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Protein Page:
G-alpha(11) (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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, heterotrimeric; G protein; G protein, heterotrimeric alpha G(q)
Cellular Component: extrinsic to internal side of plasma membrane; lysosomal membrane; cytoplasm; plasma membrane; heterotrimeric G-protein complex
Molecular Function: GTPase activity; signal transducer activity; G-protein-coupled receptor binding; GTP 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; heart development; pigmentation during development; dopamine receptor, phospholipase C activating pathway; signal transduction; blood coagulation; 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:  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(11)

Protein Structure Not Found.


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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
 

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

 
0 3 K27-u RINAEIEkQLRRDKR
0 1 K72 AGYSEEDKRGFTKLV
0 1 Y80-p RGFTKLVyQNIFTAM
0 6 K102-u ETLKILYkYEQNkAN
0 1 Y103 TLKILYkYEQNkANA
0 3 K107-u LYkYEQNkANALLIR
0 1 K120 IREVDVEKVTTFEHQ
2 0 S154-p RRREYQLsDSAkYYL
0 2 K158-u YQLsDSAkYYLTDVD
0 2 K252-u ENRMEESkALFRTII
0 12 K345-u RFVFAAVkDTILQLN
2 0 Y356 LQLNLKEYNLV____
  mouse

 
K27-u RINAEIEkQLRRDKR
K72-u AGYSEEDkRGFTKLV
Y80 RGFTKLVYQNIFTAM
K102-u ETLKILYkyEQNkAN
Y103-p TLKILYkyEQNkANA
K107-u LYkyEQNkANALLIR
K120-u IREVDVEkVTTFEHQ
S154 RRREFQLSDSAkYYL
K158-u FQLSDSAkYYLTDVD
K252-u ENRMEESkALFRTII
K345-u RFVFAAVkDTILQLN
Y356-p LQLNLKEyNLV____
  rat

 
K27 RINAEIEKQLRRDKR
K72 AGYSEEDKRGFTKLV
Y80 RGFTKLVYQNIFTAM
K102 DTLKIRYKYEQNKAN
Y103 TLKIRYKYEQNKANA
K107 RYKYEQNKANALLIR
K120 IREVDVEKVTTFEHQ
S154 RRREFQLSDSAKYYL
K158 FQLSDSAKYYLTDVD
K252 ENRMEESKALFRTII
K345-u RFVFAAVkDTILQLN
Y356 LQLNLKEYNLV____
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