Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P23819

- GRIA2_MOUSE

UniProt

P23819 - GRIA2_MOUSE

Protein

Glutamate receptor 2

Gene

Gria2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (02 Aug 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    5. protein binding 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

    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

    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. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    6. integral component of plasma membrane Source: UniProtKB
    7. membrane Source: MGI
    8. neuron projection Source: BHF-UCL
    9. postsynaptic membrane Source: MGI
    10. synapse Source: MGI
    11. synaptic vesicle Source: MGI

    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...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 543519ExtracellularBy similarityAdd
    BLAST
    Topological domaini565 – 59127CytoplasmicBy similarityAdd
    BLAST
    Topological domaini611 – 6166CytoplasmicBy similarity
    Topological domaini638 – 812175ExtracellularBy similarityAdd
    BLAST
    Topological domaini834 – 88350CytoplasmicBy similarityAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei592 – 60716Helical; Pore-formingBy similarityAdd
    BLAST
    Intramembranei608 – 6103By similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei544 – 56421HelicalBy similarityAdd
    BLAST
    Transmembranei617 – 63721HelicalBy similarityAdd
    BLAST
    Transmembranei813 – 83321Helical; Name=M4By similarityAdd
    BLAST

    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.
    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

    MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ    50
    FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI 100
    TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY 150
    LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE TYRSLFQDLE 200
    LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI 250
    QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT 300
    YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ 350
    VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT 400
    ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA 450
    AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL 500
    TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI 550
    VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF 600
    SLGAFMQQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM 650
    VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP 700
    SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS 750
    KGYGIATPKG SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD 800
    SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK 850
    NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI 883
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    BindingDBi P23819.
    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.
    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

    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: October 1, 2014
    This is version 153 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