Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
G-alpha1(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-alpha1(i) 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: G-protein coupled receptor protein signaling pathway; synaptic transmission; response to peptide hormone stimulus; platelet activation; cell division; G-protein signaling, adenylate cyclase inhibiting pathway; blood coagulation; cell cycle
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
Select Structure to View Below

G-alpha1(i)

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


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 11 K29-u NLREDGEkAAREVkL
0 2 K35 EkAAREVKLLLLGAG
0 3 K35-u EkAAREVkLLLLGAG
0 47 K46-u LGAGESGkSTIVkQM
0 42 K51-u SGkSTIVkQMKIIHE
0 1 K54 STIVkQMKIIHEAGY
0 1 K67 GYSEEECKQYKAVVY
0 11 K92-u IRAMGRLkIDFGDSA
0 1 S98 LkIDFGDSARADDAR
0 9 K132 GVIKRLWKDSGVQAC
0 6 K180 DVLRTRVKTTGIVET
0 3 K192-u VETHFTFkDLHFkMF
0 3 K197-u TFkDLHFkMFDVGGQ
0 12 K248-u NRMHESMkLFDSICN
0 5 K271 IILFLNKKDLFEEKI
0 2 K277 KKDLFEEKIKKSPLT
0 8 K312 CQFEDLNKRKDTKEI
0 2 K345-u AVTDVIIkNNLkDCG
0 8 K349-u VIIkNNLkDCGLF__
  mouse

 
K29-u NLREDGEkAAREVkL
K35 EkAAREVKLLLLGAG
K35-u EkAAREVkLLLLGAG
K46-u LGAGESGkSTIVkQM
K51-u SGkSTIVkQMkIIHE
K54-u STIVkQMkIIHEAGY
K67-u GYSEEECkQYKAVVY
K92-u IRAMGRLkIDFGDsA
S98-p LkIDFGDsARADDAR
K132-u GVIKRLWkDSGVQAC
K180-u DVLRTRVkTTGIVET
K192-u VETHFTFkDLHFkMF
K197-u TFkDLHFkMFDVGGQ
K248-u NRMHESMkLFDSICN
K271-u IILFLNKkDLFEEkI
K277-u KkDLFEEkIKKSPLT
K312-u CQFEDLNkRKDTKEI
K345-u AVTDVIIkNNLkDCG
K349-u VIIkNNLkDCGLF__
  rat

 
K29-u NLREDGEkAAREVkL
K35-a EkAAREVkLLLLGAG
K35 EkAAREVKLLLLGAG
K46-u LGAGESGkSTIVkQM
K51-u SGkSTIVkQMKIIHE
K54 STIVkQMKIIHEAGY
K67 GYSEEECKQYKAVVY
K92 IRAMGRLKIDFGDAA
A98 LKIDFGDAARADDAR
K132 GVIKRLWKDSGVQAC
K180 DVLRTRVKTTGIVET
K192 VETHFTFKDLHFKMF
K197 TFKDLHFKMFDVGGQ
K248 NRMHESMKLFDSICN
K271 IILFLNKKDLFEEKI
K277 KKDLFEEKIKKSPLT
K312 CQFEDLNKRKDTKEI
K345 AVTDVIIKNNLKDCG
K349 VIIKNNLKDCGLF__
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.