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Protein

Glutamate receptor 1

Gene

GRIA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: UniProtKB
  2. extracellular-glutamate-gated ion channel activity Source: GO_Central
  3. glutamate receptor activity Source: ProtInc
  4. PDZ domain binding Source: BHF-UCL

GO - Biological processi

  1. ionotropic glutamate receptor signaling pathway Source: GOC
  2. ion transmembrane transport Source: GOC
  3. long-term memory Source: Ensembl
  4. long term synaptic depression Source: Ensembl
  5. receptor internalization Source: Ensembl
  6. signal transduction Source: ProtInc
  7. synaptic transmission Source: Reactome
  8. synaptic transmission, glutamatergic Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_18307. Trafficking of AMPA receptors.
REACT_18338. Activation of AMPA receptors.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
SignaLinkiP42261.

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:GLUH1, GLUR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:4571. GRIA1.

Subcellular locationi

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

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=M4Add
BLAST
Topological domaini827 – 90680CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: UniProtKB
  2. axonal spine Source: Ensembl
  3. cell junction Source: UniProtKB-KW
  4. cell surface Source: BHF-UCL
  5. dendrite Source: UniProtKB
  6. dendrite membrane Source: Ensembl
  7. dendritic spine Source: UniProtKB
  8. dendritic spine membrane Source: UniProtKB
  9. endocytic vesicle membrane Source: Reactome
  10. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  11. neuronal cell body Source: BHF-UCL
  12. neuron spine Source: BHF-UCL
  13. plasma membrane Source: Reactome
  14. postsynaptic density Source: UniProtKB
  15. postsynaptic membrane Source: GO_Central
  16. recycling endosome Source: UniProtKB
  17. synaptic vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28966.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 906888Glutamate receptor 1PRO_0000011529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi75 ↔ 323By similarity
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Lipidationi603 – 6031S-palmitoyl cysteineBy similarity
Modified residuei645 – 6451PhosphoserineBy similarity
Modified residuei710 – 7101PhosphoserineBy similarity
Disulfide bondi732 ↔ 787By similarity
Lipidationi829 – 8291S-palmitoyl cysteineBy similarity
Modified residuei849 – 8491PhosphoserineBy similarity
Modified residuei863 – 8631PhosphoserineBy similarity

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

PaxDbiP42261.
PRIDEiP42261.

PTM databases

PhosphoSiteiP42261.

Expressioni

Tissue specificityi

Widely expressed in brain.

Gene expression databases

BgeeiP42261.
CleanExiHS_GRIA1.
ExpressionAtlasiP42261. baseline and differential.
GenevestigatoriP42261.

Organism-specific databases

HPAiCAB001965.
HPA035202.

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).2 Publications

Protein-protein interaction databases

BioGridi109147. 18 interactions.
DIPiDIP-41487N.
MINTiMINT-271172.
STRINGi9606.ENSP00000285900.

Structurei

3D structure databases

ProteinModelPortaliP42261.
SMRiP42261. Positions 22-831.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi903 – 9064PDZ-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.
GeneTreeiENSGT00760000118920.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP42261.
KOiK05197.
OMAiMQRSFTI.
OrthoDBiEOG7C2R0J.
PhylomeDBiP42261.
TreeFamiTF315232.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_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 (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Flop (identifier: P42261-1) [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
MQHIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT
60 70 80 90 100
EPPKLLPQID IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF
110 120 130 140 150
CGALHVCFIT PSFPVDTSNQ FVLQLRPELQ DALISIIDHY KWQKFVYIYD
160 170 180 190 200
ADRGLSVLQK VLDTAAEKNW QVTAVNILTT TEEGYRMLFQ DLEKKKERLV
210 220 230 240 250
VVDCESERLN AILGQIIKLE KNGIGYHYIL ANLGFMDIDL NKFKESGANV
260 270 280 290 300
TGFQLVNYTD TIPAKIMQQW KNSDARDHTR 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 RNSGAGASSG GSGENGRVVS HDFPKSMQSI PCMSHSSGMP

LGATGL
Length:906
Mass (Da):101,506
Last modified:October 17, 2006 - v2
Checksum:i03EA1E026D0A9A2F
GO
Isoform Flip (identifier: P42261-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     758-793: NPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD → GPVNLAVLKLSEQGVLDKLKSKWWYDKGECGSKDSG

Show »
Length:906
Mass (Da):101,482
Checksum:i4C1973DBFE98C979
GO
Isoform 3 (identifier: P42261-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-154: FCSQFSKGVY...FVYIYDADRG → C

Show »
Length:826
Mass (Da):92,172
Checksum:i53F69105FB85CFC9
GO
Isoform 4 (identifier: P42261-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.

Show »
Length:837
Mass (Da):93,900
Checksum:i54246EAC4BFFB9F0
GO
Isoform 5 (identifier: P42261-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: MQHIFAFFCTGFLGAVVGANFPNNIQIG → MCCSTHLFQPLQLAGGLEWPWSNLLCFLTPVKLHPEVW

Note: No experimental confirmation available.

Show »
Length:916
Mass (Da):102,888
Checksum:iC49F9C13D74EC7E3
GO
Isoform 6 (identifier: P42261-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: MQHIFAFFCTGFLGAVVGANFPNNIQIG → MCCSTHLFQPLQLAGGLEWPWSNLLCFLTPVKLHPEVW
     758-793: NPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD → GPVNLAVLKLSEQGVLDKLKSKWWYDKGECGSKDSG

Note: No experimental confirmation available.

Show »
Length:916
Mass (Da):102,864
Checksum:i8B6CF1CA44DC94B5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451R → A in CAA41491 (PubMed:1320959).Curated
Sequence conflicti375 – 3751G → S in AAA58395 (PubMed:1311100).Curated
Sequence conflicti738 – 7381G → E in BAH12004 (PubMed:14702039).Curated
Sequence conflicti863 – 8631S → SA in AAA58613 (PubMed:1652753).Curated
Sequence conflicti865 – 8673AGA → TAP in AAA58613 (PubMed:1652753).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti487 – 4871D → N.
Corresponds to variant rs13166146 [ dbSNP | Ensembl ].
VAR_028071
Natural varianti521 – 5211P → T.
Corresponds to variant rs13166161 [ dbSNP | Ensembl ].
VAR_028072
Natural varianti536 – 5361A → S.
Corresponds to variant rs13166438 [ dbSNP | Ensembl ].
VAR_028073
Natural varianti548 – 5481I → M.
Corresponds to variant rs13186241 [ dbSNP | Ensembl ].
VAR_028074
Natural varianti588 – 5881F → L.
Corresponds to variant rs13186534 [ dbSNP | Ensembl ].
VAR_028075

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6969Missing in isoform 4. 1 PublicationVSP_045119Add
BLAST
Alternative sequencei1 – 2828MQHIF…NIQIG → MCCSTHLFQPLQLAGGLEWP WSNLLCFLTPVKLHPEVW in isoform 5 and isoform 6. 1 PublicationVSP_047024Add
BLAST
Alternative sequencei74 – 15481FCSQF…DADRG → C in isoform 3. 1 PublicationVSP_045120Add
BLAST
Alternative sequencei758 – 79336NPVNL…SGGGD → GPVNLAVLKLSEQGVLDKLK SKWWYDKGECGSKDSG in isoform Flip and isoform 6. 2 PublicationsVSP_053349Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64752 mRNA. Translation: AAA58613.1.
X58633 mRNA. Translation: CAA41491.1.
M81886 mRNA. Translation: AAA58395.1.
AK295039 mRNA. Translation: BAH11956.1.
AK295184 mRNA. Translation: BAH12004.1.
AK295827 mRNA. Translation: BAH12192.1.
AK315934 mRNA. Translation: BAH14305.1.
AC010613 Genomic DNA. No translation available.
AC025156 Genomic DNA. No translation available.
AC091960 Genomic DNA. No translation available.
AC091962 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61649.1.
CH471062 Genomic DNA. Translation: EAW61650.1.
BC111734 mRNA. Translation: AAI11735.1.
CCDSiCCDS4322.1. [P42261-1]
CCDS47318.1. [P42261-2]
CCDS58986.1. [P42261-3]
CCDS58987.1. [P42261-5]
CCDS58988.1. [P42261-6]
CCDS58989.1. [P42261-4]
PIRiA40222.
A41273.
S25852.
S38723.
RefSeqiNP_000818.2. NM_000827.3. [P42261-1]
NP_001107655.1. NM_001114183.1. [P42261-2]
NP_001244948.1. NM_001258019.1. [P42261-3]
NP_001244950.1. NM_001258021.1. [P42261-5]
NP_001244951.1. NM_001258022.1. [P42261-6]
NP_001244952.1. NM_001258023.1. [P42261-4]
UniGeneiHs.519693.
Hs.737709.

Genome annotation databases

EnsembliENST00000285900; ENSP00000285900; ENSG00000155511. [P42261-1]
ENST00000340592; ENSP00000339343; ENSG00000155511. [P42261-2]
ENST00000448073; ENSP00000415569; ENSG00000155511. [P42261-6]
ENST00000518142; ENSP00000427920; ENSG00000155511. [P42261-3]
ENST00000518783; ENSP00000428994; ENSG00000155511. [P42261-5]
ENST00000521843; ENSP00000427864; ENSG00000155511. [P42261-4]
GeneIDi2890.
KEGGihsa:2890.
UCSCiuc003luy.4. human. [P42261-1]
uc003lva.4. human. [P42261-2]
uc011dcw.2. human.

Polymorphism databases

DMDMi116242505.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64752 mRNA. Translation: AAA58613.1.
X58633 mRNA. Translation: CAA41491.1.
M81886 mRNA. Translation: AAA58395.1.
AK295039 mRNA. Translation: BAH11956.1.
AK295184 mRNA. Translation: BAH12004.1.
AK295827 mRNA. Translation: BAH12192.1.
AK315934 mRNA. Translation: BAH14305.1.
AC010613 Genomic DNA. No translation available.
AC025156 Genomic DNA. No translation available.
AC091960 Genomic DNA. No translation available.
AC091962 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61649.1.
CH471062 Genomic DNA. Translation: EAW61650.1.
BC111734 mRNA. Translation: AAI11735.1.
CCDSiCCDS4322.1. [P42261-1]
CCDS47318.1. [P42261-2]
CCDS58986.1. [P42261-3]
CCDS58987.1. [P42261-5]
CCDS58988.1. [P42261-6]
CCDS58989.1. [P42261-4]
PIRiA40222.
A41273.
S25852.
S38723.
RefSeqiNP_000818.2. NM_000827.3. [P42261-1]
NP_001107655.1. NM_001114183.1. [P42261-2]
NP_001244948.1. NM_001258019.1. [P42261-3]
NP_001244950.1. NM_001258021.1. [P42261-5]
NP_001244951.1. NM_001258022.1. [P42261-6]
NP_001244952.1. NM_001258023.1. [P42261-4]
UniGeneiHs.519693.
Hs.737709.

3D structure databases

ProteinModelPortaliP42261.
SMRiP42261. Positions 22-831.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109147. 18 interactions.
DIPiDIP-41487N.
MINTiMINT-271172.
STRINGi9606.ENSP00000285900.

Chemistry

BindingDBiP42261.
ChEMBLiCHEMBL2096670.
DrugBankiDB01189. Desflurane.
DB00228. Enflurane.
DB00753. Isoflurane.
DB01028. Methoxyflurane.
DB08883. Perampanel.
DB01236. Sevoflurane.
GuidetoPHARMACOLOGYi444.

PTM databases

PhosphoSiteiP42261.

Polymorphism databases

DMDMi116242505.

Proteomic databases

PaxDbiP42261.
PRIDEiP42261.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285900; ENSP00000285900; ENSG00000155511. [P42261-1]
ENST00000340592; ENSP00000339343; ENSG00000155511. [P42261-2]
ENST00000448073; ENSP00000415569; ENSG00000155511. [P42261-6]
ENST00000518142; ENSP00000427920; ENSG00000155511. [P42261-3]
ENST00000518783; ENSP00000428994; ENSG00000155511. [P42261-5]
ENST00000521843; ENSP00000427864; ENSG00000155511. [P42261-4]
GeneIDi2890.
KEGGihsa:2890.
UCSCiuc003luy.4. human. [P42261-1]
uc003lva.4. human. [P42261-2]
uc011dcw.2. human.

Organism-specific databases

CTDi2890.
GeneCardsiGC05P152850.
H-InvDBHIX0032120.
HGNCiHGNC:4571. GRIA1.
HPAiCAB001965.
HPA035202.
MIMi138248. gene.
neXtProtiNX_P42261.
PharmGKBiPA28966.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG316680.
GeneTreeiENSGT00760000118920.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP42261.
KOiK05197.
OMAiMQRSFTI.
OrthoDBiEOG7C2R0J.
PhylomeDBiP42261.
TreeFamiTF315232.

Enzyme and pathway databases

ReactomeiREACT_18307. Trafficking of AMPA receptors.
REACT_18338. Activation of AMPA receptors.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
SignaLinkiP42261.

Miscellaneous databases

ChiTaRSiGRIA1. human.
GeneWikiiGRIA1.
GenomeRNAii2890.
NextBioi11425.
PROiP42261.
SOURCEiSearch...

Gene expression databases

BgeeiP42261.
CleanExiHS_GRIA1.
ExpressionAtlasiP42261. baseline and differential.
GenevestigatoriP42261.

Family and domain databases

InterProiIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu/Gly-bd.
IPR001508. Iono_rcpt_met.
IPR001320. Iontro_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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and chromosomal localization of one of the human glutamate receptor genes."
    Puckett C., Gomez C.M., Korenberg J.R., Tung H., Meier T.J., Chen X.N., Hood L.E.
    Proc. Natl. Acad. Sci. U.S.A. 88:7557-7561(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP).
  2. "The human glutamate receptor cDNA GluR1: cloning, sequencing, expression and localization to chromosome 5."
    Potier M.-C., Spillantini M.G., Carter N.P.
    DNA Seq. 2:211-218(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
    Tissue: Hippocampus.
  3. "Molecular cloning, chromosomal mapping, and functional expression of human brain glutamate receptors."
    Sun W., Ferrer-Montiel A.V., Schinder A.F., McPherson J.P., Evans G.A., Montal M.
    Proc. Natl. Acad. Sci. U.S.A. 89:1443-1447(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLOP).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5 AND 6).
    Tissue: Brain, Cerebellum and Hippocampus.
  5. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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).
  8. "Hippocampal AMPA receptor gating controlled by both TARP and cornichon proteins."
    Kato A.S., Gill M.B., Ho M.T., Yu H., Tu Y., Siuda E.R., Wang H., Qian Y.W., Nisenbaum E.S., Tomita S., Bredt D.S.
    Neuron 68:1082-1096(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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: FUNCTION, INTERACTION WITH CNIH2 AND CACNG2.
  10. "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.

Entry informationi

Entry nameiGRIA1_HUMAN
AccessioniPrimary (citable) accession number: P42261
Secondary accession number(s): B7Z2S0
, B7Z2W8, B7Z3F6, B7Z9G9, D3DQI4, E7ESV8, Q2NKM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 17, 2006
Last modified: March 4, 2015
This is version 161 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.