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Protein Page:
G-alpha 13 (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 13 a guanine nucleotide-binding protein of the G12 class of G-alpha proteins. Activates Rho. Protein kinase A blocks Rho activation by phosphorylation of G-alpha(13). Heterotrimeric G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Regulates cytoplasmic as well as nuclear signaling events such as activation of the Jun N-terminal kinase signaling module, Na+/H+ exchangers, focal adhesion assemblies, and transcriptional activation of specific primary response genes. Note: This description may include information from UniProtKB.
Protein type: G protein; G protein, heterotrimeric alpha G(12); G protein, heterotrimeric
Cellular Component: membrane; brush border membrane; plasma membrane; melanosome; heterotrimeric G-protein complex; nucleus
Molecular Function: GTPase activity; signal transducer activity; protein binding; GTP binding; metal ion binding; G-protein beta/gamma-subunit binding; type 1 angiotensin receptor binding; D5 dopamine receptor binding
Biological Process: phospholipase D activation; platelet activation; in utero embryonic development; signal transduction; G-protein signaling, adenylate cyclase activating pathway; regulation of cell migration; Rho protein signal transduction; patterning of blood vessels; regulation of cell shape; elevation of cytosolic calcium ion concentration; GTP catabolic process; cell motility; blood coagulation; cell differentiation
Reference #:  Q14344 (UniProtKB)
Alt. Names/Synonyms: G alpha-13; G-protein subunit alpha-13; G13; GNA13; guanine nucleotide binding protein (G protein), alpha 13; Guanine nucleotide-binding protein subunit alpha-13; MGC46138
Gene Symbols: GNA13
Molecular weight: 44,050 Da
Basal Isoelectric point: 8.12  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Microtubule Dynamics  |  Phospholipase Signaling  |  PI3K/Akt Signaling  |  SAPK/JNK Signaling Cascades
Select Structure to View Below

G-alpha 13

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: T203‑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 1 S9-p ADFLPSRsVLSVCFP
0 2 T43-p KCLSREKtyVKRLVK
0 1 Y44-p CLSREKtyVKRLVKI
0 3 Y145 ETRVFLQYLPAIRAL
0 1 K175 FQLGESVKYFLDNLD
0 1 K183-ub YFLDNLDkLGEPDYI
1 1 T203-p ILLARRPtKGIHEYD
0 3 K214-ub HEYDFEIkNVPFKMV
0 1 K219 EIkNVPFKMVDVGGQ
0 1 S285-p NRVFSNVsIILFLNK
0 1 K363-ac RLVFRDVkDTILHDN
0 1 K372-ac TILHDNLkQLMLQ__
0 6 K372-ub TILHDNLkQLMLQ__
  mouse

 
S9 ADFLPSRSVLSVCFP
T43-p KCLSREKtYVKRLVK
Y44 CLSREKtYVKRLVKI
Y145 ETRVFLQYLPAIRAL
K175-ub FQLGESVkYFLDNLD
K183 YFLDNLDKLGVPDYI
T203 ILLARRPTKGIHEYD
K214-ub HEYDFEIkNVPFkMV
K219-ub EIkNVPFkMVDVGGQ
S285 NRVFSNVSIILFLNK
K363 RLVFRDVKDTILHDN
K372 TILHDNLKQLMLQ__
K372 TILHDNLKQLMLQ__
  rat

 
S9 ADFLPSRSVLSVCFP
T43 KCLSREKTYVKRLVK
Y44 CLSREKTYVKRLVKI
Y145-p ETRVFLQyLPAIRAL
K175 FQLGESVKYFLDNLD
K183 YFLDNLDKLGVPDYI
T203 ILLARRPTKGIHEYD
K214 HEYDFEIKNVPFKMV
K219 EIKNVPFKMVDVGGQ
S285 NRVFSNVSIILFLNK
K363-ac RLVFRDVkDTILHDN
K372 TILHDNLKQLMLQ__
K372 TILHDNLKQLMLQ__
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