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Q13002

- GRIK2_HUMAN

UniProt

Q13002 - GRIK2_HUMAN

Protein

Glutamate receptor ionotropic, kainate 2

Gene

GRIK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 – 5231GlutamateBy similarity
    Binding sitei738 – 7381GlutamateBy similarity

    GO - Molecular functioni

    1. extracellular-glutamate-gated ion channel activity Source: RefGenome
    2. kainate selective glutamate receptor activity Source: UniProtKB

    GO - Biological processi

    1. behavioral fear response Source: Ensembl
    2. cellular calcium ion homeostasis Source: Ensembl
    3. glutamate receptor signaling pathway Source: ProtInc
    4. intracellular protein transport Source: Ensembl
    5. ionotropic glutamate receptor signaling pathway Source: RefGenome
    6. ion transmembrane transport Source: GOC
    7. negative regulation of neuron apoptotic process Source: Ensembl
    8. negative regulation of synaptic transmission, glutamatergic Source: Ensembl
    9. neuronal action potential Source: Ensembl
    10. positive regulation of synaptic transmission Source: UniProtKB
    11. regulation of excitatory postsynaptic membrane potential Source: Ensembl
    12. regulation of inhibitory postsynaptic membrane potential Source: Ensembl
    13. regulation of long-term neuronal synaptic plasticity Source: Ensembl
    14. regulation of short-term neuronal synaptic plasticity Source: UniProtKB
    15. regulation of synaptic transmission Source: UniProtKB
    16. synaptic transmission Source: Reactome
    17. synaptic transmission, glutamatergic Source: RefGenome
    18. transport Source: ProtInc

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_21343. Activation of Na-permeable Kainate Receptors.
    REACT_21346. Activation of Ca-permeable Kainate Receptor.
    SignaLinkiQ13002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate receptor ionotropic, kainate 2
    Short name:
    GluK2
    Alternative name(s):
    Excitatory amino acid receptor 4
    Short name:
    EAA4
    Glutamate receptor 6
    Short name:
    GluR-6
    Short name:
    GluR6
    Gene namesi
    Name:GRIK2
    Synonyms:GLUR6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:4580. GRIK2.

    Subcellular locationi

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. dendrite Source: RefGenome
    3. integral component of plasma membrane Source: ProtInc
    4. kainate selective glutamate receptor complex Source: RefGenome
    5. neuronal cell body Source: Ensembl
    6. plasma membrane Source: Reactome
    7. postsynaptic membrane Source: RefGenome
    8. presynaptic membrane Source: RefGenome

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, autosomal recessive 6 (MRT6) [MIM:611092]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. In contrast to syndromic or specific mental retardation which also present with associated physical, neurological and/or psychiatric manifestations, intellectual deficiency is the only primary symptom of non-syndromic mental retardation. MRT6 patients display mild to severe mental retardation and psychomotor development delay in early childhood. Patients do not have neurologic problems, congenital malformations, or facial dysmorphism. Body height, weight, and head circumference are normal.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi611092. phenotype.
    Orphaneti88616. Autosomal recessive nonsyndromic intellectual disability.
    PharmGKBiPA164741600.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 908877Glutamate receptor ionotropic, kainate 2PRO_0000011544Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi73 – 731N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi96 ↔ 347By similarity
    Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi412 – 4121N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi430 – 4301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi546 – 5461N-linked (GlcNAc...)Sequence Analysis
    Modified residuei846 – 8461Phosphoserine; by PKC1 Publication
    Modified residuei868 – 8681Phosphoserine; by PKC1 Publication
    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 By similarity.By similarity
    Ubiquitinated. Ubiquitination regulates the GRIK2 levels at the synapse by leading kainate receptor degradation through proteasome By similarity.By similarity
    Phosphorylated by PKC at Ser-868 upon agonist activation, this directly enhance sumoylation.1 Publication

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiQ13002.
    PaxDbiQ13002.
    PRIDEiQ13002.

    PTM databases

    PhosphoSiteiQ13002.

    Expressioni

    Tissue specificityi

    Expression is higher in cerebellum than in cerebral cortex.

    Gene expression databases

    ArrayExpressiQ13002.
    BgeeiQ13002.
    CleanExiHS_GRIK2.
    GenevestigatoriQ13002.

    Organism-specific databases

    HPAiCAB022463.
    HPA014395.
    HPA014623.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi109155. 12 interactions.
    IntActiQ13002. 2 interactions.
    STRINGi9606.ENSP00000397026.

    Structurei

    Secondary structure

    1
    908
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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
    Helixi671 – 6755
    Beta strandi678 – 6836
    Helixi689 – 6968
    Helixi700 – 71112
    Helixi713 – 7164
    Beta strandi718 – 7203
    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
    3QXMX-ray1.65A/B429-544[»]
    A/B667-806[»]
    ProteinModelPortaliQ13002.
    SMRiQ13002. Positions 33-415, 430-805.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 561530ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini583 – 63553CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini657 – 819163ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini841 – 90868CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei562 – 58221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei636 – 65621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei820 – 84021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG316680.
    HOVERGENiHBG051839.
    InParanoidiQ13002.
    KOiK05202.
    OMAiVNGQWNG.
    OrthoDBiEOG71G9W6.
    PhylomeDBiQ13002.
    TreeFamiTF334668.

    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 (7)i

    Sequence statusi: Complete.

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

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13002-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MKIIFPILSN PVFRRTVKLL 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 QDDANGQWNG 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):102,583
    Last modified:November 1, 1996 - v1
    Checksum:i5F34630524401E84
    GO
    Isoform 2 (identifier: Q13002-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         855-908: RSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA → ESSIWLVPPYHPDTV

    Show »
    Length:869
    Mass (Da):97,981
    Checksum:iD85D8A5CB2B0C1FA
    GO
    Isoform 3 (identifier: Q13002-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         585-908: Missing.

    Show »
    Length:584
    Mass (Da):66,108
    Checksum:iE0E9EC92339921A1
    GO
    Isoform 4 (identifier: Q13002-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         547-622: Missing.

    Show »
    Length:832
    Mass (Da):93,966
    Checksum:iC0E9B91AC6AD6012
    GO
    Isoform 5 (identifier: Q13002-5) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         856-908: SFCSAMVEEL...RRLPGKETMA → AKTKLPQDYV...PSSSSLSSCS

    Show »
    Length:892
    Mass (Da):100,243
    Checksum:i50A477CB1265AF26
    GO
    Isoform 6 (identifier: Q13002-6) [UniParc]FASTAAdd to Basket

    Also known as: D

    The sequence of this isoform differs from the canonical sequence as follows:
         509-695: Missing.
         855-908: RSFCSAMVEELRMSLKCQRRLKHKPQAPVIVKTEEVINMHTFNDRRLPGKETMA → ESSIWLVPPYHPDTV

    Note: Seems to be specific for non-neuronal cells. May not function as active channel.

    Show »
    Length:682
    Mass (Da):77,054
    Checksum:iB08053B65BE3087F
    GO
    Isoform 7 (identifier: Q13002-7) [UniParc]FASTAAdd to Basket

    Also known as: E

    The sequence of this isoform differs from the canonical sequence as follows:
         510-714: Missing.
         856-908: SFCSAMVEEL...RRLPGKETMA → AKTKLPQDYV...PSSSSLSSCS

    Note: Seems to be specific for non-neuronal cells. May not function as active channel.

    Show »
    Length:687
    Mass (Da):77,112
    Checksum:i5BBD1224CA1A5FCC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201L → P in CAC81020. 1 PublicationCurated
    Sequence conflicti20 – 201L → P in ADH93570. (PubMed:20230879)Curated
    Sequence conflicti20 – 201L → P in ADH93571. (PubMed:20230879)Curated
    Sequence conflicti20 – 201L → P in ADH93572. (PubMed:20230879)Curated
    Sequence conflicti20 – 201L → P in ADH93573. (PubMed:20230879)Curated
    Sequence conflicti789 – 7891G → S(PubMed:8034316)Curated

    RNA editingi

    Partially edited. The presence of Gln at position 621 (non-edited) determines channels with low calcium permeability, whereas Arg (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), whereas much less edited in the white matter (10% of the receptors).

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti187 – 1871E → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035694
    Natural varianti567 – 5671I → V in RNA edited version.
    VAR_000305
    Natural varianti571 – 5711Y → C in RNA edited version.
    VAR_000306
    Natural varianti621 – 6211Q → R in RNA edited version.
    VAR_000307
    Natural varianti766 – 7661V → I.
    Corresponds to variant rs3213608 [ dbSNP | Ensembl ].
    VAR_049186
    Natural varianti867 – 8671M → I.
    Corresponds to variant rs2235076 [ dbSNP | Ensembl ].
    VAR_037633

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei509 – 695187Missing in isoform 6. 1 PublicationVSP_044388Add
    BLAST
    Alternative sequencei510 – 714205Missing in isoform 7. 1 PublicationVSP_044389Add
    BLAST
    Alternative sequencei547 – 62276Missing in isoform 4. 1 PublicationVSP_022334Add
    BLAST
    Alternative sequencei585 – 908324Missing in isoform 3. 1 PublicationVSP_022337Add
    BLAST
    Alternative sequencei855 – 90854RSFCS…KETMA → ESSIWLVPPYHPDTV in isoform 2 and isoform 6. 2 PublicationsVSP_022335Add
    BLAST
    Alternative sequencei856 – 90853SFCSA…KETMA → AKTKLPQDYVFLPILESVSI STVLSSSPSSSSLSSCS in isoform 5 and isoform 7. 2 PublicationsVSP_022336Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U16126 mRNA. Translation: AAC50420.1.
    AJ252246 mRNA. Translation: CAC81020.1.
    AJ301608 mRNA. Translation: CAC67485.1.
    AJ301609 mRNA. Translation: CAC67486.1.
    AJ301610 mRNA. Translation: CAC67487.1.
    HM149335 mRNA. Translation: ADH93569.1.
    HM149336 mRNA. Translation: ADH93570.1.
    HM149337 mRNA. Translation: ADH93571.1.
    HM149338 mRNA. Translation: ADH93572.1.
    HM149339 mRNA. Translation: ADH93573.1.
    AL109919 Genomic DNA. No translation available.
    AP002528 Genomic DNA. No translation available.
    AP002529 Genomic DNA. No translation available.
    AP002530 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW48448.1.
    CCDSiCCDS5048.1. [Q13002-1]
    CCDS5049.1. [Q13002-2]
    CCDS55045.1. [Q13002-5]
    PIRiA54260.
    RefSeqiNP_001159719.1. NM_001166247.1. [Q13002-5]
    NP_068775.1. NM_021956.4. [Q13002-1]
    NP_786944.1. NM_175768.3. [Q13002-2]
    XP_005267002.1. XM_005266945.1. [Q13002-1]
    XP_006715528.1. XM_006715465.1. [Q13002-5]
    UniGeneiHs.98262.

    Genome annotation databases

    EnsembliENST00000318991; ENSP00000313276; ENSG00000164418. [Q13002-2]
    ENST00000369137; ENSP00000358133; ENSG00000164418. [Q13002-4]
    ENST00000369138; ENSP00000358134; ENSG00000164418. [Q13002-5]
    ENST00000413795; ENSP00000405596; ENSG00000164418. [Q13002-2]
    ENST00000421544; ENSP00000397026; ENSG00000164418. [Q13002-1]
    GeneIDi2898.
    KEGGihsa:2898.
    UCSCiuc003pqn.3. human. [Q13002-1]
    uc003pqo.4. human. [Q13002-2]
    uc010kcw.3. human. [Q13002-5]
    uc021zdk.1. human. [Q13002-6]

    Polymorphism databases

    DMDMi2492627.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U16126 mRNA. Translation: AAC50420.1 .
    AJ252246 mRNA. Translation: CAC81020.1 .
    AJ301608 mRNA. Translation: CAC67485.1 .
    AJ301609 mRNA. Translation: CAC67486.1 .
    AJ301610 mRNA. Translation: CAC67487.1 .
    HM149335 mRNA. Translation: ADH93569.1 .
    HM149336 mRNA. Translation: ADH93570.1 .
    HM149337 mRNA. Translation: ADH93571.1 .
    HM149338 mRNA. Translation: ADH93572.1 .
    HM149339 mRNA. Translation: ADH93573.1 .
    AL109919 Genomic DNA. No translation available.
    AP002528 Genomic DNA. No translation available.
    AP002529 Genomic DNA. No translation available.
    AP002530 Genomic DNA. No translation available.
    CH471051 Genomic DNA. Translation: EAW48448.1 .
    CCDSi CCDS5048.1. [Q13002-1 ]
    CCDS5049.1. [Q13002-2 ]
    CCDS55045.1. [Q13002-5 ]
    PIRi A54260.
    RefSeqi NP_001159719.1. NM_001166247.1. [Q13002-5 ]
    NP_068775.1. NM_021956.4. [Q13002-1 ]
    NP_786944.1. NM_175768.3. [Q13002-2 ]
    XP_005267002.1. XM_005266945.1. [Q13002-1 ]
    XP_006715528.1. XM_006715465.1. [Q13002-5 ]
    UniGenei Hs.98262.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QXM X-ray 1.65 A/B 429-544 [» ]
    A/B 667-806 [» ]
    ProteinModelPortali Q13002.
    SMRi Q13002. Positions 33-415, 430-805.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109155. 12 interactions.
    IntActi Q13002. 2 interactions.
    STRINGi 9606.ENSP00000397026.

    Chemistry

    BindingDBi Q13002.
    ChEMBLi CHEMBL3683.
    DrugBanki DB00142. L-Glutamic Acid.
    GuidetoPHARMACOLOGYi 451.

    PTM databases

    PhosphoSitei Q13002.

    Polymorphism databases

    DMDMi 2492627.

    Proteomic databases

    MaxQBi Q13002.
    PaxDbi Q13002.
    PRIDEi Q13002.

    Protocols and materials databases

    DNASUi 2898.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318991 ; ENSP00000313276 ; ENSG00000164418 . [Q13002-2 ]
    ENST00000369137 ; ENSP00000358133 ; ENSG00000164418 . [Q13002-4 ]
    ENST00000369138 ; ENSP00000358134 ; ENSG00000164418 . [Q13002-5 ]
    ENST00000413795 ; ENSP00000405596 ; ENSG00000164418 . [Q13002-2 ]
    ENST00000421544 ; ENSP00000397026 ; ENSG00000164418 . [Q13002-1 ]
    GeneIDi 2898.
    KEGGi hsa:2898.
    UCSCi uc003pqn.3. human. [Q13002-1 ]
    uc003pqo.4. human. [Q13002-2 ]
    uc010kcw.3. human. [Q13002-5 ]
    uc021zdk.1. human. [Q13002-6 ]

    Organism-specific databases

    CTDi 2898.
    GeneCardsi GC06P101846.
    H-InvDB HIX0006094.
    HGNCi HGNC:4580. GRIK2.
    HPAi CAB022463.
    HPA014395.
    HPA014623.
    MIMi 138244. gene.
    611092. phenotype.
    neXtProti NX_Q13002.
    Orphaneti 88616. Autosomal recessive nonsyndromic intellectual disability.
    PharmGKBi PA164741600.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG316680.
    HOVERGENi HBG051839.
    InParanoidi Q13002.
    KOi K05202.
    OMAi VNGQWNG.
    OrthoDBi EOG71G9W6.
    PhylomeDBi Q13002.
    TreeFami TF334668.

    Enzyme and pathway databases

    Reactomei REACT_21343. Activation of Na-permeable Kainate Receptors.
    REACT_21346. Activation of Ca-permeable Kainate Receptor.
    SignaLinki Q13002.

    Miscellaneous databases

    GeneWikii GRIK2.
    GenomeRNAii 2898.
    NextBioi 11469.
    PROi Q13002.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13002.
    Bgeei Q13002.
    CleanExi HS_GRIK2.
    Genevestigatori Q13002.

    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 and pharmacological characterization of the human EAA4 (GluR6) glutamate receptor: a kainate selective channel subunit."
      Hoo K.H., Nutt S.L., Fletcher E.J., Elliott C.E., Korczak B., Deverill R.M., Rampersad V., Fantaske R.P., Kamboj R.K.
      Recept. Channels 2:327-337(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "Human GluR6 kainate receptor (GRIK2): molecular cloning, expression, polymorphism, and chromosomal assignment."
      Paschen W., Blackstone C.D., Huganir R.L., Ross C.A.
      Genomics 20:435-440(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Myeloid progenitor cell growth and apoptosis involves know and cell-specific ionotropic glutamate receptor."
      Langer A., Xu D., Kuehcke K., Fehse B., Abdallah S., Lother H.
      Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    4. "Genomic organization of the human GRIK2 gene and characterization of multiple splicing variants."
      Barbon A., Vallini I., Barlati S.
      Gene 274:187-197(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), GENE ORGANIZATION.
    5. "Novel spliced variants of ionotropic glutamate receptor GluR6 in normal human fibroblast and brain cells are transcribed by tissue specific promoters."
      Zhawar V.K., Kaur G., deRiel J.K., Kaur G.P., Kandpal R.P., Athwal R.S.
      Gene 459:1-10(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 5; 6 AND 7), ALTERNATIVE SPLICING.
      Tissue: Brain.
    6. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 621.
    9. "RNA editing of human kainate receptor subunits."
      Nutt S.L., Kamboj R.K.
      NeuroReport 5:2625-2629(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA EDITING OF POSITIONS 567; 571 AND 621.
      Tissue: Brain.
    10. Cited for: INTERACTION WITH DLG4.
    11. "Modification and movement: Phosphorylation and SUMOylation regulate endocytosis of GluK2-containing kainate receptors."
      Wilkinson K.A., Konopacki F., Henley J.M.
      Commun. Integr. Biol. 5:223-226(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-846 AND SER-868, SUMOYLATION AT LYS-886.
    12. "Binding and selectivity of the marine toxin neodysiherbaine A and its synthetic analogues to GluK1 and GluK2 kainate receptors."
      Unno M., Shinohara M., Takayama K., Tanaka H., Teruya K., Doh-ura K., Sakai R., Sasaki M., Ikeda-Saito M.
      J. Mol. Biol. 413:667-683(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 429-806 IN COMPLEX WITH AGONIST.
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-187.
    14. "A defect in the ionotropic glutamate receptor 6 gene (GRIK2) is associated with autosomal recessive mental retardation."
      Motazacker M.M., Rost B.R., Hucho T., Garshasbi M., Kahrizi K., Ullmann R., Abedini S.S., Nieh S.E., Amini S.H., Goswami C., Tzschach A., Jensen L.R., Schmitz D., Ropers H.H., Najmabadi H., Kuss A.W.
      Am. J. Hum. Genet. 81:792-798(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MRT6.

    Entry informationi

    Entry nameiGRIK2_HUMAN
    AccessioniPrimary (citable) accession number: Q13002
    Secondary accession number(s): A6NMY9
    , B5MCV0, D7RWZ3, D7RWZ4, D7RWZ5, D7RWZ6, D7RWZ7, Q8WWS1, Q96KS6, Q96KS7, Q96KS8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 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 domoate > kainate > quisqualate > 6-cyano-7-nitroquinoxaline-2,3-dione > L-glutamate = 6,7-dinitroquinoxaline-2,3-dione > dihydrokainate.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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