Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Glutamate receptor 2  

UniProtKB / Swiss-Prot ID :  GRIA2_RAT

Gene Name (Synonyms) : 
Gria2, Glur2  

Species :  Rattus norvegicus (Rat). 

Subcellular Localization :  Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Note=Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface  

Protein Function :  Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L- glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate. 

Transmembrane Topology (topPTM) : GRIA2_RAT 

Protein Sequence MQKIMHISVLLSPVLWGLIFGVSSNSIQIGGLFPRGADQEYSAFRVGMVQFSTSEFRLTPHIDNLEVANS...
Predicted Secondary Structure CHHHHHHHHHHHHHHHCCCCCCCCCEEEEEEECCCCCHHHHHHHHHHHHHHCCCCCEEEEEEEEEECCCH...
Protein Variant
LocationDescription
607Q -> R (in RNA edited version).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
256N-linked (GlcNAc...).FGGANVSGF
HCCCCEEEE
31.59UniProtKB
Link-
370N-linked (GlcNAc...).GKRINYTIN
CCCCCCEEE
31.74UniProtKB
Link-
661PhosphoserineAEDLSKQTE
HHHHCCCCC
34.73Phosphositeplus
Link-
683Phosphoserine (PKC_group)FFRRSKIAV
HHHHCCCCC
24.94PhosphoELM
Link-
683Phosphoserine; by PKC.FFRRSKIAV
HHHHCCCCC
24.94UniProtKB
Link-
697PhosphoserineTYMRSAEPS
HHHCCCCCC
22.06Phosphositeplus
Link-
717PhosphoserineRVRKSKGKY
HHHHCCCCE
35.76Phosphositeplus
Link-
717Phosphoserine (PKC_group;PKG/cGK_group)RVRKSKGKY
HHHHCCCCE
35.76PhosphoELM
Link-
717Phosphoserine; by PKG.RVRKSKGKY
HHHHCCCCE
35.76UniProtKB
Link-
863PhosphoserineSSQNSQNFA
CCCCCCCHH
20.90Phosphositeplus
Link-
876PhosphotyrosineGYNVYGIES
CCCEEEEEE
14.56Phosphositeplus
Link-
876Phosphotyrosine.GYNVYGIES
CCCEEEEEE
14.56UniProtKB
Link-
880PhosphoserineYGIESVKI
EEEEEEEC
27.13Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"X-ray structure, symmetry and mechanism of an AMPA-subtype glutamatereceptor.";
Sobolevsky A.I., Rosconi M.P., Gouaux E.;
Nature 462:745-756(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 25-847 IN COMPLEX WITHGLUTAMATE ANALOG, X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 413-796,FUNCTION, SUBUNIT, MEMBRANE TOPOLOGY, AND GLYCOSYLATION AT ASN-370.
"Subunit-selective N-terminal domain associations organize theformation of AMPA receptor heteromers.";
Rossmann M., Sukumaran M., Penn A.C., Veprintsev D.B., Babu M.M.,Greger I.H.;
EMBO J. 30:959-971(2011).
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 25-400, FUNCTION, SUBUNIT,DISULFIDE BOND, AND GLYCOSYLATION AT ASN-256 AND ASN-370.
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylation and regulation of the AMPA receptor by SRCfamily tyrosine kinases.";
Hayashi T., Huganir R.L.;
J. Neurosci. 24:6152-6160(2004).
Cited for: PHOSPHORYLATION AT TYR-876, AND TISSUE SPECIFICITY.
"Antibody specific for phosphorylated AMPA-type glutamate receptors atGluR2 Ser-696.";
Nakazawa K., Tadakuma T., Nokihara K., Ito M.;
Neurosci. Res. 24:75-86(1995).
Cited for: PHOSPHORYLATION AT SER-683 AND SER-717.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures