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Protein Page:
GluR4 (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
GluR4 an integral membrane protein belonging to the glutamate-gated ion channel family. L-glutamate (Glu) acts as an excitatory neurotransmitter at many synapses in the central nervous system. Glutamate receptors are heteromeric protein complexes with multiple subunits, each possessing transmembrane regions, and all arranged to form a ligand-gated ion channel. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA(quisqualate) > glutamate > kainate. Each of the four GluR proteins (GRIA1-4) include flip and flop isoforms generated by alternative RNA splicing. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, multi-pass; Membrane protein, integral; Channel, ligand-gated
Cellular Component: postsynaptic membrane; dendrite; plasma membrane; cell junction
Molecular Function: extracellular-glutamate-gated ion channel activity; ionotropic glutamate receptor activity; alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity
Biological Process: synaptic transmission; transport; glutamate signaling pathway; ionotropic glutamate receptor signaling pathway
Reference #:  P48058 (UniProtKB)
Alt. Names/Synonyms: AMPA-selective glutamate receptor 4; GluR-4; GluR-D; GLUR4; GLUR4C; GLURD; Glutamate receptor 4; Glutamate receptor ionotropic, AMPA 4; glutamate receptor, ionotrophic, AMPA 4; GRIA4
Gene Symbols: GRIA4
Molecular weight: 100,871 Da
Basal Isoelectric point: 8.32  Predict pI for various phosphorylation states
CST Pathways:  Alzheimer's Disease  |  Parkinson's Disease
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

GluR4

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: S862‑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

► Hide Isoforms
 
0 1 S314-p VMAETFRsLRRQKID
1 0 S718 GVARVRKSKGKFAFL
5 5 S862-p IRNKARLsITGSVGE
0 2 T864 NKARLsITGSVGENG
0 3 S866 ARLsITGSVGENGRV
0 1 T875 GENGRVLTPDCPKAV
0 1 K880 VLTPDCPKAVHTGTA
  GluR4 iso2  
S314 VMAETFRSLRRQKID
- gap
- gap
- gap
- gap
- gap
- gap
  GluR4 iso4  
S314 VMAETFRSLRRQKID
S718 GVARVRKSKGKFAFL
- gap
- gap
- gap
- gap
- gap
  mouse

► Hide Isoforms
 
S314 VMAETFRSLRRQKID
S718 GVARVRKSKGKFAFL
S862-p IRNKARLsItGsVGE
T864-p NKARLsItGsVGENG
S866-p ARLsItGsVGENGRV
T875-p GENGRVLtPDCPkAV
K880-u VLtPDCPkAVHTGTA
  GluR4 iso2  
S314 VMAETFRSLRRQKID
S718 GVARVRKSKGKFAFL
S862 IRNKARLSITGSVGE
T864 NKARLSITGSVGENG
S866 ARLSITGSVGENGRV
T875 GENGRVLTPDCPKAV
K880 VLTPDCPKAVHTGTA
  rat

 
S314 VMAETFRSLRRQKID
S718-p GVARVRKsKGKFAFL
S862-p TRNKARLsITGSVGE
T864 NKARLsITGSVGENG
S866 ARLsITGSVGENGRV
T875 GENGRVLTPDCPKAV
K880 VLTPDCPKAVHTGTA
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