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Protein Page:
G-alpha i1 (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 i1 Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-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. Interacts with GPSM1. Interacts with RGS12. Interacts (via active GTP- or inactive GDP-bound forms) with RGS14 (via RGS and GoLoco domains); the interaction occurs in the centrosomes. Interacts (GDP-bound form) with RIC8A (via C-terminus). Interacts with DRD2. 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; G protein, heterotrimeric alpha G((i/o/t/z)); G protein, heterotrimeric
Cellular Component: centrosome; extrinsic to internal side of plasma membrane; lysosomal membrane; cytoplasm; plasma membrane; heterotrimeric G-protein complex; midbody; nucleus
Molecular Function: GTPase activity; protein binding; signal transducer activity; GTP binding; metal ion binding; G-protein beta/gamma-subunit binding; metabotropic serotonin receptor binding
Biological Process: response to peptide hormone stimulus; platelet activation; synaptic transmission; G-protein coupled receptor protein signaling pathway; cell division; GTP catabolic process; G-protein signaling, adenylate cyclase inhibiting pathway; cell cycle; blood coagulation
Reference #:  P63096 (UniProtKB)
Alt. Names/Synonyms: Adenylate cyclase-inhibiting G alpha protein; Gi; Gi1 protein alpha subunit; GNAI1; guanine nucleotide binding protein (G protein), alpha inhibiting activity polypeptide 1; Guanine nucleotide-binding protein G(i) subunit alpha-1
Gene Symbols: GNAI1
Molecular weight: 40,361 Da
Basal Isoelectric point: 5.69  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Hedgehog Signaling  |  Microtubule Dynamics  |  Parkinson's Disease  |  Phospholipase Signaling  |  PI3K/Akt Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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G-alpha i1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
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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 11 K29-ub NLREDGEkAAREVkL
0 2 K35 EkAAREVKLLLLGAG
0 3 K35-ub EkAAREVkLLLLGAG
0 2 S44-p LLLGAGEsGkSTIVk
0 47 K46-ub LGAGEsGkSTIVkQM
0 42 K51-ub sGkSTIVkQMKIIHE
0 1 K54 STIVkQMKIIHEAGY
0 1 K67 GYSEEECKQYKAVVY
0 11 K92-ub IRAMGRLkIDFGDSA
0 1 S98 LkIDFGDSARADDAR
0 1 K128 AELAGVIKRLWKDSG
0 9 K132 GVIKRLWKDSGVQAC
0 1 Y155-p LNDSAAYyLNDLDRI
0 6 K180 DVLRTRVKTTGIVET
0 3 K192-ub VETHFTFkDLHFkMF
0 1 K197 TFkDLHFKMFDVGGQ
0 3 K197-ub TFkDLHFkMFDVGGQ
0 1 K248 NRMHESMKLFDsICN
0 12 K248-ub NRMHESMkLFDsICN
0 2 S252-p ESMkLFDsICNNKWF
0 5 K271 IILFLNKKDLFEEKI
0 2 K277 KKDLFEEKIKKSPLT
0 1 Y290 LTICYPEYAGSNTYE
0 1 S293 CYPEYAGSNTYEEAA
0 8 K312 CQFEDLNKRKDTKEI
0 2 K345-ub AVTDVIIkNNLkDCG
0 8 K349-ub VIIkNNLkDCGLF__
  mouse

 
K29-ub NLREDGEkAAREVkL
K35 EkAAREVKLLLLGAG
K35-ub EkAAREVkLLLLGAG
S44-p LLLGAGEsGkSTIVk
K46-ub LGAGEsGkSTIVkQM
K51-ub sGkSTIVkQMkIIHE
K54-ub STIVkQMkIIHEAGY
K67-ub GYSEEECkQYKAVVY
K92-ub IRAMGRLkIDFGDsA
S98-p LkIDFGDsARADDAR
K128-ac AELAGVIkRLWkDSG
K132-ub GVIkRLWkDSGVQAC
Y155 LNDSAAYYLNDLDRI
K180-ub DVLRTRVkTTGIVET
K192-ub VETHFTFkDLHFkMF
K197 TFkDLHFKMFDVGGQ
K197-ub TFkDLHFkMFDVGGQ
K248 NRMHESMKLFDsICN
K248-ub NRMHESMkLFDsICN
S252-p ESMkLFDsICNNKWF
K271-ub IILFLNKkDLFEEkI
K277-ub KkDLFEEkIKKSPLT
Y290-p LTICYPEyAGsNTYE
S293-p CYPEyAGsNTYEEAA
K312-ub CQFEDLNkRKDTKEI
K345-ub AVTDVIIkNNLkDCG
K349-ub VIIkNNLkDCGLF__
  rat

 
K29-ub NLREDGEkAAREVkL
K35-ac EkAAREVkLLLLGAG
K35 EkAAREVKLLLLGAG
S44 LLLGAGESGkSTIVk
K46-ub LGAGESGkSTIVkQM
K51-ub SGkSTIVkQMKIIHE
K54 STIVkQMKIIHEAGY
K67 GYSEEECKQYKAVVY
K92 IRAMGRLKIDFGDAA
A98 LKIDFGDAARADDAR
K128 AELAGVIKRLWKDSG
K132 GVIKRLWKDSGVQAC
Y155 LNDSAAYYLNDLDRI
K180 DVLRTRVKTTGIVET
K192 VETHFTFKDLHFkMF
K197-ac TFKDLHFkMFDVGGQ
K197 TFKDLHFKMFDVGGQ
K248-ac NRMHESMkLFDSICN
K248 NRMHESMKLFDSICN
S252 ESMkLFDSICNNKWF
K271 IILFLNKKDLFEEKI
K277 KKDLFEEKIKKSPLT
Y290 LTICYPEYAGSNTYE
S293 CYPEYAGSNTYEEAA
K312 CQFEDLNKRKDTKEI
K345 AVTDVIIKNNLKDCG
K349 VIIKNNLKDCGLF__
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