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Protein Page:
G-alpha(z) (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(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; G protein, heterotrimeric; Nuclear envelope
Cellular Component: endoplasmic reticulum; plasma membrane; heterotrimeric G-protein complex; nuclear envelope; cytosol
Molecular Function: GTPase activity; signal transducer activity; GTP binding; metal ion binding; receptor signaling protein activity; G-protein beta/gamma-subunit binding; 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:  Microtubule Dynamics  |  Phospholipase Signaling  |  PI3K/Akt Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

G-alpha(z)

Protein Structure Not Found.


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Sites Implicated In
activity, induced: 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
 

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

 
3 2 S16-p EKEAARRsRRIDRHL
4 2 S27-p DRHLRSEsQRQRREI
0 1 T41-p IKLLLLGtSNSGKST
0 15 K51-ub SGKSTIVkQMKIIHS
0 1 K70 LEACKEYKPLIIYNA
0 10 Y75 EYKPLIIYNAIDSLT
0 1 R92 IRALAALRIDFHNPD
0 1 K117 LTGPAESKGEITPEL
0 3 S142-p PGAQACFsRSSEYHL
0 1 S144 AQACFsRSSEYHLED
0 2 S145 QACFsRSSEYHLEDN
0 6 Y147 CFsRSSEYHLEDNAA
0 7 Y155 HLEDNAAYYLNDLER
0 2 Y156 LEDNAAYYLNDLERI
0 3 Y168 ERIAAADYIPTVEDI
0 2 K189-ub 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
T41 IKLLLLGTSNSGKST
K51-ub SGKSTIVkQMKIIHS
K70-ub LDACKEYkPLIIyNA
Y75-p EYkPLIIyNAIDSLT
K92-ub IRALAALkIDFHNPD
K117-ub LTGPAESkGEITPEL
G142 PGAQACFGRSSEYHL
S144 AQACFGRSSEYHLED
S145 QACFGRSSEYHLEDN
Y147 CFGRSSEYHLEDNAA
Y155 HLEDNAAYYLNDLER
Y156 LEDNAAYYLNDLERI
Y168 ERIAAPDYIPTVEDI
K189-ub TTGIVENkFTFkELT
K193-ub VENkFTFkELTFKMV
S229 IIFCVELSGYDLKLY
Y231 FCVELSGYDLKLYED
T263 NNNWFINTSLILFLN
S264 NNWFINTSLILFLNK
K272-ub LILFLNKkDLLAEKI
T341 QFVFDAVTDVIIQNN
  rat

 
S16 EKEAARRSRRIDRHL
S27 DRHLRSESQRQRREI
T41 IKLLLLGTSNSGKST
K51-ub SGKSTIVkQMKIIHS
K70 LEACKEYKPLIIyNA
Y75-p EYKPLIIyNAIDSLT
K92 IRALAALKIDFHNPD
K117 LTGPAESKGEITPEL
G142 PGAQACFGRssEyHL
S144-p AQACFGRssEyHLED
S145-p QACFGRssEyHLEDN
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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