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G-alpha(z) (human)

Overview G-alpha(z) Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Belongs to the G-alpha family. G(i/o/t/z) subfamily. Note: This description may include information from UniProtKB. Protein type: G protein, heterotrimeric alpha G((i/o/t/z)); Endoplasmic reticulum; Nuclear envelope; G protein, heterotrimeric Cellular Component: extrinsic to internal side of plasma membrane; endoplasmic reticulum; plasma membrane; heterotrimeric G-protein complex; nuclear envelope Molecular Function: GTPase activity; signal transducer activity; GTP binding; metal ion binding; G-protein beta/gamma-subunit binding; receptor signaling protein activity; metabotropic serotonin receptor binding Biological Process: G-protein signaling, coupled to cAMP nucleotide second messenger; G-protein coupled receptor protein signaling pathway; GTP catabolic process; G-protein signaling, adenylate cyclase inhibiting pathway Reference #:  P19086 (UniProtKB) Alt. Names/Synonyms: G(x) alpha chain; GNAZ; guanine nucleotide binding protein (G protein), alpha z polypeptide; Guanine nucleotide-binding protein G(z) subunit alpha; Gz-alpha; transducin alpha Gene Symbols: GNAZ Molecular weight: 40,924 Da Basal Isoelectric point: 7.53  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(z)

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	Sites Implicated In
activation: S16‑p, S27‑p protein conformation: S16‑p, S27‑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
3	2		S16-p	EKEAARRsRRIDRHL
4	2		S27-p	DRHLRSEsQRQRREI
0	15		K51-u	SGKSTIVkQMKIIHS
0	1		K70	LEACKEYKPLIIyNA
0	10		Y75-p	EYKPLIIyNAIDSLT
0	1		R92	IRALAALRIDFHNPD
0	1		K117	LTGPAESKGEITPEL
0	3		S142-p	PGAQACFsRSSEyHL
0	8		Y147-p	CFsRSSEyHLEDNAA
0	8		Y155-p	HLEDNAAyyLNDLER
0	3		Y156-p	LEDNAAyyLNDLERI
0	3		Y168	ERIAAADYIPTVEDI
0	2		K189-u	TTGIVENkFTFKELT
0	1		K193	VENkFTFKELTFKMV
0	1		S229-p	IIFCVELsGyDLKLY
0	1		Y231-p	FCVELsGyDLKLYED
0	1		T263-p	NNNWFINtsLILFLN
0	1		S264-p	NNWFINtsLILFLNK
0	3		K272	LILFLNKKDLLAEKI
0	1		T341-p	QFVFDAVtDVIIQNN

	mouse
S16	EKEAARRSRRIDRHL
S27	DRHLRSESQRQRREI
K51-u	SGKSTIVkQMKIIHS
K70-u	LDACKEYkPLIIyNA
Y75-p	EYkPLIIyNAIDSLT
K92-u	IRALAALkIDFHNPD
K117-u	LTGPAESkGEITPEL
G142	PGAQACFGRSSEYHL
Y147	CFGRSSEYHLEDNAA
Y155	HLEDNAAYYLNDLER
Y156	LEDNAAYYLNDLERI
Y168	ERIAAPDYIPTVEDI
K189-u	TTGIVENkFTFkELT
K193-u	VENkFTFkELTFKMV
S229	IIFCVELSGYDLKLY
Y231	FCVELSGYDLKLYED
T263	NNNWFINTSLILFLN
S264	NNWFINTSLILFLNK
K272-u	LILFLNKkDLLAEKI
T341	QFVFDAVTDVIIQNN

	rat
S16	EKEAARRSRRIDRHL
S27	DRHLRSESQRQRREI
K51-u	SGKSTIVkQMKIIHS
K70	LEACKEYKPLIIyNA
Y75-p	EYKPLIIyNAIDSLT
K92	IRALAALKIDFHNPD
K117	LTGPAESKGEITPEL
G142	PGAQACFGRSSEyHL
Y147-p	CFGRSSEyHLEDNAA
Y155-p	HLEDNAAyyLNDLER
Y156-p	LEDNAAyyLNDLERI
Y168-p	ERIAAPDyIPTVEDI
K189	TTGIVENKFTFKELT
K193	VENKFTFKELTFKMV
S229	IIFCVELSGYDLKLY
Y231	FCVELSGYDLKLYED
T263	NNNWFINTSLILFLN
S264	NNWFINTSLILFLNK
K272	LILFLNKKDLLSEKI
T341	QFVFDAVTDVIIQNN

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