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G-alpha(q) (human)

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: extrinsic to internal side of plasma membrane; nuclear membrane; cytoplasm; plasma membrane; heterotrimeric G-protein complex Molecular Function: GTPase activity; signal transducer activity; protein binding; 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; behavior; heart development; pigmentation during development; G-protein signaling, adenylate cyclase activating pathway; post-embryonic development; regulation of melanocyte differentiation; protein amino acid ADP-ribosylation; phospholipase C activation; GTP catabolic process; forebrain neuron development; negative regulation of protein kinase activity; embryonic digit morphogenesis; dopamine receptor, phospholipase C activating pathway; blood coagulation; skeletal development; neuron remodeling; positive regulation of GTPase activity 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:  AMPK Signaling  |  ESC Pluripotency and Differentiation  |  GPCRs Signaling to MAPK/Erk  |  mTOR Signaling  |  Phospholipase Signaling  |  PI3K/Akt Signaling  |  Regulation of Actin Dynamics  |  Regulation of Microtubule Dynamics  |  Translation: eIF4E and p70S6K

Select Structure to View Below G-alpha(q) 2BCJ - Q=1-353 (mouse) 2RGN - A/D=31-323 (mouse) 3AH8 - A=37-359 (mouse) 3OHM - A=35-359 (mouse) 4EKC - D/B=72-203 (mouse) 4EKD - B=72-203 (mouse) 4GNK - D/B=10-1234 E=934-1192 (mouse)

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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

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-a	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-u	ENRMEESkALFRTII
0	5		K345-u	RFVFAAVkDTILQLN
2	0		Y356	LQLNLKEYNLV____

	mouse
S53	GTGESGKSTFIkQMR
K57-u	SGKSTFIkQMRIIHG
K98-u	IRAMDTLkIPYkYEH
K102	DTLkIPYKYEHNkAH
K102-u	DTLkIPYkYEHNkAH
K107-u	PYkYEHNkAHAQLVR
K120-u	VREVDVEkVsAFENP
S122-p	EVDVEkVsAFENPYV
S154	RRREYQLSDSTkYYL
K158-u	YQLSDSTkYYLNDLD
S198	EYPFDLQSVIFRMVD
K252-u	ENRMEESkALFRTII
K345-u	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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