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P19490

- GRIA1_RAT

UniProt

P19490 - GRIA1_RAT

Protein

Glutamate receptor 1

Gene

Gria1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (16 May 2006)
      Previous versions | rss
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    Functioni

    Ionotropic glutamate receptor. 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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei464 – 4641GlutamateBy similarity
    Binding sitei499 – 4991GlutamateBy similarity
    Binding sitei719 – 7191GlutamateBy similarity

    GO - Molecular functioni

    1. adenylate cyclase binding Source: RGD
    2. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: UniProtKB
    3. beta-2 adrenergic receptor binding Source: RGD
    4. extracellular-glutamate-gated ion channel activity Source: RefGenome
    5. G-protein alpha-subunit binding Source: RGD
    6. G-protein beta-subunit binding Source: RGD
    7. identical protein binding Source: IntAct
    8. ionotropic glutamate receptor activity Source: RGD
    9. myosin V binding Source: RGD
    10. PDZ domain binding Source: RGD
    11. protein binding Source: UniProtKB
    12. protein domain specific binding Source: RGD
    13. protein homodimerization activity Source: UniProtKB
    14. protein kinase A binding Source: RGD
    15. protein kinase binding Source: RGD
    16. small GTPase binding Source: RGD

    GO - Biological processi

    1. cellular response to amine stimulus Source: RGD
    2. cellular response to amino acid stimulus Source: RGD
    3. cellular response to dsRNA Source: RGD
    4. cellular response to growth factor stimulus Source: RGD
    5. cellular response to organic cyclic compound Source: RGD
    6. cellular response to peptide hormone stimulus Source: RGD
    7. ionotropic glutamate receptor signaling pathway Source: GOC
    8. ion transmembrane transport Source: GOC
    9. long-term memory Source: RGD
    10. neuronal action potential Source: UniProtKB
    11. positive regulation of membrane potential Source: RGD
    12. positive regulation of synaptic transmission Source: UniProtKB
    13. receptor internalization Source: UniProtKB
    14. regulation of receptor recycling Source: UniProtKB
    15. regulation of synaptic plasticity Source: UniProtKB
    16. regulation of synaptic transmission Source: UniProtKB
    17. response to arsenic-containing substance Source: RGD
    18. response to cocaine Source: RGD
    19. response to drug Source: RGD
    20. response to electrical stimulus Source: RGD
    21. response to estradiol Source: RGD
    22. response to fungicide Source: RGD
    23. response to lithium ion Source: UniProtKB
    24. response to organic cyclic compound Source: RGD
    25. response to peptide hormone Source: RGD
    26. response to toxic substance Source: RGD
    27. spinal cord development Source: RGD
    28. synaptic transmission, glutamatergic Source: UniProtKB

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Protein family/group databases

    TCDBi1.A.10.1.1. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate receptor 1
    Short name:
    GluR-1
    Alternative name(s):
    AMPA-selective glutamate receptor 1
    GluR-A
    GluR-K1
    Glutamate receptor ionotropic, AMPA 1
    Short name:
    GluA1
    Gene namesi
    Name:Gria1
    Synonyms:Glur1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621531. Gria1.

    Subcellular locationi

    GO - Cellular componenti

    1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: UniProtKB
    2. asymmetric synapse Source: RGD
    3. cell junction Source: UniProtKB-KW
    4. cell surface Source: RGD
    5. cytosol Source: RGD
    6. dendrite Source: UniProtKB
    7. dendritic shaft Source: UniProtKB
    8. dendritic spine Source: RGD
    9. early endosome Source: UniProtKB
    10. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    11. excitatory synapse Source: BHF-UCL
    12. ionotropic glutamate receptor complex Source: UniProtKB
    13. neuromuscular junction Source: RGD
    14. neuronal cell body Source: UniProtKB
    15. neuron projection Source: RGD
    16. neuron spine Source: RGD
    17. plasma membrane Source: RGD
    18. postsynaptic density Source: RGD
    19. postsynaptic membrane Source: RefGenome
    20. protein complex Source: RGD
    21. synapse Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi645 – 6451S → A: No effect on phosphorylation by CaMK2. 1 Publication
    Mutagenesisi849 – 8491S → A: Abolishes phosphorylation by CaMK2. 1 Publication
    Mutagenesisi905 – 9051T → A: Loss of interaction with DLG1. 1 Publication
    Mutagenesisi907 – 9071L → A: Loss of interaction with DLG1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 907889Glutamate receptor 1PRO_0000011531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi63 – 631N-linked (GlcNAc...)
    Disulfide bondi75 ↔ 3231 Publication
    Glycosylationi249 – 2491N-linked (GlcNAc...)1 Publication
    Glycosylationi257 – 2571N-linked (GlcNAc...)1 Publication
    Glycosylationi363 – 3631N-linked (GlcNAc...)1 Publication
    Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Lipidationi603 – 6031S-palmitoyl cysteineBy similarity
    Modified residuei645 – 6451Phosphoserine1 Publication
    Modified residuei710 – 7101Phosphoserine; by PKC1 Publication
    Disulfide bondi732 ↔ 787By similarity
    Lipidationi829 – 8291S-palmitoyl cysteineBy similarity
    Modified residuei849 – 8491Phosphoserine; by PKC, PKA and CAMK21 Publication
    Modified residuei863 – 8631Phosphoserine; by PKC and PKA1 Publication

    Post-translational modificationi

    Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-603 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-829 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PRIDEiP19490.

    PTM databases

    PhosphoSiteiP19490.

    Expressioni

    Tissue specificityi

    Detected in cerebellum (at protein level).1 Publication

    Gene expression databases

    GenevestigatoriP19490.

    Interactioni

    Subunit structurei

    Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with DLG1 via its C-terminus. Found in a complex with GRIA2, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with HIP1, RASGRF2, SYNDIG1 and LRFN1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes. Interacts (via PDZ-binding motif) with SHANK3 (via PDZ domain).10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-371642,EBI-371642
    Adrb2P106083EBI-371642,EBI-7090342
    Gria2P194913EBI-371642,EBI-77718
    Myo5bP705692EBI-371642,EBI-975940

    Protein-protein interaction databases

    BioGridi248399. 5 interactions.
    DIPiDIP-30929N.
    IntActiP19490. 17 interactions.
    MINTiMINT-726538.

    Structurei

    Secondary structure

    1
    907
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 3210
    Beta strandi34 – 363
    Helixi37 – 4610
    Beta strandi51 – 6111
    Helixi67 – 7913
    Beta strandi85 – 873
    Helixi91 – 10414
    Beta strandi108 – 1103
    Beta strandi122 – 1243
    Helixi130 – 13910
    Beta strandi144 – 1496
    Helixi156 – 16813
    Beta strandi171 – 1766
    Helixi177 – 1793
    Helixi183 – 1875
    Turni188 – 1914
    Beta strandi196 – 2038
    Helixi206 – 2083
    Helixi209 – 21810
    Beta strandi225 – 2339
    Helixi235 – 2373
    Helixi240 – 2456
    Beta strandi250 – 2545
    Helixi261 – 27616
    Helixi288 – 30922
    Helixi334 – 3429
    Beta strandi346 – 3483
    Beta strandi351 – 3533
    Beta strandi359 – 3613
    Beta strandi366 – 3727
    Beta strandi375 – 3839
    Turni384 – 3863
    Beta strandi387 – 3904
    Beta strandi905 – 9073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AWWX-ray2.21C890-907[»]
    3SAJX-ray2.50A/B/C/D22-392[»]
    ProteinModelPortaliP19490.
    SMRiP19490. Positions 406-520, 645-788.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19490.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 536518ExtracellularBy similarityAdd
    BLAST
    Topological domaini558 – 58427CytoplasmicBy similarityAdd
    BLAST
    Topological domaini604 – 6096CytoplasmicBy similarity
    Topological domaini631 – 805175ExtracellularBy similarityAdd
    BLAST
    Topological domaini827 – 90781CytoplasmicBy similarityAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei585 – 60016Helical; Pore-formingBy similarityAdd
    BLAST
    Intramembranei601 – 6033By similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei537 – 55721HelicalBy similarityAdd
    BLAST
    Transmembranei610 – 63021HelicalBy similarityAdd
    BLAST
    Transmembranei806 – 82621Helical; Name=M4By similarityAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni492 – 4943Glutamate bindingBy similarity
    Regioni668 – 6692Glutamate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi904 – 9074PDZ-binding

    Domaini

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

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    HOVERGENiHBG051839.
    KOiK05197.
    PhylomeDBiP19490.

    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.
    IPR001638. SBP_bac_3.
    [Graphical view]
    PfamiPF01094. ANF_receptor. 1 hit.
    PF00060. Lig_chan. 1 hit.
    PF00497. SBP_bac_3. 1 hit.
    [Graphical view]
    PRINTSiPR00177. NMDARECEPTOR.
    SMARTiSM00918. Lig_chan-Glu_bd. 1 hit.
    SM00079. PBPe. 1 hit.
    [Graphical view]
    SUPFAMiSSF53822. SSF53822. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Flop (identifier: P19490-1) [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

    MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT    50
    EPPKLLPQID IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF 100
    CGALHVCFIT PSFPVDTSNQ FVLQLRPELQ EALISIIDHY KWQTFVYIYD 150
    ADRGLSVLQR VLDTAAEKNW QVTAVNILTT TEEGYRMLFQ DLEKKKERLV 200
    VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL NKFKESGANV 250
    TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM 300
    AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT 350
    GNVQFNEKGR RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD 400
    NSSVQNRTYI VTTILEDPYV MLKKNANQFE GNDRYEGYCV ELAAEIAKHV 450
    GYSYRLEIVS DGKYGARDPD TKAWNGMVGE LVYGRADVAV APLTITLVRE 500
    EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW MCIVFAYIGV 550
    SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ 600
    QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA 650
    EDLAKQTEIA YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT 700
    EEGMIRVRKS KGKYAYLLES TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT 750
    PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW WYDKGECGSG GGDSKDKTSA 800
    LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK GFCLIPQQSI 850
    NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM 900
    PLGATGL 907
    Length:907
    Mass (Da):101,579
    Last modified:May 16, 2006 - v2
    Checksum:i2D4CFA7CCD532838
    GO
    Isoform Flip (identifier: P19490-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         758-758: N → G
         768-768: N → S
         772-772: L → V
         778-778: N → S
         790-793: GGGD → KDSG

    Show »
    Length:907
    Mass (Da):101,555
    Checksum:i5FA3091114C0BA6B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 671S → T in AAA63479. (PubMed:1699275)Curated
    Sequence conflicti248 – 2481A → R in AAA63479. (PubMed:1699275)Curated
    Sequence conflicti698 – 6981R → L in AAA63479. (PubMed:1699275)Curated

    Polymorphismi

    Both variants Ser-710 and Thr-710 are phosphorylated at this position.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti710 – 7101S → T.2 Publications

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei758 – 7581N → G in isoform Flip. 1 PublicationVSP_000097
    Alternative sequencei768 – 7681N → S in isoform Flip. 1 PublicationVSP_000098
    Alternative sequencei772 – 7721L → V in isoform Flip. 1 PublicationVSP_000099
    Alternative sequencei778 – 7781N → S in isoform Flip. 1 PublicationVSP_000100
    Alternative sequencei790 – 7934GGGD → KDSG in isoform Flip. 1 PublicationVSP_000101

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17184 mRNA. Translation: CAA35050.1.
    M36418 mRNA. Translation: AAA41243.2.
    M38060 mRNA. Translation: AAA63479.1.
    PIRiA40170.
    S07059. ACRTK1.
    RefSeqiNP_113796.1. NM_031608.1. [P19490-1]
    UniGeneiRn.29971.

    Genome annotation databases

    GeneIDi50592.
    KEGGirno:50592.
    UCSCiRGD:621531. rat. [P19490-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X17184 mRNA. Translation: CAA35050.1 .
    M36418 mRNA. Translation: AAA41243.2 .
    M38060 mRNA. Translation: AAA63479.1 .
    PIRi A40170.
    S07059. ACRTK1.
    RefSeqi NP_113796.1. NM_031608.1. [P19490-1 ]
    UniGenei Rn.29971.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AWW X-ray 2.21 C 890-907 [» ]
    3SAJ X-ray 2.50 A/B/C/D 22-392 [» ]
    ProteinModelPortali P19490.
    SMRi P19490. Positions 406-520, 645-788.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248399. 5 interactions.
    DIPi DIP-30929N.
    IntActi P19490. 17 interactions.
    MINTi MINT-726538.

    Chemistry

    BindingDBi P19490.
    ChEMBLi CHEMBL3753.
    GuidetoPHARMACOLOGYi 444.

    Protein family/group databases

    TCDBi 1.A.10.1.1. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    PTM databases

    PhosphoSitei P19490.

    Proteomic databases

    PRIDEi P19490.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 50592.
    KEGGi rno:50592.
    UCSCi RGD:621531. rat. [P19490-1 ]

    Organism-specific databases

    CTDi 2890.
    RGDi 621531. Gria1.

    Phylogenomic databases

    HOVERGENi HBG051839.
    KOi K05197.
    PhylomeDBi P19490.

    Miscellaneous databases

    EvolutionaryTracei P19490.
    NextBioi 610434.

    Gene expression databases

    Genevestigatori P19490.

    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.
    IPR001638. SBP_bac_3.
    [Graphical view ]
    Pfami PF01094. ANF_receptor. 1 hit.
    PF00060. Lig_chan. 1 hit.
    PF00497. SBP_bac_3. 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

    1. "Cloning by functional expression of a member of the glutamate receptor family."
      Hollmann M., O'Shea-Greenfield A., Rogers S.W., Heinemann S.F.
      Nature 342:643-648(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
      Tissue: Forebrain.
    2. Hartley M.
      Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
      Tissue: Brain.
    4. Keinaenen K., Wisden W., Sommer B., Werner P., Herb A., Verdoorn T.A., Sakmann B., Seeburg P.H.
      Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 67; 248; 698; 710; 789 AND 893.
    5. "Molecular cloning and functional expression of glutamate receptor subunit genes."
      Boulter J., Hollmann M., O'Shea-Greenfield A., Hartley M., Deneris E.S., Maron C., Heinemann S.F.
      Science 249:1033-1037(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
    6. "Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS."
      Sommer B., Keinaenen K., Verdoorn T.A., Wisden W., Burnashev N., Herb A., Koehler M., Takagi T., Sakmann B., Seeburg P.H.
      Science 249:1580-1585(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), VARIANT THR-710.
      Tissue: Brain.
    7. "Identification of a Ca2+/calmodulin-dependent protein kinase II regulatory phosphorylation site in non-N-methyl-D-aspartate glutamate receptors."
      Yakel J.L., Vissavajjhala P., Derkach V.A., Brickey D.A., Soderling T.R.
      Proc. Natl. Acad. Sci. U.S.A. 92:1376-1380(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-645.
    8. "Antibody specific for phosphorylated AMPA-type glutamate receptors at GluR2 Ser-696."
      Nakazawa K., Tadakuma T., Nokihara K., Ito M.
      Neurosci. Res. 24:75-86(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THR-710, PHOSPHORYLATION AT SER-710.
    9. "Phosphorylation of the alpha-amino-3-hydroxy-5-methylisoxazole4-propionic acid receptor GluR1 subunit by calcium/calmodulin-dependent kinase II."
      Mammen A.L., Kameyama K., Roche K.W., Huganir R.L.
      J. Biol. Chem. 272:32528-32533(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-849 AND SER-863, MUTAGENESIS OF SER-645 AND SER-849.
    10. "SAP97 is associated with the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor GluR1 subunit."
      Leonard A.S., Davare M.A., Horne M.C., Garner C.C., Hell J.W.
      J. Biol. Chem. 273:19518-19524(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG1.
    11. "Selective binding of synapse-associated protein 97 to GluR-A alpha-amino-5-hydroxy-3-methyl-4-isoxazole propionate receptor subunit is determined by a novel sequence motif."
      Cai C., Coleman S.K., Niemi K., Keinaenen K.
      J. Biol. Chem. 277:31484-31490(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DLG1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-905 AND LEU-907.
    12. "Different domains of the AMPA receptor direct stargazin-mediated trafficking and stargazin-mediated modulation of kinetics."
      Bedoukian M.A., Weeks A.M., Partin K.M.
      J. Biol. Chem. 281:23908-23921(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH CACNG2.
    13. "SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses."
      Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E.
      Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRFN1.
    14. "AMPA receptor subunit-specific regulation by a distinct family of type II TARPs."
      Kato A.S., Siuda E.R., Nisenbaum E.S., Bredt D.S.
      Neuron 59:986-996(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CACNG5.
    15. "Selective regulation of long-form calcium-permeable AMPA receptors by an atypical TARP, gamma-5."
      Soto D., Coombs I.D., Renzi M., Zonouzi M., Farrant M., Cull-Candy S.G.
      Nat. Neurosci. 12:277-285(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CACNG5.
    16. "Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors."
      Schwenk J., Harmel N., Zolles G., Bildl W., Kulik A., Heimrich B., Chisaka O., Jonas P., Schulte U., Fakler B., Kloecker N.
      Science 323:1313-1319(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "Functional comparison of the effects of TARPs and cornichons on AMPA receptor trafficking and gating."
      Shi Y., Suh Y.H., Milstein A.D., Isozaki K., Schmid S.M., Roche K.W., Nicoll R.A.
      Proc. Natl. Acad. Sci. U.S.A. 107:16315-16319(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNIH2 AND CACNG2.
    18. "Crystal structure of the second PDZ domain of SAP97 in complex with a GluR-A C-terminal peptide."
      von Ossowski I., Oksanen E., von Ossowski L., Cai C., Sundberg M., Goldman A., Keinanen K.
      FEBS J. 273:5219-5229(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 890-907 IN COMPLEX WITH DLG1, INTERACTION WITH DLG1.
    19. "Crystal structure of the glutamate receptor GluA1 N-terminal domain."
      Yao G., Zong Y., Gu S., Zhou J., Xu H., Mathews I.I., Jin R.
      Biochem. J. 438:255-263(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-392, SUBUNIT, GLYCOSYLATION AT ASN-249; ASN-257 AND ASN-363, DISULFIDE BOND.

    Entry informationi

    Entry nameiGRIA1_RAT
    AccessioniPrimary (citable) accession number: P19490
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3