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P42262

- GRIA2_HUMAN

UniProt

P42262 - GRIA2_HUMAN

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Protein

Glutamate receptor 2

Gene
GRIA2, GLUR2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei471 – 4711Glutamate
Binding sitei506 – 5061Glutamate
Binding sitei726 – 7261Glutamate

GO - Molecular functioni

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: UniProtKB
  2. extracellular-glutamate-gated ion channel activity Source: RefGenome
  3. ionotropic glutamate receptor activity Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. ionotropic glutamate receptor signaling pathway Source: UniProtKB
  2. ion transmembrane transport Source: GOC
  3. signal transduction Source: ProtInc
  4. synaptic transmission Source: Reactome
  5. synaptic transmission, glutamatergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_18338. Activation of AMPA receptors.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
SignaLinkiP42262.

Protein family/group databases

TCDBi1.A.10.1.13. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor 2
Short name:
GluR-2
Alternative name(s):
AMPA-selective glutamate receptor 2
GluR-B
GluR-K2
Glutamate receptor ionotropic, AMPA 2
Short name:
GluA2
Gene namesi
Name:GRIA2
Synonyms:GLUR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:4572. GRIA2.

Subcellular locationi

Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein
Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression By similarity.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 543519Extracellular By similarityAdd
BLAST
Transmembranei544 – 56421Helical; By similarityAdd
BLAST
Topological domaini565 – 59127Cytoplasmic By similarityAdd
BLAST
Intramembranei592 – 60716Helical; Pore-forming; By similarityAdd
BLAST
Intramembranei608 – 6103 By similarity
Topological domaini611 – 6166Cytoplasmic By similarity
Transmembranei617 – 63721Helical; By similarityAdd
BLAST
Topological domaini638 – 812175Extracellular By similarityAdd
BLAST
Transmembranei813 – 83321Helical; Name=M4Add
BLAST
Topological domaini834 – 88350Cytoplasmic By similarityAdd
BLAST

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: UniProtKB
  2. cell junction Source: UniProtKB-KW
  3. dendrite Source: RefGenome
  4. endocytic vesicle membrane Source: Reactome
  5. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  6. integral component of plasma membrane Source: UniProtKB
  7. plasma membrane Source: Reactome
  8. postsynaptic membrane Source: RefGenome
  9. synaptic vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Endoplasmic reticulum, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28967.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed predictionAdd
BLAST
Chaini25 – 883859Glutamate receptor 2PRO_0000011532Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi78 ↔ 3302 Publications
Glycosylationi256 – 2561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi370 – 3701N-linked (GlcNAc...)1 Publication
Glycosylationi406 – 4061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi413 – 4131N-linked (GlcNAc...) Reviewed prediction
Lipidationi610 – 6101S-palmitoyl cysteine By similarity
Modified residuei683 – 6831Phosphoserine; by PKC By similarity
Modified residuei717 – 7171Phosphoserine; by PKG By similarity
Disulfide bondi739 ↔ 7942 Publications
Lipidationi836 – 8361S-palmitoyl cysteine By similarity
Modified residuei876 – 8761Phosphotyrosine By similarity
Modified residuei880 – 8801Phosphoserine By similarity

Post-translational modificationi

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-610 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity.

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP42262.
PRIDEiP42262.

PTM databases

PhosphoSiteiP42262.

Expressioni

Gene expression databases

ArrayExpressiP42262.
BgeeiP42262.
CleanExiHS_GRIA2.
GenevestigatoriP42262.

Organism-specific databases

HPAiCAB006830.
CAB007812.
CAB012981.
HPA008441.

Interactioni

Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CSPG4. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to AMPAR complex disassembly By similarity. Interacts with PICK1 (via PDZ domain). Interacts with PRKCABP and GRIP2 By similarity. Interacts with GRIA1 and SYNDIG1 By similarity. Interacts with LRFN1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes By similarity. Found in a complex with GRIA1, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 By similarity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NSFP464592EBI-3909876,EBI-712251

Protein-protein interaction databases

BioGridi109148. 17 interactions.
DIPiDIP-42852N.
IntActiP42262. 2 interactions.
MINTiMINT-2791741.
STRINGi9606.ENSP00000264426.

Structurei

Secondary structure

1
883
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 348
Helixi38 – 5114
Beta strandi58 – 658
Helixi70 – 8314
Beta strandi88 – 903
Turni94 – 963
Helixi97 – 10711
Beta strandi111 – 1133
Beta strandi125 – 1273
Helixi133 – 14210
Beta strandi147 – 1526
Helixi159 – 17113
Beta strandi174 – 1796
Helixi188 – 1914
Helixi193 – 2019
Beta strandi206 – 2116
Helixi213 – 22513
Helixi230 – 2323
Beta strandi234 – 2374
Beta strandi239 – 2413
Helixi247 – 2493
Beta strandi256 – 2627
Helixi268 – 27710
Turni282 – 2843
Beta strandi289 – 2913
Helixi295 – 31622
Helixi341 – 3499
Beta strandi353 – 3553
Beta strandi358 – 3603
Beta strandi366 – 3683
Beta strandi373 – 3797
Beta strandi382 – 3909
Turni391 – 3933
Beta strandi394 – 3974
Beta strandi416 – 4205
Turni424 – 4263
Beta strandi427 – 4293
Helixi433 – 4353
Helixi438 – 4414
Beta strandi442 – 4443
Helixi445 – 45713
Beta strandi461 – 4655
Turni476 – 4783
Helixi483 – 4897
Beta strandi494 – 4963
Helixi504 – 5074
Beta strandi510 – 5123
Beta strandi516 – 5194
Beta strandi521 – 5266
Helixi657 – 6615
Beta strandi664 – 6718
Helixi675 – 6828
Helixi686 – 69712
Beta strandi704 – 7063
Helixi707 – 71610
Turni717 – 7193
Beta strandi720 – 7267
Helixi727 – 7348
Beta strandi741 – 7455
Beta strandi751 – 7533
Beta strandi756 – 7583
Helixi764 – 77613
Helixi779 – 78810
Turni789 – 7913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WJWX-ray1.80A25-412[»]
2WJXX-ray4.10A/B/C25-412[»]
2XHDX-ray1.80A/B413-527[»]
A/B653-796[»]
3R7XX-ray2.10A/B413-527[»]
A/B653-796[»]
3RN8X-ray1.70A/B/C413-527[»]
A/B/C653-812[»]
3RNNX-ray1.75A/B/C413-527[»]
A/B/C653-812[»]
3UA8X-ray1.90A413-527[»]
A653-796[»]
ProteinModelPortaliP42262.
SMRiP42262. Positions 25-838.

Miscellaneous databases

EvolutionaryTraceiP42262.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni499 – 5013Glutamate binding
Regioni675 – 6762Glutamate binding

Domaini

The M4 transmembrane segment mediates tetramerization and is required for cell surface expression.

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG316680.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
KOiK05198.
OMAiHAVPYVS.
OrthoDBiEOG7C2R0J.
PhylomeDBiP42262.
TreeFamiTF315232.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamiPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSiPR00177. NMDARECEPTOR.
SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMiSSF53822. SSF53822. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Flop (identifier: P42262-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ    50
FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI 100
TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY 150
LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE MYRSLFQDLE 200
LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI 250
QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT TTIKYTSALT 300
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ 350
VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT 400
ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA 450
AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL 500
TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI 550
VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 600
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM 650
VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP 700
SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS 750
KGYGIATPKG SSLRNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD 800
SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK 850
NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI 883
Length:883
Mass (Da):98,821
Last modified:October 10, 2002 - v3
Checksum:i6DAB96C76D1D8448
GO
Isoform Flip (identifier: P42262-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     765-800: NAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD → TPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSG

Show »
Length:883
Mass (Da):98,878
Checksum:i882141AC054254F8
GO
Isoform 3 (identifier: P42262-3) [UniParc]FASTAAdd to Basket

Also known as: Long

The sequence of this isoform differs from the canonical sequence as follows:
     848-883: VAKNAQNINP...NVYGIESVKI → MTLNDAMRNK...GMNVSVTDLS

Show »
Length:901
Mass (Da):100,594
Checksum:i6E668073D621EFBB
GO

RNA editingi

Partially edited. Fully edited in the brain. Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent ions.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti607 – 6071Q → R in RNA edited version. 2 Publications
Corresponds to variant rs17850674 [ dbSNP | Ensembl ].
VAR_000303
Natural varianti608 – 6081Q → R.1 Publication
Corresponds to variant rs17850675 [ dbSNP | Ensembl ].
VAR_037055

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei765 – 80036NAVNL…SGGGD → TPVNLAVLKLSEQGVLDKLK NKWWYDKGECGAKDSG in isoform Flip. VSP_053350Add
BLAST
Alternative sequencei848 – 88336VAKNA…ESVKI → MTLNDAMRNKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3. VSP_029309Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti140 – 1401I → V in AAH10574. 1 Publication
Sequence conflicti241 – 2411G → E in AAA58631. 1 Publication
Sequence conflicti764 – 7641R → G in AAA58631. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20814 mRNA. Translation: AAA58631.1.
BC010574 mRNA. Translation: AAH10574.1.
CCDSiCCDS3797.1. [P42262-2]
CCDS43274.1. [P42262-1]
PIRiI58181.
RefSeqiNP_000817.2. NM_000826.3.
NP_001077088.1. NM_001083619.1.
NP_001077089.1. NM_001083620.1.
UniGeneiHs.32763.

Genome annotation databases

EnsembliENST00000264426; ENSP00000264426; ENSG00000120251. [P42262-1]
ENST00000296526; ENSP00000296526; ENSG00000120251. [P42262-2]
GeneIDi2891.
KEGGihsa:2891.
UCSCiuc003ipm.4. human. [P42262-1]

Polymorphism databases

DMDMi23831146.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L20814 mRNA. Translation: AAA58631.1 .
BC010574 mRNA. Translation: AAH10574.1 .
CCDSi CCDS3797.1. [P42262-2 ]
CCDS43274.1. [P42262-1 ]
PIRi I58181.
RefSeqi NP_000817.2. NM_000826.3.
NP_001077088.1. NM_001083619.1.
NP_001077089.1. NM_001083620.1.
UniGenei Hs.32763.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WJW X-ray 1.80 A 25-412 [» ]
2WJX X-ray 4.10 A/B/C 25-412 [» ]
2XHD X-ray 1.80 A/B 413-527 [» ]
A/B 653-796 [» ]
3R7X X-ray 2.10 A/B 413-527 [» ]
A/B 653-796 [» ]
3RN8 X-ray 1.70 A/B/C 413-527 [» ]
A/B/C 653-812 [» ]
3RNN X-ray 1.75 A/B/C 413-527 [» ]
A/B/C 653-812 [» ]
3UA8 X-ray 1.90 A 413-527 [» ]
A 653-796 [» ]
ProteinModelPortali P42262.
SMRi P42262. Positions 25-838.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109148. 17 interactions.
DIPi DIP-42852N.
IntActi P42262. 2 interactions.
MINTi MINT-2791741.
STRINGi 9606.ENSP00000264426.

Chemistry

BindingDBi P42262.
ChEMBLi CHEMBL2096670.
DrugBanki DB00142. L-Glutamic Acid.
GuidetoPHARMACOLOGYi 445.

Protein family/group databases

TCDBi 1.A.10.1.13. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSitei P42262.

Polymorphism databases

DMDMi 23831146.

Proteomic databases

PaxDbi P42262.
PRIDEi P42262.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264426 ; ENSP00000264426 ; ENSG00000120251 . [P42262-1 ]
ENST00000296526 ; ENSP00000296526 ; ENSG00000120251 . [P42262-2 ]
GeneIDi 2891.
KEGGi hsa:2891.
UCSCi uc003ipm.4. human. [P42262-1 ]

Organism-specific databases

CTDi 2891.
GeneCardsi GC04P158141.
HGNCi HGNC:4572. GRIA2.
HPAi CAB006830.
CAB007812.
CAB012981.
HPA008441.
MIMi 138247. gene.
neXtProti NX_P42262.
PharmGKBi PA28967.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316680.
HOGENOMi HOG000234372.
HOVERGENi HBG051839.
KOi K05198.
OMAi HAVPYVS.
OrthoDBi EOG7C2R0J.
PhylomeDBi P42262.
TreeFami TF315232.

Enzyme and pathway databases

Reactomei REACT_18338. Activation of AMPA receptors.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
SignaLinki P42262.

Miscellaneous databases

EvolutionaryTracei P42262.
GeneWikii GRIA2.
GenomeRNAii 2891.
NextBioi 11429.
PROi P42262.
SOURCEi Search...

Gene expression databases

ArrayExpressi P42262.
Bgeei P42262.
CleanExi HS_GRIA2.
Genevestigatori P42262.

Family and domain databases

InterProi IPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view ]
Pfami PF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view ]
PRINTSi PR00177. NMDARECEPTOR.
SMARTi SM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view ]
SUPFAMi SSF53822. SSF53822. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure and functional expression of the AMPA/kainate receptor subunit 2 from human brain."
    Sun W., Ferrer-Montiel A.V., Montal M.
    NeuroReport 5:441-444(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), VARIANT ARG-607.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM FLOP), VARIANTS ARG-607 AND ARG-608.
    Tissue: Brain.
  3. "RNA editing of the glutamate receptor subunits GluR2 and GluR6 in human brain tissue."
    Paschen W., Hedreen J.C., Ross C.A.
    J. Neurochem. 63:1596-1602(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA EDITING OF POSITION 607.
  4. "Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors."
    Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T., Koehr G., Malinow R., Seeburg P.H., Osten P.
    Neuron 40:1199-1212(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION (ISOFORM 3).
  5. "The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands."
    Dev K.K., Nakanishi S., Henley J.M.
    J. Biol. Chem. 279:41393-41397(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PICK1.
  6. "A eukaryotic specific transmembrane segment is required for tetramerization in AMPA receptors."
    Salussolia C.L., Gan Q., Kazi R., Singh P., Allopenna J., Furukawa H., Wollmuth L.P.
    J. Neurosci. 33:9840-9845(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  7. "Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors."
    Clayton A., Siebold C., Gilbert R.J., Sutton G.C., Harlos K., McIlhinney R.A., Jones E.Y., Aricescu A.R.
    J. Mol. Biol. 392:1125-1132(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-412, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-370.
  8. "Discovery of N-[(2S)-5-(6-fluoro-3-pyridinyl)-2,3-dihydro-1H-inden-2-yl]-2-propanesulfonamide, a novel clinical AMPA receptor positive modulator."
    Ward S.E., Harries M., Aldegheri L., Andreotti D., Ballantine S., Bax B.D., Harris A.J., Harker A.J., Lund J., Melarange R., Mingardi A., Mookherjee C., Mosley J., Neve M., Oliosi B., Profeta R., Smith K.J., Smith P.W.
    , Spada S., Thewlis K.M., Yusaf S.P.
    J. Med. Chem. 53:5801-5812(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-795 IN COMPLEX WITH GLUTAMATE AND SYNTHETIC INHIBITOR, FUNCTION.
  9. "Quinazolinedione sulfonamides: a novel class of competitive AMPA receptor antagonists with oral activity."
    Koller M., Lingenhoehl K., Schmutz M., Vranesic I.T., Kallen J., Auberson Y.P., Carcache D.A., Mattes H., Ofner S., Orain D., Urwyler S.
    Bioorg. Med. Chem. Lett. 21:3358-3361(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE AND SYNTHETIC INHIBITOR, DISULFIDE BOND.

Entry informationi

Entry nameiGRIA2_HUMAN
AccessioniPrimary (citable) accession number: P42262
Secondary accession number(s): Q96FP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 10, 2002
Last modified: September 3, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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