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P23819

- GRIA2_MOUSE

UniProt

P23819 - GRIA2_MOUSE

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Protein

Glutamate receptor 2

Gene

Gria2

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei471 – 4711GlutamateBy similarity
Binding sitei506 – 5061GlutamateBy similarity
Binding sitei726 – 7261GlutamateBy 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: MGI
  3. ionotropic glutamate receptor activity Source: MGI
  4. kainate selective glutamate receptor activity Source: UniProtKB

GO - Biological processi

  1. ionotropic glutamate receptor signaling pathway Source: GOC
  2. ion transmembrane transport Source: GOC
  3. synaptic transmission Source: MGI
  4. synaptic transmission, glutamatergic Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Gria2
Synonyms:Glur2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:95809. Gria2.

Subcellular locationi

Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane By similarity; 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 543519ExtracellularBy similarityAdd
BLAST
Transmembranei544 – 56421HelicalBy similarityAdd
BLAST
Topological domaini565 – 59127CytoplasmicBy similarityAdd
BLAST
Intramembranei592 – 60716Helical; Pore-formingBy similarityAdd
BLAST
Intramembranei608 – 6103By similarity
Topological domaini611 – 6166CytoplasmicBy similarity
Transmembranei617 – 63721HelicalBy similarityAdd
BLAST
Topological domaini638 – 812175ExtracellularBy similarityAdd
BLAST
Transmembranei813 – 83321Helical; Name=M4By similarityAdd
BLAST
Topological domaini834 – 88350CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: MGI
  2. cell junction Source: UniProtKB-KW
  3. dendrite Source: RefGenome
  4. endoplasmic reticulum Source: MGI
  5. integral component of plasma membrane Source: UniProtKB
  6. membrane Source: MGI
  7. neuron projection Source: BHF-UCL
  8. postsynaptic membrane Source: MGI
  9. synapse Source: MGI
  10. synaptic vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi869 – 8691Y → F: No effect on tyrosine phosphorylation. Reduced tyrosine phosphorylation; when associated with F-873 and F-876. 1 Publication
Mutagenesisi873 – 8731Y → F: No effect on tyrosine phosphorylation. Reduced tyrosine phosphorylation; when associated with F-869 and F-876. 1 Publication
Mutagenesisi876 – 8761Y → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 883859Glutamate receptor 2PRO_0000011533Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi78 ↔ 330By similarity
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
Lipidationi610 – 6101S-palmitoyl cysteine1 Publication
Modified residuei683 – 6831Phosphoserine; by PKCBy similarity
Modified residuei717 – 7171Phosphoserine; by PKGBy similarity
Disulfide bondi739 ↔ 794By similarity
Lipidationi836 – 8361S-palmitoyl cysteine1 Publication
Modified residuei876 – 8761Phosphotyrosine1 Publication
Modified residuei880 – 8801Phosphoserine1 Publication

Post-translational modificationi

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.1 Publication
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP23819.
PaxDbiP23819.
PRIDEiP23819.

PTM databases

PhosphoSiteiP23819.

Expressioni

Tissue specificityi

Detected in brain cortex, hippocampus and cerebellum (at protein level). Detected in hippocampus.2 Publications

Developmental stagei

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).1 Publication

Gene expression databases

CleanExiMM_GRIA2.
GenevestigatoriP23819.

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Cspg4Q8VHY02EBI-77538,EBI-8327479
Gria1P238185EBI-77538,EBI-445486
Grip1Q925T65EBI-77538,EBI-537752

Protein-protein interaction databases

BioGridi200059. 8 interactions.
IntActiP23819. 29 interactions.
MINTiMINT-1776844.
STRINGi10090.ENSMUSP00000103375.

Structurei

3D structure databases

ProteinModelPortaliP23819.
SMRiP23819. Positions 25-838.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.
HOGENOMiHOG000234372.
HOVERGENiHBG051839.
InParanoidiP23819.
KOiK05198.
PhylomeDBiP23819.

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 (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P23819-1) [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
MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ
60 70 80 90 100
FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI
110 120 130 140 150
TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY
160 170 180 190 200
LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE TYRSLFQDLE
210 220 230 240 250
LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI
260 270 280 290 300
QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT
310 320 330 340 350
YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ
360 370 380 390 400
VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT
410 420 430 440 450
ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA
460 470 480 490 500
AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL
510 520 530 540 550
TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI
560 570 580 590 600
VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF
610 620 630 640 650
SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM
660 670 680 690 700
VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP
710 720 730 740 750
SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS
760 770 780 790 800
KGYGIATPKG SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD
810 820 830 840 850
SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK
860 870 880
NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI
Length:883
Mass (Da):98,662
Last modified:August 2, 2002 - v3
Checksum:iC44B317027C1CCC1
GO
Isoform 2 (identifier: P23819-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:767
Mass (Da):86,181
Checksum:i822F17FD67E4820E
GO
Isoform 3 (identifier: P23819-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:939
Mass (Da):104,523
Checksum:i2600BEDAF2C0583D
GO
Isoform 4 (identifier: P23819-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:921
Mass (Da):102,851
Checksum:iE38D8C26ED029219
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti264 – 2641D → V in CAA40735. (PubMed:1699805)Curated
Sequence conflicti270 – 2701V → A in CAA40735. (PubMed:1699805)Curated
Sequence conflicti282 – 2821E → G in CAA40735. (PubMed:1699805)Curated
Sequence conflicti374 – 3741N → H in BAB29316. (PubMed:16141072)Curated
Sequence conflicti482 – 4821N → K in BAC31557. (PubMed:16141072)Curated
Sequence conflicti552 – 5521F → L in BAB29316. (PubMed:16141072)Curated
Sequence conflicti764 – 7641G → R in AAC37653. (PubMed:7545935)Curated

RNA editingi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti607 – 6071Q → R in RNA edited version.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei761 – 7611S → T in isoform 2. 1 PublicationVSP_000106
Alternative sequencei765 – 7673NAV → WVE in isoform 2. 1 PublicationVSP_000107
Alternative sequencei768 – 883116Missing in isoform 2. 1 PublicationVSP_000108Add
BLAST
Alternative sequencei802 – 8021K → KTPVNLAVLKLSEQGVLDKL KNKWWYDKGECGAKDSGSK in isoform 3 and isoform 4. CuratedVSP_000109
Alternative sequencei848 – 88336VAKNA…ESVKI → MTLSAATRNKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3. CuratedVSP_000110Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57498 mRNA. Translation: CAA40735.1.
L32204
, L32189, L32190, L32192, L32194, L32196, L32198, L32200, L32202, L32203, L32201, L32199, L32197, L32195, L32193, L32191 Genomic DNA. Translation: AAC37653.1.
L32372
, 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.
CCDSiCCDS17423.1. [P23819-1]
PIRiI49695.
I49696.
RefSeqiNP_001034284.1. NM_001039195.1.
NP_001077275.1. NM_001083806.1.
NP_038568.2. NM_013540.2.
UniGeneiMm.220224.

Genome annotation databases

GeneIDi14800.
KEGGimmu:14800.
UCSCiuc008pof.1. mouse. [P23819-1]

Keywords - Coding sequence diversityi

Alternative splicing, RNA editing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57498 mRNA. Translation: CAA40735.1 .
L32204
, L32189 , L32190 , L32192 , L32194 , L32196 , L32198 , L32200 , L32202 , L32203 , L32201 , L32199 , L32197 , L32195 , L32193 , L32191 Genomic DNA. Translation: AAC37653.1 .
L32372
, 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 .
CCDSi CCDS17423.1. [P23819-1 ]
PIRi I49695.
I49696.
RefSeqi NP_001034284.1. NM_001039195.1.
NP_001077275.1. NM_001083806.1.
NP_038568.2. NM_013540.2.
UniGenei Mm.220224.

3D structure databases

ProteinModelPortali P23819.
SMRi P23819. Positions 25-838.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200059. 8 interactions.
IntActi P23819. 29 interactions.
MINTi MINT-1776844.
STRINGi 10090.ENSMUSP00000103375.

Chemistry

ChEMBLi CHEMBL2096617.
GuidetoPHARMACOLOGYi 445.

PTM databases

PhosphoSitei P23819.

Proteomic databases

MaxQBi P23819.
PaxDbi P23819.
PRIDEi P23819.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 14800.
KEGGi mmu:14800.
UCSCi uc008pof.1. mouse. [P23819-1 ]

Organism-specific databases

CTDi 2891.
MGIi MGI:95809. Gria2.

Phylogenomic databases

eggNOGi NOG316680.
HOGENOMi HOG000234372.
HOVERGENi HBG051839.
InParanoidi P23819.
KOi K05198.
PhylomeDBi P23819.

Miscellaneous databases

NextBioi 286957.
PROi P23819.
SOURCEi Search...

Gene expression databases

CleanExi MM_GRIA2.
Genevestigatori P23819.

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. "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.
    , 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.
    , 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.

Entry informationi

Entry nameiGRIA2_MOUSE
AccessioniPrimary (citable) accession number: P23819
Secondary accession number(s): Q61604
, Q61605, Q8BG69, Q8BXU3, Q9D6D3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: August 2, 2002
Last modified: November 26, 2014
This is version 155 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds AMPA (quisqualate) > glutamate > kainate.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3