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Protein Page:
G-alpha 11 (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 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, heterotrimeric alpha G(q); G protein
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; 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; 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:  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-ub RINAEIEkQLRRDKR
0 1 K57 SGKSTFIKQMRIIHG
0 1 K72 AGYSEEDKRGFTKLV
0 1 Y80-p RGFTKLVyQNIFTAM
0 1 K102 ETLKILYKYEQNkAN
0 6 K102-ub ETLKILYkYEQNkAN
0 1 Y103 TLKILYkYEQNkANA
0 3 K107-ub LYkYEQNkANALLIR
0 1 K120 IREVDVEKVTTFEHQ
2 0 S154-p RRREYQLsDSAkYYL
0 2 K158-ub YQLsDSAkYYLTDVD
0 1 T169-p TDVDRIAtLGYLPTQ
0 2 K252-ub ENRMEESkALFRTII
0 1 Y291 LYSHLVDYFPEFDGP
0 12 K345-ub RFVFAAVkDTILQLN
2 0 Y356 LQLNLKEYNLV____
  mouse

 
K27-ub RINAEIEkQLRRDKR
K57-ub SGKSTFIkQMRIIHG
K72-ub AGYSEEDkRGFTKLV
Y80 RGFTKLVYQNIFTAM
K102-ac ETLKILYkyEQNkAN
K102-ub ETLKILYkyEQNkAN
Y103-p TLKILYkyEQNkANA
K107-ub LYkyEQNkANALLIR
K120-ub IREVDVEkVTTFEHQ
S154 RRREFQLSDSAkYYL
K158-ub FQLSDSAkYYLTDVD
T169 TDVDRIATVGYLPTQ
K252-ub ENRMEESkALFRTII
Y291 LHSHLVDYFPEFDGP
K345-ub RFVFAAVkDTILQLN
Y356-p LQLNLKEyNLV____
  rat

 
K27 RINAEIEKQLRRDKR
K57 SGKSTFIKQMRIIHG
K72 AGYSEEDKRGFTKLV
Y80 RGFTKLVYQNIFTAM
K102 DTLKIRYKYEQNKAN
K102 DTLKIRYKYEQNKAN
Y103 TLKIRYKYEQNKANA
K107 RYKYEQNKANALLIR
K120 IREVDVEKVTTFEHQ
S154 RRREFQLSDSAKYYL
K158 FQLSDSAKYYLTDVD
T169 TDVDRIATVGYLPTQ
K252 ENRMEESKALFRTII
Y291-p LHSHLVDyFPEFDGP
K345-ub RFVFAAVkDTILQLN
Y356 LQLNLKEYNLV____
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