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P42263

- GRIA3_HUMAN

UniProt

P42263 - GRIA3_HUMAN

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Protein

Glutamate receptor 3

Gene

GRIA3

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 sitei480 – 4801GlutamateBy similarity
Binding sitei515 – 5151GlutamateBy similarity
Binding sitei737 – 7371GlutamateBy 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: RefGenome

GO - Biological processi

  1. glutamate receptor signaling pathway Source: ProtInc
  2. ionotropic glutamate receptor signaling pathway Source: GOC
  3. ion transmembrane transport Source: GOC
  4. synaptic transmission Source: Reactome
  5. synaptic transmission, glutamatergic Source: RefGenome
  6. transport Source: ProtInc
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.
SignaLinkiP42263.

Protein family/group databases

TCDBi1.A.10.1.4. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate receptor 3
Short name:
GluR-3
Alternative name(s):
AMPA-selective glutamate receptor 3
GluR-C
GluR-K3
Glutamate receptor ionotropic, AMPA 3
Short name:
GluA3
Gene namesi
Name:GRIA3
Synonyms:GLUR3, GLURC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:4573. GRIA3.

Subcellular locationi

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein
Note: Interaction with CNIH2 and CNIH3 promotes cell surface expression.By similarity

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. plasma membrane Source: Reactome
  6. postsynaptic membrane Source: RefGenome
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Mental retardation, X-linked 94 (MRX94) [MIM:300699]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Intellectual deficiency is the only primary symptom of non-syndromic X-linked mental retardation, while syndromic mental retardation presents with associated physical, neurological and/or psychiatric manifestations. MRX94 patients have moderate mental retardation. Other variable features are macrocephaly, seizures, myoclonic jerks, autistic behavior, asthenic body habitus, distal muscle weakness and hyporeflexia.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti450 – 4501R → Q in MRX94. 1 Publication
VAR_043484
Natural varianti631 – 6311R → S in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics. 1 Publication
VAR_043485
Natural varianti706 – 7061M → T in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics. 1 Publication
VAR_043486
Natural varianti833 – 8331G → R in MRX94; reduced receptor expression possibly due to rapid degradation. 1 Publication
VAR_043487

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi300699. phenotype.
Orphaneti364028. X-linked intellectual disability due to GRIA3 anomalies.
PharmGKBiPA28968.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence AnalysisAdd
BLAST
Chaini29 – 894866Glutamate receptor 3PRO_0000011536Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi63 – 631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi91 ↔ 340By similarity
Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi422 – 4221N-linked (GlcNAc...)Sequence Analysis
Lipidationi621 – 6211S-palmitoyl cysteineBy similarity
Disulfide bondi750 ↔ 805By similarity
Lipidationi847 – 8471S-palmitoyl cysteineBy similarity
Modified residuei877 – 8771PhosphotyrosineBy similarity
Modified residuei887 – 8871PhosphotyrosineBy similarity

Post-translational modificationi

Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-621 palmitoylation leads to Golgi retention and decreased cell surface expression. In contrast, Cys-847 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

PaxDbiP42263.
PRIDEiP42263.

PTM databases

PhosphoSiteiP42263.

Expressioni

Gene expression databases

BgeeiP42263.
CleanExiHS_GRIA3.
ExpressionAtlasiP42263. baseline and differential.
GenevestigatoriP42263.

Organism-specific databases

HPAiCAB007799.

Interactioni

Subunit structurei

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Interacts with PRKCABP, GRIP1 and GRIP2 (By similarity). Found in a complex with GRIA1, GRIA2, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 (By similarity).By similarity

Protein-protein interaction databases

BioGridi109149. 5 interactions.
DIPiDIP-46195N.
STRINGi9606.ENSP00000360302.

Structurei

3D structure databases

ProteinModelPortaliP42263.
SMRiP42263. Positions 32-849.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 552524ExtracellularBy similarityAdd
BLAST
Topological domaini574 – 60229CytoplasmicBy similarityAdd
BLAST
Topological domaini622 – 6276CytoplasmicBy similarity
Topological domaini649 – 823175ExtracellularBy similarityAdd
BLAST
Topological domaini845 – 89450CytoplasmicBy similarityAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei603 – 61816Helical; Pore-formingBy similarityAdd
BLAST
Intramembranei619 – 6213By similarity

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei553 – 57321HelicalBy similarityAdd
BLAST
Transmembranei628 – 64821HelicalBy similarityAdd
BLAST
Transmembranei824 – 84421Helical; Name=M4By similarityAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni508 – 5103Glutamate bindingBy similarity
Regioni686 – 6872Glutamate bindingBy similarity

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

eggNOGiNOG316680.
GeneTreeiENSGT00760000118920.
HOVERGENiHBG051839.
InParanoidiP42263.
KOiK05199.
OMAiMVQQFLQ.
OrthoDBiEOG7C2R0J.
PhylomeDBiP42263.
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 (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: P42263-1) [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
MARQKKMGQS VLRAVFFLVL GLLGHSHGGF PNTISIGGLF MRNTVQEHSA
60 70 80 90 100
FRFAVQLYNT NQNTTEKPFH LNYHVDHLDS SNSFSVTNAF CSQFSRGVYA
110 120 130 140 150
IFGFYDQMSM NTLTSFCGAL HTSFVTPSFP TDADVQFVIQ MRPALKGAIL
160 170 180 190 200
SLLGHYKWEK FVYLYDTERG FSILQAIMEA AVQNNWQVTA RSVGNIKDVQ
210 220 230 240 250
EFRRIIEEMD RRQEKRYLID CEVERINTIL EQVVILGKHS RGYHYMLANL
260 270 280 290 300
GFTDILLERV MHGGANITGF QIVNNENPMV QQFIQRWVRL DEREFPEAKN
310 320 330 340 350
APLKYTSALT HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ
360 370 380 390 400
GIDIERALKM VQVQGMTGNI QFDTYGRRTN YTIDVYEMKV SGSRKAGYWN
410 420 430 440 450
EYERFVPFSD QQISNDSASS ENRTIVVTTI LESPYVMYKK NHEQLEGNER
460 470 480 490 500
YEGYCVDLAY EIAKHVRIKY KLSIVGDGKY GARDPETKIW NGMVGELVYG
510 520 530 540 550
RADIAVAPLT ITLVREEVID FSKPFMSLGI SIMIKKPQKS KPGVFSFLDP
560 570 580 590 600
LAYEIWMCIV FAYIGVSVVL FLVSRFSPYE WHLEDNNEEP RDPQSPPDPP
610 620 630 640 650
NEFGIFNSLW FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA
660 670 680 690 700
NLAAFLTVER MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE
710 720 730 740 750
KMWSYMKSAE PSVFTKTTAD GVARVRKSKG KFAFLLESTM NEYIEQRKPC
760 770 780 790 800
DTMKVGGNLD SKGYGVATPK GSALRNAVNL AVLKLNEQGL LDKLKNKWWY
810 820 830 840 850
DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAMM VALIEFCYKS
860 870 880 890
RAESKRMKLT KNTQNFKPAP ATNTQNYATY REGYNVYGTE SVKI
Length:894
Mass (Da):101,157
Last modified:October 11, 2005 - v2
Checksum:i178589A870E0D102
GO
Isoform Flip (identifier: P42263-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     776-811: NAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD → TPVNLAVLKLSEQGILDKLKNKWWYDKGECGAKDSG

Show »
Length:894
Mass (Da):101,228
Checksum:iEB3ED4EBBA353021
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951N → H in AAF61847. (PubMed:10644433)Curated
Sequence conflicti775 – 7751R → G in AAA67922. (PubMed:7918660)Curated
Sequence conflicti775 – 7751R → G in AAA67923. (PubMed:7918660)Curated
Sequence conflicti775 – 7751R → G in CAA57567. 1 PublicationCurated
Sequence conflicti775 – 7751R → G in AAF61847. (PubMed:10644433)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti450 – 4501R → Q in MRX94. 1 Publication
VAR_043484
Natural varianti525 – 5251F → L.3 Publications
Corresponds to variant rs1052538 [ dbSNP | Ensembl ].
VAR_023579
Natural varianti631 – 6311R → S in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics. 1 Publication
VAR_043485
Natural varianti706 – 7061M → T in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics. 1 Publication
VAR_043486
Natural varianti833 – 8331G → R in MRX94; reduced receptor expression possibly due to rapid degradation. 1 Publication
VAR_043487

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei776 – 81136NAVNL…SGGGD → TPVNLAVLKLSEQGILDKLK NKWWYDKGECGAKDSG in isoform Flip. 1 PublicationVSP_053351Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U10302 mRNA. Translation: AAA67923.1.
U10301 mRNA. Translation: AAA67922.1.
X82068 mRNA. Translation: CAA57567.1.
AF159277
, AF159262, AF159263, AF159264, AF159265, AF159266, AF159267, AF159268, AF159269, AF159270, AF159271, AF159272, AF159273, AF159274, AF159275 Genomic DNA. Translation: AAF61847.1.
AF166365
, AF166362, AF166363, AF166364 Genomic DNA. Translation: AAF97857.1.
AF167332
, AF166366, AF166367, AF166368, AF166369, AF166370, AF166371, AF166372, AF166373, AF166375 Genomic DNA. Translation: AAF97858.1.
AF167332
, AF166366, AF166367, AF166368, AF166369, AF166370, AF166371, AF166372, AF166373, AF166374 Genomic DNA. Translation: AAF97859.1.
AL356213
, AL035426, AL590139, Z83848, Z82899 Genomic DNA. Translation: CAI95643.1.
AL356213
, AL035426, AL590139, Z83848, Z82899 Genomic DNA. Translation: CAI95644.1.
AL590139
, AL035426, AL356213, Z83848, Z82899 Genomic DNA. Translation: CAI95164.1.
AL590139
, AL035426, AL356213, Z83848, Z82899 Genomic DNA. Translation: CAI95165.1.
Z83848
, AL590139, AL356213, AL035426, Z82899 Genomic DNA. Translation: CAI95709.1.
Z83848
, AL590139, AL356213, AL035426, Z82899 Genomic DNA. Translation: CAI95710.1.
Z82899
, Z83848, AL590139, AL356213, AL035426 Genomic DNA. Translation: CAI95664.1.
Z82899
, Z83848, AL590139, AL356213, AL035426 Genomic DNA. Translation: CAI95665.1.
AL035426
, Z83848, Z82899, AL590139, AL356213 Genomic DNA. Translation: CAI95683.1.
AL035426
, Z83848, Z82899, AL590139, AL356213 Genomic DNA. Translation: CAI95684.1.
CH471107 Genomic DNA. Translation: EAX11865.1.
CH471107 Genomic DNA. Translation: EAX11867.1.
CCDSiCCDS14604.1. [P42263-1]
CCDS14605.1. [P42263-2]
PIRiS49460.
S50128.
S53696.
RefSeqiNP_000819.3. NM_000828.4.
NP_015564.4. NM_007325.4.
UniGeneiHs.377070.

Genome annotation databases

EnsembliENST00000541091; ENSP00000446440; ENSG00000125675. [P42263-1]
ENST00000620443; ENSP00000478489; ENSG00000125675. [P42263-2]
ENST00000622768; ENSP00000481554; ENSG00000125675. [P42263-1]
GeneIDi2892.
KEGGihsa:2892.
UCSCiuc004etq.4. human. [P42263-2]
uc004etr.4. human. [P42263-1]

Polymorphism databases

DMDMi77416864.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U10302 mRNA. Translation: AAA67923.1 .
U10301 mRNA. Translation: AAA67922.1 .
X82068 mRNA. Translation: CAA57567.1 .
AF159277
, AF159262 , AF159263 , AF159264 , AF159265 , AF159266 , AF159267 , AF159268 , AF159269 , AF159270 , AF159271 , AF159272 , AF159273 , AF159274 , AF159275 Genomic DNA. Translation: AAF61847.1 .
AF166365
, AF166362 , AF166363 , AF166364 Genomic DNA. Translation: AAF97857.1 .
AF167332
, AF166366 , AF166367 , AF166368 , AF166369 , AF166370 , AF166371 , AF166372 , AF166373 , AF166375 Genomic DNA. Translation: AAF97858.1 .
AF167332
, AF166366 , AF166367 , AF166368 , AF166369 , AF166370 , AF166371 , AF166372 , AF166373 , AF166374 Genomic DNA. Translation: AAF97859.1 .
AL356213
, AL035426 , AL590139 , Z83848 , Z82899 Genomic DNA. Translation: CAI95643.1 .
AL356213
, AL035426 , AL590139 , Z83848 , Z82899 Genomic DNA. Translation: CAI95644.1 .
AL590139
, AL035426 , AL356213 , Z83848 , Z82899 Genomic DNA. Translation: CAI95164.1 .
AL590139
, AL035426 , AL356213 , Z83848 , Z82899 Genomic DNA. Translation: CAI95165.1 .
Z83848
, AL590139 , AL356213 , AL035426 , Z82899 Genomic DNA. Translation: CAI95709.1 .
Z83848
, AL590139 , AL356213 , AL035426 , Z82899 Genomic DNA. Translation: CAI95710.1 .
Z82899
, Z83848 , AL590139 , AL356213 , AL035426 Genomic DNA. Translation: CAI95664.1 .
Z82899
, Z83848 , AL590139 , AL356213 , AL035426 Genomic DNA. Translation: CAI95665.1 .
AL035426
, Z83848 , Z82899 , AL590139 , AL356213 Genomic DNA. Translation: CAI95683.1 .
AL035426
, Z83848 , Z82899 , AL590139 , AL356213 Genomic DNA. Translation: CAI95684.1 .
CH471107 Genomic DNA. Translation: EAX11865.1 .
CH471107 Genomic DNA. Translation: EAX11867.1 .
CCDSi CCDS14604.1. [P42263-1 ]
CCDS14605.1. [P42263-2 ]
PIRi S49460.
S50128.
S53696.
RefSeqi NP_000819.3. NM_000828.4.
NP_015564.4. NM_007325.4.
UniGenei Hs.377070.

3D structure databases

ProteinModelPortali P42263.
SMRi P42263. Positions 32-849.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109149. 5 interactions.
DIPi DIP-46195N.
STRINGi 9606.ENSP00000360302.

Chemistry

BindingDBi P42263.
ChEMBLi CHEMBL2096670.
DrugBanki DB01356. Lithium.
GuidetoPHARMACOLOGYi 446.

Protein family/group databases

TCDBi 1.A.10.1.4. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSitei P42263.

Polymorphism databases

DMDMi 77416864.

Proteomic databases

PaxDbi P42263.
PRIDEi P42263.

Protocols and materials databases

DNASUi 2892.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000541091 ; ENSP00000446440 ; ENSG00000125675 . [P42263-1 ]
ENST00000620443 ; ENSP00000478489 ; ENSG00000125675 . [P42263-2 ]
ENST00000622768 ; ENSP00000481554 ; ENSG00000125675 . [P42263-1 ]
GeneIDi 2892.
KEGGi hsa:2892.
UCSCi uc004etq.4. human. [P42263-2 ]
uc004etr.4. human. [P42263-1 ]

Organism-specific databases

CTDi 2892.
GeneCardsi GC0XP122318.
HGNCi HGNC:4573. GRIA3.
HPAi CAB007799.
MIMi 300699. phenotype.
305915. gene.
neXtProti NX_P42263.
Orphaneti 364028. X-linked intellectual disability due to GRIA3 anomalies.
PharmGKBi PA28968.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG316680.
GeneTreei ENSGT00760000118920.
HOVERGENi HBG051839.
InParanoidi P42263.
KOi K05199.
OMAi MVQQFLQ.
OrthoDBi EOG7C2R0J.
PhylomeDBi P42263.
TreeFami TF315232.

Enzyme and pathway databases

Reactomei REACT_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.
SignaLinki P42263.

Miscellaneous databases

ChiTaRSi GRIA3. human.
GeneWikii GRIA3.
GenomeRNAii 2892.
NextBioi 11437.
PROi P42263.
SOURCEi Search...

Gene expression databases

Bgeei P42263.
CleanExi HS_GRIA3.
ExpressionAtlasi P42263. baseline and differential.
Genevestigatori P42263.

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. "Human glutamate receptor hGluR3 flip and flop isoforms: cloning and sequencing of the cDNAs and primary structure of the proteins."
    Rampersad V., Elliott C.E., Nutt S.L., Foldes R.L., Kamboj R.K.
    Biochim. Biophys. Acta 1219:563-566(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS FLIP AND FLOP), VARIANT LEU-525.
    Tissue: Hippocampus.
  2. McLaughlin D.P., Kerwin R.W.
    Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Characterization of the human glutamate receptor subunit 3 gene (GRIA3), a candidate for bipolar disorder and nonspecific X-linked mental retardation."
    Gecz J., Barnett S., Liu J., Hollway G., Donnelly A., Eyre H., Eshkevari H.S., Baltazar R., Grunn A., Nagaraja R., Gilliam C., Peltonen L., Sutherland G.R., Baron M., Mulley J.C.
    Genomics 62:356-368(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-525.
  4. "Candidate gene analysis in Rett syndrome and the identification of 21 SNPs in Xq."
    Amir R., Dahle E.J., Toriolo D., Zoghbi H.Y.
    Am. J. Med. Genet. 90:69-71(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-525.
  5. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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.
  8. Cited for: VARIANTS MRX94 GLN-450; SER-631; THR-706 AND ARG-833, CHARACTERIZATION OF VARIANTS MRX94 SER-631; THR-706 AND ARG-833.

Entry informationi

Entry nameiGRIA3_HUMAN
AccessioniPrimary (citable) accession number: P42263
Secondary accession number(s): D3DTF1
, Q4VXD5, Q4VXD6, Q9HDA0, Q9HDA1, Q9HDA2, Q9P0H1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 11, 2005
Last modified: October 29, 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
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.

Caution

It is uncertain whether Met-1 or Met-7 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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