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P42260

- GRIK2_RAT

UniProt

P42260 - GRIK2_RAT

Protein

Glutamate receptor ionotropic, kainate 2

Gene

Grik2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Ionotropic glutamate receptor. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. May be involved in the transmission of light information from the retina to the hypothalamus. Modulates cell surface expression of NETO2 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei523 – 5231Glutamate
    Binding sitei738 – 7381Glutamate

    GO - Molecular functioni

    1. extracellular-glutamate-gated ion channel activity Source: RefGenome
    2. glutamate receptor activity Source: UniProtKB
    3. identical protein binding Source: RGD
    4. ionotropic glutamate receptor activity Source: RGD
    5. kainate selective glutamate receptor activity Source: RGD
    6. PDZ domain binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein homodimerization activity Source: RGD
    9. ubiquitin conjugating enzyme binding Source: RGD
    10. ubiquitin protein ligase binding Source: RGD

    GO - Biological processi

    1. ionotropic glutamate receptor signaling pathway Source: GOC
    2. ion transmembrane transport Source: GOC
    3. negative regulation of synaptic transmission, glutamatergic Source: UniProtKB
    4. neuron apoptotic process Source: UniProtKB
    5. positive regulation of neuron apoptotic process Source: RGD
    6. receptor clustering Source: UniProtKB
    7. regulation of JNK cascade Source: UniProtKB
    8. signal transduction Source: GOC
    9. synaptic transmission Source: RGD

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Protein family/group databases

    TCDBi1.A.10.1.11. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate receptor ionotropic, kainate 2
    Short name:
    GluK2
    Alternative name(s):
    Glutamate receptor 6
    Short name:
    GluR-6
    Short name:
    GluR6
    Gene namesi
    Name:Grik2
    Synonyms:Glur6
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2733. Grik2.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Cell junctionsynapsepostsynaptic cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. axon Source: RGD
    2. cell junction Source: UniProtKB-KW
    3. dendrite Source: UniProtKB
    4. dendrite cytoplasm Source: RGD
    5. integral component of plasma membrane Source: UniProtKB
    6. ionotropic glutamate receptor complex Source: UniProtKB
    7. kainate selective glutamate receptor complex Source: RefGenome
    8. perikaryon Source: RGD
    9. postsynaptic membrane Source: RefGenome
    10. presynaptic membrane Source: RefGenome
    11. synapse Source: RGD
    12. terminal bouton Source: RGD

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi883 – 8831V → A: Abolishes interaction with KLHL17. Abolishes actinfilin-mediated degradation. 1 Publication
    Mutagenesisi884 – 8841I → A: Abolishes interaction with KLHL17. Abolishes actinfilin-mediated degradation. 1 Publication
    Mutagenesisi886 – 8861K → R: Abolishes sumoylation. Loss of kainate-mediated endocytosis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 908877Glutamate receptor ionotropic, kainate 2PRO_0000011546Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi67 – 671N-linked (GlcNAc...)1 Publication
    Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi96 ↔ 3471 Publication
    Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi378 – 3781N-linked (GlcNAc...)1 Publication
    Glycosylationi412 – 4121N-linked (GlcNAc...)1 Publication
    Glycosylationi423 – 4231N-linked (GlcNAc...)1 Publication
    Glycosylationi430 – 4301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi751 – 7511N-linked (GlcNAc...)1 Publication
    Modified residuei846 – 8461Phosphoserine; by PKCBy similarity
    Modified residuei868 – 8681Phosphoserine; by PKCBy similarity
    Cross-linki886 – 886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)

    Post-translational modificationi

    Sumoylation mediates kainate receptor-mediated endocytosis and regulates synaptic transmission. Sumoylation is enhanced by PIAS3 and desumoylated by SENP1.1 Publication
    Ubiquitinated. Ubiquitination regulates the GRIK2 levels at the synapse by leading kainate receptor degradation through proteasome.1 Publication
    Phosphorylated by PKC at Ser-868 upon agonist activation, this directly enhance sumoylation.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP42260.
    PRIDEiP42260.

    PTM databases

    PhosphoSiteiP42260.

    Expressioni

    Tissue specificityi

    Highest expression is found in the olfactory lobe, piriform cortex, dentate gyrus, hippocampus, granular cell layer of the cerebellum, and in caudate-putamen.

    Gene expression databases

    GenevestigatoriP42260.

    Interactioni

    Subunit structurei

    Homotetramer or heterotetramer of pore-forming glutamate receptor subunits. Tetramers may be formed by the dimerization of dimers. Assembles into a kainate-gated homomeric channel that does not bind AMPA By similarity. GRIK2 associated to GRIK5 forms functional channels that can be gated by AMPA. Interacts with DLG4. Interacts with NETO2. Interacts (via C-terminus) with KLHL17 (via kelch repeats); the interaction targets GRIK2 for degradation via ubiquitin-proteasome pathway.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Map3k11Q66HA12EBI-7809795,EBI-4279420

    Protein-protein interaction databases

    BioGridi248480. 3 interactions.
    DIPiDIP-29256N.
    IntActiP42260. 3 interactions.
    MINTiMINT-8359884.
    STRINGi10116.ENSRNOP00000000415.

    Structurei

    Secondary structure

    1
    908
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 4714
    Helixi52 – 6615
    Beta strandi68 – 8417
    Helixi88 – 10114
    Helixi112 – 12413
    Beta strandi129 – 1313
    Beta strandi145 – 1517
    Helixi153 – 16614
    Beta strandi170 – 1789
    Helixi180 – 1845
    Helixi186 – 1894
    Helixi191 – 1933
    Beta strandi198 – 2036
    Helixi208 – 2114
    Helixi212 – 2209
    Beta strandi225 – 2306
    Helixi232 – 24413
    Beta strandi249 – 2513
    Beta strandi253 – 2564
    Helixi261 – 2633
    Turni267 – 2715
    Beta strandi275 – 2806
    Helixi287 – 29812
    Beta strandi309 – 3113
    Helixi318 – 33518
    Beta strandi347 – 3493
    Helixi356 – 36510
    Beta strandi367 – 3704
    Beta strandi373 – 3764
    Turni379 – 3813
    Beta strandi382 – 3843
    Beta strandi389 – 3957
    Beta strandi398 – 4069
    Turni407 – 4093
    Beta strandi410 – 4134
    Turni425 – 4284
    Beta strandi433 – 4375
    Turni441 – 4433
    Beta strandi444 – 4463
    Helixi455 – 4584
    Beta strandi459 – 4613
    Helixi462 – 47413
    Beta strandi478 – 4825
    Turni493 – 4953
    Helixi500 – 5067
    Beta strandi511 – 5133
    Helixi521 – 5244
    Beta strandi527 – 5293
    Beta strandi533 – 5364
    Beta strandi538 – 5447
    Beta strandi665 – 6673
    Helixi671 – 6755
    Beta strandi678 – 6858
    Helixi689 – 6968
    Helixi700 – 71112
    Helixi713 – 7164
    Beta strandi717 – 7204
    Helixi721 – 73010
    Beta strandi731 – 7388
    Helixi739 – 74810
    Beta strandi752 – 7576
    Beta strandi762 – 7643
    Beta strandi767 – 7693
    Helixi774 – 78714
    Helixi790 – 79910

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S50X-ray1.65A428-806[»]
    1S7YX-ray1.75A/B429-544[»]
    A/B667-806[»]
    1S9TX-ray1.80A/B429-544[»]
    A/B667-806[»]
    1SD3X-ray1.80A/B429-544[»]
    A/B667-806[»]
    1TT1X-ray1.93A/B429-806[»]
    1YAEX-ray3.11A/B/C/D/E/F419-557[»]
    A/B/C/D/E/F662-819[»]
    2I0BX-ray1.96A/B/C429-544[»]
    A/B/C667-806[»]
    2I0CX-ray2.25A/B429-544[»]
    A/B667-806[»]
    2XXRX-ray1.60A/B429-544[»]
    A/B667-806[»]
    2XXTX-ray1.90A/B667-806[»]
    2XXUX-ray1.50A/B667-806[»]
    2XXVX-ray1.70A/B667-806[»]
    2XXWX-ray2.30A/B667-806[»]
    2XXXX-ray2.10A/B/C/D667-806[»]
    2XXYX-ray3.00A/B/C/D667-806[»]
    3G3FX-ray1.38A/B429-544[»]
    A/B667-806[»]
    3G3GX-ray1.30A/B429-544[»]
    A/B667-806[»]
    3G3HX-ray1.50A/B429-544[»]
    A/B667-806[»]
    3G3IX-ray1.37A/B429-544[»]
    A/B667-806[»]
    3G3JX-ray1.32A/B429-544[»]
    A/B667-806[»]
    3G3KX-ray1.24A/B429-544[»]
    A/B667-806[»]
    3H6GX-ray2.70A/B32-420[»]
    3H6HX-ray2.90A/B32-420[»]
    3QLTX-ray2.99A/B32-420[»]
    3QLUX-ray2.91C/D32-420[»]
    3QLVX-ray3.94C/D/F/H/J32-420[»]
    4BDLX-ray1.75A/B429-544[»]
    A/B667-806[»]
    4BDMX-ray3.40A/B/C/D429-544[»]
    A/B/C/D667-806[»]
    4BDNX-ray2.50A/B/C/D429-544[»]
    A/B/C/D667-806[»]
    4BDOX-ray2.55A/B/C/D429-544[»]
    A/B/C/D667-806[»]
    4BDQX-ray1.90A/B429-544[»]
    A/B667-806[»]
    4BDRX-ray1.65A/B429-544[»]
    A/B667-806[»]
    4H8IX-ray2.00A/B429-544[»]
    A/B667-806[»]
    ProteinModelPortaliP42260.
    SMRiP42260. Positions 423-546, 668-804.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42260.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 561530ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini583 – 63856CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini660 – 819160ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini841 – 90868CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei562 – 58221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei639 – 65921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei820 – 84021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni516 – 5183Glutamate binding
    Regioni689 – 6902Glutamate binding

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG316680.
    HOGENOMiHOG000234371.
    HOVERGENiHBG051839.
    InParanoidiP42260.
    KOiK05202.
    PhylomeDBiP42260.

    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.

    Sequencei

    Sequence statusi: Complete.

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

    P42260-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIISPVLSN LVFSRSIKVL LCLLWIGYSQ GTTHVLRFGG IFEYVESGPM    50
    GAEELAFRFA VNTINRNRTL LPNTTLTYDT QKINLYDSFE ASKKACDQLS 100
    LGVAAIFGPS HSSSANAVQS ICNALGVPHI QTRWKHQVSD NKDSFYVSLY 150
    PDFSSLSRAI LDLVQFFKWK TVTVVYDDST GLIRLQELIK APSRYNLRLK 200
    IRQLPADTKD AKPLLKEMKR GKEFHVIFDC SHEMAAGILK QALAMGMMTE 250
    YYHYIFTTLD LFALDVEPYR YSGVNMTGFR ILNTENTQVS SIIEKWSMER 300
    LQAPPKPDSG LLDGFMTTDA ALMYDAVHVV SVAVQQFPQM TVSSLQCNRH 350
    KPWRFGTRFM SLIKEAHWEG LTGRITFNKT NGLRTDFDLD VISLKEEGLE 400
    KIGTWDPASG LNMTESQKGK PANITDSLSN RSLIVTTILE EPYVLFKKSD 450
    KPLYGNDRFE GYCIDLLREL STILGFTYEI RLVEDGKYGA QDDVNGQWNG 500
    MVRELIDHKA DLAVAPLAIT YVREKVIDFS KPFMTLGISI LYRKPNGTNP 550
    GVFSFLNPLS PDIWMYILLA YLGVSCVLFV IARFSPYEWY NPHPCNPDSD 600
    VVENNFTLLN SFWFGVGALM QQGSELMPKA LSTRIVGGIW WFFTLIIISS 650
    YTANLAAFLT VERMESPIDS ADDLAKQTKI EYGAVEDGAT MTFFKKSKIS 700
    TYDKMWAFMS SRRQSVLVKS NEEGIQRVLT SDYAFLMEST TIEFVTQRNC 750
    NLTQIGGLID SKGYGVGTPM GSPYRDKITI AILQLQEEGK LHMMKEKWWR 800
    GNGCPEEESK EASALGVQNI GGIFIVLAAG LVLSVFVAVG EFLYKSKKNA 850
    QLEKRSFCSA MVEELRMSLK CQRRLKHKPQ APVIVKTEEV INMHTFNDRR 900
    LPGKETMA 908
    Length:908
    Mass (Da):102,470
    Last modified:July 15, 1998 - v2
    Checksum:i7F430E2D8B2E982B
    GO

    RNA editingi

    Partially edited. The presence of Gln at position 621 (non-edited) determines channels with low calcium permeability, whereas an arginine residue (edited) determines a higher calcium permeability especially if the preceding sites are fully edited. This receptor is nearly completely edited in all gray matter structures (90% of the receptors).

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti567 – 5671I → C in RNA edited version.
    Natural varianti571 – 5711Y → C in RNA edited version.
    Natural varianti621 – 6211Q → R in RNA edited version.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11548 mRNA. Translation: CAA77647.1.
    Z11715 mRNA. Translation: CAA77778.1.
    PIRiS19098.
    RefSeqiNP_062182.1. NM_019309.2.
    UniGeneiRn.87696.

    Genome annotation databases

    GeneIDi54257.
    KEGGirno:54257.
    UCSCiRGD:2733. rat.

    Keywords - Coding sequence diversityi

    RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11548 mRNA. Translation: CAA77647.1 .
    Z11715 mRNA. Translation: CAA77778.1 .
    PIRi S19098.
    RefSeqi NP_062182.1. NM_019309.2.
    UniGenei Rn.87696.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S50 X-ray 1.65 A 428-806 [» ]
    1S7Y X-ray 1.75 A/B 429-544 [» ]
    A/B 667-806 [» ]
    1S9T X-ray 1.80 A/B 429-544 [» ]
    A/B 667-806 [» ]
    1SD3 X-ray 1.80 A/B 429-544 [» ]
    A/B 667-806 [» ]
    1TT1 X-ray 1.93 A/B 429-806 [» ]
    1YAE X-ray 3.11 A/B/C/D/E/F 419-557 [» ]
    A/B/C/D/E/F 662-819 [» ]
    2I0B X-ray 1.96 A/B/C 429-544 [» ]
    A/B/C 667-806 [» ]
    2I0C X-ray 2.25 A/B 429-544 [» ]
    A/B 667-806 [» ]
    2XXR X-ray 1.60 A/B 429-544 [» ]
    A/B 667-806 [» ]
    2XXT X-ray 1.90 A/B 667-806 [» ]
    2XXU X-ray 1.50 A/B 667-806 [» ]
    2XXV X-ray 1.70 A/B 667-806 [» ]
    2XXW X-ray 2.30 A/B 667-806 [» ]
    2XXX X-ray 2.10 A/B/C/D 667-806 [» ]
    2XXY X-ray 3.00 A/B/C/D 667-806 [» ]
    3G3F X-ray 1.38 A/B 429-544 [» ]
    A/B 667-806 [» ]
    3G3G X-ray 1.30 A/B 429-544 [» ]
    A/B 667-806 [» ]
    3G3H X-ray 1.50 A/B 429-544 [» ]
    A/B 667-806 [» ]
    3G3I X-ray 1.37 A/B 429-544 [» ]
    A/B 667-806 [» ]
    3G3J X-ray 1.32 A/B 429-544 [» ]
    A/B 667-806 [» ]
    3G3K X-ray 1.24 A/B 429-544 [» ]
    A/B 667-806 [» ]
    3H6G X-ray 2.70 A/B 32-420 [» ]
    3H6H X-ray 2.90 A/B 32-420 [» ]
    3QLT X-ray 2.99 A/B 32-420 [» ]
    3QLU X-ray 2.91 C/D 32-420 [» ]
    3QLV X-ray 3.94 C/D/F/H/J 32-420 [» ]
    4BDL X-ray 1.75 A/B 429-544 [» ]
    A/B 667-806 [» ]
    4BDM X-ray 3.40 A/B/C/D 429-544 [» ]
    A/B/C/D 667-806 [» ]
    4BDN X-ray 2.50 A/B/C/D 429-544 [» ]
    A/B/C/D 667-806 [» ]
    4BDO X-ray 2.55 A/B/C/D 429-544 [» ]
    A/B/C/D 667-806 [» ]
    4BDQ X-ray 1.90 A/B 429-544 [» ]
    A/B 667-806 [» ]
    4BDR X-ray 1.65 A/B 429-544 [» ]
    A/B 667-806 [» ]
    4H8I X-ray 2.00 A/B 429-544 [» ]
    A/B 667-806 [» ]
    ProteinModelPortali P42260.
    SMRi P42260. Positions 423-546, 668-804.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248480. 3 interactions.
    DIPi DIP-29256N.
    IntActi P42260. 3 interactions.
    MINTi MINT-8359884.
    STRINGi 10116.ENSRNOP00000000415.

    Chemistry

    BindingDBi P42260.
    ChEMBLi CHEMBL3038481.
    GuidetoPHARMACOLOGYi 451.

    Protein family/group databases

    TCDBi 1.A.10.1.11. the glutamate-gated ion channel (gic) family of neurotransmitter receptors.

    PTM databases

    PhosphoSitei P42260.

    Proteomic databases

    PaxDbi P42260.
    PRIDEi P42260.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 54257.
    KEGGi rno:54257.
    UCSCi RGD:2733. rat.

    Organism-specific databases

    CTDi 2898.
    RGDi 2733. Grik2.

    Phylogenomic databases

    eggNOGi NOG316680.
    HOGENOMi HOG000234371.
    HOVERGENi HBG051839.
    InParanoidi P42260.
    KOi K05202.
    PhylomeDBi P42260.

    Miscellaneous databases

    EvolutionaryTracei P42260.
    NextBioi 610770.
    PROi P42260.

    Gene expression databases

    Genevestigatori P42260.

    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. "Cloning of a cDNA for a glutamate receptor subunit activated by kainate but not AMPA."
      Egebjerg J., Bettler B., Hermans-Borgmeyer I., Heinemann S.F.
      Nature 351:745-748(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Brain.
    2. "High-affinity kainate and domoate receptors in rat brain."
      Lomeli H., Wisden W., Koehler M., Keinaenen K., Sommer B., Seeburg P.H.
      FEBS Lett. 307:139-143(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    3. "Determinants of Ca2+ permeability in both TM1 and TM2 of high affinity kainate receptor channels: diversity by RNA editing."
      Koehler M., Burnashev N., Sakmann B., Seeburg P.H.
      Neuron 10:491-500(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 560-585, RNA EDITING.
      Tissue: Brain.
    4. Cited for: INTERACTION WITH DLG4.
    5. "Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor subunits to the ubiquitin-proteasome pathway."
      Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M., Singer J.D., Marshall J.
      J. Biol. Chem. 281:40164-40173(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KLHL17, UBIQUITINATION, MUTAGENESIS OF VAL-883 AND ILE-884.
    6. "SUMOylation regulates kainate-receptor-mediated synaptic transmission."
      Martin S., Nishimune A., Mellor J.R., Henley J.M.
      Nature 447:321-325(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-886, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-886.
    7. Cited for: INTERACTION WITH NETO2.
    8. "Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular mechanisms underlying kainate receptor selectivity."
      Mayer M.L.
      Neuron 45:539-552(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 429-806 IN COMPLEXES WITH GLUTAMATE; KAINATE; METHYLGLUTAMATE AND QUISQUALATE.
    9. "Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid."
      Nanao M.H., Green T., Stern-Bach Y., Heinemann S.F., Choe S.
      Proc. Natl. Acad. Sci. U.S.A. 102:1708-1713(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) OF 419-819 IN COMPLEX WITH DOMOATE, SUBUNIT, GLYCOSYLATION AT ASN-423 AND ASN-751.
    10. "Conformational restriction blocks glutamate receptor desensitization."
      Weston M.C., Schuck P., Ghosal A., Rosenmund C., Mayer M.L.
      Nat. Struct. Mol. Biol. 13:1120-1127(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 663-806, FUNCTION, SUBUNIT.
    11. "Structure and assembly mechanism for heteromeric kainate receptors."
      Kumar J., Schuck P., Mayer M.L.
      Neuron 71:319-331(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 32-420 IN COMPLEX WITH GRIK5, DISULFIDE BONDS, GLYCOSYLATION AT ASN-67; ASN-378 AND ASN-412, SUBUNIT.

    Entry informationi

    Entry nameiGRIK2_RAT
    AccessioniPrimary (citable) accession number: P42260
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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 domoate > kainate > quisqualate > glutamate. It does not bind AMPA without coexpression with GRIK5.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3