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P42262

- GRIA2_HUMAN

UniProt

P42262 - GRIA2_HUMAN

Protein

Glutamate receptor 2

Gene

GRIA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (10 Oct 2002)
      Previous versions | rss
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    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei471 – 4711Glutamate2 Publications
    Binding sitei506 – 5061Glutamate2 Publications
    Binding sitei726 – 7261Glutamate2 Publications

    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: RefGenome
    3. ionotropic glutamate receptor activity Source: UniProtKB
    4. protein binding Source: IntAct

    GO - Biological processi

    1. ionotropic glutamate receptor signaling pathway Source: UniProtKB
    2. ion transmembrane transport Source: GOC
    3. signal transduction Source: ProtInc
    4. synaptic transmission Source: Reactome
    5. synaptic transmission, glutamatergic Source: RefGenome

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_18338. Activation of AMPA receptors.
    REACT_18422. Trafficking of GluR2-containing AMPA receptors.
    REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
    SignaLinkiP42262.

    Protein family/group databases

    TCDBi1.A.10.1.13. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:4572. GRIA2.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity. Cell junctionsynapsepostsynaptic cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
    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: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. dendrite Source: RefGenome
    4. endocytic vesicle membrane Source: Reactome
    5. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    6. integral component of plasma membrane Source: UniProtKB
    7. plasma membrane Source: Reactome
    8. postsynaptic membrane Source: RefGenome
    9. synaptic vesicle Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28967.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 883859Glutamate receptor 2PRO_0000011532Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi78 ↔ 330
    Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi370 – 3701N-linked (GlcNAc...)1 Publication
    Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
    Lipidationi610 – 6101S-palmitoyl cysteineBy similarity
    Modified residuei683 – 6831Phosphoserine; by PKCBy similarity
    Modified residuei717 – 7171Phosphoserine; by PKGBy similarity
    Disulfide bondi739 ↔ 794
    Lipidationi836 – 8361S-palmitoyl cysteineBy similarity
    Modified residuei876 – 8761PhosphotyrosineBy similarity
    Modified residuei880 – 8801PhosphoserineBy similarity

    Post-translational modificationi

    Palmitoylated. Depalmitoylated upon glutamate stimulation. Cys-610 palmitoylation 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 By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    PaxDbiP42262.
    PRIDEiP42262.

    PTM databases

    PhosphoSiteiP42262.

    Expressioni

    Gene expression databases

    ArrayExpressiP42262.
    BgeeiP42262.
    CleanExiHS_GRIA2.
    GenevestigatoriP42262.

    Organism-specific databases

    HPAiCAB006830.
    CAB007812.
    CAB012981.
    HPA008441.

    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 By similarity. Interacts with PICK1 (via PDZ domain). Interacts with PRKCABP and GRIP2 By similarity. Interacts with GRIA1 and SYNDIG1 By similarity. Interacts with LRFN1. Interacts with SNX27 (via PDZ domain); the interaction is required for recycling to the plasma membrane when endocytosed and prevent degradation in lysosomes By similarity. Found in a complex with GRIA1, GRIA3, GRIA4, CNIH2, CNIH3, CACNG2, CACNG3, CACNG4, CACNG5, CACNG7 and CACNG8. Interacts with CACNG5 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NSFP464592EBI-3909876,EBI-712251

    Protein-protein interaction databases

    BioGridi109148. 17 interactions.
    DIPiDIP-42852N.
    IntActiP42262. 2 interactions.
    MINTiMINT-2791741.
    STRINGi9606.ENSP00000264426.

    Structurei

    Secondary structure

    1
    883
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi27 – 348
    Helixi38 – 5114
    Beta strandi58 – 658
    Helixi70 – 8314
    Beta strandi88 – 903
    Turni94 – 963
    Helixi97 – 10711
    Beta strandi111 – 1133
    Beta strandi125 – 1273
    Helixi133 – 14210
    Beta strandi147 – 1526
    Helixi159 – 17113
    Beta strandi174 – 1796
    Helixi188 – 1914
    Helixi193 – 2019
    Beta strandi206 – 2116
    Helixi213 – 22513
    Helixi230 – 2323
    Beta strandi234 – 2374
    Beta strandi239 – 2413
    Helixi247 – 2493
    Beta strandi256 – 2627
    Helixi268 – 27710
    Turni282 – 2843
    Beta strandi289 – 2913
    Helixi295 – 31622
    Helixi341 – 3499
    Beta strandi353 – 3553
    Beta strandi358 – 3603
    Beta strandi366 – 3683
    Beta strandi373 – 3797
    Beta strandi382 – 3909
    Turni391 – 3933
    Beta strandi394 – 3974
    Beta strandi416 – 4205
    Turni424 – 4263
    Beta strandi427 – 4293
    Helixi433 – 4353
    Helixi438 – 4414
    Beta strandi442 – 4443
    Helixi445 – 45713
    Beta strandi461 – 4655
    Turni476 – 4783
    Helixi483 – 4897
    Beta strandi494 – 4963
    Helixi504 – 5074
    Beta strandi510 – 5123
    Beta strandi516 – 5194
    Beta strandi521 – 5266
    Helixi657 – 6615
    Beta strandi664 – 6718
    Helixi675 – 6828
    Helixi686 – 69712
    Beta strandi704 – 7063
    Helixi707 – 71610
    Turni717 – 7193
    Beta strandi720 – 7267
    Helixi727 – 7348
    Beta strandi741 – 7455
    Beta strandi751 – 7533
    Beta strandi756 – 7583
    Helixi764 – 77613
    Helixi779 – 78810
    Turni789 – 7913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WJWX-ray1.80A25-412[»]
    2WJXX-ray4.10A/B/C25-412[»]
    2XHDX-ray1.80A/B413-527[»]
    A/B653-796[»]
    3R7XX-ray2.10A/B413-527[»]
    A/B653-796[»]
    3RN8X-ray1.70A/B/C413-527[»]
    A/B/C653-812[»]
    3RNNX-ray1.75A/B/C413-527[»]
    A/B/C653-812[»]
    3UA8X-ray1.90A413-527[»]
    A653-796[»]
    ProteinModelPortaliP42262.
    SMRiP42262. Positions 25-838.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42262.

    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=M4Add
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni499 – 5013Glutamate binding
    Regioni675 – 6762Glutamate binding

    Domaini

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

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG316680.
    HOGENOMiHOG000234372.
    HOVERGENiHBG051839.
    KOiK05198.
    OMAiHAVPYVS.
    OrthoDBiEOG7C2R0J.
    PhylomeDBiP42262.
    TreeFamiTF315232.

    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 Flop (identifier: P42262-1) [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 MYRSLFQDLE 200
    LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI 250
    QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT TTIKYTSALT 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 SSLRNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD 800
    SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK 850
    NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI 883
    Length:883
    Mass (Da):98,821
    Last modified:October 10, 2002 - v3
    Checksum:i6DAB96C76D1D8448
    GO
    Isoform Flip (identifier: P42262-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         765-800: NAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD → TPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSG

    Show »
    Length:883
    Mass (Da):98,878
    Checksum:i882141AC054254F8
    GO
    Isoform 3 (identifier: P42262-3) [UniParc]FASTAAdd to Basket

    Also known as: Long

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

    Show »
    Length:901
    Mass (Da):100,594
    Checksum:i6E668073D621EFBB
    GO
    Isoform 4 (identifier: P42262-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-47: Missing.
         765-800: NAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGD → TPVNLAVLKLSEQGVLDKLKNKWWYDKGECGAKDSG

    Note: No experimental confirmation available.

    Show »
    Length:836
    Mass (Da):93,775
    Checksum:i1B3F13BC745D4A45
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti140 – 1401I → V in AAH10574. (PubMed:15489334)Curated
    Sequence conflicti241 – 2411G → E in AAA58631. (PubMed:8003671)Curated
    Sequence conflicti415 – 4151T → I in AAH28736. (PubMed:15489334)Curated
    Sequence conflicti764 – 7641R → G in AAA58631. (PubMed:8003671)Curated

    RNA editingi

    Partially edited. 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. 2 Publications
    Corresponds to variant rs17850674 [ dbSNP | Ensembl ].
    VAR_000303
    Natural varianti608 – 6081Q → R.1 Publication
    Corresponds to variant rs17850675 [ dbSNP | Ensembl ].
    VAR_037055

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4747Missing in isoform 4. 1 PublicationVSP_055920Add
    BLAST
    Alternative sequencei765 – 80036NAVNL…SGGGD → TPVNLAVLKLSEQGVLDKLK NKWWYDKGECGAKDSG in isoform Flip and isoform 4. 2 PublicationsVSP_053350Add
    BLAST
    Alternative sequencei848 – 88336VAKNA…ESVKI → MTLNDAMRNKARLSITGSTG ENGRVMTPEFPKAVHAVPYV SPGMGMNVSVTDLS in isoform 3. CuratedVSP_029309Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20814 mRNA. Translation: AAA58631.1.
    AC079233 Genomic DNA. No translation available.
    AC112240 Genomic DNA. No translation available.
    BC010574 mRNA. Translation: AAH10574.1.
    BC028736 mRNA. Translation: AAH28736.2.
    CCDSiCCDS3797.1. [P42262-2]
    CCDS43274.1. [P42262-1]
    PIRiI58181.
    RefSeqiNP_000817.2. NM_000826.3.
    NP_001077088.1. NM_001083619.1.
    NP_001077089.1. NM_001083620.1.
    UniGeneiHs.32763.

    Genome annotation databases

    EnsembliENST00000264426; ENSP00000264426; ENSG00000120251. [P42262-1]
    ENST00000296526; ENSP00000296526; ENSG00000120251. [P42262-2]
    ENST00000393815; ENSP00000377403; ENSG00000120251.
    ENST00000449365; ENSP00000389837; ENSG00000120251.
    ENST00000507898; ENSP00000426845; ENSG00000120251.
    GeneIDi2891.
    KEGGihsa:2891.
    UCSCiuc003ipm.4. human. [P42262-1]
    uc011cit.2. human.

    Polymorphism databases

    DMDMi23831146.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L20814 mRNA. Translation: AAA58631.1 .
    AC079233 Genomic DNA. No translation available.
    AC112240 Genomic DNA. No translation available.
    BC010574 mRNA. Translation: AAH10574.1 .
    BC028736 mRNA. Translation: AAH28736.2 .
    CCDSi CCDS3797.1. [P42262-2 ]
    CCDS43274.1. [P42262-1 ]
    PIRi I58181.
    RefSeqi NP_000817.2. NM_000826.3.
    NP_001077088.1. NM_001083619.1.
    NP_001077089.1. NM_001083620.1.
    UniGenei Hs.32763.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WJW X-ray 1.80 A 25-412 [» ]
    2WJX X-ray 4.10 A/B/C 25-412 [» ]
    2XHD X-ray 1.80 A/B 413-527 [» ]
    A/B 653-796 [» ]
    3R7X X-ray 2.10 A/B 413-527 [» ]
    A/B 653-796 [» ]
    3RN8 X-ray 1.70 A/B/C 413-527 [» ]
    A/B/C 653-812 [» ]
    3RNN X-ray 1.75 A/B/C 413-527 [» ]
    A/B/C 653-812 [» ]
    3UA8 X-ray 1.90 A 413-527 [» ]
    A 653-796 [» ]
    ProteinModelPortali P42262.
    SMRi P42262. Positions 25-838.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109148. 17 interactions.
    DIPi DIP-42852N.
    IntActi P42262. 2 interactions.
    MINTi MINT-2791741.
    STRINGi 9606.ENSP00000264426.

    Chemistry

    BindingDBi P42262.
    ChEMBLi CHEMBL2096670.
    DrugBanki DB00142. L-Glutamic Acid.
    GuidetoPHARMACOLOGYi 445.

    Protein family/group databases

    TCDBi 1.A.10.1.13. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    PTM databases

    PhosphoSitei P42262.

    Polymorphism databases

    DMDMi 23831146.

    Proteomic databases

    PaxDbi P42262.
    PRIDEi P42262.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264426 ; ENSP00000264426 ; ENSG00000120251 . [P42262-1 ]
    ENST00000296526 ; ENSP00000296526 ; ENSG00000120251 . [P42262-2 ]
    ENST00000393815 ; ENSP00000377403 ; ENSG00000120251 .
    ENST00000449365 ; ENSP00000389837 ; ENSG00000120251 .
    ENST00000507898 ; ENSP00000426845 ; ENSG00000120251 .
    GeneIDi 2891.
    KEGGi hsa:2891.
    UCSCi uc003ipm.4. human. [P42262-1 ]
    uc011cit.2. human.

    Organism-specific databases

    CTDi 2891.
    GeneCardsi GC04P158141.
    HGNCi HGNC:4572. GRIA2.
    HPAi CAB006830.
    CAB007812.
    CAB012981.
    HPA008441.
    MIMi 138247. gene.
    neXtProti NX_P42262.
    PharmGKBi PA28967.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG316680.
    HOGENOMi HOG000234372.
    HOVERGENi HBG051839.
    KOi K05198.
    OMAi HAVPYVS.
    OrthoDBi EOG7C2R0J.
    PhylomeDBi P42262.
    TreeFami TF315232.

    Enzyme and pathway databases

    Reactomei REACT_18338. Activation of AMPA receptors.
    REACT_18422. Trafficking of GluR2-containing AMPA receptors.
    REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
    SignaLinki P42262.

    Miscellaneous databases

    EvolutionaryTracei P42262.
    GeneWikii GRIA2.
    GenomeRNAii 2891.
    NextBioi 11429.
    PROi P42262.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42262.
    Bgeei P42262.
    CleanExi HS_GRIA2.
    Genevestigatori P42262.

    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. "Primary structure and functional expression of the AMPA/kainate receptor subunit 2 from human brain."
      Sun W., Ferrer-Montiel A.V., Montal M.
      NeuroReport 5:441-444(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FLIP), VARIANT ARG-607.
      Tissue: Brain.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORMS FLOP AND 4), VARIANTS ARG-607 AND ARG-608.
      Tissue: Brain.
    4. "RNA editing of the glutamate receptor subunits GluR2 and GluR6 in human brain tissue."
      Paschen W., Hedreen J.C., Ross C.A.
      J. Neurochem. 63:1596-1602(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA EDITING OF POSITION 607.
    5. "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 (ISOFORM 3).
    6. "The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands."
      Dev K.K., Nakanishi S., Henley J.M.
      J. Biol. Chem. 279:41393-41397(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PICK1.
    7. "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.
    8. "Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors."
      Clayton A., Siebold C., Gilbert R.J., Sutton G.C., Harlos K., McIlhinney R.A., Jones E.Y., Aricescu A.R.
      J. Mol. Biol. 392:1125-1132(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 25-412, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION AT ASN-370.
    9. "Discovery of N-[(2S)-5-(6-fluoro-3-pyridinyl)-2,3-dihydro-1H-inden-2-yl]-2-propanesulfonamide, a novel clinical AMPA receptor positive modulator."
      Ward S.E., Harries M., Aldegheri L., Andreotti D., Ballantine S., Bax B.D., Harris A.J., Harker A.J., Lund J., Melarange R., Mingardi A., Mookherjee C., Mosley J., Neve M., Oliosi B., Profeta R., Smith K.J., Smith P.W.
      , Spada S., Thewlis K.M., Yusaf S.P.
      J. Med. Chem. 53:5801-5812(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 413-795 IN COMPLEX WITH GLUTAMATE AND SYNTHETIC INHIBITOR, FUNCTION.
    10. "Quinazolinedione sulfonamides: a novel class of competitive AMPA receptor antagonists with oral activity."
      Koller M., Lingenhoehl K., Schmutz M., Vranesic I.T., Kallen J., Auberson Y.P., Carcache D.A., Mattes H., Ofner S., Orain D., Urwyler S.
      Bioorg. Med. Chem. Lett. 21:3358-3361(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 413-796 IN COMPLEX WITH GLUTAMATE AND SYNTHETIC INHIBITOR, DISULFIDE BOND.

    Entry informationi

    Entry nameiGRIA2_HUMAN
    AccessioniPrimary (citable) accession number: P42262
    Secondary accession number(s): A8MT92, I6L997, Q96FP6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 10, 2002
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3