Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
G-alpha(q) (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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; G protein, heterotrimeric; G protein, heterotrimeric alpha G(q)
Chromosomal Location of Human Ortholog: 9q21
Cellular Component: cytoplasm; dendrite; lysosomal membrane; nuclear membrane; photoreceptor outer segment; plasma membrane
Molecular Function: G-protein beta/gamma-subunit binding; GTP binding; GTPase activator activity; GTPase activity; metal ion binding; protein binding; signal transducer activity; type 2A serotonin receptor binding
Biological Process: acetylcholine receptor signaling, muscarinic pathway; blood coagulation; dopamine receptor, phospholipase C activating pathway; embryonic digit morphogenesis; entrainment of circadian clock; forebrain neuron development; G-protein signaling, adenylate cyclase activating pathway; glutamate signaling pathway; heart development; maternal behavior; metabolic process; negative regulation of protein kinase activity; neuron remodeling; phospholipase C activation; phototransduction, visible light; pigmentation during development; platelet activation; positive regulation of GTPase activity; post-embryonic development; protein stabilization; regulation of action potential; regulation of melanocyte differentiation; skeletal development
Disease: Capillary Malformations, Congenital; Sturge-weber Syndrome
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
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

G-alpha(q)

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


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


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 K16‑ub CCLSEEAkEARRIND
1 1 S53‑p GTGESGKsTFIKQMR
0 1 K57 SGKsTFIKQMRIIHG
0 1 S68‑p IIHGSGYsDEDKRGF
0 1 K98 IRAMDTLKIPYkYEH
0 2 K102‑ac DTLKIPYkYEHNKAH
0 3 K102‑ub DTLKIPYkYEHNKAH
0 1 K107 PYkYEHNKAHAQLVR
0 1 K120 VREVDVEKVSAFENP
0 1 K120 VREVDVEKVSAFENP
0 2 S122 EVDVEKVSAFENPyV
0 1 Y128‑p VSAFENPyVDAIKSL
1 0 S154‑p RRREYQLsDSTkYYL
0 2 K158‑ub YQLsDSTkYYLNDLD
0 1 T187‑p LRVRVPTtGIIEYPF
0 1 S198‑p EYPFDLQsVIFRMVD
0 3 K252‑ub ENRMEESkALFRTII
0 1 Y291‑p MYSHLVDyFPEYDGP
0 5 K345‑ub RFVFAAVkDTILQLN
2 0 Y356 LQLNLKEYNLV____
  mouse

 
K16 CCLSEEAKEARRIND
S53 GTGESGKSTFIkQMR
K57‑ub SGKSTFIkQMRIIHG
S68 IIHGSGYSDEDKRGF
K98‑ub IRAMDTLkIPYkYEH
K102 DTLkIPYKYEHNkAH
K102‑ub DTLkIPYkYEHNkAH
K107‑ub PYkYEHNkAHAQLVR
K120 VREVDVEKVsAFENP
K120‑ub VREVDVEkVsAFENP
S122‑p EVDVEkVsAFENPYV
Y128 VsAFENPYVDAIKSL
S154 RRREYQLSDSTkYYL
K158‑ub YQLSDSTkYYLNDLD
T187 LRVRVPTTGIIEYPF
S198 EYPFDLQSVIFRMVD
K252‑ub ENRMEESkALFRTII
Y291 MYSHLVDYFPEYDGP
K345‑ub RFVFAAVkDTILQLN
Y356‑p LQLNLKEyNLV____
  rat

 
K16 CCLSEEAKEARRIND
S53 GTGESGKSTFIKQMR
K57 SGKSTFIKQMRIIHG
S68 IIHGSGYSDEDKRGF
K98 VRAMDTLKIPYkYEH
K102‑ac DTLKIPYkYEHNKAH
K102 DTLKIPYKYEHNKAH
K107 PYkYEHNKAHAQLVR
K120‑ac VREVDVEkVSAFENP
K120 VREVDVEKVSAFENP
S122 EVDVEkVSAFENPYV
Y128 VSAFENPYVDAIKSL
S154 RRREYQLSDSTKYYL
K158 YQLSDSTKYYLNDLD
T187 LRVRVPTTGIIEYPF
S198 EYPFDLQSVIFRMVD
K252 ENRMEESKALFRTII
Y291 MYSHLVDYFPEYDGP
K345 RFVFAAVKDTILQLN
Y356 LQLNLKEYNLV____
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.