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Protein Page:
G-alpha3(i) (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-alpha3(i) Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(k) is the stimulatory G protein of receptor- regulated K(+) channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division. Defects in GNAI3 are the cause of auriculocondylar syndrome 1 (ARCND1). ARCND1 is an autosomal dominant craniofacial malformation syndrome characterized by variable mandibular anomalies, including mild to severe micrognathia, temporomandibular joint ankylosis, cleft palate, and a characteristic ear malformation that consists of separation of the lobule from the external ear, giving the appearance of a question mark (question-mark ear). Other frequently described features include prominent cheeks, cupped and posteriorly rotated ears, preauricular tags, and microstomia. Belongs to the G-alpha family. G(i/o/t/z) subfamily. Note: This description may include information from UniProtKB.
Protein type: G protein; G protein, heterotrimeric alpha G((i/o/t/z)); G protein, heterotrimeric
Cellular Component: Golgi apparatus; centrosome; extrinsic to internal side of plasma membrane; lysosomal membrane; cytoplasm; plasma membrane; heterotrimeric G-protein complex; midbody; lipid raft
Molecular Function: GTPase activity; protein domain specific binding; signal transducer activity; GTP binding; metal ion binding; G-protein beta/gamma-subunit binding; GTPase activating protein binding; metabotropic serotonin receptor binding
Biological Process: vesicle fusion; synaptic transmission; platelet activation; transport; cell division; negative regulation of adenylate cyclase activity; G-protein signaling, adenylate cyclase inhibiting pathway; cell cycle; blood coagulation
Reference #:  P08754 (UniProtKB)
Alt. Names/Synonyms: 87U6; FLJ26559; G(i) alpha-3; GNAI3; guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 3; Guanine nucleotide-binding protein G(k) subunit alpha
Gene Symbols: GNAI3
Molecular weight: 40,532 Da
Basal Isoelectric point: 5.5  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Hedgehog Signaling  |  Microtubule Dynamics  |  Parkinson's Disease  |  Phospholipase Signaling  |  PI3K/Akt Signaling
Select Structure to View Below

G-alpha3(i)

Protein Structure Not Found.


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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 2 K29-u NLREDGEkAAKEVkL
0 3 K35-u EkAAKEVkLLLLGAG
0 1 S44-p LLLGAGEsGkSTIVk
0 46 K46-u LGAGEsGkSTIVkQM
0 36 K51-u sGkSTIVkQMKIIHE
0 52 Y61-p KIIHEDGysEDECKQ
0 14 S62-p IIHEDGysEDECKQy
0 40 Y69-p sEDECKQyKVVVYSN
0 3 K92-u IRAMGRLkIDFGEAA
0 1 A98 LkIDFGEAARADDAR
0 1 K128-u PELAGVIkRLWRDGG
0 2 Y167-p DRISQSNyIPTQQDV
0 6 K180 DVLRTRVKTTGIVET
0 8 K192-u VETHFTFkDLYFkMF
0 1 K197-u TFkDLYFkMFDVGGQ
0 2 S206 FDVGGQRSERKKWIH
0 12 K248-u NRMHESMkLFDsICN
0 1 S252-p ESMkLFDsICNNKWF
0 5 K271 IILFLNKKDLFEEKI
0 2 K277 KKDLFEEKIKRSPLT
0 2 K345-u AVTDVIIkNNLkECG
0 7 K349-u VIIkNNLkECGLy__
0 194 Y354-p NLkECGLy_______
  mouse

 
K29 NLREDGEKAAKEVkL
K35-u EKAAKEVkLLLLGAG
S44-p LLLGAGEsGkSTIVk
K46-u LGAGEsGkSTIVkQM
K51-u sGkSTIVkQMKIIHE
Y61 KIIHEDGYsEDECKQ
S62-p IIHEDGYsEDECKQy
Y69-p sEDECKQyKVVVYSN
K92-u IRAMGRLkIDFGEsA
S98-p LkIDFGEsARADDAR
K128 SELAGVIKRLWRDGG
Y167 DRISQTNYIPTQQDV
K180-u DVLRTRVkTTGIVET
K192-u VETHFTFkELYFKMF
K197 TFkELYFKMFDVGGQ
S206-p FDVGGQRsERKKWIH
K248-u NRMHESMkLFDsICN
S252-p ESMkLFDsICNNKWF
K271-u IILFLNKkDLFEEkI
K277-u KkDLFEEkIKRSPLT
K345-u AVTDVIIkNNLkECG
K349-u VIIkNNLkECGLy__
Y354-p NLkECGLy_______
  rat

 
K29 NLREDGEKAAKEVKL
K35 EKAAKEVKLLLLGAG
S44 LLLGAGESGKSTIVK
K46 LGAGESGKSTIVKQM
K51 SGKSTIVKQMKIIHE
Y61 KIIHEDGYSEDECKQ
S62 IIHEDGYSEDECKQY
Y69 SEDECKQYKVVVYSN
K92 IRAMGRLKIDFGEAA
A98 LKIDFGEAARADDAR
K128 SELAGVIKRLWRDGG
Y167 DRISQTNYIPTQQDV
K180 DVLRTRVKTTGIVET
K192 VETHFTFKELYFKMF
K197 TFKELYFKMFDVGGQ
S206 FDVGGQRSERKKWIH
K248 NRMHESMKLFDSICN
S252 ESMKLFDSICNNKWF
K271 IILFLNKKDLFEEKI
K277 KKDLFEEKIKRSPLT
K345 AVTDVIIKNNLKECG
K349 VIIKNNLKECGLY__
Y354 NLKECGLY_______
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