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P42261 (GRIA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. 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 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 names
Name:GRIA1
Synonyms:GLUH1, GLUR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length906 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9

Subunit structure

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). Ref.9 Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. 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. Ref.10

Tissue specificity

Widely expressed in brain.

Domain

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

Post-translational modification

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.

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. GRIA1 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Cell projection
Endoplasmic reticulum
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   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_procession transmembrane transport

Inferred from Biological aspect of Ancestor. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from direct assay Ref.9Ref.8. Source: GOC

long-term memory

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.3. Source: ProtInc

synaptic transmission

Traceable author statement. Source: Reactome

synaptic transmission, glutamatergic

Inferred from Biological aspect of Ancestor. Source: RefGenome

   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

cell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite membrane

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from sequence or structural similarity. Source: UniProtKB

endocytic vesicle membrane

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron spine

Inferred from sequence or structural similarity. Source: BHF-UCL

neuronal cell body

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from sequence or structural similarity. Source: UniProtKB

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionPDZ domain binding

Inferred from sequence or structural similarity. Source: BHF-UCL

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

Inferred from direct assay Ref.9Ref.8. Source: UniProtKB

extracellular-glutamate-gated ion channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

glutamate receptor activity

Traceable author statement Ref.2. Source: ProtInc

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform Flop (identifier: P42261-1)

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: P42261-2)

The sequence of this isoform differs from the canonical sequence as follows:
     758-793: NPVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD → GPVNLAVLKLSEQGVLDKLKSKWWYDKGECGSKDSG
Isoform 3 (identifier: P42261-3)

The sequence of this isoform differs from the canonical sequence as follows:
     74-154: FCSQFSKGVY...FVYIYDADRG → C
Isoform 4 (identifier: P42261-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: Missing.
Isoform 5 (identifier: P42261-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: MQHIFAFFCTGFLGAVVGANFPNNIQIG → MCCSTHLFQPLQLAGGLEWPWSNLLCFLTPVKLHPEVW
Note: No experimental confirmation available.
Isoform 6 (identifier: P42261-6)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 906888Glutamate receptor 1
PRO_0000011529

Regions

Topological domain19 – 536518Extracellular By similarity
Transmembrane537 – 55721Helical; By similarity
Topological domain558 – 58427Cytoplasmic By similarity
Intramembrane585 – 60016Helical; Pore-forming; By similarity
Intramembrane601 – 6033 By similarity
Topological domain604 – 6096Cytoplasmic By similarity
Transmembrane610 – 63021Helical; By similarity
Topological domain631 – 805175Extracellular By similarity
Transmembrane806 – 82621Helical; Name=M4
Topological domain827 – 90680Cytoplasmic By similarity
Region492 – 4943Glutamate binding By similarity
Region668 – 6692Glutamate binding By similarity
Motif903 – 9064PDZ-binding

Sites

Binding site4641Glutamate By similarity
Binding site4991Glutamate By similarity
Binding site7191Glutamate By similarity

Amino acid modifications

Modified residue6451Phosphoserine By similarity
Modified residue7101Phosphoserine By similarity
Modified residue8491Phosphoserine By similarity
Modified residue8631Phosphoserine By similarity
Lipidation6031S-palmitoyl cysteine By similarity
Lipidation8291S-palmitoyl cysteine By similarity
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Potential
Glycosylation4011N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Disulfide bond75 ↔ 323 By similarity
Disulfide bond732 ↔ 787 By similarity

Natural variations

Alternative sequence1 – 6969Missing in isoform 4.
VSP_045119
Alternative sequence1 – 2828MQHIF…NIQIG → MCCSTHLFQPLQLAGGLEWP WSNLLCFLTPVKLHPEVW in isoform 5 and isoform 6.
VSP_047024
Alternative sequence74 – 15481FCSQF…DADRG → C in isoform 3.
VSP_045120
Alternative sequence758 – 79336NPVNL…SGGGD → GPVNLAVLKLSEQGVLDKLK SKWWYDKGECGSKDSG in isoform Flip and isoform 6.
VSP_053349
Natural variant4871D → N.
Corresponds to variant rs13166146 [ dbSNP | Ensembl ].
VAR_028071
Natural variant5211P → T.
Corresponds to variant rs13166161 [ dbSNP | Ensembl ].
VAR_028072
Natural variant5361A → S.
Corresponds to variant rs13166438 [ dbSNP | Ensembl ].
VAR_028073
Natural variant5481I → M.
Corresponds to variant rs13186241 [ dbSNP | Ensembl ].
VAR_028074
Natural variant5881F → L.
Corresponds to variant rs13186534 [ dbSNP | Ensembl ].
VAR_028075

Experimental info

Sequence conflict3451R → A in CAA41491. Ref.2
Sequence conflict3751G → S in AAA58395. Ref.3
Sequence conflict7381G → E in BAH12004. Ref.4
Sequence conflict8631S → SA in AAA58613. Ref.1
Sequence conflict865 – 8673AGA → TAP in AAA58613. Ref.1

Sequences

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

Last modified October 17, 2006. Version 2.
Checksum: 03EA1E026D0A9A2F

FASTA906101,506
        10         20         30         40         50         60 
MQHIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID 

        70         80         90        100        110        120 
IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ 

       130        140        150        160        170        180 
FVLQLRPELQ DALISIIDHY KWQKFVYIYD ADRGLSVLQK VLDTAAEKNW QVTAVNILTT 

       190        200        210        220        230        240 
TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIIKLE KNGIGYHYIL ANLGFMDIDL 

       250        260        270        280        290        300 
NKFKESGANV TGFQLVNYTD TIPAKIMQQW KNSDARDHTR VDWKRPKYTS ALTYDGVKVM 

       310        320        330        340        350        360 
AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR 

       370        380        390        400        410        420 
RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV 

       430        440        450        460        470        480 
MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE 

       490        500        510        520        530        540 
LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW 

       550        560        570        580        590        600 
MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ 

       610        620        630        640        650        660 
QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA 

       670        680        690        700        710        720 
YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES 

       730        740        750        760        770        780 
TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRNPV NLAVLKLNEQ GLLDKLKNKW 

       790        800        810        820        830        840 
WYDKGECGSG GGDSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK 

       850        860        870        880        890        900 
GFCLIPQQSI NEAIRTSTLP RNSGAGASSG GSGENGRVVS HDFPKSMQSI PCMSHSSGMP 


LGATGL 

« Hide

Isoform Flip [UniParc].

Checksum: 4C1973DBFE98C979
Show »

FASTA906101,482
Isoform 3 [UniParc].

Checksum: 53F69105FB85CFC9
Show »

FASTA82692,172
Isoform 4 [UniParc].

Checksum: 54246EAC4BFFB9F0
Show »

FASTA83793,900
Isoform 5 [UniParc].

Checksum: C49F9C13D74EC7E3
Show »

FASTA916102,888
Isoform 6 [UniParc].

Checksum: 8B6CF1CA44DC94B5
Show »

FASTA916102,864

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4322.1. [P42261-1]
CCDS47318.1. [P42261-2]
CCDS58986.1. [P42261-3]
CCDS58987.1. [P42261-5]
CCDS58988.1. [P42261-6]
CCDS58989.1. [P42261-4]
PIRA40222.
A41273.
S25852.
S38723.
RefSeqNP_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]
UniGeneHs.519693.
Hs.737709.

3D structure databases

ProteinModelPortalP42261.
SMRP42261. Positions 22-831.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109147. 18 interactions.
DIPDIP-41487N.
MINTMINT-271172.
STRING9606.ENSP00000285900.

Chemistry

BindingDBP42261.
ChEMBLCHEMBL2096670.
DrugBankDB01189. Desflurane.
DB00228. Enflurane.
DB01159. Halothane.
DB00753. Isoflurane.
DB00142. L-Glutamic Acid.
DB01028. Methoxyflurane.
DB01236. Sevoflurane.
GuidetoPHARMACOLOGY444.

PTM databases

PhosphoSiteP42261.

Polymorphism databases

DMDM116242505.

Proteomic databases

PaxDbP42261.
PRIDEP42261.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285900; 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]
GeneID2890.
KEGGhsa:2890.
UCSCuc003luy.4. human. [P42261-1]
uc003lva.4. human. [P42261-2]
uc011dcw.2. human.

Organism-specific databases

CTD2890.
GeneCardsGC05P152850.
H-InvDBHIX0032120.
HGNCHGNC:4571. GRIA1.
HPACAB001965.
HPA035202.
MIM138248. gene.
neXtProtNX_P42261.
PharmGKBPA28966.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG316680.
HOGENOMHOG000234372.
HOVERGENHBG051839.
KOK05197.
OMAFAFFCTS.
OrthoDBEOG7C2R0J.
PhylomeDBP42261.
TreeFamTF315232.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.
SignaLinkP42261.

Gene expression databases

ArrayExpressP42261.
BgeeP42261.
CleanExHS_GRIA1.
GenevestigatorP42261.

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.
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GeneWikiGRIA1.
GenomeRNAi2890.
NextBio11425.
PROP42261.
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Entry information

Entry nameGRIA1_HUMAN
AccessionPrimary (citable) accession number: P42261
Secondary accession number(s): B7Z2S0 expand/collapse secondary AC list , B7Z2W8, B7Z3F6, B7Z9G9, D3DQI4, E7ESV8, Q2NKM6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 154 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 5

Human chromosome 5: entries, gene names and cross-references to MIM