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P19490

- GRIA1_RAT

UniProt

P19490 - GRIA1_RAT

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Protein

Glutamate receptor 1

Gene

Gria1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 domain specific binding Source: RGD
  12. protein homodimerization activity Source: UniProtKB
  13. protein kinase A binding Source: RGD
  14. protein kinase binding Source: RGD
  15. 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 536518ExtracellularBy similarityAdd
BLAST
Transmembranei537 – 55721HelicalBy similarityAdd
BLAST
Topological domaini558 – 58427CytoplasmicBy similarityAdd
BLAST
Intramembranei585 – 60016Helical; Pore-formingBy similarityAdd
BLAST
Intramembranei601 – 6033By similarity
Topological domaini604 – 6096CytoplasmicBy similarity
Transmembranei610 – 63021HelicalBy similarityAdd
BLAST
Topological domaini631 – 805175ExtracellularBy similarityAdd
BLAST
Transmembranei806 – 82621Helical; Name=M4By similarityAdd
BLAST
Topological domaini827 – 90781CytoplasmicBy similarityAdd
BLAST

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 Source: UniProtKB-KW
  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
Complete GO annotation...

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. 6 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 – 3210Combined sources
Beta strandi34 – 363Combined sources
Helixi37 – 4610Combined sources
Beta strandi51 – 6111Combined sources
Helixi67 – 7913Combined sources
Beta strandi85 – 873Combined sources
Helixi91 – 10414Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi122 – 1243Combined sources
Helixi130 – 13910Combined sources
Beta strandi144 – 1496Combined sources
Helixi156 – 16813Combined sources
Beta strandi171 – 1766Combined sources
Helixi177 – 1793Combined sources
Helixi183 – 1875Combined sources
Turni188 – 1914Combined sources
Beta strandi196 – 2038Combined sources
Helixi206 – 2083Combined sources
Helixi209 – 21810Combined sources
Beta strandi225 – 2339Combined sources
Helixi235 – 2373Combined sources
Helixi240 – 2456Combined sources
Beta strandi250 – 2545Combined sources
Helixi261 – 27616Combined sources
Helixi288 – 30922Combined sources
Helixi334 – 3429Combined sources
Beta strandi346 – 3483Combined sources
Beta strandi351 – 3533Combined sources
Beta strandi359 – 3613Combined sources
Beta strandi366 – 3727Combined sources
Beta strandi375 – 3839Combined sources
Turni384 – 3863Combined sources
Beta strandi387 – 3904Combined sources
Beta strandi905 – 9073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
InParanoidiP19490.
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

        10         20         30         40         50
MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT
60 70 80 90 100
EPPKLLPQID IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF
110 120 130 140 150
CGALHVCFIT PSFPVDTSNQ FVLQLRPELQ EALISIIDHY KWQTFVYIYD
160 170 180 190 200
ADRGLSVLQR VLDTAAEKNW QVTAVNILTT TEEGYRMLFQ DLEKKKERLV
210 220 230 240 250
VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL NKFKESGANV
260 270 280 290 300
TGFQLVNYTD TIPARIMQQW RTSDSRDHTR VDWKRPKYTS ALTYDGVKVM
310 320 330 340 350
AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT
360 370 380 390 400
GNVQFNEKGR RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD
410 420 430 440 450
NSSVQNRTYI VTTILEDPYV MLKKNANQFE GNDRYEGYCV ELAAEIAKHV
460 470 480 490 500
GYSYRLEIVS DGKYGARDPD TKAWNGMVGE LVYGRADVAV APLTITLVRE
510 520 530 540 550
EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW MCIVFAYIGV
560 570 580 590 600
SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ
610 620 630 640 650
QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA
660 670 680 690 700
EDLAKQTEIA YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT
710 720 730 740 750
EEGMIRVRKS KGKYAYLLES TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT
760 770 780 790 800
PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW WYDKGECGSG GGDSKDKTSA
810 820 830 840 850
LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK GFCLIPQQSI
860 870 880 890 900
NEAIRTSTLP RNSGAGASGG GGSGENGRVV SQDFPKSMQS IPCMSHSSGM

PLGATGL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 6 interactions.
DIPi DIP-30929N.
IntActi P19490. 17 interactions.
MINTi MINT-726538.

Chemistry

BindingDBi P19490.
ChEMBLi CHEMBL2093871.
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.
InParanoidi P19490.
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: November 26, 2014
This is version 154 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