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Gene and Protein Information  |
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| Species | TM | P Loops | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
| Human | 3 | 1 | 883 | 4q32.1 | GRIA2 | glutamate ionotropic receptor AMPA type subunit 2 | 43,63 |
| Mouse | 3 | 1 | 883 | 3 E3 | Gria2 | glutamate receptor, ionotropic, AMPA2 (alpha 2) | 55 |
| Rat | 3 | 1 | 883 | 2q33 | Gria2 | glutamate ionotropic receptor AMPA type subunit 2 | 6,32,47,60 |
| Previous and Unofficial Names |
| GluR2 | GluRB | HBGR2 | AMPA-selective glutamate receptor 2 | glutamate receptor |
| Database Links |
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| Alphafold | P42262 (Hs), P23819 (Mm), P19491 (Rn) |
| ChEMBL Target | CHEMBL4016 (Hs), CHEMBL2096617 (Mm), CHEMBL3503 (Rn) |
| Ensembl Gene | ENSG00000120251 (Hs), ENSMUSG00000033981 (Mm), ENSRNOG00000054204 (Rn) |
| Entrez Gene | 2891 (Hs), 14800 (Mm), 29627 (Rn) |
| Human Protein Atlas | ENSG00000120251 (Hs) |
| KEGG Gene | hsa:2891 (Hs), mmu:14800 (Mm), rno:29627 (Rn) |
| OMIM | 138247 (Hs) |
| Pharos | P42262 (Hs) |
| RefSeq Nucleotide | NM_001083619 (Hs), NM_000826 (Hs), NM_013540 (Mm), NM_001083806 (Mm), NM_001039195 (Mm), NM_017261 (Rn), NM_001083811 (Rn) |
| RefSeq Protein | NP_000817 (Hs), NP_001077088 (Hs), NP_001077275 (Mm), NP_038568 (Mm), NP_001034284 (Mm), NP_001077280 (Rn), NP_058957 (Rn) |
| UniProtKB | P42262 (Hs), P23819 (Mm), P19491 (Rn) |
| Wikipedia | GRIA2 (Hs) |
| Selected 3D Structures |
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| Natural/Endogenous Ligands |
| L-glutamic acid |
Download all structure-activity data for this target as a CSV file 
| Agonists | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| View species-specific antagonist tables | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Channel Blockers | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Channel Blocker Comments | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| GluA2 is also blocked by intracellular polyamines. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Allosteric Modulators | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Allosteric Modulator Comments | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Piracetam and aniracetam are examples of pyrrolidinones. Cyclothiazide, S18986, and IDRA-21 are examples of benzothiadiazides. CX516 and CX546 are examples of benzylpiperidines. LY392098, LY404187 and LY503430 are examples of biarylpropylsulfonamides. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Immuno Process Associations | ||
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| Physiological Consequences of Altering Gene Expression
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| Biologically Significant Variants
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| Biologically Significant Variant Comments | ||||||||||||||
| Structure: a GluA2 subunit consists of 1 extracellular N-terminal domain, 1 ligand binding domain (S1 (a domain of the N-terminal region) + S2 (a domain of the extracellular loop between M3 and M4)), 3 membrane-spanning domains (M1, M3, M4), 1 cytoplasmic re-entrant loop (M2) and 1 C-terminal intracellular domain. GluA2 exists as several splice variants: 2 C-terminal splice variants: a minor one with a long C-terminal domain (GluA2L) and the predominant variant with a short C-terminal domain. GluA2 exists as alternatively spliced ‘flip’ and ‘flop’ isoforms which differ with respect to a cassette of 35 amino acids in the extracellular loop between M3 and M4 [32,60]. Tetrameric receptors assembled from the ‘flip’ isoform enter the desensitized state more slowly, and recover more quickly, than those formed from the ‘flop’ isoform [34,46,60]. In addition, RNA editing by adenosine deaminase type 2 (CAG->CIG), which occurs in virtually all GluA2 subunits, changes residue 607 within the channel pore from glutamine to arginine (at the ‘Q/R site’) [61]. GluA1, GluA3 and GluA4 are not subject to this form of editing and thus retain glutamine at the Q/R site. AMPA receptors that lack edited GluA2 subunits are (i) of relatively high single channel conductance [5]; (ii) permeable to Ca2+ [11,26], (iii) blocked by intracellular polyamines, causing inward rectification at depolarized potentials and (iv) blocked by extracellular argiotoxin and Joro spider toxins [27]. Q/R editing also influences the oligomerisation and trafficking of GluA2 subunits [23]. RNA editing (AGA->IGA) also occurs at a codon for arginine (unedited), or glycine (edited) at a locus with the extracellular loop that immediately precedes the alternatively spliced ‘flip’ and ‘flop’ modules. Edited channels recover from desensitization at a faster rate than those that are unedited [39]. GluA2 may express with long, or short, C-termini as a consequence of alternative splicing, the short form is predominant in mouse brain [35]. |
| General Comments |
| For general reviews please see:[3,28] |
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