Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P23819 (GRIA2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate receptor 2

Short name=GluR-2
Alternative name(s):
AMPA-selective glutamate receptor 2
GluR-B
GluR-K2
Glutamate receptor ionotropic, AMPA 2
Short name=GluA2
Gene names
Name:Gria2
Synonyms:Glur2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length883 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 By similarity.

Subunit structure

Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. May interact with MPP4. Forms a ternary complex with GRIP1 and CSPG4. Interacts with ATAD1 in an ATP-dependent manner. ATAD1-catalyzed ATP hydrolysis disrupts binding to ATAD1 and to GRIP1 and leads to AMPAR complex disassembly. Interacts with GRIP2. Isoform 1, but not isoform 3, interacts with PICK1/PRKCABP. Interacts with GRIA1 and SYNDIG1. Interacts with LRFN1 By similarity. Found in a complex with GRIA1, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 By similarity. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes. Ref.5 Ref.7 Ref.8 Ref.11 Ref.12 Ref.13 Ref.14

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. Note: Interaction with CACNG2, CNIH2 and CNIH3 promotes cell surface expression By similarity. Ref.10 Ref.11

Tissue specificity

Detected in brain cortex, hippocampus and cerebellum (at protein level). Detected in hippocampus. Ref.10 Ref.11

Developmental stage

Detected at low levels in newborns. Levels increase strongly and are highest in hippocampus from 7 day olds. Detected at low levels in hippocampus and olfactory bulb of 3 month olds (at protein level). Ref.10

Domain

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

Post-translational modification

Palmitoylated. Depalmitoylated upon glutamate stimulation. ZDHHC3/GODZ specifically palmitoylates Cys-610, which leads to Golgi retention and decreased cell surface expression. In contrast, Cys-836 palmitoylation does not affect cell surface expression but regulates stimulation-dependent endocytosis. Ref.9

N-glycosylated. Ref.10

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. GRIA2 subfamily. [View classification]

RNA editing

Edited at position 607.
Fully edited in the brain. Heteromerically expressed edited GLUR2 (R) receptor complexes are impermeable to calcium, whereas the unedited (Q) forms are highly permeable to divalent ions. Ref.4

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Endoplasmic reticulum
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
RNA editing
   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 direct assay Ref.10. Source: GOC

ionotropic glutamate receptor signaling pathway

Inferred from direct assay Ref.10. Source: GOC

synaptic transmission

Inferred from direct assay Ref.10. Source: MGI

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 direct assay PubMed 15883194PubMed 22632720. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite

Inferred from Biological aspect of Ancestor. Source: RefGenome

endoplasmic reticulum

Inferred from direct assay PubMed 16814779. Source: MGI

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from direct assay Ref.10PubMed 17093100PubMed 18190519. Source: MGI

neuron projection

Inferred from direct assay PubMed 21558424. Source: BHF-UCL

postsynaptic membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

synapse

Inferred from direct assay PubMed 22632720. Source: MGI

synaptic vesicle

Inferred from direct assay PubMed 20418887. Source: MGI

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

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular-glutamate-gated ion channel activity

Inferred from direct assay Ref.10. Source: MGI

ionotropic glutamate receptor activity

Inferred from direct assay Ref.10. Source: MGI

kainate selective glutamate receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P23819-1)

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 2 (identifier: P23819-2)

The sequence of this isoform differs from the canonical sequence as follows:
     761-761: S → T
     765-767: NAV → WVE
     768-883: Missing.
Isoform 3 (identifier: P23819-3)

The sequence of this isoform differs from the canonical sequence as follows:
     802-802: K → KTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGSK
     848-883: VAKNAQNINP...NVYGIESVKI → MTLSAATRNK...GMNVSVTDLS
Isoform 4 (identifier: P23819-4)

The sequence of this isoform differs from the canonical sequence as follows:
     802-802: K → KTPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSGSK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 883859Glutamate receptor 2
PRO_0000011533

Regions

Topological domain25 – 543519Extracellular By similarity
Transmembrane544 – 56421Helical; By similarity
Topological domain565 – 59127Cytoplasmic By similarity
Intramembrane592 – 60716Helical; Pore-forming; By similarity
Intramembrane608 – 6103 By similarity
Topological domain611 – 6166Cytoplasmic By similarity
Transmembrane617 – 63721Helical; By similarity
Topological domain638 – 812175Extracellular By similarity
Transmembrane813 – 83321Helical; Name=M4; By similarity
Topological domain834 – 88350Cytoplasmic By similarity

Sites

Binding site4711Glutamate By similarity
Binding site5061Glutamate By similarity
Binding site7261Glutamate By similarity

Amino acid modifications

Modified residue6831Phosphoserine; by PKC By similarity
Modified residue7171Phosphoserine; by PKG By similarity
Modified residue8761Phosphotyrosine Ref.11
Modified residue8801Phosphoserine Ref.6
Lipidation6101S-palmitoyl cysteine Ref.9
Lipidation8361S-palmitoyl cysteine Ref.9
Glycosylation2561N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4131N-linked (GlcNAc...) Potential
Disulfide bond78 ↔ 330 By similarity
Disulfide bond739 ↔ 794 By similarity

Natural variations

Alternative sequence7611S → T in isoform 2.
VSP_000106
Alternative sequence765 – 7673NAV → WVE in isoform 2.
VSP_000107
Alternative sequence768 – 883116Missing in isoform 2.
VSP_000108
Alternative sequence8021K → KTPVNLAVLKLSEQGVLDKL KNKWWYDKGECGAKDSGSK in isoform 3 and isoform 4.
VSP_000109
Alternative sequence848 – 88336VAKNA…ESVKI → MTLSAATRNKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3.
VSP_000110
Natural variant6071Q → R in RNA edited version.

Experimental info

Mutagenesis8691Y → F: No effect on tyrosine phosphorylation. Reduced tyrosine phosphorylation; when associated with F-873 and F-876. Ref.11
Mutagenesis8731Y → F: No effect on tyrosine phosphorylation. Reduced tyrosine phosphorylation; when associated with F-869 and F-876. Ref.11
Mutagenesis8761Y → F: Loss of tyrosine phosphorylation at the C-terminus. Reduced tyrosine phosphorylation; when associated with F-869 and F-873. Interferes with accumulation at synapses. Interferes with AMPA-mediated receptor internalization. Ref.11
Sequence conflict2641D → V in CAA40735. Ref.1
Sequence conflict2701V → A in CAA40735. Ref.1
Sequence conflict2821E → G in CAA40735. Ref.1
Sequence conflict3741N → H in BAB29316. Ref.3
Sequence conflict4821N → K in BAC31557. Ref.3
Sequence conflict5521F → L in BAB29316. Ref.3
Sequence conflict7641G → R in AAC37653. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 2, 2002. Version 3.
Checksum: C44B317027C1CCC1

FASTA88398,662
        10         20         30         40         50         60 
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP 

        70         80         90        100        110        120 
HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG 

       130        140        150        160        170        180 
THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV 

       190        200        210        220        230        240 
GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL 

       250        260        270        280        290        300 
GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT 

       310        320        330        340        350        360 
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI 

       370        380        390        400        410        420 
KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT 

       430        440        450        460        470        480 
ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI 

       490        500        510        520        530        540 
WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD 

       550        560        570        580        590        600 
PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 

       610        620        630        640        650        660 
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL 

       670        680        690        700        710        720 
SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK 

       730        740        750        760        770        780 
YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL 

       790        800        810        820        830        840 
DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR 

       850        860        870        880 
AEAKRMKVAK NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI 

« Hide

Isoform 2 [UniParc].

Checksum: 822F17FD67E4820E
Show »

FASTA76786,181
Isoform 3 [UniParc].

Checksum: 2600BEDAF2C0583D
Show »

FASTA939104,523
Isoform 4 [UniParc].

Checksum: E38D8C26ED029219
Show »

FASTA921102,851

References

« Hide 'large scale' references
[1]"Functional expression from cloned cDNAs of glutamate receptor species responsive to kainate and quisqualate."
Sakimura K., Bujo H., Kushiya E., Araki K., Yamazaki M., Yamazaki M., Meguro H., Warashina A., Numa S., Mishina M.
FEBS Lett. 272:73-80(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The organization of the gene for the functionally dominant alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluR-B."
Koehler M., Kornau H.-C., Seeburg P.H.
J. Biol. Chem. 269:17367-17370(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 3 AND 4).
Strain: BALB/c.
Tissue: Liver.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Brain, Cerebellum, Medulla oblongata and Retina.
[4]"RNA editing in brain controls a determinant of ion flow in glutamate-gated channels."
Sommer B., Koehler M., Sprengel R., Seeburg P.H.
Cell 67:11-19(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA EDITING OF POSITION 607.
[5]"rDLG6: a novel homolog of Drosophila DLG expressed in rat brain."
Inagaki H., Maeda S., Lin K.H., Shimizu N., Saito T.
Biochem. Biophys. Res. Commun. 265:462-468(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MPP4.
[6]"Phosphorylation of serine-880 in GluR2 by protein kinase C prevents its C terminus from binding with glutamate receptor-interacting protein."
Matsuda S., Mikawa S., Hirai H.
J. Neurochem. 73:1765-1768(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-880.
[7]"The protein kinase C alpha binding protein PICK1 interacts with short but not long form alternative splice variants of AMPA receptor subunits."
Dev K.K., Nishimune A., Henley J.M., Nakanishi S.
Neuropharmacology 38:635-644(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKCABP (ISOFORM 1).
[8]"The proteoglycan NG2 is complexed with alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors by the PDZ glutamate receptor interaction protein (GRIP) in glial progenitor cells. Implications for glial-neuronal signaling."
Stegmueller J., Werner H., Nave K.-A., Trotter J.
J. Biol. Chem. 278:3590-3598(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIP1 AND CSPG4.
[9]"Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites."
Hayashi T., Rumbaugh G., Huganir R.L.
Neuron 47:709-723(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-610 AND CYS-836.
[10]"Glutamatergic plasticity by synaptic delivery of GluR-B(long)-containing AMPA receptors."
Kolleker A., Zhu J.J., Schupp B.J., Qin Y., Mack V., Borchardt T., Koehr G., Malinow R., Seeburg P.H., Osten P.
Neuron 40:1199-1212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF ISOFORM 3, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[11]"Tyrosine phosphorylation and regulation of the AMPA receptor by SRC family tyrosine kinases."
Hayashi T., Huganir R.L.
J. Neurosci. 24:6152-6160(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-876, MUTAGENESIS OF TYR-869; TYR-873 AND TYR-876, SUBCELLULAR LOCATION, INTERACTION WITH GRIP1; GRIP2 AND PICK1, TISSUE SPECIFICITY.
[12]"SynDIG1: an activity-regulated, AMPA- receptor-interacting transmembrane protein that regulates excitatory synapse development."
Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B., Ishimaru T., Trimmer J.S., Mohapatra D.P., Diaz E.
Neuron 65:80-93(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIA1 AND SYNDIG1.
[13]"The AAA+ ATPase Thorase regulates AMPA receptor-dependent synaptic plasticity and behavior."
Zhang J., Wang Y., Chi Z., Keuss M.J., Pai Y.M., Kang H.C., Shin J.H., Bugayenko A., Wang H., Xiong Y., Pletnikov M.V., Mattson M.P., Dawson T.M., Dawson V.L.
Cell 145:284-299(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATAD1 AND GRIP1.
[14]"Loss of sorting nexin 27 contributes to excitatory synaptic dysfunction by modulating glutamate receptor recycling in Down's syndrome."
Wang X., Zhao Y., Zhang X., Badie H., Zhou Y., Mu Y., Loo L.S., Cai L., Thompson R.C., Yang B., Chen Y., Johnson P.F., Wu C., Bu G., Mobley W.C., Zhang D., Gage F.H., Ranscht B. expand/collapse author list , Zhang Y.W., Lipton S.A., Hong W., Xu H.
Nat. Med. 19:473-480(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX27.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57498 mRNA. Translation: CAA40735.1.
L32204 expand/collapse EMBL AC list , L32189, L32190, L32192, L32194, L32196, L32198, L32200, L32202, L32203, L32201, L32199, L32197, L32195, L32193, L32191 Genomic DNA. Translation: AAC37653.1.
L32372 expand/collapse EMBL AC list , L32189, L32190, L32191, L32192, L32193, L32194, L32195, L32196, L32197, L32198, L32199, L32200, L32201, L32202, L32203, L32204 Genomic DNA. Translation: AAC37654.1.
AK014389 mRNA. Translation: BAB29316.1.
AK043490 mRNA. Translation: BAC31557.1.
AK044574 mRNA. Translation: BAC31986.1.
AK046861 mRNA. Translation: BAC32899.1.
CCDSCCDS17423.1. [P23819-1]
PIRI49695.
I49696.
RefSeqNP_001034284.1. NM_001039195.1.
NP_001077275.1. NM_001083806.1.
NP_038568.2. NM_013540.2.
UniGeneMm.220224.

3D structure databases

ProteinModelPortalP23819.
SMRP23819. Positions 25-838.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200059. 8 interactions.
IntActP23819. 29 interactions.
MINTMINT-1776844.
STRING10090.ENSMUSP00000103375.

Chemistry

BindingDBP23819.
ChEMBLCHEMBL2096617.
GuidetoPHARMACOLOGY445.

PTM databases

PhosphoSiteP23819.

Proteomic databases

MaxQBP23819.
PaxDbP23819.
PRIDEP23819.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID14800.
KEGGmmu:14800.
UCSCuc008pof.1. mouse. [P23819-1]

Organism-specific databases

CTD2891.
MGIMGI:95809. Gria2.

Phylogenomic databases

eggNOGNOG316680.
HOGENOMHOG000234372.
HOVERGENHBG051839.
KOK05198.
PhylomeDBP23819.

Gene expression databases

CleanExMM_GRIA2.
GenevestigatorP23819.

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

NextBio286957.
PROP23819.
SOURCESearch...

Entry information

Entry nameGRIA2_MOUSE
AccessionPrimary (citable) accession number: P23819
Secondary accession number(s): Q61604 expand/collapse secondary AC list , Q61605, Q8BG69, Q8BXU3, Q9D6D3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: August 2, 2002
Last modified: July 9, 2014
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot