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G-alpha(11) (human)

Overview G-alpha(11) a guanine nucleotide-binding protein of the G-alpha family. Acts as an activator of phospholipase C. Involved in signaling of gonadotropin-releasing hormone receptor, negatively regulating cell growth. Down-regulation may be involved in human breast cancers. 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 alpha G(q); G protein, heterotrimeric Cellular Component: extrinsic to internal side of plasma membrane; cytoplasm; plasma membrane; heterotrimeric G-protein complex Molecular Function: GTPase activity; signal transducer activity; GTP binding; G-protein-coupled receptor binding; metal ion binding; G-protein beta/gamma-subunit binding Biological Process: G-protein signaling, coupled to cAMP nucleotide second messenger; platelet activation; regulation of action potential; protein amino acid ADP-ribosylation; GTP catabolic process; heart development; pigmentation during development; dopamine receptor, phospholipase C activating pathway; blood coagulation; signal transduction; skeletal development; regulation of melanocyte differentiation Reference #:  P29992 (UniProtKB) Alt. Names/Synonyms: G alpha-11; G-protein subunit alpha-11; GA11; GNA-11; GNA11; guanine nucleotide binding protein (G protein), alpha 11 (Gq class); Guanine nucleotide-binding protein G(y) subunit alpha; Guanine nucleotide-binding protein subunit alpha-11; guanine nucleotide-binding protein, Gq class, GNA11 Gene Symbols: GNA11 Molecular weight: 42,123 Da Basal Isoelectric point: 5.51  Predict pI for various phosphorylation states CST Pathways:  Phospholipase Signaling  |  PI3K/Akt Signaling  |  Regulation of Microtubule Dynamics Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below G-alpha(11)

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	Sites Implicated In
molecular association, regulation: S154‑p receptor desensitization, altered: S154‑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
0	3		K27-u	RINAEIEkQLRRDKR
0	1		K57	SGKSTFIKQMRIIHG
0	1		K72	AGYSEEDKRGFTKLV
0	1		Y80-p	RGFTKLVyQNIFTAM
0	6		K102-u	ETLKILYkYEQNkAN
0	3		K107-u	LYkYEQNkANALLIR
0	1		K120	IREVDVEKVTTFEHQ
2	0		S154-p	RRREYQLsDSAkYYL
0	2		K158-u	YQLsDSAkYYLTDVD
0	1		T169-p	TDVDRIAtLGYLPTQ
0	2		K252-u	ENRMEESkALFRTII
0	1		Y291	LYSHLVDYFPEFDGP
0	12		K345-u	RFVFAAVkDTILQLN
2	0		Y356	LQLNLKEYNLV____

	mouse
K27-u	RINAEIEkQLRRDKR
K57-u	SGKSTFIkQMRIIHG
K72-u	AGYSEEDkRGFTKLV
Y80	RGFTKLVYQNIFTAM
K102-u	ETLKILYkYEQNkAN
K107-u	LYkYEQNkANALLIR
K120-u	IREVDVEkVTTFEHQ
S154	RRREFQLSDSAkYYL
K158-u	FQLSDSAkYYLTDVD
T169	TDVDRIATVGYLPTQ
K252-u	ENRMEESkALFRTII
Y291	LHSHLVDYFPEFDGP
K345-u	RFVFAAVkDTILQLN
Y356-p	LQLNLKEyNLV____

	rat
K27	RINAEIEKQLRRDKR
K57	SGKSTFIKQMRIIHG
K72	AGYSEEDKRGFTKLV
Y80	RGFTKLVYQNIFTAM
K102	DTLKIRYKYEQNKAN
K107	RYKYEQNKANALLIR
K120	IREVDVEKVTTFEHQ
S154	RRREFQLSDSAKYYL
K158	FQLSDSAKYYLTDVD
T169	TDVDRIATVGYLPTQ
K252	ENRMEESKALFRTII
Y291-p	LHSHLVDyFPEFDGP
K345-u	RFVFAAVkDTILQLN
Y356	LQLNLKEYNLV____

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