dopamine receptor, phospholipase C activating pathway; embryonic digit morphogenesis; blood coagulation; skeletal development; positive regulation of GTPase activity; neuron remodeling
Reference #:  P50148 (UniProtKB)
Alt. Names/Synonyms: G-ALPHA-q; GAQ; GNAQ; guanine nucleotide binding protein (G protein), q polypeptide; Guanine nucleotide-binding protein alpha-q; Guanine nucleotide-binding protein G(q) subunit alpha
Gene Symbols: GNAQ
Molecular weight: 42,142 Da
Basal Isoelectric point: 5.48  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  AMPK Signaling  |  ESC Pluripotency and Differentiation  |  GPCR Signaling to MAPKs  |  Microtubule Dynamics  |  mTOR Signaling  |  Phospholipase Signaling  |  PI3K/Akt Signaling  |  Translation: eIF4E and p70S6K
Select Structure to View Below

G-alpha(q)

Protein Structure Not Found.


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Sites Implicated In
enzymatic activity, inhibited: S53‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 1 S53-p GTGESGKsTFIKQMR
0 1 K57 SGKsTFIKQMRIIHG
0 1 K98 IRAMDTLKIPYkYEH
0 1 K102-ac DTLKIPYkYEHNKAH
0 1 K102 DTLKIPYKYEHNKAH
0 1 K107 PYkYEHNKAHAQLVR
0 1 K120 VREVDVEKVSAFENP
0 2 S122 EVDVEKVSAFENPYV
1 0 S154-p RRREYQLsDSTKYYL
0 1 K158 YQLsDSTKYYLNDLD
0 1 S198-p EYPFDLQsVIFRMVD
0 2 K252-ub ENRMEESkALFRTII
0 5 K345-ub RFVFAAVkDTILQLN
2 0 Y356 LQLNLKEYNLV____
  mouse

 
S53 GTGESGKSTFIkQMR
K57-ub SGKSTFIkQMRIIHG
K98-ub IRAMDTLkIPYkYEH
K102 DTLkIPYKYEHNkAH
K102-ub DTLkIPYkYEHNkAH
K107-ub PYkYEHNkAHAQLVR
K120-ub VREVDVEkVsAFENP
S122-p EVDVEkVsAFENPYV
S154 RRREYQLSDSTkYYL
K158-ub YQLSDSTkYYLNDLD
S198 EYPFDLQSVIFRMVD
K252-ub ENRMEESkALFRTII
K345-ub RFVFAAVkDTILQLN
Y356-p LQLNLKEyNLV____
  rat

 
S53 GTGESGKSTFIKQMR
K57 SGKSTFIKQMRIIHG
K98 VRAMDTLKIPYKYEH
K102 DTLKIPYKYEHNKAH
K102 DTLKIPYKYEHNKAH
K107 PYKYEHNKAHAQLVR
K120 VREVDVEKVSAFENP
S122 EVDVEKVSAFENPYV
S154 RRREYQLSDSTKYYL
K158 YQLSDSTKYYLNDLD
S198 EYPFDLQSVIFRMVD
K252 ENRMEESKALFRTII
K345 RFVFAAVKDTILQLN
Y356 LQLNLKEYNLV____
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