Details for: Gria2

Gene ID: 29627

Symbol: Gria2

Ensembl ID: ENSRNOG00000054204

Description: glutamate ionotropic receptor AMPA type subunit 2

Associated with

Other Information

Genular Protein ID: 4207985022

Symbol: GRIA2_RAT

Name: AMPA-selective glutamate receptor 2

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 2166337

Title: A family of AMPA-selective glutamate receptors.

PubMed ID: 2166337

DOI: 10.1126/science.2166337

PubMed ID: 2168579

Title: Molecular cloning and functional expression of glutamate receptor subunit genes.

PubMed ID: 2168579

DOI: 10.1126/science.2168579

PubMed ID: 1699567

Title: A family of glutamate receptor genes: evidence for the formation of heteromultimeric receptors with distinct channel properties.

PubMed ID: 1699567

DOI: 10.1016/0896-6273(90)90212-x

PubMed ID: 9351977

Title: N-glycosylation is not a prerequisite for glutamate receptor function but is essential for lectin modulation.

PubMed ID: 9351977

DOI: 10.1124/mol.52.5.861

PubMed ID: 1717158

Title: RNA editing in brain controls a determinant of ion flow in glutamate-gated channels.

PubMed ID: 1717158

DOI: 10.1016/0092-8674(91)90568-j

PubMed ID: 9697855

Title: The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and alpha- and beta-SNAPs.

PubMed ID: 9697855

DOI: 10.1016/s0896-6273(00)80518-8

PubMed ID: 10027300

Title: Clustering of AMPA receptors by the synaptic PDZ domain-containing protein PICK1.

PubMed ID: 10027300

DOI: 10.1016/s0896-6273(00)80689-3

PubMed ID: 1699275

Title: Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS.

PubMed ID: 1699275

DOI: 10.1126/science.1699275

PubMed ID: 8848293

Title: Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696.

PubMed ID: 8848293

DOI: 10.1016/0168-0102(95)00977-9

PubMed ID: 9069286

Title: GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors.

PubMed ID: 9069286

DOI: 10.1038/386279a0

PubMed ID: 10414981

Title: Association of AMPA receptors with a subset of glutamate receptor-interacting protein in vivo.

PubMed ID: 10414981

DOI: 10.1523/jneurosci.19-15-06528.1999

PubMed ID: 12657670

Title: Ischemic insults derepress the gene silencer REST in neurons destined to die.

PubMed ID: 12657670

DOI: 10.1523/jneurosci.23-06-02112.2003

PubMed ID: 14687553

Title: Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors.

PubMed ID: 14687553

DOI: 10.1016/s0896-6273(03)00722-0

PubMed ID: 15240807

Title: Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases.

PubMed ID: 15240807

DOI: 10.1523/jneurosci.0799-04.2004

PubMed ID: 16037816

Title: Interactions between NEEP21, GRIP1 and GluR2 regulate sorting and recycling of the glutamate receptor subunit GluR2.

PubMed ID: 16037816

DOI: 10.1038/sj.emboj.7600755

PubMed ID: 16793768

Title: Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics.

PubMed ID: 16793768

DOI: 10.1074/jbc.m600679200

PubMed ID: 16630835

Title: SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses.

PubMed ID: 16630835

DOI: 10.1016/j.neuron.2006.04.005

PubMed ID: 18817736

Title: AMPA receptor subunit-specific regulation by a distinct family of type II TARPs.

PubMed ID: 18817736

DOI: 10.1016/j.neuron.2008.07.034

PubMed ID: 19234459

Title: Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5.

PubMed ID: 19234459

DOI: 10.1038/nn.2266

PubMed ID: 19265014

Title: Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors.

PubMed ID: 19265014

DOI: 10.1126/science.1167852

PubMed ID: 20547133

Title: AMPA receptor signaling through BRAG2 and Arf6 critical for long-term synaptic depression.

PubMed ID: 20547133

DOI: 10.1016/j.neuron.2010.05.003

PubMed ID: 21172611

Title: Hippocampal AMPA receptor gating controlled by both TARP and cornichon proteins.

PubMed ID: 21172611

DOI: 10.1016/j.neuron.2010.11.026

PubMed ID: 21496646

Title: The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic plasticity and behavior.

PubMed ID: 21496646

DOI: 10.1016/j.cell.2011.03.016

PubMed ID: 27756895

Title: MPP2 is a postsynaptic MAGUK scaffold protein that links SynCAM1 cell adhesion molecules to core components of the postsynaptic density.

PubMed ID: 27756895

DOI: 10.1038/srep35283

PubMed ID: 9804426

Title: Structure of a glutamate-receptor ligand-binding core in complex with kainate.

PubMed ID: 9804426

DOI: 10.1038/27692

PubMed ID: 11086992

Title: Mechanisms for activation and antagonism of an AMPA-sensitive glutamate receptor: crystal structures of the GluR2 ligand binding core.

PubMed ID: 11086992

DOI: 10.1016/s0896-6273(00)00094-5

PubMed ID: 12501192

Title: Mechanism of activation and selectivity in a ligand-gated ion channel: structural and functional studies of GluR2 and quisqualate.

PubMed ID: 12501192

DOI: 10.1021/bi020583k

PubMed ID: 12215417

Title: Structural basis for AMPA receptor activation and ligand selectivity: crystal structures of five agonist complexes with the GluR2 ligand-binding core.

PubMed ID: 12215417

DOI: 10.1016/s0022-2836(02)00650-2

PubMed ID: 12015593

Title: Mechanism of glutamate receptor desensitization.

PubMed ID: 12015593

DOI: 10.1038/417245a

PubMed ID: 12593667

Title: Three-dimensional structure of the ligand-binding core of GluR2 in complex with the agonist (S)-ATPA: implications for receptor subunit selectivity.

PubMed ID: 12593667

DOI: 10.1021/jm021020+

PubMed ID: 12872125

Title: Structural basis for partial agonist action at ionotropic glutamate receptors.

PubMed ID: 12872125

DOI: 10.1038/nn1091

PubMed ID: 12730367

Title: Tuning activation of the AMPA-sensitive GluR2 ion channel by genetic adjustment of agonist-induced conformational changes.

PubMed ID: 12730367

DOI: 10.1073/pnas.1037393100

PubMed ID: 16192394

Title: Mechanism of positive allosteric modulators acting on AMPA receptors.

PubMed ID: 16192394

DOI: 10.1523/jneurosci.2567-05.2005

PubMed ID: 15591246

Title: Tyr702 is an important determinant of agonist binding and domain closure of the ligand-binding core of GluR2.

PubMed ID: 15591246

DOI: 10.1124/mol.104.002931

PubMed ID: 17018279

Title: Measurement of conformational changes accompanying desensitization in an ionotropic glutamate receptor.

PubMed ID: 17018279

DOI: 10.1016/j.cell.2006.08.037

PubMed ID: 16483599

Title: The structure of a mixed GluR2 ligand-binding core dimer in complex with (S)-glutamate and the antagonist (S)-NS1209.

PubMed ID: 16483599

DOI: 10.1016/j.jmb.2006.01.024

PubMed ID: 19946266

Title: X-ray structure, symmetry and mechanism of an AMPA-subtype glutamate receptor.

PubMed ID: 19946266

DOI: 10.1038/nature08624

PubMed ID: 21317873

Title: Subunit-selective N-terminal domain associations organize the formation of AMPA receptor heteromers.

PubMed ID: 21317873

DOI: 10.1038/emboj.2011.16

PubMed ID: 21846932

Title: Mechanism of AMPA receptor activation by partial agonists: disulfide trapping of closed lobe conformations.

PubMed ID: 21846932

DOI: 10.1074/jbc.m111.269001

PubMed ID: 25103405

Title: X-ray structures of AMPA receptor-cone snail toxin complexes illuminate activation mechanism.

PubMed ID: 25103405

DOI: 10.1126/science.1258409

Sequence Information:

  • Length: 883
  • Mass: 98688
  • Checksum: DEFA817027C1CCD1
  • Sequence:
  • MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP 
    HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG 
    THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV 
    GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL 
    GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT 
    YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI 
    KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT 
    ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI 
    WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD 
    PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 
    SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL 
    SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK 
    YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL 
    DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR 
    AEAKRMKVAK NPQNINPSSS QNSQNFATYK EGYNVYGIES VKI

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.