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P42263 (GRIA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GRIA3
Synonyms:GLUR3, GLURC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length894 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

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.

Subcellular location

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.

Domain

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

Post-translational modification

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

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.

Sequence similarities

Belongs to the glutamate-gated ion channel (TC 1.A.10.1) family. GRIA3 subfamily. [View classification]

Caution

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

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Mental retardation
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamate receptor signaling pathway

Traceable author statement PubMed 1709304. Source: ProtInc

ion transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from direct assay Ref.7. Source: GOC

synaptic transmission

Traceable author statement. Source: Reactome

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

transport

Traceable author statement PubMed 1709304. Source: ProtInc

   Cellular_componentalpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionalpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity

Inferred from direct assay Ref.7. Source: UniProtKB

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Flop (identifier: P42263-1)

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.
Isoform Flip (identifier: P42263-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 894866Glutamate receptor 3
PRO_0000011536

Regions

Topological domain29 – 552524Extracellular By similarity
Transmembrane553 – 57321Helical; By similarity
Topological domain574 – 60229Cytoplasmic By similarity
Intramembrane603 – 61816Helical; Pore-forming; By similarity
Intramembrane619 – 6213 By similarity
Topological domain622 – 6276Cytoplasmic By similarity
Transmembrane628 – 64821Helical; By similarity
Topological domain649 – 823175Extracellular By similarity
Transmembrane824 – 84421Helical; Name=M4; By similarity
Topological domain845 – 89450Cytoplasmic By similarity
Region508 – 5103Glutamate binding By similarity
Region686 – 6872Glutamate binding By similarity

Sites

Binding site4801Glutamate By similarity
Binding site5151Glutamate By similarity
Binding site7371Glutamate By similarity

Amino acid modifications

Modified residue8771Phosphotyrosine By similarity
Modified residue8871Phosphotyrosine By similarity
Lipidation6211S-palmitoyl cysteine By similarity
Lipidation8471S-palmitoyl cysteine By similarity
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Glycosylation4151N-linked (GlcNAc...) Potential
Glycosylation4221N-linked (GlcNAc...) Potential
Disulfide bond91 ↔ 340 By similarity
Disulfide bond750 ↔ 805 By similarity

Natural variations

Alternative sequence776 – 81136NAVNL…SGGGD → TPVNLAVLKLSEQGILDKLK NKWWYDKGECGAKDSG in isoform Flip.
VSP_053351
Natural variant4501R → Q in MRX94. Ref.8
VAR_043484
Natural variant5251F → L. Ref.1 Ref.3 Ref.4
Corresponds to variant rs1052538 [ dbSNP | Ensembl ].
VAR_023579
Natural variant6311R → S in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics. Ref.8
VAR_043485
Natural variant7061M → T in MRX94; homomers have minimal or no current; heteromers have altered desensitization kinetics. Ref.8
VAR_043486
Natural variant8331G → R in MRX94; reduced receptor expression possibly due to rapid degradation. Ref.8
VAR_043487

Experimental info

Sequence conflict1951N → H in AAF61847. Ref.3
Sequence conflict7751R → G in AAA67922. Ref.1
Sequence conflict7751R → G in AAA67923. Ref.1
Sequence conflict7751R → G in CAA57567. Ref.2
Sequence conflict7751R → G in AAF61847. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform Flop [UniParc].

Last modified October 11, 2005. Version 2.
Checksum: 178589A870E0D102

FASTA894101,157
        10         20         30         40         50         60 
MARQKKMGQS VLRAVFFLVL GLLGHSHGGF PNTISIGGLF MRNTVQEHSA FRFAVQLYNT 

        70         80         90        100        110        120 
NQNTTEKPFH LNYHVDHLDS SNSFSVTNAF CSQFSRGVYA IFGFYDQMSM NTLTSFCGAL 

       130        140        150        160        170        180 
HTSFVTPSFP TDADVQFVIQ MRPALKGAIL SLLGHYKWEK FVYLYDTERG FSILQAIMEA 

       190        200        210        220        230        240 
AVQNNWQVTA RSVGNIKDVQ EFRRIIEEMD RRQEKRYLID CEVERINTIL EQVVILGKHS 

       250        260        270        280        290        300 
RGYHYMLANL GFTDILLERV MHGGANITGF QIVNNENPMV QQFIQRWVRL DEREFPEAKN 

       310        320        330        340        350        360 
APLKYTSALT HDAILVIAEA FRYLRRQRVD VSRRGSAGDC LANPAVPWSQ GIDIERALKM 

       370        380        390        400        410        420 
VQVQGMTGNI QFDTYGRRTN YTIDVYEMKV SGSRKAGYWN EYERFVPFSD QQISNDSASS 

       430        440        450        460        470        480 
ENRTIVVTTI LESPYVMYKK NHEQLEGNER YEGYCVDLAY EIAKHVRIKY KLSIVGDGKY 

       490        500        510        520        530        540 
GARDPETKIW NGMVGELVYG RADIAVAPLT ITLVREEVID FSKPFMSLGI SIMIKKPQKS 

       550        560        570        580        590        600 
KPGVFSFLDP LAYEIWMCIV FAYIGVSVVL FLVSRFSPYE WHLEDNNEEP RDPQSPPDPP 

       610        620        630        640        650        660 
NEFGIFNSLW FSLGAFMQQG CDISPRSLSG RIVGGVWWFF TLIIISSYTA NLAAFLTVER 

       670        680        690        700        710        720 
MVSPIESAED LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWSYMKSAE PSVFTKTTAD 

       730        740        750        760        770        780 
GVARVRKSKG KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSALRNAVNL 

       790        800        810        820        830        840 
AVLKLNEQGL LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAMM 

       850        860        870        880        890 
VALIEFCYKS RAESKRMKLT KNTQNFKPAP ATNTQNYATY REGYNVYGTE SVKI 

« Hide

Isoform Flip [UniParc].

Checksum: EB3ED4EBBA353021
Show »

FASTA894101,228

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Mutations in ionotropic AMPA receptor 3 alter channel properties and are associated with moderate cognitive impairment in humans."
Wu Y., Arai A.C., Rumbaugh G., Srivastava A.K., Turner G., Hayashi T., Suzuki E., Jiang Y., Zhang L., Rodriguez J., Boyle J., Tarpey P., Raymond F.L., Nevelsteen J., Froyen G., Stratton M., Futreal A., Gecz J. expand/collapse author list , Stevenson R., Schwartz C.E., Valle D., Huganir R.L., Wang T.
Proc. Natl. Acad. Sci. U.S.A. 104:18163-18168(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MRX94 GLN-450; SER-631; THR-706 AND ARG-833, CHARACTERIZATION OF VARIANTS MRX94 SER-631; THR-706 AND ARG-833.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U10302 mRNA. Translation: AAA67923.1.
U10301 mRNA. Translation: AAA67922.1.
X82068 mRNA. Translation: CAA57567.1.
AF159277 expand/collapse EMBL AC list , AF159262, AF159263, AF159264, AF159265, AF159266, AF159267, AF159268, AF159269, AF159270, AF159271, AF159272, AF159273, AF159274, AF159275 Genomic DNA. Translation: AAF61847.1.
AF166365 expand/collapse EMBL AC list , AF166362, AF166363, AF166364 Genomic DNA. Translation: AAF97857.1.
AF167332 expand/collapse EMBL AC list , AF166366, AF166367, AF166368, AF166369, AF166370, AF166371, AF166372, AF166373, AF166375 Genomic DNA. Translation: AAF97858.1.
AF167332 expand/collapse EMBL AC list , AF166366, AF166367, AF166368, AF166369, AF166370, AF166371, AF166372, AF166373, AF166374 Genomic DNA. Translation: AAF97859.1.
AL356213 expand/collapse EMBL AC list , AL035426, AL590139, Z83848, Z82899 Genomic DNA. Translation: CAI95643.1.
AL356213 expand/collapse EMBL AC list , AL035426, AL590139, Z83848, Z82899 Genomic DNA. Translation: CAI95644.1.
AL590139 expand/collapse EMBL AC list , AL035426, AL356213, Z83848, Z82899 Genomic DNA. Translation: CAI95164.1.
AL590139 expand/collapse EMBL AC list , AL035426, AL356213, Z83848, Z82899 Genomic DNA. Translation: CAI95165.1.
Z83848 expand/collapse EMBL AC list , AL590139, AL356213, AL035426, Z82899 Genomic DNA. Translation: CAI95709.1.
Z83848 expand/collapse EMBL AC list , AL590139, AL356213, AL035426, Z82899 Genomic DNA. Translation: CAI95710.1.
Z82899 expand/collapse EMBL AC list , Z83848, AL590139, AL356213, AL035426 Genomic DNA. Translation: CAI95664.1.
Z82899 expand/collapse EMBL AC list , Z83848, AL590139, AL356213, AL035426 Genomic DNA. Translation: CAI95665.1.
AL035426 expand/collapse EMBL AC list , Z83848, Z82899, AL590139, AL356213 Genomic DNA. Translation: CAI95683.1.
AL035426 expand/collapse EMBL AC list , Z83848, Z82899, AL590139, AL356213 Genomic DNA. Translation: CAI95684.1.
CH471107 Genomic DNA. Translation: EAX11865.1.
CH471107 Genomic DNA. Translation: EAX11867.1.
PIRS49460.
S50128.
S53696.
RefSeqNP_000819.3. NM_000828.4.
NP_015564.4. NM_007325.4.
UniGeneHs.377070.

3D structure databases

ProteinModelPortalP42263.
SMRP42263. Positions 32-849.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109149. 4 interactions.
DIPDIP-46195N.
STRING9606.ENSP00000360302.

Chemistry

BindingDBP42263.
ChEMBLCHEMBL2096670.
DrugBankDB00142. L-Glutamic Acid.
GuidetoPHARMACOLOGY446.

Protein family/group databases

TCDB1.A.10.1.4. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

PTM databases

PhosphoSiteP42263.

Polymorphism databases

DMDM77416864.

Proteomic databases

PaxDbP42263.
PRIDEP42263.

Protocols and materials databases

DNASU2892.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264357; ENSP00000264357; ENSG00000125675. [P42263-1]
ENST00000371251; ENSP00000360297; ENSG00000125675. [P42263-1]
ENST00000371256; ENSP00000360302; ENSG00000125675. [P42263-2]
GeneID2892.
KEGGhsa:2892.
UCSCuc004etq.4. human. [P42263-2]
uc004etr.4. human. [P42263-1]

Organism-specific databases

CTD2892.
GeneCardsGC0XP122318.
HGNCHGNC:4573. GRIA3.
HPACAB007799.
MIM300699. phenotype.
305915. gene.
neXtProtNX_P42263.
Orphanet364028. X-linked intellectual disability due to GRIA3 anomalies.
PharmGKBPA28968.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316680.
HOVERGENHBG051839.
InParanoidP42263.
KOK05199.
OMADQQVSND.
OrthoDBEOG7C2R0J.
PhylomeDBP42263.
TreeFamTF315232.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
SignaLinkP42263.

Gene expression databases

ArrayExpressP42263.
BgeeP42263.
CleanExHS_GRIA3.
GenevestigatorP42263.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR019594. Glu_rcpt_Glu/Gly-bd.
IPR001320. Iontro_glu_rcpt.
IPR001508. NMDA_rcpt.
IPR028082. Peripla_BP_I.
[Graphical view]
PfamPF01094. ANF_receptor. 1 hit.
PF00060. Lig_chan. 1 hit.
PF10613. Lig_chan-Glu_bd. 1 hit.
[Graphical view]
PRINTSPR00177. NMDARECEPTOR.
SMARTSM00918. Lig_chan-Glu_bd. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
SUPFAMSSF53822. SSF53822. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGRIA3. human.
GeneWikiGRIA3.
GenomeRNAi2892.
NextBio11437.
PROP42263.
SOURCESearch...

Entry information

Entry nameGRIA3_HUMAN
AccessionPrimary (citable) accession number: P42263
Secondary accession number(s): D3DTF1 expand/collapse secondary AC list , Q4VXD5, Q4VXD6, Q9HDA0, Q9HDA1, Q9HDA2, Q9P0H1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 11, 2005
Last modified: April 16, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM